data_9J1F
# 
_entry.id   9J1F 
# 
_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   9J1F         pdb_00009j1f 10.2210/pdb9j1f/pdb 
WWPDB D_1300050152 ?            ?                   
# 
_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                        9J1F 
_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                     'Dimeric Structure of ConA/M2P-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 4  ? ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION' 54.938    4  ? ? ? ? 
3 non-polymer syn 'CALCIUM ION' 40.078    4  ? ? ? ? 
4 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   2  ? ? ? ? 
5 water       nat water 18.015    65 ? ? ? ? 
# 
_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,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION' MN    
3 'CALCIUM ION' CA    
4 
;~{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 
5 water HOH   
# 
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 
HOH   non-polymer         . WATER ?                             'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                             'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE ?                             'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE ?                             'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE ?                             'C5 H11 N O2 S'  149.211 
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 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   ASP 2   2   2   ASP ASP C . n 
C 1 3   THR 3   3   3   THR THR C . n 
C 1 4   ILE 4   4   4   ILE ILE C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   ALA 6   6   6   ALA ALA C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   GLU 8   8   8   GLU GLU C . n 
C 1 9   LEU 9   9   9   LEU LEU C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  THR 11  11  11  THR THR C . n 
C 1 12  TYR 12  12  12  TYR TYR C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  ASN 14  14  14  ASN ASN C . n 
C 1 15  THR 15  15  15  THR THR C . n 
C 1 16  ASP 16  16  16  ASP ASP C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  GLY 18  18  18  GLY GLY C . n 
C 1 19  ASP 19  19  19  ASP ASP C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  TYR 22  22  22  TYR TYR C . n 
C 1 23  PRO 23  23  23  PRO PRO C . n 
C 1 24  HIS 24  24  24  HIS HIS C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  GLY 26  26  26  GLY GLY C . n 
C 1 27  ILE 27  27  27  ILE ILE C . n 
C 1 28  ASP 28  28  28  ASP ASP C . n 
C 1 29  ILE 29  29  29  ILE ILE C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  SER 31  31  31  SER SER C . n 
C 1 32  VAL 32  32  32  VAL VAL C . n 
C 1 33  ARG 33  33  33  ARG ARG C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  LYS 35  35  35  LYS LYS C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  THR 37  37  37  THR THR C . n 
C 1 38  ALA 38  38  38  ALA ALA C . n 
C 1 39  LYS 39  39  39  LYS LYS C . n 
C 1 40  TRP 40  40  40  TRP TRP C . n 
C 1 41  ASN 41  41  41  ASN ASN C . n 
C 1 42  MET 42  42  42  MET MET C . n 
C 1 43  GLN 43  43  43  GLN GLN C . n 
C 1 44  ASN 44  44  44  ASN ASN C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  GLY 48  48  48  GLY GLY C . n 
C 1 49  THR 49  49  49  THR THR C . n 
C 1 50  ALA 50  50  50  ALA ALA C . n 
C 1 51  HIS 51  51  51  HIS HIS C . n 
C 1 52  ILE 52  52  52  ILE ILE C . n 
C 1 53  ILE 53  53  53  ILE ILE C . n 
C 1 54  TYR 54  54  54  TYR TYR C . n 
C 1 55  ASN 55  55  55  ASN ASN C . n 
C 1 56  SER 56  56  56  SER SER C . n 
C 1 57  VAL 57  57  57  VAL VAL C . n 
C 1 58  ASP 58  58  58  ASP ASP C . n 
C 1 59  LYS 59  59  59  LYS LYS C . n 
C 1 60  ARG 60  60  60  ARG ARG C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  SER 62  62  62  SER SER C . n 
C 1 63  ALA 63  63  63  ALA ALA C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  VAL 65  65  65  VAL VAL C . n 
C 1 66  SER 66  66  66  SER SER C . n 
C 1 67  TYR 67  67  67  TYR TYR C . n 
C 1 68  PRO 68  68  68  PRO PRO C . n 
C 1 69  ASN 69  69  69  ASN ASN C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  ASP 71  71  71  ASP ASP C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  ALA 73  73  73  ALA ALA C . n 
C 1 74  THR 74  74  74  THR THR C . n 
C 1 75  VAL 75  75  75  VAL VAL C . n 
C 1 76  SER 76  76  76  SER SER C . n 
C 1 77  TYR 77  77  77  TYR TYR C . n 
C 1 78  ASP 78  78  78  ASP ASP C . n 
C 1 79  VAL 79  79  79  VAL VAL C . n 
C 1 80  ASP 80  80  80  ASP ASP C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  ASP 82  82  82  ASP ASP C . n 
C 1 83  ASN 83  83  83  ASN ASN C . n 
C 1 84  VAL 84  84  84  VAL VAL C . n 
C 1 85  LEU 85  85  85  LEU LEU C . n 
C 1 86  PRO 86  86  86  PRO PRO C . n 
C 1 87  GLU 87  87  87  GLU GLU C . n 
C 1 88  TRP 88  88  88  TRP TRP C . n 
C 1 89  VAL 89  89  89  VAL VAL C . n 
C 1 90  ARG 90  90  90  ARG ARG C . n 
C 1 91  VAL 91  91  91  VAL VAL C . n 
C 1 92  GLY 92  92  92  GLY GLY C . n 
C 1 93  LEU 93  93  93  LEU LEU C . n 
C 1 94  SER 94  94  94  SER SER C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  SER 96  96  96  SER SER C . n 
C 1 97  THR 97  97  97  THR THR C . n 
C 1 98  GLY 98  98  98  GLY GLY C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 TYR 100 100 100 TYR TYR C . n 
C 1 101 LYS 101 101 101 LYS LYS C . n 
C 1 102 GLU 102 102 102 GLU GLU C . n 
C 1 103 THR 103 103 103 THR THR C . n 
C 1 104 ASN 104 104 104 ASN ASN C . n 
C 1 105 THR 105 105 105 THR THR C . n 
C 1 106 ILE 106 106 106 ILE ILE C . n 
C 1 107 LEU 107 107 107 LEU LEU C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 TRP 109 109 109 TRP TRP C . n 
C 1 110 SER 110 110 110 SER SER C . n 
C 1 111 PHE 111 111 111 PHE PHE C . n 
C 1 112 THR 112 112 112 THR THR C . n 
C 1 113 SER 113 113 113 SER SER C . n 
C 1 114 LYS 114 114 114 LYS LYS C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 LYS 116 116 116 LYS LYS C . n 
C 1 117 SER 117 117 117 SER SER C . n 
C 1 118 ASN 118 118 118 ASN ASN C . n 
C 1 119 SER 119 119 119 SER SER C . n 
C 1 120 THR 120 120 120 THR THR C . n 
C 1 121 HIS 121 121 121 HIS HIS C . n 
C 1 122 GLU 122 122 122 GLU GLU C . n 
C 1 123 THR 123 123 123 THR THR C . n 
C 1 124 ASN 124 124 124 ASN ASN C . n 
C 1 125 ALA 125 125 125 ALA ALA C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 HIS 127 127 127 HIS HIS C . n 
C 1 128 PHE 128 128 128 PHE PHE C . n 
C 1 129 MET 129 129 129 MET MET C . n 
C 1 130 PHE 130 130 130 PHE PHE C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLN 132 132 132 GLN GLN C . n 
C 1 133 PHE 133 133 133 PHE PHE C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 ASP 136 136 136 ASP ASP C . n 
C 1 137 GLN 137 137 137 GLN GLN C . n 
C 1 138 LYS 138 138 138 LYS LYS C . n 
C 1 139 ASP 139 139 139 ASP ASP C . n 
C 1 140 LEU 140 140 140 LEU LEU C . n 
C 1 141 ILE 141 141 141 ILE ILE C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 GLN 143 143 143 GLN GLN C . n 
C 1 144 GLY 144 144 144 GLY GLY C . n 
C 1 145 ASP 145 145 145 ASP ASP C . n 
C 1 146 ALA 146 146 146 ALA ALA C . n 
C 1 147 THR 147 147 147 THR THR C . n 
C 1 148 THR 148 148 148 THR THR C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 THR 150 150 150 THR THR C . n 
C 1 151 ASP 151 151 151 ASP ASP C . n 
C 1 152 GLY 152 152 152 GLY GLY C . n 
C 1 153 ASN 153 153 153 ASN ASN C . n 
C 1 154 LEU 154 154 154 LEU LEU C . n 
C 1 155 GLU 155 155 155 GLU GLU C . n 
C 1 156 LEU 156 156 156 LEU LEU C . n 
C 1 157 THR 157 157 157 THR THR C . n 
C 1 158 ARG 158 158 158 ARG ARG C . n 
C 1 159 VAL 159 159 159 VAL VAL C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 SER 161 161 161 SER SER C . n 
C 1 162 ASN 162 162 162 ASN ASN C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 SER 164 164 164 SER SER C . n 
C 1 165 PRO 165 165 165 PRO PRO C . n 
C 1 166 GLN 166 166 166 GLN GLN C . n 
C 1 167 GLY 167 167 167 GLY GLY C . n 
C 1 168 SER 168 168 168 SER SER C . n 
C 1 169 SER 169 169 169 SER SER C . n 
C 1 170 VAL 170 170 170 VAL VAL C . n 
C 1 171 GLY 171 171 171 GLY GLY C . n 
C 1 172 ARG 172 172 172 ARG ARG C . n 
C 1 173 ALA 173 173 173 ALA ALA C . n 
C 1 174 LEU 174 174 174 LEU LEU C . n 
C 1 175 PHE 175 175 175 PHE PHE C . n 
C 1 176 TYR 176 176 176 TYR TYR C . n 
C 1 177 ALA 177 177 177 ALA ALA C . n 
C 1 178 PRO 178 178 178 PRO PRO C . n 
C 1 179 VAL 179 179 179 VAL VAL C . n 
C 1 180 HIS 180 180 180 HIS HIS C . n 
C 1 181 ILE 181 181 181 ILE ILE C . n 
C 1 182 TRP 182 182 182 TRP TRP C . n 
C 1 183 GLU 183 183 183 GLU GLU C . n 
C 1 184 SER 184 184 184 SER SER C . n 
C 1 185 SER 185 185 185 SER SER C . n 
C 1 186 ALA 186 186 186 ALA ALA C . n 
C 1 187 VAL 187 187 187 VAL VAL C . n 
C 1 188 VAL 188 188 188 VAL VAL C . n 
C 1 189 ALA 189 189 189 ALA ALA C . n 
C 1 190 SER 190 190 190 SER SER C . n 
C 1 191 PHE 191 191 191 PHE PHE C . n 
C 1 192 GLU 192 192 192 GLU GLU C . n 
C 1 193 ALA 193 193 193 ALA ALA C . n 
C 1 194 THR 194 194 194 THR THR C . n 
C 1 195 PHE 195 195 195 PHE PHE C . n 
C 1 196 THR 196 196 196 THR THR C . n 
C 1 197 PHE 197 197 197 PHE PHE C . n 
C 1 198 LEU 198 198 198 LEU LEU C . n 
C 1 199 ILE 199 199 199 ILE ILE C . n 
C 1 200 LYS 200 200 200 LYS LYS C . n 
C 1 201 SER 201 201 201 SER SER C . n 
C 1 202 PRO 202 202 202 PRO PRO C . n 
C 1 203 ASP 203 203 203 ASP ASP C . n 
C 1 204 SER 204 204 204 SER SER C . n 
C 1 205 HIS 205 205 205 HIS HIS C . n 
C 1 206 PRO 206 206 206 PRO PRO C . n 
C 1 207 ALA 207 207 207 ALA ALA C . n 
C 1 208 ASP 208 208 208 ASP ASP C . n 
C 1 209 GLY 209 209 209 GLY GLY C . n 
C 1 210 ILE 210 210 210 ILE ILE C . n 
C 1 211 ALA 211 211 211 ALA ALA C . n 
C 1 212 PHE 212 212 212 PHE PHE C . n 
C 1 213 PHE 213 213 213 PHE PHE C . n 
C 1 214 ILE 214 214 214 ILE ILE C . n 
C 1 215 SER 215 215 215 SER SER C . n 
C 1 216 ASN 216 216 216 ASN ASN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 ASP 218 218 218 ASP ASP C . n 
C 1 219 SER 219 219 219 SER SER C . n 
C 1 220 SER 220 220 220 SER SER C . n 
C 1 221 ILE 221 221 221 ILE ILE C . n 
C 1 222 PRO 222 222 222 PRO PRO C . n 
C 1 223 SER 223 223 223 SER SER C . n 
C 1 224 GLY 224 224 224 GLY GLY C . n 
C 1 225 SER 225 225 225 SER SER C . n 
C 1 226 THR 226 226 226 THR THR C . n 
C 1 227 GLY 227 227 227 GLY GLY C . n 
C 1 228 ARG 228 228 228 ARG ARG C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 LEU 230 230 230 LEU LEU C . n 
C 1 231 GLY 231 231 231 GLY GLY C . n 
C 1 232 LEU 232 232 232 LEU LEU C . n 
C 1 233 PHE 233 233 233 PHE PHE C . n 
C 1 234 PRO 234 234 234 PRO PRO C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ALA 236 236 236 ALA ALA C . n 
C 1 237 ASN 237 237 237 ASN ASN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   ASP 2   2   2   ASP ASP D . n 
D 1 3   THR 3   3   3   THR THR D . n 
D 1 4   ILE 4   4   4   ILE ILE D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   ALA 6   6   6   ALA ALA D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   GLU 8   8   8   GLU GLU D . n 
D 1 9   LEU 9   9   9   LEU LEU D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  THR 11  11  11  THR THR D . n 
D 1 12  TYR 12  12  12  TYR TYR D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  ASN 14  14  14  ASN ASN D . n 
D 1 15  THR 15  15  15  THR THR D . n 
D 1 16  ASP 16  16  16  ASP ASP D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  GLY 18  18  18  GLY GLY D . n 
D 1 19  ASP 19  19  19  ASP ASP D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  TYR 22  22  22  TYR TYR D . n 
D 1 23  PRO 23  23  23  PRO PRO D . n 
D 1 24  HIS 24  24  24  HIS HIS D . n 
D 1 25  ILE 25  25  25  ILE ILE D . n 
D 1 26  GLY 26  26  26  GLY GLY D . n 
D 1 27  ILE 27  27  27  ILE ILE D . n 
D 1 28  ASP 28  28  28  ASP ASP D . n 
D 1 29  ILE 29  29  29  ILE ILE D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  SER 31  31  31  SER SER D . n 
D 1 32  VAL 32  32  32  VAL VAL D . n 
D 1 33  ARG 33  33  33  ARG ARG D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  LYS 35  35  35  LYS LYS D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  THR 37  37  37  THR THR D . n 
D 1 38  ALA 38  38  38  ALA ALA D . n 
D 1 39  LYS 39  39  39  LYS LYS D . n 
D 1 40  TRP 40  40  40  TRP TRP D . n 
D 1 41  ASN 41  41  41  ASN ASN D . n 
D 1 42  MET 42  42  42  MET MET D . n 
D 1 43  GLN 43  43  43  GLN GLN D . n 
D 1 44  ASN 44  44  44  ASN ASN D . n 
D 1 45  GLY 45  45  45  GLY GLY D . n 
D 1 46  LYS 46  46  46  LYS LYS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  GLY 48  48  48  GLY GLY D . n 
D 1 49  THR 49  49  49  THR THR D . n 
D 1 50  ALA 50  50  50  ALA ALA D . n 
D 1 51  HIS 51  51  51  HIS HIS D . n 
D 1 52  ILE 52  52  52  ILE ILE D . n 
D 1 53  ILE 53  53  53  ILE ILE D . n 
D 1 54  TYR 54  54  54  TYR TYR D . n 
D 1 55  ASN 55  55  55  ASN ASN D . n 
D 1 56  SER 56  56  56  SER SER D . n 
D 1 57  VAL 57  57  57  VAL VAL D . n 
D 1 58  ASP 58  58  58  ASP ASP D . n 
D 1 59  LYS 59  59  59  LYS LYS D . n 
D 1 60  ARG 60  60  60  ARG ARG D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  SER 62  62  62  SER SER D . n 
D 1 63  ALA 63  63  63  ALA ALA D . n 
D 1 64  VAL 64  64  64  VAL VAL D . n 
D 1 65  VAL 65  65  65  VAL VAL D . n 
D 1 66  SER 66  66  66  SER SER D . n 
D 1 67  TYR 67  67  67  TYR TYR D . n 
D 1 68  PRO 68  68  68  PRO PRO D . n 
D 1 69  ASN 69  69  69  ASN ASN D . n 
D 1 70  ALA 70  70  70  ALA ALA D . n 
D 1 71  ASP 71  71  71  ASP ASP D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  ALA 73  73  73  ALA ALA D . n 
D 1 74  THR 74  74  74  THR THR D . n 
D 1 75  VAL 75  75  75  VAL VAL D . n 
D 1 76  SER 76  76  76  SER SER D . n 
D 1 77  TYR 77  77  77  TYR TYR D . n 
D 1 78  ASP 78  78  78  ASP ASP D . n 
D 1 79  VAL 79  79  79  VAL VAL D . n 
D 1 80  ASP 80  80  80  ASP ASP D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  ASP 82  82  82  ASP ASP D . n 
D 1 83  ASN 83  83  83  ASN ASN D . n 
D 1 84  VAL 84  84  84  VAL VAL D . n 
D 1 85  LEU 85  85  85  LEU LEU D . n 
D 1 86  PRO 86  86  86  PRO PRO D . n 
D 1 87  GLU 87  87  87  GLU GLU D . n 
D 1 88  TRP 88  88  88  TRP TRP D . n 
D 1 89  VAL 89  89  89  VAL VAL D . n 
D 1 90  ARG 90  90  90  ARG ARG D . n 
D 1 91  VAL 91  91  91  VAL VAL D . n 
D 1 92  GLY 92  92  92  GLY GLY D . n 
D 1 93  LEU 93  93  93  LEU LEU D . n 
D 1 94  SER 94  94  94  SER SER D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  SER 96  96  96  SER SER D . n 
D 1 97  THR 97  97  97  THR THR D . n 
D 1 98  GLY 98  98  98  GLY GLY D . n 
D 1 99  LEU 99  99  99  LEU LEU D . n 
D 1 100 TYR 100 100 100 TYR TYR D . n 
D 1 101 LYS 101 101 101 LYS LYS D . n 
D 1 102 GLU 102 102 102 GLU GLU D . n 
D 1 103 THR 103 103 103 THR THR D . n 
D 1 104 ASN 104 104 104 ASN ASN D . n 
D 1 105 THR 105 105 105 THR THR D . n 
D 1 106 ILE 106 106 106 ILE ILE D . n 
D 1 107 LEU 107 107 107 LEU LEU D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 TRP 109 109 109 TRP TRP D . n 
D 1 110 SER 110 110 110 SER SER D . n 
D 1 111 PHE 111 111 111 PHE PHE D . n 
D 1 112 THR 112 112 112 THR THR D . n 
D 1 113 SER 113 113 113 SER SER D . n 
D 1 114 LYS 114 114 114 LYS LYS D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 LYS 116 116 116 LYS LYS D . n 
D 1 117 SER 117 117 117 SER SER D . n 
D 1 118 ASN 118 118 118 ASN ASN D . n 
D 1 119 SER 119 119 119 SER SER D . n 
D 1 120 THR 120 120 120 THR THR D . n 
D 1 121 HIS 121 121 121 HIS HIS D . n 
D 1 122 GLU 122 122 122 GLU GLU D . n 
D 1 123 THR 123 123 123 THR THR D . n 
D 1 124 ASN 124 124 124 ASN ASN D . n 
D 1 125 ALA 125 125 125 ALA ALA D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 HIS 127 127 127 HIS HIS D . n 
D 1 128 PHE 128 128 128 PHE PHE D . n 
D 1 129 MET 129 129 129 MET MET D . n 
D 1 130 PHE 130 130 130 PHE PHE D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLN 132 132 132 GLN GLN D . n 
D 1 133 PHE 133 133 133 PHE PHE D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 ASP 136 136 136 ASP ASP D . n 
D 1 137 GLN 137 137 137 GLN GLN D . n 
D 1 138 LYS 138 138 138 LYS LYS D . n 
D 1 139 ASP 139 139 139 ASP ASP D . n 
D 1 140 LEU 140 140 140 LEU LEU D . n 
D 1 141 ILE 141 141 141 ILE ILE D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 GLN 143 143 143 GLN GLN D . n 
D 1 144 GLY 144 144 144 GLY GLY D . n 
D 1 145 ASP 145 145 145 ASP ASP D . n 
D 1 146 ALA 146 146 146 ALA ALA D . n 
D 1 147 THR 147 147 147 THR THR D . n 
D 1 148 THR 148 148 148 THR THR D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 THR 150 150 150 THR THR D . n 
D 1 151 ASP 151 151 151 ASP ASP D . n 
D 1 152 GLY 152 152 152 GLY GLY D . n 
D 1 153 ASN 153 153 153 ASN ASN D . n 
D 1 154 LEU 154 154 154 LEU LEU D . n 
D 1 155 GLU 155 155 155 GLU GLU D . n 
D 1 156 LEU 156 156 156 LEU LEU D . n 
D 1 157 THR 157 157 157 THR THR D . n 
D 1 158 ARG 158 158 158 ARG ARG D . n 
D 1 159 VAL 159 159 159 VAL VAL D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 SER 161 161 161 SER SER D . n 
D 1 162 ASN 162 162 162 ASN ASN D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 SER 164 164 164 SER SER D . n 
D 1 165 PRO 165 165 165 PRO PRO D . n 
D 1 166 GLN 166 166 166 GLN GLN D . n 
D 1 167 GLY 167 167 167 GLY GLY D . n 
D 1 168 SER 168 168 168 SER SER D . n 
D 1 169 SER 169 169 169 SER SER D . n 
D 1 170 VAL 170 170 170 VAL VAL D . n 
D 1 171 GLY 171 171 171 GLY GLY D . n 
D 1 172 ARG 172 172 172 ARG ARG D . n 
D 1 173 ALA 173 173 173 ALA ALA D . n 
D 1 174 LEU 174 174 174 LEU LEU D . n 
D 1 175 PHE 175 175 175 PHE PHE D . n 
D 1 176 TYR 176 176 176 TYR TYR D . n 
D 1 177 ALA 177 177 177 ALA ALA D . n 
D 1 178 PRO 178 178 178 PRO PRO D . n 
D 1 179 VAL 179 179 179 VAL VAL D . n 
D 1 180 HIS 180 180 180 HIS HIS D . n 
D 1 181 ILE 181 181 181 ILE ILE D . n 
D 1 182 TRP 182 182 182 TRP TRP D . n 
D 1 183 GLU 183 183 183 GLU GLU D . n 
D 1 184 SER 184 184 184 SER SER D . n 
D 1 185 SER 185 185 185 SER SER D . n 
D 1 186 ALA 186 186 186 ALA ALA D . n 
D 1 187 VAL 187 187 187 VAL VAL D . n 
D 1 188 VAL 188 188 188 VAL VAL D . n 
D 1 189 ALA 189 189 189 ALA ALA D . n 
D 1 190 SER 190 190 190 SER SER D . n 
D 1 191 PHE 191 191 191 PHE PHE D . n 
D 1 192 GLU 192 192 192 GLU GLU D . n 
D 1 193 ALA 193 193 193 ALA ALA D . n 
D 1 194 THR 194 194 194 THR THR D . n 
D 1 195 PHE 195 195 195 PHE PHE D . n 
D 1 196 THR 196 196 196 THR THR D . n 
D 1 197 PHE 197 197 197 PHE PHE D . n 
D 1 198 LEU 198 198 198 LEU LEU D . n 
D 1 199 ILE 199 199 199 ILE ILE D . n 
D 1 200 LYS 200 200 200 LYS LYS D . n 
D 1 201 SER 201 201 201 SER SER D . n 
D 1 202 PRO 202 202 202 PRO PRO D . n 
D 1 203 ASP 203 203 203 ASP ASP D . n 
D 1 204 SER 204 204 204 SER SER D . n 
D 1 205 HIS 205 205 205 HIS HIS D . n 
D 1 206 PRO 206 206 206 PRO PRO D . n 
D 1 207 ALA 207 207 207 ALA ALA D . n 
D 1 208 ASP 208 208 208 ASP ASP D . n 
D 1 209 GLY 209 209 209 GLY GLY D . n 
D 1 210 ILE 210 210 210 ILE ILE D . n 
D 1 211 ALA 211 211 211 ALA ALA D . n 
D 1 212 PHE 212 212 212 PHE PHE D . n 
D 1 213 PHE 213 213 213 PHE PHE D . n 
D 1 214 ILE 214 214 214 ILE ILE D . n 
D 1 215 SER 215 215 215 SER SER D . n 
D 1 216 ASN 216 216 216 ASN ASN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 ASP 218 218 218 ASP ASP D . n 
D 1 219 SER 219 219 219 SER SER D . n 
D 1 220 SER 220 220 220 SER SER D . n 
D 1 221 ILE 221 221 221 ILE ILE D . n 
D 1 222 PRO 222 222 222 PRO PRO D . n 
D 1 223 SER 223 223 223 SER SER D . n 
D 1 224 GLY 224 224 224 GLY GLY D . n 
D 1 225 SER 225 225 225 SER SER D . n 
D 1 226 THR 226 226 226 THR THR D . n 
D 1 227 GLY 227 227 227 GLY GLY D . n 
D 1 228 ARG 228 228 228 ARG ARG D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 LEU 230 230 230 LEU LEU D . n 
D 1 231 GLY 231 231 231 GLY GLY D . n 
D 1 232 LEU 232 232 232 LEU LEU D . n 
D 1 233 PHE 233 233 233 PHE PHE D . n 
D 1 234 PRO 234 234 234 PRO PRO D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ALA 236 236 236 ALA ALA D . n 
D 1 237 ASN 237 237 237 ASN ASN D . 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 
E 2 MN    1  301 1   MN    MN  A . 
F 3 CA    1  302 1   CA    CA  A . 
G 4 A1EAW 1  301 301 A1EAW M2P B . 
H 2 MN    1  302 2   MN    MN  B . 
I 3 CA    1  303 2   CA    CA  B . 
J 4 A1EAW 1  301 301 A1EAW M2P C . 
K 2 MN    1  302 3   MN    MN  C . 
L 3 CA    1  303 3   CA    CA  C . 
M 2 MN    1  301 4   MN    MN  D . 
N 3 CA    1  302 4   CA    CA  D . 
O 5 HOH   1  401 38  HOH   HOH A . 
O 5 HOH   2  402 54  HOH   HOH A . 
O 5 HOH   3  403 62  HOH   HOH A . 
O 5 HOH   4  404 3   HOH   HOH A . 
O 5 HOH   5  405 6   HOH   HOH A . 
O 5 HOH   6  406 1   HOH   HOH A . 
O 5 HOH   7  407 51  HOH   HOH A . 
O 5 HOH   8  408 24  HOH   HOH A . 
O 5 HOH   9  409 14  HOH   HOH A . 
O 5 HOH   10 410 50  HOH   HOH A . 
O 5 HOH   11 411 19  HOH   HOH A . 
O 5 HOH   12 412 15  HOH   HOH A . 
O 5 HOH   13 413 17  HOH   HOH A . 
O 5 HOH   14 414 60  HOH   HOH A . 
O 5 HOH   15 415 48  HOH   HOH A . 
O 5 HOH   16 416 33  HOH   HOH A . 
O 5 HOH   17 417 20  HOH   HOH A . 
O 5 HOH   18 418 37  HOH   HOH A . 
O 5 HOH   19 419 9   HOH   HOH A . 
O 5 HOH   20 420 46  HOH   HOH A . 
O 5 HOH   21 421 23  HOH   HOH A . 
O 5 HOH   22 422 30  HOH   HOH A . 
O 5 HOH   23 423 28  HOH   HOH A . 
P 5 HOH   1  401 12  HOH   HOH B . 
P 5 HOH   2  402 43  HOH   HOH B . 
P 5 HOH   3  403 31  HOH   HOH B . 
P 5 HOH   4  404 2   HOH   HOH B . 
P 5 HOH   5  405 29  HOH   HOH B . 
P 5 HOH   6  406 39  HOH   HOH B . 
P 5 HOH   7  407 35  HOH   HOH B . 
P 5 HOH   8  408 5   HOH   HOH B . 
P 5 HOH   9  409 4   HOH   HOH B . 
P 5 HOH   10 410 36  HOH   HOH B . 
P 5 HOH   11 411 65  HOH   HOH B . 
P 5 HOH   12 412 53  HOH   HOH B . 
P 5 HOH   13 413 66  HOH   HOH B . 
P 5 HOH   14 414 61  HOH   HOH B . 
P 5 HOH   15 415 42  HOH   HOH B . 
Q 5 HOH   1  401 56  HOH   HOH C . 
Q 5 HOH   2  402 21  HOH   HOH C . 
Q 5 HOH   3  403 44  HOH   HOH C . 
Q 5 HOH   4  404 64  HOH   HOH C . 
Q 5 HOH   5  405 25  HOH   HOH C . 
Q 5 HOH   6  406 10  HOH   HOH C . 
Q 5 HOH   7  407 59  HOH   HOH C . 
Q 5 HOH   8  408 49  HOH   HOH C . 
Q 5 HOH   9  409 7   HOH   HOH C . 
Q 5 HOH   10 410 27  HOH   HOH C . 
Q 5 HOH   11 411 47  HOH   HOH C . 
Q 5 HOH   12 412 63  HOH   HOH C . 
Q 5 HOH   13 413 57  HOH   HOH C . 
Q 5 HOH   14 414 32  HOH   HOH C . 
Q 5 HOH   15 415 18  HOH   HOH C . 
Q 5 HOH   16 416 8   HOH   HOH C . 
Q 5 HOH   17 417 55  HOH   HOH C . 
Q 5 HOH   18 418 16  HOH   HOH C . 
Q 5 HOH   19 419 13  HOH   HOH C . 
Q 5 HOH   20 420 22  HOH   HOH C . 
Q 5 HOH   21 421 45  HOH   HOH C . 
R 5 HOH   1  401 40  HOH   HOH D . 
R 5 HOH   2  402 52  HOH   HOH D . 
R 5 HOH   3  403 26  HOH   HOH D . 
R 5 HOH   4  404 11  HOH   HOH D . 
R 5 HOH   5  405 58  HOH   HOH D . 
R 5 HOH   6  406 41  HOH   HOH D . 
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   117.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J1F 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.216 
_cell.length_a_esd                 ? 
_cell.length_b                     79.070 
_cell.length_b_esd                 ? 
_cell.length_c                     87.917 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9J1F 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9J1F 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.79 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Sodium chloride, 0.1M Phosphate-citrate pH 4.2 10% (w/v) PEG 3000' 
_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         2024-06-08 
_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                                       9J1F 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.17 
_reflns.d_resolution_low                               78.20 
_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                                     52760 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.69 
_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                                0.161 
_reflns.pdbx_Rpim_I_all                                0.084 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       184071 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.136 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.17 
_reflns_shell.d_res_low                                     2.28 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           22043 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7613 
_reflns_shell.percent_possible_obs                          99.4 
_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                               2.9 
_reflns_shell.pdbx_chi_squared                              0.86 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.1 
_reflns_shell.pdbx_Rrim_I_all                               1.058 
_reflns_shell.pdbx_Rpim_I_all                               0.602 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.369 
_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                                  0.862 
_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]                            0.01 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.02 
_refine.aniso_B[2][2]                            -0.11 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.05 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.965 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.932 
_refine.correlation_coeff_Fo_to_Fc_free          0.898 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 9J1F 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.17 
_refine.ls_d_res_low                             78.20 
_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                     49425 
_refine.ls_number_reflns_R_free                  2477 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.22 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21093 
_refine.ls_R_factor_R_free                       0.25690 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20870 
_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                    MASK 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4P9W 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.283 
_refine.pdbx_overall_ESU_R_Free                  0.220 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             8.426 
_refine.overall_SU_ML                            0.203 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.17 
_refine_hist.d_res_low                        78.20 
_refine_hist.number_atoms_solvent             65 
_refine_hist.number_atoms_total               7417 
_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        7236 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         116 
_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' ? 0.008  0.013  7520  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  6692  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.599  1.654  10256 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.222  1.592  15604 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.818  5.000  944   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 35.228 23.810 336   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.739 15.000 1156  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 20.613 15.000 24    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.063  0.200  1040  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  8428  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  1516  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.751  2.941  3788  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.750  2.940  3787  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 4.694  4.401  4730  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.694  4.402  4731  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.583  3.196  3732  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.581  3.194  3729  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.301  4.684  5525  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.030  33.413 7702  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.029  33.432 7695  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.17 
_refine_ls_shell.d_res_low                        2.222 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             156 
_refine_ls_shell.number_reflns_R_work             3622 
_refine_ls_shell.percent_reflns_obs               96.87 
_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                  0.311 
_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                  0.368 
# 
_struct.entry_id                     9J1F 
_struct.title                        'Dimeric Structure of ConA/M2P-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        9J1F 
_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 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 2 ? 
L N N 3 ? 
M N N 2 ? 
N N N 3 ? 
O N N 5 ? 
P N N 5 ? 
Q N N 5 ? 
R N N 5 ? 
# 
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 9J1F A 1   ? 118 ? P02866 164 ? 281 ? 1   118 
2 2 9J1F A 119 ? 237 ? P02866 30  ? 148 ? 119 237 
3 1 9J1F B 1   ? 118 ? P02866 164 ? 281 ? 1   118 
4 2 9J1F B 119 ? 237 ? P02866 30  ? 148 ? 119 237 
5 1 9J1F C 1   ? 118 ? P02866 164 ? 281 ? 1   118 
6 2 9J1F C 119 ? 237 ? P02866 30  ? 148 ? 119 237 
7 1 9J1F D 1   ? 118 ? P02866 164 ? 281 ? 1   118 
8 2 9J1F D 119 ? 237 ? P02866 30  ? 148 ? 119 237 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
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)' 2220  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  18960 ? 
2 'ABSA (A^2)' 2190  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  19630 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,D,E,F,M,N,O,R 
2 1 B,G,H,I,P       
2 2 C,J,K,L,Q       
# 
_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' 2_445 -x-1,y-1/2,-z -1.0000000000 0.0000000000 0.0000000000 -81.2160000000 0.0000000000 
1.0000000000 0.0000000000 -39.5350000000 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  ? VAL A 84  ? ASP A 80  VAL A 84  5 ? 5 
HELX_P HELX_P3  AA3 THR A 226 ? LEU A 230 ? THR A 226 LEU A 230 5 ? 5 
HELX_P HELX_P4  AA4 ASN B 14  ? GLY B 18  ? ASN B 14  GLY B 18  5 ? 5 
HELX_P HELX_P5  AA5 ASP B 80  ? VAL B 84  ? ASP B 80  VAL B 84  5 ? 5 
HELX_P HELX_P6  AA6 THR B 150 ? GLY B 152 ? THR B 150 GLY B 152 5 ? 3 
HELX_P HELX_P7  AA7 THR B 226 ? LEU B 230 ? THR B 226 LEU B 230 5 ? 5 
HELX_P HELX_P8  AA8 ASN C 14  ? GLY C 18  ? ASN C 14  GLY C 18  5 ? 5 
HELX_P HELX_P9  AA9 ASP C 80  ? VAL C 84  ? ASP C 80  VAL C 84  5 ? 5 
HELX_P HELX_P10 AB1 THR C 150 ? GLY C 152 ? THR C 150 GLY C 152 5 ? 3 
HELX_P HELX_P11 AB2 THR C 226 ? LEU C 230 ? THR C 226 LEU C 230 5 ? 5 
HELX_P HELX_P12 AB3 ASN D 14  ? GLY D 18  ? ASN D 14  GLY D 18  5 ? 5 
HELX_P HELX_P13 AB4 ASP D 80  ? VAL D 84  ? ASP D 80  VAL D 84  5 ? 5 
HELX_P HELX_P14 AB5 THR D 226 ? LEU D 230 ? THR D 226 LEU D 230 5 ? 5 
# 
_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  301 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc2  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 E MN  . MN ? ? A ASP 10  A MN  301 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
metalc3  metalc ? ? A ASP 10 OD1 ? ? ? 1_555 F CA  . CA ? ? A ASP 10  A CA  302 1_555 ? ? ? ? ? ? ? 2.460 ? ? 
metalc4  metalc ? ? A ASP 10 OD2 ? ? ? 1_555 F CA  . CA ? ? A ASP 10  A CA  302 1_555 ? ? ? ? ? ? ? 2.620 ? ? 
metalc5  metalc ? ? A TYR 12 O   ? ? ? 1_555 F CA  . CA ? ? A TYR 12  A CA  302 1_555 ? ? ? ? ? ? ? 2.422 ? ? 
metalc6  metalc ? ? A ASN 14 OD1 ? ? ? 1_555 F CA  . CA ? ? A ASN 14  A CA  302 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc7  metalc ? ? A ASP 19 OD1 ? ? ? 1_555 E MN  . MN ? ? A ASP 19  A MN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc8  metalc ? ? A ASP 19 OD2 ? ? ? 1_555 F CA  . CA ? ? A ASP 19  A CA  302 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc9  metalc ? ? A HIS 24 NE2 ? ? ? 1_555 E MN  . MN ? ? A HIS 24  A MN  301 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc10 metalc ? ? E MN  .  MN  ? ? ? 1_555 O HOH . O  ? ? A MN  301 A HOH 409 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc11 metalc ? ? E MN  .  MN  ? ? ? 1_555 O HOH . O  ? ? A MN  301 A HOH 411 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc12 metalc ? ? F CA  .  CA  ? ? ? 1_555 O HOH . O  ? ? A CA  302 A HOH 406 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc13 metalc ? ? F CA  .  CA  ? ? ? 1_555 O HOH . O  ? ? A CA  302 A HOH 413 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc14 metalc ? ? B GLU 8  OE1 ? ? ? 1_555 H MN  . MN ? ? B GLU 8   B MN  302 1_555 ? ? ? ? ? ? ? 2.112 ? ? 
metalc15 metalc ? ? B ASP 10 OD2 ? ? ? 1_555 H MN  . MN ? ? B ASP 10  B MN  302 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc16 metalc ? ? B ASP 10 OD1 ? ? ? 1_555 I CA  . CA ? ? B ASP 10  B CA  303 1_555 ? ? ? ? ? ? ? 2.345 ? ? 
metalc17 metalc ? ? B ASP 10 OD2 ? ? ? 1_555 I CA  . CA ? ? B ASP 10  B CA  303 1_555 ? ? ? ? ? ? ? 2.510 ? ? 
metalc18 metalc ? ? B TYR 12 O   ? ? ? 1_555 I CA  . CA ? ? B TYR 12  B CA  303 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc19 metalc ? ? B ASN 14 OD1 ? ? ? 1_555 I CA  . CA ? ? B ASN 14  B CA  303 1_555 ? ? ? ? ? ? ? 2.478 ? ? 
metalc20 metalc ? ? B ASP 19 OD1 ? ? ? 1_555 H MN  . MN ? ? B ASP 19  B MN  302 1_555 ? ? ? ? ? ? ? 2.184 ? ? 
metalc21 metalc ? ? B ASP 19 OD2 ? ? ? 1_555 I CA  . CA ? ? B ASP 19  B CA  303 1_555 ? ? ? ? ? ? ? 2.357 ? ? 
metalc22 metalc ? ? B HIS 24 NE2 ? ? ? 1_555 H MN  . MN ? ? B HIS 24  B MN  302 1_555 ? ? ? ? ? ? ? 2.263 ? ? 
metalc23 metalc ? ? H MN  .  MN  ? ? ? 1_555 P HOH . O  ? ? B MN  302 B HOH 401 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc24 metalc ? ? H MN  .  MN  ? ? ? 1_555 P HOH . O  ? ? B MN  302 B HOH 408 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
metalc25 metalc ? ? I CA  .  CA  ? ? ? 1_555 P HOH . O  ? ? B CA  303 B HOH 407 1_555 ? ? ? ? ? ? ? 2.570 ? ? 
metalc26 metalc ? ? I CA  .  CA  ? ? ? 1_555 P HOH . O  ? ? B CA  303 B HOH 409 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc27 metalc ? ? C GLU 8  OE2 ? ? ? 1_555 K MN  . MN ? ? C GLU 8   C MN  302 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc28 metalc ? ? C ASP 10 OD2 ? ? ? 1_555 K MN  . MN ? ? C ASP 10  C MN  302 1_555 ? ? ? ? ? ? ? 1.955 ? ? 
metalc29 metalc ? ? C ASP 10 OD1 ? ? ? 1_555 L CA  . CA ? ? C ASP 10  C CA  303 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc30 metalc ? ? C ASP 10 OD2 ? ? ? 1_555 L CA  . CA ? ? C ASP 10  C CA  303 1_555 ? ? ? ? ? ? ? 2.663 ? ? 
metalc31 metalc ? ? C TYR 12 O   ? ? ? 1_555 L CA  . CA ? ? C TYR 12  C CA  303 1_555 ? ? ? ? ? ? ? 2.443 ? ? 
metalc32 metalc ? ? C ASN 14 OD1 ? ? ? 1_555 L CA  . CA ? ? C ASN 14  C CA  303 1_555 ? ? ? ? ? ? ? 2.585 ? ? 
metalc33 metalc ? ? C ASP 19 OD1 ? ? ? 1_555 K MN  . MN ? ? C ASP 19  C MN  302 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc34 metalc ? ? C ASP 19 OD2 ? ? ? 1_555 L CA  . CA ? ? C ASP 19  C CA  303 1_555 ? ? ? ? ? ? ? 2.445 ? ? 
metalc35 metalc ? ? C HIS 24 NE2 ? ? ? 1_555 K MN  . MN ? ? C HIS 24  C MN  302 1_555 ? ? ? ? ? ? ? 2.180 ? ? 
metalc36 metalc ? ? K MN  .  MN  ? ? ? 1_555 Q HOH . O  ? ? C MN  302 C HOH 406 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc37 metalc ? ? K MN  .  MN  ? ? ? 1_555 Q HOH . O  ? ? C MN  302 C HOH 409 1_555 ? ? ? ? ? ? ? 1.968 ? ? 
metalc38 metalc ? ? L CA  .  CA  ? ? ? 1_555 Q HOH . O  ? ? C CA  303 C HOH 410 1_555 ? ? ? ? ? ? ? 2.431 ? ? 
metalc39 metalc ? ? L CA  .  CA  ? ? ? 1_555 Q HOH . O  ? ? C CA  303 C HOH 414 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc40 metalc ? ? D GLU 8  OE2 ? ? ? 1_555 M MN  . MN ? ? D GLU 8   D MN  301 1_555 ? ? ? ? ? ? ? 2.256 ? ? 
metalc41 metalc ? ? D ASP 10 OD2 ? ? ? 1_555 M MN  . MN ? ? D ASP 10  D MN  301 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
metalc42 metalc ? ? D ASP 10 OD1 ? ? ? 1_555 N CA  . CA ? ? D ASP 10  D CA  302 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc43 metalc ? ? D ASP 10 OD2 ? ? ? 1_555 N CA  . CA ? ? D ASP 10  D CA  302 1_555 ? ? ? ? ? ? ? 2.565 ? ? 
metalc44 metalc ? ? D TYR 12 O   ? ? ? 1_555 N CA  . CA ? ? D TYR 12  D CA  302 1_555 ? ? ? ? ? ? ? 2.498 ? ? 
metalc45 metalc ? ? D ASN 14 OD1 ? ? ? 1_555 N CA  . CA ? ? D ASN 14  D CA  302 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc46 metalc ? ? D ASP 19 OD1 ? ? ? 1_555 M MN  . MN ? ? D ASP 19  D MN  301 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc47 metalc ? ? D ASP 19 OD2 ? ? ? 1_555 N CA  . CA ? ? D ASP 19  D CA  302 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc48 metalc ? ? D HIS 24 NE2 ? ? ? 1_555 M MN  . MN ? ? D HIS 24  D MN  301 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc49 metalc ? ? M MN  .  MN  ? ? ? 1_555 R HOH . O  ? ? D MN  301 D HOH 404 1_555 ? ? ? ? ? ? ? 1.895 ? ? 
metalc50 metalc ? ? N CA  .  CA  ? ? ? 1_555 R HOH . O  ? ? D CA  302 D HOH 401 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc51 metalc ? ? N CA  .  CA  ? ? ? 1_555 R HOH . O  ? ? D CA  302 D HOH 406 1_555 ? ? ? ? ? ? ? 2.727 ? ? 
# 
_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 301 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 90.6  ? 
2   OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 167.4 ? 
3   OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 OD1 ? A ASP 19 ? A ASP 19  ? 1_555 102.0 ? 
4   OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 93.9  ? 
5   OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 86.6  ? 
6   OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 NE2 ? A HIS 24 ? A HIS 24  ? 1_555 88.1  ? 
7   OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 409 ? 1_555 83.9  ? 
8   OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 409 ? 1_555 90.9  ? 
9   OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 409 ? 1_555 94.6  ? 
10  NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 409 ? 1_555 176.6 ? 
11  OE2 ? A GLU 8  ? A GLU 8   ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 411 ? 1_555 82.1  ? 
12  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 411 ? 1_555 172.7 ? 
13  OD1 ? A ASP 19 ? A ASP 19  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 411 ? 1_555 85.3  ? 
14  NE2 ? A HIS 24 ? A HIS 24  ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 411 ? 1_555 94.1  ? 
15  O   ? O HOH .  ? A HOH 409 ? 1_555 MN ? E MN . ? A MN 301 ? 1_555 O   ? O HOH .  ? A HOH 411 ? 1_555 88.1  ? 
16  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD2 ? A ASP 10 ? A ASP 10  ? 1_555 51.9  ? 
17  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 77.9  ? 
18  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? A TYR 12 ? A TYR 12  ? 1_555 111.8 ? 
19  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 146.1 ? 
20  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 161.9 ? 
21  O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD1 ? A ASN 14 ? A ASN 14  ? 1_555 78.1  ? 
22  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 109.5 ? 
23  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 76.6  ? 
24  O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 81.8  ? 
25  OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 OD2 ? A ASP 19 ? A ASP 19  ? 1_555 90.4  ? 
26  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 406 ? 1_555 75.1  ? 
27  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 406 ? 1_555 110.6 ? 
28  O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 406 ? 1_555 93.7  ? 
29  OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 406 ? 1_555 82.9  ? 
30  OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 406 ? 1_555 172.6 ? 
31  OD1 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 108.1 ? 
32  OD2 ? A ASP 10 ? A ASP 10  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 71.0  ? 
33  O   ? A TYR 12 ? A TYR 12  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 173.2 ? 
34  OD1 ? A ASN 14 ? A ASN 14  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 97.6  ? 
35  OD2 ? A ASP 19 ? A ASP 19  ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 93.0  ? 
36  O   ? O HOH .  ? A HOH 406 ? 1_555 CA ? F CA . ? A CA 302 ? 1_555 O   ? O HOH .  ? A HOH 413 ? 1_555 90.9  ? 
37  OE1 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 98.0  ? 
38  OE1 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 166.9 ? 
39  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 OD1 ? B ASP 19 ? B ASP 19  ? 1_555 94.7  ? 
40  OE1 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 91.3  ? 
41  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 89.0  ? 
42  OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 NE2 ? B HIS 24 ? B HIS 24  ? 1_555 92.2  ? 
43  OE1 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 401 ? 1_555 82.4  ? 
44  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 401 ? 1_555 175.5 ? 
45  OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 401 ? 1_555 85.3  ? 
46  NE2 ? B HIS 24 ? B HIS 24  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 401 ? 1_555 86.5  ? 
47  OE1 ? B GLU 8  ? B GLU 8   ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 408 ? 1_555 88.8  ? 
48  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 408 ? 1_555 94.5  ? 
49  OD1 ? B ASP 19 ? B ASP 19  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 408 ? 1_555 87.0  ? 
50  NE2 ? B HIS 24 ? B HIS 24  ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 408 ? 1_555 176.5 ? 
51  O   ? P HOH .  ? B HOH 401 ? 1_555 MN ? H MN . ? B MN 302 ? 1_555 O   ? P HOH .  ? B HOH 408 ? 1_555 90.1  ? 
52  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD2 ? B ASP 10 ? B ASP 10  ? 1_555 54.6  ? 
53  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? B TYR 12 ? B TYR 12  ? 1_555 78.8  ? 
54  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? B TYR 12 ? B TYR 12  ? 1_555 112.9 ? 
55  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 151.1 ? 
56  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 154.2 ? 
57  O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD1 ? B ASN 14 ? B ASN 14  ? 1_555 83.6  ? 
58  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 111.5 ? 
59  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 72.4  ? 
60  O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 86.4  ? 
61  OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 OD2 ? B ASP 19 ? B ASP 19  ? 1_555 89.8  ? 
62  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 407 ? 1_555 115.4 ? 
63  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 407 ? 1_555 76.5  ? 
64  O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 407 ? 1_555 165.7 ? 
65  OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 407 ? 1_555 84.1  ? 
66  OD2 ? B ASP 19 ? B ASP 19  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 407 ? 1_555 86.5  ? 
67  OD1 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 73.5  ? 
68  OD2 ? B ASP 10 ? B ASP 10  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 113.1 ? 
69  O   ? B TYR 12 ? B TYR 12  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 92.1  ? 
70  OD1 ? B ASN 14 ? B ASN 14  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 84.7  ? 
71  OD2 ? B ASP 19 ? B ASP 19  ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 174.4 ? 
72  O   ? P HOH .  ? B HOH 407 ? 1_555 CA ? I CA . ? B CA 303 ? 1_555 O   ? P HOH .  ? B HOH 409 ? 1_555 93.8  ? 
73  OE2 ? C GLU 8  ? C GLU 8   ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 OD2 ? C ASP 10 ? C ASP 10  ? 1_555 96.8  ? 
74  OE2 ? C GLU 8  ? C GLU 8   ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 OD1 ? C ASP 19 ? C ASP 19  ? 1_555 165.9 ? 
75  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 OD1 ? C ASP 19 ? C ASP 19  ? 1_555 97.2  ? 
76  OE2 ? C GLU 8  ? C GLU 8   ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 NE2 ? C HIS 24 ? C HIS 24  ? 1_555 92.6  ? 
77  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 NE2 ? C HIS 24 ? C HIS 24  ? 1_555 84.8  ? 
78  OD1 ? C ASP 19 ? C ASP 19  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 NE2 ? C HIS 24 ? C HIS 24  ? 1_555 90.2  ? 
79  OE2 ? C GLU 8  ? C GLU 8   ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 406 ? 1_555 89.4  ? 
80  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 406 ? 1_555 95.8  ? 
81  OD1 ? C ASP 19 ? C ASP 19  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 406 ? 1_555 87.7  ? 
82  NE2 ? C HIS 24 ? C HIS 24  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 406 ? 1_555 177.9 ? 
83  OE2 ? C GLU 8  ? C GLU 8   ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 409 ? 1_555 86.0  ? 
84  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 409 ? 1_555 175.0 ? 
85  OD1 ? C ASP 19 ? C ASP 19  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 409 ? 1_555 80.1  ? 
86  NE2 ? C HIS 24 ? C HIS 24  ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 409 ? 1_555 91.0  ? 
87  O   ? Q HOH .  ? C HOH 406 ? 1_555 MN ? K MN . ? C MN 302 ? 1_555 O   ? Q HOH .  ? C HOH 409 ? 1_555 88.4  ? 
88  OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD2 ? C ASP 10 ? C ASP 10  ? 1_555 51.7  ? 
89  OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? C TYR 12 ? C TYR 12  ? 1_555 83.4  ? 
90  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? C TYR 12 ? C TYR 12  ? 1_555 115.7 ? 
91  OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD1 ? C ASN 14 ? C ASN 14  ? 1_555 150.2 ? 
92  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD1 ? C ASN 14 ? C ASN 14  ? 1_555 158.1 ? 
93  O   ? C TYR 12 ? C TYR 12  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD1 ? C ASN 14 ? C ASN 14  ? 1_555 77.1  ? 
94  OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 111.0 ? 
95  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 74.9  ? 
96  O   ? C TYR 12 ? C TYR 12  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 84.6  ? 
97  OD1 ? C ASN 14 ? C ASN 14  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 89.4  ? 
98  OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 410 ? 1_555 110.5 ? 
99  OD2 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 410 ? 1_555 75.9  ? 
100 O   ? C TYR 12 ? C TYR 12  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 410 ? 1_555 166.0 ? 
101 OD1 ? C ASN 14 ? C ASN 14  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 410 ? 1_555 89.5  ? 
102 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 410 ? 1_555 91.4  ? 
103 OD1 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 75.2  ? 
104 OD2 ? C ASP 10 ? C ASP 10  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 112.0 ? 
105 O   ? C TYR 12 ? C TYR 12  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 93.0  ? 
106 OD1 ? C ASN 14 ? C ASN 14  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 83.6  ? 
107 OD2 ? C ASP 19 ? C ASP 19  ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 172.9 ? 
108 O   ? Q HOH .  ? C HOH 410 ? 1_555 CA ? L CA . ? C CA 303 ? 1_555 O   ? Q HOH .  ? C HOH 414 ? 1_555 89.3  ? 
109 OE2 ? D GLU 8  ? D GLU 8   ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 93.7  ? 
110 OE2 ? D GLU 8  ? D GLU 8   ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 OD1 ? D ASP 19 ? D ASP 19  ? 1_555 171.0 ? 
111 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 OD1 ? D ASP 19 ? D ASP 19  ? 1_555 94.0  ? 
112 OE2 ? D GLU 8  ? D GLU 8   ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 NE2 ? D HIS 24 ? D HIS 24  ? 1_555 94.0  ? 
113 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 NE2 ? D HIS 24 ? D HIS 24  ? 1_555 84.6  ? 
114 OD1 ? D ASP 19 ? D ASP 19  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 NE2 ? D HIS 24 ? D HIS 24  ? 1_555 91.4  ? 
115 OE2 ? D GLU 8  ? D GLU 8   ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 O   ? R HOH .  ? D HOH 404 ? 1_555 85.3  ? 
116 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 O   ? R HOH .  ? D HOH 404 ? 1_555 172.9 ? 
117 OD1 ? D ASP 19 ? D ASP 19  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 O   ? R HOH .  ? D HOH 404 ? 1_555 87.6  ? 
118 NE2 ? D HIS 24 ? D HIS 24  ? 1_555 MN ? M MN . ? D MN 301 ? 1_555 O   ? R HOH .  ? D HOH 404 ? 1_555 88.4  ? 
119 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 53.1  ? 
120 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? D TYR 12 ? D TYR 12  ? 1_555 77.6  ? 
121 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? D TYR 12 ? D TYR 12  ? 1_555 105.8 ? 
122 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 150.2 ? 
123 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 155.8 ? 
124 O   ? D TYR 12 ? D TYR 12  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 82.2  ? 
125 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 105.5 ? 
126 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 67.5  ? 
127 O   ? D TYR 12 ? D TYR 12  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 79.9  ? 
128 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 92.2  ? 
129 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 401 ? 1_555 77.1  ? 
130 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 401 ? 1_555 120.1 ? 
131 O   ? D TYR 12 ? D TYR 12  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 401 ? 1_555 91.5  ? 
132 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 401 ? 1_555 81.8  ? 
133 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 401 ? 1_555 170.1 ? 
134 OD1 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 109.2 ? 
135 OD2 ? D ASP 10 ? D ASP 10  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 65.6  ? 
136 O   ? D TYR 12 ? D TYR 12  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 156.8 ? 
137 OD1 ? D ASN 14 ? D ASN 14  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 97.9  ? 
138 OD2 ? D ASP 19 ? D ASP 19  ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 76.9  ? 
139 O   ? R HOH .  ? D HOH 401 ? 1_555 CA ? N CA . ? D CA 302 ? 1_555 O   ? R HOH .  ? D HOH 406 ? 1_555 111.6 ? 
# 
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 2.93  
2 ALA 207 B . ? ALA 207 B ASP 208 B ? ASP 208 B 1 6.35  
3 ALA 207 C . ? ALA 207 C ASP 208 C ? ASP 208 C 1 -0.69 
4 ALA 207 D . ? ALA 207 D ASP 208 D ? ASP 208 D 1 9.46  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7  ? 
AA2 ? 6  ? 
AA3 ? 12 ? 
AA4 ? 8  ? 
AA5 ? 2  ? 
AA6 ? 7  ? 
AA7 ? 6  ? 
AA8 ? 6  ? 
AA9 ? 7  ? 
AB1 ? 2  ? 
AB2 ? 7  ? 
AB3 ? 6  ? 
AB4 ? 6  ? 
AB5 ? 7  ? 
AB6 ? 2  ? 
AB7 ? 7  ? 
AB8 ? 6  ? 
AB9 ? 2  ? 
# 
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 
AA3 6  7  ? anti-parallel 
AA3 7  8  ? anti-parallel 
AA3 8  9  ? anti-parallel 
AA3 9  10 ? anti-parallel 
AA3 10 11 ? anti-parallel 
AA3 11 12 ? 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 
AA4 7  8  ? anti-parallel 
AA5 1  2  ? anti-parallel 
AA6 1  2  ? anti-parallel 
AA6 2  3  ? anti-parallel 
AA6 3  4  ? anti-parallel 
AA6 4  5  ? anti-parallel 
AA6 5  6  ? anti-parallel 
AA6 6  7  ? anti-parallel 
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 
AA9 1  2  ? anti-parallel 
AA9 2  3  ? anti-parallel 
AA9 3  4  ? anti-parallel 
AA9 4  5  ? anti-parallel 
AA9 5  6  ? anti-parallel 
AA9 6  7  ? anti-parallel 
AB1 1  2  ? anti-parallel 
AB2 1  2  ? anti-parallel 
AB2 2  3  ? anti-parallel 
AB2 3  4  ? anti-parallel 
AB2 4  5  ? anti-parallel 
AB2 5  6  ? anti-parallel 
AB2 6  7  ? anti-parallel 
AB3 1  2  ? anti-parallel 
AB3 2  3  ? anti-parallel 
AB3 3  4  ? anti-parallel 
AB3 4  5  ? anti-parallel 
AB3 5  6  ? anti-parallel 
AB4 1  2  ? anti-parallel 
AB4 2  3  ? anti-parallel 
AB4 3  4  ? anti-parallel 
AB4 4  5  ? anti-parallel 
AB4 5  6  ? anti-parallel 
AB5 1  2  ? anti-parallel 
AB5 2  3  ? anti-parallel 
AB5 3  4  ? anti-parallel 
AB5 4  5  ? anti-parallel 
AB5 5  6  ? anti-parallel 
AB5 6  7  ? anti-parallel 
AB6 1  2  ? anti-parallel 
AB7 1  2  ? anti-parallel 
AB7 2  3  ? anti-parallel 
AB7 3  4  ? anti-parallel 
AB7 4  5  ? anti-parallel 
AB7 5  6  ? anti-parallel 
AB7 6  7  ? anti-parallel 
AB8 1  2  ? anti-parallel 
AB8 2  3  ? anti-parallel 
AB8 3  4  ? anti-parallel 
AB8 4  5  ? anti-parallel 
AB8 5  6  ? anti-parallel 
AB9 1  2  ? 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  SER A 190 ? LEU A 198 ? SER A 190 LEU A 198 
AA3 5  THR A 105 ? LYS A 116 ? THR A 105 LYS A 116 
AA3 6  THR A 123 ? PHE A 130 ? THR A 123 PHE A 130 
AA3 7  THR D 123 ? PHE D 130 ? THR D 123 PHE D 130 
AA3 8  THR D 105 ? LYS D 116 ? THR D 105 LYS D 116 
AA3 9  SER D 190 ? LEU D 198 ? SER D 190 LEU D 198 
AA3 10 VAL D 47  ? ASN D 55  ? VAL D 47  ASN D 55  
AA3 11 ARG D 60  ? SER D 66  ? ARG D 60  SER D 66  
AA3 12 ALA D 73  ? ASP D 78  ? ALA D 73  ASP D 78  
AA4 1  THR A 147 ? THR A 148 ? THR A 147 THR A 148 
AA4 2  LEU A 154 ? GLU A 155 ? LEU A 154 GLU A 155 
AA4 3  THR A 105 ? LYS A 116 ? THR A 105 LYS A 116 
AA4 4  THR A 123 ? PHE A 130 ? THR A 123 PHE A 130 
AA4 5  THR D 123 ? PHE D 130 ? THR D 123 PHE D 130 
AA4 6  THR D 105 ? LYS D 116 ? THR D 105 LYS D 116 
AA4 7  LEU D 154 ? GLU D 155 ? LEU D 154 GLU D 155 
AA4 8  THR D 147 ? THR D 148 ? THR D 147 THR D 148 
AA5 1  TRP A 182 ? SER A 184 ? TRP A 182 SER A 184 
AA5 2  VAL A 187 ? VAL A 188 ? VAL A 187 VAL A 188 
AA6 1  LYS B 36  ? LYS B 39  ? LYS B 36  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 ? SER B 215 ? GLY B 209 SER B 215 
AA6 5  TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA6 6  VAL B 170 ? PHE B 175 ? VAL B 170 PHE B 175 
AA6 7  LEU B 140 ? GLY B 144 ? LEU B 140 GLY B 144 
AA7 1  LYS B 36  ? LYS B 39  ? LYS B 36  LYS B 39  
AA7 2  HIS B 24  ? ILE B 29  ? HIS B 24  ILE B 29  
AA7 3  ILE B 4   ? ASP B 10  ? ILE B 4   ASP B 10  
AA7 4  GLY B 209 ? SER B 215 ? GLY B 209 SER B 215 
AA7 5  TRP B 88  ? SER B 96  ? TRP B 88  SER B 96  
AA7 6  VAL B 179 ? HIS B 180 ? VAL B 179 HIS B 180 
AA8 1  ALA B 73  ? ASP B 78  ? ALA B 73  ASP B 78  
AA8 2  ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA8 3  VAL B 47  ? ASN B 55  ? VAL B 47  ASN B 55  
AA8 4  SER B 190 ? LEU B 198 ? SER B 190 LEU B 198 
AA8 5  THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA8 6  THR B 123 ? PHE B 130 ? THR B 123 PHE B 130 
AA9 1  ALA B 73  ? ASP B 78  ? ALA B 73  ASP B 78  
AA9 2  ARG B 60  ? SER B 66  ? ARG B 60  SER B 66  
AA9 3  VAL B 47  ? ASN B 55  ? VAL B 47  ASN B 55  
AA9 4  SER B 190 ? LEU B 198 ? SER B 190 LEU B 198 
AA9 5  THR B 105 ? LYS B 116 ? THR B 105 LYS B 116 
AA9 6  LEU B 154 ? GLU B 155 ? LEU B 154 GLU B 155 
AA9 7  THR B 147 ? THR B 148 ? THR B 147 THR B 148 
AB1 1  TRP B 182 ? SER B 184 ? TRP B 182 SER B 184 
AB1 2  VAL B 187 ? VAL B 188 ? VAL B 187 VAL B 188 
AB2 1  LYS C 36  ? LYS C 39  ? LYS C 36  LYS C 39  
AB2 2  HIS C 24  ? ILE C 29  ? HIS C 24  ILE C 29  
AB2 3  ILE C 4   ? ASP C 10  ? ILE C 4   ASP C 10  
AB2 4  GLY C 209 ? SER C 215 ? GLY C 209 SER C 215 
AB2 5  TRP C 88  ? SER C 96  ? TRP C 88  SER C 96  
AB2 6  VAL C 170 ? PHE C 175 ? VAL C 170 PHE C 175 
AB2 7  LEU C 140 ? GLY C 144 ? LEU C 140 GLY C 144 
AB3 1  LYS C 36  ? LYS C 39  ? LYS C 36  LYS C 39  
AB3 2  HIS C 24  ? ILE C 29  ? HIS C 24  ILE C 29  
AB3 3  ILE C 4   ? ASP C 10  ? ILE C 4   ASP C 10  
AB3 4  GLY C 209 ? SER C 215 ? GLY C 209 SER C 215 
AB3 5  TRP C 88  ? SER C 96  ? TRP C 88  SER C 96  
AB3 6  VAL C 179 ? HIS C 180 ? VAL C 179 HIS C 180 
AB4 1  ALA C 73  ? ASP C 78  ? ALA C 73  ASP C 78  
AB4 2  ARG C 60  ? SER C 66  ? ARG C 60  SER C 66  
AB4 3  VAL C 47  ? ASN C 55  ? VAL C 47  ASN C 55  
AB4 4  SER C 190 ? LEU C 198 ? SER C 190 LEU C 198 
AB4 5  THR C 105 ? LYS C 116 ? THR C 105 LYS C 116 
AB4 6  THR C 123 ? PHE C 130 ? THR C 123 PHE C 130 
AB5 1  ALA C 73  ? ASP C 78  ? ALA C 73  ASP C 78  
AB5 2  ARG C 60  ? SER C 66  ? ARG C 60  SER C 66  
AB5 3  VAL C 47  ? ASN C 55  ? VAL C 47  ASN C 55  
AB5 4  SER C 190 ? LEU C 198 ? SER C 190 LEU C 198 
AB5 5  THR C 105 ? LYS C 116 ? THR C 105 LYS C 116 
AB5 6  LEU C 154 ? GLU C 155 ? LEU C 154 GLU C 155 
AB5 7  THR C 147 ? THR C 148 ? THR C 147 THR C 148 
AB6 1  TRP C 182 ? SER C 184 ? TRP C 182 SER C 184 
AB6 2  VAL C 187 ? VAL C 188 ? VAL C 187 VAL C 188 
AB7 1  LYS D 36  ? LYS D 39  ? LYS D 36  LYS D 39  
AB7 2  HIS D 24  ? ILE D 29  ? HIS D 24  ILE D 29  
AB7 3  ILE D 4   ? ASP D 10  ? ILE D 4   ASP D 10  
AB7 4  GLY D 209 ? SER D 215 ? GLY D 209 SER D 215 
AB7 5  TRP D 88  ? THR D 97  ? TRP D 88  THR D 97  
AB7 6  SER D 169 ? PHE D 175 ? SER D 169 PHE D 175 
AB7 7  LEU D 140 ? GLY D 144 ? LEU D 140 GLY D 144 
AB8 1  LYS D 36  ? LYS D 39  ? LYS D 36  LYS D 39  
AB8 2  HIS D 24  ? ILE D 29  ? HIS D 24  ILE D 29  
AB8 3  ILE D 4   ? ASP D 10  ? ILE D 4   ASP D 10  
AB8 4  GLY D 209 ? SER D 215 ? GLY D 209 SER D 215 
AB8 5  TRP D 88  ? THR D 97  ? TRP D 88  THR D 97  
AB8 6  VAL D 179 ? HIS D 180 ? VAL D 179 HIS D 180 
AB9 1  TRP D 182 ? GLU D 183 ? TRP D 182 GLU D 183 
AB9 2  VAL D 187 ? VAL D 188 ? VAL D 187 VAL D 188 
# 
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 ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA1 2  3  O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA1 3  4  N LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
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 LEU A 174 ? O LEU A 174 N ILE A 141 ? N ILE A 141 
AA2 1  2  O ALA A 38  ? O ALA A 38  N ILE A 25  ? N ILE A 25  
AA2 2  3  O ASP A 28  ? O ASP A 28  N ALA A 6   ? N ALA A 6   
AA2 3  4  N LEU A 9   ? N LEU A 9   O ILE A 210 ? O ILE A 210 
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 TYR A 77  ? O TYR A 77  N LEU A 61  ? N LEU A 61  
AA3 2  3  O SER A 62  ? O SER A 62  N ILE A 53  ? N ILE A 53  
AA3 3  4  N ILE A 52  ? N ILE A 52  O ALA A 193 ? O ALA A 193 
AA3 4  5  O GLU A 192 ? O GLU A 192 N THR A 112 ? N THR A 112 
AA3 5  6  N LEU A 115 ? N LEU A 115 O ASN A 124 ? O ASN A 124 
AA3 6  7  N HIS A 127 ? N HIS A 127 O HIS D 127 ? O HIS D 127 
AA3 7  8  O PHE D 130 ? O PHE D 130 N TRP D 109 ? N TRP D 109 
AA3 8  9  N SER D 110 ? N SER D 110 O THR D 194 ? O THR D 194 
AA3 9  10 O PHE D 197 ? O PHE D 197 N GLY D 48  ? N GLY D 48  
AA3 10 11 N ILE D 53  ? N ILE D 53  O SER D 62  ? O SER D 62  
AA3 11 12 N VAL D 65  ? N VAL D 65  O ALA D 73  ? O ALA D 73  
AA4 1  2  N THR A 147 ? N THR A 147 O GLU A 155 ? O GLU A 155 
AA4 2  3  O LEU A 154 ? O LEU A 154 N ILE A 106 ? N ILE A 106 
AA4 3  4  N LEU A 115 ? N LEU A 115 O ASN A 124 ? O ASN A 124 
AA4 4  5  N HIS A 127 ? N HIS A 127 O HIS D 127 ? O HIS D 127 
AA4 5  6  O PHE D 130 ? O PHE D 130 N TRP D 109 ? N TRP D 109 
AA4 6  7  N ILE D 106 ? N ILE D 106 O LEU D 154 ? O LEU D 154 
AA4 7  8  O GLU D 155 ? O GLU D 155 N THR D 147 ? N THR D 147 
AA5 1  2  N GLU A 183 ? N GLU A 183 O VAL A 187 ? O VAL A 187 
AA6 1  2  O LYS B 36  ? O LYS B 36  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 LEU B 9   ? N LEU B 9   O ILE B 210 ? O ILE B 210 
AA6 4  5  O PHE B 213 ? O PHE B 213 N GLY B 92  ? N GLY B 92  
AA6 5  6  N LEU B 93  ? N LEU B 93  O ALA B 173 ? O ALA B 173 
AA6 6  7  O LEU B 174 ? O LEU B 174 N ILE B 141 ? N ILE B 141 
AA7 1  2  O LYS B 36  ? O LYS B 36  N ILE B 27  ? N ILE B 27  
AA7 2  3  O ASP B 28  ? O ASP B 28  N ALA B 6   ? N ALA B 6   
AA7 3  4  N LEU B 9   ? N LEU B 9   O ILE B 210 ? O ILE B 210 
AA7 4  5  O PHE B 213 ? O PHE B 213 N GLY B 92  ? N GLY B 92  
AA7 5  6  N VAL B 89  ? N VAL B 89  O VAL B 179 ? O VAL B 179 
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 ALA B 50  ? N ALA B 50  O PHE B 195 ? O PHE B 195 
AA8 4  5  O THR B 194 ? O THR B 194 N SER B 110 ? N SER B 110 
AA8 5  6  N LEU B 115 ? N LEU B 115 O ASN B 124 ? O ASN B 124 
AA9 1  2  O ALA B 73  ? O ALA B 73  N VAL B 65  ? N VAL B 65  
AA9 2  3  O SER B 62  ? O SER B 62  N ILE B 53  ? N ILE B 53  
AA9 3  4  N ALA B 50  ? N ALA B 50  O PHE B 195 ? O PHE B 195 
AA9 4  5  O THR B 194 ? O THR B 194 N SER B 110 ? N SER B 110 
AA9 5  6  N ILE B 106 ? N ILE B 106 O LEU B 154 ? O LEU B 154 
AA9 6  7  O GLU B 155 ? O GLU B 155 N THR B 147 ? N THR B 147 
AB1 1  2  N GLU B 183 ? N GLU B 183 O VAL B 187 ? O VAL B 187 
AB2 1  2  O ALA C 38  ? O ALA C 38  N ILE C 25  ? N ILE C 25  
AB2 2  3  O ASP C 28  ? O ASP C 28  N ALA C 6   ? N ALA C 6   
AB2 3  4  N LEU C 9   ? N LEU C 9   O ILE C 210 ? O ILE C 210 
AB2 4  5  O ALA C 211 ? O ALA C 211 N SER C 94  ? N SER C 94  
AB2 5  6  N VAL C 91  ? N VAL C 91  O PHE C 175 ? O PHE C 175 
AB2 6  7  O LEU C 174 ? O LEU C 174 N ILE C 141 ? N ILE C 141 
AB3 1  2  O ALA C 38  ? O ALA C 38  N ILE C 25  ? N ILE C 25  
AB3 2  3  O ASP C 28  ? O ASP C 28  N ALA C 6   ? N ALA C 6   
AB3 3  4  N LEU C 9   ? N LEU C 9   O ILE C 210 ? O ILE C 210 
AB3 4  5  O ALA C 211 ? O ALA C 211 N SER C 94  ? N SER C 94  
AB3 5  6  N VAL C 89  ? N VAL C 89  O VAL C 179 ? O VAL C 179 
AB4 1  2  O ALA C 73  ? O ALA C 73  N VAL C 65  ? N VAL C 65  
AB4 2  3  O SER C 62  ? O SER C 62  N ILE C 53  ? N ILE C 53  
AB4 3  4  N ILE C 52  ? N ILE C 52  O ALA C 193 ? O ALA C 193 
AB4 4  5  O THR C 194 ? O THR C 194 N SER C 110 ? N SER C 110 
AB4 5  6  N LEU C 115 ? N LEU C 115 O ASN C 124 ? O ASN C 124 
AB5 1  2  O ALA C 73  ? O ALA C 73  N VAL C 65  ? N VAL C 65  
AB5 2  3  O SER C 62  ? O SER C 62  N ILE C 53  ? N ILE C 53  
AB5 3  4  N ILE C 52  ? N ILE C 52  O ALA C 193 ? O ALA C 193 
AB5 4  5  O THR C 194 ? O THR C 194 N SER C 110 ? N SER C 110 
AB5 5  6  N ILE C 106 ? N ILE C 106 O LEU C 154 ? O LEU C 154 
AB5 6  7  O GLU C 155 ? O GLU C 155 N THR C 147 ? N THR C 147 
AB6 1  2  N GLU C 183 ? N GLU C 183 O VAL C 187 ? O VAL C 187 
AB7 1  2  O ALA D 38  ? O ALA D 38  N ILE D 25  ? N ILE D 25  
AB7 2  3  O ASP D 28  ? O ASP D 28  N ALA D 6   ? N ALA D 6   
AB7 3  4  N LEU D 9   ? N LEU D 9   O ILE D 210 ? O ILE D 210 
AB7 4  5  O SER D 215 ? O SER D 215 N ARG D 90  ? N ARG D 90  
AB7 5  6  N LEU D 93  ? N LEU D 93  O ALA D 173 ? O ALA D 173 
AB7 6  7  O LEU D 174 ? O LEU D 174 N ILE D 141 ? N ILE D 141 
AB8 1  2  O ALA D 38  ? O ALA D 38  N ILE D 25  ? N ILE D 25  
AB8 2  3  O ASP D 28  ? O ASP D 28  N ALA D 6   ? N ALA D 6   
AB8 3  4  N LEU D 9   ? N LEU D 9   O ILE D 210 ? O ILE D 210 
AB8 4  5  O SER D 215 ? O SER D 215 N ARG D 90  ? N ARG D 90  
AB8 5  6  N VAL D 89  ? N VAL D 89  O VAL D 179 ? O VAL D 179 
AB9 1  2  N GLU D 183 ? N GLU D 183 O VAL D 187 ? O VAL D 187 
# 
_pdbx_entry_details.entry_id                   9J1F 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 VAL B 84  ? ? -123.53 -57.63 
2 1 ASN B 104 ? ? -119.19 70.74  
3 1 HIS B 121 ? ? 70.49   42.63  
4 1 ASN C 14  ? ? -103.11 76.65  
5 1 SER C 31  ? ? -171.48 142.68 
6 1 ASN C 104 ? ? -119.96 65.39  
7 1 ASN D 14  ? ? -106.15 75.93  
8 1 TYR D 77  ? ? -171.66 119.73 
# 
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 
HOH   O    O  N N 245 
HOH   H1   H  N N 246 
HOH   H2   H  N N 247 
ILE   N    N  N N 248 
ILE   CA   C  N S 249 
ILE   C    C  N N 250 
ILE   O    O  N N 251 
ILE   CB   C  N S 252 
ILE   CG1  C  N N 253 
ILE   CG2  C  N N 254 
ILE   CD1  C  N N 255 
ILE   OXT  O  N N 256 
ILE   H    H  N N 257 
ILE   H2   H  N N 258 
ILE   HA   H  N N 259 
ILE   HB   H  N N 260 
ILE   HG12 H  N N 261 
ILE   HG13 H  N N 262 
ILE   HG21 H  N N 263 
ILE   HG22 H  N N 264 
ILE   HG23 H  N N 265 
ILE   HD11 H  N N 266 
ILE   HD12 H  N N 267 
ILE   HD13 H  N N 268 
ILE   HXT  H  N N 269 
LEU   N    N  N N 270 
LEU   CA   C  N S 271 
LEU   C    C  N N 272 
LEU   O    O  N N 273 
LEU   CB   C  N N 274 
LEU   CG   C  N N 275 
LEU   CD1  C  N N 276 
LEU   CD2  C  N N 277 
LEU   OXT  O  N N 278 
LEU   H    H  N N 279 
LEU   H2   H  N N 280 
LEU   HA   H  N N 281 
LEU   HB2  H  N N 282 
LEU   HB3  H  N N 283 
LEU   HG   H  N N 284 
LEU   HD11 H  N N 285 
LEU   HD12 H  N N 286 
LEU   HD13 H  N N 287 
LEU   HD21 H  N N 288 
LEU   HD22 H  N N 289 
LEU   HD23 H  N N 290 
LEU   HXT  H  N N 291 
LYS   N    N  N N 292 
LYS   CA   C  N S 293 
LYS   C    C  N N 294 
LYS   O    O  N N 295 
LYS   CB   C  N N 296 
LYS   CG   C  N N 297 
LYS   CD   C  N N 298 
LYS   CE   C  N N 299 
LYS   NZ   N  N N 300 
LYS   OXT  O  N N 301 
LYS   H    H  N N 302 
LYS   H2   H  N N 303 
LYS   HA   H  N N 304 
LYS   HB2  H  N N 305 
LYS   HB3  H  N N 306 
LYS   HG2  H  N N 307 
LYS   HG3  H  N N 308 
LYS   HD2  H  N N 309 
LYS   HD3  H  N N 310 
LYS   HE2  H  N N 311 
LYS   HE3  H  N N 312 
LYS   HZ1  H  N N 313 
LYS   HZ2  H  N N 314 
LYS   HZ3  H  N N 315 
LYS   HXT  H  N N 316 
MET   N    N  N N 317 
MET   CA   C  N S 318 
MET   C    C  N N 319 
MET   O    O  N N 320 
MET   CB   C  N N 321 
MET   CG   C  N N 322 
MET   SD   S  N N 323 
MET   CE   C  N N 324 
MET   OXT  O  N N 325 
MET   H    H  N N 326 
MET   H2   H  N N 327 
MET   HA   H  N N 328 
MET   HB2  H  N N 329 
MET   HB3  H  N N 330 
MET   HG2  H  N N 331 
MET   HG3  H  N N 332 
MET   HE1  H  N N 333 
MET   HE2  H  N N 334 
MET   HE3  H  N N 335 
MET   HXT  H  N N 336 
MN    MN   MN N N 337 
PHE   N    N  N N 338 
PHE   CA   C  N S 339 
PHE   C    C  N N 340 
PHE   O    O  N N 341 
PHE   CB   C  N N 342 
PHE   CG   C  Y N 343 
PHE   CD1  C  Y N 344 
PHE   CD2  C  Y N 345 
PHE   CE1  C  Y N 346 
PHE   CE2  C  Y N 347 
PHE   CZ   C  Y N 348 
PHE   OXT  O  N N 349 
PHE   H    H  N N 350 
PHE   H2   H  N N 351 
PHE   HA   H  N N 352 
PHE   HB2  H  N N 353 
PHE   HB3  H  N N 354 
PHE   HD1  H  N N 355 
PHE   HD2  H  N N 356 
PHE   HE1  H  N N 357 
PHE   HE2  H  N N 358 
PHE   HZ   H  N N 359 
PHE   HXT  H  N N 360 
PRO   N    N  N N 361 
PRO   CA   C  N S 362 
PRO   C    C  N N 363 
PRO   O    O  N N 364 
PRO   CB   C  N N 365 
PRO   CG   C  N N 366 
PRO   CD   C  N N 367 
PRO   OXT  O  N N 368 
PRO   H    H  N N 369 
PRO   HA   H  N N 370 
PRO   HB2  H  N N 371 
PRO   HB3  H  N N 372 
PRO   HG2  H  N N 373 
PRO   HG3  H  N N 374 
PRO   HD2  H  N N 375 
PRO   HD3  H  N N 376 
PRO   HXT  H  N N 377 
SER   N    N  N N 378 
SER   CA   C  N S 379 
SER   C    C  N N 380 
SER   O    O  N N 381 
SER   CB   C  N N 382 
SER   OG   O  N N 383 
SER   OXT  O  N N 384 
SER   H    H  N N 385 
SER   H2   H  N N 386 
SER   HA   H  N N 387 
SER   HB2  H  N N 388 
SER   HB3  H  N N 389 
SER   HG   H  N N 390 
SER   HXT  H  N N 391 
THR   N    N  N N 392 
THR   CA   C  N S 393 
THR   C    C  N N 394 
THR   O    O  N N 395 
THR   CB   C  N R 396 
THR   OG1  O  N N 397 
THR   CG2  C  N N 398 
THR   OXT  O  N N 399 
THR   H    H  N N 400 
THR   H2   H  N N 401 
THR   HA   H  N N 402 
THR   HB   H  N N 403 
THR   HG1  H  N N 404 
THR   HG21 H  N N 405 
THR   HG22 H  N N 406 
THR   HG23 H  N N 407 
THR   HXT  H  N N 408 
TRP   N    N  N N 409 
TRP   CA   C  N S 410 
TRP   C    C  N N 411 
TRP   O    O  N N 412 
TRP   CB   C  N N 413 
TRP   CG   C  Y N 414 
TRP   CD1  C  Y N 415 
TRP   CD2  C  Y N 416 
TRP   NE1  N  Y N 417 
TRP   CE2  C  Y N 418 
TRP   CE3  C  Y N 419 
TRP   CZ2  C  Y N 420 
TRP   CZ3  C  Y N 421 
TRP   CH2  C  Y N 422 
TRP   OXT  O  N N 423 
TRP   H    H  N N 424 
TRP   H2   H  N N 425 
TRP   HA   H  N N 426 
TRP   HB2  H  N N 427 
TRP   HB3  H  N N 428 
TRP   HD1  H  N N 429 
TRP   HE1  H  N N 430 
TRP   HE3  H  N N 431 
TRP   HZ2  H  N N 432 
TRP   HZ3  H  N N 433 
TRP   HH2  H  N N 434 
TRP   HXT  H  N N 435 
TYR   N    N  N N 436 
TYR   CA   C  N S 437 
TYR   C    C  N N 438 
TYR   O    O  N N 439 
TYR   CB   C  N N 440 
TYR   CG   C  Y N 441 
TYR   CD1  C  Y N 442 
TYR   CD2  C  Y N 443 
TYR   CE1  C  Y N 444 
TYR   CE2  C  Y N 445 
TYR   CZ   C  Y N 446 
TYR   OH   O  N N 447 
TYR   OXT  O  N N 448 
TYR   H    H  N N 449 
TYR   H2   H  N N 450 
TYR   HA   H  N N 451 
TYR   HB2  H  N N 452 
TYR   HB3  H  N N 453 
TYR   HD1  H  N N 454 
TYR   HD2  H  N N 455 
TYR   HE1  H  N N 456 
TYR   HE2  H  N N 457 
TYR   HH   H  N N 458 
TYR   HXT  H  N N 459 
VAL   N    N  N N 460 
VAL   CA   C  N S 461 
VAL   C    C  N N 462 
VAL   O    O  N N 463 
VAL   CB   C  N N 464 
VAL   CG1  C  N N 465 
VAL   CG2  C  N N 466 
VAL   OXT  O  N N 467 
VAL   H    H  N N 468 
VAL   H2   H  N N 469 
VAL   HA   H  N N 470 
VAL   HB   H  N N 471 
VAL   HG11 H  N N 472 
VAL   HG12 H  N N 473 
VAL   HG13 H  N N 474 
VAL   HG21 H  N N 475 
VAL   HG22 H  N N 476 
VAL   HG23 H  N N 477 
VAL   HXT  H  N N 478 
# 
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 
HOH   O    H1   sing N N 241 
HOH   O    H2   sing N N 242 
ILE   N    CA   sing N N 243 
ILE   N    H    sing N N 244 
ILE   N    H2   sing N N 245 
ILE   CA   C    sing N N 246 
ILE   CA   CB   sing N N 247 
ILE   CA   HA   sing N N 248 
ILE   C    O    doub N N 249 
ILE   C    OXT  sing N N 250 
ILE   CB   CG1  sing N N 251 
ILE   CB   CG2  sing N N 252 
ILE   CB   HB   sing N N 253 
ILE   CG1  CD1  sing N N 254 
ILE   CG1  HG12 sing N N 255 
ILE   CG1  HG13 sing N N 256 
ILE   CG2  HG21 sing N N 257 
ILE   CG2  HG22 sing N N 258 
ILE   CG2  HG23 sing N N 259 
ILE   CD1  HD11 sing N N 260 
ILE   CD1  HD12 sing N N 261 
ILE   CD1  HD13 sing N N 262 
ILE   OXT  HXT  sing N N 263 
LEU   N    CA   sing N N 264 
LEU   N    H    sing N N 265 
LEU   N    H2   sing N N 266 
LEU   CA   C    sing N N 267 
LEU   CA   CB   sing N N 268 
LEU   CA   HA   sing N N 269 
LEU   C    O    doub N N 270 
LEU   C    OXT  sing N N 271 
LEU   CB   CG   sing N N 272 
LEU   CB   HB2  sing N N 273 
LEU   CB   HB3  sing N N 274 
LEU   CG   CD1  sing N N 275 
LEU   CG   CD2  sing N N 276 
LEU   CG   HG   sing N N 277 
LEU   CD1  HD11 sing N N 278 
LEU   CD1  HD12 sing N N 279 
LEU   CD1  HD13 sing N N 280 
LEU   CD2  HD21 sing N N 281 
LEU   CD2  HD22 sing N N 282 
LEU   CD2  HD23 sing N N 283 
LEU   OXT  HXT  sing N N 284 
LYS   N    CA   sing N N 285 
LYS   N    H    sing N N 286 
LYS   N    H2   sing N N 287 
LYS   CA   C    sing N N 288 
LYS   CA   CB   sing N N 289 
LYS   CA   HA   sing N N 290 
LYS   C    O    doub N N 291 
LYS   C    OXT  sing N N 292 
LYS   CB   CG   sing N N 293 
LYS   CB   HB2  sing N N 294 
LYS   CB   HB3  sing N N 295 
LYS   CG   CD   sing N N 296 
LYS   CG   HG2  sing N N 297 
LYS   CG   HG3  sing N N 298 
LYS   CD   CE   sing N N 299 
LYS   CD   HD2  sing N N 300 
LYS   CD   HD3  sing N N 301 
LYS   CE   NZ   sing N N 302 
LYS   CE   HE2  sing N N 303 
LYS   CE   HE3  sing N N 304 
LYS   NZ   HZ1  sing N N 305 
LYS   NZ   HZ2  sing N N 306 
LYS   NZ   HZ3  sing N N 307 
LYS   OXT  HXT  sing N N 308 
MET   N    CA   sing N N 309 
MET   N    H    sing N N 310 
MET   N    H2   sing N N 311 
MET   CA   C    sing N N 312 
MET   CA   CB   sing N N 313 
MET   CA   HA   sing N N 314 
MET   C    O    doub N N 315 
MET   C    OXT  sing N N 316 
MET   CB   CG   sing N N 317 
MET   CB   HB2  sing N N 318 
MET   CB   HB3  sing N N 319 
MET   CG   SD   sing N N 320 
MET   CG   HG2  sing N N 321 
MET   CG   HG3  sing N N 322 
MET   SD   CE   sing N N 323 
MET   CE   HE1  sing N N 324 
MET   CE   HE2  sing N N 325 
MET   CE   HE3  sing N N 326 
MET   OXT  HXT  sing N N 327 
PHE   N    CA   sing N N 328 
PHE   N    H    sing N N 329 
PHE   N    H2   sing N N 330 
PHE   CA   C    sing N N 331 
PHE   CA   CB   sing N N 332 
PHE   CA   HA   sing N N 333 
PHE   C    O    doub N N 334 
PHE   C    OXT  sing N N 335 
PHE   CB   CG   sing N N 336 
PHE   CB   HB2  sing N N 337 
PHE   CB   HB3  sing N N 338 
PHE   CG   CD1  doub Y N 339 
PHE   CG   CD2  sing Y N 340 
PHE   CD1  CE1  sing Y N 341 
PHE   CD1  HD1  sing N N 342 
PHE   CD2  CE2  doub Y N 343 
PHE   CD2  HD2  sing N N 344 
PHE   CE1  CZ   doub Y N 345 
PHE   CE1  HE1  sing N N 346 
PHE   CE2  CZ   sing Y N 347 
PHE   CE2  HE2  sing N N 348 
PHE   CZ   HZ   sing N N 349 
PHE   OXT  HXT  sing N N 350 
PRO   N    CA   sing N N 351 
PRO   N    CD   sing N N 352 
PRO   N    H    sing N N 353 
PRO   CA   C    sing N N 354 
PRO   CA   CB   sing N N 355 
PRO   CA   HA   sing N N 356 
PRO   C    O    doub N N 357 
PRO   C    OXT  sing N N 358 
PRO   CB   CG   sing N N 359 
PRO   CB   HB2  sing N N 360 
PRO   CB   HB3  sing N N 361 
PRO   CG   CD   sing N N 362 
PRO   CG   HG2  sing N N 363 
PRO   CG   HG3  sing N N 364 
PRO   CD   HD2  sing N N 365 
PRO   CD   HD3  sing N N 366 
PRO   OXT  HXT  sing N N 367 
SER   N    CA   sing N N 368 
SER   N    H    sing N N 369 
SER   N    H2   sing N N 370 
SER   CA   C    sing N N 371 
SER   CA   CB   sing N N 372 
SER   CA   HA   sing N N 373 
SER   C    O    doub N N 374 
SER   C    OXT  sing N N 375 
SER   CB   OG   sing N N 376 
SER   CB   HB2  sing N N 377 
SER   CB   HB3  sing N N 378 
SER   OG   HG   sing N N 379 
SER   OXT  HXT  sing N N 380 
THR   N    CA   sing N N 381 
THR   N    H    sing N N 382 
THR   N    H2   sing N N 383 
THR   CA   C    sing N N 384 
THR   CA   CB   sing N N 385 
THR   CA   HA   sing N N 386 
THR   C    O    doub N N 387 
THR   C    OXT  sing N N 388 
THR   CB   OG1  sing N N 389 
THR   CB   CG2  sing N N 390 
THR   CB   HB   sing N N 391 
THR   OG1  HG1  sing N N 392 
THR   CG2  HG21 sing N N 393 
THR   CG2  HG22 sing N N 394 
THR   CG2  HG23 sing N N 395 
THR   OXT  HXT  sing N N 396 
TRP   N    CA   sing N N 397 
TRP   N    H    sing N N 398 
TRP   N    H2   sing N N 399 
TRP   CA   C    sing N N 400 
TRP   CA   CB   sing N N 401 
TRP   CA   HA   sing N N 402 
TRP   C    O    doub N N 403 
TRP   C    OXT  sing N N 404 
TRP   CB   CG   sing N N 405 
TRP   CB   HB2  sing N N 406 
TRP   CB   HB3  sing N N 407 
TRP   CG   CD1  doub Y N 408 
TRP   CG   CD2  sing Y N 409 
TRP   CD1  NE1  sing Y N 410 
TRP   CD1  HD1  sing N N 411 
TRP   CD2  CE2  doub Y N 412 
TRP   CD2  CE3  sing Y N 413 
TRP   NE1  CE2  sing Y N 414 
TRP   NE1  HE1  sing N N 415 
TRP   CE2  CZ2  sing Y N 416 
TRP   CE3  CZ3  doub Y N 417 
TRP   CE3  HE3  sing N N 418 
TRP   CZ2  CH2  doub Y N 419 
TRP   CZ2  HZ2  sing N N 420 
TRP   CZ3  CH2  sing Y N 421 
TRP   CZ3  HZ3  sing N N 422 
TRP   CH2  HH2  sing N N 423 
TRP   OXT  HXT  sing N N 424 
TYR   N    CA   sing N N 425 
TYR   N    H    sing N N 426 
TYR   N    H2   sing N N 427 
TYR   CA   C    sing N N 428 
TYR   CA   CB   sing N N 429 
TYR   CA   HA   sing N N 430 
TYR   C    O    doub N N 431 
TYR   C    OXT  sing N N 432 
TYR   CB   CG   sing N N 433 
TYR   CB   HB2  sing N N 434 
TYR   CB   HB3  sing N N 435 
TYR   CG   CD1  doub Y N 436 
TYR   CG   CD2  sing Y N 437 
TYR   CD1  CE1  sing Y N 438 
TYR   CD1  HD1  sing N N 439 
TYR   CD2  CE2  doub Y N 440 
TYR   CD2  HD2  sing N N 441 
TYR   CE1  CZ   doub Y N 442 
TYR   CE1  HE1  sing N N 443 
TYR   CE2  CZ   sing Y N 444 
TYR   CE2  HE2  sing N N 445 
TYR   CZ   OH   sing N N 446 
TYR   OH   HH   sing N N 447 
TYR   OXT  HXT  sing N N 448 
VAL   N    CA   sing N N 449 
VAL   N    H    sing N N 450 
VAL   N    H2   sing N N 451 
VAL   CA   C    sing N N 452 
VAL   CA   CB   sing N N 453 
VAL   CA   HA   sing N N 454 
VAL   C    O    doub N N 455 
VAL   C    OXT  sing N N 456 
VAL   CB   CG1  sing N N 457 
VAL   CB   CG2  sing N N 458 
VAL   CB   HB   sing N N 459 
VAL   CG1  HG11 sing N N 460 
VAL   CG1  HG12 sing N N 461 
VAL   CG1  HG13 sing N N 462 
VAL   CG2  HG21 sing N N 463 
VAL   CG2  HG22 sing N N 464 
VAL   CG2  HG23 sing N N 465 
VAL   OXT  HXT  sing N N 466 
# 
_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                    9J1F 
_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]   0.012313 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006328 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012647 
_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]   0.012788 
_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   ? -12.424 -3.590  -11.821 1.00 41.02  ? 1   ALA   A N    1 
ATOM   2    C  CA   . ALA   A 1 1   ? -11.086 -4.004  -12.264 1.00 37.19  ? 1   ALA   A CA   1 
ATOM   3    C  C    . ALA   A 1 1   ? -11.195 -5.343  -13.003 1.00 36.82  ? 1   ALA   A C    1 
ATOM   4    O  O    . ALA   A 1 1   ? -12.293 -5.937  -13.068 1.00 37.09  ? 1   ALA   A O    1 
ATOM   5    C  CB   . ALA   A 1 1   ? -10.152 -4.095  -11.076 1.00 38.28  ? 1   ALA   A CB   1 
ATOM   6    N  N    . ASP   A 1 2   ? -10.078 -5.785  -13.565 1.00 33.01  ? 2   ASP   A N    1 
ATOM   7    C  CA   . ASP   A 1 2   ? -9.937  -7.132  -14.162 1.00 30.41  ? 2   ASP   A CA   1 
ATOM   8    C  C    . ASP   A 1 2   ? -9.765  -8.147  -13.024 1.00 27.66  ? 2   ASP   A C    1 
ATOM   9    O  O    . ASP   A 1 2   ? -9.343  -7.746  -11.918 1.00 26.70  ? 2   ASP   A O    1 
ATOM   10   C  CB   . ASP   A 1 2   ? -8.793  -7.143  -15.171 1.00 28.21  ? 2   ASP   A CB   1 
ATOM   11   C  CG   . ASP   A 1 2   ? -9.039  -6.212  -16.337 1.00 29.75  ? 2   ASP   A CG   1 
ATOM   12   O  OD1  . ASP   A 1 2   ? -10.234 -5.899  -16.591 1.00 27.51  ? 2   ASP   A OD1  1 
ATOM   13   O  OD2  . ASP   A 1 2   ? -8.038  -5.843  -17.005 1.00 29.43  ? 2   ASP   A OD2  1 
ATOM   14   N  N    . THR   A 1 3   ? -10.126 -9.400  -13.289 1.00 24.61  ? 3   THR   A N    1 
ATOM   15   C  CA   . THR   A 1 3   ? -9.747  -10.581 -12.475 1.00 24.83  ? 3   THR   A CA   1 
ATOM   16   C  C    . THR   A 1 3   ? -8.541  -11.252 -13.129 1.00 23.75  ? 3   THR   A C    1 
ATOM   17   O  O    . THR   A 1 3   ? -8.695  -11.757 -14.253 1.00 23.18  ? 3   THR   A O    1 
ATOM   18   C  CB   . THR   A 1 3   ? -10.915 -11.556 -12.390 1.00 26.26  ? 3   THR   A CB   1 
ATOM   19   O  OG1  . THR   A 1 3   ? -12.001 -10.792 -11.879 1.00 28.66  ? 3   THR   A OG1  1 
ATOM   20   C  CG2  . THR   A 1 3   ? -10.631 -12.738 -11.497 1.00 28.57  ? 3   THR   A CG2  1 
ATOM   21   N  N    . ILE   A 1 4   ? -7.392  -11.245 -12.461 1.00 22.37  ? 4   ILE   A N    1 
ATOM   22   C  CA   . ILE   A 1 4   ? -6.123  -11.794 -13.012 1.00 21.01  ? 4   ILE   A CA   1 
ATOM   23   C  C    . ILE   A 1 4   ? -5.661  -12.951 -12.135 1.00 19.90  ? 4   ILE   A C    1 
ATOM   24   O  O    . ILE   A 1 4   ? -5.559  -12.760 -10.913 1.00 21.86  ? 4   ILE   A O    1 
ATOM   25   C  CB   . ILE   A 1 4   ? -5.017  -10.733 -13.083 1.00 21.23  ? 4   ILE   A CB   1 
ATOM   26   C  CG1  . ILE   A 1 4   ? -5.424  -9.527  -13.932 1.00 22.69  ? 4   ILE   A CG1  1 
ATOM   27   C  CG2  . ILE   A 1 4   ? -3.729  -11.379 -13.570 1.00 20.92  ? 4   ILE   A CG2  1 
ATOM   28   C  CD1  . ILE   A 1 4   ? -5.647  -9.838  -15.399 1.00 23.78  ? 4   ILE   A CD1  1 
ATOM   29   N  N    . VAL   A 1 5   ? -5.369  -14.085 -12.764 1.00 17.58  ? 5   VAL   A N    1 
ATOM   30   C  CA   . VAL   A 1 5   ? -4.516  -15.166 -12.211 1.00 16.92  ? 5   VAL   A CA   1 
ATOM   31   C  C    . VAL   A 1 5   ? -3.255  -15.171 -13.072 1.00 16.87  ? 5   VAL   A C    1 
ATOM   32   O  O    . VAL   A 1 5   ? -3.400  -15.087 -14.308 1.00 17.42  ? 5   VAL   A O    1 
ATOM   33   C  CB   . VAL   A 1 5   ? -5.236  -16.524 -12.254 1.00 16.94  ? 5   VAL   A CB   1 
ATOM   34   C  CG1  . VAL   A 1 5   ? -4.319  -17.657 -11.826 1.00 17.33  ? 5   VAL   A CG1  1 
ATOM   35   C  CG2  . VAL   A 1 5   ? -6.509  -16.509 -11.426 1.00 17.04  ? 5   VAL   A CG2  1 
ATOM   36   N  N    . ALA   A 1 6   ? -2.069  -15.239 -12.475 1.00 15.38  ? 6   ALA   A N    1 
ATOM   37   C  CA   . ALA   A 1 6   ? -0.814  -15.131 -13.238 1.00 15.21  ? 6   ALA   A CA   1 
ATOM   38   C  C    . ALA   A 1 6   ? 0.317   -15.907 -12.592 1.00 14.29  ? 6   ALA   A C    1 
ATOM   39   O  O    . ALA   A 1 6   ? 0.367   -16.028 -11.352 1.00 15.16  ? 6   ALA   A O    1 
ATOM   40   C  CB   . ALA   A 1 6   ? -0.423  -13.675 -13.418 1.00 16.11  ? 6   ALA   A CB   1 
ATOM   41   N  N    . VAL   A 1 7   ? 1.241   -16.308 -13.450 1.00 13.90  ? 7   VAL   A N    1 
ATOM   42   C  CA   . VAL   A 1 7   ? 2.610   -16.768 -13.105 1.00 13.35  ? 7   VAL   A CA   1 
ATOM   43   C  C    . VAL   A 1 7   ? 3.593   -15.699 -13.583 1.00 13.29  ? 7   VAL   A C    1 
ATOM   44   O  O    . VAL   A 1 7   ? 3.690   -15.465 -14.855 1.00 12.41  ? 7   VAL   A O    1 
ATOM   45   C  CB   . VAL   A 1 7   ? 2.899   -18.111 -13.782 1.00 13.11  ? 7   VAL   A CB   1 
ATOM   46   C  CG1  . VAL   A 1 7   ? 4.295   -18.593 -13.433 1.00 13.41  ? 7   VAL   A CG1  1 
ATOM   47   C  CG2  . VAL   A 1 7   ? 1.850   -19.140 -13.426 1.00 13.76  ? 7   VAL   A CG2  1 
ATOM   48   N  N    . GLU   A 1 8   ? 4.295   -15.087 -12.636 1.00 13.73  ? 8   GLU   A N    1 
ATOM   49   C  CA   . GLU   A 1 8   ? 5.214   -13.948 -12.911 1.00 14.95  ? 8   GLU   A CA   1 
ATOM   50   C  C    . GLU   A 1 8   ? 6.648   -14.485 -12.913 1.00 14.24  ? 8   GLU   A C    1 
ATOM   51   O  O    . GLU   A 1 8   ? 6.964   -15.322 -12.052 1.00 14.06  ? 8   GLU   A O    1 
ATOM   52   C  CB   . GLU   A 1 8   ? 4.977   -12.823 -11.896 1.00 15.70  ? 8   GLU   A CB   1 
ATOM   53   C  CG   . GLU   A 1 8   ? 5.379   -13.147 -10.450 1.00 16.16  ? 8   GLU   A CG   1 
ATOM   54   C  CD   . GLU   A 1 8   ? 5.375   -11.954 -9.499  1.00 16.40  ? 8   GLU   A CD   1 
ATOM   55   O  OE1  . GLU   A 1 8   ? 4.353   -11.200 -9.479  1.00 15.75  ? 8   GLU   A OE1  1 
ATOM   56   O  OE2  . GLU   A 1 8   ? 6.393   -11.767 -8.765  1.00 15.30  ? 8   GLU   A OE2  1 
ATOM   57   N  N    . LEU   A 1 9   ? 7.417   -14.098 -13.921 1.00 13.81  ? 9   LEU   A N    1 
ATOM   58   C  CA   . LEU   A 1 9   ? 8.893   -14.152 -13.970 1.00 14.08  ? 9   LEU   A CA   1 
ATOM   59   C  C    . LEU   A 1 9   ? 9.356   -12.739 -13.607 1.00 14.47  ? 9   LEU   A C    1 
ATOM   60   O  O    . LEU   A 1 9   ? 9.381   -11.856 -14.475 1.00 13.55  ? 9   LEU   A O    1 
ATOM   61   C  CB   . LEU   A 1 9   ? 9.376   -14.574 -15.362 1.00 14.49  ? 9   LEU   A CB   1 
ATOM   62   C  CG   . LEU   A 1 9   ? 9.333   -16.075 -15.671 1.00 14.42  ? 9   LEU   A CG   1 
ATOM   63   C  CD1  . LEU   A 1 9   ? 7.984   -16.670 -15.379 1.00 15.13  ? 9   LEU   A CD1  1 
ATOM   64   C  CD2  . LEU   A 1 9   ? 9.698   -16.333 -17.128 1.00 15.16  ? 9   LEU   A CD2  1 
ATOM   65   N  N    . ASP   A 1 10  ? 9.640   -12.538 -12.326 1.00 14.17  ? 10  ASP   A N    1 
ATOM   66   C  CA   . ASP   A 1 10  ? 9.862   -11.206 -11.735 1.00 14.32  ? 10  ASP   A CA   1 
ATOM   67   C  C    . ASP   A 1 10  ? 11.375  -10.988 -11.610 1.00 15.41  ? 10  ASP   A C    1 
ATOM   68   O  O    . ASP   A 1 10  ? 11.993  -11.618 -10.730 1.00 14.09  ? 10  ASP   A O    1 
ATOM   69   C  CB   . ASP   A 1 10  ? 9.109   -11.121 -10.412 1.00 14.16  ? 10  ASP   A CB   1 
ATOM   70   C  CG   . ASP   A 1 10  ? 9.051   -9.724  -9.853  1.00 13.98  ? 10  ASP   A CG   1 
ATOM   71   O  OD1  . ASP   A 1 10  ? 9.884   -8.903  -10.292 1.00 13.42  ? 10  ASP   A OD1  1 
ATOM   72   O  OD2  . ASP   A 1 10  ? 8.175   -9.472  -8.982  1.00 14.10  ? 10  ASP   A OD2  1 
ATOM   73   N  N    . THR   A 1 11  ? 11.920  -10.081 -12.433 1.00 16.13  ? 11  THR   A N    1 
ATOM   74   C  CA   . THR   A 1 11  ? 13.371  -9.819  -12.569 1.00 16.76  ? 11  THR   A CA   1 
ATOM   75   C  C    . THR   A 1 11  ? 13.836  -8.855  -11.462 1.00 18.17  ? 11  THR   A C    1 
ATOM   76   O  O    . THR   A 1 11  ? 15.010  -8.949  -11.064 1.00 19.76  ? 11  THR   A O    1 
ATOM   77   C  CB   . THR   A 1 11  ? 13.711  -9.354  -13.995 1.00 16.70  ? 11  THR   A CB   1 
ATOM   78   O  OG1  . THR   A 1 11  ? 12.977  -8.199  -14.422 1.00 13.97  ? 11  THR   A OG1  1 
ATOM   79   C  CG2  . THR   A 1 11  ? 13.496  -10.465 -15.003 1.00 16.67  ? 11  THR   A CG2  1 
ATOM   80   N  N    . TYR   A 1 12  ? 12.957  -7.993  -10.957 1.00 17.40  ? 12  TYR   A N    1 
ATOM   81   C  CA   . TYR   A 1 12  ? 13.329  -6.843  -10.102 1.00 18.10  ? 12  TYR   A CA   1 
ATOM   82   C  C    . TYR   A 1 12  ? 12.713  -6.969  -8.705  1.00 18.30  ? 12  TYR   A C    1 
ATOM   83   O  O    . TYR   A 1 12  ? 11.500  -6.985  -8.520  1.00 16.97  ? 12  TYR   A O    1 
ATOM   84   C  CB   . TYR   A 1 12  ? 12.929  -5.513  -10.738 1.00 18.52  ? 12  TYR   A CB   1 
ATOM   85   C  CG   . TYR   A 1 12  ? 13.491  -4.379  -9.928  1.00 19.37  ? 12  TYR   A CG   1 
ATOM   86   C  CD1  . TYR   A 1 12  ? 14.831  -4.037  -10.026 1.00 20.33  ? 12  TYR   A CD1  1 
ATOM   87   C  CD2  . TYR   A 1 12  ? 12.732  -3.758  -8.957  1.00 19.57  ? 12  TYR   A CD2  1 
ATOM   88   C  CE1  . TYR   A 1 12  ? 15.379  -3.049  -9.227  1.00 20.63  ? 12  TYR   A CE1  1 
ATOM   89   C  CE2  . TYR   A 1 12  ? 13.267  -2.787  -8.134  1.00 20.76  ? 12  TYR   A CE2  1 
ATOM   90   C  CZ   . TYR   A 1 12  ? 14.593  -2.425  -8.280  1.00 22.20  ? 12  TYR   A CZ   1 
ATOM   91   O  OH   . TYR   A 1 12  ? 15.112  -1.443  -7.492  1.00 26.82  ? 12  TYR   A OH   1 
ATOM   92   N  N    . PRO   A 1 13  ? 13.552  -7.071  -7.659  1.00 18.38  ? 13  PRO   A N    1 
ATOM   93   C  CA   . PRO   A 1 13  ? 13.060  -7.133  -6.286  1.00 17.92  ? 13  PRO   A CA   1 
ATOM   94   C  C    . PRO   A 1 13  ? 12.471  -5.797  -5.808  1.00 17.38  ? 13  PRO   A C    1 
ATOM   95   O  O    . PRO   A 1 13  ? 13.201  -4.901  -5.541  1.00 18.49  ? 13  PRO   A O    1 
ATOM   96   C  CB   . PRO   A 1 13  ? 14.309  -7.483  -5.465  1.00 17.97  ? 13  PRO   A CB   1 
ATOM   97   C  CG   . PRO   A 1 13  ? 15.349  -7.914  -6.481  1.00 18.06  ? 13  PRO   A CG   1 
ATOM   98   C  CD   . PRO   A 1 13  ? 15.013  -7.171  -7.750  1.00 18.42  ? 13  PRO   A CD   1 
ATOM   99   N  N    . ASN   A 1 14  ? 11.144  -5.709  -5.735  1.00 17.42  ? 14  ASN   A N    1 
ATOM   100  C  CA   . ASN   A 1 14  ? 10.375  -4.594  -5.122  1.00 16.44  ? 14  ASN   A CA   1 
ATOM   101  C  C    . ASN   A 1 14  ? 10.062  -4.996  -3.670  1.00 16.86  ? 14  ASN   A C    1 
ATOM   102  O  O    . ASN   A 1 14  ? 8.912   -5.472  -3.419  1.00 17.95  ? 14  ASN   A O    1 
ATOM   103  C  CB   . ASN   A 1 14  ? 9.110   -4.289  -5.944  1.00 15.41  ? 14  ASN   A CB   1 
ATOM   104  C  CG   . ASN   A 1 14  ? 9.415   -3.900  -7.372  1.00 15.67  ? 14  ASN   A CG   1 
ATOM   105  O  OD1  . ASN   A 1 14  ? 9.468   -4.750  -8.266  1.00 14.76  ? 14  ASN   A OD1  1 
ATOM   106  N  ND2  . ASN   A 1 14  ? 9.648   -2.610  -7.601  1.00 15.78  ? 14  ASN   A ND2  1 
ATOM   107  N  N    . THR   A 1 15  ? 11.012  -4.864  -2.740  1.00 16.90  ? 15  THR   A N    1 
ATOM   108  C  CA   . THR   A 1 15  ? 10.841  -5.388  -1.353  1.00 18.84  ? 15  THR   A CA   1 
ATOM   109  C  C    . THR   A 1 15  ? 9.804   -4.568  -0.565  1.00 19.40  ? 15  THR   A C    1 
ATOM   110  O  O    . THR   A 1 15  ? 9.205   -5.128  0.348   1.00 21.22  ? 15  THR   A O    1 
ATOM   111  C  CB   . THR   A 1 15  ? 12.172  -5.536  -0.613  1.00 18.82  ? 15  THR   A CB   1 
ATOM   112  O  OG1  . THR   A 1 15  ? 12.727  -4.229  -0.519  1.00 21.51  ? 15  THR   A OG1  1 
ATOM   113  C  CG2  . THR   A 1 15  ? 13.114  -6.489  -1.309  1.00 18.03  ? 15  THR   A CG2  1 
ATOM   114  N  N    . ASP   A 1 16  ? 9.518   -3.333  -0.948  1.00 20.77  ? 16  ASP   A N    1 
ATOM   115  C  CA   . ASP   A 1 16  ? 8.489   -2.499  -0.265  1.00 22.42  ? 16  ASP   A CA   1 
ATOM   116  C  C    . ASP   A 1 16  ? 7.073   -3.038  -0.537  1.00 24.19  ? 16  ASP   A C    1 
ATOM   117  O  O    . ASP   A 1 16  ? 6.161   -2.663  0.220   1.00 26.77  ? 16  ASP   A O    1 
ATOM   118  C  CB   . ASP   A 1 16  ? 8.557   -1.041  -0.716  1.00 23.62  ? 16  ASP   A CB   1 
ATOM   119  C  CG   . ASP   A 1 16  ? 8.463   -0.918  -2.227  1.00 24.73  ? 16  ASP   A CG   1 
ATOM   120  O  OD1  . ASP   A 1 16  ? 9.086   -1.750  -2.916  1.00 25.35  ? 16  ASP   A OD1  1 
ATOM   121  O  OD2  . ASP   A 1 16  ? 7.751   -0.023  -2.698  1.00 27.73  ? 16  ASP   A OD2  1 
ATOM   122  N  N    . ILE   A 1 17  ? 6.868   -3.884  -1.548  1.00 22.85  ? 17  ILE   A N    1 
ATOM   123  C  CA   . ILE   A 1 17  ? 5.526   -4.476  -1.830  1.00 22.50  ? 17  ILE   A CA   1 
ATOM   124  C  C    . ILE   A 1 17  ? 5.610   -6.006  -1.741  1.00 22.23  ? 17  ILE   A C    1 
ATOM   125  O  O    . ILE   A 1 17  ? 4.818   -6.672  -2.403  1.00 22.13  ? 17  ILE   A O    1 
ATOM   126  C  CB   . ILE   A 1 17  ? 4.946   -3.970  -3.171  1.00 22.15  ? 17  ILE   A CB   1 
ATOM   127  C  CG1  . ILE   A 1 17  ? 5.802   -4.384  -4.366  1.00 22.86  ? 17  ILE   A CG1  1 
ATOM   128  C  CG2  . ILE   A 1 17  ? 4.746   -2.463  -3.145  1.00 22.04  ? 17  ILE   A CG2  1 
ATOM   129  C  CD1  . ILE   A 1 17  ? 5.015   -4.484  -5.655  1.00 22.79  ? 17  ILE   A CD1  1 
ATOM   130  N  N    . GLY   A 1 18  ? 6.502   -6.545  -0.902  1.00 21.62  ? 18  GLY   A N    1 
ATOM   131  C  CA   . GLY   A 1 18  ? 6.466   -7.960  -0.487  1.00 20.43  ? 18  GLY   A CA   1 
ATOM   132  C  C    . GLY   A 1 18  ? 7.226   -8.912  -1.393  1.00 20.11  ? 18  GLY   A C    1 
ATOM   133  O  O    . GLY   A 1 18  ? 7.209   -10.095 -1.069  1.00 20.22  ? 18  GLY   A O    1 
ATOM   134  N  N    . ASP   A 1 19  ? 7.856   -8.459  -2.486  1.00 19.19  ? 19  ASP   A N    1 
ATOM   135  C  CA   . ASP   A 1 19  ? 8.768   -9.319  -3.285  1.00 20.11  ? 19  ASP   A CA   1 
ATOM   136  C  C    . ASP   A 1 19  ? 9.893   -9.792  -2.365  1.00 23.24  ? 19  ASP   A C    1 
ATOM   137  O  O    . ASP   A 1 19  ? 10.331  -9.043  -1.489  1.00 23.23  ? 19  ASP   A O    1 
ATOM   138  C  CB   . ASP   A 1 19  ? 9.454   -8.595  -4.449  1.00 19.31  ? 19  ASP   A CB   1 
ATOM   139  C  CG   . ASP   A 1 19  ? 8.664   -8.477  -5.735  1.00 18.23  ? 19  ASP   A CG   1 
ATOM   140  O  OD1  . ASP   A 1 19  ? 7.649   -9.199  -5.879  1.00 19.52  ? 19  ASP   A OD1  1 
ATOM   141  O  OD2  . ASP   A 1 19  ? 9.095   -7.684  -6.609  1.00 16.32  ? 19  ASP   A OD2  1 
ATOM   142  N  N    . PRO   A 1 20  ? 10.418  -11.027 -2.537  1.00 24.39  ? 20  PRO   A N    1 
ATOM   143  C  CA   . PRO   A 1 20  ? 11.633  -11.429 -1.839  1.00 24.66  ? 20  PRO   A CA   1 
ATOM   144  C  C    . PRO   A 1 20  ? 12.758  -10.532 -2.386  1.00 24.87  ? 20  PRO   A C    1 
ATOM   145  O  O    . PRO   A 1 20  ? 12.554  -9.824  -3.342  1.00 23.64  ? 20  PRO   A O    1 
ATOM   146  C  CB   . PRO   A 1 20  ? 11.809  -12.918 -2.199  1.00 23.99  ? 20  PRO   A CB   1 
ATOM   147  C  CG   . PRO   A 1 20  ? 11.106  -13.037 -3.533  1.00 24.61  ? 20  PRO   A CG   1 
ATOM   148  C  CD   . PRO   A 1 20  ? 9.949   -12.057 -3.481  1.00 24.34  ? 20  PRO   A CD   1 
ATOM   149  N  N    . SER   A 1 21  ? 13.935  -10.606 -1.784  1.00 25.39  ? 21  SER   A N    1 
ATOM   150  C  CA   . SER   A 1 21  ? 15.069  -9.699  -2.067  1.00 25.70  ? 21  SER   A CA   1 
ATOM   151  C  C    . SER   A 1 21  ? 15.823  -10.134 -3.328  1.00 24.47  ? 21  SER   A C    1 
ATOM   152  O  O    . SER   A 1 21  ? 16.907  -9.588  -3.561  1.00 30.80  ? 21  SER   A O    1 
ATOM   153  C  CB   . SER   A 1 21  ? 15.978  -9.639  -0.872  1.00 27.32  ? 21  SER   A CB   1 
ATOM   154  O  OG   . SER   A 1 21  ? 16.413  -8.306  -0.693  1.00 33.12  ? 21  SER   A OG   1 
ATOM   155  N  N    . TYR   A 1 22  ? 15.307  -11.079 -4.115  1.00 21.39  ? 22  TYR   A N    1 
ATOM   156  C  CA   . TYR   A 1 22  ? 16.030  -11.651 -5.287  1.00 19.59  ? 22  TYR   A CA   1 
ATOM   157  C  C    . TYR   A 1 22  ? 15.078  -11.812 -6.473  1.00 18.48  ? 22  TYR   A C    1 
ATOM   158  O  O    . TYR   A 1 22  ? 13.857  -11.832 -6.311  1.00 18.42  ? 22  TYR   A O    1 
ATOM   159  C  CB   . TYR   A 1 22  ? 16.692  -12.974 -4.891  1.00 19.04  ? 22  TYR   A CB   1 
ATOM   160  C  CG   . TYR   A 1 22  ? 15.870  -13.829 -3.956  1.00 18.88  ? 22  TYR   A CG   1 
ATOM   161  C  CD1  . TYR   A 1 22  ? 14.800  -14.553 -4.428  1.00 18.96  ? 22  TYR   A CD1  1 
ATOM   162  C  CD2  . TYR   A 1 22  ? 16.164  -13.931 -2.607  1.00 19.12  ? 22  TYR   A CD2  1 
ATOM   163  C  CE1  . TYR   A 1 22  ? 14.025  -15.336 -3.593  1.00 19.62  ? 22  TYR   A CE1  1 
ATOM   164  C  CE2  . TYR   A 1 22  ? 15.409  -14.718 -1.755  1.00 18.88  ? 22  TYR   A CE2  1 
ATOM   165  C  CZ   . TYR   A 1 22  ? 14.342  -15.433 -2.253  1.00 20.40  ? 22  TYR   A CZ   1 
ATOM   166  O  OH   . TYR   A 1 22  ? 13.553  -16.206 -1.452  1.00 22.31  ? 22  TYR   A OH   1 
ATOM   167  N  N    . PRO   A 1 23  ? 15.597  -11.981 -7.705  1.00 16.67  ? 23  PRO   A N    1 
ATOM   168  C  CA   . PRO   A 1 23  ? 14.749  -12.391 -8.823  1.00 15.86  ? 23  PRO   A CA   1 
ATOM   169  C  C    . PRO   A 1 23  ? 13.984  -13.655 -8.409  1.00 15.10  ? 23  PRO   A C    1 
ATOM   170  O  O    . PRO   A 1 23  ? 14.536  -14.456 -7.662  1.00 14.20  ? 23  PRO   A O    1 
ATOM   171  C  CB   . PRO   A 1 23  ? 15.731  -12.625 -9.996  1.00 16.13  ? 23  PRO   A CB   1 
ATOM   172  C  CG   . PRO   A 1 23  ? 16.956  -11.807 -9.626  1.00 16.32  ? 23  PRO   A CG   1 
ATOM   173  C  CD   . PRO   A 1 23  ? 17.000  -11.784 -8.103  1.00 16.11  ? 23  PRO   A CD   1 
ATOM   174  N  N    . HIS   A 1 24  ? 12.735  -13.804 -8.874  1.00 14.04  ? 24  HIS   A N    1 
ATOM   175  C  CA   . HIS   A 1 24  ? 11.851  -14.908 -8.431  1.00 13.42  ? 24  HIS   A CA   1 
ATOM   176  C  C    . HIS   A 1 24  ? 10.761  -15.209 -9.462  1.00 13.58  ? 24  HIS   A C    1 
ATOM   177  O  O    . HIS   A 1 24  ? 10.394  -14.342 -10.258 1.00 13.23  ? 24  HIS   A O    1 
ATOM   178  C  CB   . HIS   A 1 24  ? 11.263  -14.571 -7.062  1.00 13.43  ? 24  HIS   A CB   1 
ATOM   179  C  CG   . HIS   A 1 24  ? 10.553  -13.258 -7.043  1.00 14.07  ? 24  HIS   A CG   1 
ATOM   180  N  ND1  . HIS   A 1 24  ? 11.237  -12.054 -7.141  1.00 13.59  ? 24  HIS   A ND1  1 
ATOM   181  C  CD2  . HIS   A 1 24  ? 9.234   -12.956 -7.016  1.00 13.65  ? 24  HIS   A CD2  1 
ATOM   182  C  CE1  . HIS   A 1 24  ? 10.360  -11.072 -7.156  1.00 14.50  ? 24  HIS   A CE1  1 
ATOM   183  N  NE2  . HIS   A 1 24  ? 9.121   -11.589 -7.059  1.00 13.39  ? 24  HIS   A NE2  1 
ATOM   184  N  N    . ILE   A 1 25  ? 10.243  -16.422 -9.403  1.00 13.66  ? 25  ILE   A N    1 
ATOM   185  C  CA   . ILE   A 1 25  ? 8.959   -16.794 -10.034 1.00 14.80  ? 25  ILE   A CA   1 
ATOM   186  C  C    . ILE   A 1 25  ? 7.919   -16.806 -8.919  1.00 14.74  ? 25  ILE   A C    1 
ATOM   187  O  O    . ILE   A 1 25  ? 8.312   -17.083 -7.734  1.00 14.18  ? 25  ILE   A O    1 
ATOM   188  C  CB   . ILE   A 1 25  ? 9.066   -18.137 -10.775 1.00 16.82  ? 25  ILE   A CB   1 
ATOM   189  C  CG1  . ILE   A 1 25  ? 9.632   -19.235 -9.878  1.00 18.13  ? 25  ILE   A CG1  1 
ATOM   190  C  CG2  . ILE   A 1 25  ? 9.899   -17.970 -12.035 1.00 17.66  ? 25  ILE   A CG2  1 
ATOM   191  C  CD1  . ILE   A 1 25  ? 9.439   -20.617 -10.449 1.00 20.19  ? 25  ILE   A CD1  1 
ATOM   192  N  N    . GLY   A 1 26  ? 6.676   -16.451 -9.276  1.00 13.46  ? 26  GLY   A N    1 
ATOM   193  C  CA   . GLY   A 1 26  ? 5.540   -16.414 -8.339  1.00 13.53  ? 26  GLY   A CA   1 
ATOM   194  C  C    . GLY   A 1 26  ? 4.205   -16.804 -8.966  1.00 13.16  ? 26  GLY   A C    1 
ATOM   195  O  O    . GLY   A 1 26  ? 4.045   -16.700 -10.211 1.00 14.26  ? 26  GLY   A O    1 
ATOM   196  N  N    . ILE   A 1 27  ? 3.250   -17.188 -8.128  1.00 12.56  ? 27  ILE   A N    1 
ATOM   197  C  CA   . ILE   A 1 27  ? 1.832   -17.363 -8.538  1.00 13.72  ? 27  ILE   A CA   1 
ATOM   198  C  C    . ILE   A 1 27  ? 1.046   -16.196 -7.950  1.00 14.02  ? 27  ILE   A C    1 
ATOM   199  O  O    . ILE   A 1 27  ? 1.146   -15.984 -6.725  1.00 15.08  ? 27  ILE   A O    1 
ATOM   200  C  CB   . ILE   A 1 27  ? 1.278   -18.733 -8.119  1.00 14.15  ? 27  ILE   A CB   1 
ATOM   201  C  CG1  . ILE   A 1 27  ? 1.932   -19.827 -8.971  1.00 14.79  ? 27  ILE   A CG1  1 
ATOM   202  C  CG2  . ILE   A 1 27  ? -0.252  -18.742 -8.232  1.00 14.19  ? 27  ILE   A CG2  1 
ATOM   203  C  CD1  . ILE   A 1 27  ? 1.816   -21.206 -8.421  1.00 15.33  ? 27  ILE   A CD1  1 
ATOM   204  N  N    . ASP   A 1 28  ? 0.350   -15.445 -8.810  1.00 14.54  ? 28  ASP   A N    1 
ATOM   205  C  CA   . ASP   A 1 28  ? -0.402  -14.210 -8.435  1.00 14.66  ? 28  ASP   A CA   1 
ATOM   206  C  C    . ASP   A 1 28  ? -1.907  -14.487 -8.592  1.00 13.84  ? 28  ASP   A C    1 
ATOM   207  O  O    . ASP   A 1 28  ? -2.352  -14.756 -9.716  1.00 13.51  ? 28  ASP   A O    1 
ATOM   208  C  CB   . ASP   A 1 28  ? 0.054   -13.004 -9.262  1.00 14.69  ? 28  ASP   A CB   1 
ATOM   209  C  CG   . ASP   A 1 28  ? 1.519   -12.619 -9.109  1.00 15.21  ? 28  ASP   A CG   1 
ATOM   210  O  OD1  . ASP   A 1 28  ? 2.120   -13.026 -8.121  1.00 16.20  ? 28  ASP   A OD1  1 
ATOM   211  O  OD2  . ASP   A 1 28  ? 2.038   -11.868 -9.971  1.00 15.22  ? 28  ASP   A OD2  1 
ATOM   212  N  N    . ILE   A 1 29  ? -2.663  -14.469 -7.500  1.00 14.14  ? 29  ILE   A N    1 
ATOM   213  C  CA   . ILE   A 1 29  ? -4.141  -14.630 -7.542  1.00 15.73  ? 29  ILE   A CA   1 
ATOM   214  C  C    . ILE   A 1 29  ? -4.770  -13.285 -7.194  1.00 16.74  ? 29  ILE   A C    1 
ATOM   215  O  O    . ILE   A 1 29  ? -4.880  -12.992 -6.010  1.00 17.25  ? 29  ILE   A O    1 
ATOM   216  C  CB   . ILE   A 1 29  ? -4.614  -15.737 -6.590  1.00 16.08  ? 29  ILE   A CB   1 
ATOM   217  C  CG1  . ILE   A 1 29  ? -3.893  -17.070 -6.823  1.00 16.37  ? 29  ILE   A CG1  1 
ATOM   218  C  CG2  . ILE   A 1 29  ? -6.131  -15.860 -6.666  1.00 16.05  ? 29  ILE   A CG2  1 
ATOM   219  C  CD1  . ILE   A 1 29  ? -3.756  -17.480 -8.270  1.00 17.18  ? 29  ILE   A CD1  1 
ATOM   220  N  N    . LYS   A 1 30  ? -5.168  -12.513 -8.210  1.00 18.89  ? 30  LYS   A N    1 
ATOM   221  C  CA   . LYS   A 1 30  ? -5.906  -11.226 -8.071  1.00 19.87  ? 30  LYS   A CA   1 
ATOM   222  C  C    . LYS   A 1 30  ? -5.066  -10.183 -7.314  1.00 20.59  ? 30  LYS   A C    1 
ATOM   223  O  O    . LYS   A 1 30  ? -5.660  -9.217  -6.781  1.00 21.59  ? 30  LYS   A O    1 
ATOM   224  C  CB   . LYS   A 1 30  ? -7.243  -11.467 -7.374  1.00 21.04  ? 30  LYS   A CB   1 
ATOM   225  C  CG   . LYS   A 1 30  ? -8.291  -12.157 -8.239  1.00 22.74  ? 30  LYS   A CG   1 
ATOM   226  C  CD   . LYS   A 1 30  ? -9.560  -12.457 -7.481  1.00 23.84  ? 30  LYS   A CD   1 
ATOM   227  C  CE   . LYS   A 1 30  ? -10.252 -11.199 -7.003  1.00 25.69  ? 30  LYS   A CE   1 
ATOM   228  N  NZ   . LYS   A 1 30  ? -11.411 -11.532 -6.144  1.00 27.73  ? 30  LYS   A NZ   1 
ATOM   229  N  N    . SER   A 1 31  ? -3.739  -10.342 -7.303  1.00 19.13  ? 31  SER   A N    1 
ATOM   230  C  CA   . SER   A 1 31  ? -2.780  -9.443  -6.618  1.00 18.70  ? 31  SER   A CA   1 
ATOM   231  C  C    . SER   A 1 31  ? -1.356  -9.683  -7.138  1.00 18.03  ? 31  SER   A C    1 
ATOM   232  O  O    . SER   A 1 31  ? -0.974  -10.841 -7.364  1.00 17.30  ? 31  SER   A O    1 
ATOM   233  C  CB   . SER   A 1 31  ? -2.831  -9.613  -5.123  1.00 18.69  ? 31  SER   A CB   1 
ATOM   234  O  OG   . SER   A 1 31  ? -1.747  -8.917  -4.519  1.00 18.60  ? 31  SER   A OG   1 
ATOM   235  N  N    . VAL   A 1 32  ? -0.591  -8.606  -7.250  1.00 17.38  ? 32  VAL   A N    1 
ATOM   236  C  CA   . VAL   A 1 32  ? 0.844   -8.632  -7.626  1.00 17.84  ? 32  VAL   A CA   1 
ATOM   237  C  C    . VAL   A 1 32  ? 1.663   -9.144  -6.427  1.00 17.02  ? 32  VAL   A C    1 
ATOM   238  O  O    . VAL   A 1 32  ? 2.827   -9.536  -6.626  1.00 17.63  ? 32  VAL   A O    1 
ATOM   239  C  CB   . VAL   A 1 32  ? 1.312   -7.244  -8.105  1.00 17.53  ? 32  VAL   A CB   1 
ATOM   240  C  CG1  . VAL   A 1 32  ? 1.719   -6.381  -6.925  1.00 17.63  ? 32  VAL   A CG1  1 
ATOM   241  C  CG2  . VAL   A 1 32  ? 2.457   -7.362  -9.090  1.00 17.94  ? 32  VAL   A CG2  1 
ATOM   242  N  N    . ARG   A 1 33  ? 1.115   -9.156  -5.219  1.00 16.85  ? 33  ARG   A N    1 
ATOM   243  C  CA   . ARG   A 1 33  ? 1.812   -9.813  -4.074  1.00 16.93  ? 33  ARG   A CA   1 
ATOM   244  C  C    . ARG   A 1 33  ? 1.595   -11.328 -4.181  1.00 16.39  ? 33  ARG   A C    1 
ATOM   245  O  O    . ARG   A 1 33  ? 0.552   -11.857 -3.687  1.00 14.53  ? 33  ARG   A O    1 
ATOM   246  C  CB   . ARG   A 1 33  ? 1.371   -9.213  -2.741  1.00 17.36  ? 33  ARG   A CB   1 
ATOM   247  C  CG   . ARG   A 1 33  ? 1.660   -7.724  -2.680  1.00 18.55  ? 33  ARG   A CG   1 
ATOM   248  C  CD   . ARG   A 1 33  ? 1.331   -7.160  -1.325  1.00 19.51  ? 33  ARG   A CD   1 
ATOM   249  N  NE   . ARG   A 1 33  ? 1.365   -5.706  -1.366  1.00 20.16  ? 33  ARG   A NE   1 
ATOM   250  C  CZ   . ARG   A 1 33  ? 2.067   -4.924  -0.553  1.00 20.05  ? 33  ARG   A CZ   1 
ATOM   251  N  NH1  . ARG   A 1 33  ? 2.836   -5.443  0.382   1.00 19.46  ? 33  ARG   A NH1  1 
ATOM   252  N  NH2  . ARG   A 1 33  ? 1.999   -3.608  -0.680  1.00 21.37  ? 33  ARG   A NH2  1 
ATOM   253  N  N    . SER   A 1 34  ? 2.569   -12.000 -4.795  1.00 15.21  ? 34  SER   A N    1 
ATOM   254  C  CA   . SER   A 1 34  ? 2.536   -13.448 -5.083  1.00 15.20  ? 34  SER   A CA   1 
ATOM   255  C  C    . SER   A 1 34  ? 2.067   -14.203 -3.840  1.00 15.65  ? 34  SER   A C    1 
ATOM   256  O  O    . SER   A 1 34  ? 2.566   -13.923 -2.759  1.00 15.90  ? 34  SER   A O    1 
ATOM   257  C  CB   . SER   A 1 34  ? 3.884   -13.928 -5.538  1.00 15.06  ? 34  SER   A CB   1 
ATOM   258  O  OG   . SER   A 1 34  ? 4.219   -13.348 -6.792  1.00 15.17  ? 34  SER   A OG   1 
ATOM   259  N  N    . LYS   A 1 35  ? 1.162   -15.154 -4.020  1.00 16.59  ? 35  LYS   A N    1 
ATOM   260  C  CA   . LYS   A 1 35  ? 0.691   -16.034 -2.936  1.00 18.12  ? 35  LYS   A CA   1 
ATOM   261  C  C    . LYS   A 1 35  ? 1.795   -17.030 -2.599  1.00 17.65  ? 35  LYS   A C    1 
ATOM   262  O  O    . LYS   A 1 35  ? 1.783   -17.513 -1.487  1.00 17.01  ? 35  LYS   A O    1 
ATOM   263  C  CB   . LYS   A 1 35  ? -0.600  -16.744 -3.336  1.00 20.04  ? 35  LYS   A CB   1 
ATOM   264  C  CG   . LYS   A 1 35  ? -1.777  -15.817 -3.639  1.00 20.76  ? 35  LYS   A CG   1 
ATOM   265  C  CD   . LYS   A 1 35  ? -2.305  -15.048 -2.432  1.00 21.26  ? 35  LYS   A CD   1 
ATOM   266  C  CE   . LYS   A 1 35  ? -3.387  -14.042 -2.797  1.00 21.77  ? 35  LYS   A CE   1 
ATOM   267  N  NZ   . LYS   A 1 35  ? -3.556  -13.000 -1.755  1.00 23.15  ? 35  LYS   A NZ   1 
ATOM   268  N  N    . LYS   A 1 36  ? 2.728   -17.259 -3.517  1.00 18.59  ? 36  LYS   A N    1 
ATOM   269  C  CA   . LYS   A 1 36  ? 3.838   -18.231 -3.368  1.00 20.24  ? 36  LYS   A CA   1 
ATOM   270  C  C    . LYS   A 1 36  ? 4.950   -17.858 -4.355  1.00 18.99  ? 36  LYS   A C    1 
ATOM   271  O  O    . LYS   A 1 36  ? 4.623   -17.488 -5.506  1.00 17.19  ? 36  LYS   A O    1 
ATOM   272  C  CB   . LYS   A 1 36  ? 3.304   -19.638 -3.646  1.00 24.42  ? 36  LYS   A CB   1 
ATOM   273  C  CG   . LYS   A 1 36  ? 4.114   -20.761 -3.034  1.00 29.67  ? 36  LYS   A CG   1 
ATOM   274  C  CD   . LYS   A 1 36  ? 3.791   -21.056 -1.566  1.00 32.05  ? 36  LYS   A CD   1 
ATOM   275  C  CE   . LYS   A 1 36  ? 4.524   -22.296 -1.078  1.00 34.20  ? 36  LYS   A CE   1 
ATOM   276  N  NZ   . LYS   A 1 36  ? 3.848   -23.533 -1.546  1.00 34.56  ? 36  LYS   A NZ   1 
ATOM   277  N  N    . THR   A 1 37  ? 6.209   -17.929 -3.938  1.00 16.69  ? 37  THR   A N    1 
ATOM   278  C  CA   . THR   A 1 37  ? 7.368   -17.515 -4.771  1.00 17.24  ? 37  THR   A CA   1 
ATOM   279  C  C    . THR   A 1 37  ? 8.508   -18.504 -4.582  1.00 15.90  ? 37  THR   A C    1 
ATOM   280  O  O    . THR   A 1 37  ? 8.539   -19.197 -3.566  1.00 14.13  ? 37  THR   A O    1 
ATOM   281  C  CB   . THR   A 1 37  ? 7.896   -16.115 -4.425  1.00 17.57  ? 37  THR   A CB   1 
ATOM   282  O  OG1  . THR   A 1 37  ? 8.489   -16.154 -3.141  1.00 18.25  ? 37  THR   A OG1  1 
ATOM   283  C  CG2  . THR   A 1 37  ? 6.825   -15.055 -4.403  1.00 17.79  ? 37  THR   A CG2  1 
ATOM   284  N  N    . ALA   A 1 38  ? 9.413   -18.556 -5.550  1.00 16.20  ? 38  ALA   A N    1 
ATOM   285  C  CA   . ALA   A 1 38  ? 10.665  -19.322 -5.449  1.00 16.14  ? 38  ALA   A CA   1 
ATOM   286  C  C    . ALA   A 1 38  ? 11.759  -18.476 -6.088  1.00 17.24  ? 38  ALA   A C    1 
ATOM   287  O  O    . ALA   A 1 38  ? 11.478  -17.772 -7.106  1.00 16.96  ? 38  ALA   A O    1 
ATOM   288  C  CB   . ALA   A 1 38  ? 10.523  -20.685 -6.092  1.00 16.43  ? 38  ALA   A CB   1 
ATOM   289  N  N    . LYS   A 1 39  ? 12.955  -18.537 -5.501  1.00 17.65  ? 39  LYS   A N    1 
ATOM   290  C  CA   . LYS   A 1 39  ? 14.171  -17.867 -6.017  1.00 18.61  ? 39  LYS   A CA   1 
ATOM   291  C  C    . LYS   A 1 39  ? 14.399  -18.300 -7.477  1.00 17.56  ? 39  LYS   A C    1 
ATOM   292  O  O    . LYS   A 1 39  ? 14.304  -19.513 -7.791  1.00 14.50  ? 39  LYS   A O    1 
ATOM   293  C  CB   . LYS   A 1 39  ? 15.349  -18.204 -5.096  1.00 20.45  ? 39  LYS   A CB   1 
ATOM   294  C  CG   . LYS   A 1 39  ? 16.626  -17.409 -5.328  1.00 22.85  ? 39  LYS   A CG   1 
ATOM   295  C  CD   . LYS   A 1 39  ? 17.555  -17.443 -4.108  1.00 24.90  ? 39  LYS   A CD   1 
ATOM   296  C  CE   . LYS   A 1 39  ? 18.894  -16.774 -4.332  1.00 26.89  ? 39  LYS   A CE   1 
ATOM   297  N  NZ   . LYS   A 1 39  ? 19.469  -17.202 -5.630  1.00 30.05  ? 39  LYS   A NZ   1 
ATOM   298  N  N    . TRP   A 1 40  ? 14.704  -17.344 -8.349  1.00 16.39  ? 40  TRP   A N    1 
ATOM   299  C  CA   . TRP   A 1 40  ? 14.936  -17.645 -9.774  1.00 17.67  ? 40  TRP   A CA   1 
ATOM   300  C  C    . TRP   A 1 40  ? 16.296  -17.071 -10.176 1.00 19.61  ? 40  TRP   A C    1 
ATOM   301  O  O    . TRP   A 1 40  ? 16.442  -15.835 -10.158 1.00 19.87  ? 40  TRP   A O    1 
ATOM   302  C  CB   . TRP   A 1 40  ? 13.752  -17.122 -10.597 1.00 17.26  ? 40  TRP   A CB   1 
ATOM   303  C  CG   . TRP   A 1 40  ? 13.944  -17.226 -12.074 1.00 18.09  ? 40  TRP   A CG   1 
ATOM   304  C  CD1  . TRP   A 1 40  ? 14.511  -18.263 -12.756 1.00 17.82  ? 40  TRP   A CD1  1 
ATOM   305  C  CD2  . TRP   A 1 40  ? 13.562  -16.245 -13.059 1.00 18.47  ? 40  TRP   A CD2  1 
ATOM   306  N  NE1  . TRP   A 1 40  ? 14.544  -17.982 -14.094 1.00 18.39  ? 40  TRP   A NE1  1 
ATOM   307  C  CE2  . TRP   A 1 40  ? 13.978  -16.746 -14.309 1.00 18.68  ? 40  TRP   A CE2  1 
ATOM   308  C  CE3  . TRP   A 1 40  ? 12.950  -14.982 -13.000 1.00 19.01  ? 40  TRP   A CE3  1 
ATOM   309  C  CZ2  . TRP   A 1 40  ? 13.770  -16.040 -15.490 1.00 18.08  ? 40  TRP   A CZ2  1 
ATOM   310  C  CZ3  . TRP   A 1 40  ? 12.757  -14.280 -14.167 1.00 18.62  ? 40  TRP   A CZ3  1 
ATOM   311  C  CH2  . TRP   A 1 40  ? 13.163  -14.808 -15.395 1.00 18.30  ? 40  TRP   A CH2  1 
ATOM   312  N  N    . ASN   A 1 41  ? 17.268  -17.935 -10.477 1.00 21.92  ? 41  ASN   A N    1 
ATOM   313  C  CA   . ASN   A 1 41  ? 18.606  -17.515 -10.987 1.00 23.75  ? 41  ASN   A CA   1 
ATOM   314  C  C    . ASN   A 1 41  ? 18.444  -17.192 -12.473 1.00 24.42  ? 41  ASN   A C    1 
ATOM   315  O  O    . ASN   A 1 41  ? 18.714  -18.076 -13.329 1.00 24.75  ? 41  ASN   A O    1 
ATOM   316  C  CB   . ASN   A 1 41  ? 19.686  -18.560 -10.722 1.00 26.18  ? 41  ASN   A CB   1 
ATOM   317  C  CG   . ASN   A 1 41  ? 19.833  -18.896 -9.254  1.00 30.24  ? 41  ASN   A CG   1 
ATOM   318  O  OD1  . ASN   A 1 41  ? 19.826  -18.001 -8.400  1.00 32.72  ? 41  ASN   A OD1  1 
ATOM   319  N  ND2  . ASN   A 1 41  ? 19.911  -20.183 -8.942  1.00 31.09  ? 41  ASN   A ND2  1 
ATOM   320  N  N    . MET   A 1 42  ? 17.923  -15.999 -12.754 1.00 25.14  ? 42  MET   A N    1 
ATOM   321  C  CA   . MET   A 1 42  ? 17.747  -15.463 -14.125 1.00 27.33  ? 42  MET   A CA   1 
ATOM   322  C  C    . MET   A 1 42  ? 19.138  -15.263 -14.735 1.00 26.04  ? 42  MET   A C    1 
ATOM   323  O  O    . MET   A 1 42  ? 20.035  -14.805 -13.988 1.00 22.37  ? 42  MET   A O    1 
ATOM   324  C  CB   . MET   A 1 42  ? 16.979  -14.136 -14.115 1.00 31.29  ? 42  MET   A CB   1 
ATOM   325  C  CG   . MET   A 1 42  ? 16.622  -13.637 -15.512 1.00 35.21  ? 42  MET   A CG   1 
ATOM   326  S  SD   . MET   A 1 42  ? 17.753  -12.353 -16.094 1.00 44.32  ? 42  MET   A SD   1 
ATOM   327  C  CE   . MET   A 1 42  ? 17.159  -10.998 -15.088 1.00 42.64  ? 42  MET   A CE   1 
ATOM   328  N  N    . GLN   A 1 43  ? 19.298  -15.641 -16.014 1.00 24.36  ? 43  GLN   A N    1 
ATOM   329  C  CA   . GLN   A 1 43  ? 20.576  -15.576 -16.771 1.00 24.99  ? 43  GLN   A CA   1 
ATOM   330  C  C    . GLN   A 1 43  ? 20.432  -14.517 -17.870 1.00 24.38  ? 43  GLN   A C    1 
ATOM   331  O  O    . GLN   A 1 43  ? 19.818  -14.827 -18.917 1.00 25.06  ? 43  GLN   A O    1 
ATOM   332  C  CB   . GLN   A 1 43  ? 20.960  -16.945 -17.333 1.00 24.89  ? 43  GLN   A CB   1 
ATOM   333  C  CG   . GLN   A 1 43  ? 21.322  -17.953 -16.245 1.00 25.80  ? 43  GLN   A CG   1 
ATOM   334  C  CD   . GLN   A 1 43  ? 21.742  -19.282 -16.816 1.00 24.68  ? 43  GLN   A CD   1 
ATOM   335  O  OE1  . GLN   A 1 43  ? 22.360  -19.343 -17.876 1.00 28.06  ? 43  GLN   A OE1  1 
ATOM   336  N  NE2  . GLN   A 1 43  ? 21.371  -20.356 -16.141 1.00 23.53  ? 43  GLN   A NE2  1 
ATOM   337  N  N    . ASN   A 1 44  ? 20.960  -13.318 -17.608 1.00 23.32  ? 44  ASN   A N    1 
ATOM   338  C  CA   . ASN   A 1 44  ? 20.938  -12.148 -18.519 1.00 25.69  ? 44  ASN   A CA   1 
ATOM   339  C  C    . ASN   A 1 44  ? 21.486  -12.614 -19.870 1.00 25.53  ? 44  ASN   A C    1 
ATOM   340  O  O    . ASN   A 1 44  ? 22.616  -13.067 -19.878 1.00 28.61  ? 44  ASN   A O    1 
ATOM   341  C  CB   . ASN   A 1 44  ? 21.732  -10.966 -17.942 1.00 26.37  ? 44  ASN   A CB   1 
ATOM   342  C  CG   . ASN   A 1 44  ? 21.460  -9.663  -18.668 1.00 27.35  ? 44  ASN   A CG   1 
ATOM   343  O  OD1  . ASN   A 1 44  ? 21.296  -9.648  -19.886 1.00 28.72  ? 44  ASN   A OD1  1 
ATOM   344  N  ND2  . ASN   A 1 44  ? 21.399  -8.566  -17.934 1.00 28.28  ? 44  ASN   A ND2  1 
ATOM   345  N  N    . GLY   A 1 45  ? 20.659  -12.593 -20.921 1.00 23.65  ? 45  GLY   A N    1 
ATOM   346  C  CA   . GLY   A 1 45  ? 21.052  -12.837 -22.318 1.00 23.78  ? 45  GLY   A CA   1 
ATOM   347  C  C    . GLY   A 1 45  ? 20.852  -14.277 -22.745 1.00 24.24  ? 45  GLY   A C    1 
ATOM   348  O  O    . GLY   A 1 45  ? 21.152  -14.575 -23.889 1.00 22.36  ? 45  GLY   A O    1 
ATOM   349  N  N    . LYS   A 1 46  ? 20.343  -15.147 -21.875 1.00 26.30  ? 46  LYS   A N    1 
ATOM   350  C  CA   . LYS   A 1 46  ? 20.118  -16.569 -22.235 1.00 26.92  ? 46  LYS   A CA   1 
ATOM   351  C  C    . LYS   A 1 46  ? 18.640  -16.819 -22.518 1.00 23.44  ? 46  LYS   A C    1 
ATOM   352  O  O    . LYS   A 1 46  ? 17.778  -16.147 -21.919 1.00 23.31  ? 46  LYS   A O    1 
ATOM   353  C  CB   . LYS   A 1 46  ? 20.607  -17.502 -21.130 1.00 32.42  ? 46  LYS   A CB   1 
ATOM   354  C  CG   . LYS   A 1 46  ? 22.058  -17.313 -20.717 1.00 38.55  ? 46  LYS   A CG   1 
ATOM   355  C  CD   . LYS   A 1 46  ? 23.082  -17.618 -21.790 1.00 42.98  ? 46  LYS   A CD   1 
ATOM   356  C  CE   . LYS   A 1 46  ? 24.490  -17.499 -21.237 1.00 46.32  ? 46  LYS   A CE   1 
ATOM   357  N  NZ   . LYS   A 1 46  ? 25.515  -17.583 -22.301 1.00 47.89  ? 46  LYS   A NZ   1 
ATOM   358  N  N    . VAL   A 1 47  ? 18.387  -17.759 -23.422 1.00 22.43  ? 47  VAL   A N    1 
ATOM   359  C  CA   . VAL   A 1 47  ? 17.030  -18.254 -23.789 1.00 22.82  ? 47  VAL   A CA   1 
ATOM   360  C  C    . VAL   A 1 47  ? 16.596  -19.270 -22.725 1.00 21.82  ? 47  VAL   A C    1 
ATOM   361  O  O    . VAL   A 1 47  ? 17.328  -20.218 -22.508 1.00 21.54  ? 47  VAL   A O    1 
ATOM   362  C  CB   . VAL   A 1 47  ? 17.012  -18.843 -25.211 1.00 21.96  ? 47  VAL   A CB   1 
ATOM   363  C  CG1  . VAL   A 1 47  ? 15.704  -19.550 -25.526 1.00 22.26  ? 47  VAL   A CG1  1 
ATOM   364  C  CG2  . VAL   A 1 47  ? 17.296  -17.769 -26.245 1.00 22.98  ? 47  VAL   A CG2  1 
ATOM   365  N  N    . GLY   A 1 48  ? 15.478  -19.008 -22.051 1.00 20.98  ? 48  GLY   A N    1 
ATOM   366  C  CA   . GLY   A 1 48  ? 14.878  -19.892 -21.037 1.00 21.07  ? 48  GLY   A CA   1 
ATOM   367  C  C    . GLY   A 1 48  ? 13.522  -20.421 -21.484 1.00 20.68  ? 48  GLY   A C    1 
ATOM   368  O  O    . GLY   A 1 48  ? 13.001  -19.948 -22.501 1.00 21.50  ? 48  GLY   A O    1 
ATOM   369  N  N    . THR   A 1 49  ? 13.012  -21.420 -20.768 1.00 20.24  ? 49  THR   A N    1 
ATOM   370  C  CA   . THR   A 1 49  ? 11.710  -22.072 -21.000 1.00 19.97  ? 49  THR   A CA   1 
ATOM   371  C  C    . THR   A 1 49  ? 10.880  -21.952 -19.729 1.00 20.07  ? 49  THR   A C    1 
ATOM   372  O  O    . THR   A 1 49  ? 11.455  -22.097 -18.622 1.00 18.31  ? 49  THR   A O    1 
ATOM   373  C  CB   . THR   A 1 49  ? 11.864  -23.549 -21.379 1.00 21.90  ? 49  THR   A CB   1 
ATOM   374  O  OG1  . THR   A 1 49  ? 12.864  -23.584 -22.392 1.00 20.53  ? 49  THR   A OG1  1 
ATOM   375  C  CG2  . THR   A 1 49  ? 10.575  -24.165 -21.890 1.00 21.47  ? 49  THR   A CG2  1 
ATOM   376  N  N    . ALA   A 1 50  ? 9.588   -21.651 -19.907 1.00 20.22  ? 50  ALA   A N    1 
ATOM   377  C  CA   . ALA   A 1 50  ? 8.567   -21.616 -18.849 1.00 18.49  ? 50  ALA   A CA   1 
ATOM   378  C  C    . ALA   A 1 50  ? 7.541   -22.709 -19.145 1.00 18.35  ? 50  ALA   A C    1 
ATOM   379  O  O    . ALA   A 1 50  ? 7.071   -22.812 -20.292 1.00 19.11  ? 50  ALA   A O    1 
ATOM   380  C  CB   . ALA   A 1 50  ? 7.954   -20.247 -18.801 1.00 18.94  ? 50  ALA   A CB   1 
ATOM   381  N  N    . HIS   A 1 51  ? 7.202   -23.506 -18.138 1.00 17.37  ? 51  HIS   A N    1 
ATOM   382  C  CA   . HIS   A 1 51  ? 6.217   -24.606 -18.259 1.00 17.06  ? 51  HIS   A CA   1 
ATOM   383  C  C    . HIS   A 1 51  ? 5.185   -24.419 -17.151 1.00 15.79  ? 51  HIS   A C    1 
ATOM   384  O  O    . HIS   A 1 51  ? 5.599   -24.367 -15.986 1.00 14.79  ? 51  HIS   A O    1 
ATOM   385  C  CB   . HIS   A 1 51  ? 6.943   -25.948 -18.179 1.00 17.18  ? 51  HIS   A CB   1 
ATOM   386  C  CG   . HIS   A 1 51  ? 6.080   -27.078 -18.601 1.00 17.49  ? 51  HIS   A CG   1 
ATOM   387  N  ND1  . HIS   A 1 51  ? 6.448   -28.392 -18.423 1.00 18.28  ? 51  HIS   A ND1  1 
ATOM   388  C  CD2  . HIS   A 1 51  ? 4.868   -27.093 -19.181 1.00 17.74  ? 51  HIS   A CD2  1 
ATOM   389  C  CE1  . HIS   A 1 51  ? 5.500   -29.166 -18.896 1.00 19.58  ? 51  HIS   A CE1  1 
ATOM   390  N  NE2  . HIS   A 1 51  ? 4.516   -28.396 -19.355 1.00 18.29  ? 51  HIS   A NE2  1 
ATOM   391  N  N    . ILE   A 1 52  ? 3.920   -24.227 -17.508 1.00 14.74  ? 52  ILE   A N    1 
ATOM   392  C  CA   . ILE   A 1 52  ? 2.832   -23.960 -16.523 1.00 14.66  ? 52  ILE   A CA   1 
ATOM   393  C  C    . ILE   A 1 52  ? 1.731   -25.002 -16.738 1.00 14.47  ? 52  ILE   A C    1 
ATOM   394  O  O    . ILE   A 1 52  ? 1.377   -25.255 -17.898 1.00 13.86  ? 52  ILE   A O    1 
ATOM   395  C  CB   . ILE   A 1 52  ? 2.272   -22.536 -16.662 1.00 13.39  ? 52  ILE   A CB   1 
ATOM   396  C  CG1  . ILE   A 1 52  ? 3.362   -21.482 -16.496 1.00 13.20  ? 52  ILE   A CG1  1 
ATOM   397  C  CG2  . ILE   A 1 52  ? 1.133   -22.310 -15.694 1.00 13.75  ? 52  ILE   A CG2  1 
ATOM   398  C  CD1  . ILE   A 1 52  ? 3.040   -20.198 -17.127 1.00 12.88  ? 52  ILE   A CD1  1 
ATOM   399  N  N    . ILE   A 1 53  ? 1.205   -25.540 -15.642 1.00 13.69  ? 53  ILE   A N    1 
ATOM   400  C  CA   . ILE   A 1 53  ? 0.092   -26.518 -15.651 1.00 14.38  ? 53  ILE   A CA   1 
ATOM   401  C  C    . ILE   A 1 53  ? -0.928  -26.120 -14.586 1.00 14.37  ? 53  ILE   A C    1 
ATOM   402  O  O    . ILE   A 1 53  ? -0.526  -25.784 -13.435 1.00 12.54  ? 53  ILE   A O    1 
ATOM   403  C  CB   . ILE   A 1 53  ? 0.579   -27.961 -15.462 1.00 15.19  ? 53  ILE   A CB   1 
ATOM   404  C  CG1  . ILE   A 1 53  ? 1.443   -28.393 -16.655 1.00 15.53  ? 53  ILE   A CG1  1 
ATOM   405  C  CG2  . ILE   A 1 53  ? -0.637  -28.880 -15.248 1.00 14.96  ? 53  ILE   A CG2  1 
ATOM   406  C  CD1  . ILE   A 1 53  ? 2.045   -29.765 -16.544 1.00 15.78  ? 53  ILE   A CD1  1 
ATOM   407  N  N    . TYR   A 1 54  ? -2.198  -26.110 -14.995 1.00 14.72  ? 54  TYR   A N    1 
ATOM   408  C  CA   . TYR   A 1 54  ? -3.340  -26.169 -14.054 1.00 15.87  ? 54  TYR   A CA   1 
ATOM   409  C  C    . TYR   A 1 54  ? -3.941  -27.572 -14.166 1.00 15.93  ? 54  TYR   A C    1 
ATOM   410  O  O    . TYR   A 1 54  ? -4.361  -27.966 -15.237 1.00 17.53  ? 54  TYR   A O    1 
ATOM   411  C  CB   . TYR   A 1 54  ? -4.361  -25.063 -14.307 1.00 15.74  ? 54  TYR   A CB   1 
ATOM   412  C  CG   . TYR   A 1 54  ? -5.413  -25.038 -13.225 1.00 16.14  ? 54  TYR   A CG   1 
ATOM   413  C  CD1  . TYR   A 1 54  ? -5.079  -24.661 -11.935 1.00 15.90  ? 54  TYR   A CD1  1 
ATOM   414  C  CD2  . TYR   A 1 54  ? -6.693  -25.510 -13.445 1.00 15.74  ? 54  TYR   A CD2  1 
ATOM   415  C  CE1  . TYR   A 1 54  ? -6.008  -24.678 -10.915 1.00 16.06  ? 54  TYR   A CE1  1 
ATOM   416  C  CE2  . TYR   A 1 54  ? -7.635  -25.544 -12.427 1.00 15.55  ? 54  TYR   A CE2  1 
ATOM   417  C  CZ   . TYR   A 1 54  ? -7.299  -25.099 -11.169 1.00 15.71  ? 54  TYR   A CZ   1 
ATOM   418  O  OH   . TYR   A 1 54  ? -8.210  -25.079 -10.155 1.00 15.85  ? 54  TYR   A OH   1 
ATOM   419  N  N    . ASN   A 1 55  ? -3.910  -28.325 -13.083 1.00 16.31  ? 55  ASN   A N    1 
ATOM   420  C  CA   . ASN   A 1 55  ? -4.418  -29.719 -13.016 1.00 16.15  ? 55  ASN   A CA   1 
ATOM   421  C  C    . ASN   A 1 55  ? -5.734  -29.678 -12.228 1.00 16.79  ? 55  ASN   A C    1 
ATOM   422  O  O    . ASN   A 1 55  ? -5.692  -29.462 -10.974 1.00 16.26  ? 55  ASN   A O    1 
ATOM   423  C  CB   . ASN   A 1 55  ? -3.322  -30.611 -12.423 1.00 16.39  ? 55  ASN   A CB   1 
ATOM   424  C  CG   . ASN   A 1 55  ? -3.626  -32.087 -12.522 1.00 16.80  ? 55  ASN   A CG   1 
ATOM   425  O  OD1  . ASN   A 1 55  ? -4.635  -32.476 -13.116 1.00 16.61  ? 55  ASN   A OD1  1 
ATOM   426  N  ND2  . ASN   A 1 55  ? -2.747  -32.903 -11.956 1.00 16.00  ? 55  ASN   A ND2  1 
ATOM   427  N  N    . SER   A 1 56  ? -6.865  -29.811 -12.921 1.00 17.58  ? 56  SER   A N    1 
ATOM   428  C  CA   . SER   A 1 56  ? -8.217  -29.701 -12.313 1.00 19.95  ? 56  SER   A CA   1 
ATOM   429  C  C    . SER   A 1 56  ? -8.426  -30.794 -11.254 1.00 20.91  ? 56  SER   A C    1 
ATOM   430  O  O    . SER   A 1 56  ? -9.152  -30.549 -10.275 1.00 21.23  ? 56  SER   A O    1 
ATOM   431  C  CB   . SER   A 1 56  ? -9.287  -29.722 -13.362 1.00 19.91  ? 56  SER   A CB   1 
ATOM   432  O  OG   . SER   A 1 56  ? -9.160  -30.879 -14.174 1.00 22.48  ? 56  SER   A OG   1 
ATOM   433  N  N    . VAL   A 1 57  ? -7.769  -31.935 -11.410 1.00 21.88  ? 57  VAL   A N    1 
ATOM   434  C  CA   . VAL   A 1 57  ? -7.842  -33.093 -10.472 1.00 24.11  ? 57  VAL   A CA   1 
ATOM   435  C  C    . VAL   A 1 57  ? -7.415  -32.673 -9.054  1.00 23.75  ? 57  VAL   A C    1 
ATOM   436  O  O    . VAL   A 1 57  ? -8.117  -33.052 -8.105  1.00 24.42  ? 57  VAL   A O    1 
ATOM   437  C  CB   . VAL   A 1 57  ? -6.988  -34.250 -11.031 1.00 26.48  ? 57  VAL   A CB   1 
ATOM   438  C  CG1  . VAL   A 1 57  ? -6.594  -35.277 -9.986  1.00 27.41  ? 57  VAL   A CG1  1 
ATOM   439  C  CG2  . VAL   A 1 57  ? -7.731  -34.910 -12.181 1.00 27.84  ? 57  VAL   A CG2  1 
ATOM   440  N  N    . ASP   A 1 58  ? -6.296  -31.964 -8.911  1.00 23.06  ? 58  ASP   A N    1 
ATOM   441  C  CA   . ASP   A 1 58  ? -5.769  -31.438 -7.623  1.00 24.43  ? 58  ASP   A CA   1 
ATOM   442  C  C    . ASP   A 1 58  ? -6.203  -29.974 -7.403  1.00 24.30  ? 58  ASP   A C    1 
ATOM   443  O  O    . ASP   A 1 58  ? -5.897  -29.445 -6.332  1.00 23.67  ? 58  ASP   A O    1 
ATOM   444  C  CB   . ASP   A 1 58  ? -4.236  -31.424 -7.616  1.00 27.19  ? 58  ASP   A CB   1 
ATOM   445  C  CG   . ASP   A 1 58  ? -3.558  -32.779 -7.759  1.00 30.79  ? 58  ASP   A CG   1 
ATOM   446  O  OD1  . ASP   A 1 58  ? -4.074  -33.763 -7.192  1.00 26.56  ? 58  ASP   A OD1  1 
ATOM   447  O  OD2  . ASP   A 1 58  ? -2.477  -32.827 -8.423  1.00 35.76  ? 58  ASP   A OD2  1 
ATOM   448  N  N    . LYS   A 1 59  ? -6.809  -29.310 -8.396  1.00 24.23  ? 59  LYS   A N    1 
ATOM   449  C  CA   . LYS   A 1 59  ? -6.977  -27.827 -8.431  1.00 24.99  ? 59  LYS   A CA   1 
ATOM   450  C  C    . LYS   A 1 59  ? -5.657  -27.144 -8.028  1.00 24.44  ? 59  LYS   A C    1 
ATOM   451  O  O    . LYS   A 1 59  ? -5.659  -26.297 -7.112  1.00 22.97  ? 59  LYS   A O    1 
ATOM   452  C  CB   . LYS   A 1 59  ? -8.178  -27.443 -7.563  1.00 26.31  ? 59  LYS   A CB   1 
ATOM   453  C  CG   . LYS   A 1 59  ? -9.492  -27.948 -8.147  1.00 29.93  ? 59  LYS   A CG   1 
ATOM   454  C  CD   . LYS   A 1 59  ? -10.720 -27.228 -7.670  1.00 33.47  ? 59  LYS   A CD   1 
ATOM   455  C  CE   . LYS   A 1 59  ? -11.852 -27.298 -8.672  1.00 33.98  ? 59  LYS   A CE   1 
ATOM   456  N  NZ   . LYS   A 1 59  ? -13.171 -27.200 -8.013  1.00 33.52  ? 59  LYS   A NZ   1 
ATOM   457  N  N    . ARG   A 1 60  ? -4.569  -27.509 -8.700  1.00 23.17  ? 60  ARG   A N    1 
ATOM   458  C  CA   . ARG   A 1 60  ? -3.193  -27.016 -8.410  1.00 24.62  ? 60  ARG   A CA   1 
ATOM   459  C  C    . ARG   A 1 60  ? -2.612  -26.341 -9.659  1.00 21.89  ? 60  ARG   A C    1 
ATOM   460  O  O    . ARG   A 1 60  ? -2.611  -26.982 -10.744 1.00 22.35  ? 60  ARG   A O    1 
ATOM   461  C  CB   . ARG   A 1 60  ? -2.316  -28.185 -7.972  1.00 27.90  ? 60  ARG   A CB   1 
ATOM   462  C  CG   . ARG   A 1 60  ? -0.941  -27.787 -7.471  1.00 33.70  ? 60  ARG   A CG   1 
ATOM   463  C  CD   . ARG   A 1 60  ? -0.315  -28.987 -6.798  1.00 37.08  ? 60  ARG   A CD   1 
ATOM   464  N  NE   . ARG   A 1 60  ? -1.017  -29.319 -5.566  1.00 41.77  ? 60  ARG   A NE   1 
ATOM   465  C  CZ   . ARG   A 1 60  ? -1.047  -30.530 -5.003  1.00 47.43  ? 60  ARG   A CZ   1 
ATOM   466  N  NH1  . ARG   A 1 60  ? -0.412  -31.560 -5.549  1.00 50.32  ? 60  ARG   A NH1  1 
ATOM   467  N  NH2  . ARG   A 1 60  ? -1.713  -30.705 -3.878  1.00 49.21  ? 60  ARG   A NH2  1 
ATOM   468  N  N    . LEU   A 1 61  ? -2.209  -25.078 -9.520  1.00 19.46  ? 61  LEU   A N    1 
ATOM   469  C  CA   . LEU   A 1 61  ? -1.420  -24.317 -10.509 1.00 19.43  ? 61  LEU   A CA   1 
ATOM   470  C  C    . LEU   A 1 61  ? 0.073   -24.539 -10.222 1.00 19.99  ? 61  LEU   A C    1 
ATOM   471  O  O    . LEU   A 1 61  ? 0.484   -24.324 -9.072  1.00 21.44  ? 61  LEU   A O    1 
ATOM   472  C  CB   . LEU   A 1 61  ? -1.792  -22.840 -10.398 1.00 19.73  ? 61  LEU   A CB   1 
ATOM   473  C  CG   . LEU   A 1 61  ? -1.233  -21.921 -11.479 1.00 19.63  ? 61  LEU   A CG   1 
ATOM   474  C  CD1  . LEU   A 1 61  ? -1.576  -22.417 -12.881 1.00 18.64  ? 61  LEU   A CD1  1 
ATOM   475  C  CD2  . LEU   A 1 61  ? -1.744  -20.496 -11.273 1.00 20.12  ? 61  LEU   A CD2  1 
ATOM   476  N  N    . SER   A 1 62  ? 0.827   -24.923 -11.249 1.00 18.90  ? 62  SER   A N    1 
ATOM   477  C  CA   . SER   A 1 62  ? 2.252   -25.322 -11.210 1.00 18.67  ? 62  SER   A CA   1 
ATOM   478  C  C    . SER   A 1 62  ? 2.999   -24.547 -12.283 1.00 16.56  ? 62  SER   A C    1 
ATOM   479  O  O    . SER   A 1 62  ? 2.451   -24.430 -13.374 1.00 14.97  ? 62  SER   A O    1 
ATOM   480  C  CB   . SER   A 1 62  ? 2.390   -26.794 -11.511 1.00 20.04  ? 62  SER   A CB   1 
ATOM   481  O  OG   . SER   A 1 62  ? 2.059   -27.550 -10.383 1.00 24.45  ? 62  SER   A OG   1 
ATOM   482  N  N    . ALA   A 1 63  ? 4.248   -24.190 -12.020 1.00 15.51  ? 63  ALA   A N    1 
ATOM   483  C  CA   . ALA   A 1 63  ? 5.128   -23.509 -12.988 1.00 15.78  ? 63  ALA   A CA   1 
ATOM   484  C  C    . ALA   A 1 63  ? 6.571   -23.925 -12.733 1.00 16.59  ? 63  ALA   A C    1 
ATOM   485  O  O    . ALA   A 1 63  ? 7.002   -23.993 -11.548 1.00 17.76  ? 63  ALA   A O    1 
ATOM   486  C  CB   . ALA   A 1 63  ? 4.965   -22.030 -12.884 1.00 15.70  ? 63  ALA   A CB   1 
ATOM   487  N  N    . VAL   A 1 64  ? 7.261   -24.252 -13.813 1.00 17.55  ? 64  VAL   A N    1 
ATOM   488  C  CA   . VAL   A 1 64  ? 8.719   -24.561 -13.845 1.00 19.38  ? 64  VAL   A CA   1 
ATOM   489  C  C    . VAL   A 1 64  ? 9.353   -23.585 -14.827 1.00 18.17  ? 64  VAL   A C    1 
ATOM   490  O  O    . VAL   A 1 64  ? 8.809   -23.427 -15.931 1.00 18.33  ? 64  VAL   A O    1 
ATOM   491  C  CB   . VAL   A 1 64  ? 9.041   -26.005 -14.277 1.00 20.78  ? 64  VAL   A CB   1 
ATOM   492  C  CG1  . VAL   A 1 64  ? 10.485  -26.349 -13.926 1.00 24.03  ? 64  VAL   A CG1  1 
ATOM   493  C  CG2  . VAL   A 1 64  ? 8.117   -27.022 -13.638 1.00 23.28  ? 64  VAL   A CG2  1 
ATOM   494  N  N    . VAL   A 1 65  ? 10.478  -22.994 -14.440 1.00 17.92  ? 65  VAL   A N    1 
ATOM   495  C  CA   . VAL   A 1 65  ? 11.274  -22.107 -15.325 1.00 18.05  ? 65  VAL   A CA   1 
ATOM   496  C  C    . VAL   A 1 65  ? 12.717  -22.610 -15.322 1.00 17.71  ? 65  VAL   A C    1 
ATOM   497  O  O    . VAL   A 1 65  ? 13.284  -22.831 -14.244 1.00 17.11  ? 65  VAL   A O    1 
ATOM   498  C  CB   . VAL   A 1 65  ? 11.168  -20.638 -14.886 1.00 17.35  ? 65  VAL   A CB   1 
ATOM   499  C  CG1  . VAL   A 1 65  ? 12.046  -19.743 -15.733 1.00 17.95  ? 65  VAL   A CG1  1 
ATOM   500  C  CG2  . VAL   A 1 65  ? 9.727   -20.162 -14.923 1.00 18.07  ? 65  VAL   A CG2  1 
ATOM   501  N  N    . SER   A 1 66  ? 13.295  -22.775 -16.493 1.00 18.09  ? 66  SER   A N    1 
ATOM   502  C  CA   . SER   A 1 66  ? 14.601  -23.446 -16.605 1.00 21.04  ? 66  SER   A CA   1 
ATOM   503  C  C    . SER   A 1 66  ? 15.434  -22.857 -17.748 1.00 20.44  ? 66  SER   A C    1 
ATOM   504  O  O    . SER   A 1 66  ? 14.858  -22.263 -18.682 1.00 20.46  ? 66  SER   A O    1 
ATOM   505  C  CB   . SER   A 1 66  ? 14.343  -24.927 -16.733 1.00 21.61  ? 66  SER   A CB   1 
ATOM   506  O  OG   . SER   A 1 66  ? 13.995  -25.224 -18.050 1.00 25.78  ? 66  SER   A OG   1 
ATOM   507  N  N    . TYR   A 1 67  ? 16.751  -23.000 -17.646 1.00 21.49  ? 67  TYR   A N    1 
ATOM   508  C  CA   . TYR   A 1 67  ? 17.743  -22.736 -18.724 1.00 22.26  ? 67  TYR   A CA   1 
ATOM   509  C  C    . TYR   A 1 67  ? 18.458  -24.037 -19.065 1.00 23.54  ? 67  TYR   A C    1 
ATOM   510  O  O    . TYR   A 1 67  ? 18.541  -24.921 -18.224 1.00 21.05  ? 67  TYR   A O    1 
ATOM   511  C  CB   . TYR   A 1 67  ? 18.765  -21.685 -18.298 1.00 21.09  ? 67  TYR   A CB   1 
ATOM   512  C  CG   . TYR   A 1 67  ? 18.198  -20.296 -18.178 1.00 20.92  ? 67  TYR   A CG   1 
ATOM   513  C  CD1  . TYR   A 1 67  ? 17.993  -19.497 -19.295 1.00 21.65  ? 67  TYR   A CD1  1 
ATOM   514  C  CD2  . TYR   A 1 67  ? 17.843  -19.781 -16.940 1.00 21.26  ? 67  TYR   A CD2  1 
ATOM   515  C  CE1  . TYR   A 1 67  ? 17.470  -18.213 -19.184 1.00 21.32  ? 67  TYR   A CE1  1 
ATOM   516  C  CE2  . TYR   A 1 67  ? 17.301  -18.514 -16.816 1.00 22.12  ? 67  TYR   A CE2  1 
ATOM   517  C  CZ   . TYR   A 1 67  ? 17.121  -17.726 -17.938 1.00 21.03  ? 67  TYR   A CZ   1 
ATOM   518  O  OH   . TYR   A 1 67  ? 16.619  -16.473 -17.784 1.00 24.24  ? 67  TYR   A OH   1 
ATOM   519  N  N    . PRO   A 1 68  ? 18.993  -24.199 -20.298 1.00 27.67  ? 68  PRO   A N    1 
ATOM   520  C  CA   . PRO   A 1 68  ? 19.756  -25.401 -20.639 1.00 30.77  ? 68  PRO   A CA   1 
ATOM   521  C  C    . PRO   A 1 68  ? 20.938  -25.559 -19.663 1.00 34.91  ? 68  PRO   A C    1 
ATOM   522  O  O    . PRO   A 1 68  ? 21.519  -24.564 -19.288 1.00 33.24  ? 68  PRO   A O    1 
ATOM   523  C  CB   . PRO   A 1 68  ? 20.223  -25.140 -22.079 1.00 29.84  ? 68  PRO   A CB   1 
ATOM   524  C  CG   . PRO   A 1 68  ? 19.283  -24.073 -22.609 1.00 28.66  ? 68  PRO   A CG   1 
ATOM   525  C  CD   . PRO   A 1 68  ? 18.951  -23.224 -21.403 1.00 27.23  ? 68  PRO   A CD   1 
ATOM   526  N  N    . ASN   A 1 69  ? 21.205  -26.786 -19.203 1.00 42.26  ? 69  ASN   A N    1 
ATOM   527  C  CA   . ASN   A 1 69  ? 22.356  -27.134 -18.319 1.00 49.00  ? 69  ASN   A CA   1 
ATOM   528  C  C    . ASN   A 1 69  ? 22.399  -26.188 -17.087 1.00 47.64  ? 69  ASN   A C    1 
ATOM   529  O  O    . ASN   A 1 69  ? 23.491  -25.711 -16.709 1.00 51.58  ? 69  ASN   A O    1 
ATOM   530  C  CB   . ASN   A 1 69  ? 23.655  -27.194 -19.148 1.00 53.45  ? 69  ASN   A CB   1 
ATOM   531  C  CG   . ASN   A 1 69  ? 23.507  -27.947 -20.463 1.00 56.66  ? 69  ASN   A CG   1 
ATOM   532  O  OD1  . ASN   A 1 69  ? 23.982  -27.495 -21.505 1.00 59.20  ? 69  ASN   A OD1  1 
ATOM   533  N  ND2  . ASN   A 1 69  ? 22.831  -29.086 -20.450 1.00 55.66  ? 69  ASN   A ND2  1 
ATOM   534  N  N    . ALA   A 1 70  ? 21.243  -25.913 -16.481 1.00 40.53  ? 70  ALA   A N    1 
ATOM   535  C  CA   . ALA   A 1 70  ? 21.086  -25.315 -15.136 1.00 35.91  ? 70  ALA   A CA   1 
ATOM   536  C  C    . ALA   A 1 70  ? 19.846  -25.937 -14.481 1.00 33.34  ? 70  ALA   A C    1 
ATOM   537  O  O    . ALA   A 1 70  ? 18.959  -26.414 -15.195 1.00 31.63  ? 70  ALA   A O    1 
ATOM   538  C  CB   . ALA   A 1 70  ? 20.978  -23.811 -15.215 1.00 33.75  ? 70  ALA   A CB   1 
ATOM   539  N  N    . ASP   A 1 71  ? 19.810  -25.922 -13.152 1.00 32.92  ? 71  ASP   A N    1 
ATOM   540  C  CA   . ASP   A 1 71  ? 18.673  -26.471 -12.376 1.00 35.18  ? 71  ASP   A CA   1 
ATOM   541  C  C    . ASP   A 1 71  ? 17.491  -25.501 -12.446 1.00 30.69  ? 71  ASP   A C    1 
ATOM   542  O  O    . ASP   A 1 71  ? 17.719  -24.309 -12.506 1.00 31.11  ? 71  ASP   A O    1 
ATOM   543  C  CB   . ASP   A 1 71  ? 19.085  -26.830 -10.954 1.00 39.68  ? 71  ASP   A CB   1 
ATOM   544  C  CG   . ASP   A 1 71  ? 19.948  -25.756 -10.339 1.00 48.29  ? 71  ASP   A CG   1 
ATOM   545  O  OD1  . ASP   A 1 71  ? 20.650  -25.076 -11.094 1.00 54.44  ? 71  ASP   A OD1  1 
ATOM   546  O  OD2  . ASP   A 1 71  ? 19.881  -25.591 -9.124  1.00 57.46  ? 71  ASP   A OD2  1 
ATOM   547  N  N    . SER   A 1 72  ? 16.279  -26.031 -12.394 1.00 24.28  ? 72  SER   A N    1 
ATOM   548  C  CA   . SER   A 1 72  ? 15.056  -25.214 -12.536 1.00 22.18  ? 72  SER   A CA   1 
ATOM   549  C  C    . SER   A 1 72  ? 14.634  -24.521 -11.247 1.00 20.50  ? 72  SER   A C    1 
ATOM   550  O  O    . SER   A 1 72  ? 15.155  -24.826 -10.206 1.00 19.72  ? 72  SER   A O    1 
ATOM   551  C  CB   . SER   A 1 72  ? 13.968  -26.072 -13.013 1.00 21.95  ? 72  SER   A CB   1 
ATOM   552  O  OG   . SER   A 1 72  ? 14.299  -26.619 -14.252 1.00 20.76  ? 72  SER   A OG   1 
ATOM   553  N  N    . ALA   A 1 73  ? 13.728  -23.574 -11.399 1.00 18.02  ? 73  ALA   A N    1 
ATOM   554  C  CA   . ALA   A 1 73  ? 13.038  -22.895 -10.291 1.00 18.33  ? 73  ALA   A CA   1 
ATOM   555  C  C    . ALA   A 1 73  ? 11.570  -23.318 -10.413 1.00 16.81  ? 73  ALA   A C    1 
ATOM   556  O  O    . ALA   A 1 73  ? 11.085  -23.353 -11.511 1.00 15.54  ? 73  ALA   A O    1 
ATOM   557  C  CB   . ALA   A 1 73  ? 13.220  -21.407 -10.354 1.00 17.56  ? 73  ALA   A CB   1 
ATOM   558  N  N    . THR   A 1 74  ? 10.929  -23.652 -9.305  1.00 16.98  ? 74  THR   A N    1 
ATOM   559  C  CA   . THR   A 1 74  ? 9.535   -24.156 -9.306  1.00 17.50  ? 74  THR   A CA   1 
ATOM   560  C  C    . THR   A 1 74  ? 8.695   -23.560 -8.176  1.00 15.90  ? 74  THR   A C    1 
ATOM   561  O  O    . THR   A 1 74  ? 9.204   -23.351 -7.104  1.00 15.03  ? 74  THR   A O    1 
ATOM   562  C  CB   . THR   A 1 74  ? 9.492   -25.691 -9.319  1.00 19.28  ? 74  THR   A CB   1 
ATOM   563  O  OG1  . THR   A 1 74  ? 8.318   -26.118 -9.989  1.00 20.17  ? 74  THR   A OG1  1 
ATOM   564  C  CG2  . THR   A 1 74  ? 9.621   -26.333 -7.957  1.00 20.04  ? 74  THR   A CG2  1 
ATOM   565  N  N    . VAL   A 1 75  ? 7.412   -23.436 -8.466  1.00 15.64  ? 75  VAL   A N    1 
ATOM   566  C  CA   . VAL   A 1 75  ? 6.385   -22.837 -7.590  1.00 17.23  ? 75  VAL   A CA   1 
ATOM   567  C  C    . VAL   A 1 75  ? 5.046   -23.522 -7.908  1.00 18.02  ? 75  VAL   A C    1 
ATOM   568  O  O    . VAL   A 1 75  ? 4.867   -23.937 -8.997  1.00 17.59  ? 75  VAL   A O    1 
ATOM   569  C  CB   . VAL   A 1 75  ? 6.414   -21.313 -7.748  1.00 18.03  ? 75  VAL   A CB   1 
ATOM   570  C  CG1  . VAL   A 1 75  ? 5.680   -20.812 -8.970  1.00 17.91  ? 75  VAL   A CG1  1 
ATOM   571  C  CG2  . VAL   A 1 75  ? 6.000   -20.614 -6.481  1.00 19.72  ? 75  VAL   A CG2  1 
ATOM   572  N  N    . SER   A 1 76  ? 4.161   -23.615 -6.931  1.00 20.40  ? 76  SER   A N    1 
ATOM   573  C  CA   . SER   A 1 76  ? 2.925   -24.419 -7.010  1.00 21.80  ? 76  SER   A CA   1 
ATOM   574  C  C    . SER   A 1 76  ? 1.945   -23.823 -5.998  1.00 21.12  ? 76  SER   A C    1 
ATOM   575  O  O    . SER   A 1 76  ? 2.408   -23.440 -4.901  1.00 19.20  ? 76  SER   A O    1 
ATOM   576  C  CB   . SER   A 1 76  ? 3.276   -25.847 -6.716  1.00 22.48  ? 76  SER   A CB   1 
ATOM   577  O  OG   . SER   A 1 76  ? 2.165   -26.679 -6.890  1.00 26.59  ? 76  SER   A OG   1 
ATOM   578  N  N    . TYR   A 1 77  ? 0.669   -23.693 -6.351  1.00 20.54  ? 77  TYR   A N    1 
ATOM   579  C  CA   . TYR   A 1 77  ? -0.366  -23.167 -5.424  1.00 20.58  ? 77  TYR   A CA   1 
ATOM   580  C  C    . TYR   A 1 77  ? -1.715  -23.827 -5.710  1.00 19.99  ? 77  TYR   A C    1 
ATOM   581  O  O    . TYR   A 1 77  ? -2.090  -23.959 -6.882  1.00 18.99  ? 77  TYR   A O    1 
ATOM   582  C  CB   . TYR   A 1 77  ? -0.439  -21.644 -5.521  1.00 20.00  ? 77  TYR   A CB   1 
ATOM   583  C  CG   . TYR   A 1 77  ? -1.228  -21.002 -4.409  1.00 20.99  ? 77  TYR   A CG   1 
ATOM   584  C  CD1  . TYR   A 1 77  ? -0.822  -21.125 -3.088  1.00 22.96  ? 77  TYR   A CD1  1 
ATOM   585  C  CD2  . TYR   A 1 77  ? -2.379  -20.271 -4.666  1.00 21.60  ? 77  TYR   A CD2  1 
ATOM   586  C  CE1  . TYR   A 1 77  ? -1.537  -20.535 -2.054  1.00 23.82  ? 77  TYR   A CE1  1 
ATOM   587  C  CE2  . TYR   A 1 77  ? -3.089  -19.655 -3.649  1.00 20.53  ? 77  TYR   A CE2  1 
ATOM   588  C  CZ   . TYR   A 1 77  ? -2.679  -19.806 -2.338  1.00 21.83  ? 77  TYR   A CZ   1 
ATOM   589  O  OH   . TYR   A 1 77  ? -3.352  -19.197 -1.321  1.00 25.11  ? 77  TYR   A OH   1 
ATOM   590  N  N    . ASP   A 1 78  ? -2.396  -24.262 -4.651  1.00 21.78  ? 78  ASP   A N    1 
ATOM   591  C  CA   . ASP   A 1 78  ? -3.761  -24.842 -4.712  1.00 22.93  ? 78  ASP   A CA   1 
ATOM   592  C  C    . ASP   A 1 78  ? -4.743  -23.684 -4.786  1.00 22.89  ? 78  ASP   A C    1 
ATOM   593  O  O    . ASP   A 1 78  ? -4.715  -22.886 -3.870  1.00 23.87  ? 78  ASP   A O    1 
ATOM   594  C  CB   . ASP   A 1 78  ? -4.050  -25.726 -3.506  1.00 24.59  ? 78  ASP   A CB   1 
ATOM   595  C  CG   . ASP   A 1 78  ? -3.286  -27.022 -3.594  1.00 27.29  ? 78  ASP   A CG   1 
ATOM   596  O  OD1  . ASP   A 1 78  ? -2.584  -27.226 -4.630  1.00 26.94  ? 78  ASP   A OD1  1 
ATOM   597  O  OD2  . ASP   A 1 78  ? -3.428  -27.823 -2.657  1.00 32.66  ? 78  ASP   A OD2  1 
ATOM   598  N  N    . VAL   A 1 79  ? -5.513  -23.598 -5.872  1.00 21.72  ? 79  VAL   A N    1 
ATOM   599  C  CA   . VAL   A 1 79  ? -6.492  -22.514 -6.118  1.00 22.92  ? 79  VAL   A CA   1 
ATOM   600  C  C    . VAL   A 1 79  ? -7.647  -23.057 -6.970  1.00 24.10  ? 79  VAL   A C    1 
ATOM   601  O  O    . VAL   A 1 79  ? -7.388  -23.650 -8.042  1.00 24.87  ? 79  VAL   A O    1 
ATOM   602  C  CB   . VAL   A 1 79  ? -5.814  -21.289 -6.758  1.00 22.03  ? 79  VAL   A CB   1 
ATOM   603  C  CG1  . VAL   A 1 79  ? -4.946  -21.666 -7.944  1.00 21.24  ? 79  VAL   A CG1  1 
ATOM   604  C  CG2  . VAL   A 1 79  ? -6.836  -20.222 -7.126  1.00 21.34  ? 79  VAL   A CG2  1 
ATOM   605  N  N    . ASP   A 1 80  ? -8.870  -22.841 -6.483  1.00 26.48  ? 80  ASP   A N    1 
ATOM   606  C  CA   . ASP   A 1 80  ? -10.150 -23.196 -7.151  1.00 28.31  ? 80  ASP   A CA   1 
ATOM   607  C  C    . ASP   A 1 80  ? -10.443 -22.146 -8.215  1.00 24.44  ? 80  ASP   A C    1 
ATOM   608  O  O    . ASP   A 1 80  ? -11.135 -21.204 -7.895  1.00 25.10  ? 80  ASP   A O    1 
ATOM   609  C  CB   . ASP   A 1 80  ? -11.331 -23.211 -6.170  1.00 32.55  ? 80  ASP   A CB   1 
ATOM   610  C  CG   . ASP   A 1 80  ? -11.070 -23.925 -4.857  1.00 39.09  ? 80  ASP   A CG   1 
ATOM   611  O  OD1  . ASP   A 1 80  ? -10.811 -25.155 -4.892  1.00 42.37  ? 80  ASP   A OD1  1 
ATOM   612  O  OD2  . ASP   A 1 80  ? -11.104 -23.233 -3.806  1.00 44.71  ? 80  ASP   A OD2  1 
ATOM   613  N  N    . LEU   A 1 81  ? -9.940  -22.311 -9.433  1.00 25.17  ? 81  LEU   A N    1 
ATOM   614  C  CA   . LEU   A 1 81  ? -10.107 -21.317 -10.539 1.00 25.68  ? 81  LEU   A CA   1 
ATOM   615  C  C    . LEU   A 1 81  ? -11.602 -21.047 -10.814 1.00 24.54  ? 81  LEU   A C    1 
ATOM   616  O  O    . LEU   A 1 81  ? -11.906 -19.936 -11.272 1.00 24.03  ? 81  LEU   A O    1 
ATOM   617  C  CB   . LEU   A 1 81  ? -9.374  -21.816 -11.791 1.00 25.25  ? 81  LEU   A CB   1 
ATOM   618  C  CG   . LEU   A 1 81  ? -7.853  -21.702 -11.756 1.00 26.90  ? 81  LEU   A CG   1 
ATOM   619  C  CD1  . LEU   A 1 81  ? -7.278  -22.030 -13.117 1.00 28.78  ? 81  LEU   A CD1  1 
ATOM   620  C  CD2  . LEU   A 1 81  ? -7.393  -20.310 -11.334 1.00 28.58  ? 81  LEU   A CD2  1 
ATOM   621  N  N    . ASP   A 1 82  ? -12.493 -21.999 -10.496 1.00 24.03  ? 82  ASP   A N    1 
ATOM   622  C  CA   . ASP   A 1 82  ? -13.978 -21.858 -10.582 1.00 25.02  ? 82  ASP   A CA   1 
ATOM   623  C  C    . ASP   A 1 82  ? -14.495 -20.787 -9.617  1.00 23.32  ? 82  ASP   A C    1 
ATOM   624  O  O    . ASP   A 1 82  ? -15.578 -20.298 -9.870  1.00 21.65  ? 82  ASP   A O    1 
ATOM   625  C  CB   . ASP   A 1 82  ? -14.711 -23.179 -10.293 1.00 26.63  ? 82  ASP   A CB   1 
ATOM   626  C  CG   . ASP   A 1 82  ? -14.357 -23.841 -8.968  1.00 28.76  ? 82  ASP   A CG   1 
ATOM   627  O  OD1  . ASP   A 1 82  ? -13.219 -24.356 -8.845  1.00 30.87  ? 82  ASP   A OD1  1 
ATOM   628  O  OD2  . ASP   A 1 82  ? -15.216 -23.849 -8.064  1.00 30.86  ? 82  ASP   A OD2  1 
ATOM   629  N  N    . ASN   A 1 83  ? -13.774 -20.490 -8.527  1.00 23.92  ? 83  ASN   A N    1 
ATOM   630  C  CA   . ASN   A 1 83  ? -14.206 -19.555 -7.457  1.00 23.45  ? 83  ASN   A CA   1 
ATOM   631  C  C    . ASN   A 1 83  ? -13.497 -18.203 -7.627  1.00 23.86  ? 83  ASN   A C    1 
ATOM   632  O  O    . ASN   A 1 83  ? -13.749 -17.323 -6.811  1.00 23.75  ? 83  ASN   A O    1 
ATOM   633  C  CB   . ASN   A 1 83  ? -13.945 -20.168 -6.073  1.00 26.30  ? 83  ASN   A CB   1 
ATOM   634  C  CG   . ASN   A 1 83  ? -14.359 -19.286 -4.906  1.00 27.20  ? 83  ASN   A CG   1 
ATOM   635  O  OD1  . ASN   A 1 83  ? -13.515 -18.855 -4.129  1.00 29.24  ? 83  ASN   A OD1  1 
ATOM   636  N  ND2  . ASN   A 1 83  ? -15.640 -18.978 -4.796  1.00 24.05  ? 83  ASN   A ND2  1 
ATOM   637  N  N    . VAL   A 1 84  ? -12.613 -18.043 -8.618  1.00 22.71  ? 84  VAL   A N    1 
ATOM   638  C  CA   . VAL   A 1 84  ? -11.800 -16.808 -8.786  1.00 22.08  ? 84  VAL   A CA   1 
ATOM   639  C  C    . VAL   A 1 84  ? -12.077 -16.185 -10.160 1.00 21.24  ? 84  VAL   A C    1 
ATOM   640  O  O    . VAL   A 1 84  ? -12.261 -14.961 -10.233 1.00 22.59  ? 84  VAL   A O    1 
ATOM   641  C  CB   . VAL   A 1 84  ? -10.300 -17.129 -8.601  1.00 24.30  ? 84  VAL   A CB   1 
ATOM   642  C  CG1  . VAL   A 1 84  ? -9.423  -15.959 -9.002  1.00 25.27  ? 84  VAL   A CG1  1 
ATOM   643  C  CG2  . VAL   A 1 84  ? -9.987  -17.562 -7.181  1.00 24.27  ? 84  VAL   A CG2  1 
ATOM   644  N  N    . LEU   A 1 85  ? -12.033 -16.968 -11.238 1.00 19.15  ? 85  LEU   A N    1 
ATOM   645  C  CA   . LEU   A 1 85  ? -12.103 -16.415 -12.616 1.00 17.45  ? 85  LEU   A CA   1 
ATOM   646  C  C    . LEU   A 1 85  ? -13.544 -16.457 -13.092 1.00 17.78  ? 85  LEU   A C    1 
ATOM   647  O  O    . LEU   A 1 85  ? -14.316 -17.236 -12.555 1.00 18.35  ? 85  LEU   A O    1 
ATOM   648  C  CB   . LEU   A 1 85  ? -11.215 -17.271 -13.506 1.00 17.25  ? 85  LEU   A CB   1 
ATOM   649  C  CG   . LEU   A 1 85  ? -9.722  -17.016 -13.344 1.00 17.12  ? 85  LEU   A CG   1 
ATOM   650  C  CD1  . LEU   A 1 85  ? -8.931  -18.143 -13.971 1.00 17.10  ? 85  LEU   A CD1  1 
ATOM   651  C  CD2  . LEU   A 1 85  ? -9.340  -15.667 -13.949 1.00 17.60  ? 85  LEU   A CD2  1 
ATOM   652  N  N    . PRO   A 1 86  ? -13.945 -15.684 -14.124 1.00 17.29  ? 86  PRO   A N    1 
ATOM   653  C  CA   . PRO   A 1 86  ? -15.203 -15.966 -14.816 1.00 18.42  ? 86  PRO   A CA   1 
ATOM   654  C  C    . PRO   A 1 86  ? -15.097 -17.288 -15.602 1.00 18.34  ? 86  PRO   A C    1 
ATOM   655  O  O    . PRO   A 1 86  ? -14.016 -17.851 -15.737 1.00 16.78  ? 86  PRO   A O    1 
ATOM   656  C  CB   . PRO   A 1 86  ? -15.439 -14.740 -15.712 1.00 16.86  ? 86  PRO   A CB   1 
ATOM   657  C  CG   . PRO   A 1 86  ? -14.052 -14.163 -15.918 1.00 16.95  ? 86  PRO   A CG   1 
ATOM   658  C  CD   . PRO   A 1 86  ? -13.216 -14.564 -14.724 1.00 16.72  ? 86  PRO   A CD   1 
ATOM   659  N  N    . GLU   A 1 87  ? -16.246 -17.759 -16.071 1.00 18.01  ? 87  GLU   A N    1 
ATOM   660  C  CA   . GLU   A 1 87  ? -16.446 -19.031 -16.810 1.00 19.68  ? 87  GLU   A CA   1 
ATOM   661  C  C    . GLU   A 1 87  ? -15.602 -18.998 -18.090 1.00 18.22  ? 87  GLU   A C    1 
ATOM   662  O  O    . GLU   A 1 87  ? -14.974 -20.028 -18.440 1.00 16.41  ? 87  GLU   A O    1 
ATOM   663  C  CB   . GLU   A 1 87  ? -17.960 -19.174 -17.029 1.00 21.55  ? 87  GLU   A CB   1 
ATOM   664  C  CG   . GLU   A 1 87  ? -18.393 -20.288 -17.941 1.00 24.80  ? 87  GLU   A CG   1 
ATOM   665  C  CD   . GLU   A 1 87  ? -19.825 -20.784 -17.712 1.00 27.85  ? 87  GLU   A CD   1 
ATOM   666  O  OE1  . GLU   A 1 87  ? -20.569 -20.156 -16.885 1.00 25.25  ? 87  GLU   A OE1  1 
ATOM   667  O  OE2  . GLU   A 1 87  ? -20.181 -21.836 -18.334 1.00 26.84  ? 87  GLU   A OE2  1 
ATOM   668  N  N    . TRP   A 1 88  ? -15.575 -17.843 -18.756 1.00 17.89  ? 88  TRP   A N    1 
ATOM   669  C  CA   . TRP   A 1 88  ? -14.858 -17.629 -20.038 1.00 17.39  ? 88  TRP   A CA   1 
ATOM   670  C  C    . TRP   A 1 88  ? -13.739 -16.614 -19.813 1.00 16.44  ? 88  TRP   A C    1 
ATOM   671  O  O    . TRP   A 1 88  ? -14.022 -15.600 -19.183 1.00 17.63  ? 88  TRP   A O    1 
ATOM   672  C  CB   . TRP   A 1 88  ? -15.833 -17.147 -21.103 1.00 17.63  ? 88  TRP   A CB   1 
ATOM   673  C  CG   . TRP   A 1 88  ? -16.696 -18.232 -21.653 1.00 18.70  ? 88  TRP   A CG   1 
ATOM   674  C  CD1  . TRP   A 1 88  ? -17.949 -18.580 -21.231 1.00 19.04  ? 88  TRP   A CD1  1 
ATOM   675  C  CD2  . TRP   A 1 88  ? -16.383 -19.102 -22.755 1.00 18.06  ? 88  TRP   A CD2  1 
ATOM   676  N  NE1  . TRP   A 1 88  ? -18.431 -19.615 -21.995 1.00 18.54  ? 88  TRP   A NE1  1 
ATOM   677  C  CE2  . TRP   A 1 88  ? -17.496 -19.950 -22.940 1.00 18.48  ? 88  TRP   A CE2  1 
ATOM   678  C  CE3  . TRP   A 1 88  ? -15.275 -19.256 -23.586 1.00 19.27  ? 88  TRP   A CE3  1 
ATOM   679  C  CZ2  . TRP   A 1 88  ? -17.530 -20.936 -23.923 1.00 18.75  ? 88  TRP   A CZ2  1 
ATOM   680  C  CZ3  . TRP   A 1 88  ? -15.307 -20.234 -24.558 1.00 19.71  ? 88  TRP   A CZ3  1 
ATOM   681  C  CH2  . TRP   A 1 88  ? -16.426 -21.056 -24.727 1.00 19.19  ? 88  TRP   A CH2  1 
ATOM   682  N  N    . VAL   A 1 89  ? -12.549 -16.878 -20.345 1.00 14.61  ? 89  VAL   A N    1 
ATOM   683  C  CA   . VAL   A 1 89  ? -11.300 -16.102 -20.079 1.00 14.69  ? 89  VAL   A CA   1 
ATOM   684  C  C    . VAL   A 1 89  ? -10.512 -15.968 -21.382 1.00 14.06  ? 89  VAL   A C    1 
ATOM   685  O  O    . VAL   A 1 89  ? -10.799 -16.698 -22.336 1.00 14.29  ? 89  VAL   A O    1 
ATOM   686  C  CB   . VAL   A 1 89  ? -10.435 -16.770 -18.988 1.00 14.41  ? 89  VAL   A CB   1 
ATOM   687  C  CG1  . VAL   A 1 89  ? -11.129 -16.766 -17.633 1.00 14.68  ? 89  VAL   A CG1  1 
ATOM   688  C  CG2  . VAL   A 1 89  ? -10.041 -18.194 -19.347 1.00 14.23  ? 89  VAL   A CG2  1 
ATOM   689  N  N    . ARG   A 1 90  ? -9.592  -15.018 -21.420 1.00 13.89  ? 90  ARG   A N    1 
ATOM   690  C  CA   . ARG   A 1 90  ? -8.510  -14.971 -22.426 1.00 14.38  ? 90  ARG   A CA   1 
ATOM   691  C  C    . ARG   A 1 90  ? -7.203  -15.271 -21.703 1.00 13.45  ? 90  ARG   A C    1 
ATOM   692  O  O    . ARG   A 1 90  ? -7.115  -14.988 -20.504 1.00 12.68  ? 90  ARG   A O    1 
ATOM   693  C  CB   . ARG   A 1 90  ? -8.498  -13.635 -23.174 1.00 14.81  ? 90  ARG   A CB   1 
ATOM   694  C  CG   . ARG   A 1 90  ? -9.516  -13.583 -24.300 1.00 15.92  ? 90  ARG   A CG   1 
ATOM   695  C  CD   . ARG   A 1 90  ? -9.125  -12.546 -25.326 1.00 17.36  ? 90  ARG   A CD   1 
ATOM   696  N  NE   . ARG   A 1 90  ? -9.985  -12.623 -26.494 1.00 18.66  ? 90  ARG   A NE   1 
ATOM   697  C  CZ   . ARG   A 1 90  ? -10.955 -11.758 -26.805 1.00 20.60  ? 90  ARG   A CZ   1 
ATOM   698  N  NH1  . ARG   A 1 90  ? -11.214 -10.710 -26.039 1.00 20.97  ? 90  ARG   A NH1  1 
ATOM   699  N  NH2  . ARG   A 1 90  ? -11.665 -11.945 -27.905 1.00 21.63  ? 90  ARG   A NH2  1 
ATOM   700  N  N    . VAL   A 1 91  ? -6.289  -15.940 -22.393 1.00 14.05  ? 91  VAL   A N    1 
ATOM   701  C  CA   . VAL   A 1 91  ? -4.916  -16.205 -21.887 1.00 14.32  ? 91  VAL   A CA   1 
ATOM   702  C  C    . VAL   A 1 91  ? -3.972  -15.308 -22.673 1.00 13.35  ? 91  VAL   A C    1 
ATOM   703  O  O    . VAL   A 1 91  ? -4.265  -15.029 -23.857 1.00 11.99  ? 91  VAL   A O    1 
ATOM   704  C  CB   . VAL   A 1 91  ? -4.520  -17.675 -21.991 1.00 15.12  ? 91  VAL   A CB   1 
ATOM   705  C  CG1  . VAL   A 1 91  ? -5.460  -18.522 -21.154 1.00 16.64  ? 91  VAL   A CG1  1 
ATOM   706  C  CG2  . VAL   A 1 91  ? -4.473  -18.140 -23.442 1.00 15.72  ? 91  VAL   A CG2  1 
ATOM   707  N  N    . GLY   A 1 92  ? -2.882  -14.917 -22.022 1.00 12.85  ? 92  GLY   A N    1 
ATOM   708  C  CA   . GLY   A 1 92  ? -1.952  -13.921 -22.564 1.00 13.12  ? 92  GLY   A CA   1 
ATOM   709  C  C    . GLY   A 1 92  ? -0.569  -13.981 -21.946 1.00 12.94  ? 92  GLY   A C    1 
ATOM   710  O  O    . GLY   A 1 92  ? -0.330  -14.784 -21.027 1.00 13.19  ? 92  GLY   A O    1 
ATOM   711  N  N    . LEU   A 1 93  ? 0.325   -13.177 -22.510 1.00 12.69  ? 93  LEU   A N    1 
ATOM   712  C  CA   . LEU   A 1 93  ? 1.670   -12.895 -21.994 1.00 13.01  ? 93  LEU   A CA   1 
ATOM   713  C  C    . LEU   A 1 93  ? 1.736   -11.383 -21.791 1.00 13.21  ? 93  LEU   A C    1 
ATOM   714  O  O    . LEU   A 1 93  ? 1.188   -10.671 -22.621 1.00 14.09  ? 93  LEU   A O    1 
ATOM   715  C  CB   . LEU   A 1 93  ? 2.706   -13.392 -23.008 1.00 12.73  ? 93  LEU   A CB   1 
ATOM   716  C  CG   . LEU   A 1 93  ? 2.815   -14.905 -23.207 1.00 12.43  ? 93  LEU   A CG   1 
ATOM   717  C  CD1  . LEU   A 1 93  ? 3.890   -15.235 -24.229 1.00 12.92  ? 93  LEU   A CD1  1 
ATOM   718  C  CD2  . LEU   A 1 93  ? 3.137   -15.632 -21.918 1.00 12.54  ? 93  LEU   A CD2  1 
ATOM   719  N  N    . SER   A 1 94  ? 2.327   -10.929 -20.695 1.00 13.49  ? 94  SER   A N    1 
ATOM   720  C  CA   . SER   A 1 94  ? 2.473   -9.499  -20.338 1.00 14.49  ? 94  SER   A CA   1 
ATOM   721  C  C    . SER   A 1 94  ? 3.935   -9.266  -19.986 1.00 15.23  ? 94  SER   A C    1 
ATOM   722  O  O    . SER   A 1 94  ? 4.585   -10.235 -19.568 1.00 16.02  ? 94  SER   A O    1 
ATOM   723  C  CB   . SER   A 1 94  ? 1.570   -9.166  -19.189 1.00 14.82  ? 94  SER   A CB   1 
ATOM   724  O  OG   . SER   A 1 94  ? 1.546   -7.764  -18.919 1.00 14.95  ? 94  SER   A OG   1 
ATOM   725  N  N    . ALA   A 1 95  ? 4.443   -8.057  -20.172 1.00 14.76  ? 95  ALA   A N    1 
ATOM   726  C  CA   . ALA   A 1 95  ? 5.780   -7.683  -19.669 1.00 15.00  ? 95  ALA   A CA   1 
ATOM   727  C  C    . ALA   A 1 95  ? 5.811   -6.172  -19.403 1.00 15.26  ? 95  ALA   A C    1 
ATOM   728  O  O    . ALA   A 1 95  ? 4.909   -5.450  -19.888 1.00 16.08  ? 95  ALA   A O    1 
ATOM   729  C  CB   . ALA   A 1 95  ? 6.835   -8.132  -20.642 1.00 14.77  ? 95  ALA   A CB   1 
ATOM   730  N  N    . SER   A 1 96  ? 6.770   -5.728  -18.594 1.00 14.75  ? 96  SER   A N    1 
ATOM   731  C  CA   . SER   A 1 96  ? 6.972   -4.304  -18.268 1.00 14.75  ? 96  SER   A CA   1 
ATOM   732  C  C    . SER   A 1 96  ? 8.440   -4.003  -17.933 1.00 14.94  ? 96  SER   A C    1 
ATOM   733  O  O    . SER   A 1 96  ? 9.210   -4.918  -17.588 1.00 13.62  ? 96  SER   A O    1 
ATOM   734  C  CB   . SER   A 1 96  ? 6.046   -3.874  -17.182 1.00 15.26  ? 96  SER   A CB   1 
ATOM   735  O  OG   . SER   A 1 96  ? 6.455   -4.426  -15.937 1.00 16.06  ? 96  SER   A OG   1 
ATOM   736  N  N    . THR   A 1 97  ? 8.786   -2.729  -18.104 1.00 15.52  ? 97  THR   A N    1 
ATOM   737  C  CA   . THR   A 1 97  ? 10.028  -2.061  -17.661 1.00 15.63  ? 97  THR   A CA   1 
ATOM   738  C  C    . THR   A 1 97  ? 9.646   -0.799  -16.878 1.00 17.10  ? 97  THR   A C    1 
ATOM   739  O  O    . THR   A 1 97  ? 8.475   -0.347  -16.986 1.00 15.40  ? 97  THR   A O    1 
ATOM   740  C  CB   . THR   A 1 97  ? 10.891  -1.757  -18.882 1.00 15.41  ? 97  THR   A CB   1 
ATOM   741  O  OG1  . THR   A 1 97  ? 10.160  -0.898  -19.745 1.00 15.14  ? 97  THR   A OG1  1 
ATOM   742  C  CG2  . THR   A 1 97  ? 11.266  -3.011  -19.633 1.00 15.51  ? 97  THR   A CG2  1 
ATOM   743  N  N    . GLY   A 1 98  ? 10.575  -0.275  -16.078 1.00 17.23  ? 98  GLY   A N    1 
ATOM   744  C  CA   . GLY   A 1 98  ? 10.316  0.884   -15.199 1.00 17.80  ? 98  GLY   A CA   1 
ATOM   745  C  C    . GLY   A 1 98  ? 11.450  1.878   -15.335 1.00 18.54  ? 98  GLY   A C    1 
ATOM   746  O  O    . GLY   A 1 98  ? 11.799  2.166   -16.485 1.00 17.35  ? 98  GLY   A O    1 
ATOM   747  N  N    . LEU   A 1 99  ? 12.048  2.300   -14.208 1.00 19.15  ? 99  LEU   A N    1 
ATOM   748  C  CA   . LEU   A 1 99  ? 13.351  3.012   -14.176 1.00 18.85  ? 99  LEU   A CA   1 
ATOM   749  C  C    . LEU   A 1 99  ? 14.414  2.098   -14.794 1.00 18.19  ? 99  LEU   A C    1 
ATOM   750  O  O    . LEU   A 1 99  ? 15.214  2.571   -15.581 1.00 19.40  ? 99  LEU   A O    1 
ATOM   751  C  CB   . LEU   A 1 99  ? 13.698  3.390   -12.736 1.00 19.20  ? 99  LEU   A CB   1 
ATOM   752  C  CG   . LEU   A 1 99  ? 15.025  4.126   -12.574 1.00 19.22  ? 99  LEU   A CG   1 
ATOM   753  C  CD1  . LEU   A 1 99  ? 14.967  5.459   -13.316 1.00 18.47  ? 99  LEU   A CD1  1 
ATOM   754  C  CD2  . LEU   A 1 99  ? 15.359  4.318   -11.090 1.00 18.65  ? 99  LEU   A CD2  1 
ATOM   755  N  N    . TYR   A 1 100 ? 14.368  0.811   -14.482 1.00 19.02  ? 100 TYR   A N    1 
ATOM   756  C  CA   . TYR   A 1 100 ? 15.253  -0.219  -15.075 1.00 20.45  ? 100 TYR   A CA   1 
ATOM   757  C  C    . TYR   A 1 100 ? 14.494  -0.955  -16.185 1.00 18.54  ? 100 TYR   A C    1 
ATOM   758  O  O    . TYR   A 1 100 ? 13.247  -0.909  -16.245 1.00 16.04  ? 100 TYR   A O    1 
ATOM   759  C  CB   . TYR   A 1 100 ? 15.764  -1.147  -13.977 1.00 21.82  ? 100 TYR   A CB   1 
ATOM   760  C  CG   . TYR   A 1 100 ? 16.521  -0.438  -12.887 1.00 25.31  ? 100 TYR   A CG   1 
ATOM   761  C  CD1  . TYR   A 1 100 ? 17.764  0.126   -13.123 1.00 27.05  ? 100 TYR   A CD1  1 
ATOM   762  C  CD2  . TYR   A 1 100 ? 16.002  -0.340  -11.611 1.00 27.66  ? 100 TYR   A CD2  1 
ATOM   763  C  CE1  . TYR   A 1 100 ? 18.479  0.745   -12.110 1.00 28.53  ? 100 TYR   A CE1  1 
ATOM   764  C  CE2  . TYR   A 1 100 ? 16.699  0.282   -10.588 1.00 29.13  ? 100 TYR   A CE2  1 
ATOM   765  C  CZ   . TYR   A 1 100 ? 17.939  0.828   -10.843 1.00 27.74  ? 100 TYR   A CZ   1 
ATOM   766  O  OH   . TYR   A 1 100 ? 18.600  1.454   -9.844  1.00 28.37  ? 100 TYR   A OH   1 
ATOM   767  N  N    . LYS   A 1 101 ? 15.250  -1.642  -17.026 1.00 18.71  ? 101 LYS   A N    1 
ATOM   768  C  CA   . LYS   A 1 101 ? 14.744  -2.169  -18.305 1.00 20.57  ? 101 LYS   A CA   1 
ATOM   769  C  C    . LYS   A 1 101 ? 15.425  -3.485  -18.663 1.00 18.23  ? 101 LYS   A C    1 
ATOM   770  O  O    . LYS   A 1 101 ? 16.476  -3.829  -18.093 1.00 17.02  ? 101 LYS   A O    1 
ATOM   771  C  CB   . LYS   A 1 101 ? 14.972  -1.132  -19.402 1.00 23.93  ? 101 LYS   A CB   1 
ATOM   772  C  CG   . LYS   A 1 101 ? 16.389  -0.599  -19.485 1.00 27.75  ? 101 LYS   A CG   1 
ATOM   773  C  CD   . LYS   A 1 101 ? 16.449  0.723   -20.209 1.00 33.78  ? 101 LYS   A CD   1 
ATOM   774  C  CE   . LYS   A 1 101 ? 17.826  1.353   -20.250 1.00 37.72  ? 101 LYS   A CE   1 
ATOM   775  N  NZ   . LYS   A 1 101 ? 17.783  2.720   -19.678 1.00 41.10  ? 101 LYS   A NZ   1 
ATOM   776  N  N    . GLU   A 1 102 ? 14.799  -4.167  -19.606 1.00 17.18  ? 102 GLU   A N    1 
ATOM   777  C  CA   . GLU   A 1 102 ? 15.232  -5.439  -20.206 1.00 18.59  ? 102 GLU   A CA   1 
ATOM   778  C  C    . GLU   A 1 102 ? 14.440  -5.612  -21.505 1.00 18.59  ? 102 GLU   A C    1 
ATOM   779  O  O    . GLU   A 1 102 ? 13.328  -5.092  -21.587 1.00 18.53  ? 102 GLU   A O    1 
ATOM   780  C  CB   . GLU   A 1 102 ? 14.973  -6.599  -19.236 1.00 18.98  ? 102 GLU   A CB   1 
ATOM   781  C  CG   . GLU   A 1 102 ? 13.494  -6.933  -19.042 1.00 19.33  ? 102 GLU   A CG   1 
ATOM   782  C  CD   . GLU   A 1 102 ? 13.139  -7.701  -17.772 1.00 20.46  ? 102 GLU   A CD   1 
ATOM   783  O  OE1  . GLU   A 1 102 ? 13.957  -7.680  -16.839 1.00 19.70  ? 102 GLU   A OE1  1 
ATOM   784  O  OE2  . GLU   A 1 102 ? 12.001  -8.292  -17.694 1.00 22.87  ? 102 GLU   A OE2  1 
ATOM   785  N  N    . THR   A 1 103 ? 14.992  -6.346  -22.465 1.00 19.72  ? 103 THR   A N    1 
ATOM   786  C  CA   . THR   A 1 103 ? 14.210  -6.980  -23.550 1.00 20.67  ? 103 THR   A CA   1 
ATOM   787  C  C    . THR   A 1 103 ? 13.278  -8.018  -22.919 1.00 20.06  ? 103 THR   A C    1 
ATOM   788  O  O    . THR   A 1 103 ? 13.697  -8.720  -21.964 1.00 17.54  ? 103 THR   A O    1 
ATOM   789  C  CB   . THR   A 1 103 ? 15.114  -7.642  -24.594 1.00 22.18  ? 103 THR   A CB   1 
ATOM   790  O  OG1  . THR   A 1 103 ? 15.772  -8.728  -23.937 1.00 23.69  ? 103 THR   A OG1  1 
ATOM   791  C  CG2  . THR   A 1 103 ? 16.122  -6.688  -25.195 1.00 21.72  ? 103 THR   A CG2  1 
ATOM   792  N  N    . ASN   A 1 104 ? 12.064  -8.101  -23.444 1.00 19.09  ? 104 ASN   A N    1 
ATOM   793  C  CA   . ASN   A 1 104 ? 11.046  -9.087  -23.037 1.00 19.10  ? 104 ASN   A CA   1 
ATOM   794  C  C    . ASN   A 1 104 ? 10.644  -9.854  -24.302 1.00 19.43  ? 104 ASN   A C    1 
ATOM   795  O  O    . ASN   A 1 104 ? 9.486   -9.774  -24.746 1.00 17.20  ? 104 ASN   A O    1 
ATOM   796  C  CB   . ASN   A 1 104 ? 9.943   -8.362  -22.285 1.00 19.65  ? 104 ASN   A CB   1 
ATOM   797  C  CG   . ASN   A 1 104 ? 10.408  -7.848  -20.943 1.00 19.47  ? 104 ASN   A CG   1 
ATOM   798  O  OD1  . ASN   A 1 104 ? 10.293  -6.657  -20.629 1.00 22.85  ? 104 ASN   A OD1  1 
ATOM   799  N  ND2  . ASN   A 1 104 ? 10.893  -8.746  -20.115 1.00 19.54  ? 104 ASN   A ND2  1 
ATOM   800  N  N    . THR   A 1 105 ? 11.609  -10.573 -24.860 1.00 19.34  ? 105 THR   A N    1 
ATOM   801  C  CA   . THR   A 1 105 ? 11.458  -11.335 -26.122 1.00 20.15  ? 105 THR   A CA   1 
ATOM   802  C  C    . THR   A 1 105 ? 10.842  -12.703 -25.818 1.00 19.83  ? 105 THR   A C    1 
ATOM   803  O  O    . THR   A 1 105 ? 11.365  -13.398 -24.954 1.00 20.76  ? 105 THR   A O    1 
ATOM   804  C  CB   . THR   A 1 105 ? 12.808  -11.395 -26.857 1.00 20.97  ? 105 THR   A CB   1 
ATOM   805  O  OG1  . THR   A 1 105 ? 13.353  -10.067 -26.883 1.00 22.84  ? 105 THR   A OG1  1 
ATOM   806  C  CG2  . THR   A 1 105 ? 12.679  -11.882 -28.278 1.00 20.31  ? 105 THR   A CG2  1 
ATOM   807  N  N    . ILE   A 1 106 ? 9.744   -13.028 -26.501 1.00 19.50  ? 106 ILE   A N    1 
ATOM   808  C  CA   . ILE   A 1 106 ? 9.082   -14.361 -26.566 1.00 18.14  ? 106 ILE   A CA   1 
ATOM   809  C  C    . ILE   A 1 106 ? 9.415   -14.975 -27.926 1.00 18.81  ? 106 ILE   A C    1 
ATOM   810  O  O    . ILE   A 1 106 ? 9.067   -14.345 -28.924 1.00 21.21  ? 106 ILE   A O    1 
ATOM   811  C  CB   . ILE   A 1 106 ? 7.562   -14.197 -26.386 1.00 17.03  ? 106 ILE   A CB   1 
ATOM   812  C  CG1  . ILE   A 1 106 ? 7.219   -13.409 -25.126 1.00 16.36  ? 106 ILE   A CG1  1 
ATOM   813  C  CG2  . ILE   A 1 106 ? 6.855   -15.543 -26.418 1.00 17.02  ? 106 ILE   A CG2  1 
ATOM   814  C  CD1  . ILE   A 1 106 ? 7.754   -14.024 -23.848 1.00 16.86  ? 106 ILE   A CD1  1 
ATOM   815  N  N    . LEU   A 1 107 ? 10.069  -16.138 -27.960 1.00 19.52  ? 107 LEU   A N    1 
ATOM   816  C  CA   . LEU   A 1 107 ? 10.487  -16.842 -29.198 1.00 19.51  ? 107 LEU   A CA   1 
ATOM   817  C  C    . LEU   A 1 107 ? 9.445   -17.899 -29.542 1.00 20.80  ? 107 LEU   A C    1 
ATOM   818  O  O    . LEU   A 1 107 ? 9.312   -18.246 -30.741 1.00 21.11  ? 107 LEU   A O    1 
ATOM   819  C  CB   . LEU   A 1 107 ? 11.852  -17.503 -29.021 1.00 20.92  ? 107 LEU   A CB   1 
ATOM   820  C  CG   . LEU   A 1 107 ? 13.064  -16.573 -29.031 1.00 22.17  ? 107 LEU   A CG   1 
ATOM   821  C  CD1  . LEU   A 1 107 ? 13.101  -15.702 -27.799 1.00 23.62  ? 107 LEU   A CD1  1 
ATOM   822  C  CD2  . LEU   A 1 107 ? 14.340  -17.375 -29.091 1.00 24.39  ? 107 LEU   A CD2  1 
ATOM   823  N  N    . SER   A 1 108 ? 8.726   -18.409 -28.546 1.00 19.88  ? 108 SER   A N    1 
ATOM   824  C  CA   . SER   A 1 108 ? 7.696   -19.442 -28.792 1.00 19.90  ? 108 SER   A CA   1 
ATOM   825  C  C    . SER   A 1 108 ? 6.658   -19.419 -27.677 1.00 18.72  ? 108 SER   A C    1 
ATOM   826  O  O    . SER   A 1 108 ? 7.005   -19.030 -26.546 1.00 18.14  ? 108 SER   A O    1 
ATOM   827  C  CB   . SER   A 1 108 ? 8.314   -20.801 -28.950 1.00 20.16  ? 108 SER   A CB   1 
ATOM   828  O  OG   . SER   A 1 108 ? 8.748   -21.289 -27.704 1.00 22.26  ? 108 SER   A OG   1 
ATOM   829  N  N    . TRP   A 1 109 ? 5.448   -19.853 -28.001 1.00 16.27  ? 109 TRP   A N    1 
ATOM   830  C  CA   . TRP   A 1 109 ? 4.344   -19.936 -27.027 1.00 16.38  ? 109 TRP   A CA   1 
ATOM   831  C  C    . TRP   A 1 109 ? 3.351   -21.000 -27.481 1.00 16.21  ? 109 TRP   A C    1 
ATOM   832  O  O    . TRP   A 1 109 ? 2.881   -20.916 -28.604 1.00 16.38  ? 109 TRP   A O    1 
ATOM   833  C  CB   . TRP   A 1 109 ? 3.721   -18.551 -26.883 1.00 16.42  ? 109 TRP   A CB   1 
ATOM   834  C  CG   . TRP   A 1 109 ? 2.583   -18.454 -25.921 1.00 16.83  ? 109 TRP   A CG   1 
ATOM   835  C  CD1  . TRP   A 1 109 ? 2.368   -19.208 -24.814 1.00 17.41  ? 109 TRP   A CD1  1 
ATOM   836  C  CD2  . TRP   A 1 109 ? 1.530   -17.490 -25.954 1.00 17.30  ? 109 TRP   A CD2  1 
ATOM   837  N  NE1  . TRP   A 1 109 ? 1.256   -18.781 -24.160 1.00 17.49  ? 109 TRP   A NE1  1 
ATOM   838  C  CE2  . TRP   A 1 109 ? 0.723   -17.726 -24.834 1.00 17.56  ? 109 TRP   A CE2  1 
ATOM   839  C  CE3  . TRP   A 1 109 ? 1.206   -16.442 -26.822 1.00 18.61  ? 109 TRP   A CE3  1 
ATOM   840  C  CZ2  . TRP   A 1 109 ? -0.413  -16.973 -24.560 1.00 19.09  ? 109 TRP   A CZ2  1 
ATOM   841  C  CZ3  . TRP   A 1 109 ? 0.084   -15.693 -26.558 1.00 19.13  ? 109 TRP   A CZ3  1 
ATOM   842  C  CH2  . TRP   A 1 109 ? -0.718  -15.960 -25.442 1.00 19.76  ? 109 TRP   A CH2  1 
ATOM   843  N  N    . SER   A 1 110 ? 3.076   -21.983 -26.628 1.00 17.43  ? 110 SER   A N    1 
ATOM   844  C  CA   . SER   A 1 110 ? 2.035   -23.006 -26.853 1.00 18.84  ? 110 SER   A CA   1 
ATOM   845  C  C    . SER   A 1 110 ? 1.091   -23.029 -25.649 1.00 19.14  ? 110 SER   A C    1 
ATOM   846  O  O    . SER   A 1 110 ? 1.514   -22.726 -24.511 1.00 19.05  ? 110 SER   A O    1 
ATOM   847  C  CB   . SER   A 1 110 ? 2.639   -24.375 -27.155 1.00 20.58  ? 110 SER   A CB   1 
ATOM   848  O  OG   . SER   A 1 110 ? 3.108   -24.990 -25.966 1.00 23.19  ? 110 SER   A OG   1 
ATOM   849  N  N    . PHE   A 1 111 ? -0.169  -23.355 -25.906 1.00 18.49  ? 111 PHE   A N    1 
ATOM   850  C  CA   . PHE   A 1 111 ? -1.218  -23.459 -24.873 1.00 17.05  ? 111 PHE   A CA   1 
ATOM   851  C  C    . PHE   A 1 111 ? -2.190  -24.577 -25.267 1.00 16.59  ? 111 PHE   A C    1 
ATOM   852  O  O    . PHE   A 1 111 ? -2.619  -24.650 -26.450 1.00 15.22  ? 111 PHE   A O    1 
ATOM   853  C  CB   . PHE   A 1 111 ? -1.908  -22.103 -24.720 1.00 16.93  ? 111 PHE   A CB   1 
ATOM   854  C  CG   . PHE   A 1 111 ? -3.078  -22.129 -23.775 1.00 16.19  ? 111 PHE   A CG   1 
ATOM   855  C  CD1  . PHE   A 1 111 ? -4.343  -22.447 -24.231 1.00 16.40  ? 111 PHE   A CD1  1 
ATOM   856  C  CD2  . PHE   A 1 111 ? -2.909  -21.865 -22.426 1.00 15.97  ? 111 PHE   A CD2  1 
ATOM   857  C  CE1  . PHE   A 1 111 ? -5.417  -22.464 -23.360 1.00 15.94  ? 111 PHE   A CE1  1 
ATOM   858  C  CE2  . PHE   A 1 111 ? -3.980  -21.893 -21.556 1.00 15.11  ? 111 PHE   A CE2  1 
ATOM   859  C  CZ   . PHE   A 1 111 ? -5.230  -22.202 -22.026 1.00 15.56  ? 111 PHE   A CZ   1 
ATOM   860  N  N    . THR   A 1 112 ? -2.541  -25.413 -24.291 1.00 16.27  ? 112 THR   A N    1 
ATOM   861  C  CA   . THR   A 1 112 ? -3.646  -26.391 -24.400 1.00 17.53  ? 112 THR   A CA   1 
ATOM   862  C  C    . THR   A 1 112 ? -4.584  -26.290 -23.204 1.00 17.30  ? 112 THR   A C    1 
ATOM   863  O  O    . THR   A 1 112 ? -4.090  -26.190 -22.078 1.00 15.96  ? 112 THR   A O    1 
ATOM   864  C  CB   . THR   A 1 112 ? -3.174  -27.844 -24.534 1.00 17.05  ? 112 THR   A CB   1 
ATOM   865  O  OG1  . THR   A 1 112 ? -2.247  -27.901 -25.615 1.00 18.15  ? 112 THR   A OG1  1 
ATOM   866  C  CG2  . THR   A 1 112 ? -4.323  -28.779 -24.852 1.00 17.22  ? 112 THR   A CG2  1 
ATOM   867  N  N    . SER   A 1 113 ? -5.885  -26.371 -23.486 1.00 17.60  ? 113 SER   A N    1 
ATOM   868  C  CA   . SER   A 1 113 ? -6.993  -26.373 -22.505 1.00 18.44  ? 113 SER   A CA   1 
ATOM   869  C  C    . SER   A 1 113 ? -7.960  -27.508 -22.833 1.00 16.97  ? 113 SER   A C    1 
ATOM   870  O  O    . SER   A 1 113 ? -8.344  -27.614 -23.985 1.00 15.73  ? 113 SER   A O    1 
ATOM   871  C  CB   . SER   A 1 113 ? -7.698  -25.044 -22.516 1.00 19.98  ? 113 SER   A CB   1 
ATOM   872  O  OG   . SER   A 1 113 ? -8.653  -25.006 -21.473 1.00 22.68  ? 113 SER   A OG   1 
ATOM   873  N  N    . LYS   A 1 114 ? -8.334  -28.308 -21.843 1.00 18.50  ? 114 LYS   A N    1 
ATOM   874  C  CA   . LYS   A 1 114 ? -9.308  -29.428 -21.966 1.00 20.66  ? 114 LYS   A CA   1 
ATOM   875  C  C    . LYS   A 1 114 ? -10.366 -29.308 -20.872 1.00 19.17  ? 114 LYS   A C    1 
ATOM   876  O  O    . LYS   A 1 114 ? -10.002 -29.236 -19.670 1.00 19.77  ? 114 LYS   A O    1 
ATOM   877  C  CB   . LYS   A 1 114 ? -8.671  -30.807 -21.792 1.00 22.63  ? 114 LYS   A CB   1 
ATOM   878  C  CG   . LYS   A 1 114 ? -7.674  -31.249 -22.849 1.00 28.44  ? 114 LYS   A CG   1 
ATOM   879  C  CD   . LYS   A 1 114 ? -7.458  -32.770 -22.793 1.00 33.30  ? 114 LYS   A CD   1 
ATOM   880  C  CE   . LYS   A 1 114 ? -6.082  -33.230 -23.244 1.00 37.17  ? 114 LYS   A CE   1 
ATOM   881  N  NZ   . LYS   A 1 114 ? -5.951  -33.282 -24.724 1.00 39.42  ? 114 LYS   A NZ   1 
ATOM   882  N  N    . LEU   A 1 115 ? -11.626 -29.295 -21.264 1.00 18.98  ? 115 LEU   A N    1 
ATOM   883  C  CA   . LEU   A 1 115 ? -12.751 -29.250 -20.305 1.00 22.39  ? 115 LEU   A CA   1 
ATOM   884  C  C    . LEU   A 1 115 ? -13.653 -30.461 -20.568 1.00 24.61  ? 115 LEU   A C    1 
ATOM   885  O  O    . LEU   A 1 115 ? -14.089 -30.618 -21.732 1.00 22.63  ? 115 LEU   A O    1 
ATOM   886  C  CB   . LEU   A 1 115 ? -13.469 -27.915 -20.488 1.00 21.27  ? 115 LEU   A CB   1 
ATOM   887  C  CG   . LEU   A 1 115 ? -14.678 -27.713 -19.593 1.00 22.02  ? 115 LEU   A CG   1 
ATOM   888  C  CD1  . LEU   A 1 115 ? -14.255 -27.450 -18.161 1.00 20.49  ? 115 LEU   A CD1  1 
ATOM   889  C  CD2  . LEU   A 1 115 ? -15.539 -26.571 -20.117 1.00 24.30  ? 115 LEU   A CD2  1 
ATOM   890  N  N    . LYS   A 1 116 ? -13.810 -31.294 -19.549 1.00 30.95  ? 116 LYS   A N    1 
ATOM   891  C  CA   . LYS   A 1 116 ? -14.467 -32.612 -19.692 1.00 44.52  ? 116 LYS   A CA   1 
ATOM   892  C  C    . LYS   A 1 116 ? -15.611 -32.805 -18.712 1.00 54.96  ? 116 LYS   A C    1 
ATOM   893  O  O    . LYS   A 1 116 ? -15.339 -33.048 -17.536 1.00 53.91  ? 116 LYS   A O    1 
ATOM   894  C  CB   . LYS   A 1 116 ? -13.445 -33.699 -19.361 1.00 54.16  ? 116 LYS   A CB   1 
ATOM   895  C  CG   . LYS   A 1 116 ? -14.008 -35.117 -19.283 1.00 65.09  ? 116 LYS   A CG   1 
ATOM   896  C  CD   . LYS   A 1 116 ? -12.972 -36.171 -18.983 1.00 68.16  ? 116 LYS   A CD   1 
ATOM   897  C  CE   . LYS   A 1 116 ? -13.449 -37.575 -19.296 1.00 75.56  ? 116 LYS   A CE   1 
ATOM   898  N  NZ   . LYS   A 1 116 ? -12.369 -38.589 -19.172 1.00 77.77  ? 116 LYS   A NZ   1 
ATOM   899  N  N    . SER   A 1 117 ? -16.839 -32.825 -19.229 1.00 71.37  ? 117 SER   A N    1 
ATOM   900  C  CA   . SER   A 1 117 ? -18.070 -33.002 -18.412 1.00 76.78  ? 117 SER   A CA   1 
ATOM   901  C  C    . SER   A 1 117 ? -18.093 -34.375 -17.720 1.00 89.92  ? 117 SER   A C    1 
ATOM   902  O  O    . SER   A 1 117 ? -17.559 -35.327 -18.266 1.00 91.57  ? 117 SER   A O    1 
ATOM   903  C  CB   . SER   A 1 117 ? -19.295 -32.793 -19.265 1.00 68.32  ? 117 SER   A CB   1 
ATOM   904  O  OG   . SER   A 1 117 ? -20.178 -31.850 -18.691 1.00 59.94  ? 117 SER   A OG   1 
ATOM   905  N  N    . ASN   A 1 118 ? -18.625 -34.436 -16.504 1.00 106.09 ? 118 ASN   A N    1 
ATOM   906  C  CA   . ASN   A 1 118 ? -18.795 -35.716 -15.766 1.00 111.72 ? 118 ASN   A CA   1 
ATOM   907  C  C    . ASN   A 1 118 ? -19.858 -36.538 -16.506 1.00 126.32 ? 118 ASN   A C    1 
ATOM   908  O  O    . ASN   A 1 118 ? -19.701 -37.770 -16.631 1.00 122.31 ? 118 ASN   A O    1 
ATOM   909  C  CB   . ASN   A 1 118 ? -19.189 -35.448 -14.305 1.00 104.09 ? 118 ASN   A CB   1 
ATOM   910  C  CG   . ASN   A 1 118 ? -19.398 -36.707 -13.493 1.00 95.47  ? 118 ASN   A CG   1 
ATOM   911  O  OD1  . ASN   A 1 118 ? -18.764 -37.723 -13.760 1.00 79.19  ? 118 ASN   A OD1  1 
ATOM   912  N  ND2  . ASN   A 1 118 ? -20.297 -36.662 -12.523 1.00 87.28  ? 118 ASN   A ND2  1 
ATOM   913  N  N    . SER   A 1 119 ? -20.912 -35.843 -16.950 1.00 141.42 ? 119 SER   A N    1 
ATOM   914  C  CA   . SER   A 1 119 ? -22.079 -36.467 -17.624 1.00 144.36 ? 119 SER   A CA   1 
ATOM   915  C  C    . SER   A 1 119 ? -21.729 -37.121 -18.954 1.00 153.46 ? 119 SER   A C    1 
ATOM   916  O  O    . SER   A 1 119 ? -22.104 -38.293 -19.148 1.00 164.04 ? 119 SER   A O    1 
ATOM   917  C  CB   . SER   A 1 119 ? -23.105 -35.393 -17.913 1.00 137.58 ? 119 SER   A CB   1 
ATOM   918  O  OG   . SER   A 1 119 ? -22.542 -34.315 -18.655 1.00 127.32 ? 119 SER   A OG   1 
ATOM   919  N  N    . THR   A 1 120 ? -21.087 -36.361 -19.842 1.00 149.20 ? 120 THR   A N    1 
ATOM   920  C  CA   . THR   A 1 120 ? -20.764 -36.874 -21.194 1.00 139.32 ? 120 THR   A CA   1 
ATOM   921  C  C    . THR   A 1 120 ? -19.605 -37.866 -21.155 1.00 129.09 ? 120 THR   A C    1 
ATOM   922  O  O    . THR   A 1 120 ? -19.736 -38.930 -21.782 1.00 132.35 ? 120 THR   A O    1 
ATOM   923  C  CB   . THR   A 1 120 ? -20.588 -35.734 -22.202 1.00 146.44 ? 120 THR   A CB   1 
ATOM   924  O  OG1  . THR   A 1 120 ? -19.184 -35.576 -22.418 1.00 148.76 ? 120 THR   A OG1  1 
ATOM   925  C  CG2  . THR   A 1 120 ? -21.186 -34.436 -21.703 1.00 146.41 ? 120 THR   A CG2  1 
ATOM   926  N  N    . HIS   A 1 121 ? -18.587 -37.555 -20.351 1.00 114.21 ? 121 HIS   A N    1 
ATOM   927  C  CA   . HIS   A 1 121 ? -17.280 -38.272 -20.342 1.00 103.93 ? 121 HIS   A CA   1 
ATOM   928  C  C    . HIS   A 1 121 ? -16.595 -38.099 -21.708 1.00 91.55  ? 121 HIS   A C    1 
ATOM   929  O  O    . HIS   A 1 121 ? -16.021 -39.073 -22.199 1.00 81.39  ? 121 HIS   A O    1 
ATOM   930  C  CB   . HIS   A 1 121 ? -17.360 -39.704 -19.793 1.00 106.93 ? 121 HIS   A CB   1 
ATOM   931  C  CG   . HIS   A 1 121 ? -16.680 -39.862 -18.481 1.00 111.64 ? 121 HIS   A CG   1 
ATOM   932  N  ND1  . HIS   A 1 121 ? -15.366 -40.250 -18.380 1.00 119.32 ? 121 HIS   A ND1  1 
ATOM   933  C  CD2  . HIS   A 1 121 ? -17.118 -39.670 -17.220 1.00 109.45 ? 121 HIS   A CD2  1 
ATOM   934  C  CE1  . HIS   A 1 121 ? -15.016 -40.292 -17.113 1.00 117.21 ? 121 HIS   A CE1  1 
ATOM   935  N  NE2  . HIS   A 1 121 ? -16.076 -39.950 -16.381 1.00 112.85 ? 121 HIS   A NE2  1 
ATOM   936  N  N    . GLU   A 1 122 ? -16.726 -36.895 -22.284 1.00 75.22  ? 122 GLU   A N    1 
ATOM   937  C  CA   . GLU   A 1 122 ? -16.129 -36.440 -23.559 1.00 64.44  ? 122 GLU   A CA   1 
ATOM   938  C  C    . GLU   A 1 122 ? -15.556 -35.031 -23.325 1.00 55.36  ? 122 GLU   A C    1 
ATOM   939  O  O    . GLU   A 1 122 ? -16.070 -34.319 -22.476 1.00 48.86  ? 122 GLU   A O    1 
ATOM   940  C  CB   . GLU   A 1 122 ? -17.122 -36.565 -24.711 1.00 66.71  ? 122 GLU   A CB   1 
ATOM   941  C  CG   . GLU   A 1 122 ? -16.457 -36.487 -26.070 1.00 68.64  ? 122 GLU   A CG   1 
ATOM   942  C  CD   . GLU   A 1 122 ? -16.245 -37.791 -26.819 1.00 69.18  ? 122 GLU   A CD   1 
ATOM   943  O  OE1  . GLU   A 1 122 ? -16.821 -38.796 -26.400 1.00 74.71  ? 122 GLU   A OE1  1 
ATOM   944  O  OE2  . GLU   A 1 122 ? -15.503 -37.798 -27.800 1.00 60.10  ? 122 GLU   A OE2  1 
ATOM   945  N  N    . THR   A 1 123 ? -14.570 -34.625 -24.112 1.00 46.81  ? 123 THR   A N    1 
ATOM   946  C  CA   . THR   A 1 123 ? -13.822 -33.366 -23.810 1.00 42.08  ? 123 THR   A CA   1 
ATOM   947  C  C    . THR   A 1 123 ? -13.999 -32.308 -24.918 1.00 35.09  ? 123 THR   A C    1 
ATOM   948  O  O    . THR   A 1 123 ? -14.111 -32.669 -26.103 1.00 31.92  ? 123 THR   A O    1 
ATOM   949  C  CB   . THR   A 1 123 ? -12.339 -33.650 -23.512 1.00 42.75  ? 123 THR   A CB   1 
ATOM   950  O  OG1  . THR   A 1 123 ? -11.637 -33.815 -24.742 1.00 47.13  ? 123 THR   A OG1  1 
ATOM   951  C  CG2  . THR   A 1 123 ? -12.128 -34.871 -22.643 1.00 42.27  ? 123 THR   A CG2  1 
ATOM   952  N  N    . ASN   A 1 124 ? -14.031 -31.031 -24.517 1.00 28.62  ? 124 ASN   A N    1 
ATOM   953  C  CA   . ASN   A 1 124 ? -13.850 -29.852 -25.407 1.00 25.33  ? 124 ASN   A CA   1 
ATOM   954  C  C    . ASN   A 1 124 ? -12.388 -29.403 -25.251 1.00 23.03  ? 124 ASN   A C    1 
ATOM   955  O  O    . ASN   A 1 124 ? -11.818 -29.577 -24.148 1.00 22.72  ? 124 ASN   A O    1 
ATOM   956  C  CB   . ASN   A 1 124 ? -14.867 -28.751 -25.087 1.00 23.14  ? 124 ASN   A CB   1 
ATOM   957  C  CG   . ASN   A 1 124 ? -16.254 -28.979 -25.669 1.00 23.10  ? 124 ASN   A CG   1 
ATOM   958  O  OD1  . ASN   A 1 124 ? -16.667 -30.102 -25.924 1.00 20.28  ? 124 ASN   A OD1  1 
ATOM   959  N  ND2  . ASN   A 1 124 ? -16.998 -27.900 -25.887 1.00 22.94  ? 124 ASN   A ND2  1 
ATOM   960  N  N    . ALA   A 1 125 ? -11.748 -28.898 -26.303 1.00 21.87  ? 125 ALA   A N    1 
ATOM   961  C  CA   . ALA   A 1 125 ? -10.301 -28.557 -26.231 1.00 20.80  ? 125 ALA   A CA   1 
ATOM   962  C  C    . ALA   A 1 125 ? -9.923  -27.441 -27.206 1.00 19.28  ? 125 ALA   A C    1 
ATOM   963  O  O    . ALA   A 1 125 ? -10.506 -27.361 -28.319 1.00 18.46  ? 125 ALA   A O    1 
ATOM   964  C  CB   . ALA   A 1 125 ? -9.441  -29.783 -26.458 1.00 20.96  ? 125 ALA   A CB   1 
ATOM   965  N  N    . LEU   A 1 126 ? -8.946  -26.643 -26.777 1.00 17.67  ? 126 LEU   A N    1 
ATOM   966  C  CA   . LEU   A 1 126 ? -8.269  -25.598 -27.565 1.00 17.66  ? 126 LEU   A CA   1 
ATOM   967  C  C    . LEU   A 1 126 ? -6.759  -25.808 -27.443 1.00 17.63  ? 126 LEU   A C    1 
ATOM   968  O  O    . LEU   A 1 126 ? -6.232  -25.935 -26.302 1.00 18.06  ? 126 LEU   A O    1 
ATOM   969  C  CB   . LEU   A 1 126 ? -8.673  -24.212 -27.041 1.00 17.81  ? 126 LEU   A CB   1 
ATOM   970  C  CG   . LEU   A 1 126 ? -8.084  -23.049 -27.846 1.00 19.08  ? 126 LEU   A CG   1 
ATOM   971  C  CD1  . LEU   A 1 126 ? -8.732  -22.983 -29.223 1.00 18.93  ? 126 LEU   A CD1  1 
ATOM   972  C  CD2  . LEU   A 1 126 ? -8.206  -21.702 -27.118 1.00 18.17  ? 126 LEU   A CD2  1 
ATOM   973  N  N    . HIS   A 1 127 ? -6.063  -25.768 -28.573 1.00 16.67  ? 127 HIS   A N    1 
ATOM   974  C  CA   . HIS   A 1 127 ? -4.587  -25.785 -28.604 1.00 17.04  ? 127 HIS   A CA   1 
ATOM   975  C  C    . HIS   A 1 127 ? -4.122  -24.789 -29.662 1.00 16.69  ? 127 HIS   A C    1 
ATOM   976  O  O    . HIS   A 1 127 ? -4.665  -24.826 -30.787 1.00 17.05  ? 127 HIS   A O    1 
ATOM   977  C  CB   . HIS   A 1 127 ? -4.069  -27.206 -28.867 1.00 18.15  ? 127 HIS   A CB   1 
ATOM   978  C  CG   . HIS   A 1 127 ? -2.621  -27.257 -29.165 1.00 18.41  ? 127 HIS   A CG   1 
ATOM   979  N  ND1  . HIS   A 1 127 ? -1.673  -27.181 -28.179 1.00 20.65  ? 127 HIS   A ND1  1 
ATOM   980  C  CD2  . HIS   A 1 127 ? -1.960  -27.307 -30.333 1.00 20.30  ? 127 HIS   A CD2  1 
ATOM   981  C  CE1  . HIS   A 1 127 ? -0.473  -27.223 -28.719 1.00 21.56  ? 127 HIS   A CE1  1 
ATOM   982  N  NE2  . HIS   A 1 127 ? -0.625  -27.293 -30.044 1.00 22.69  ? 127 HIS   A NE2  1 
ATOM   983  N  N    . PHE   A 1 128 ? -3.139  -23.959 -29.316 1.00 14.92  ? 128 PHE   A N    1 
ATOM   984  C  CA   . PHE   A 1 128 ? -2.376  -23.187 -30.307 1.00 15.43  ? 128 PHE   A CA   1 
ATOM   985  C  C    . PHE   A 1 128 ? -0.896  -23.304 -29.975 1.00 16.53  ? 128 PHE   A C    1 
ATOM   986  O  O    . PHE   A 1 128 ? -0.531  -23.566 -28.818 1.00 14.56  ? 128 PHE   A O    1 
ATOM   987  C  CB   . PHE   A 1 128 ? -2.884  -21.750 -30.379 1.00 15.30  ? 128 PHE   A CB   1 
ATOM   988  C  CG   . PHE   A 1 128 ? -2.765  -20.958 -29.106 1.00 15.36  ? 128 PHE   A CG   1 
ATOM   989  C  CD1  . PHE   A 1 128 ? -1.561  -20.373 -28.754 1.00 14.83  ? 128 PHE   A CD1  1 
ATOM   990  C  CD2  . PHE   A 1 128 ? -3.854  -20.790 -28.268 1.00 15.56  ? 128 PHE   A CD2  1 
ATOM   991  C  CE1  . PHE   A 1 128 ? -1.441  -19.650 -27.583 1.00 15.19  ? 128 PHE   A CE1  1 
ATOM   992  C  CE2  . PHE   A 1 128 ? -3.730  -20.056 -27.094 1.00 15.45  ? 128 PHE   A CE2  1 
ATOM   993  C  CZ   . PHE   A 1 128 ? -2.529  -19.483 -26.757 1.00 15.32  ? 128 PHE   A CZ   1 
ATOM   994  N  N    . MET   A 1 129 ? -0.086  -23.088 -31.005 1.00 19.34  ? 129 MET   A N    1 
ATOM   995  C  CA   . MET   A 1 129 ? 1.393   -23.178 -30.963 1.00 22.06  ? 129 MET   A CA   1 
ATOM   996  C  C    . MET   A 1 129 ? 1.972   -22.156 -31.937 1.00 20.18  ? 129 MET   A C    1 
ATOM   997  O  O    . MET   A 1 129 ? 1.620   -22.208 -33.121 1.00 17.62  ? 129 MET   A O    1 
ATOM   998  C  CB   . MET   A 1 129 ? 1.862   -24.576 -31.376 1.00 24.46  ? 129 MET   A CB   1 
ATOM   999  C  CG   . MET   A 1 129 ? 3.365   -24.743 -31.309 1.00 26.87  ? 129 MET   A CG   1 
ATOM   1000 S  SD   . MET   A 1 129 ? 3.896   -26.446 -31.563 1.00 33.37  ? 129 MET   A SD   1 
ATOM   1001 C  CE   . MET   A 1 129 ? 2.426   -27.385 -31.141 1.00 32.58  ? 129 MET   A CE   1 
ATOM   1002 N  N    . PHE   A 1 130 ? 2.792   -21.255 -31.418 1.00 19.79  ? 130 PHE   A N    1 
ATOM   1003 C  CA   . PHE   A 1 130 ? 3.569   -20.271 -32.198 1.00 21.03  ? 130 PHE   A CA   1 
ATOM   1004 C  C    . PHE   A 1 130 ? 5.028   -20.618 -31.976 1.00 21.70  ? 130 PHE   A C    1 
ATOM   1005 O  O    . PHE   A 1 130 ? 5.478   -20.469 -30.855 1.00 22.78  ? 130 PHE   A O    1 
ATOM   1006 C  CB   . PHE   A 1 130 ? 3.309   -18.827 -31.760 1.00 20.53  ? 130 PHE   A CB   1 
ATOM   1007 C  CG   . PHE   A 1 130 ? 1.869   -18.413 -31.698 1.00 21.04  ? 130 PHE   A CG   1 
ATOM   1008 C  CD1  . PHE   A 1 130 ? 1.105   -18.331 -32.852 1.00 24.36  ? 130 PHE   A CD1  1 
ATOM   1009 C  CD2  . PHE   A 1 130 ? 1.274   -18.088 -30.492 1.00 22.34  ? 130 PHE   A CD2  1 
ATOM   1010 C  CE1  . PHE   A 1 130 ? -0.228  -17.950 -32.800 1.00 24.00  ? 130 PHE   A CE1  1 
ATOM   1011 C  CE2  . PHE   A 1 130 ? -0.057  -17.704 -30.436 1.00 23.45  ? 130 PHE   A CE2  1 
ATOM   1012 C  CZ   . PHE   A 1 130 ? -0.802  -17.614 -31.595 1.00 24.19  ? 130 PHE   A CZ   1 
ATOM   1013 N  N    . ASN   A 1 131 ? 5.698   -21.122 -33.007 1.00 26.14  ? 131 ASN   A N    1 
ATOM   1014 C  CA   . ASN   A 1 131 ? 7.171   -21.248 -33.034 1.00 28.54  ? 131 ASN   A CA   1 
ATOM   1015 C  C    . ASN   A 1 131 ? 7.762   -20.039 -33.759 1.00 29.10  ? 131 ASN   A C    1 
ATOM   1016 O  O    . ASN   A 1 131 ? 8.963   -19.844 -33.610 1.00 27.51  ? 131 ASN   A O    1 
ATOM   1017 C  CB   . ASN   A 1 131 ? 7.607   -22.593 -33.611 1.00 31.54  ? 131 ASN   A CB   1 
ATOM   1018 C  CG   . ASN   A 1 131 ? 7.588   -23.687 -32.563 1.00 35.44  ? 131 ASN   A CG   1 
ATOM   1019 O  OD1  . ASN   A 1 131 ? 7.957   -23.453 -31.412 1.00 38.34  ? 131 ASN   A OD1  1 
ATOM   1020 N  ND2  . ASN   A 1 131 ? 7.156   -24.879 -32.938 1.00 36.43  ? 131 ASN   A ND2  1 
ATOM   1021 N  N    . GLN   A 1 132 ? 6.954   -19.269 -34.503 1.00 31.72  ? 132 GLN   A N    1 
ATOM   1022 C  CA   . GLN   A 1 132 ? 7.390   -18.008 -35.171 1.00 34.15  ? 132 GLN   A CA   1 
ATOM   1023 C  C    . GLN   A 1 132 ? 6.223   -17.016 -35.133 1.00 33.12  ? 132 GLN   A C    1 
ATOM   1024 O  O    . GLN   A 1 132 ? 5.064   -17.444 -35.282 1.00 32.34  ? 132 GLN   A O    1 
ATOM   1025 C  CB   . GLN   A 1 132 ? 7.849   -18.202 -36.629 1.00 37.33  ? 132 GLN   A CB   1 
ATOM   1026 C  CG   . GLN   A 1 132 ? 9.121   -19.038 -36.825 1.00 44.80  ? 132 GLN   A CG   1 
ATOM   1027 C  CD   . GLN   A 1 132 ? 10.407  -18.481 -36.238 1.00 47.61  ? 132 GLN   A CD   1 
ATOM   1028 O  OE1  . GLN   A 1 132 ? 10.778  -17.327 -36.438 1.00 50.62  ? 132 GLN   A OE1  1 
ATOM   1029 N  NE2  . GLN   A 1 132 ? 11.137  -19.325 -35.527 1.00 48.85  ? 132 GLN   A NE2  1 
ATOM   1030 N  N    . PHE   A 1 133 ? 6.524   -15.732 -34.965 1.00 29.93  ? 133 PHE   A N    1 
ATOM   1031 C  CA   . PHE   A 1 133 ? 5.506   -14.655 -34.951 1.00 31.65  ? 133 PHE   A CA   1 
ATOM   1032 C  C    . PHE   A 1 133 ? 5.656   -13.872 -36.253 1.00 34.04  ? 133 PHE   A C    1 
ATOM   1033 O  O    . PHE   A 1 133 ? 6.781   -13.717 -36.772 1.00 34.69  ? 133 PHE   A O    1 
ATOM   1034 C  CB   . PHE   A 1 133 ? 5.619   -13.806 -33.683 1.00 28.58  ? 133 PHE   A CB   1 
ATOM   1035 C  CG   . PHE   A 1 133 ? 5.337   -14.562 -32.407 1.00 27.11  ? 133 PHE   A CG   1 
ATOM   1036 C  CD1  . PHE   A 1 133 ? 6.341   -15.291 -31.777 1.00 27.19  ? 133 PHE   A CD1  1 
ATOM   1037 C  CD2  . PHE   A 1 133 ? 4.066   -14.568 -31.848 1.00 26.08  ? 133 PHE   A CD2  1 
ATOM   1038 C  CE1  . PHE   A 1 133 ? 6.083   -16.001 -30.613 1.00 25.96  ? 133 PHE   A CE1  1 
ATOM   1039 C  CE2  . PHE   A 1 133 ? 3.818   -15.261 -30.671 1.00 26.64  ? 133 PHE   A CE2  1 
ATOM   1040 C  CZ   . PHE   A 1 133 ? 4.824   -15.979 -30.059 1.00 25.92  ? 133 PHE   A CZ   1 
ATOM   1041 N  N    . SER   A 1 134 ? 4.519   -13.431 -36.769 1.00 35.81  ? 134 SER   A N    1 
ATOM   1042 C  CA   . SER   A 1 134 ? 4.364   -12.783 -38.091 1.00 39.69  ? 134 SER   A CA   1 
ATOM   1043 C  C    . SER   A 1 134 ? 4.146   -11.281 -37.884 1.00 38.36  ? 134 SER   A C    1 
ATOM   1044 O  O    . SER   A 1 134 ? 3.586   -10.919 -36.834 1.00 33.83  ? 134 SER   A O    1 
ATOM   1045 C  CB   . SER   A 1 134 ? 3.217   -13.406 -38.834 1.00 40.34  ? 134 SER   A CB   1 
ATOM   1046 O  OG   . SER   A 1 134 ? 2.735   -12.489 -39.796 1.00 47.97  ? 134 SER   A OG   1 
ATOM   1047 N  N    . LYS   A 1 135 ? 4.511   -10.470 -38.882 1.00 41.56  ? 135 LYS   A N    1 
ATOM   1048 C  CA   . LYS   A 1 135 ? 4.430   -8.985  -38.868 1.00 44.84  ? 135 LYS   A CA   1 
ATOM   1049 C  C    . LYS   A 1 135 ? 2.982   -8.558  -38.607 1.00 44.10  ? 135 LYS   A C    1 
ATOM   1050 O  O    . LYS   A 1 135 ? 2.788   -7.526  -37.945 1.00 46.19  ? 135 LYS   A O    1 
ATOM   1051 C  CB   . LYS   A 1 135 ? 4.896   -8.381  -40.199 1.00 51.94  ? 135 LYS   A CB   1 
ATOM   1052 C  CG   . LYS   A 1 135 ? 6.385   -8.500  -40.524 1.00 59.15  ? 135 LYS   A CG   1 
ATOM   1053 C  CD   . LYS   A 1 135 ? 6.897   -9.914  -40.822 1.00 64.66  ? 135 LYS   A CD   1 
ATOM   1054 C  CE   . LYS   A 1 135 ? 6.160   -10.638 -41.935 1.00 66.35  ? 135 LYS   A CE   1 
ATOM   1055 N  NZ   . LYS   A 1 135 ? 6.209   -12.110 -41.755 1.00 66.31  ? 135 LYS   A NZ   1 
ATOM   1056 N  N    . ASP   A 1 136 ? 2.003   -9.322  -39.100 1.00 41.96  ? 136 ASP   A N    1 
ATOM   1057 C  CA   . ASP   A 1 136 ? 0.559   -8.996  -38.962 1.00 44.37  ? 136 ASP   A CA   1 
ATOM   1058 C  C    . ASP   A 1 136 ? -0.146  -10.242 -38.398 1.00 42.48  ? 136 ASP   A C    1 
ATOM   1059 O  O    . ASP   A 1 136 ? -0.708  -11.027 -39.186 1.00 48.09  ? 136 ASP   A O    1 
ATOM   1060 C  CB   . ASP   A 1 136 ? 0.060   -8.485  -40.317 1.00 49.27  ? 136 ASP   A CB   1 
ATOM   1061 C  CG   . ASP   A 1 136 ? -1.438  -8.275  -40.444 1.00 54.83  ? 136 ASP   A CG   1 
ATOM   1062 O  OD1  . ASP   A 1 136 ? -1.993  -7.564  -39.589 1.00 59.20  ? 136 ASP   A OD1  1 
ATOM   1063 O  OD2  . ASP   A 1 136 ? -2.029  -8.809  -41.423 1.00 56.95  ? 136 ASP   A OD2  1 
ATOM   1064 N  N    . GLN   A 1 137 ? -0.083  -10.444 -37.082 1.00 35.22  ? 137 GLN   A N    1 
ATOM   1065 C  CA   . GLN   A 1 137 ? -0.464  -11.722 -36.423 1.00 33.90  ? 137 GLN   A CA   1 
ATOM   1066 C  C    . GLN   A 1 137 ? -1.891  -11.596 -35.896 1.00 30.32  ? 137 GLN   A C    1 
ATOM   1067 O  O    . GLN   A 1 137 ? -2.062  -11.133 -34.767 1.00 29.44  ? 137 GLN   A O    1 
ATOM   1068 C  CB   . GLN   A 1 137 ? 0.520   -12.060 -35.303 1.00 35.98  ? 137 GLN   A CB   1 
ATOM   1069 C  CG   . GLN   A 1 137 ? 0.287   -13.426 -34.675 1.00 36.62  ? 137 GLN   A CG   1 
ATOM   1070 C  CD   . GLN   A 1 137 ? 1.009   -14.536 -35.389 1.00 37.88  ? 137 GLN   A CD   1 
ATOM   1071 O  OE1  . GLN   A 1 137 ? 2.128   -14.362 -35.880 1.00 35.37  ? 137 GLN   A OE1  1 
ATOM   1072 N  NE2  . GLN   A 1 137 ? 0.375   -15.702 -35.414 1.00 39.71  ? 137 GLN   A NE2  1 
ATOM   1073 N  N    . LYS   A 1 138 ? -2.861  -12.036 -36.693 1.00 29.75  ? 138 LYS   A N    1 
ATOM   1074 C  CA   . LYS   A 1 138 ? -4.300  -11.707 -36.543 1.00 29.55  ? 138 LYS   A CA   1 
ATOM   1075 C  C    . LYS   A 1 138 ? -4.956  -12.576 -35.469 1.00 27.82  ? 138 LYS   A C    1 
ATOM   1076 O  O    . LYS   A 1 138 ? -6.024  -12.161 -34.961 1.00 27.82  ? 138 LYS   A O    1 
ATOM   1077 C  CB   . LYS   A 1 138 ? -4.993  -11.843 -37.900 1.00 32.64  ? 138 LYS   A CB   1 
ATOM   1078 C  CG   . LYS   A 1 138 ? -4.475  -10.860 -38.934 1.00 33.81  ? 138 LYS   A CG   1 
ATOM   1079 C  CD   . LYS   A 1 138 ? -5.503  -10.399 -39.922 1.00 38.75  ? 138 LYS   A CD   1 
ATOM   1080 C  CE   . LYS   A 1 138 ? -4.921  -9.407  -40.907 1.00 41.45  ? 138 LYS   A CE   1 
ATOM   1081 N  NZ   . LYS   A 1 138 ? -5.949  -8.942  -41.859 1.00 44.29  ? 138 LYS   A NZ   1 
ATOM   1082 N  N    . ASP   A 1 139 ? -4.332  -13.690 -35.075 1.00 25.74  ? 139 ASP   A N    1 
ATOM   1083 C  CA   . ASP   A 1 139 ? -4.839  -14.519 -33.944 1.00 25.79  ? 139 ASP   A CA   1 
ATOM   1084 C  C    . ASP   A 1 139 ? -4.290  -14.021 -32.589 1.00 23.14  ? 139 ASP   A C    1 
ATOM   1085 O  O    . ASP   A 1 139 ? -4.528  -14.701 -31.586 1.00 23.13  ? 139 ASP   A O    1 
ATOM   1086 C  CB   . ASP   A 1 139 ? -4.629  -16.011 -34.211 1.00 26.98  ? 139 ASP   A CB   1 
ATOM   1087 C  CG   . ASP   A 1 139 ? -3.206  -16.423 -34.533 1.00 31.41  ? 139 ASP   A CG   1 
ATOM   1088 O  OD1  . ASP   A 1 139 ? -2.320  -15.531 -34.581 1.00 32.76  ? 139 ASP   A OD1  1 
ATOM   1089 O  OD2  . ASP   A 1 139 ? -2.996  -17.641 -34.757 1.00 32.55  ? 139 ASP   A OD2  1 
ATOM   1090 N  N    . LEU   A 1 140 ? -3.641  -12.856 -32.535 1.00 21.83  ? 140 LEU   A N    1 
ATOM   1091 C  CA   . LEU   A 1 140 ? -3.160  -12.236 -31.271 1.00 21.61  ? 140 LEU   A CA   1 
ATOM   1092 C  C    . LEU   A 1 140 ? -3.743  -10.824 -31.143 1.00 20.78  ? 140 LEU   A C    1 
ATOM   1093 O  O    . LEU   A 1 140 ? -3.779  -10.094 -32.130 1.00 20.38  ? 140 LEU   A O    1 
ATOM   1094 C  CB   . LEU   A 1 140 ? -1.621  -12.197 -31.255 1.00 22.56  ? 140 LEU   A CB   1 
ATOM   1095 C  CG   . LEU   A 1 140 ? -0.902  -13.542 -31.097 1.00 23.34  ? 140 LEU   A CG   1 
ATOM   1096 C  CD1  . LEU   A 1 140 ? 0.594   -13.354 -30.891 1.00 23.98  ? 140 LEU   A CD1  1 
ATOM   1097 C  CD2  . LEU   A 1 140 ? -1.475  -14.356 -29.945 1.00 23.28  ? 140 LEU   A CD2  1 
ATOM   1098 N  N    . ILE   A 1 141 ? -4.212  -10.465 -29.958 1.00 18.78  ? 141 ILE   A N    1 
ATOM   1099 C  CA   . ILE   A 1 141 ? -4.557  -9.067  -29.633 1.00 19.00  ? 141 ILE   A CA   1 
ATOM   1100 C  C    . ILE   A 1 141 ? -3.323  -8.478  -28.939 1.00 18.69  ? 141 ILE   A C    1 
ATOM   1101 O  O    . ILE   A 1 141 ? -3.004  -8.926  -27.852 1.00 17.66  ? 141 ILE   A O    1 
ATOM   1102 C  CB   . ILE   A 1 141 ? -5.824  -9.010  -28.768 1.00 19.63  ? 141 ILE   A CB   1 
ATOM   1103 C  CG1  . ILE   A 1 141 ? -7.022  -9.705  -29.422 1.00 19.77  ? 141 ILE   A CG1  1 
ATOM   1104 C  CG2  . ILE   A 1 141 ? -6.158  -7.575  -28.399 1.00 19.71  ? 141 ILE   A CG2  1 
ATOM   1105 C  CD1  . ILE   A 1 141 ? -8.053  -10.166 -28.413 1.00 19.38  ? 141 ILE   A CD1  1 
ATOM   1106 N  N    . LEU   A 1 142 ? -2.649  -7.528  -29.574 1.00 17.66  ? 142 LEU   A N    1 
ATOM   1107 C  CA   . LEU   A 1 142 ? -1.470  -6.829  -29.010 1.00 18.05  ? 142 LEU   A CA   1 
ATOM   1108 C  C    . LEU   A 1 142 ? -1.961  -5.579  -28.293 1.00 17.92  ? 142 LEU   A C    1 
ATOM   1109 O  O    . LEU   A 1 142 ? -2.739  -4.877  -28.877 1.00 17.95  ? 142 LEU   A O    1 
ATOM   1110 C  CB   . LEU   A 1 142 ? -0.514  -6.462  -30.147 1.00 18.26  ? 142 LEU   A CB   1 
ATOM   1111 C  CG   . LEU   A 1 142 ? -0.027  -7.631  -30.989 1.00 17.91  ? 142 LEU   A CG   1 
ATOM   1112 C  CD1  . LEU   A 1 142 ? 1.027   -7.179  -31.988 1.00 18.15  ? 142 LEU   A CD1  1 
ATOM   1113 C  CD2  . LEU   A 1 142 ? 0.499   -8.737  -30.079 1.00 18.66  ? 142 LEU   A CD2  1 
ATOM   1114 N  N    . GLN   A 1 143 ? -1.510  -5.324  -27.063 1.00 19.13  ? 143 GLN   A N    1 
ATOM   1115 C  CA   . GLN   A 1 143 ? -1.885  -4.119  -26.274 1.00 17.55  ? 143 GLN   A CA   1 
ATOM   1116 C  C    . GLN   A 1 143 ? -0.586  -3.417  -25.882 1.00 17.22  ? 143 GLN   A C    1 
ATOM   1117 O  O    . GLN   A 1 143 ? 0.437   -4.109  -25.743 1.00 17.38  ? 143 GLN   A O    1 
ATOM   1118 C  CB   . GLN   A 1 143 ? -2.693  -4.534  -25.047 1.00 18.73  ? 143 GLN   A CB   1 
ATOM   1119 C  CG   . GLN   A 1 143 ? -3.880  -5.448  -25.373 1.00 19.18  ? 143 GLN   A CG   1 
ATOM   1120 C  CD   . GLN   A 1 143 ? -4.650  -5.876  -24.144 1.00 19.29  ? 143 GLN   A CD   1 
ATOM   1121 O  OE1  . GLN   A 1 143 ? -4.066  -6.107  -23.083 1.00 20.87  ? 143 GLN   A OE1  1 
ATOM   1122 N  NE2  . GLN   A 1 143 ? -5.964  -6.022  -24.274 1.00 17.28  ? 143 GLN   A NE2  1 
ATOM   1123 N  N    . GLY   A 1 144 ? -0.615  -2.100  -25.729 1.00 16.36  ? 144 GLY   A N    1 
ATOM   1124 C  CA   . GLY   A 1 144 ? 0.547   -1.284  -25.340 1.00 16.49  ? 144 GLY   A CA   1 
ATOM   1125 C  C    . GLY   A 1 144 ? 1.661   -1.336  -26.375 1.00 17.31  ? 144 GLY   A C    1 
ATOM   1126 O  O    . GLY   A 1 144 ? 1.380   -1.128  -27.581 1.00 14.88  ? 144 GLY   A O    1 
ATOM   1127 N  N    . ASP   A 1 145 ? 2.894   -1.596  -25.924 1.00 18.62  ? 145 ASP   A N    1 
ATOM   1128 C  CA   . ASP   A 1 145 ? 4.098   -1.512  -26.778 1.00 20.35  ? 145 ASP   A CA   1 
ATOM   1129 C  C    . ASP   A 1 145 ? 4.371   -2.856  -27.467 1.00 20.25  ? 145 ASP   A C    1 
ATOM   1130 O  O    . ASP   A 1 145 ? 5.379   -2.941  -28.146 1.00 21.06  ? 145 ASP   A O    1 
ATOM   1131 C  CB   . ASP   A 1 145 ? 5.296   -1.044  -25.951 1.00 24.39  ? 145 ASP   A CB   1 
ATOM   1132 C  CG   . ASP   A 1 145 ? 5.076   0.291   -25.243 1.00 26.34  ? 145 ASP   A CG   1 
ATOM   1133 O  OD1  . ASP   A 1 145 ? 4.210   1.048   -25.693 1.00 27.81  ? 145 ASP   A OD1  1 
ATOM   1134 O  OD2  . ASP   A 1 145 ? 5.770   0.552   -24.230 1.00 27.27  ? 145 ASP   A OD2  1 
ATOM   1135 N  N    . ALA   A 1 146 ? 3.529   -3.880  -27.313 1.00 19.45  ? 146 ALA   A N    1 
ATOM   1136 C  CA   . ALA   A 1 146 ? 3.826   -5.225  -27.862 1.00 19.99  ? 146 ALA   A CA   1 
ATOM   1137 C  C    . ALA   A 1 146 ? 3.792   -5.196  -29.397 1.00 19.43  ? 146 ALA   A C    1 
ATOM   1138 O  O    . ALA   A 1 146 ? 2.807   -4.719  -29.945 1.00 19.16  ? 146 ALA   A O    1 
ATOM   1139 C  CB   . ALA   A 1 146 ? 2.833   -6.230  -27.321 1.00 20.34  ? 146 ALA   A CB   1 
ATOM   1140 N  N    . THR   A 1 147 ? 4.794   -5.773  -30.054 1.00 20.27  ? 147 THR   A N    1 
ATOM   1141 C  CA   . THR   A 1 147 ? 4.904   -5.888  -31.532 1.00 22.12  ? 147 THR   A CA   1 
ATOM   1142 C  C    . THR   A 1 147 ? 5.342   -7.312  -31.892 1.00 23.38  ? 147 THR   A C    1 
ATOM   1143 O  O    . THR   A 1 147 ? 5.912   -7.989  -31.006 1.00 23.59  ? 147 THR   A O    1 
ATOM   1144 C  CB   . THR   A 1 147 ? 5.889   -4.845  -32.087 1.00 24.03  ? 147 THR   A CB   1 
ATOM   1145 O  OG1  . THR   A 1 147 ? 7.182   -5.234  -31.629 1.00 26.07  ? 147 THR   A OG1  1 
ATOM   1146 C  CG2  . THR   A 1 147 ? 5.615   -3.425  -31.627 1.00 24.11  ? 147 THR   A CG2  1 
ATOM   1147 N  N    . THR   A 1 148 ? 5.109   -7.741  -33.138 1.00 25.37  ? 148 THR   A N    1 
ATOM   1148 C  CA   . THR   A 1 148 ? 5.545   -9.054  -33.691 1.00 29.05  ? 148 THR   A CA   1 
ATOM   1149 C  C    . THR   A 1 148 ? 6.355   -8.861  -34.973 1.00 33.78  ? 148 THR   A C    1 
ATOM   1150 O  O    . THR   A 1 148 ? 6.325   -7.743  -35.518 1.00 34.48  ? 148 THR   A O    1 
ATOM   1151 C  CB   . THR   A 1 148 ? 4.348   -9.976  -33.933 1.00 30.91  ? 148 THR   A CB   1 
ATOM   1152 O  OG1  . THR   A 1 148 ? 3.324   -9.294  -34.655 1.00 31.45  ? 148 THR   A OG1  1 
ATOM   1153 C  CG2  . THR   A 1 148 ? 3.766   -10.500 -32.640 1.00 31.60  ? 148 THR   A CG2  1 
ATOM   1154 N  N    . GLY   A 1 149 ? 7.099   -9.895  -35.394 1.00 37.17  ? 149 GLY   A N    1 
ATOM   1155 C  CA   . GLY   A 1 149 ? 7.698   -10.007 -36.743 1.00 40.95  ? 149 GLY   A CA   1 
ATOM   1156 C  C    . GLY   A 1 149 ? 9.190   -9.683  -36.795 1.00 46.51  ? 149 GLY   A C    1 
ATOM   1157 O  O    . GLY   A 1 149 ? 9.843   -10.070 -37.799 1.00 45.91  ? 149 GLY   A O    1 
ATOM   1158 N  N    . THR   A 1 150 ? 9.728   -8.990  -35.783 1.00 46.12  ? 150 THR   A N    1 
ATOM   1159 C  CA   . THR   A 1 150 ? 11.183  -8.697  -35.663 1.00 48.23  ? 150 THR   A CA   1 
ATOM   1160 C  C    . THR   A 1 150 ? 11.905  -10.005 -35.317 1.00 45.91  ? 150 THR   A C    1 
ATOM   1161 O  O    . THR   A 1 150 ? 11.779  -10.443 -34.146 1.00 41.02  ? 150 THR   A O    1 
ATOM   1162 C  CB   . THR   A 1 150 ? 11.454  -7.577  -34.645 1.00 51.40  ? 150 THR   A CB   1 
ATOM   1163 O  OG1  . THR   A 1 150 ? 10.546  -6.500  -34.897 1.00 55.05  ? 150 THR   A OG1  1 
ATOM   1164 C  CG2  . THR   A 1 150 ? 12.876  -7.055  -34.694 1.00 49.01  ? 150 THR   A CG2  1 
ATOM   1165 N  N    . ASP   A 1 151 ? 12.585  -10.603 -36.312 1.00 42.27  ? 151 ASP   A N    1 
ATOM   1166 C  CA   . ASP   A 1 151 ? 13.308  -11.906 -36.237 1.00 43.63  ? 151 ASP   A CA   1 
ATOM   1167 C  C    . ASP   A 1 151 ? 12.335  -13.069 -35.996 1.00 38.27  ? 151 ASP   A C    1 
ATOM   1168 O  O    . ASP   A 1 151 ? 12.772  -14.067 -35.401 1.00 39.98  ? 151 ASP   A O    1 
ATOM   1169 C  CB   . ASP   A 1 151 ? 14.355  -11.911 -35.117 1.00 48.66  ? 151 ASP   A CB   1 
ATOM   1170 C  CG   . ASP   A 1 151 ? 15.202  -10.651 -35.047 1.00 54.96  ? 151 ASP   A CG   1 
ATOM   1171 O  OD1  . ASP   A 1 151 ? 15.910  -10.354 -36.043 1.00 56.64  ? 151 ASP   A OD1  1 
ATOM   1172 O  OD2  . ASP   A 1 151 ? 15.156  -9.978  -33.992 1.00 59.29  ? 151 ASP   A OD2  1 
ATOM   1173 N  N    . GLY   A 1 152 ? 11.065  -12.925 -36.395 1.00 34.84  ? 152 GLY   A N    1 
ATOM   1174 C  CA   . GLY   A 1 152 ? 9.956   -13.852 -36.074 1.00 31.11  ? 152 GLY   A CA   1 
ATOM   1175 C  C    . GLY   A 1 152 ? 9.605   -13.919 -34.579 1.00 29.04  ? 152 GLY   A C    1 
ATOM   1176 O  O    . GLY   A 1 152 ? 9.048   -14.962 -34.153 1.00 27.27  ? 152 GLY   A O    1 
ATOM   1177 N  N    . ASN   A 1 153 ? 9.879   -12.866 -33.795 1.00 25.23  ? 153 ASN   A N    1 
ATOM   1178 C  CA   . ASN   A 1 153 ? 9.662   -12.872 -32.325 1.00 24.01  ? 153 ASN   A CA   1 
ATOM   1179 C  C    . ASN   A 1 153 ? 8.503   -11.941 -31.955 1.00 24.54  ? 153 ASN   A C    1 
ATOM   1180 O  O    . ASN   A 1 153 ? 8.064   -11.130 -32.785 1.00 23.24  ? 153 ASN   A O    1 
ATOM   1181 C  CB   . ASN   A 1 153 ? 10.922  -12.495 -31.543 1.00 23.47  ? 153 ASN   A CB   1 
ATOM   1182 C  CG   . ASN   A 1 153 ? 12.074  -13.460 -31.757 1.00 23.42  ? 153 ASN   A CG   1 
ATOM   1183 O  OD1  . ASN   A 1 153 ? 11.877  -14.647 -31.980 1.00 22.93  ? 153 ASN   A OD1  1 
ATOM   1184 N  ND2  . ASN   A 1 153 ? 13.293  -12.959 -31.685 1.00 23.32  ? 153 ASN   A ND2  1 
ATOM   1185 N  N    . LEU   A 1 154 ? 8.005   -12.120 -30.738 1.00 24.18  ? 154 LEU   A N    1 
ATOM   1186 C  CA   . LEU   A 1 154 ? 7.005   -11.258 -30.066 1.00 24.01  ? 154 LEU   A CA   1 
ATOM   1187 C  C    . LEU   A 1 154 ? 7.776   -10.407 -29.046 1.00 23.97  ? 154 LEU   A C    1 
ATOM   1188 O  O    . LEU   A 1 154 ? 8.322   -10.985 -28.082 1.00 24.12  ? 154 LEU   A O    1 
ATOM   1189 C  CB   . LEU   A 1 154 ? 5.939   -12.177 -29.441 1.00 23.87  ? 154 LEU   A CB   1 
ATOM   1190 C  CG   . LEU   A 1 154 ? 5.065   -11.596 -28.328 1.00 24.84  ? 154 LEU   A CG   1 
ATOM   1191 C  CD1  . LEU   A 1 154 ? 4.257   -10.418 -28.831 1.00 26.42  ? 154 LEU   A CD1  1 
ATOM   1192 C  CD2  . LEU   A 1 154 ? 4.132   -12.655 -27.758 1.00 24.51  ? 154 LEU   A CD2  1 
ATOM   1193 N  N    . GLU   A 1 155 ? 7.880   -9.095  -29.280 1.00 23.00  ? 155 GLU   A N    1 
ATOM   1194 C  CA   . GLU   A 1 155 ? 8.585   -8.154  -28.367 1.00 22.78  ? 155 GLU   A CA   1 
ATOM   1195 C  C    . GLU   A 1 155 ? 7.544   -7.510  -27.458 1.00 21.27  ? 155 GLU   A C    1 
ATOM   1196 O  O    . GLU   A 1 155 ? 6.783   -6.660  -27.949 1.00 19.53  ? 155 GLU   A O    1 
ATOM   1197 C  CB   . GLU   A 1 155 ? 9.366   -7.091  -29.132 1.00 23.71  ? 155 GLU   A CB   1 
ATOM   1198 C  CG   . GLU   A 1 155 ? 10.550  -7.643  -29.894 1.00 27.77  ? 155 GLU   A CG   1 
ATOM   1199 C  CD   . GLU   A 1 155 ? 11.798  -7.956  -29.072 1.00 29.68  ? 155 GLU   A CD   1 
ATOM   1200 O  OE1  . GLU   A 1 155 ? 11.676  -8.224  -27.849 1.00 30.89  ? 155 GLU   A OE1  1 
ATOM   1201 O  OE2  . GLU   A 1 155 ? 12.900  -7.925  -29.668 1.00 30.55  ? 155 GLU   A OE2  1 
ATOM   1202 N  N    . LEU   A 1 156 ? 7.472   -7.941  -26.199 1.00 19.16  ? 156 LEU   A N    1 
ATOM   1203 C  CA   . LEU   A 1 156 ? 6.353   -7.508  -25.331 1.00 19.58  ? 156 LEU   A CA   1 
ATOM   1204 C  C    . LEU   A 1 156 ? 6.549   -6.034  -24.986 1.00 20.33  ? 156 LEU   A C    1 
ATOM   1205 O  O    . LEU   A 1 156 ? 5.527   -5.308  -24.931 1.00 20.03  ? 156 LEU   A O    1 
ATOM   1206 C  CB   . LEU   A 1 156 ? 6.242   -8.401  -24.091 1.00 18.72  ? 156 LEU   A CB   1 
ATOM   1207 C  CG   . LEU   A 1 156 ? 5.564   -9.750  -24.343 1.00 18.80  ? 156 LEU   A CG   1 
ATOM   1208 C  CD1  . LEU   A 1 156 ? 5.702   -10.676 -23.138 1.00 18.31  ? 156 LEU   A CD1  1 
ATOM   1209 C  CD2  . LEU   A 1 156 ? 4.097   -9.543  -24.710 1.00 18.41  ? 156 LEU   A CD2  1 
ATOM   1210 N  N    . THR   A 1 157 ? 7.795   -5.600  -24.776 1.00 20.16  ? 157 THR   A N    1 
ATOM   1211 C  CA   . THR   A 1 157 ? 8.108   -4.189  -24.414 1.00 20.76  ? 157 THR   A CA   1 
ATOM   1212 C  C    . THR   A 1 157 ? 8.975   -3.521  -25.492 1.00 21.33  ? 157 THR   A C    1 
ATOM   1213 O  O    . THR   A 1 157 ? 9.633   -4.224  -26.293 1.00 17.86  ? 157 THR   A O    1 
ATOM   1214 C  CB   . THR   A 1 157 ? 8.724   -4.066  -23.013 1.00 20.36  ? 157 THR   A CB   1 
ATOM   1215 O  OG1  . THR   A 1 157 ? 9.916   -4.848  -22.928 1.00 20.01  ? 157 THR   A OG1  1 
ATOM   1216 C  CG2  . THR   A 1 157 ? 7.733   -4.450  -21.936 1.00 21.52  ? 157 THR   A CG2  1 
ATOM   1217 N  N    . ARG   A 1 158 ? 8.982   -2.190  -25.476 1.00 25.56  ? 158 ARG   A N    1 
ATOM   1218 C  CA   . ARG   A 1 158 ? 9.635   -1.356  -26.513 1.00 32.21  ? 158 ARG   A CA   1 
ATOM   1219 C  C    . ARG   A 1 158 ? 11.150  -1.607  -26.499 1.00 29.89  ? 158 ARG   A C    1 
ATOM   1220 O  O    . ARG   A 1 158 ? 11.782  -1.464  -25.442 1.00 29.47  ? 158 ARG   A O    1 
ATOM   1221 C  CB   . ARG   A 1 158 ? 9.290   0.120   -26.312 1.00 39.00  ? 158 ARG   A CB   1 
ATOM   1222 C  CG   . ARG   A 1 158 ? 9.532   0.964   -27.557 1.00 49.21  ? 158 ARG   A CG   1 
ATOM   1223 C  CD   . ARG   A 1 158 ? 9.465   2.452   -27.243 1.00 63.51  ? 158 ARG   A CD   1 
ATOM   1224 N  NE   . ARG   A 1 158 ? 8.102   2.980   -27.312 1.00 73.46  ? 158 ARG   A NE   1 
ATOM   1225 C  CZ   . ARG   A 1 158 ? 7.651   3.856   -28.220 1.00 85.59  ? 158 ARG   A CZ   1 
ATOM   1226 N  NH1  . ARG   A 1 158 ? 8.447   4.337   -29.167 1.00 85.57  ? 158 ARG   A NH1  1 
ATOM   1227 N  NH2  . ARG   A 1 158 ? 6.391   4.260   -28.171 1.00 87.32  ? 158 ARG   A NH2  1 
ATOM   1228 N  N    . VAL   A 1 159 ? 11.678  -2.020  -27.651 1.00 31.05  ? 159 VAL   A N    1 
ATOM   1229 C  CA   . VAL   A 1 159 ? 13.128  -2.098  -27.982 1.00 32.78  ? 159 VAL   A CA   1 
ATOM   1230 C  C    . VAL   A 1 159 ? 13.388  -1.134  -29.155 1.00 36.17  ? 159 VAL   A C    1 
ATOM   1231 O  O    . VAL   A 1 159 ? 12.575  -1.090  -30.097 1.00 33.08  ? 159 VAL   A O    1 
ATOM   1232 C  CB   . VAL   A 1 159 ? 13.546  -3.542  -28.317 1.00 32.11  ? 159 VAL   A CB   1 
ATOM   1233 C  CG1  . VAL   A 1 159 ? 15.063  -3.697  -28.389 1.00 33.80  ? 159 VAL   A CG1  1 
ATOM   1234 C  CG2  . VAL   A 1 159 ? 12.958  -4.545  -27.336 1.00 30.09  ? 159 VAL   A CG2  1 
ATOM   1235 N  N    . SER   A 1 160 ? 14.469  -0.356  -29.081 1.00 37.97  ? 160 SER   A N    1 
ATOM   1236 C  CA   . SER   A 1 160 ? 14.953  0.526   -30.176 1.00 39.91  ? 160 SER   A CA   1 
ATOM   1237 C  C    . SER   A 1 160 ? 15.573  -0.336  -31.293 1.00 42.16  ? 160 SER   A C    1 
ATOM   1238 O  O    . SER   A 1 160 ? 15.843  -1.530  -31.049 1.00 40.07  ? 160 SER   A O    1 
ATOM   1239 C  CB   . SER   A 1 160 ? 15.935  1.535   -29.644 1.00 39.87  ? 160 SER   A CB   1 
ATOM   1240 O  OG   . SER   A 1 160 ? 17.235  0.958   -29.555 1.00 41.83  ? 160 SER   A OG   1 
ATOM   1241 N  N    . SER   A 1 161 ? 15.806  0.252   -32.471 1.00 48.00  ? 161 SER   A N    1 
ATOM   1242 C  CA   . SER   A 1 161 ? 16.291  -0.442  -33.698 1.00 50.80  ? 161 SER   A CA   1 
ATOM   1243 C  C    . SER   A 1 161 ? 17.742  -0.918  -33.533 1.00 47.99  ? 161 SER   A C    1 
ATOM   1244 O  O    . SER   A 1 161 ? 18.120  -1.860  -34.232 1.00 44.27  ? 161 SER   A O    1 
ATOM   1245 C  CB   . SER   A 1 161 ? 16.137  0.442   -34.912 1.00 54.25  ? 161 SER   A CB   1 
ATOM   1246 O  OG   . SER   A 1 161 ? 16.750  1.708   -34.691 1.00 60.25  ? 161 SER   A OG   1 
ATOM   1247 N  N    . ASN   A 1 162 ? 18.522  -0.311  -32.635 1.00 52.78  ? 162 ASN   A N    1 
ATOM   1248 C  CA   . ASN   A 1 162 ? 19.910  -0.758  -32.317 1.00 55.82  ? 162 ASN   A CA   1 
ATOM   1249 C  C    . ASN   A 1 162 ? 19.883  -1.994  -31.395 1.00 54.24  ? 162 ASN   A C    1 
ATOM   1250 O  O    . ASN   A 1 162 ? 20.957  -2.557  -31.175 1.00 56.84  ? 162 ASN   A O    1 
ATOM   1251 C  CB   . ASN   A 1 162 ? 20.758  0.375   -31.724 1.00 55.83  ? 162 ASN   A CB   1 
ATOM   1252 C  CG   . ASN   A 1 162 ? 20.361  0.738   -30.309 1.00 62.33  ? 162 ASN   A CG   1 
ATOM   1253 O  OD1  . ASN   A 1 162 ? 20.237  -0.136  -29.455 1.00 62.92  ? 162 ASN   A OD1  1 
ATOM   1254 N  ND2  . ASN   A 1 162 ? 20.159  2.021   -30.044 1.00 68.25  ? 162 ASN   A ND2  1 
ATOM   1255 N  N    . GLY   A 1 163 ? 18.721  -2.383  -30.853 1.00 51.98  ? 163 GLY   A N    1 
ATOM   1256 C  CA   . GLY   A 1 163 ? 18.557  -3.561  -29.976 1.00 48.03  ? 163 GLY   A CA   1 
ATOM   1257 C  C    . GLY   A 1 163 ? 18.355  -3.192  -28.506 1.00 46.10  ? 163 GLY   A C    1 
ATOM   1258 O  O    . GLY   A 1 163 ? 18.132  -4.116  -27.706 1.00 50.37  ? 163 GLY   A O    1 
ATOM   1259 N  N    . SER   A 1 164 ? 18.413  -1.905  -28.144 1.00 42.87  ? 164 SER   A N    1 
ATOM   1260 C  CA   . SER   A 1 164 ? 18.356  -1.406  -26.739 1.00 40.77  ? 164 SER   A CA   1 
ATOM   1261 C  C    . SER   A 1 164 ? 16.916  -1.385  -26.236 1.00 36.72  ? 164 SER   A C    1 
ATOM   1262 O  O    . SER   A 1 164 ? 16.044  -0.810  -26.895 1.00 34.05  ? 164 SER   A O    1 
ATOM   1263 C  CB   . SER   A 1 164 ? 18.980  -0.037  -26.585 1.00 42.45  ? 164 SER   A CB   1 
ATOM   1264 O  OG   . SER   A 1 164 ? 20.396  -0.132  -26.627 1.00 49.23  ? 164 SER   A OG   1 
ATOM   1265 N  N    . PRO   A 1 165 ? 16.647  -1.987  -25.048 1.00 30.55  ? 165 PRO   A N    1 
ATOM   1266 C  CA   . PRO   A 1 165 ? 15.318  -1.965  -24.434 1.00 29.43  ? 165 PRO   A CA   1 
ATOM   1267 C  C    . PRO   A 1 165 ? 15.059  -0.605  -23.774 1.00 27.90  ? 165 PRO   A C    1 
ATOM   1268 O  O    . PRO   A 1 165 ? 16.029  0.024   -23.411 1.00 28.13  ? 165 PRO   A O    1 
ATOM   1269 C  CB   . PRO   A 1 165 ? 15.389  -3.075  -23.370 1.00 29.00  ? 165 PRO   A CB   1 
ATOM   1270 C  CG   . PRO   A 1 165 ? 16.852  -3.095  -22.957 1.00 29.68  ? 165 PRO   A CG   1 
ATOM   1271 C  CD   . PRO   A 1 165 ? 17.618  -2.725  -24.218 1.00 30.81  ? 165 PRO   A CD   1 
ATOM   1272 N  N    . GLN   A 1 166 ? 13.792  -0.207  -23.615 1.00 26.48  ? 166 GLN   A N    1 
ATOM   1273 C  CA   . GLN   A 1 166 ? 13.404  1.137   -23.110 1.00 26.79  ? 166 GLN   A CA   1 
ATOM   1274 C  C    . GLN   A 1 166 ? 12.709  0.994   -21.754 1.00 24.73  ? 166 GLN   A C    1 
ATOM   1275 O  O    . GLN   A 1 166 ? 12.018  -0.046  -21.535 1.00 23.35  ? 166 GLN   A O    1 
ATOM   1276 C  CB   . GLN   A 1 166 ? 12.472  1.851   -24.097 1.00 30.70  ? 166 GLN   A CB   1 
ATOM   1277 C  CG   . GLN   A 1 166 ? 13.047  2.041   -25.500 1.00 34.38  ? 166 GLN   A CG   1 
ATOM   1278 C  CD   . GLN   A 1 166 ? 14.239  2.970   -25.559 1.00 38.61  ? 166 GLN   A CD   1 
ATOM   1279 O  OE1  . GLN   A 1 166 ? 15.248  2.679   -26.209 1.00 36.42  ? 166 GLN   A OE1  1 
ATOM   1280 N  NE2  . GLN   A 1 166 ? 14.132  4.099   -24.868 1.00 42.57  ? 166 GLN   A NE2  1 
ATOM   1281 N  N    . GLY   A 1 167 ? 12.870  2.011   -20.900 1.00 21.94  ? 167 GLY   A N    1 
ATOM   1282 C  CA   . GLY   A 1 167 ? 12.168  2.149   -19.612 1.00 21.05  ? 167 GLY   A CA   1 
ATOM   1283 C  C    . GLY   A 1 167 ? 10.692  2.472   -19.808 1.00 21.45  ? 167 GLY   A C    1 
ATOM   1284 O  O    . GLY   A 1 167 ? 10.287  2.808   -20.932 1.00 20.96  ? 167 GLY   A O    1 
ATOM   1285 N  N    . SER   A 1 168 ? 9.914   2.392   -18.733 1.00 21.54  ? 168 SER   A N    1 
ATOM   1286 C  CA   . SER   A 1 168 ? 8.499   2.835   -18.652 1.00 22.61  ? 168 SER   A CA   1 
ATOM   1287 C  C    . SER   A 1 168 ? 7.673   2.263   -19.805 1.00 20.92  ? 168 SER   A C    1 
ATOM   1288 O  O    . SER   A 1 168 ? 6.822   2.973   -20.368 1.00 21.85  ? 168 SER   A O    1 
ATOM   1289 C  CB   . SER   A 1 168 ? 8.448   4.325   -18.596 1.00 25.42  ? 168 SER   A CB   1 
ATOM   1290 O  OG   . SER   A 1 168 ? 8.980   4.751   -17.350 1.00 29.32  ? 168 SER   A OG   1 
ATOM   1291 N  N    . SER   A 1 169 ? 7.896   0.993   -20.103 1.00 20.16  ? 169 SER   A N    1 
ATOM   1292 C  CA   . SER   A 1 169 ? 7.269   0.248   -21.216 1.00 18.67  ? 169 SER   A CA   1 
ATOM   1293 C  C    . SER   A 1 169 ? 6.351   -0.821  -20.623 1.00 17.61  ? 169 SER   A C    1 
ATOM   1294 O  O    . SER   A 1 169 ? 6.705   -1.360  -19.572 1.00 17.72  ? 169 SER   A O    1 
ATOM   1295 C  CB   . SER   A 1 169 ? 8.335   -0.352  -22.097 1.00 19.30  ? 169 SER   A CB   1 
ATOM   1296 O  OG   . SER   A 1 169 ? 7.754   -0.823  -23.303 1.00 21.90  ? 169 SER   A OG   1 
ATOM   1297 N  N    . VAL   A 1 170 ? 5.208   -1.069  -21.255 1.00 17.70  ? 170 VAL   A N    1 
ATOM   1298 C  CA   . VAL   A 1 170 ? 4.295   -2.203  -20.957 1.00 19.07  ? 170 VAL   A CA   1 
ATOM   1299 C  C    . VAL   A 1 170 ? 3.690   -2.697  -22.276 1.00 19.29  ? 170 VAL   A C    1 
ATOM   1300 O  O    . VAL   A 1 170 ? 3.483   -1.879  -23.171 1.00 20.00  ? 170 VAL   A O    1 
ATOM   1301 C  CB   . VAL   A 1 170 ? 3.215   -1.808  -19.935 1.00 20.51  ? 170 VAL   A CB   1 
ATOM   1302 C  CG1  . VAL   A 1 170 ? 2.230   -0.778  -20.476 1.00 21.60  ? 170 VAL   A CG1  1 
ATOM   1303 C  CG2  . VAL   A 1 170 ? 2.462   -3.026  -19.455 1.00 21.58  ? 170 VAL   A CG2  1 
ATOM   1304 N  N    . GLY   A 1 171 ? 3.442   -4.006  -22.382 1.00 19.16  ? 171 GLY   A N    1 
ATOM   1305 C  CA   . GLY   A 1 171 ? 2.867   -4.661  -23.571 1.00 17.66  ? 171 GLY   A CA   1 
ATOM   1306 C  C    . GLY   A 1 171 ? 2.398   -6.086  -23.279 1.00 17.16  ? 171 GLY   A C    1 
ATOM   1307 O  O    . GLY   A 1 171 ? 3.023   -6.789  -22.457 1.00 16.16  ? 171 GLY   A O    1 
ATOM   1308 N  N    . ARG   A 1 172 ? 1.300   -6.483  -23.928 1.00 16.19  ? 172 ARG   A N    1 
ATOM   1309 C  CA   . ARG   A 1 172 ? 0.594   -7.759  -23.697 1.00 15.14  ? 172 ARG   A CA   1 
ATOM   1310 C  C    . ARG   A 1 172 ? 0.169   -8.317  -25.051 1.00 15.58  ? 172 ARG   A C    1 
ATOM   1311 O  O    . ARG   A 1 172 ? -0.012  -7.545  -26.025 1.00 15.82  ? 172 ARG   A O    1 
ATOM   1312 C  CB   . ARG   A 1 172 ? -0.599  -7.557  -22.768 1.00 14.68  ? 172 ARG   A CB   1 
ATOM   1313 C  CG   . ARG   A 1 172 ? -0.255  -6.846  -21.462 1.00 15.19  ? 172 ARG   A CG   1 
ATOM   1314 C  CD   . ARG   A 1 172 ? -1.265  -6.958  -20.317 1.00 14.55  ? 172 ARG   A CD   1 
ATOM   1315 N  NE   . ARG   A 1 172 ? -2.668  -6.876  -20.720 1.00 14.42  ? 172 ARG   A NE   1 
ATOM   1316 C  CZ   . ARG   A 1 172 ? -3.724  -6.917  -19.899 1.00 14.52  ? 172 ARG   A CZ   1 
ATOM   1317 N  NH1  . ARG   A 1 172 ? -3.569  -6.981  -18.581 1.00 14.26  ? 172 ARG   A NH1  1 
ATOM   1318 N  NH2  . ARG   A 1 172 ? -4.946  -6.902  -20.415 1.00 15.08  ? 172 ARG   A NH2  1 
ATOM   1319 N  N    . ALA   A 1 173 ? 0.042   -9.629  -25.120 1.00 15.95  ? 173 ALA   A N    1 
ATOM   1320 C  CA   . ALA   A 1 173 ? -0.496  -10.347 -26.298 1.00 15.87  ? 173 ALA   A CA   1 
ATOM   1321 C  C    . ALA   A 1 173 ? -1.474  -11.396 -25.773 1.00 15.75  ? 173 ALA   A C    1 
ATOM   1322 O  O    . ALA   A 1 173 ? -1.067  -12.208 -24.922 1.00 14.47  ? 173 ALA   A O    1 
ATOM   1323 C  CB   . ALA   A 1 173 ? 0.637   -10.931 -27.107 1.00 15.32  ? 173 ALA   A CB   1 
ATOM   1324 N  N    . LEU   A 1 174 ? -2.736  -11.289 -26.167 1.00 16.52  ? 174 LEU   A N    1 
ATOM   1325 C  CA   . LEU   A 1 174 ? -3.808  -12.244 -25.784 1.00 18.11  ? 174 LEU   A CA   1 
ATOM   1326 C  C    . LEU   A 1 174 ? -4.144  -13.112 -27.001 1.00 18.15  ? 174 LEU   A C    1 
ATOM   1327 O  O    . LEU   A 1 174 ? -4.182  -12.574 -28.119 1.00 16.55  ? 174 LEU   A O    1 
ATOM   1328 C  CB   . LEU   A 1 174 ? -5.038  -11.473 -25.294 1.00 19.16  ? 174 LEU   A CB   1 
ATOM   1329 C  CG   . LEU   A 1 174 ? -4.872  -10.681 -23.990 1.00 19.90  ? 174 LEU   A CG   1 
ATOM   1330 C  CD1  . LEU   A 1 174 ? -3.969  -9.462  -24.186 1.00 20.98  ? 174 LEU   A CD1  1 
ATOM   1331 C  CD2  . LEU   A 1 174 ? -6.222  -10.204 -23.479 1.00 20.34  ? 174 LEU   A CD2  1 
ATOM   1332 N  N    . PHE   A 1 175 ? -4.382  -14.410 -26.791 1.00 17.56  ? 175 PHE   A N    1 
ATOM   1333 C  CA   . PHE   A 1 175 ? -4.916  -15.289 -27.855 1.00 18.04  ? 175 PHE   A CA   1 
ATOM   1334 C  C    . PHE   A 1 175 ? -6.318  -14.771 -28.169 1.00 18.75  ? 175 PHE   A C    1 
ATOM   1335 O  O    . PHE   A 1 175 ? -7.075  -14.391 -27.202 1.00 18.89  ? 175 PHE   A O    1 
ATOM   1336 C  CB   . PHE   A 1 175 ? -4.864  -16.786 -27.500 1.00 17.82  ? 175 PHE   A CB   1 
ATOM   1337 C  CG   . PHE   A 1 175 ? -5.159  -17.662 -28.692 1.00 18.68  ? 175 PHE   A CG   1 
ATOM   1338 C  CD1  . PHE   A 1 175 ? -4.312  -17.669 -29.785 1.00 18.35  ? 175 PHE   A CD1  1 
ATOM   1339 C  CD2  . PHE   A 1 175 ? -6.340  -18.388 -28.776 1.00 20.61  ? 175 PHE   A CD2  1 
ATOM   1340 C  CE1  . PHE   A 1 175 ? -4.598  -18.435 -30.900 1.00 19.78  ? 175 PHE   A CE1  1 
ATOM   1341 C  CE2  . PHE   A 1 175 ? -6.642  -19.127 -29.911 1.00 19.75  ? 175 PHE   A CE2  1 
ATOM   1342 C  CZ   . PHE   A 1 175 ? -5.771  -19.154 -30.968 1.00 19.88  ? 175 PHE   A CZ   1 
ATOM   1343 N  N    . TYR   A 1 176 ? -6.664  -14.739 -29.458 1.00 19.07  ? 176 TYR   A N    1 
ATOM   1344 C  CA   . TYR   A 1 176 ? -7.939  -14.145 -29.941 1.00 22.04  ? 176 TYR   A CA   1 
ATOM   1345 C  C    . TYR   A 1 176 ? -9.146  -14.889 -29.351 1.00 21.17  ? 176 TYR   A C    1 
ATOM   1346 O  O    . TYR   A 1 176 ? -10.130 -14.228 -28.893 1.00 20.79  ? 176 TYR   A O    1 
ATOM   1347 C  CB   . TYR   A 1 176 ? -7.986  -14.134 -31.471 1.00 25.32  ? 176 TYR   A CB   1 
ATOM   1348 C  CG   . TYR   A 1 176 ? -8.880  -13.074 -32.060 1.00 27.40  ? 176 TYR   A CG   1 
ATOM   1349 C  CD1  . TYR   A 1 176 ? -10.236 -13.291 -32.237 1.00 32.25  ? 176 TYR   A CD1  1 
ATOM   1350 C  CD2  . TYR   A 1 176 ? -8.366  -11.862 -32.479 1.00 31.07  ? 176 TYR   A CD2  1 
ATOM   1351 C  CE1  . TYR   A 1 176 ? -11.060 -12.320 -32.791 1.00 32.44  ? 176 TYR   A CE1  1 
ATOM   1352 C  CE2  . TYR   A 1 176 ? -9.173  -10.884 -33.043 1.00 32.60  ? 176 TYR   A CE2  1 
ATOM   1353 C  CZ   . TYR   A 1 176 ? -10.524 -11.117 -33.202 1.00 31.98  ? 176 TYR   A CZ   1 
ATOM   1354 O  OH   . TYR   A 1 176 ? -11.330 -10.157 -33.742 1.00 40.10  ? 176 TYR   A OH   1 
ATOM   1355 N  N    . ALA   A 1 177 ? -9.140  -16.224 -29.397 1.00 19.37  ? 177 ALA   A N    1 
ATOM   1356 C  CA   . ALA   A 1 177 ? -10.320 -17.014 -28.970 1.00 19.16  ? 177 ALA   A CA   1 
ATOM   1357 C  C    . ALA   A 1 177 ? -10.398 -17.035 -27.448 1.00 18.60  ? 177 ALA   A C    1 
ATOM   1358 O  O    . ALA   A 1 177 ? -9.433  -17.358 -26.770 1.00 15.41  ? 177 ALA   A O    1 
ATOM   1359 C  CB   . ALA   A 1 177 ? -10.283 -18.412 -29.538 1.00 20.12  ? 177 ALA   A CB   1 
ATOM   1360 N  N    . PRO   A 1 178 ? -11.574 -16.731 -26.867 1.00 19.36  ? 178 PRO   A N    1 
ATOM   1361 C  CA   . PRO   A 1 178 ? -11.780 -16.933 -25.441 1.00 20.09  ? 178 PRO   A CA   1 
ATOM   1362 C  C    . PRO   A 1 178 ? -11.784 -18.437 -25.108 1.00 20.49  ? 178 PRO   A C    1 
ATOM   1363 O  O    . PRO   A 1 178 ? -12.017 -19.232 -25.986 1.00 17.87  ? 178 PRO   A O    1 
ATOM   1364 C  CB   . PRO   A 1 178 ? -13.131 -16.277 -25.195 1.00 22.00  ? 178 PRO   A CB   1 
ATOM   1365 C  CG   . PRO   A 1 178 ? -13.860 -16.396 -26.514 1.00 21.73  ? 178 PRO   A CG   1 
ATOM   1366 C  CD   . PRO   A 1 178 ? -12.780 -16.267 -27.562 1.00 21.14  ? 178 PRO   A CD   1 
ATOM   1367 N  N    . VAL   A 1 179 ? -11.460 -18.765 -23.858 1.00 18.81  ? 179 VAL   A N    1 
ATOM   1368 C  CA   . VAL   A 1 179 ? -11.179 -20.145 -23.386 1.00 18.91  ? 179 VAL   A CA   1 
ATOM   1369 C  C    . VAL   A 1 179 ? -12.196 -20.457 -22.304 1.00 17.82  ? 179 VAL   A C    1 
ATOM   1370 O  O    . VAL   A 1 179 ? -12.327 -19.612 -21.422 1.00 16.34  ? 179 VAL   A O    1 
ATOM   1371 C  CB   . VAL   A 1 179 ? -9.763  -20.270 -22.802 1.00 17.84  ? 179 VAL   A CB   1 
ATOM   1372 C  CG1  . VAL   A 1 179 ? -9.529  -21.667 -22.304 1.00 18.19  ? 179 VAL   A CG1  1 
ATOM   1373 C  CG2  . VAL   A 1 179 ? -8.705  -19.854 -23.799 1.00 18.91  ? 179 VAL   A CG2  1 
ATOM   1374 N  N    . HIS   A 1 180 ? -12.814 -21.635 -22.366 1.00 17.65  ? 180 HIS   A N    1 
ATOM   1375 C  CA   . HIS   A 1 180 ? -13.851 -22.084 -21.410 1.00 18.74  ? 180 HIS   A CA   1 
ATOM   1376 C  C    . HIS   A 1 180 ? -13.151 -22.821 -20.261 1.00 19.70  ? 180 HIS   A C    1 
ATOM   1377 O  O    . HIS   A 1 180 ? -12.629 -23.922 -20.490 1.00 20.57  ? 180 HIS   A O    1 
ATOM   1378 C  CB   . HIS   A 1 180 ? -14.933 -22.903 -22.136 1.00 18.94  ? 180 HIS   A CB   1 
ATOM   1379 C  CG   . HIS   A 1 180 ? -16.238 -22.990 -21.396 1.00 18.85  ? 180 HIS   A CG   1 
ATOM   1380 N  ND1  . HIS   A 1 180 ? -17.295 -23.763 -21.841 1.00 18.70  ? 180 HIS   A ND1  1 
ATOM   1381 C  CD2  . HIS   A 1 180 ? -16.665 -22.423 -20.244 1.00 19.16  ? 180 HIS   A CD2  1 
ATOM   1382 C  CE1  . HIS   A 1 180 ? -18.319 -23.646 -21.003 1.00 19.35  ? 180 HIS   A CE1  1 
ATOM   1383 N  NE2  . HIS   A 1 180 ? -17.964 -22.839 -20.016 1.00 19.53  ? 180 HIS   A NE2  1 
ATOM   1384 N  N    . ILE   A 1 181 ? -13.118 -22.216 -19.074 1.00 20.77  ? 181 ILE   A N    1 
ATOM   1385 C  CA   . ILE   A 1 181 ? -12.184 -22.623 -17.986 1.00 21.58  ? 181 ILE   A CA   1 
ATOM   1386 C  C    . ILE   A 1 181 ? -12.947 -23.378 -16.892 1.00 21.87  ? 181 ILE   A C    1 
ATOM   1387 O  O    . ILE   A 1 181 ? -12.283 -24.126 -16.158 1.00 24.04  ? 181 ILE   A O    1 
ATOM   1388 C  CB   . ILE   A 1 181 ? -11.390 -21.396 -17.490 1.00 23.45  ? 181 ILE   A CB   1 
ATOM   1389 C  CG1  . ILE   A 1 181 ? -9.944  -21.764 -17.171 1.00 26.23  ? 181 ILE   A CG1  1 
ATOM   1390 C  CG2  . ILE   A 1 181 ? -12.050 -20.695 -16.318 1.00 23.38  ? 181 ILE   A CG2  1 
ATOM   1391 C  CD1  . ILE   A 1 181 ? -9.145  -22.139 -18.380 1.00 28.30  ? 181 ILE   A CD1  1 
ATOM   1392 N  N    . TRP   A 1 182 ? -14.277 -23.245 -16.803 1.00 21.71  ? 182 TRP   A N    1 
ATOM   1393 C  CA   . TRP   A 1 182 ? -15.124 -24.105 -15.931 1.00 22.78  ? 182 TRP   A CA   1 
ATOM   1394 C  C    . TRP   A 1 182 ? -16.588 -24.052 -16.377 1.00 24.58  ? 182 TRP   A C    1 
ATOM   1395 O  O    . TRP   A 1 182 ? -16.995 -23.069 -17.038 1.00 22.54  ? 182 TRP   A O    1 
ATOM   1396 C  CB   . TRP   A 1 182 ? -14.984 -23.730 -14.442 1.00 24.23  ? 182 TRP   A CB   1 
ATOM   1397 C  CG   . TRP   A 1 182 ? -15.271 -22.298 -14.082 1.00 26.67  ? 182 TRP   A CG   1 
ATOM   1398 C  CD1  . TRP   A 1 182 ? -14.348 -21.290 -13.974 1.00 28.28  ? 182 TRP   A CD1  1 
ATOM   1399 C  CD2  . TRP   A 1 182 ? -16.546 -21.691 -13.784 1.00 26.34  ? 182 TRP   A CD2  1 
ATOM   1400 N  NE1  . TRP   A 1 182 ? -14.948 -20.115 -13.618 1.00 26.99  ? 182 TRP   A NE1  1 
ATOM   1401 C  CE2  . TRP   A 1 182 ? -16.301 -20.324 -13.508 1.00 26.62  ? 182 TRP   A CE2  1 
ATOM   1402 C  CE3  . TRP   A 1 182 ? -17.869 -22.153 -13.723 1.00 28.49  ? 182 TRP   A CE3  1 
ATOM   1403 C  CZ2  . TRP   A 1 182 ? -17.324 -19.434 -13.164 1.00 26.57  ? 182 TRP   A CZ2  1 
ATOM   1404 C  CZ3  . TRP   A 1 182 ? -18.886 -21.271 -13.389 1.00 27.74  ? 182 TRP   A CZ3  1 
ATOM   1405 C  CH2  . TRP   A 1 182 ? -18.613 -19.927 -13.114 1.00 26.61  ? 182 TRP   A CH2  1 
ATOM   1406 N  N    . GLU   A 1 183 ? -17.353 -25.089 -16.040 1.00 25.42  ? 183 GLU   A N    1 
ATOM   1407 C  CA   . GLU   A 1 183 ? -18.821 -25.102 -16.244 1.00 29.73  ? 183 GLU   A CA   1 
ATOM   1408 C  C    . GLU   A 1 183 ? -19.511 -25.154 -14.879 1.00 29.14  ? 183 GLU   A C    1 
ATOM   1409 O  O    . GLU   A 1 183 ? -20.627 -24.620 -14.757 1.00 31.13  ? 183 GLU   A O    1 
ATOM   1410 C  CB   . GLU   A 1 183 ? -19.236 -26.250 -17.165 1.00 37.49  ? 183 GLU   A CB   1 
ATOM   1411 C  CG   . GLU   A 1 183 ? -20.544 -25.953 -17.883 1.00 45.54  ? 183 GLU   A CG   1 
ATOM   1412 C  CD   . GLU   A 1 183 ? -20.829 -26.692 -19.187 1.00 53.53  ? 183 GLU   A CD   1 
ATOM   1413 O  OE1  . GLU   A 1 183 ? -20.795 -27.956 -19.185 1.00 55.89  ? 183 GLU   A OE1  1 
ATOM   1414 O  OE2  . GLU   A 1 183 ? -21.139 -25.994 -20.201 1.00 58.63  ? 183 GLU   A OE2  1 
ATOM   1415 N  N    . SER   A 1 184 ? -18.855 -25.734 -13.876 1.00 24.45  ? 184 SER   A N    1 
ATOM   1416 C  CA   . SER   A 1 184 ? -19.325 -25.749 -12.476 1.00 22.66  ? 184 SER   A CA   1 
ATOM   1417 C  C    . SER   A 1 184 ? -18.112 -25.912 -11.572 1.00 22.16  ? 184 SER   A C    1 
ATOM   1418 O  O    . SER   A 1 184 ? -17.001 -26.117 -12.111 1.00 19.47  ? 184 SER   A O    1 
ATOM   1419 C  CB   . SER   A 1 184 ? -20.292 -26.869 -12.258 1.00 21.71  ? 184 SER   A CB   1 
ATOM   1420 O  OG   . SER   A 1 184 ? -19.591 -28.093 -12.279 1.00 22.41  ? 184 SER   A OG   1 
ATOM   1421 N  N    . SER   A 1 185 ? -18.343 -25.929 -10.263 1.00 20.98  ? 185 SER   A N    1 
ATOM   1422 C  CA   . SER   A 1 185 ? -17.272 -26.120 -9.266  1.00 22.32  ? 185 SER   A CA   1 
ATOM   1423 C  C    . SER   A 1 185 ? -16.744 -27.549 -9.381  1.00 22.11  ? 185 SER   A C    1 
ATOM   1424 O  O    . SER   A 1 185 ? -15.583 -27.754 -9.026  1.00 21.66  ? 185 SER   A O    1 
ATOM   1425 C  CB   . SER   A 1 185 ? -17.752 -25.775 -7.890  1.00 24.38  ? 185 SER   A CB   1 
ATOM   1426 O  OG   . SER   A 1 185 ? -18.962 -26.447 -7.598  1.00 30.60  ? 185 SER   A OG   1 
ATOM   1427 N  N    . ALA   A 1 186 ? -17.541 -28.466 -9.954  1.00 20.52  ? 186 ALA   A N    1 
ATOM   1428 C  CA   . ALA   A 1 186 ? -17.223 -29.905 -10.120 1.00 19.45  ? 186 ALA   A CA   1 
ATOM   1429 C  C    . ALA   A 1 186 ? -16.581 -30.185 -11.486 1.00 20.38  ? 186 ALA   A C    1 
ATOM   1430 O  O    . ALA   A 1 186 ? -16.002 -31.268 -11.625 1.00 20.04  ? 186 ALA   A O    1 
ATOM   1431 C  CB   . ALA   A 1 186 ? -18.484 -30.719 -9.966  1.00 18.95  ? 186 ALA   A CB   1 
ATOM   1432 N  N    . VAL   A 1 187 ? -16.728 -29.282 -12.475 1.00 19.62  ? 187 VAL   A N    1 
ATOM   1433 C  CA   . VAL   A 1 187 ? -16.191 -29.487 -13.855 1.00 19.15  ? 187 VAL   A CA   1 
ATOM   1434 C  C    . VAL   A 1 187 ? -15.325 -28.280 -14.256 1.00 19.29  ? 187 VAL   A C    1 
ATOM   1435 O  O    . VAL   A 1 187 ? -15.866 -27.256 -14.726 1.00 16.66  ? 187 VAL   A O    1 
ATOM   1436 C  CB   . VAL   A 1 187 ? -17.311 -29.778 -14.872 1.00 19.26  ? 187 VAL   A CB   1 
ATOM   1437 C  CG1  . VAL   A 1 187 ? -16.758 -29.871 -16.281 1.00 20.24  ? 187 VAL   A CG1  1 
ATOM   1438 C  CG2  . VAL   A 1 187 ? -18.057 -31.056 -14.529 1.00 19.20  ? 187 VAL   A CG2  1 
ATOM   1439 N  N    . VAL   A 1 188 ? -14.006 -28.425 -14.083 1.00 18.73  ? 188 VAL   A N    1 
ATOM   1440 C  CA   . VAL   A 1 188 ? -13.011 -27.338 -14.254 1.00 17.90  ? 188 VAL   A CA   1 
ATOM   1441 C  C    . VAL   A 1 188 ? -11.992 -27.810 -15.290 1.00 16.35  ? 188 VAL   A C    1 
ATOM   1442 O  O    . VAL   A 1 188 ? -11.677 -29.018 -15.329 1.00 16.35  ? 188 VAL   A O    1 
ATOM   1443 C  CB   . VAL   A 1 188 ? -12.371 -26.946 -12.904 1.00 18.49  ? 188 VAL   A CB   1 
ATOM   1444 C  CG1  . VAL   A 1 188 ? -11.513 -25.694 -13.036 1.00 20.10  ? 188 VAL   A CG1  1 
ATOM   1445 C  CG2  . VAL   A 1 188 ? -13.432 -26.715 -11.847 1.00 18.74  ? 188 VAL   A CG2  1 
ATOM   1446 N  N    . ALA   A 1 189 ? -11.512 -26.892 -16.120 1.00 15.34  ? 189 ALA   A N    1 
ATOM   1447 C  CA   . ALA   A 1 189 ? -10.548 -27.209 -17.185 1.00 15.45  ? 189 ALA   A CA   1 
ATOM   1448 C  C    . ALA   A 1 189 ? -9.164  -27.459 -16.560 1.00 14.54  ? 189 ALA   A C    1 
ATOM   1449 O  O    . ALA   A 1 189 ? -8.847  -26.904 -15.526 1.00 14.99  ? 189 ALA   A O    1 
ATOM   1450 C  CB   . ALA   A 1 189 ? -10.505 -26.108 -18.195 1.00 15.57  ? 189 ALA   A CB   1 
ATOM   1451 N  N    . SER   A 1 190 ? -8.404  -28.340 -17.166 1.00 14.49  ? 190 SER   A N    1 
ATOM   1452 C  CA   . SER   A 1 190 ? -6.943  -28.437 -17.004 1.00 14.12  ? 190 SER   A CA   1 
ATOM   1453 C  C    . SER   A 1 190 ? -6.338  -27.702 -18.196 1.00 15.25  ? 190 SER   A C    1 
ATOM   1454 O  O    . SER   A 1 190 ? -6.997  -27.632 -19.296 1.00 13.98  ? 190 SER   A O    1 
ATOM   1455 C  CB   . SER   A 1 190 ? -6.520  -29.886 -16.917 1.00 14.42  ? 190 SER   A CB   1 
ATOM   1456 O  OG   . SER   A 1 190 ? -6.927  -30.468 -15.680 1.00 13.79  ? 190 SER   A OG   1 
ATOM   1457 N  N    . PHE   A 1 191 ? -5.164  -27.110 -18.013 1.00 15.29  ? 191 PHE   A N    1 
ATOM   1458 C  CA   . PHE   A 1 191 ? -4.486  -26.443 -19.143 1.00 15.09  ? 191 PHE   A CA   1 
ATOM   1459 C  C    . PHE   A 1 191 ? -2.979  -26.572 -18.953 1.00 14.26  ? 191 PHE   A C    1 
ATOM   1460 O  O    . PHE   A 1 191 ? -2.524  -26.905 -17.877 1.00 15.80  ? 191 PHE   A O    1 
ATOM   1461 C  CB   . PHE   A 1 191 ? -5.056  -25.030 -19.333 1.00 15.48  ? 191 PHE   A CB   1 
ATOM   1462 C  CG   . PHE   A 1 191 ? -4.791  -24.062 -18.223 1.00 15.14  ? 191 PHE   A CG   1 
ATOM   1463 C  CD1  . PHE   A 1 191 ? -3.513  -23.575 -18.002 1.00 16.76  ? 191 PHE   A CD1  1 
ATOM   1464 C  CD2  . PHE   A 1 191 ? -5.815  -23.625 -17.408 1.00 15.81  ? 191 PHE   A CD2  1 
ATOM   1465 C  CE1  . PHE   A 1 191 ? -3.268  -22.685 -16.965 1.00 16.75  ? 191 PHE   A CE1  1 
ATOM   1466 C  CE2  . PHE   A 1 191 ? -5.572  -22.723 -16.384 1.00 16.05  ? 191 PHE   A CE2  1 
ATOM   1467 C  CZ   . PHE   A 1 191 ? -4.298  -22.267 -16.157 1.00 16.41  ? 191 PHE   A CZ   1 
ATOM   1468 N  N    . GLU   A 1 192 ? -2.259  -26.373 -20.039 1.00 15.33  ? 192 GLU   A N    1 
ATOM   1469 C  CA   . GLU   A 1 192 ? -0.788  -26.425 -20.143 1.00 16.13  ? 192 GLU   A CA   1 
ATOM   1470 C  C    . GLU   A 1 192 ? -0.375  -25.236 -21.013 1.00 15.90  ? 192 GLU   A C    1 
ATOM   1471 O  O    . GLU   A 1 192 ? -0.989  -25.030 -22.078 1.00 14.09  ? 192 GLU   A O    1 
ATOM   1472 C  CB   . GLU   A 1 192 ? -0.366  -27.770 -20.738 1.00 17.67  ? 192 GLU   A CB   1 
ATOM   1473 C  CG   . GLU   A 1 192 ? 1.123   -28.066 -20.614 1.00 19.88  ? 192 GLU   A CG   1 
ATOM   1474 C  CD   . GLU   A 1 192 ? 1.541   -29.462 -21.076 1.00 21.93  ? 192 GLU   A CD   1 
ATOM   1475 O  OE1  . GLU   A 1 192 ? 0.726   -30.136 -21.747 1.00 21.08  ? 192 GLU   A OE1  1 
ATOM   1476 O  OE2  . GLU   A 1 192 ? 2.700   -29.873 -20.774 1.00 25.14  ? 192 GLU   A OE2  1 
ATOM   1477 N  N    . ALA   A 1 193 ? 0.615   -24.472 -20.558 1.00 16.07  ? 193 ALA   A N    1 
ATOM   1478 C  CA   . ALA   A 1 193 ? 1.323   -23.455 -21.358 1.00 16.46  ? 193 ALA   A CA   1 
ATOM   1479 C  C    . ALA   A 1 193 ? 2.842   -23.689 -21.297 1.00 16.43  ? 193 ALA   A C    1 
ATOM   1480 O  O    . ALA   A 1 193 ? 3.390   -23.990 -20.238 1.00 16.76  ? 193 ALA   A O    1 
ATOM   1481 C  CB   . ALA   A 1 193 ? 0.935   -22.067 -20.904 1.00 16.26  ? 193 ALA   A CB   1 
ATOM   1482 N  N    . THR   A 1 194 ? 3.493   -23.489 -22.429 1.00 16.88  ? 194 THR   A N    1 
ATOM   1483 C  CA   . THR   A 1 194 ? 4.962   -23.394 -22.575 1.00 18.54  ? 194 THR   A CA   1 
ATOM   1484 C  C    . THR   A 1 194 ? 5.271   -22.086 -23.318 1.00 17.23  ? 194 THR   A C    1 
ATOM   1485 O  O    . THR   A 1 194 ? 4.479   -21.692 -24.227 1.00 15.20  ? 194 THR   A O    1 
ATOM   1486 C  CB   . THR   A 1 194 ? 5.502   -24.651 -23.270 1.00 20.33  ? 194 THR   A CB   1 
ATOM   1487 O  OG1  . THR   A 1 194 ? 5.106   -25.754 -22.456 1.00 23.09  ? 194 THR   A OG1  1 
ATOM   1488 C  CG2  . THR   A 1 194 ? 7.010   -24.684 -23.375 1.00 22.83  ? 194 THR   A CG2  1 
ATOM   1489 N  N    . PHE   A 1 195 ? 6.349   -21.415 -22.927 1.00 15.05  ? 195 PHE   A N    1 
ATOM   1490 C  CA   . PHE   A 1 195 ? 6.930   -20.329 -23.735 1.00 15.19  ? 195 PHE   A CA   1 
ATOM   1491 C  C    . PHE   A 1 195 ? 8.429   -20.321 -23.514 1.00 15.48  ? 195 PHE   A C    1 
ATOM   1492 O  O    . PHE   A 1 195 ? 8.901   -20.767 -22.460 1.00 13.73  ? 195 PHE   A O    1 
ATOM   1493 C  CB   . PHE   A 1 195 ? 6.251   -18.979 -23.476 1.00 15.98  ? 195 PHE   A CB   1 
ATOM   1494 C  CG   . PHE   A 1 195 ? 6.369   -18.386 -22.094 1.00 16.16  ? 195 PHE   A CG   1 
ATOM   1495 C  CD1  . PHE   A 1 195 ? 5.408   -18.648 -21.123 1.00 15.59  ? 195 PHE   A CD1  1 
ATOM   1496 C  CD2  . PHE   A 1 195 ? 7.414   -17.526 -21.781 1.00 15.92  ? 195 PHE   A CD2  1 
ATOM   1497 C  CE1  . PHE   A 1 195 ? 5.494   -18.076 -19.870 1.00 15.65  ? 195 PHE   A CE1  1 
ATOM   1498 C  CE2  . PHE   A 1 195 ? 7.480   -16.940 -20.529 1.00 16.37  ? 195 PHE   A CE2  1 
ATOM   1499 C  CZ   . PHE   A 1 195 ? 6.518   -17.216 -19.575 1.00 16.33  ? 195 PHE   A CZ   1 
ATOM   1500 N  N    . THR   A 1 196 ? 9.145   -19.869 -24.545 1.00 17.00  ? 196 THR   A N    1 
ATOM   1501 C  CA   . THR   A 1 196 ? 10.594  -19.603 -24.496 1.00 17.59  ? 196 THR   A CA   1 
ATOM   1502 C  C    . THR   A 1 196 ? 10.770  -18.090 -24.563 1.00 18.81  ? 196 THR   A C    1 
ATOM   1503 O  O    . THR   A 1 196 ? 9.968   -17.426 -25.240 1.00 19.85  ? 196 THR   A O    1 
ATOM   1504 C  CB   . THR   A 1 196 ? 11.308  -20.354 -25.615 1.00 17.13  ? 196 THR   A CB   1 
ATOM   1505 O  OG1  . THR   A 1 196 ? 10.852  -19.746 -26.826 1.00 18.86  ? 196 THR   A OG1  1 
ATOM   1506 C  CG2  . THR   A 1 196 ? 11.041  -21.838 -25.579 1.00 16.63  ? 196 THR   A CG2  1 
ATOM   1507 N  N    . PHE   A 1 197 ? 11.786  -17.568 -23.885 1.00 19.05  ? 197 PHE   A N    1 
ATOM   1508 C  CA   . PHE   A 1 197 ? 11.938  -16.115 -23.645 1.00 19.44  ? 197 PHE   A CA   1 
ATOM   1509 C  C    . PHE   A 1 197 ? 13.428  -15.748 -23.631 1.00 20.03  ? 197 PHE   A C    1 
ATOM   1510 O  O    . PHE   A 1 197 ? 14.279  -16.584 -23.313 1.00 22.16  ? 197 PHE   A O    1 
ATOM   1511 C  CB   . PHE   A 1 197 ? 11.218  -15.746 -22.341 1.00 19.20  ? 197 PHE   A CB   1 
ATOM   1512 C  CG   . PHE   A 1 197 ? 11.754  -16.434 -21.111 1.00 18.60  ? 197 PHE   A CG   1 
ATOM   1513 C  CD1  . PHE   A 1 197 ? 12.788  -15.870 -20.375 1.00 19.74  ? 197 PHE   A CD1  1 
ATOM   1514 C  CD2  . PHE   A 1 197 ? 11.241  -17.655 -20.705 1.00 19.31  ? 197 PHE   A CD2  1 
ATOM   1515 C  CE1  . PHE   A 1 197 ? 13.293  -16.504 -19.250 1.00 19.68  ? 197 PHE   A CE1  1 
ATOM   1516 C  CE2  . PHE   A 1 197 ? 11.735  -18.287 -19.576 1.00 19.45  ? 197 PHE   A CE2  1 
ATOM   1517 C  CZ   . PHE   A 1 197 ? 12.764  -17.716 -18.856 1.00 20.11  ? 197 PHE   A CZ   1 
ATOM   1518 N  N    . LEU   A 1 198 ? 13.730  -14.507 -23.981 1.00 20.84  ? 198 LEU   A N    1 
ATOM   1519 C  CA   . LEU   A 1 198 ? 15.100  -13.959 -23.920 1.00 22.21  ? 198 LEU   A CA   1 
ATOM   1520 C  C    . LEU   A 1 198 ? 15.014  -12.600 -23.208 1.00 20.93  ? 198 LEU   A C    1 
ATOM   1521 O  O    . LEU   A 1 198 ? 14.450  -11.656 -23.766 1.00 19.36  ? 198 LEU   A O    1 
ATOM   1522 C  CB   . LEU   A 1 198 ? 15.662  -13.865 -25.340 1.00 22.65  ? 198 LEU   A CB   1 
ATOM   1523 C  CG   . LEU   A 1 198 ? 17.192  -13.903 -25.446 1.00 24.62  ? 198 LEU   A CG   1 
ATOM   1524 C  CD1  . LEU   A 1 198 ? 17.641  -13.617 -26.885 1.00 24.83  ? 198 LEU   A CD1  1 
ATOM   1525 C  CD2  . LEU   A 1 198 ? 17.850  -12.934 -24.482 1.00 24.20  ? 198 LEU   A CD2  1 
ATOM   1526 N  N    . ILE   A 1 199 ? 15.505  -12.556 -21.981 1.00 20.36  ? 199 ILE   A N    1 
ATOM   1527 C  CA   . ILE   A 1 199 ? 15.590  -11.334 -21.140 1.00 22.50  ? 199 ILE   A CA   1 
ATOM   1528 C  C    . ILE   A 1 199 ? 17.044  -10.874 -21.135 1.00 25.51  ? 199 ILE   A C    1 
ATOM   1529 O  O    . ILE   A 1 199 ? 17.854  -11.525 -20.459 1.00 23.25  ? 199 ILE   A O    1 
ATOM   1530 C  CB   . ILE   A 1 199 ? 15.059  -11.601 -19.720 1.00 21.82  ? 199 ILE   A CB   1 
ATOM   1531 C  CG1  . ILE   A 1 199 ? 13.557  -11.878 -19.766 1.00 22.03  ? 199 ILE   A CG1  1 
ATOM   1532 C  CG2  . ILE   A 1 199 ? 15.390  -10.430 -18.815 1.00 22.12  ? 199 ILE   A CG2  1 
ATOM   1533 C  CD1  . ILE   A 1 199 ? 13.021  -12.586 -18.565 1.00 22.85  ? 199 ILE   A CD1  1 
ATOM   1534 N  N    . LYS   A 1 200 ? 17.328  -9.802  -21.881 1.00 29.50  ? 200 LYS   A N    1 
ATOM   1535 C  CA   . LYS   A 1 200 ? 18.675  -9.211  -22.036 1.00 34.71  ? 200 LYS   A CA   1 
ATOM   1536 C  C    . LYS   A 1 200 ? 18.611  -7.786  -21.484 1.00 33.80  ? 200 LYS   A C    1 
ATOM   1537 O  O    . LYS   A 1 200 ? 17.692  -7.046  -21.845 1.00 29.58  ? 200 LYS   A O    1 
ATOM   1538 C  CB   . LYS   A 1 200 ? 19.128  -9.256  -23.502 1.00 40.35  ? 200 LYS   A CB   1 
ATOM   1539 C  CG   . LYS   A 1 200 ? 20.637  -9.205  -23.699 1.00 46.11  ? 200 LYS   A CG   1 
ATOM   1540 C  CD   . LYS   A 1 200 ? 21.102  -8.267  -24.805 1.00 54.33  ? 200 LYS   A CD   1 
ATOM   1541 C  CE   . LYS   A 1 200 ? 22.555  -7.847  -24.641 1.00 58.46  ? 200 LYS   A CE   1 
ATOM   1542 N  NZ   . LYS   A 1 200 ? 23.481  -8.997  -24.806 1.00 59.02  ? 200 LYS   A NZ   1 
ATOM   1543 N  N    . SER   A 1 201 ? 19.557  -7.422  -20.622 1.00 36.43  ? 201 SER   A N    1 
ATOM   1544 C  CA   . SER   A 1 201 ? 19.676  -6.049  -20.082 1.00 39.64  ? 201 SER   A CA   1 
ATOM   1545 C  C    . SER   A 1 201 ? 21.126  -5.576  -20.134 1.00 41.50  ? 201 SER   A C    1 
ATOM   1546 O  O    . SER   A 1 201 ? 22.010  -6.310  -19.699 1.00 37.07  ? 201 SER   A O    1 
ATOM   1547 C  CB   . SER   A 1 201 ? 19.130  -5.999  -18.688 1.00 39.77  ? 201 SER   A CB   1 
ATOM   1548 O  OG   . SER   A 1 201 ? 19.169  -4.671  -18.187 1.00 43.05  ? 201 SER   A OG   1 
ATOM   1549 N  N    . PRO   A 1 202 ? 21.401  -4.338  -20.626 1.00 49.10  ? 202 PRO   A N    1 
ATOM   1550 C  CA   . PRO   A 1 202 ? 22.687  -3.662  -20.390 1.00 51.11  ? 202 PRO   A CA   1 
ATOM   1551 C  C    . PRO   A 1 202 ? 22.934  -3.297  -18.913 1.00 52.53  ? 202 PRO   A C    1 
ATOM   1552 O  O    . PRO   A 1 202 ? 24.071  -3.285  -18.507 1.00 51.74  ? 202 PRO   A O    1 
ATOM   1553 C  CB   . PRO   A 1 202 ? 22.576  -2.363  -21.209 1.00 49.86  ? 202 PRO   A CB   1 
ATOM   1554 C  CG   . PRO   A 1 202 ? 21.084  -2.108  -21.278 1.00 50.59  ? 202 PRO   A CG   1 
ATOM   1555 C  CD   . PRO   A 1 202 ? 20.478  -3.496  -21.410 1.00 49.93  ? 202 PRO   A CD   1 
ATOM   1556 N  N    . ASP   A 1 203 ? 21.861  -3.019  -18.159 1.00 58.81  ? 203 ASP   A N    1 
ATOM   1557 C  CA   . ASP   A 1 203 ? 21.889  -2.643  -16.715 1.00 61.02  ? 203 ASP   A CA   1 
ATOM   1558 C  C    . ASP   A 1 203 ? 22.413  -3.798  -15.848 1.00 62.15  ? 203 ASP   A C    1 
ATOM   1559 O  O    . ASP   A 1 203 ? 22.132  -4.977  -16.151 1.00 55.87  ? 203 ASP   A O    1 
ATOM   1560 C  CB   . ASP   A 1 203 ? 20.496  -2.312  -16.161 1.00 63.00  ? 203 ASP   A CB   1 
ATOM   1561 C  CG   . ASP   A 1 203 ? 19.761  -1.126  -16.775 1.00 60.87  ? 203 ASP   A CG   1 
ATOM   1562 O  OD1  . ASP   A 1 203 ? 20.453  -0.222  -17.341 1.00 57.94  ? 203 ASP   A OD1  1 
ATOM   1563 O  OD2  . ASP   A 1 203 ? 18.487  -1.106  -16.653 1.00 44.05  ? 203 ASP   A OD2  1 
ATOM   1564 N  N    . SER   A 1 204 ? 23.101  -3.453  -14.759 1.00 66.95  ? 204 SER   A N    1 
ATOM   1565 C  CA   . SER   A 1 204 ? 23.427  -4.363  -13.626 1.00 68.19  ? 204 SER   A CA   1 
ATOM   1566 C  C    . SER   A 1 204 ? 22.126  -4.971  -13.078 1.00 63.54  ? 204 SER   A C    1 
ATOM   1567 O  O    . SER   A 1 204 ? 22.171  -6.134  -12.579 1.00 57.83  ? 204 SER   A O    1 
ATOM   1568 C  CB   . SER   A 1 204 ? 24.203  -3.638  -12.530 1.00 66.61  ? 204 SER   A CB   1 
ATOM   1569 O  OG   . SER   A 1 204 ? 23.339  -2.852  -11.709 1.00 57.97  ? 204 SER   A OG   1 
ATOM   1570 N  N    . HIS   A 1 205 ? 21.027  -4.199  -13.133 1.00 55.07  ? 205 HIS   A N    1 
ATOM   1571 C  CA   . HIS   A 1 205 ? 19.689  -4.575  -12.603 1.00 52.85  ? 205 HIS   A CA   1 
ATOM   1572 C  C    . HIS   A 1 205 ? 18.660  -4.523  -13.736 1.00 41.28  ? 205 HIS   A C    1 
ATOM   1573 O  O    . HIS   A 1 205 ? 18.159  -3.458  -14.095 1.00 38.48  ? 205 HIS   A O    1 
ATOM   1574 C  CB   . HIS   A 1 205 ? 19.313  -3.696  -11.394 1.00 63.23  ? 205 HIS   A CB   1 
ATOM   1575 C  CG   . HIS   A 1 205 ? 20.253  -3.760  -10.227 1.00 72.93  ? 205 HIS   A CG   1 
ATOM   1576 N  ND1  . HIS   A 1 205 ? 20.560  -2.638  -9.454  1.00 80.28  ? 205 HIS   A ND1  1 
ATOM   1577 C  CD2  . HIS   A 1 205 ? 20.949  -4.787  -9.683  1.00 77.84  ? 205 HIS   A CD2  1 
ATOM   1578 C  CE1  . HIS   A 1 205 ? 21.401  -2.977  -8.495  1.00 77.51  ? 205 HIS   A CE1  1 
ATOM   1579 N  NE2  . HIS   A 1 205 ? 21.659  -4.291  -8.615  1.00 78.07  ? 205 HIS   A NE2  1 
ATOM   1580 N  N    . PRO   A 1 206 ? 18.334  -5.671  -14.371 1.00 31.22  ? 206 PRO   A N    1 
ATOM   1581 C  CA   . PRO   A 1 206 ? 17.152  -5.755  -15.232 1.00 25.94  ? 206 PRO   A CA   1 
ATOM   1582 C  C    . PRO   A 1 206 ? 15.825  -5.594  -14.469 1.00 21.02  ? 206 PRO   A C    1 
ATOM   1583 O  O    . PRO   A 1 206 ? 15.771  -5.827  -13.288 1.00 18.34  ? 206 PRO   A O    1 
ATOM   1584 C  CB   . PRO   A 1 206 ? 17.239  -7.152  -15.852 1.00 26.60  ? 206 PRO   A CB   1 
ATOM   1585 C  CG   . PRO   A 1 206 ? 18.139  -7.923  -14.917 1.00 28.43  ? 206 PRO   A CG   1 
ATOM   1586 C  CD   . PRO   A 1 206 ? 19.101  -6.921  -14.332 1.00 28.33  ? 206 PRO   A CD   1 
ATOM   1587 N  N    . ALA   A 1 207 ? 14.769  -5.221  -15.189 1.00 18.67  ? 207 ALA   A N    1 
ATOM   1588 C  CA   . ALA   A 1 207 ? 13.402  -5.065  -14.652 1.00 16.58  ? 207 ALA   A CA   1 
ATOM   1589 C  C    . ALA   A 1 207 ? 12.466  -4.976  -15.846 1.00 16.98  ? 207 ALA   A C    1 
ATOM   1590 O  O    . ALA   A 1 207 ? 12.947  -4.670  -16.939 1.00 15.00  ? 207 ALA   A O    1 
ATOM   1591 C  CB   . ALA   A 1 207 ? 13.315  -3.851  -13.771 1.00 15.83  ? 207 ALA   A CB   1 
ATOM   1592 N  N    . ASP   A 1 208 ? 11.175  -5.325  -15.662 1.00 15.85  ? 208 ASP   A N    1 
ATOM   1593 C  CA   . ASP   A 1 208 ? 10.575  -5.727  -14.398 1.00 15.87  ? 208 ASP   A CA   1 
ATOM   1594 C  C    . ASP   A 1 208 ? 10.073  -7.186  -14.432 1.00 17.22  ? 208 ASP   A C    1 
ATOM   1595 O  O    . ASP   A 1 208 ? 9.812   -7.780  -13.355 1.00 15.94  ? 208 ASP   A O    1 
ATOM   1596 C  CB   . ASP   A 1 208 ? 9.401   -4.803  -14.057 1.00 15.74  ? 208 ASP   A CB   1 
ATOM   1597 C  CG   . ASP   A 1 208 ? 9.827   -3.604  -13.227 1.00 15.39  ? 208 ASP   A CG   1 
ATOM   1598 O  OD1  . ASP   A 1 208 ? 10.224  -2.592  -13.849 1.00 14.46  ? 208 ASP   A OD1  1 
ATOM   1599 O  OD2  . ASP   A 1 208 ? 9.793   -3.705  -11.960 1.00 14.64  ? 208 ASP   A OD2  1 
ATOM   1600 N  N    . GLY   A 1 209 ? 9.916   -7.775  -15.611 1.00 18.30  ? 209 GLY   A N    1 
ATOM   1601 C  CA   . GLY   A 1 209 ? 9.549   -9.197  -15.707 1.00 18.85  ? 209 GLY   A CA   1 
ATOM   1602 C  C    . GLY   A 1 209 ? 8.561   -9.490  -16.825 1.00 17.90  ? 209 GLY   A C    1 
ATOM   1603 O  O    . GLY   A 1 209 ? 8.117   -8.557  -17.507 1.00 17.14  ? 209 GLY   A O    1 
ATOM   1604 N  N    . ILE   A 1 210 ? 8.299   -10.786 -17.015 1.00 18.50  ? 210 ILE   A N    1 
ATOM   1605 C  CA   . ILE   A 1 210 ? 7.299   -11.387 -17.950 1.00 17.64  ? 210 ILE   A CA   1 
ATOM   1606 C  C    . ILE   A 1 210 ? 6.273   -12.136 -17.109 1.00 17.02  ? 210 ILE   A C    1 
ATOM   1607 O  O    . ILE   A 1 210 ? 6.691   -12.753 -16.135 1.00 16.53  ? 210 ILE   A O    1 
ATOM   1608 C  CB   . ILE   A 1 210 ? 7.987   -12.358 -18.927 1.00 17.31  ? 210 ILE   A CB   1 
ATOM   1609 C  CG1  . ILE   A 1 210 ? 9.133   -11.675 -19.669 1.00 17.06  ? 210 ILE   A CG1  1 
ATOM   1610 C  CG2  . ILE   A 1 210 ? 6.968   -12.969 -19.880 1.00 17.06  ? 210 ILE   A CG2  1 
ATOM   1611 C  CD1  . ILE   A 1 210 ? 9.935   -12.622 -20.514 1.00 18.15  ? 210 ILE   A CD1  1 
ATOM   1612 N  N    . ALA   A 1 211 ? 5.010   -12.177 -17.543 1.00 17.28  ? 211 ALA   A N    1 
ATOM   1613 C  CA   . ALA   A 1 211 ? 3.948   -12.969 -16.890 1.00 15.94  ? 211 ALA   A CA   1 
ATOM   1614 C  C    . ALA   A 1 211 ? 3.121   -13.686 -17.950 1.00 16.41  ? 211 ALA   A C    1 
ATOM   1615 O  O    . ALA   A 1 211 ? 2.854   -13.085 -19.018 1.00 16.67  ? 211 ALA   A O    1 
ATOM   1616 C  CB   . ALA   A 1 211 ? 3.095   -12.084 -16.026 1.00 16.19  ? 211 ALA   A CB   1 
ATOM   1617 N  N    . PHE   A 1 212 ? 2.768   -14.943 -17.666 1.00 14.96  ? 212 PHE   A N    1 
ATOM   1618 C  CA   . PHE   A 1 212 ? 1.634   -15.665 -18.283 1.00 14.74  ? 212 PHE   A CA   1 
ATOM   1619 C  C    . PHE   A 1 212 ? 0.408   -15.403 -17.413 1.00 14.29  ? 212 PHE   A C    1 
ATOM   1620 O  O    . PHE   A 1 212 ? 0.510   -15.531 -16.177 1.00 13.63  ? 212 PHE   A O    1 
ATOM   1621 C  CB   . PHE   A 1 212 ? 1.923   -17.159 -18.390 1.00 15.49  ? 212 PHE   A CB   1 
ATOM   1622 C  CG   . PHE   A 1 212 ? 0.723   -17.983 -18.774 1.00 16.12  ? 212 PHE   A CG   1 
ATOM   1623 C  CD1  . PHE   A 1 212 ? 0.342   -18.117 -20.097 1.00 16.50  ? 212 PHE   A CD1  1 
ATOM   1624 C  CD2  . PHE   A 1 212 ? -0.037  -18.610 -17.805 1.00 16.67  ? 212 PHE   A CD2  1 
ATOM   1625 C  CE1  . PHE   A 1 212 ? -0.764  -18.878 -20.438 1.00 16.44  ? 212 PHE   A CE1  1 
ATOM   1626 C  CE2  . PHE   A 1 212 ? -1.154  -19.354 -18.147 1.00 16.07  ? 212 PHE   A CE2  1 
ATOM   1627 C  CZ   . PHE   A 1 212 ? -1.503  -19.500 -19.463 1.00 16.43  ? 212 PHE   A CZ   1 
ATOM   1628 N  N    . PHE   A 1 213 ? -0.720  -15.031 -18.017 1.00 13.95  ? 213 PHE   A N    1 
ATOM   1629 C  CA   . PHE   A 1 213 ? -1.919  -14.665 -17.232 1.00 13.71  ? 213 PHE   A CA   1 
ATOM   1630 C  C    . PHE   A 1 213 ? -3.185  -15.154 -17.910 1.00 13.69  ? 213 PHE   A C    1 
ATOM   1631 O  O    . PHE   A 1 213 ? -3.184  -15.424 -19.111 1.00 12.46  ? 213 PHE   A O    1 
ATOM   1632 C  CB   . PHE   A 1 213 ? -1.931  -13.154 -16.986 1.00 14.50  ? 213 PHE   A CB   1 
ATOM   1633 C  CG   . PHE   A 1 213 ? -2.329  -12.306 -18.165 1.00 15.01  ? 213 PHE   A CG   1 
ATOM   1634 C  CD1  . PHE   A 1 213 ? -1.400  -11.950 -19.128 1.00 14.47  ? 213 PHE   A CD1  1 
ATOM   1635 C  CD2  . PHE   A 1 213 ? -3.624  -11.824 -18.283 1.00 15.57  ? 213 PHE   A CD2  1 
ATOM   1636 C  CE1  . PHE   A 1 213 ? -1.778  -11.169 -20.210 1.00 15.89  ? 213 PHE   A CE1  1 
ATOM   1637 C  CE2  . PHE   A 1 213 ? -3.996  -11.019 -19.356 1.00 15.89  ? 213 PHE   A CE2  1 
ATOM   1638 C  CZ   . PHE   A 1 213 ? -3.078  -10.698 -20.326 1.00 15.70  ? 213 PHE   A CZ   1 
ATOM   1639 N  N    . ILE   A 1 214 ? -4.230  -15.238 -17.093 1.00 14.77  ? 214 ILE   A N    1 
ATOM   1640 C  CA   . ILE   A 1 214 ? -5.632  -15.561 -17.454 1.00 15.57  ? 214 ILE   A CA   1 
ATOM   1641 C  C    . ILE   A 1 214 ? -6.484  -14.420 -16.905 1.00 15.71  ? 214 ILE   A C    1 
ATOM   1642 O  O    . ILE   A 1 214 ? -6.298  -14.052 -15.729 1.00 14.69  ? 214 ILE   A O    1 
ATOM   1643 C  CB   . ILE   A 1 214 ? -6.055  -16.927 -16.888 1.00 17.19  ? 214 ILE   A CB   1 
ATOM   1644 C  CG1  . ILE   A 1 214 ? -5.100  -18.045 -17.324 1.00 18.68  ? 214 ILE   A CG1  1 
ATOM   1645 C  CG2  . ILE   A 1 214 ? -7.485  -17.243 -17.281 1.00 17.88  ? 214 ILE   A CG2  1 
ATOM   1646 C  CD1  . ILE   A 1 214 ? -4.147  -18.469 -16.249 1.00 19.38  ? 214 ILE   A CD1  1 
ATOM   1647 N  N    . SER   A 1 215 ? -7.287  -13.847 -17.748 1.00 15.91  ? 215 SER   A N    1 
ATOM   1648 C  CA   . SER   A 1 215 ? -8.111  -12.733 -17.277 1.00 18.10  ? 215 SER   A CA   1 
ATOM   1649 C  C    . SER   A 1 215 ? -9.504  -12.895 -17.839 1.00 17.03  ? 215 SER   A C    1 
ATOM   1650 O  O    . SER   A 1 215 ? -9.708  -13.683 -18.720 1.00 16.40  ? 215 SER   A O    1 
ATOM   1651 C  CB   . SER   A 1 215 ? -7.521  -11.446 -17.791 1.00 19.62  ? 215 SER   A CB   1 
ATOM   1652 O  OG   . SER   A 1 215 ? -7.351  -11.504 -19.199 1.00 20.85  ? 215 SER   A OG   1 
ATOM   1653 N  N    . ASN   A 1 216 ? -10.330 -11.927 -17.495 1.00 17.40  ? 216 ASN   A N    1 
ATOM   1654 C  CA   . ASN   A 1 216 ? -11.657 -11.738 -18.105 1.00 18.15  ? 216 ASN   A CA   1 
ATOM   1655 C  C    . ASN   A 1 216 ? -11.392 -11.439 -19.590 1.00 17.78  ? 216 ASN   A C    1 
ATOM   1656 O  O    . ASN   A 1 216 ? -10.445 -10.741 -19.917 1.00 18.10  ? 216 ASN   A O    1 
ATOM   1657 C  CB   . ASN   A 1 216 ? -12.431 -10.632 -17.397 1.00 18.53  ? 216 ASN   A CB   1 
ATOM   1658 C  CG   . ASN   A 1 216 ? -11.560 -9.427  -17.114 1.00 21.53  ? 216 ASN   A CG   1 
ATOM   1659 O  OD1  . ASN   A 1 216 ? -10.654 -9.480  -16.304 1.00 20.47  ? 216 ASN   A OD1  1 
ATOM   1660 N  ND2  . ASN   A 1 216 ? -11.799 -8.354  -17.819 1.00 22.32  ? 216 ASN   A ND2  1 
ATOM   1661 N  N    . ILE   A 1 217 ? -12.296 -11.845 -20.460 1.00 18.16  ? 217 ILE   A N    1 
ATOM   1662 C  CA   . ILE   A 1 217 ? -12.096 -11.730 -21.931 1.00 18.48  ? 217 ILE   A CA   1 
ATOM   1663 C  C    . ILE   A 1 217 ? -11.809 -10.291 -22.383 1.00 18.67  ? 217 ILE   A C    1 
ATOM   1664 O  O    . ILE   A 1 217 ? -11.056 -10.171 -23.294 1.00 19.82  ? 217 ILE   A O    1 
ATOM   1665 C  CB   . ILE   A 1 217 ? -13.241 -12.380 -22.728 1.00 20.01  ? 217 ILE   A CB   1 
ATOM   1666 C  CG1  . ILE   A 1 217 ? -14.565 -11.649 -22.530 1.00 21.40  ? 217 ILE   A CG1  1 
ATOM   1667 C  CG2  . ILE   A 1 217 ? -13.344 -13.871 -22.442 1.00 19.72  ? 217 ILE   A CG2  1 
ATOM   1668 C  CD1  . ILE   A 1 217 ? -15.641 -12.056 -23.475 1.00 22.62  ? 217 ILE   A CD1  1 
ATOM   1669 N  N    . ASP   A 1 218 ? -12.411 -9.280  -21.770 1.00 19.64  ? 218 ASP   A N    1 
ATOM   1670 C  CA   . ASP   A 1 218 ? -12.250 -7.845  -22.123 1.00 21.86  ? 218 ASP   A CA   1 
ATOM   1671 C  C    . ASP   A 1 218 ? -11.105 -7.141  -21.371 1.00 21.35  ? 218 ASP   A C    1 
ATOM   1672 O  O    . ASP   A 1 218 ? -11.037 -5.944  -21.437 1.00 19.82  ? 218 ASP   A O    1 
ATOM   1673 C  CB   . ASP   A 1 218 ? -13.588 -7.127  -22.003 1.00 24.28  ? 218 ASP   A CB   1 
ATOM   1674 C  CG   . ASP   A 1 218 ? -14.126 -7.111  -20.590 1.00 28.57  ? 218 ASP   A CG   1 
ATOM   1675 O  OD1  . ASP   A 1 218 ? -14.080 -8.130  -19.931 1.00 29.39  ? 218 ASP   A OD1  1 
ATOM   1676 O  OD2  . ASP   A 1 218 ? -14.551 -6.070  -20.172 1.00 33.68  ? 218 ASP   A OD2  1 
ATOM   1677 N  N    . SER   A 1 219 ? -10.224 -7.881  -20.711 1.00 20.60  ? 219 SER   A N    1 
ATOM   1678 C  CA   . SER   A 1 219 ? -9.051  -7.319  -19.999 1.00 20.18  ? 219 SER   A CA   1 
ATOM   1679 C  C    . SER   A 1 219 ? -8.261  -6.358  -20.906 1.00 19.89  ? 219 SER   A C    1 
ATOM   1680 O  O    . SER   A 1 219 ? -7.942  -6.701  -22.061 1.00 18.69  ? 219 SER   A O    1 
ATOM   1681 C  CB   . SER   A 1 219 ? -8.163  -8.420  -19.453 1.00 21.66  ? 219 SER   A CB   1 
ATOM   1682 O  OG   . SER   A 1 219 ? -7.214  -7.904  -18.522 1.00 22.68  ? 219 SER   A OG   1 
ATOM   1683 N  N    . SER   A 1 220 ? -7.871  -5.214  -20.348 1.00 19.14  ? 220 SER   A N    1 
ATOM   1684 C  CA   . SER   A 1 220 ? -6.940  -4.235  -20.968 1.00 20.67  ? 220 SER   A CA   1 
ATOM   1685 C  C    . SER   A 1 220 ? -5.816  -3.879  -19.985 1.00 18.99  ? 220 SER   A C    1 
ATOM   1686 O  O    . SER   A 1 220 ? -5.998  -4.067  -18.759 1.00 18.03  ? 220 SER   A O    1 
ATOM   1687 C  CB   . SER   A 1 220 ? -7.714  -2.995  -21.364 1.00 21.44  ? 220 SER   A CB   1 
ATOM   1688 O  OG   . SER   A 1 220 ? -8.379  -2.507  -20.206 1.00 21.68  ? 220 SER   A OG   1 
ATOM   1689 N  N    . ILE   A 1 221 ? -4.724  -3.305  -20.489 1.00 19.76  ? 221 ILE   A N    1 
ATOM   1690 C  CA   . ILE   A 1 221 ? -3.593  -2.832  -19.636 1.00 19.62  ? 221 ILE   A CA   1 
ATOM   1691 C  C    . ILE   A 1 221 ? -4.159  -1.828  -18.643 1.00 18.98  ? 221 ILE   A C    1 
ATOM   1692 O  O    . ILE   A 1 221 ? -4.674  -0.813  -19.060 1.00 20.37  ? 221 ILE   A O    1 
ATOM   1693 C  CB   . ILE   A 1 221 ? -2.444  -2.228  -20.460 1.00 19.78  ? 221 ILE   A CB   1 
ATOM   1694 C  CG1  . ILE   A 1 221 ? -1.795  -3.279  -21.359 1.00 20.43  ? 221 ILE   A CG1  1 
ATOM   1695 C  CG2  . ILE   A 1 221 ? -1.428  -1.619  -19.512 1.00 21.35  ? 221 ILE   A CG2  1 
ATOM   1696 C  CD1  . ILE   A 1 221 ? -0.713  -2.770  -22.271 1.00 19.52  ? 221 ILE   A CD1  1 
ATOM   1697 N  N    . PRO   A 1 222 ? -4.110  -2.064  -17.313 1.00 19.67  ? 222 PRO   A N    1 
ATOM   1698 C  CA   . PRO   A 1 222 ? -4.501  -1.035  -16.345 1.00 19.59  ? 222 PRO   A CA   1 
ATOM   1699 C  C    . PRO   A 1 222 ? -3.595  0.214   -16.382 1.00 20.95  ? 222 PRO   A C    1 
ATOM   1700 O  O    . PRO   A 1 222 ? -2.418  0.119   -16.707 1.00 17.82  ? 222 PRO   A O    1 
ATOM   1701 C  CB   . PRO   A 1 222 ? -4.405  -1.712  -14.971 1.00 18.87  ? 222 PRO   A CB   1 
ATOM   1702 C  CG   . PRO   A 1 222 ? -4.359  -3.206  -15.302 1.00 19.10  ? 222 PRO   A CG   1 
ATOM   1703 C  CD   . PRO   A 1 222 ? -3.684  -3.312  -16.657 1.00 18.96  ? 222 PRO   A CD   1 
ATOM   1704 N  N    . SER   A 1 223 ? -4.202  1.368   -16.091 1.00 21.71  ? 223 SER   A N    1 
ATOM   1705 C  CA   . SER   A 1 223 ? -3.553  2.702   -16.065 1.00 23.79  ? 223 SER   A CA   1 
ATOM   1706 C  C    . SER   A 1 223 ? -2.409  2.693   -15.044 1.00 21.27  ? 223 SER   A C    1 
ATOM   1707 O  O    . SER   A 1 223 ? -2.615  2.254   -13.912 1.00 21.49  ? 223 SER   A O    1 
ATOM   1708 C  CB   . SER   A 1 223 ? -4.581  3.776   -15.773 1.00 27.02  ? 223 SER   A CB   1 
ATOM   1709 O  OG   . SER   A 1 223 ? -3.948  5.023   -15.500 1.00 33.38  ? 223 SER   A OG   1 
ATOM   1710 N  N    . GLY   A 1 224 ? -1.218  3.109   -15.456 1.00 22.39  ? 224 GLY   A N    1 
ATOM   1711 C  CA   . GLY   A 1 224 ? -0.037  3.172   -14.576 1.00 21.91  ? 224 GLY   A CA   1 
ATOM   1712 C  C    . GLY   A 1 224 ? 0.555   1.807   -14.235 1.00 22.03  ? 224 GLY   A C    1 
ATOM   1713 O  O    . GLY   A 1 224 ? 1.399   1.770   -13.338 1.00 27.28  ? 224 GLY   A O    1 
ATOM   1714 N  N    . SER   A 1 225 ? 0.234   0.725   -14.947 1.00 19.41  ? 225 SER   A N    1 
ATOM   1715 C  CA   . SER   A 1 225 ? 0.701   -0.643  -14.594 1.00 18.35  ? 225 SER   A CA   1 
ATOM   1716 C  C    . SER   A 1 225 ? 2.086   -0.965  -15.200 1.00 17.82  ? 225 SER   A C    1 
ATOM   1717 O  O    . SER   A 1 225 ? 2.388   -2.187  -15.389 1.00 16.18  ? 225 SER   A O    1 
ATOM   1718 C  CB   . SER   A 1 225 ? -0.345  -1.663  -15.000 1.00 18.12  ? 225 SER   A CB   1 
ATOM   1719 O  OG   . SER   A 1 225 ? -0.362  -1.819  -16.404 1.00 18.24  ? 225 SER   A OG   1 
ATOM   1720 N  N    . THR   A 1 226 ? 2.907   0.051   -15.532 1.00 16.67  ? 226 THR   A N    1 
ATOM   1721 C  CA   . THR   A 1 226 ? 4.334   -0.142  -15.914 1.00 16.48  ? 226 THR   A CA   1 
ATOM   1722 C  C    . THR   A 1 226 ? 5.122   -0.593  -14.675 1.00 16.11  ? 226 THR   A C    1 
ATOM   1723 O  O    . THR   A 1 226 ? 4.579   -0.577  -13.553 1.00 16.14  ? 226 THR   A O    1 
ATOM   1724 C  CB   . THR   A 1 226 ? 4.983   1.107   -16.547 1.00 17.53  ? 226 THR   A CB   1 
ATOM   1725 O  OG1  . THR   A 1 226 ? 4.904   2.188   -15.609 1.00 19.14  ? 226 THR   A OG1  1 
ATOM   1726 C  CG2  . THR   A 1 226 ? 4.376   1.525   -17.875 1.00 17.20  ? 226 THR   A CG2  1 
ATOM   1727 N  N    . GLY   A 1 227 ? 6.379   -0.985  -14.878 1.00 16.24  ? 227 GLY   A N    1 
ATOM   1728 C  CA   . GLY   A 1 227 ? 7.299   -1.392  -13.802 1.00 15.78  ? 227 GLY   A CA   1 
ATOM   1729 C  C    . GLY   A 1 227 ? 6.762   -2.566  -13.008 1.00 15.58  ? 227 GLY   A C    1 
ATOM   1730 O  O    . GLY   A 1 227 ? 6.343   -3.552  -13.614 1.00 15.79  ? 227 GLY   A O    1 
ATOM   1731 N  N    . ARG   A 1 228 ? 6.741   -2.454  -11.685 1.00 15.59  ? 228 ARG   A N    1 
ATOM   1732 C  CA   . ARG   A 1 228 ? 6.541   -3.617  -10.791 1.00 16.30  ? 228 ARG   A CA   1 
ATOM   1733 C  C    . ARG   A 1 228 ? 5.138   -4.237  -10.926 1.00 15.98  ? 228 ARG   A C    1 
ATOM   1734 O  O    . ARG   A 1 228 ? 4.958   -5.352  -10.349 1.00 15.34  ? 228 ARG   A O    1 
ATOM   1735 C  CB   . ARG   A 1 228 ? 6.808   -3.205  -9.344  1.00 16.52  ? 228 ARG   A CB   1 
ATOM   1736 C  CG   . ARG   A 1 228 ? 5.764   -2.256  -8.782  1.00 16.45  ? 228 ARG   A CG   1 
ATOM   1737 C  CD   . ARG   A 1 228 ? 6.374   -1.375  -7.717  1.00 16.91  ? 228 ARG   A CD   1 
ATOM   1738 N  NE   . ARG   A 1 228 ? 5.347   -0.544  -7.105  1.00 16.76  ? 228 ARG   A NE   1 
ATOM   1739 C  CZ   . ARG   A 1 228 ? 5.461   0.046   -5.934  1.00 16.94  ? 228 ARG   A CZ   1 
ATOM   1740 N  NH1  . ARG   A 1 228 ? 6.574   -0.098  -5.218  1.00 16.27  ? 228 ARG   A NH1  1 
ATOM   1741 N  NH2  . ARG   A 1 228 ? 4.446   0.774   -5.482  1.00 17.89  ? 228 ARG   A NH2  1 
ATOM   1742 N  N    . LEU   A 1 229 ? 4.191   -3.588  -11.621 1.00 15.89  ? 229 LEU   A N    1 
ATOM   1743 C  CA   . LEU   A 1 229 ? 2.792   -4.092  -11.747 1.00 16.66  ? 229 LEU   A CA   1 
ATOM   1744 C  C    . LEU   A 1 229 ? 2.625   -4.990  -12.980 1.00 16.48  ? 229 LEU   A C    1 
ATOM   1745 O  O    . LEU   A 1 229 ? 1.493   -5.533  -13.160 1.00 16.90  ? 229 LEU   A O    1 
ATOM   1746 C  CB   . LEU   A 1 229 ? 1.806   -2.915  -11.773 1.00 16.53  ? 229 LEU   A CB   1 
ATOM   1747 C  CG   . LEU   A 1 229 ? 1.766   -2.077  -10.495 1.00 17.31  ? 229 LEU   A CG   1 
ATOM   1748 C  CD1  . LEU   A 1 229 ? 0.593   -1.117  -10.513 1.00 18.06  ? 229 LEU   A CD1  1 
ATOM   1749 C  CD2  . LEU   A 1 229 ? 1.725   -2.935  -9.234  1.00 17.06  ? 229 LEU   A CD2  1 
ATOM   1750 N  N    . LEU   A 1 230 ? 3.668   -5.110  -13.806 1.00 15.45  ? 230 LEU   A N    1 
ATOM   1751 C  CA   . LEU   A 1 230 ? 3.816   -6.145  -14.865 1.00 16.59  ? 230 LEU   A CA   1 
ATOM   1752 C  C    . LEU   A 1 230 ? 2.703   -6.060  -15.922 1.00 15.68  ? 230 LEU   A C    1 
ATOM   1753 O  O    . LEU   A 1 230 ? 2.571   -7.021  -16.737 1.00 13.70  ? 230 LEU   A O    1 
ATOM   1754 C  CB   . LEU   A 1 230 ? 3.844   -7.512  -14.183 1.00 18.62  ? 230 LEU   A CB   1 
ATOM   1755 C  CG   . LEU   A 1 230 ? 4.975   -7.657  -13.164 1.00 21.25  ? 230 LEU   A CG   1 
ATOM   1756 C  CD1  . LEU   A 1 230 ? 4.859   -8.960  -12.364 1.00 23.59  ? 230 LEU   A CD1  1 
ATOM   1757 C  CD2  . LEU   A 1 230 ? 6.318   -7.581  -13.868 1.00 21.47  ? 230 LEU   A CD2  1 
ATOM   1758 N  N    . GLY   A 1 231 ? 2.003   -4.927  -15.954 1.00 15.18  ? 231 GLY   A N    1 
ATOM   1759 C  CA   . GLY   A 1 231 ? 0.926   -4.607  -16.904 1.00 16.36  ? 231 GLY   A CA   1 
ATOM   1760 C  C    . GLY   A 1 231 ? -0.349  -5.354  -16.576 1.00 17.02  ? 231 GLY   A C    1 
ATOM   1761 O  O    . GLY   A 1 231 ? -1.174  -5.515  -17.487 1.00 17.27  ? 231 GLY   A O    1 
ATOM   1762 N  N    . LEU   A 1 232 ? -0.494  -5.811  -15.330 1.00 18.07  ? 232 LEU   A N    1 
ATOM   1763 C  CA   . LEU   A 1 232 ? -1.584  -6.731  -14.914 1.00 18.89  ? 232 LEU   A CA   1 
ATOM   1764 C  C    . LEU   A 1 232 ? -2.510  -6.079  -13.888 1.00 18.20  ? 232 LEU   A C    1 
ATOM   1765 O  O    . LEU   A 1 232 ? -3.712  -6.359  -13.946 1.00 17.66  ? 232 LEU   A O    1 
ATOM   1766 C  CB   . LEU   A 1 232 ? -0.954  -7.995  -14.324 1.00 19.45  ? 232 LEU   A CB   1 
ATOM   1767 C  CG   . LEU   A 1 232 ? -0.205  -8.892  -15.313 1.00 20.97  ? 232 LEU   A CG   1 
ATOM   1768 C  CD1  . LEU   A 1 232 ? 0.190   -10.193 -14.636 1.00 22.15  ? 232 LEU   A CD1  1 
ATOM   1769 C  CD2  . LEU   A 1 232 ? -1.031  -9.186  -16.549 1.00 21.56  ? 232 LEU   A CD2  1 
ATOM   1770 N  N    . PHE   A 1 233 ? -1.968  -5.305  -12.945 1.00 18.63  ? 233 PHE   A N    1 
ATOM   1771 C  CA   . PHE   A 1 233 ? -2.707  -4.833  -11.739 1.00 19.62  ? 233 PHE   A CA   1 
ATOM   1772 C  C    . PHE   A 1 233 ? -2.758  -3.306  -11.706 1.00 19.10  ? 233 PHE   A C    1 
ATOM   1773 O  O    . PHE   A 1 233 ? -1.843  -2.638  -12.163 1.00 17.58  ? 233 PHE   A O    1 
ATOM   1774 C  CB   . PHE   A 1 233 ? -2.085  -5.426  -10.475 1.00 20.59  ? 233 PHE   A CB   1 
ATOM   1775 C  CG   . PHE   A 1 233 ? -2.006  -6.930  -10.509 1.00 21.50  ? 233 PHE   A CG   1 
ATOM   1776 C  CD1  . PHE   A 1 233 ? -3.111  -7.702  -10.189 1.00 21.64  ? 233 PHE   A CD1  1 
ATOM   1777 C  CD2  . PHE   A 1 233 ? -0.858  -7.565  -10.953 1.00 21.43  ? 233 PHE   A CD2  1 
ATOM   1778 C  CE1  . PHE   A 1 233 ? -3.044  -9.083  -10.254 1.00 20.95  ? 233 PHE   A CE1  1 
ATOM   1779 C  CE2  . PHE   A 1 233 ? -0.794  -8.950  -11.004 1.00 22.09  ? 233 PHE   A CE2  1 
ATOM   1780 C  CZ   . PHE   A 1 233 ? -1.884  -9.699  -10.640 1.00 20.61  ? 233 PHE   A CZ   1 
ATOM   1781 N  N    . PRO   A 1 234 ? -3.875  -2.715  -11.229 1.00 20.87  ? 234 PRO   A N    1 
ATOM   1782 C  CA   . PRO   A 1 234 ? -3.998  -1.260  -11.138 1.00 20.93  ? 234 PRO   A CA   1 
ATOM   1783 C  C    . PRO   A 1 234 ? -3.171  -0.679  -9.983  1.00 21.28  ? 234 PRO   A C    1 
ATOM   1784 O  O    . PRO   A 1 234 ? -2.806  0.441   -10.091 1.00 21.14  ? 234 PRO   A O    1 
ATOM   1785 C  CB   . PRO   A 1 234 ? -5.503  -1.067  -10.878 1.00 20.47  ? 234 PRO   A CB   1 
ATOM   1786 C  CG   . PRO   A 1 234 ? -5.912  -2.319  -10.105 1.00 20.57  ? 234 PRO   A CG   1 
ATOM   1787 C  CD   . PRO   A 1 234 ? -5.091  -3.414  -10.759 1.00 20.36  ? 234 PRO   A CD   1 
ATOM   1788 N  N    . ASP   A 1 235 ? -2.958  -1.448  -8.904  1.00 25.30  ? 235 ASP   A N    1 
ATOM   1789 C  CA   . ASP   A 1 235 ? -2.192  -1.056  -7.683  1.00 24.92  ? 235 ASP   A CA   1 
ATOM   1790 C  C    . ASP   A 1 235 ? -1.427  -2.274  -7.143  1.00 23.75  ? 235 ASP   A C    1 
ATOM   1791 O  O    . ASP   A 1 235 ? -1.656  -3.373  -7.652  1.00 22.20  ? 235 ASP   A O    1 
ATOM   1792 C  CB   . ASP   A 1 235 ? -3.110  -0.434  -6.625  1.00 26.05  ? 235 ASP   A CB   1 
ATOM   1793 C  CG   . ASP   A 1 235 ? -4.036  -1.374  -5.848  1.00 30.00  ? 235 ASP   A CG   1 
ATOM   1794 O  OD1  . ASP   A 1 235 ? -3.791  -2.599  -5.843  1.00 31.00  ? 235 ASP   A OD1  1 
ATOM   1795 O  OD2  . ASP   A 1 235 ? -5.000  -0.860  -5.200  1.00 33.54  ? 235 ASP   A OD2  1 
ATOM   1796 N  N    . ALA   A 1 236 ? -0.596  -2.078  -6.115  1.00 22.85  ? 236 ALA   A N    1 
ATOM   1797 C  CA   . ALA   A 1 236 ? 0.303   -3.094  -5.526  1.00 25.08  ? 236 ALA   A CA   1 
ATOM   1798 C  C    . ALA   A 1 236 ? -0.347  -3.755  -4.306  1.00 27.52  ? 236 ALA   A C    1 
ATOM   1799 O  O    . ALA   A 1 236 ? 0.403   -4.230  -3.426  1.00 34.88  ? 236 ALA   A O    1 
ATOM   1800 C  CB   . ALA   A 1 236 ? 1.628   -2.475  -5.144  1.00 23.38  ? 236 ALA   A CB   1 
ATOM   1801 N  N    . ASN   A 1 237 ? -1.672  -3.825  -4.258  1.00 30.40  ? 237 ASN   A N    1 
ATOM   1802 C  CA   . ASN   A 1 237 ? -2.406  -4.483  -3.144  1.00 32.50  ? 237 ASN   A CA   1 
ATOM   1803 C  C    . ASN   A 1 237 ? -2.733  -5.940  -3.501  1.00 35.51  ? 237 ASN   A C    1 
ATOM   1804 O  O    . ASN   A 1 237 ? -2.647  -6.398  -4.656  1.00 35.80  ? 237 ASN   A O    1 
ATOM   1805 C  CB   . ASN   A 1 237 ? -3.626  -3.657  -2.748  1.00 33.68  ? 237 ASN   A CB   1 
ATOM   1806 C  CG   . ASN   A 1 237 ? -3.215  -2.429  -1.970  1.00 31.10  ? 237 ASN   A CG   1 
ATOM   1807 O  OD1  . ASN   A 1 237 ? -2.372  -2.517  -1.081  1.00 33.99  ? 237 ASN   A OD1  1 
ATOM   1808 N  ND2  . ASN   A 1 237 ? -3.799  -1.296  -2.292  1.00 28.10  ? 237 ASN   A ND2  1 
ATOM   1809 O  OXT  . ASN   A 1 237 ? -3.072  -6.691  -2.573  1.00 38.19  ? 237 ASN   A OXT  1 
ATOM   1810 N  N    . ALA   B 1 1   ? -29.451 -49.609 -10.343 1.00 49.81  ? 1   ALA   B N    1 
ATOM   1811 C  CA   . ALA   B 1 1   ? -29.469 -48.307 -9.618  1.00 45.18  ? 1   ALA   B CA   1 
ATOM   1812 C  C    . ALA   B 1 1   ? -30.571 -47.415 -10.205 1.00 41.64  ? 1   ALA   B C    1 
ATOM   1813 O  O    . ALA   B 1 1   ? -30.976 -47.648 -11.350 1.00 39.83  ? 1   ALA   B O    1 
ATOM   1814 C  CB   . ALA   B 1 1   ? -28.111 -47.641 -9.687  1.00 42.68  ? 1   ALA   B CB   1 
ATOM   1815 N  N    . ASP   B 1 2   ? -31.021 -46.428 -9.425  1.00 37.79  ? 2   ASP   B N    1 
ATOM   1816 C  CA   . ASP   B 1 2   ? -32.143 -45.520 -9.760  1.00 35.01  ? 2   ASP   B CA   1 
ATOM   1817 C  C    . ASP   B 1 2   ? -31.647 -44.468 -10.748 1.00 31.35  ? 2   ASP   B C    1 
ATOM   1818 O  O    . ASP   B 1 2   ? -30.442 -44.288 -10.836 1.00 31.03  ? 2   ASP   B O    1 
ATOM   1819 C  CB   . ASP   B 1 2   ? -32.713 -44.893 -8.492  1.00 35.42  ? 2   ASP   B CB   1 
ATOM   1820 C  CG   . ASP   B 1 2   ? -33.256 -45.911 -7.505  1.00 37.96  ? 2   ASP   B CG   1 
ATOM   1821 O  OD1  . ASP   B 1 2   ? -33.561 -47.045 -7.939  1.00 36.57  ? 2   ASP   B OD1  1 
ATOM   1822 O  OD2  . ASP   B 1 2   ? -33.365 -45.558 -6.305  1.00 40.25  ? 2   ASP   B OD2  1 
ATOM   1823 N  N    . THR   B 1 3   ? -32.552 -43.864 -11.513 1.00 29.43  ? 3   THR   B N    1 
ATOM   1824 C  CA   . THR   B 1 3   ? -32.266 -42.719 -12.405 1.00 30.88  ? 3   THR   B CA   1 
ATOM   1825 C  C    . THR   B 1 3   ? -32.799 -41.482 -11.694 1.00 28.23  ? 3   THR   B C    1 
ATOM   1826 O  O    . THR   B 1 3   ? -33.983 -41.496 -11.343 1.00 30.24  ? 3   THR   B O    1 
ATOM   1827 C  CB   . THR   B 1 3   ? -32.869 -42.915 -13.804 1.00 33.24  ? 3   THR   B CB   1 
ATOM   1828 O  OG1  . THR   B 1 3   ? -32.352 -44.125 -14.347 1.00 34.05  ? 3   THR   B OG1  1 
ATOM   1829 C  CG2  . THR   B 1 3   ? -32.514 -41.808 -14.772 1.00 34.54  ? 3   THR   B CG2  1 
ATOM   1830 N  N    . ILE   B 1 4   ? -31.957 -40.478 -11.453 1.00 26.13  ? 4   ILE   B N    1 
ATOM   1831 C  CA   . ILE   B 1 4   ? -32.348 -39.305 -10.621 1.00 24.40  ? 4   ILE   B CA   1 
ATOM   1832 C  C    . ILE   B 1 4   ? -32.065 -38.021 -11.383 1.00 24.74  ? 4   ILE   B C    1 
ATOM   1833 O  O    . ILE   B 1 4   ? -30.902 -37.819 -11.781 1.00 24.60  ? 4   ILE   B O    1 
ATOM   1834 C  CB   . ILE   B 1 4   ? -31.620 -39.287 -9.270  1.00 23.78  ? 4   ILE   B CB   1 
ATOM   1835 C  CG1  . ILE   B 1 4   ? -31.959 -40.511 -8.412  1.00 23.01  ? 4   ILE   B CG1  1 
ATOM   1836 C  CG2  . ILE   B 1 4   ? -31.920 -37.979 -8.557  1.00 24.70  ? 4   ILE   B CG2  1 
ATOM   1837 C  CD1  . ILE   B 1 4   ? -33.272 -40.428 -7.702  1.00 23.66  ? 4   ILE   B CD1  1 
ATOM   1838 N  N    . VAL   B 1 5   ? -33.102 -37.195 -11.545 1.00 22.43  ? 5   VAL   B N    1 
ATOM   1839 C  CA   . VAL   B 1 5   ? -32.968 -35.745 -11.825 1.00 19.66  ? 5   VAL   B CA   1 
ATOM   1840 C  C    . VAL   B 1 5   ? -33.427 -35.021 -10.567 1.00 19.69  ? 5   VAL   B C    1 
ATOM   1841 O  O    . VAL   B 1 5   ? -34.456 -35.429 -10.029 1.00 19.31  ? 5   VAL   B O    1 
ATOM   1842 C  CB   . VAL   B 1 5   ? -33.772 -35.351 -13.070 1.00 19.30  ? 5   VAL   B CB   1 
ATOM   1843 C  CG1  . VAL   B 1 5   ? -33.829 -33.837 -13.255 1.00 18.78  ? 5   VAL   B CG1  1 
ATOM   1844 C  CG2  . VAL   B 1 5   ? -33.198 -36.042 -14.297 1.00 19.08  ? 5   VAL   B CG2  1 
ATOM   1845 N  N    . ALA   B 1 6   ? -32.690 -34.006 -10.098 1.00 19.26  ? 6   ALA   B N    1 
ATOM   1846 C  CA   . ALA   B 1 6   ? -33.003 -33.327 -8.813  1.00 18.44  ? 6   ALA   B CA   1 
ATOM   1847 C  C    . ALA   B 1 6   ? -32.611 -31.846 -8.844  1.00 18.20  ? 6   ALA   B C    1 
ATOM   1848 O  O    . ALA   B 1 6   ? -31.700 -31.458 -9.605  1.00 16.95  ? 6   ALA   B O    1 
ATOM   1849 C  CB   . ALA   B 1 6   ? -32.333 -34.062 -7.678  1.00 19.12  ? 6   ALA   B CB   1 
ATOM   1850 N  N    . VAL   B 1 7   ? -33.333 -31.033 -8.074  1.00 17.84  ? 7   VAL   B N    1 
ATOM   1851 C  CA   . VAL   B 1 7   ? -32.894 -29.674 -7.675  1.00 17.24  ? 7   VAL   B CA   1 
ATOM   1852 C  C    . VAL   B 1 7   ? -32.541 -29.746 -6.190  1.00 17.85  ? 7   VAL   B C    1 
ATOM   1853 O  O    . VAL   B 1 7   ? -33.438 -30.061 -5.371  1.00 17.05  ? 7   VAL   B O    1 
ATOM   1854 C  CB   . VAL   B 1 7   ? -33.947 -28.608 -7.992  1.00 17.56  ? 7   VAL   B CB   1 
ATOM   1855 C  CG1  . VAL   B 1 7   ? -33.531 -27.249 -7.466  1.00 18.05  ? 7   VAL   B CG1  1 
ATOM   1856 C  CG2  . VAL   B 1 7   ? -34.214 -28.525 -9.487  1.00 17.89  ? 7   VAL   B CG2  1 
ATOM   1857 N  N    . GLU   B 1 8   ? -31.267 -29.484 -5.861  1.00 18.09  ? 8   GLU   B N    1 
ATOM   1858 C  CA   . GLU   B 1 8   ? -30.759 -29.571 -4.468  1.00 17.86  ? 8   GLU   B CA   1 
ATOM   1859 C  C    . GLU   B 1 8   ? -30.705 -28.183 -3.822  1.00 17.42  ? 8   GLU   B C    1 
ATOM   1860 O  O    . GLU   B 1 8   ? -30.219 -27.223 -4.433  1.00 18.31  ? 8   GLU   B O    1 
ATOM   1861 C  CB   . GLU   B 1 8   ? -29.407 -30.281 -4.408  1.00 18.98  ? 8   GLU   B CB   1 
ATOM   1862 C  CG   . GLU   B 1 8   ? -28.281 -29.644 -5.209  1.00 19.90  ? 8   GLU   B CG   1 
ATOM   1863 C  CD   . GLU   B 1 8   ? -26.898 -30.199 -4.864  1.00 21.66  ? 8   GLU   B CD   1 
ATOM   1864 O  OE1  . GLU   B 1 8   ? -26.047 -29.391 -4.405  1.00 18.67  ? 8   GLU   B OE1  1 
ATOM   1865 O  OE2  . GLU   B 1 8   ? -26.686 -31.459 -5.003  1.00 20.59  ? 8   GLU   B OE2  1 
ATOM   1866 N  N    . LEU   B 1 9   ? -31.175 -28.101 -2.589  1.00 16.68  ? 9   LEU   B N    1 
ATOM   1867 C  CA   . LEU   B 1 9   ? -30.941 -26.946 -1.692  1.00 16.23  ? 9   LEU   B CA   1 
ATOM   1868 C  C    . LEU   B 1 9   ? -29.893 -27.409 -0.679  1.00 16.21  ? 9   LEU   B C    1 
ATOM   1869 O  O    . LEU   B 1 9   ? -30.286 -27.953 0.360   1.00 17.94  ? 9   LEU   B O    1 
ATOM   1870 C  CB   . LEU   B 1 9   ? -32.261 -26.556 -1.027  1.00 15.80  ? 9   LEU   B CB   1 
ATOM   1871 C  CG   . LEU   B 1 9   ? -33.165 -25.634 -1.834  1.00 15.94  ? 9   LEU   B CG   1 
ATOM   1872 C  CD1  . LEU   B 1 9   ? -33.370 -26.142 -3.255  1.00 16.08  ? 9   LEU   B CD1  1 
ATOM   1873 C  CD2  . LEU   B 1 9   ? -34.489 -25.454 -1.118  1.00 15.86  ? 9   LEU   B CD2  1 
ATOM   1874 N  N    . ASP   B 1 10  ? -28.617 -27.275 -1.041  1.00 15.70  ? 10  ASP   B N    1 
ATOM   1875 C  CA   . ASP   B 1 10  ? -27.442 -27.880 -0.358  1.00 14.64  ? 10  ASP   B CA   1 
ATOM   1876 C  C    . ASP   B 1 10  ? -26.896 -26.879 0.673   1.00 14.96  ? 10  ASP   B C    1 
ATOM   1877 O  O    . ASP   B 1 10  ? -26.306 -25.868 0.299   1.00 14.63  ? 10  ASP   B O    1 
ATOM   1878 C  CB   . ASP   B 1 10  ? -26.422 -28.334 -1.405  1.00 14.11  ? 10  ASP   B CB   1 
ATOM   1879 C  CG   . ASP   B 1 10  ? -25.260 -29.152 -0.871  1.00 13.82  ? 10  ASP   B CG   1 
ATOM   1880 O  OD1  . ASP   B 1 10  ? -25.103 -29.183 0.373   1.00 13.28  ? 10  ASP   B OD1  1 
ATOM   1881 O  OD2  . ASP   B 1 10  ? -24.497 -29.732 -1.705  1.00 12.85  ? 10  ASP   B OD2  1 
ATOM   1882 N  N    . THR   B 1 11  ? -27.121 -27.154 1.949   1.00 15.26  ? 11  THR   B N    1 
ATOM   1883 C  CA   . THR   B 1 11  ? -26.798 -26.239 3.057   1.00 15.90  ? 11  THR   B CA   1 
ATOM   1884 C  C    . THR   B 1 11  ? -25.354 -26.437 3.490   1.00 17.52  ? 11  THR   B C    1 
ATOM   1885 O  O    . THR   B 1 11  ? -24.910 -25.555 4.220   1.00 18.41  ? 11  THR   B O    1 
ATOM   1886 C  CB   . THR   B 1 11  ? -27.710 -26.453 4.265   1.00 16.06  ? 11  THR   B CB   1 
ATOM   1887 O  OG1  . THR   B 1 11  ? -27.662 -27.838 4.624   1.00 15.56  ? 11  THR   B OG1  1 
ATOM   1888 C  CG2  . THR   B 1 11  ? -29.135 -26.046 3.957   1.00 15.71  ? 11  THR   B CG2  1 
ATOM   1889 N  N    . TYR   B 1 12  ? -24.666 -27.519 3.067   1.00 17.72  ? 12  TYR   B N    1 
ATOM   1890 C  CA   . TYR   B 1 12  ? -23.323 -27.890 3.588   1.00 17.76  ? 12  TYR   B CA   1 
ATOM   1891 C  C    . TYR   B 1 12  ? -22.320 -28.144 2.466   1.00 18.00  ? 12  TYR   B C    1 
ATOM   1892 O  O    . TYR   B 1 12  ? -22.483 -29.048 1.651   1.00 20.74  ? 12  TYR   B O    1 
ATOM   1893 C  CB   . TYR   B 1 12  ? -23.393 -29.079 4.543   1.00 19.24  ? 12  TYR   B CB   1 
ATOM   1894 C  CG   . TYR   B 1 12  ? -22.073 -29.370 5.214   1.00 20.46  ? 12  TYR   B CG   1 
ATOM   1895 C  CD1  . TYR   B 1 12  ? -21.635 -28.637 6.309   1.00 20.93  ? 12  TYR   B CD1  1 
ATOM   1896 C  CD2  . TYR   B 1 12  ? -21.240 -30.358 4.729   1.00 20.17  ? 12  TYR   B CD2  1 
ATOM   1897 C  CE1  . TYR   B 1 12  ? -20.419 -28.905 6.922   1.00 21.58  ? 12  TYR   B CE1  1 
ATOM   1898 C  CE2  . TYR   B 1 12  ? -20.017 -30.621 5.317   1.00 21.48  ? 12  TYR   B CE2  1 
ATOM   1899 C  CZ   . TYR   B 1 12  ? -19.607 -29.901 6.421   1.00 20.59  ? 12  TYR   B CZ   1 
ATOM   1900 O  OH   . TYR   B 1 12  ? -18.396 -30.178 6.967   1.00 22.29  ? 12  TYR   B OH   1 
ATOM   1901 N  N    . PRO   B 1 13  ? -21.221 -27.365 2.420   1.00 17.90  ? 13  PRO   B N    1 
ATOM   1902 C  CA   . PRO   B 1 13  ? -20.180 -27.513 1.405   1.00 17.56  ? 13  PRO   B CA   1 
ATOM   1903 C  C    . PRO   B 1 13  ? -19.257 -28.736 1.531   1.00 17.46  ? 13  PRO   B C    1 
ATOM   1904 O  O    . PRO   B 1 13  ? -18.375 -28.721 2.334   1.00 18.85  ? 13  PRO   B O    1 
ATOM   1905 C  CB   . PRO   B 1 13  ? -19.288 -26.273 1.607   1.00 17.99  ? 13  PRO   B CB   1 
ATOM   1906 C  CG   . PRO   B 1 13  ? -20.105 -25.317 2.440   1.00 18.30  ? 13  PRO   B CG   1 
ATOM   1907 C  CD   . PRO   B 1 13  ? -20.957 -26.218 3.317   1.00 19.08  ? 13  PRO   B CD   1 
ATOM   1908 N  N    . ASN   B 1 14  ? -19.471 -29.770 0.719   1.00 17.67  ? 14  ASN   B N    1 
ATOM   1909 C  CA   . ASN   B 1 14  ? -18.568 -30.947 0.629   1.00 17.42  ? 14  ASN   B CA   1 
ATOM   1910 C  C    . ASN   B 1 14  ? -17.600 -30.668 -0.534  1.00 17.96  ? 14  ASN   B C    1 
ATOM   1911 O  O    . ASN   B 1 14  ? -17.871 -31.120 -1.673  1.00 15.49  ? 14  ASN   B O    1 
ATOM   1912 C  CB   . ASN   B 1 14  ? -19.367 -32.251 0.505   1.00 17.24  ? 14  ASN   B CB   1 
ATOM   1913 C  CG   . ASN   B 1 14  ? -20.419 -32.443 1.582   1.00 17.36  ? 14  ASN   B CG   1 
ATOM   1914 O  OD1  . ASN   B 1 14  ? -21.571 -32.060 1.403   1.00 14.08  ? 14  ASN   B OD1  1 
ATOM   1915 N  ND2  . ASN   B 1 14  ? -20.027 -33.036 2.705   1.00 17.78  ? 14  ASN   B ND2  1 
ATOM   1916 N  N    . THR   B 1 15  ? -16.539 -29.895 -0.272  1.00 18.96  ? 15  THR   B N    1 
ATOM   1917 C  CA   . THR   B 1 15  ? -15.626 -29.370 -1.330  1.00 20.11  ? 15  THR   B CA   1 
ATOM   1918 C  C    . THR   B 1 15  ? -14.800 -30.513 -1.924  1.00 20.74  ? 15  THR   B C    1 
ATOM   1919 O  O    . THR   B 1 15  ? -14.215 -30.324 -2.998  1.00 21.24  ? 15  THR   B O    1 
ATOM   1920 C  CB   . THR   B 1 15  ? -14.731 -28.230 -0.828  1.00 19.39  ? 15  THR   B CB   1 
ATOM   1921 O  OG1  . THR   B 1 15  ? -13.873 -28.715 0.195   1.00 19.74  ? 15  THR   B OG1  1 
ATOM   1922 C  CG2  . THR   B 1 15  ? -15.513 -27.040 -0.314  1.00 20.15  ? 15  THR   B CG2  1 
ATOM   1923 N  N    . ASP   B 1 16  ? -14.746 -31.660 -1.257  1.00 22.45  ? 16  ASP   B N    1 
ATOM   1924 C  CA   . ASP   B 1 16  ? -13.986 -32.831 -1.762  1.00 23.13  ? 16  ASP   B CA   1 
ATOM   1925 C  C    . ASP   B 1 16  ? -14.771 -33.552 -2.862  1.00 24.44  ? 16  ASP   B C    1 
ATOM   1926 O  O    . ASP   B 1 16  ? -14.122 -34.285 -3.599  1.00 26.55  ? 16  ASP   B O    1 
ATOM   1927 C  CB   . ASP   B 1 16  ? -13.602 -33.770 -0.623  1.00 23.99  ? 16  ASP   B CB   1 
ATOM   1928 C  CG   . ASP   B 1 16  ? -14.780 -34.273 0.182   1.00 26.24  ? 16  ASP   B CG   1 
ATOM   1929 O  OD1  . ASP   B 1 16  ? -15.839 -33.574 0.199   1.00 23.59  ? 16  ASP   B OD1  1 
ATOM   1930 O  OD2  . ASP   B 1 16  ? -14.624 -35.363 0.799   1.00 27.37  ? 16  ASP   B OD2  1 
ATOM   1931 N  N    . ILE   B 1 17  ? -16.099 -33.372 -2.976  1.00 24.65  ? 17  ILE   B N    1 
ATOM   1932 C  CA   . ILE   B 1 17  ? -16.926 -34.034 -4.036  1.00 24.03  ? 17  ILE   B CA   1 
ATOM   1933 C  C    . ILE   B 1 17  ? -17.581 -32.977 -4.942  1.00 22.76  ? 17  ILE   B C    1 
ATOM   1934 O  O    . ILE   B 1 17  ? -18.680 -33.251 -5.479  1.00 21.89  ? 17  ILE   B O    1 
ATOM   1935 C  CB   . ILE   B 1 17  ? -17.974 -35.006 -3.443  1.00 24.31  ? 17  ILE   B CB   1 
ATOM   1936 C  CG1  . ILE   B 1 17  ? -19.008 -34.297 -2.564  1.00 24.51  ? 17  ILE   B CG1  1 
ATOM   1937 C  CG2  . ILE   B 1 17  ? -17.291 -36.154 -2.709  1.00 25.15  ? 17  ILE   B CG2  1 
ATOM   1938 C  CD1  . ILE   B 1 17  ? -20.285 -35.085 -2.354  1.00 23.50  ? 17  ILE   B CD1  1 
ATOM   1939 N  N    . GLY   B 1 18  ? -16.921 -31.831 -5.135  1.00 21.68  ? 18  GLY   B N    1 
ATOM   1940 C  CA   . GLY   B 1 18  ? -17.233 -30.870 -6.212  1.00 20.13  ? 18  GLY   B CA   1 
ATOM   1941 C  C    . GLY   B 1 18  ? -18.222 -29.792 -5.810  1.00 19.19  ? 18  GLY   B C    1 
ATOM   1942 O  O    . GLY   B 1 18  ? -18.565 -29.003 -6.694  1.00 19.70  ? 18  GLY   B O    1 
ATOM   1943 N  N    . ASP   B 1 19  ? -18.729 -29.791 -4.573  1.00 17.74  ? 19  ASP   B N    1 
ATOM   1944 C  CA   . ASP   B 1 19  ? -19.562 -28.685 -4.040  1.00 18.30  ? 19  ASP   B CA   1 
ATOM   1945 C  C    . ASP   B 1 19  ? -18.719 -27.418 -4.029  1.00 19.66  ? 19  ASP   B C    1 
ATOM   1946 O  O    . ASP   B 1 19  ? -17.554 -27.457 -3.650  1.00 19.86  ? 19  ASP   B O    1 
ATOM   1947 C  CB   . ASP   B 1 19  ? -20.005 -28.882 -2.580  1.00 18.57  ? 19  ASP   B CB   1 
ATOM   1948 C  CG   . ASP   B 1 19  ? -21.302 -29.653 -2.414  1.00 17.04  ? 19  ASP   B CG   1 
ATOM   1949 O  OD1  . ASP   B 1 19  ? -21.928 -29.955 -3.438  1.00 16.44  ? 19  ASP   B OD1  1 
ATOM   1950 O  OD2  . ASP   B 1 19  ? -21.660 -29.934 -1.266  1.00 15.53  ? 19  ASP   B OD2  1 
ATOM   1951 N  N    . PRO   B 1 20  ? -19.299 -26.252 -4.382  1.00 20.92  ? 20  PRO   B N    1 
ATOM   1952 C  CA   . PRO   B 1 20  ? -18.602 -24.981 -4.229  1.00 20.86  ? 20  PRO   B CA   1 
ATOM   1953 C  C    . PRO   B 1 20  ? -18.496 -24.771 -2.713  1.00 22.05  ? 20  PRO   B C    1 
ATOM   1954 O  O    . PRO   B 1 20  ? -19.142 -25.525 -1.970  1.00 21.52  ? 20  PRO   B O    1 
ATOM   1955 C  CB   . PRO   B 1 20  ? -19.526 -23.976 -4.945  1.00 22.18  ? 20  PRO   B CB   1 
ATOM   1956 C  CG   . PRO   B 1 20  ? -20.912 -24.581 -4.797  1.00 22.10  ? 20  PRO   B CG   1 
ATOM   1957 C  CD   . PRO   B 1 20  ? -20.682 -26.085 -4.859  1.00 21.61  ? 20  PRO   B CD   1 
ATOM   1958 N  N    . SER   B 1 21  ? -17.745 -23.756 -2.284  1.00 23.37  ? 21  SER   B N    1 
ATOM   1959 C  CA   . SER   B 1 21  ? -17.317 -23.562 -0.872  1.00 23.80  ? 21  SER   B CA   1 
ATOM   1960 C  C    . SER   B 1 21  ? -18.347 -22.761 -0.081  1.00 22.91  ? 21  SER   B C    1 
ATOM   1961 O  O    . SER   B 1 21  ? -17.924 -22.104 0.876   1.00 24.84  ? 21  SER   B O    1 
ATOM   1962 C  CB   . SER   B 1 21  ? -15.954 -22.904 -0.797  1.00 25.03  ? 21  SER   B CB   1 
ATOM   1963 O  OG   . SER   B 1 21  ? -16.036 -21.556 -1.233  1.00 24.84  ? 21  SER   B OG   1 
ATOM   1964 N  N    . TYR   B 1 22  ? -19.644 -22.830 -0.422  1.00 22.27  ? 22  TYR   B N    1 
ATOM   1965 C  CA   . TYR   B 1 22  ? -20.727 -22.099 0.301   1.00 20.54  ? 22  TYR   B CA   1 
ATOM   1966 C  C    . TYR   B 1 22  ? -22.077 -22.787 0.096   1.00 20.42  ? 22  TYR   B C    1 
ATOM   1967 O  O    . TYR   B 1 22  ? -22.250 -23.549 -0.854  1.00 20.61  ? 22  TYR   B O    1 
ATOM   1968 C  CB   . TYR   B 1 22  ? -20.788 -20.647 -0.193  1.00 20.35  ? 22  TYR   B CB   1 
ATOM   1969 C  CG   . TYR   B 1 22  ? -20.598 -20.521 -1.685  1.00 19.51  ? 22  TYR   B CG   1 
ATOM   1970 C  CD1  . TYR   B 1 22  ? -21.576 -20.949 -2.563  1.00 18.90  ? 22  TYR   B CD1  1 
ATOM   1971 C  CD2  . TYR   B 1 22  ? -19.414 -20.035 -2.221  1.00 19.92  ? 22  TYR   B CD2  1 
ATOM   1972 C  CE1  . TYR   B 1 22  ? -21.400 -20.867 -3.934  1.00 18.55  ? 22  TYR   B CE1  1 
ATOM   1973 C  CE2  . TYR   B 1 22  ? -19.222 -19.946 -3.591  1.00 19.05  ? 22  TYR   B CE2  1 
ATOM   1974 C  CZ   . TYR   B 1 22  ? -20.215 -20.378 -4.449  1.00 18.23  ? 22  TYR   B CZ   1 
ATOM   1975 O  OH   . TYR   B 1 22  ? -20.022 -20.319 -5.794  1.00 17.08  ? 22  TYR   B OH   1 
ATOM   1976 N  N    . PRO   B 1 23  ? -23.099 -22.494 0.942   1.00 20.73  ? 23  PRO   B N    1 
ATOM   1977 C  CA   . PRO   B 1 23  ? -24.455 -22.996 0.699   1.00 20.57  ? 23  PRO   B CA   1 
ATOM   1978 C  C    . PRO   B 1 23  ? -24.866 -22.622 -0.730  1.00 20.00  ? 23  PRO   B C    1 
ATOM   1979 O  O    . PRO   B 1 23  ? -24.570 -21.531 -1.188  1.00 21.58  ? 23  PRO   B O    1 
ATOM   1980 C  CB   . PRO   B 1 23  ? -25.315 -22.328 1.793   1.00 20.74  ? 23  PRO   B CB   1 
ATOM   1981 C  CG   . PRO   B 1 23  ? -24.310 -21.955 2.876   1.00 21.09  ? 23  PRO   B CG   1 
ATOM   1982 C  CD   . PRO   B 1 23  ? -23.019 -21.647 2.145   1.00 20.28  ? 23  PRO   B CD   1 
ATOM   1983 N  N    . HIS   B 1 24  ? -25.462 -23.558 -1.449  1.00 19.92  ? 24  HIS   B N    1 
ATOM   1984 C  CA   . HIS   B 1 24  ? -25.838 -23.368 -2.873  1.00 19.12  ? 24  HIS   B CA   1 
ATOM   1985 C  C    . HIS   B 1 24  ? -27.138 -24.112 -3.210  1.00 19.49  ? 24  HIS   B C    1 
ATOM   1986 O  O    . HIS   B 1 24  ? -27.570 -24.956 -2.404  1.00 19.25  ? 24  HIS   B O    1 
ATOM   1987 C  CB   . HIS   B 1 24  ? -24.682 -23.830 -3.741  1.00 18.19  ? 24  HIS   B CB   1 
ATOM   1988 C  CG   . HIS   B 1 24  ? -24.265 -25.231 -3.463  1.00 17.71  ? 24  HIS   B CG   1 
ATOM   1989 N  ND1  . HIS   B 1 24  ? -23.648 -25.588 -2.285  1.00 18.55  ? 24  HIS   B ND1  1 
ATOM   1990 C  CD2  . HIS   B 1 24  ? -24.375 -26.356 -4.203  1.00 16.85  ? 24  HIS   B CD2  1 
ATOM   1991 C  CE1  . HIS   B 1 24  ? -23.379 -26.879 -2.314  1.00 18.43  ? 24  HIS   B CE1  1 
ATOM   1992 N  NE2  . HIS   B 1 24  ? -23.836 -27.380 -3.478  1.00 17.41  ? 24  HIS   B NE2  1 
ATOM   1993 N  N    . ILE   B 1 25  ? -27.715 -23.800 -4.378  1.00 19.94  ? 25  ILE   B N    1 
ATOM   1994 C  CA   . ILE   B 1 25  ? -28.785 -24.597 -5.050  1.00 21.26  ? 25  ILE   B CA   1 
ATOM   1995 C  C    . ILE   B 1 25  ? -28.146 -25.216 -6.293  1.00 20.95  ? 25  ILE   B C    1 
ATOM   1996 O  O    . ILE   B 1 25  ? -27.279 -24.558 -6.889  1.00 19.77  ? 25  ILE   B O    1 
ATOM   1997 C  CB   . ILE   B 1 25  ? -30.028 -23.747 -5.404  1.00 22.03  ? 25  ILE   B CB   1 
ATOM   1998 C  CG1  . ILE   B 1 25  ? -29.652 -22.553 -6.294  1.00 23.29  ? 25  ILE   B CG1  1 
ATOM   1999 C  CG2  . ILE   B 1 25  ? -30.786 -23.333 -4.145  1.00 20.84  ? 25  ILE   B CG2  1 
ATOM   2000 C  CD1  . ILE   B 1 25  ? -30.827 -21.713 -6.754  1.00 23.99  ? 25  ILE   B CD1  1 
ATOM   2001 N  N    . GLY   B 1 26  ? -28.541 -26.434 -6.663  1.00 20.38  ? 26  GLY   B N    1 
ATOM   2002 C  CA   . GLY   B 1 26  ? -27.948 -27.138 -7.817  1.00 19.54  ? 26  GLY   B CA   1 
ATOM   2003 C  C    . GLY   B 1 26  ? -28.952 -27.951 -8.612  1.00 19.43  ? 26  GLY   B C    1 
ATOM   2004 O  O    . GLY   B 1 26  ? -30.008 -28.320 -8.067  1.00 17.93  ? 26  GLY   B O    1 
ATOM   2005 N  N    . ILE   B 1 27  ? -28.602 -28.213 -9.870  1.00 19.68  ? 27  ILE   B N    1 
ATOM   2006 C  CA   . ILE   B 1 27  ? -29.314 -29.138 -10.790 1.00 20.36  ? 27  ILE   B CA   1 
ATOM   2007 C  C    . ILE   B 1 27  ? -28.415 -30.367 -10.977 1.00 19.83  ? 27  ILE   B C    1 
ATOM   2008 O  O    . ILE   B 1 27  ? -27.293 -30.246 -11.469 1.00 19.48  ? 27  ILE   B O    1 
ATOM   2009 C  CB   . ILE   B 1 27  ? -29.698 -28.430 -12.102 1.00 19.83  ? 27  ILE   B CB   1 
ATOM   2010 C  CG1  . ILE   B 1 27  ? -30.810 -27.419 -11.840 1.00 21.26  ? 27  ILE   B CG1  1 
ATOM   2011 C  CG2  . ILE   B 1 27  ? -30.083 -29.426 -13.188 1.00 19.55  ? 27  ILE   B CG2  1 
ATOM   2012 C  CD1  . ILE   B 1 27  ? -30.895 -26.361 -12.889 1.00 23.10  ? 27  ILE   B CD1  1 
ATOM   2013 N  N    . ASP   B 1 28  ? -28.927 -31.504 -10.534 1.00 21.20  ? 28  ASP   B N    1 
ATOM   2014 C  CA   . ASP   B 1 28  ? -28.255 -32.817 -10.446 1.00 21.66  ? 28  ASP   B CA   1 
ATOM   2015 C  C    . ASP   B 1 28  ? -28.859 -33.728 -11.513 1.00 20.84  ? 28  ASP   B C    1 
ATOM   2016 O  O    . ASP   B 1 28  ? -30.058 -34.007 -11.447 1.00 22.97  ? 28  ASP   B O    1 
ATOM   2017 C  CB   . ASP   B 1 28  ? -28.485 -33.385 -9.051  1.00 22.97  ? 28  ASP   B CB   1 
ATOM   2018 C  CG   . ASP   B 1 28  ? -27.834 -32.568 -7.960  1.00 23.19  ? 28  ASP   B CG   1 
ATOM   2019 O  OD1  . ASP   B 1 28  ? -27.097 -31.644 -8.319  1.00 25.23  ? 28  ASP   B OD1  1 
ATOM   2020 O  OD2  . ASP   B 1 28  ? -28.058 -32.891 -6.757  1.00 23.43  ? 28  ASP   B OD2  1 
ATOM   2021 N  N    . ILE   B 1 29  ? -28.073 -34.122 -12.498 1.00 22.37  ? 29  ILE   B N    1 
ATOM   2022 C  CA   . ILE   B 1 29  ? -28.502 -35.059 -13.566 1.00 23.39  ? 29  ILE   B CA   1 
ATOM   2023 C  C    . ILE   B 1 29  ? -27.757 -36.368 -13.314 1.00 24.45  ? 29  ILE   B C    1 
ATOM   2024 O  O    . ILE   B 1 29  ? -26.603 -36.456 -13.737 1.00 27.01  ? 29  ILE   B O    1 
ATOM   2025 C  CB   . ILE   B 1 29  ? -28.242 -34.445 -14.952 1.00 23.05  ? 29  ILE   B CB   1 
ATOM   2026 C  CG1  . ILE   B 1 29  ? -28.888 -33.070 -15.087 1.00 22.66  ? 29  ILE   B CG1  1 
ATOM   2027 C  CG2  . ILE   B 1 29  ? -28.700 -35.369 -16.069 1.00 24.42  ? 29  ILE   B CG2  1 
ATOM   2028 C  CD1  . ILE   B 1 29  ? -30.383 -33.077 -14.885 1.00 24.68  ? 29  ILE   B CD1  1 
ATOM   2029 N  N    . LYS   B 1 30  ? -28.371 -37.292 -12.565 1.00 25.03  ? 30  LYS   B N    1 
ATOM   2030 C  CA   . LYS   B 1 30  ? -27.888 -38.684 -12.317 1.00 26.86  ? 30  LYS   B CA   1 
ATOM   2031 C  C    . LYS   B 1 30  ? -26.534 -38.651 -11.601 1.00 25.01  ? 30  LYS   B C    1 
ATOM   2032 O  O    . LYS   B 1 30  ? -25.816 -39.655 -11.637 1.00 26.18  ? 30  LYS   B O    1 
ATOM   2033 C  CB   . LYS   B 1 30  ? -27.771 -39.477 -13.625 1.00 29.43  ? 30  LYS   B CB   1 
ATOM   2034 C  CG   . LYS   B 1 30  ? -29.088 -39.759 -14.328 1.00 31.91  ? 30  LYS   B CG   1 
ATOM   2035 C  CD   . LYS   B 1 30  ? -28.942 -40.176 -15.779 1.00 34.73  ? 30  LYS   B CD   1 
ATOM   2036 C  CE   . LYS   B 1 30  ? -28.015 -41.361 -15.945 1.00 39.46  ? 30  LYS   B CE   1 
ATOM   2037 N  NZ   . LYS   B 1 30  ? -28.144 -41.973 -17.288 1.00 42.94  ? 30  LYS   B NZ   1 
ATOM   2038 N  N    . SER   B 1 31  ? -26.223 -37.553 -10.924 1.00 22.96  ? 31  SER   B N    1 
ATOM   2039 C  CA   . SER   B 1 31  ? -25.000 -37.396 -10.105 1.00 21.95  ? 31  SER   B CA   1 
ATOM   2040 C  C    . SER   B 1 31  ? -25.243 -36.345 -9.026  1.00 20.93  ? 31  SER   B C    1 
ATOM   2041 O  O    . SER   B 1 31  ? -25.838 -35.295 -9.355  1.00 20.79  ? 31  SER   B O    1 
ATOM   2042 C  CB   . SER   B 1 31  ? -23.821 -37.004 -10.964 1.00 21.38  ? 31  SER   B CB   1 
ATOM   2043 O  OG   . SER   B 1 31  ? -22.698 -36.705 -10.146 1.00 22.09  ? 31  SER   B OG   1 
ATOM   2044 N  N    . VAL   B 1 32  ? -24.731 -36.594 -7.823  1.00 20.23  ? 32  VAL   B N    1 
ATOM   2045 C  CA   . VAL   B 1 32  ? -24.614 -35.571 -6.743  1.00 22.10  ? 32  VAL   B CA   1 
ATOM   2046 C  C    . VAL   B 1 32  ? -23.751 -34.375 -7.194  1.00 21.90  ? 32  VAL   B C    1 
ATOM   2047 O  O    . VAL   B 1 32  ? -23.930 -33.290 -6.606  1.00 22.19  ? 32  VAL   B O    1 
ATOM   2048 C  CB   . VAL   B 1 32  ? -24.055 -36.194 -5.453  1.00 22.61  ? 32  VAL   B CB   1 
ATOM   2049 C  CG1  . VAL   B 1 32  ? -22.540 -36.290 -5.500  1.00 22.03  ? 32  VAL   B CG1  1 
ATOM   2050 C  CG2  . VAL   B 1 32  ? -24.520 -35.434 -4.221  1.00 22.40  ? 32  VAL   B CG2  1 
ATOM   2051 N  N    . ARG   B 1 33  ? -22.835 -34.546 -8.155  1.00 22.25  ? 33  ARG   B N    1 
ATOM   2052 C  CA   . ARG   B 1 33  ? -21.926 -33.465 -8.647  1.00 23.06  ? 33  ARG   B CA   1 
ATOM   2053 C  C    . ARG   B 1 33  ? -22.708 -32.603 -9.631  1.00 21.79  ? 33  ARG   B C    1 
ATOM   2054 O  O    . ARG   B 1 33  ? -22.822 -33.014 -10.789 1.00 23.23  ? 33  ARG   B O    1 
ATOM   2055 C  CB   . ARG   B 1 33  ? -20.663 -34.015 -9.316  1.00 22.64  ? 33  ARG   B CB   1 
ATOM   2056 C  CG   . ARG   B 1 33  ? -19.768 -34.774 -8.355  1.00 24.04  ? 33  ARG   B CG   1 
ATOM   2057 C  CD   . ARG   B 1 33  ? -18.485 -35.324 -8.947  1.00 23.86  ? 33  ARG   B CD   1 
ATOM   2058 N  NE   . ARG   B 1 33  ? -17.959 -36.215 -7.926  1.00 24.88  ? 33  ARG   B NE   1 
ATOM   2059 C  CZ   . ARG   B 1 33  ? -16.768 -36.127 -7.350  1.00 23.99  ? 33  ARG   B CZ   1 
ATOM   2060 N  NH1  . ARG   B 1 33  ? -15.906 -35.186 -7.699  1.00 22.88  ? 33  ARG   B NH1  1 
ATOM   2061 N  NH2  . ARG   B 1 33  ? -16.457 -36.993 -6.406  1.00 24.44  ? 33  ARG   B NH2  1 
ATOM   2062 N  N    . SER   B 1 34  ? -23.261 -31.491 -9.150  1.00 20.53  ? 34  SER   B N    1 
ATOM   2063 C  CA   . SER   B 1 34  ? -24.283 -30.691 -9.856  1.00 21.68  ? 34  SER   B CA   1 
ATOM   2064 C  C    . SER   B 1 34  ? -23.737 -30.286 -11.228 1.00 21.87  ? 34  SER   B C    1 
ATOM   2065 O  O    . SER   B 1 34  ? -22.565 -29.881 -11.312 1.00 21.05  ? 34  SER   B O    1 
ATOM   2066 C  CB   . SER   B 1 34  ? -24.695 -29.484 -9.047  1.00 22.04  ? 34  SER   B CB   1 
ATOM   2067 O  OG   . SER   B 1 34  ? -24.962 -29.810 -7.691  1.00 22.34  ? 34  SER   B OG   1 
ATOM   2068 N  N    . LYS   B 1 35  ? -24.565 -30.369 -12.265 1.00 21.66  ? 35  LYS   B N    1 
ATOM   2069 C  CA   . LYS   B 1 35  ? -24.236 -29.824 -13.609 1.00 22.41  ? 35  LYS   B CA   1 
ATOM   2070 C  C    . LYS   B 1 35  ? -24.085 -28.303 -13.514 1.00 21.52  ? 35  LYS   B C    1 
ATOM   2071 O  O    . LYS   B 1 35  ? -23.286 -27.730 -14.245 1.00 21.82  ? 35  LYS   B O    1 
ATOM   2072 C  CB   . LYS   B 1 35  ? -25.317 -30.223 -14.618 1.00 24.67  ? 35  LYS   B CB   1 
ATOM   2073 C  CG   . LYS   B 1 35  ? -25.506 -31.725 -14.762 1.00 26.88  ? 35  LYS   B CG   1 
ATOM   2074 C  CD   . LYS   B 1 35  ? -24.216 -32.516 -14.892 1.00 29.48  ? 35  LYS   B CD   1 
ATOM   2075 C  CE   . LYS   B 1 35  ? -24.497 -34.000 -15.060 1.00 32.67  ? 35  LYS   B CE   1 
ATOM   2076 N  NZ   . LYS   B 1 35  ? -23.286 -34.854 -14.993 1.00 35.19  ? 35  LYS   B NZ   1 
ATOM   2077 N  N    . LYS   B 1 36  ? -24.814 -27.665 -12.607 1.00 22.10  ? 36  LYS   B N    1 
ATOM   2078 C  CA   . LYS   B 1 36  ? -24.804 -26.194 -12.460 1.00 21.11  ? 36  LYS   B CA   1 
ATOM   2079 C  C    . LYS   B 1 36  ? -25.231 -25.891 -11.031 1.00 20.41  ? 36  LYS   B C    1 
ATOM   2080 O  O    . LYS   B 1 36  ? -26.094 -26.640 -10.512 1.00 19.59  ? 36  LYS   B O    1 
ATOM   2081 C  CB   . LYS   B 1 36  ? -25.721 -25.589 -13.526 1.00 24.60  ? 36  LYS   B CB   1 
ATOM   2082 C  CG   . LYS   B 1 36  ? -25.414 -24.155 -13.907 1.00 28.89  ? 36  LYS   B CG   1 
ATOM   2083 C  CD   . LYS   B 1 36  ? -24.034 -23.967 -14.510 1.00 28.37  ? 36  LYS   B CD   1 
ATOM   2084 C  CE   . LYS   B 1 36  ? -23.939 -24.540 -15.899 1.00 28.31  ? 36  LYS   B CE   1 
ATOM   2085 N  NZ   . LYS   B 1 36  ? -22.749 -23.982 -16.580 1.00 30.64  ? 36  LYS   B NZ   1 
ATOM   2086 N  N    . THR   B 1 37  ? -24.599 -24.895 -10.403 1.00 19.51  ? 37  THR   B N    1 
ATOM   2087 C  CA   . THR   B 1 37  ? -24.950 -24.369 -9.061  1.00 18.84  ? 37  THR   B CA   1 
ATOM   2088 C  C    . THR   B 1 37  ? -25.002 -22.845 -9.098  1.00 17.93  ? 37  THR   B C    1 
ATOM   2089 O  O    . THR   B 1 37  ? -24.555 -22.225 -10.075 1.00 16.96  ? 37  THR   B O    1 
ATOM   2090 C  CB   . THR   B 1 37  ? -23.973 -24.837 -7.974  1.00 20.67  ? 37  THR   B CB   1 
ATOM   2091 O  OG1  . THR   B 1 37  ? -22.717 -24.194 -8.182  1.00 22.10  ? 37  THR   B OG1  1 
ATOM   2092 C  CG2  . THR   B 1 37  ? -23.777 -26.337 -7.978  1.00 21.16  ? 37  THR   B CG2  1 
ATOM   2093 N  N    . ALA   B 1 38  ? -25.571 -22.268 -8.058  1.00 17.57  ? 38  ALA   B N    1 
ATOM   2094 C  CA   . ALA   B 1 38  ? -25.604 -20.811 -7.829  1.00 19.16  ? 38  ALA   B CA   1 
ATOM   2095 C  C    . ALA   B 1 38  ? -25.563 -20.622 -6.319  1.00 19.19  ? 38  ALA   B C    1 
ATOM   2096 O  O    . ALA   B 1 38  ? -26.007 -21.537 -5.610  1.00 21.70  ? 38  ALA   B O    1 
ATOM   2097 C  CB   . ALA   B 1 38  ? -26.818 -20.196 -8.470  1.00 18.61  ? 38  ALA   B CB   1 
ATOM   2098 N  N    . LYS   B 1 39  ? -24.968 -19.532 -5.859  1.00 19.73  ? 39  LYS   B N    1 
ATOM   2099 C  CA   . LYS   B 1 39  ? -24.784 -19.233 -4.424  1.00 19.23  ? 39  LYS   B CA   1 
ATOM   2100 C  C    . LYS   B 1 39  ? -26.156 -19.034 -3.793  1.00 19.47  ? 39  LYS   B C    1 
ATOM   2101 O  O    . LYS   B 1 39  ? -27.041 -18.462 -4.435  1.00 21.73  ? 39  LYS   B O    1 
ATOM   2102 C  CB   . LYS   B 1 39  ? -23.913 -17.992 -4.254  1.00 20.19  ? 39  LYS   B CB   1 
ATOM   2103 C  CG   . LYS   B 1 39  ? -23.478 -17.709 -2.820  1.00 21.46  ? 39  LYS   B CG   1 
ATOM   2104 C  CD   . LYS   B 1 39  ? -22.253 -16.805 -2.743  1.00 23.09  ? 39  LYS   B CD   1 
ATOM   2105 C  CE   . LYS   B 1 39  ? -21.614 -16.782 -1.374  1.00 25.01  ? 39  LYS   B CE   1 
ATOM   2106 N  NZ   . LYS   B 1 39  ? -22.592 -16.379 -0.332  1.00 27.87  ? 39  LYS   B NZ   1 
ATOM   2107 N  N    . TRP   B 1 40  ? -26.316 -19.497 -2.563  1.00 20.68  ? 40  TRP   B N    1 
ATOM   2108 C  CA   . TRP   B 1 40  ? -27.602 -19.506 -1.831  1.00 20.78  ? 40  TRP   B CA   1 
ATOM   2109 C  C    . TRP   B 1 40  ? -27.366 -19.034 -0.400  1.00 20.28  ? 40  TRP   B C    1 
ATOM   2110 O  O    . TRP   B 1 40  ? -26.698 -19.726 0.371   1.00 18.38  ? 40  TRP   B O    1 
ATOM   2111 C  CB   . TRP   B 1 40  ? -28.262 -20.897 -1.885  1.00 19.70  ? 40  TRP   B CB   1 
ATOM   2112 C  CG   . TRP   B 1 40  ? -29.547 -20.966 -1.120  1.00 18.36  ? 40  TRP   B CG   1 
ATOM   2113 C  CD1  . TRP   B 1 40  ? -30.527 -20.016 -1.093  1.00 18.19  ? 40  TRP   B CD1  1 
ATOM   2114 C  CD2  . TRP   B 1 40  ? -30.007 -22.044 -0.283  1.00 18.29  ? 40  TRP   B CD2  1 
ATOM   2115 N  NE1  . TRP   B 1 40  ? -31.555 -20.419 -0.280  1.00 18.24  ? 40  TRP   B NE1  1 
ATOM   2116 C  CE2  . TRP   B 1 40  ? -31.260 -21.649 0.242   1.00 17.84  ? 40  TRP   B CE2  1 
ATOM   2117 C  CE3  . TRP   B 1 40  ? -29.489 -23.296 0.079   1.00 18.43  ? 40  TRP   B CE3  1 
ATOM   2118 C  CZ2  . TRP   B 1 40  ? -31.996 -22.465 1.091   1.00 17.88  ? 40  TRP   B CZ2  1 
ATOM   2119 C  CZ3  . TRP   B 1 40  ? -30.215 -24.102 0.931   1.00 18.38  ? 40  TRP   B CZ3  1 
ATOM   2120 C  CH2  . TRP   B 1 40  ? -31.450 -23.685 1.434   1.00 18.19  ? 40  TRP   B CH2  1 
ATOM   2121 N  N    . ASN   B 1 41  ? -27.946 -17.894 -0.070  1.00 24.59  ? 41  ASN   B N    1 
ATOM   2122 C  CA   . ASN   B 1 41  ? -27.887 -17.314 1.291   1.00 27.55  ? 41  ASN   B CA   1 
ATOM   2123 C  C    . ASN   B 1 41  ? -29.045 -17.931 2.089   1.00 28.74  ? 41  ASN   B C    1 
ATOM   2124 O  O    . ASN   B 1 41  ? -30.066 -17.252 2.279   1.00 33.26  ? 41  ASN   B O    1 
ATOM   2125 C  CB   . ASN   B 1 41  ? -27.821 -15.787 1.187   1.00 30.37  ? 41  ASN   B CB   1 
ATOM   2126 C  CG   . ASN   B 1 41  ? -26.622 -15.327 0.375   1.00 33.20  ? 41  ASN   B CG   1 
ATOM   2127 O  OD1  . ASN   B 1 41  ? -25.471 -15.556 0.762   1.00 34.31  ? 41  ASN   B OD1  1 
ATOM   2128 N  ND2  . ASN   B 1 41  ? -26.872 -14.731 -0.781  1.00 35.09  ? 41  ASN   B ND2  1 
ATOM   2129 N  N    . MET   B 1 42  ? -28.897 -19.203 2.484   1.00 27.96  ? 42  MET   B N    1 
ATOM   2130 C  CA   . MET   B 1 42  ? -29.841 -19.936 3.365   1.00 29.38  ? 42  MET   B CA   1 
ATOM   2131 C  C    . MET   B 1 42  ? -29.971 -19.123 4.655   1.00 29.30  ? 42  MET   B C    1 
ATOM   2132 O  O    . MET   B 1 42  ? -28.932 -18.667 5.147   1.00 29.06  ? 42  MET   B O    1 
ATOM   2133 C  CB   . MET   B 1 42  ? -29.324 -21.346 3.684   1.00 31.95  ? 42  MET   B CB   1 
ATOM   2134 C  CG   . MET   B 1 42  ? -30.373 -22.278 4.261   1.00 34.63  ? 42  MET   B CG   1 
ATOM   2135 S  SD   . MET   B 1 42  ? -30.787 -21.995 6.013   1.00 41.24  ? 42  MET   B SD   1 
ATOM   2136 C  CE   . MET   B 1 42  ? -29.251 -22.502 6.781   1.00 37.23  ? 42  MET   B CE   1 
ATOM   2137 N  N    . GLN   B 1 43  ? -31.193 -18.946 5.167   1.00 28.97  ? 43  GLN   B N    1 
ATOM   2138 C  CA   . GLN   B 1 43  ? -31.497 -18.135 6.377   1.00 28.40  ? 43  GLN   B CA   1 
ATOM   2139 C  C    . GLN   B 1 43  ? -32.035 -19.055 7.476   1.00 26.54  ? 43  GLN   B C    1 
ATOM   2140 O  O    . GLN   B 1 43  ? -33.167 -19.537 7.336   1.00 28.87  ? 43  GLN   B O    1 
ATOM   2141 C  CB   . GLN   B 1 43  ? -32.493 -17.026 6.030   1.00 30.33  ? 43  GLN   B CB   1 
ATOM   2142 C  CG   . GLN   B 1 43  ? -31.873 -15.906 5.209   1.00 31.57  ? 43  GLN   B CG   1 
ATOM   2143 C  CD   . GLN   B 1 43  ? -32.730 -14.664 5.201   1.00 32.77  ? 43  GLN   B CD   1 
ATOM   2144 O  OE1  . GLN   B 1 43  ? -33.211 -14.212 6.241   1.00 36.31  ? 43  GLN   B OE1  1 
ATOM   2145 N  NE2  . GLN   B 1 43  ? -32.920 -14.104 4.019   1.00 28.67  ? 43  GLN   B NE2  1 
ATOM   2146 N  N    . ASN   B 1 44  ? -31.242 -19.290 8.520   1.00 26.23  ? 44  ASN   B N    1 
ATOM   2147 C  CA   . ASN   B 1 44  ? -31.578 -20.200 9.646   1.00 27.13  ? 44  ASN   B CA   1 
ATOM   2148 C  C    . ASN   B 1 44  ? -32.908 -19.754 10.256  1.00 26.31  ? 44  ASN   B C    1 
ATOM   2149 O  O    . ASN   B 1 44  ? -33.019 -18.586 10.676  1.00 27.02  ? 44  ASN   B O    1 
ATOM   2150 C  CB   . ASN   B 1 44  ? -30.470 -20.257 10.705  1.00 27.80  ? 44  ASN   B CB   1 
ATOM   2151 C  CG   . ASN   B 1 44  ? -30.476 -21.532 11.531  1.00 29.34  ? 44  ASN   B CG   1 
ATOM   2152 O  OD1  . ASN   B 1 44  ? -31.431 -22.297 11.546  1.00 34.34  ? 44  ASN   B OD1  1 
ATOM   2153 N  ND2  . ASN   B 1 44  ? -29.392 -21.788 12.228  1.00 30.17  ? 44  ASN   B ND2  1 
ATOM   2154 N  N    . GLY   B 1 45  ? -33.893 -20.645 10.259  1.00 25.24  ? 45  GLY   B N    1 
ATOM   2155 C  CA   . GLY   B 1 45  ? -35.149 -20.465 11.007  1.00 25.61  ? 45  GLY   B CA   1 
ATOM   2156 C  C    . GLY   B 1 45  ? -36.176 -19.664 10.222  1.00 26.79  ? 45  GLY   B C    1 
ATOM   2157 O  O    . GLY   B 1 45  ? -37.267 -19.419 10.767  1.00 25.12  ? 45  GLY   B O    1 
ATOM   2158 N  N    . LYS   B 1 46  ? -35.859 -19.260 8.990   1.00 29.27  ? 46  LYS   B N    1 
ATOM   2159 C  CA   . LYS   B 1 46  ? -36.799 -18.505 8.123   1.00 29.47  ? 46  LYS   B CA   1 
ATOM   2160 C  C    . LYS   B 1 46  ? -37.493 -19.509 7.194   1.00 27.54  ? 46  LYS   B C    1 
ATOM   2161 O  O    . LYS   B 1 46  ? -36.874 -20.526 6.817   1.00 26.20  ? 46  LYS   B O    1 
ATOM   2162 C  CB   . LYS   B 1 46  ? -36.074 -17.407 7.334   1.00 33.70  ? 46  LYS   B CB   1 
ATOM   2163 C  CG   . LYS   B 1 46  ? -35.370 -16.315 8.141   1.00 37.67  ? 46  LYS   B CG   1 
ATOM   2164 C  CD   . LYS   B 1 46  ? -36.237 -15.551 9.150   1.00 42.29  ? 46  LYS   B CD   1 
ATOM   2165 C  CE   . LYS   B 1 46  ? -36.105 -16.103 10.560  1.00 48.55  ? 46  LYS   B CE   1 
ATOM   2166 N  NZ   . LYS   B 1 46  ? -37.089 -15.527 11.512  1.00 52.08  ? 46  LYS   B NZ   1 
ATOM   2167 N  N    . VAL   B 1 47  ? -38.747 -19.234 6.865   1.00 25.17  ? 47  VAL   B N    1 
ATOM   2168 C  CA   . VAL   B 1 47  ? -39.549 -20.008 5.885   1.00 23.55  ? 47  VAL   B CA   1 
ATOM   2169 C  C    . VAL   B 1 47  ? -39.145 -19.545 4.492   1.00 21.43  ? 47  VAL   B C    1 
ATOM   2170 O  O    . VAL   B 1 47  ? -39.264 -18.353 4.230   1.00 22.35  ? 47  VAL   B O    1 
ATOM   2171 C  CB   . VAL   B 1 47  ? -41.050 -19.833 6.149   1.00 24.44  ? 47  VAL   B CB   1 
ATOM   2172 C  CG1  . VAL   B 1 47  ? -41.900 -20.287 4.967   1.00 25.41  ? 47  VAL   B CG1  1 
ATOM   2173 C  CG2  . VAL   B 1 47  ? -41.433 -20.564 7.423   1.00 24.53  ? 47  VAL   B CG2  1 
ATOM   2174 N  N    . GLY   B 1 48  ? -38.636 -20.465 3.668   1.00 20.54  ? 48  GLY   B N    1 
ATOM   2175 C  CA   . GLY   B 1 48  ? -38.227 -20.205 2.275   1.00 19.67  ? 48  GLY   B CA   1 
ATOM   2176 C  C    . GLY   B 1 48  ? -39.235 -20.769 1.288   1.00 19.62  ? 48  GLY   B C    1 
ATOM   2177 O  O    . GLY   B 1 48  ? -40.117 -21.543 1.725   1.00 20.52  ? 48  GLY   B O    1 
ATOM   2178 N  N    . THR   B 1 49  ? -39.114 -20.394 0.016   1.00 18.96  ? 49  THR   B N    1 
ATOM   2179 C  CA   . THR   B 1 49  ? -39.931 -20.882 -1.114  1.00 19.81  ? 49  THR   B CA   1 
ATOM   2180 C  C    . THR   B 1 49  ? -38.975 -21.365 -2.191  1.00 21.34  ? 49  THR   B C    1 
ATOM   2181 O  O    . THR   B 1 49  ? -38.027 -20.626 -2.496  1.00 22.73  ? 49  THR   B O    1 
ATOM   2182 C  CB   . THR   B 1 49  ? -40.840 -19.793 -1.699  1.00 20.58  ? 49  THR   B CB   1 
ATOM   2183 O  OG1  . THR   B 1 49  ? -41.644 -19.283 -0.640  1.00 20.84  ? 49  THR   B OG1  1 
ATOM   2184 C  CG2  . THR   B 1 49  ? -41.764 -20.304 -2.787  1.00 21.21  ? 49  THR   B CG2  1 
ATOM   2185 N  N    . ALA   B 1 50  ? -39.202 -22.572 -2.713  1.00 21.69  ? 50  ALA   B N    1 
ATOM   2186 C  CA   . ALA   B 1 50  ? -38.523 -23.118 -3.907  1.00 20.48  ? 50  ALA   B CA   1 
ATOM   2187 C  C    . ALA   B 1 50  ? -39.555 -23.209 -5.041  1.00 20.32  ? 50  ALA   B C    1 
ATOM   2188 O  O    . ALA   B 1 50  ? -40.689 -23.640 -4.767  1.00 20.35  ? 50  ALA   B O    1 
ATOM   2189 C  CB   . ALA   B 1 50  ? -37.926 -24.464 -3.574  1.00 19.66  ? 50  ALA   B CB   1 
ATOM   2190 N  N    . HIS   B 1 51  ? -39.176 -22.820 -6.257  1.00 21.08  ? 51  HIS   B N    1 
ATOM   2191 C  CA   . HIS   B 1 51  ? -40.015 -22.905 -7.483  1.00 23.04  ? 51  HIS   B CA   1 
ATOM   2192 C  C    . HIS   B 1 51  ? -39.160 -23.546 -8.568  1.00 24.26  ? 51  HIS   B C    1 
ATOM   2193 O  O    . HIS   B 1 51  ? -38.041 -23.013 -8.798  1.00 24.90  ? 51  HIS   B O    1 
ATOM   2194 C  CB   . HIS   B 1 51  ? -40.566 -21.526 -7.860  1.00 24.94  ? 51  HIS   B CB   1 
ATOM   2195 C  CG   . HIS   B 1 51  ? -41.567 -21.552 -8.967  1.00 27.02  ? 51  HIS   B CG   1 
ATOM   2196 N  ND1  . HIS   B 1 51  ? -41.817 -20.449 -9.760  1.00 29.07  ? 51  HIS   B ND1  1 
ATOM   2197 C  CD2  . HIS   B 1 51  ? -42.391 -22.525 -9.417  1.00 28.35  ? 51  HIS   B CD2  1 
ATOM   2198 C  CE1  . HIS   B 1 51  ? -42.752 -20.745 -10.648 1.00 31.01  ? 51  HIS   B CE1  1 
ATOM   2199 N  NE2  . HIS   B 1 51  ? -43.104 -22.016 -10.473 1.00 27.90  ? 51  HIS   B NE2  1 
ATOM   2200 N  N    . ILE   B 1 52  ? -39.588 -24.710 -9.081  1.00 22.68  ? 52  ILE   B N    1 
ATOM   2201 C  CA   . ILE   B 1 52  ? -38.875 -25.460 -10.153 1.00 23.55  ? 52  ILE   B CA   1 
ATOM   2202 C  C    . ILE   B 1 52  ? -39.771 -25.475 -11.398 1.00 22.96  ? 52  ILE   B C    1 
ATOM   2203 O  O    . ILE   B 1 52  ? -40.977 -25.775 -11.256 1.00 21.84  ? 52  ILE   B O    1 
ATOM   2204 C  CB   . ILE   B 1 52  ? -38.470 -26.879 -9.703  1.00 23.25  ? 52  ILE   B CB   1 
ATOM   2205 C  CG1  . ILE   B 1 52  ? -37.442 -26.855 -8.566  1.00 25.20  ? 52  ILE   B CG1  1 
ATOM   2206 C  CG2  . ILE   B 1 52  ? -37.965 -27.706 -10.877 1.00 22.91  ? 52  ILE   B CG2  1 
ATOM   2207 C  CD1  . ILE   B 1 52  ? -38.019 -27.175 -7.212  1.00 25.15  ? 52  ILE   B CD1  1 
ATOM   2208 N  N    . ILE   B 1 53  ? -39.193 -25.210 -12.572 1.00 23.23  ? 53  ILE   B N    1 
ATOM   2209 C  CA   . ILE   B 1 53  ? -39.923 -25.283 -13.871 1.00 26.06  ? 53  ILE   B CA   1 
ATOM   2210 C  C    . ILE   B 1 53  ? -39.060 -26.035 -14.873 1.00 23.94  ? 53  ILE   B C    1 
ATOM   2211 O  O    . ILE   B 1 53  ? -37.850 -25.748 -14.976 1.00 21.51  ? 53  ILE   B O    1 
ATOM   2212 C  CB   . ILE   B 1 53  ? -40.350 -23.895 -14.405 1.00 28.83  ? 53  ILE   B CB   1 
ATOM   2213 C  CG1  . ILE   B 1 53  ? -39.155 -22.953 -14.590 1.00 34.34  ? 53  ILE   B CG1  1 
ATOM   2214 C  CG2  . ILE   B 1 53  ? -41.414 -23.273 -13.513 1.00 30.32  ? 53  ILE   B CG2  1 
ATOM   2215 C  CD1  . ILE   B 1 53  ? -39.517 -21.530 -15.018 1.00 36.24  ? 53  ILE   B CD1  1 
ATOM   2216 N  N    . TYR   B 1 54  ? -39.695 -26.969 -15.573 1.00 24.68  ? 54  TYR   B N    1 
ATOM   2217 C  CA   . TYR   B 1 54  ? -39.204 -27.579 -16.828 1.00 27.62  ? 54  TYR   B CA   1 
ATOM   2218 C  C    . TYR   B 1 54  ? -40.204 -27.280 -17.938 1.00 32.86  ? 54  TYR   B C    1 
ATOM   2219 O  O    . TYR   B 1 54  ? -41.356 -27.750 -17.835 1.00 31.47  ? 54  TYR   B O    1 
ATOM   2220 C  CB   . TYR   B 1 54  ? -39.025 -29.091 -16.689 1.00 26.76  ? 54  TYR   B CB   1 
ATOM   2221 C  CG   . TYR   B 1 54  ? -38.374 -29.705 -17.898 1.00 28.16  ? 54  TYR   B CG   1 
ATOM   2222 C  CD1  . TYR   B 1 54  ? -37.025 -29.512 -18.144 1.00 27.68  ? 54  TYR   B CD1  1 
ATOM   2223 C  CD2  . TYR   B 1 54  ? -39.104 -30.431 -18.822 1.00 28.27  ? 54  TYR   B CD2  1 
ATOM   2224 C  CE1  . TYR   B 1 54  ? -36.407 -30.055 -19.256 1.00 27.27  ? 54  TYR   B CE1  1 
ATOM   2225 C  CE2  . TYR   B 1 54  ? -38.498 -30.999 -19.933 1.00 29.51  ? 54  TYR   B CE2  1 
ATOM   2226 C  CZ   . TYR   B 1 54  ? -37.148 -30.793 -20.157 1.00 27.99  ? 54  TYR   B CZ   1 
ATOM   2227 O  OH   . TYR   B 1 54  ? -36.538 -31.325 -21.245 1.00 26.75  ? 54  TYR   B OH   1 
ATOM   2228 N  N    . ASN   B 1 55  ? -39.808 -26.522 -18.964 1.00 38.68  ? 55  ASN   B N    1 
ATOM   2229 C  CA   . ASN   B 1 55  ? -40.639 -26.460 -20.202 1.00 42.99  ? 55  ASN   B CA   1 
ATOM   2230 C  C    . ASN   B 1 55  ? -39.894 -27.189 -21.317 1.00 38.41  ? 55  ASN   B C    1 
ATOM   2231 O  O    . ASN   B 1 55  ? -38.678 -26.995 -21.463 1.00 39.29  ? 55  ASN   B O    1 
ATOM   2232 C  CB   . ASN   B 1 55  ? -41.103 -25.055 -20.597 1.00 47.77  ? 55  ASN   B CB   1 
ATOM   2233 C  CG   . ASN   B 1 55  ? -39.994 -24.033 -20.584 1.00 50.38  ? 55  ASN   B CG   1 
ATOM   2234 O  OD1  . ASN   B 1 55  ? -38.939 -24.267 -19.986 1.00 53.81  ? 55  ASN   B OD1  1 
ATOM   2235 N  ND2  . ASN   B 1 55  ? -40.237 -22.901 -21.225 1.00 47.87  ? 55  ASN   B ND2  1 
ATOM   2236 N  N    . SER   B 1 56  ? -40.640 -28.020 -22.035 1.00 35.54  ? 56  SER   B N    1 
ATOM   2237 C  CA   . SER   B 1 56  ? -40.197 -28.894 -23.145 1.00 35.85  ? 56  SER   B CA   1 
ATOM   2238 C  C    . SER   B 1 56  ? -39.963 -28.074 -24.424 1.00 34.24  ? 56  SER   B C    1 
ATOM   2239 O  O    . SER   B 1 56  ? -39.367 -28.631 -25.365 1.00 33.89  ? 56  SER   B O    1 
ATOM   2240 C  CB   . SER   B 1 56  ? -41.225 -29.971 -23.356 1.00 36.18  ? 56  SER   B CB   1 
ATOM   2241 O  OG   . SER   B 1 56  ? -42.515 -29.491 -22.992 1.00 33.11  ? 56  SER   B OG   1 
ATOM   2242 N  N    . VAL   B 1 57  ? -40.409 -26.813 -24.448 1.00 32.94  ? 57  VAL   B N    1 
ATOM   2243 C  CA   . VAL   B 1 57  ? -40.136 -25.851 -25.556 1.00 37.83  ? 57  VAL   B CA   1 
ATOM   2244 C  C    . VAL   B 1 57  ? -38.644 -25.479 -25.493 1.00 37.56  ? 57  VAL   B C    1 
ATOM   2245 O  O    . VAL   B 1 57  ? -37.898 -25.905 -26.386 1.00 37.57  ? 57  VAL   B O    1 
ATOM   2246 C  CB   . VAL   B 1 57  ? -41.075 -24.629 -25.475 1.00 40.72  ? 57  VAL   B CB   1 
ATOM   2247 C  CG1  . VAL   B 1 57  ? -40.671 -23.516 -26.436 1.00 41.91  ? 57  VAL   B CG1  1 
ATOM   2248 C  CG2  . VAL   B 1 57  ? -42.533 -25.027 -25.692 1.00 41.12  ? 57  VAL   B CG2  1 
ATOM   2249 N  N    . ASP   B 1 58  ? -38.221 -24.827 -24.410 1.00 37.89  ? 58  ASP   B N    1 
ATOM   2250 C  CA   . ASP   B 1 58  ? -36.809 -24.441 -24.140 1.00 42.87  ? 58  ASP   B CA   1 
ATOM   2251 C  C    . ASP   B 1 58  ? -35.904 -25.656 -23.870 1.00 41.41  ? 58  ASP   B C    1 
ATOM   2252 O  O    . ASP   B 1 58  ? -34.704 -25.518 -24.110 1.00 43.07  ? 58  ASP   B O    1 
ATOM   2253 C  CB   . ASP   B 1 58  ? -36.736 -23.478 -22.958 1.00 45.63  ? 58  ASP   B CB   1 
ATOM   2254 C  CG   . ASP   B 1 58  ? -37.544 -22.211 -23.181 1.00 51.92  ? 58  ASP   B CG   1 
ATOM   2255 O  OD1  . ASP   B 1 58  ? -37.892 -21.940 -24.360 1.00 53.24  ? 58  ASP   B OD1  1 
ATOM   2256 O  OD2  . ASP   B 1 58  ? -37.831 -21.513 -22.173 1.00 54.24  ? 58  ASP   B OD2  1 
ATOM   2257 N  N    . LYS   B 1 59  ? -36.439 -26.781 -23.378 1.00 41.50  ? 59  LYS   B N    1 
ATOM   2258 C  CA   . LYS   B 1 59  ? -35.670 -27.973 -22.913 1.00 40.86  ? 59  LYS   B CA   1 
ATOM   2259 C  C    . LYS   B 1 59  ? -34.689 -27.538 -21.811 1.00 38.55  ? 59  LYS   B C    1 
ATOM   2260 O  O    . LYS   B 1 59  ? -33.478 -27.774 -21.936 1.00 36.57  ? 59  LYS   B O    1 
ATOM   2261 C  CB   . LYS   B 1 59  ? -35.000 -28.662 -24.104 1.00 44.81  ? 59  LYS   B CB   1 
ATOM   2262 C  CG   . LYS   B 1 59  ? -35.967 -29.171 -25.166 1.00 50.36  ? 59  LYS   B CG   1 
ATOM   2263 C  CD   . LYS   B 1 59  ? -35.320 -29.434 -26.511 1.00 55.32  ? 59  LYS   B CD   1 
ATOM   2264 C  CE   . LYS   B 1 59  ? -36.311 -29.547 -27.655 1.00 60.20  ? 59  LYS   B CE   1 
ATOM   2265 N  NZ   . LYS   B 1 59  ? -37.280 -30.647 -27.440 1.00 66.12  ? 59  LYS   B NZ   1 
ATOM   2266 N  N    . ARG   B 1 60  ? -35.223 -26.934 -20.748 1.00 36.57  ? 60  ARG   B N    1 
ATOM   2267 C  CA   . ARG   B 1 60  ? -34.454 -26.190 -19.717 1.00 36.00  ? 60  ARG   B CA   1 
ATOM   2268 C  C    . ARG   B 1 60  ? -35.149 -26.323 -18.352 1.00 31.93  ? 60  ARG   B C    1 
ATOM   2269 O  O    . ARG   B 1 60  ? -36.356 -25.962 -18.254 1.00 26.05  ? 60  ARG   B O    1 
ATOM   2270 C  CB   . ARG   B 1 60  ? -34.345 -24.743 -20.186 1.00 37.73  ? 60  ARG   B CB   1 
ATOM   2271 C  CG   . ARG   B 1 60  ? -33.609 -23.787 -19.261 1.00 45.77  ? 60  ARG   B CG   1 
ATOM   2272 C  CD   . ARG   B 1 60  ? -33.584 -22.477 -20.031 1.00 52.72  ? 60  ARG   B CD   1 
ATOM   2273 N  NE   . ARG   B 1 60  ? -33.065 -21.341 -19.302 1.00 57.62  ? 60  ARG   B NE   1 
ATOM   2274 C  CZ   . ARG   B 1 60  ? -31.790 -20.957 -19.285 1.00 65.01  ? 60  ARG   B CZ   1 
ATOM   2275 N  NH1  . ARG   B 1 60  ? -31.445 -19.877 -18.598 1.00 67.70  ? 60  ARG   B NH1  1 
ATOM   2276 N  NH2  . ARG   B 1 60  ? -30.867 -21.648 -19.938 1.00 61.13  ? 60  ARG   B NH2  1 
ATOM   2277 N  N    . LEU   B 1 61  ? -34.406 -26.824 -17.354 1.00 27.61  ? 61  LEU   B N    1 
ATOM   2278 C  CA   . LEU   B 1 61  ? -34.839 -26.966 -15.941 1.00 25.59  ? 61  LEU   B CA   1 
ATOM   2279 C  C    . LEU   B 1 61  ? -34.311 -25.754 -15.173 1.00 25.01  ? 61  LEU   B C    1 
ATOM   2280 O  O    . LEU   B 1 61  ? -33.100 -25.519 -15.198 1.00 27.27  ? 61  LEU   B O    1 
ATOM   2281 C  CB   . LEU   B 1 61  ? -34.313 -28.294 -15.383 1.00 24.40  ? 61  LEU   B CB   1 
ATOM   2282 C  CG   . LEU   B 1 61  ? -34.646 -28.625 -13.926 1.00 26.44  ? 61  LEU   B CG   1 
ATOM   2283 C  CD1  . LEU   B 1 61  ? -36.150 -28.738 -13.690 1.00 27.99  ? 61  LEU   B CD1  1 
ATOM   2284 C  CD2  . LEU   B 1 61  ? -33.974 -29.921 -13.498 1.00 27.46  ? 61  LEU   B CD2  1 
ATOM   2285 N  N    . SER   B 1 62  ? -35.192 -25.034 -14.493 1.00 23.58  ? 62  SER   B N    1 
ATOM   2286 C  CA   . SER   B 1 62  ? -34.863 -23.824 -13.706 1.00 23.77  ? 62  SER   B CA   1 
ATOM   2287 C  C    . SER   B 1 62  ? -35.403 -23.976 -12.299 1.00 22.67  ? 62  SER   B C    1 
ATOM   2288 O  O    . SER   B 1 62  ? -36.441 -24.622 -12.133 1.00 24.65  ? 62  SER   B O    1 
ATOM   2289 C  CB   . SER   B 1 62  ? -35.408 -22.592 -14.345 1.00 26.32  ? 62  SER   B CB   1 
ATOM   2290 O  OG   . SER   B 1 62  ? -34.656 -22.321 -15.514 1.00 29.64  ? 62  SER   B OG   1 
ATOM   2291 N  N    . ALA   B 1 63  ? -34.701 -23.399 -11.339 1.00 21.41  ? 63  ALA   B N    1 
ATOM   2292 C  CA   . ALA   B 1 63  ? -35.082 -23.375 -9.918  1.00 21.15  ? 63  ALA   B CA   1 
ATOM   2293 C  C    . ALA   B 1 63  ? -34.831 -21.957 -9.423  1.00 22.10  ? 63  ALA   B C    1 
ATOM   2294 O  O    . ALA   B 1 63  ? -33.767 -21.418 -9.784  1.00 26.68  ? 63  ALA   B O    1 
ATOM   2295 C  CB   . ALA   B 1 63  ? -34.285 -24.391 -9.151  1.00 20.61  ? 63  ALA   B CB   1 
ATOM   2296 N  N    . VAL   B 1 64  ? -35.777 -21.384 -8.680  1.00 20.54  ? 64  VAL   B N    1 
ATOM   2297 C  CA   . VAL   B 1 64  ? -35.610 -20.101 -7.950  1.00 21.93  ? 64  VAL   B CA   1 
ATOM   2298 C  C    . VAL   B 1 64  ? -35.896 -20.415 -6.487  1.00 21.89  ? 64  VAL   B C    1 
ATOM   2299 O  O    . VAL   B 1 64  ? -36.917 -21.073 -6.210  1.00 20.67  ? 64  VAL   B O    1 
ATOM   2300 C  CB   . VAL   B 1 64  ? -36.528 -18.987 -8.493  1.00 23.17  ? 64  VAL   B CB   1 
ATOM   2301 C  CG1  . VAL   B 1 64  ? -36.309 -17.672 -7.765  1.00 23.40  ? 64  VAL   B CG1  1 
ATOM   2302 C  CG2  . VAL   B 1 64  ? -36.341 -18.807 -9.998  1.00 24.79  ? 64  VAL   B CG2  1 
ATOM   2303 N  N    . VAL   B 1 65  ? -35.010 -19.997 -5.591  1.00 20.68  ? 65  VAL   B N    1 
ATOM   2304 C  CA   . VAL   B 1 65  ? -35.234 -20.183 -4.133  1.00 21.42  ? 65  VAL   B CA   1 
ATOM   2305 C  C    . VAL   B 1 65  ? -35.201 -18.811 -3.463  1.00 20.93  ? 65  VAL   B C    1 
ATOM   2306 O  O    . VAL   B 1 65  ? -34.281 -18.072 -3.712  1.00 21.19  ? 65  VAL   B O    1 
ATOM   2307 C  CB   . VAL   B 1 65  ? -34.204 -21.168 -3.559  1.00 20.08  ? 65  VAL   B CB   1 
ATOM   2308 C  CG1  . VAL   B 1 65  ? -34.424 -21.397 -2.074  1.00 19.95  ? 65  VAL   B CG1  1 
ATOM   2309 C  CG2  . VAL   B 1 65  ? -34.251 -22.479 -4.332  1.00 21.40  ? 65  VAL   B CG2  1 
ATOM   2310 N  N    . SER   B 1 66  ? -36.177 -18.501 -2.627  1.00 24.54  ? 66  SER   B N    1 
ATOM   2311 C  CA   . SER   B 1 66  ? -36.355 -17.145 -2.054  1.00 26.53  ? 66  SER   B CA   1 
ATOM   2312 C  C    . SER   B 1 66  ? -36.807 -17.180 -0.590  1.00 27.92  ? 66  SER   B C    1 
ATOM   2313 O  O    . SER   B 1 66  ? -37.251 -18.220 -0.066  1.00 27.72  ? 66  SER   B O    1 
ATOM   2314 C  CB   . SER   B 1 66  ? -37.285 -16.315 -2.896  1.00 28.47  ? 66  SER   B CB   1 
ATOM   2315 O  OG   . SER   B 1 66  ? -38.574 -16.895 -2.991  1.00 30.33  ? 66  SER   B OG   1 
ATOM   2316 N  N    . TYR   B 1 67  ? -36.617 -16.039 0.050   1.00 28.06  ? 67  TYR   B N    1 
ATOM   2317 C  CA   . TYR   B 1 67  ? -37.118 -15.674 1.389   1.00 29.60  ? 67  TYR   B CA   1 
ATOM   2318 C  C    . TYR   B 1 67  ? -37.762 -14.298 1.236   1.00 31.60  ? 67  TYR   B C    1 
ATOM   2319 O  O    . TYR   B 1 67  ? -37.415 -13.559 0.308   1.00 26.86  ? 67  TYR   B O    1 
ATOM   2320 C  CB   . TYR   B 1 67  ? -35.954 -15.645 2.382   1.00 29.63  ? 67  TYR   B CB   1 
ATOM   2321 C  CG   . TYR   B 1 67  ? -35.318 -16.970 2.720   1.00 30.03  ? 67  TYR   B CG   1 
ATOM   2322 C  CD1  . TYR   B 1 67  ? -35.912 -17.827 3.634   1.00 32.19  ? 67  TYR   B CD1  1 
ATOM   2323 C  CD2  . TYR   B 1 67  ? -34.094 -17.350 2.188   1.00 29.08  ? 67  TYR   B CD2  1 
ATOM   2324 C  CE1  . TYR   B 1 67  ? -35.320 -19.023 4.010   1.00 29.80  ? 67  TYR   B CE1  1 
ATOM   2325 C  CE2  . TYR   B 1 67  ? -33.493 -18.545 2.555   1.00 29.41  ? 67  TYR   B CE2  1 
ATOM   2326 C  CZ   . TYR   B 1 67  ? -34.101 -19.380 3.476   1.00 27.22  ? 67  TYR   B CZ   1 
ATOM   2327 O  OH   . TYR   B 1 67  ? -33.534 -20.555 3.863   1.00 26.09  ? 67  TYR   B OH   1 
ATOM   2328 N  N    . PRO   B 1 68  ? -38.720 -13.915 2.111   1.00 34.39  ? 68  PRO   B N    1 
ATOM   2329 C  CA   . PRO   B 1 68  ? -39.337 -12.589 2.022   1.00 36.71  ? 68  PRO   B CA   1 
ATOM   2330 C  C    . PRO   B 1 68  ? -38.282 -11.482 2.204   1.00 37.14  ? 68  PRO   B C    1 
ATOM   2331 O  O    . PRO   B 1 68  ? -37.410 -11.634 3.050   1.00 38.07  ? 68  PRO   B O    1 
ATOM   2332 C  CB   . PRO   B 1 68  ? -40.399 -12.562 3.132   1.00 39.12  ? 68  PRO   B CB   1 
ATOM   2333 C  CG   . PRO   B 1 68  ? -40.133 -13.792 4.004   1.00 39.93  ? 68  PRO   B CG   1 
ATOM   2334 C  CD   . PRO   B 1 68  ? -39.231 -14.725 3.220   1.00 35.89  ? 68  PRO   B CD   1 
ATOM   2335 N  N    . ASN   B 1 69  ? -38.313 -10.455 1.348   1.00 38.31  ? 69  ASN   B N    1 
ATOM   2336 C  CA   . ASN   B 1 69  ? -37.453 -9.236  1.455   1.00 41.43  ? 69  ASN   B CA   1 
ATOM   2337 C  C    . ASN   B 1 69  ? -35.962 -9.580  1.279   1.00 42.22  ? 69  ASN   B C    1 
ATOM   2338 O  O    . ASN   B 1 69  ? -35.150 -8.930  1.947   1.00 45.84  ? 69  ASN   B O    1 
ATOM   2339 C  CB   . ASN   B 1 69  ? -37.631 -8.512  2.804   1.00 38.42  ? 69  ASN   B CB   1 
ATOM   2340 C  CG   . ASN   B 1 69  ? -39.032 -7.996  3.054   1.00 36.46  ? 69  ASN   B CG   1 
ATOM   2341 O  OD1  . ASN   B 1 69  ? -39.824 -7.830  2.119   1.00 31.93  ? 69  ASN   B OD1  1 
ATOM   2342 N  ND2  . ASN   B 1 69  ? -39.332 -7.717  4.313   1.00 39.18  ? 69  ASN   B ND2  1 
ATOM   2343 N  N    . ALA   B 1 70  ? -35.601 -10.552 0.431   1.00 43.84  ? 70  ALA   B N    1 
ATOM   2344 C  CA   . ALA   B 1 70  ? -34.199 -11.002 0.230   1.00 41.94  ? 70  ALA   B CA   1 
ATOM   2345 C  C    . ALA   B 1 70  ? -33.932 -11.334 -1.240  1.00 40.03  ? 70  ALA   B C    1 
ATOM   2346 O  O    . ALA   B 1 70  ? -34.882 -11.584 -1.996  1.00 33.71  ? 70  ALA   B O    1 
ATOM   2347 C  CB   . ALA   B 1 70  ? -33.887 -12.196 1.105   1.00 41.81  ? 70  ALA   B CB   1 
ATOM   2348 N  N    . ASP   B 1 71  ? -32.652 -11.346 -1.605  1.00 43.49  ? 71  ASP   B N    1 
ATOM   2349 C  CA   . ASP   B 1 71  ? -32.176 -11.722 -2.958  1.00 46.91  ? 71  ASP   B CA   1 
ATOM   2350 C  C    . ASP   B 1 71  ? -32.587 -13.183 -3.205  1.00 43.43  ? 71  ASP   B C    1 
ATOM   2351 O  O    . ASP   B 1 71  ? -32.462 -14.011 -2.271  1.00 39.88  ? 71  ASP   B O    1 
ATOM   2352 C  CB   . ASP   B 1 71  ? -30.665 -11.481 -3.107  1.00 54.09  ? 71  ASP   B CB   1 
ATOM   2353 C  CG   . ASP   B 1 71  ? -30.221 -10.017 -3.111  1.00 60.49  ? 71  ASP   B CG   1 
ATOM   2354 O  OD1  . ASP   B 1 71  ? -30.864 -9.192  -3.806  1.00 56.07  ? 71  ASP   B OD1  1 
ATOM   2355 O  OD2  . ASP   B 1 71  ? -29.216 -9.711  -2.428  1.00 67.83  ? 71  ASP   B OD2  1 
ATOM   2356 N  N    . SER   B 1 72  ? -33.141 -13.444 -4.392  1.00 37.88  ? 72  SER   B N    1 
ATOM   2357 C  CA   . SER   B 1 72  ? -33.426 -14.786 -4.950  1.00 36.94  ? 72  SER   B CA   1 
ATOM   2358 C  C    . SER   B 1 72  ? -32.100 -15.438 -5.339  1.00 34.76  ? 72  SER   B C    1 
ATOM   2359 O  O    . SER   B 1 72  ? -31.192 -14.690 -5.708  1.00 32.95  ? 72  SER   B O    1 
ATOM   2360 C  CB   . SER   B 1 72  ? -34.331 -14.696 -6.154  1.00 35.29  ? 72  SER   B CB   1 
ATOM   2361 O  OG   . SER   B 1 72  ? -35.679 -14.612 -5.740  1.00 37.67  ? 72  SER   B OG   1 
ATOM   2362 N  N    . ALA   B 1 73  ? -32.013 -16.768 -5.287  1.00 30.28  ? 73  ALA   B N    1 
ATOM   2363 C  CA   . ALA   B 1 73  ? -30.980 -17.555 -6.000  1.00 29.45  ? 73  ALA   B CA   1 
ATOM   2364 C  C    . ALA   B 1 73  ? -31.661 -18.335 -7.130  1.00 27.44  ? 73  ALA   B C    1 
ATOM   2365 O  O    . ALA   B 1 73  ? -32.710 -18.945 -6.870  1.00 28.31  ? 73  ALA   B O    1 
ATOM   2366 C  CB   . ALA   B 1 73  ? -30.239 -18.453 -5.042  1.00 28.45  ? 73  ALA   B CB   1 
ATOM   2367 N  N    . THR   B 1 74  ? -31.105 -18.284 -8.343  1.00 26.12  ? 74  THR   B N    1 
ATOM   2368 C  CA   . THR   B 1 74  ? -31.641 -18.989 -9.533  1.00 27.83  ? 74  THR   B CA   1 
ATOM   2369 C  C    . THR   B 1 74  ? -30.525 -19.800 -10.192 1.00 26.28  ? 74  THR   B C    1 
ATOM   2370 O  O    . THR   B 1 74  ? -29.373 -19.353 -10.227 1.00 26.13  ? 74  THR   B O    1 
ATOM   2371 C  CB   . THR   B 1 74  ? -32.359 -18.021 -10.487 1.00 30.24  ? 74  THR   B CB   1 
ATOM   2372 O  OG1  . THR   B 1 74  ? -31.412 -17.200 -11.168 1.00 34.63  ? 74  THR   B OG1  1 
ATOM   2373 C  CG2  . THR   B 1 74  ? -33.312 -17.102 -9.760  1.00 29.77  ? 74  THR   B CG2  1 
ATOM   2374 N  N    . VAL   B 1 75  ? -30.863 -20.995 -10.653 1.00 26.33  ? 75  VAL   B N    1 
ATOM   2375 C  CA   . VAL   B 1 75  ? -29.939 -21.894 -11.398 1.00 24.45  ? 75  VAL   B CA   1 
ATOM   2376 C  C    . VAL   B 1 75  ? -30.753 -22.496 -12.536 1.00 25.31  ? 75  VAL   B C    1 
ATOM   2377 O  O    . VAL   B 1 75  ? -31.952 -22.720 -12.344 1.00 24.29  ? 75  VAL   B O    1 
ATOM   2378 C  CB   . VAL   B 1 75  ? -29.330 -22.941 -10.453 1.00 24.89  ? 75  VAL   B CB   1 
ATOM   2379 C  CG1  . VAL   B 1 75  ? -30.356 -23.942 -9.944  1.00 24.03  ? 75  VAL   B CG1  1 
ATOM   2380 C  CG2  . VAL   B 1 75  ? -28.129 -23.650 -11.068 1.00 26.21  ? 75  VAL   B CG2  1 
ATOM   2381 N  N    . SER   B 1 76  ? -30.142 -22.662 -13.697 1.00 27.76  ? 76  SER   B N    1 
ATOM   2382 C  CA   . SER   B 1 76  ? -30.791 -23.221 -14.909 1.00 30.20  ? 76  SER   B CA   1 
ATOM   2383 C  C    . SER   B 1 76  ? -29.796 -24.121 -15.595 1.00 28.00  ? 76  SER   B C    1 
ATOM   2384 O  O    . SER   B 1 76  ? -28.607 -23.839 -15.495 1.00 27.49  ? 76  SER   B O    1 
ATOM   2385 C  CB   . SER   B 1 76  ? -31.247 -22.169 -15.869 1.00 31.98  ? 76  SER   B CB   1 
ATOM   2386 O  OG   . SER   B 1 76  ? -32.101 -21.266 -15.209 1.00 37.62  ? 76  SER   B OG   1 
ATOM   2387 N  N    . TYR   B 1 77  ? -30.309 -25.127 -16.287 1.00 27.98  ? 77  TYR   B N    1 
ATOM   2388 C  CA   . TYR   B 1 77  ? -29.509 -26.114 -17.034 1.00 28.43  ? 77  TYR   B CA   1 
ATOM   2389 C  C    . TYR   B 1 77  ? -30.351 -26.616 -18.191 1.00 29.93  ? 77  TYR   B C    1 
ATOM   2390 O  O    . TYR   B 1 77  ? -31.482 -27.046 -17.932 1.00 29.13  ? 77  TYR   B O    1 
ATOM   2391 C  CB   . TYR   B 1 77  ? -29.088 -27.269 -16.137 1.00 28.35  ? 77  TYR   B CB   1 
ATOM   2392 C  CG   . TYR   B 1 77  ? -28.172 -28.251 -16.813 1.00 27.88  ? 77  TYR   B CG   1 
ATOM   2393 C  CD1  . TYR   B 1 77  ? -26.951 -27.843 -17.337 1.00 28.73  ? 77  TYR   B CD1  1 
ATOM   2394 C  CD2  . TYR   B 1 77  ? -28.516 -29.587 -16.910 1.00 29.04  ? 77  TYR   B CD2  1 
ATOM   2395 C  CE1  . TYR   B 1 77  ? -26.091 -28.742 -17.944 1.00 28.76  ? 77  TYR   B CE1  1 
ATOM   2396 C  CE2  . TYR   B 1 77  ? -27.669 -30.497 -17.520 1.00 30.09  ? 77  TYR   B CE2  1 
ATOM   2397 C  CZ   . TYR   B 1 77  ? -26.452 -30.074 -18.033 1.00 28.22  ? 77  TYR   B CZ   1 
ATOM   2398 O  OH   . TYR   B 1 77  ? -25.635 -30.980 -18.637 1.00 30.27  ? 77  TYR   B OH   1 
ATOM   2399 N  N    . ASP   B 1 78  ? -29.816 -26.488 -19.404 1.00 33.17  ? 78  ASP   B N    1 
ATOM   2400 C  CA   . ASP   B 1 78  ? -30.449 -26.970 -20.653 1.00 34.74  ? 78  ASP   B CA   1 
ATOM   2401 C  C    . ASP   B 1 78  ? -30.322 -28.488 -20.639 1.00 34.06  ? 78  ASP   B C    1 
ATOM   2402 O  O    . ASP   B 1 78  ? -29.198 -28.968 -20.453 1.00 36.24  ? 78  ASP   B O    1 
ATOM   2403 C  CB   . ASP   B 1 78  ? -29.805 -26.325 -21.878 1.00 38.93  ? 78  ASP   B CB   1 
ATOM   2404 C  CG   . ASP   B 1 78  ? -29.951 -24.813 -21.915 1.00 43.54  ? 78  ASP   B CG   1 
ATOM   2405 O  OD1  . ASP   B 1 78  ? -29.424 -24.138 -20.995 1.00 48.17  ? 78  ASP   B OD1  1 
ATOM   2406 O  OD2  . ASP   B 1 78  ? -30.584 -24.319 -22.866 1.00 51.98  ? 78  ASP   B OD2  1 
ATOM   2407 N  N    . VAL   B 1 79  ? -31.435 -29.206 -20.760 1.00 31.97  ? 79  VAL   B N    1 
ATOM   2408 C  CA   . VAL   B 1 79  ? -31.438 -30.690 -20.741 1.00 33.06  ? 79  VAL   B CA   1 
ATOM   2409 C  C    . VAL   B 1 79  ? -32.707 -31.199 -21.425 1.00 32.46  ? 79  VAL   B C    1 
ATOM   2410 O  O    . VAL   B 1 79  ? -33.762 -30.573 -21.296 1.00 31.24  ? 79  VAL   B O    1 
ATOM   2411 C  CB   . VAL   B 1 79  ? -31.281 -31.224 -19.306 1.00 34.66  ? 79  VAL   B CB   1 
ATOM   2412 C  CG1  . VAL   B 1 79  ? -32.323 -30.654 -18.353 1.00 34.94  ? 79  VAL   B CG1  1 
ATOM   2413 C  CG2  . VAL   B 1 79  ? -31.279 -32.744 -19.267 1.00 34.11  ? 79  VAL   B CG2  1 
ATOM   2414 N  N    . ASP   B 1 80  ? -32.565 -32.301 -22.148 1.00 36.40  ? 80  ASP   B N    1 
ATOM   2415 C  CA   . ASP   B 1 80  ? -33.668 -33.029 -22.827 1.00 39.64  ? 80  ASP   B CA   1 
ATOM   2416 C  C    . ASP   B 1 80  ? -33.985 -34.255 -21.964 1.00 35.24  ? 80  ASP   B C    1 
ATOM   2417 O  O    . ASP   B 1 80  ? -33.216 -35.216 -22.012 1.00 40.48  ? 80  ASP   B O    1 
ATOM   2418 C  CB   . ASP   B 1 80  ? -33.263 -33.360 -24.268 1.00 43.22  ? 80  ASP   B CB   1 
ATOM   2419 C  CG   . ASP   B 1 80  ? -34.332 -33.076 -25.311 1.00 49.76  ? 80  ASP   B CG   1 
ATOM   2420 O  OD1  . ASP   B 1 80  ? -35.483 -33.544 -25.124 1.00 55.16  ? 80  ASP   B OD1  1 
ATOM   2421 O  OD2  . ASP   B 1 80  ? -34.006 -32.390 -26.310 1.00 54.44  ? 80  ASP   B OD2  1 
ATOM   2422 N  N    . LEU   B 1 81  ? -35.068 -34.205 -21.187 1.00 35.82  ? 81  LEU   B N    1 
ATOM   2423 C  CA   . LEU   B 1 81  ? -35.352 -35.146 -20.071 1.00 33.97  ? 81  LEU   B CA   1 
ATOM   2424 C  C    . LEU   B 1 81  ? -35.804 -36.498 -20.626 1.00 32.53  ? 81  LEU   B C    1 
ATOM   2425 O  O    . LEU   B 1 81  ? -35.729 -37.495 -19.869 1.00 30.44  ? 81  LEU   B O    1 
ATOM   2426 C  CB   . LEU   B 1 81  ? -36.406 -34.545 -19.134 1.00 36.19  ? 81  LEU   B CB   1 
ATOM   2427 C  CG   . LEU   B 1 81  ? -35.905 -33.536 -18.097 1.00 38.36  ? 81  LEU   B CG   1 
ATOM   2428 C  CD1  . LEU   B 1 81  ? -37.067 -33.008 -17.265 1.00 39.88  ? 81  LEU   B CD1  1 
ATOM   2429 C  CD2  . LEU   B 1 81  ? -34.841 -34.129 -17.180 1.00 38.96  ? 81  LEU   B CD2  1 
ATOM   2430 N  N    . ASP   B 1 82  ? -36.225 -36.554 -21.891 1.00 34.14  ? 82  ASP   B N    1 
ATOM   2431 C  CA   . ASP   B 1 82  ? -36.505 -37.844 -22.581 1.00 37.32  ? 82  ASP   B CA   1 
ATOM   2432 C  C    . ASP   B 1 82  ? -35.214 -38.652 -22.755 1.00 37.62  ? 82  ASP   B C    1 
ATOM   2433 O  O    . ASP   B 1 82  ? -35.320 -39.894 -22.779 1.00 39.35  ? 82  ASP   B O    1 
ATOM   2434 C  CB   . ASP   B 1 82  ? -37.198 -37.634 -23.923 1.00 42.86  ? 82  ASP   B CB   1 
ATOM   2435 C  CG   . ASP   B 1 82  ? -36.418 -36.745 -24.870 1.00 44.82  ? 82  ASP   B CG   1 
ATOM   2436 O  OD1  . ASP   B 1 82  ? -36.107 -35.595 -24.471 1.00 46.90  ? 82  ASP   B OD1  1 
ATOM   2437 O  OD2  . ASP   B 1 82  ? -36.103 -37.221 -25.976 1.00 46.49  ? 82  ASP   B OD2  1 
ATOM   2438 N  N    . ASN   B 1 83  ? -34.049 -37.992 -22.845 1.00 38.69  ? 83  ASN   B N    1 
ATOM   2439 C  CA   . ASN   B 1 83  ? -32.725 -38.653 -23.011 1.00 40.04  ? 83  ASN   B CA   1 
ATOM   2440 C  C    . ASN   B 1 83  ? -32.157 -39.032 -21.636 1.00 39.77  ? 83  ASN   B C    1 
ATOM   2441 O  O    . ASN   B 1 83  ? -31.031 -39.567 -21.592 1.00 37.53  ? 83  ASN   B O    1 
ATOM   2442 C  CB   . ASN   B 1 83  ? -31.702 -37.777 -23.745 1.00 43.23  ? 83  ASN   B CB   1 
ATOM   2443 C  CG   . ASN   B 1 83  ? -32.142 -37.335 -25.126 1.00 47.44  ? 83  ASN   B CG   1 
ATOM   2444 O  OD1  . ASN   B 1 83  ? -31.798 -36.245 -25.572 1.00 45.42  ? 83  ASN   B OD1  1 
ATOM   2445 N  ND2  . ASN   B 1 83  ? -32.906 -38.169 -25.809 1.00 52.66  ? 83  ASN   B ND2  1 
ATOM   2446 N  N    . VAL   B 1 84  ? -32.882 -38.764 -20.546 1.00 37.49  ? 84  VAL   B N    1 
ATOM   2447 C  CA   . VAL   B 1 84  ? -32.351 -38.955 -19.163 1.00 38.58  ? 84  VAL   B CA   1 
ATOM   2448 C  C    . VAL   B 1 84  ? -33.268 -39.896 -18.372 1.00 35.18  ? 84  VAL   B C    1 
ATOM   2449 O  O    . VAL   B 1 84  ? -32.779 -40.907 -17.838 1.00 38.72  ? 84  VAL   B O    1 
ATOM   2450 C  CB   . VAL   B 1 84  ? -32.192 -37.603 -18.444 1.00 37.90  ? 84  VAL   B CB   1 
ATOM   2451 C  CG1  . VAL   B 1 84  ? -31.610 -37.795 -17.058 1.00 39.20  ? 84  VAL   B CG1  1 
ATOM   2452 C  CG2  . VAL   B 1 84  ? -31.356 -36.617 -19.247 1.00 39.66  ? 84  VAL   B CG2  1 
ATOM   2453 N  N    . LEU   B 1 85  ? -34.539 -39.533 -18.256 1.00 33.58  ? 85  LEU   B N    1 
ATOM   2454 C  CA   . LEU   B 1 85  ? -35.519 -40.218 -17.378 1.00 32.20  ? 85  LEU   B CA   1 
ATOM   2455 C  C    . LEU   B 1 85  ? -36.287 -41.267 -18.170 1.00 30.42  ? 85  LEU   B C    1 
ATOM   2456 O  O    . LEU   B 1 85  ? -36.427 -41.168 -19.387 1.00 32.70  ? 85  LEU   B O    1 
ATOM   2457 C  CB   . LEU   B 1 85  ? -36.473 -39.172 -16.801 1.00 31.05  ? 85  LEU   B CB   1 
ATOM   2458 C  CG   . LEU   B 1 85  ? -35.901 -38.316 -15.675 1.00 29.07  ? 85  LEU   B CG   1 
ATOM   2459 C  CD1  . LEU   B 1 85  ? -36.838 -37.164 -15.342 1.00 29.71  ? 85  LEU   B CD1  1 
ATOM   2460 C  CD2  . LEU   B 1 85  ? -35.655 -39.160 -14.446 1.00 29.53  ? 85  LEU   B CD2  1 
ATOM   2461 N  N    . PRO   B 1 86  ? -36.836 -42.292 -17.493 1.00 28.03  ? 86  PRO   B N    1 
ATOM   2462 C  CA   . PRO   B 1 86  ? -37.779 -43.199 -18.133 1.00 27.86  ? 86  PRO   B CA   1 
ATOM   2463 C  C    . PRO   B 1 86  ? -39.094 -42.442 -18.382 1.00 29.04  ? 86  PRO   B C    1 
ATOM   2464 O  O    . PRO   B 1 86  ? -39.289 -41.367 -17.836 1.00 30.81  ? 86  PRO   B O    1 
ATOM   2465 C  CB   . PRO   B 1 86  ? -37.937 -44.369 -17.152 1.00 26.04  ? 86  PRO   B CB   1 
ATOM   2466 C  CG   . PRO   B 1 86  ? -37.474 -43.836 -15.818 1.00 26.22  ? 86  PRO   B CG   1 
ATOM   2467 C  CD   . PRO   B 1 86  ? -36.624 -42.604 -16.076 1.00 26.95  ? 86  PRO   B CD   1 
ATOM   2468 N  N    . GLU   B 1 87  ? -39.936 -43.007 -19.241 1.00 29.67  ? 87  GLU   B N    1 
ATOM   2469 C  CA   . GLU   B 1 87  ? -41.206 -42.417 -19.723 1.00 28.02  ? 87  GLU   B CA   1 
ATOM   2470 C  C    . GLU   B 1 87  ? -42.133 -42.146 -18.528 1.00 24.38  ? 87  GLU   B C    1 
ATOM   2471 O  O    . GLU   B 1 87  ? -42.811 -41.085 -18.524 1.00 22.53  ? 87  GLU   B O    1 
ATOM   2472 C  CB   . GLU   B 1 87  ? -41.779 -43.373 -20.766 1.00 33.00  ? 87  GLU   B CB   1 
ATOM   2473 C  CG   . GLU   B 1 87  ? -42.943 -42.784 -21.525 1.00 41.88  ? 87  GLU   B CG   1 
ATOM   2474 C  CD   . GLU   B 1 87  ? -43.544 -43.674 -22.607 1.00 46.34  ? 87  GLU   B CD   1 
ATOM   2475 O  OE1  . GLU   B 1 87  ? -42.827 -44.590 -23.098 1.00 47.75  ? 87  GLU   B OE1  1 
ATOM   2476 O  OE2  . GLU   B 1 87  ? -44.722 -43.430 -22.967 1.00 46.17  ? 87  GLU   B OE2  1 
ATOM   2477 N  N    . TRP   B 1 88  ? -42.140 -43.036 -17.531 1.00 23.83  ? 88  TRP   B N    1 
ATOM   2478 C  CA   . TRP   B 1 88  ? -42.933 -42.904 -16.278 1.00 23.30  ? 88  TRP   B CA   1 
ATOM   2479 C  C    . TRP   B 1 88  ? -42.002 -42.704 -15.073 1.00 22.99  ? 88  TRP   B C    1 
ATOM   2480 O  O    . TRP   B 1 88  ? -40.981 -43.426 -14.955 1.00 25.06  ? 88  TRP   B O    1 
ATOM   2481 C  CB   . TRP   B 1 88  ? -43.851 -44.116 -16.085 1.00 23.27  ? 88  TRP   B CB   1 
ATOM   2482 C  CG   . TRP   B 1 88  ? -44.990 -44.165 -17.053 1.00 24.36  ? 88  TRP   B CG   1 
ATOM   2483 C  CD1  . TRP   B 1 88  ? -45.009 -44.756 -18.289 1.00 24.61  ? 88  TRP   B CD1  1 
ATOM   2484 C  CD2  . TRP   B 1 88  ? -46.289 -43.571 -16.866 1.00 25.45  ? 88  TRP   B CD2  1 
ATOM   2485 N  NE1  . TRP   B 1 88  ? -46.227 -44.559 -18.884 1.00 24.36  ? 88  TRP   B NE1  1 
ATOM   2486 C  CE2  . TRP   B 1 88  ? -47.035 -43.840 -18.035 1.00 24.85  ? 88  TRP   B CE2  1 
ATOM   2487 C  CE3  . TRP   B 1 88  ? -46.893 -42.855 -15.821 1.00 24.80  ? 88  TRP   B CE3  1 
ATOM   2488 C  CZ2  . TRP   B 1 88  ? -48.356 -43.413 -18.182 1.00 24.36  ? 88  TRP   B CZ2  1 
ATOM   2489 C  CZ3  . TRP   B 1 88  ? -48.193 -42.426 -15.978 1.00 24.93  ? 88  TRP   B CZ3  1 
ATOM   2490 C  CH2  . TRP   B 1 88  ? -48.918 -42.720 -17.133 1.00 24.11  ? 88  TRP   B CH2  1 
ATOM   2491 N  N    . VAL   B 1 89  ? -42.383 -41.805 -14.170 1.00 20.83  ? 89  VAL   B N    1 
ATOM   2492 C  CA   . VAL   B 1 89  ? -41.548 -41.384 -13.016 1.00 20.07  ? 89  VAL   B CA   1 
ATOM   2493 C  C    . VAL   B 1 89  ? -42.453 -41.203 -11.805 1.00 20.55  ? 89  VAL   B C    1 
ATOM   2494 O  O    . VAL   B 1 89  ? -43.660 -41.057 -11.992 1.00 20.79  ? 89  VAL   B O    1 
ATOM   2495 C  CB   . VAL   B 1 89  ? -40.786 -40.078 -13.313 1.00 19.92  ? 89  VAL   B CB   1 
ATOM   2496 C  CG1  . VAL   B 1 89  ? -39.859 -40.255 -14.506 1.00 19.48  ? 89  VAL   B CG1  1 
ATOM   2497 C  CG2  . VAL   B 1 89  ? -41.713 -38.862 -13.504 1.00 18.98  ? 89  VAL   B CG2  1 
ATOM   2498 N  N    . ARG   B 1 90  ? -41.854 -41.176 -10.617 1.00 20.90  ? 90  ARG   B N    1 
ATOM   2499 C  CA   . ARG   B 1 90  ? -42.450 -40.567 -9.405  1.00 19.93  ? 90  ARG   B CA   1 
ATOM   2500 C  C    . ARG   B 1 90  ? -41.678 -39.290 -9.072  1.00 20.10  ? 90  ARG   B C    1 
ATOM   2501 O  O    . ARG   B 1 90  ? -40.485 -39.212 -9.404  1.00 20.11  ? 90  ARG   B O    1 
ATOM   2502 C  CB   . ARG   B 1 90  ? -42.472 -41.585 -8.273  1.00 20.22  ? 90  ARG   B CB   1 
ATOM   2503 C  CG   . ARG   B 1 90  ? -43.650 -42.548 -8.363  1.00 21.10  ? 90  ARG   B CG   1 
ATOM   2504 C  CD   . ARG   B 1 90  ? -43.934 -43.198 -7.017  1.00 23.00  ? 90  ARG   B CD   1 
ATOM   2505 N  NE   . ARG   B 1 90  ? -45.173 -43.972 -6.966  1.00 23.15  ? 90  ARG   B NE   1 
ATOM   2506 C  CZ   . ARG   B 1 90  ? -45.252 -45.307 -6.948  1.00 23.73  ? 90  ARG   B CZ   1 
ATOM   2507 N  NH1  . ARG   B 1 90  ? -44.163 -46.056 -6.999  1.00 23.27  ? 90  ARG   B NH1  1 
ATOM   2508 N  NH2  . ARG   B 1 90  ? -46.434 -45.888 -6.849  1.00 23.79  ? 90  ARG   B NH2  1 
ATOM   2509 N  N    . VAL   B 1 91  ? -42.373 -38.301 -8.514  1.00 18.69  ? 91  VAL   B N    1 
ATOM   2510 C  CA   . VAL   B 1 91  ? -41.789 -37.012 -8.065  1.00 18.40  ? 91  VAL   B CA   1 
ATOM   2511 C  C    . VAL   B 1 91  ? -41.745 -37.074 -6.546  1.00 17.27  ? 91  VAL   B C    1 
ATOM   2512 O  O    . VAL   B 1 91  ? -42.677 -37.640 -5.952  1.00 16.40  ? 91  VAL   B O    1 
ATOM   2513 C  CB   . VAL   B 1 91  ? -42.558 -35.775 -8.570  1.00 19.28  ? 91  VAL   B CB   1 
ATOM   2514 C  CG1  . VAL   B 1 91  ? -42.307 -35.549 -10.054 1.00 21.12  ? 91  VAL   B CG1  1 
ATOM   2515 C  CG2  . VAL   B 1 91  ? -44.059 -35.826 -8.281  1.00 19.38  ? 91  VAL   B CG2  1 
ATOM   2516 N  N    . GLY   B 1 92  ? -40.706 -36.500 -5.954  1.00 16.55  ? 92  GLY   B N    1 
ATOM   2517 C  CA   . GLY   B 1 92  ? -40.526 -36.519 -4.496  1.00 16.15  ? 92  GLY   B CA   1 
ATOM   2518 C  C    . GLY   B 1 92  ? -39.771 -35.322 -3.958  1.00 15.45  ? 92  GLY   B C    1 
ATOM   2519 O  O    . GLY   B 1 92  ? -39.266 -34.516 -4.734  1.00 14.96  ? 92  GLY   B O    1 
ATOM   2520 N  N    . LEU   B 1 93  ? -39.763 -35.230 -2.634  1.00 16.28  ? 93  LEU   B N    1 
ATOM   2521 C  CA   . LEU   B 1 93  ? -38.864 -34.404 -1.800  1.00 17.67  ? 93  LEU   B CA   1 
ATOM   2522 C  C    . LEU   B 1 93  ? -37.993 -35.355 -0.967  1.00 19.57  ? 93  LEU   B C    1 
ATOM   2523 O  O    . LEU   B 1 93  ? -38.555 -36.321 -0.409  1.00 21.18  ? 93  LEU   B O    1 
ATOM   2524 C  CB   . LEU   B 1 93  ? -39.717 -33.521 -0.882  1.00 18.57  ? 93  LEU   B CB   1 
ATOM   2525 C  CG   . LEU   B 1 93  ? -40.724 -32.610 -1.574  1.00 17.07  ? 93  LEU   B CG   1 
ATOM   2526 C  CD1  . LEU   B 1 93  ? -41.539 -31.865 -0.545  1.00 17.58  ? 93  LEU   B CD1  1 
ATOM   2527 C  CD2  . LEU   B 1 93  ? -40.004 -31.645 -2.477  1.00 17.87  ? 93  LEU   B CD2  1 
ATOM   2528 N  N    . SER   B 1 94  ? -36.695 -35.072 -0.859  1.00 19.13  ? 94  SER   B N    1 
ATOM   2529 C  CA   . SER   B 1 94  ? -35.715 -35.840 -0.056  1.00 18.37  ? 94  SER   B CA   1 
ATOM   2530 C  C    . SER   B 1 94  ? -34.909 -34.888 0.839   1.00 17.03  ? 94  SER   B C    1 
ATOM   2531 O  O    . SER   B 1 94  ? -34.747 -33.735 0.485   1.00 17.90  ? 94  SER   B O    1 
ATOM   2532 C  CB   . SER   B 1 94  ? -34.830 -36.625 -0.972  1.00 18.77  ? 94  SER   B CB   1 
ATOM   2533 O  OG   . SER   B 1 94  ? -33.904 -37.386 -0.228  1.00 19.40  ? 94  SER   B OG   1 
ATOM   2534 N  N    . ALA   B 1 95  ? -34.431 -35.347 1.987   1.00 17.56  ? 95  ALA   B N    1 
ATOM   2535 C  CA   . ALA   B 1 95  ? -33.565 -34.552 2.887   1.00 17.01  ? 95  ALA   B CA   1 
ATOM   2536 C  C    . ALA   B 1 95  ? -32.658 -35.487 3.685   1.00 16.71  ? 95  ALA   B C    1 
ATOM   2537 O  O    . ALA   B 1 95  ? -32.989 -36.682 3.814   1.00 15.80  ? 95  ALA   B O    1 
ATOM   2538 C  CB   . ALA   B 1 95  ? -34.403 -33.670 3.780   1.00 17.05  ? 95  ALA   B CB   1 
ATOM   2539 N  N    . SER   B 1 96  ? -31.553 -34.940 4.184   1.00 16.46  ? 96  SER   B N    1 
ATOM   2540 C  CA   . SER   B 1 96  ? -30.540 -35.660 4.982   1.00 17.65  ? 96  SER   B CA   1 
ATOM   2541 C  C    . SER   B 1 96  ? -29.818 -34.746 5.979   1.00 17.44  ? 96  SER   B C    1 
ATOM   2542 O  O    . SER   B 1 96  ? -29.822 -33.518 5.832   1.00 17.14  ? 96  SER   B O    1 
ATOM   2543 C  CB   . SER   B 1 96  ? -29.561 -36.331 4.089   1.00 18.80  ? 96  SER   B CB   1 
ATOM   2544 O  OG   . SER   B 1 96  ? -28.885 -35.368 3.295   1.00 21.73  ? 96  SER   B OG   1 
ATOM   2545 N  N    . THR   B 1 97  ? -29.237 -35.381 6.987   1.00 18.41  ? 97  THR   B N    1 
ATOM   2546 C  CA   . THR   B 1 97  ? -28.281 -34.819 7.963   1.00 18.12  ? 97  THR   B CA   1 
ATOM   2547 C  C    . THR   B 1 97  ? -27.145 -35.830 8.094   1.00 18.67  ? 97  THR   B C    1 
ATOM   2548 O  O    . THR   B 1 97  ? -27.327 -37.000 7.686   1.00 18.35  ? 97  THR   B O    1 
ATOM   2549 C  CB   . THR   B 1 97  ? -28.952 -34.561 9.317   1.00 18.21  ? 97  THR   B CB   1 
ATOM   2550 O  OG1  . THR   B 1 97  ? -29.382 -35.824 9.815   1.00 15.61  ? 97  THR   B OG1  1 
ATOM   2551 C  CG2  . THR   B 1 97  ? -30.131 -33.612 9.238   1.00 17.80  ? 97  THR   B CG2  1 
ATOM   2552 N  N    . GLY   B 1 98  ? -26.020 -35.390 8.640   1.00 19.21  ? 98  GLY   B N    1 
ATOM   2553 C  CA   . GLY   B 1 98  ? -24.779 -36.180 8.722   1.00 20.36  ? 98  GLY   B CA   1 
ATOM   2554 C  C    . GLY   B 1 98  ? -24.223 -36.065 10.116  1.00 20.47  ? 98  GLY   B C    1 
ATOM   2555 O  O    . GLY   B 1 98  ? -24.994 -36.215 11.038  1.00 21.08  ? 98  GLY   B O    1 
ATOM   2556 N  N    . LEU   B 1 99  ? -22.950 -35.728 10.256  1.00 22.74  ? 99  LEU   B N    1 
ATOM   2557 C  CA   . LEU   B 1 99  ? -22.404 -35.223 11.538  1.00 23.53  ? 99  LEU   B CA   1 
ATOM   2558 C  C    . LEU   B 1 99  ? -23.163 -33.957 11.933  1.00 23.43  ? 99  LEU   B C    1 
ATOM   2559 O  O    . LEU   B 1 99  ? -23.471 -33.789 13.112  1.00 25.49  ? 99  LEU   B O    1 
ATOM   2560 C  CB   . LEU   B 1 99  ? -20.910 -34.948 11.362  1.00 25.87  ? 99  LEU   B CB   1 
ATOM   2561 C  CG   . LEU   B 1 99  ? -20.186 -34.479 12.624  1.00 26.72  ? 99  LEU   B CG   1 
ATOM   2562 C  CD1  . LEU   B 1 99  ? -20.496 -35.397 13.808  1.00 24.62  ? 99  LEU   B CD1  1 
ATOM   2563 C  CD2  . LEU   B 1 99  ? -18.676 -34.392 12.362  1.00 28.45  ? 99  LEU   B CD2  1 
ATOM   2564 N  N    . TYR   B 1 100 ? -23.442 -33.084 10.974  1.00 24.72  ? 100 TYR   B N    1 
ATOM   2565 C  CA   . TYR   B 1 100 ? -24.164 -31.809 11.210  1.00 27.82  ? 100 TYR   B CA   1 
ATOM   2566 C  C    . TYR   B 1 100 ? -25.623 -32.014 10.792  1.00 26.56  ? 100 TYR   B C    1 
ATOM   2567 O  O    . TYR   B 1 100 ? -25.915 -32.929 9.999   1.00 23.82  ? 100 TYR   B O    1 
ATOM   2568 C  CB   . TYR   B 1 100 ? -23.461 -30.658 10.488  1.00 31.21  ? 100 TYR   B CB   1 
ATOM   2569 C  CG   . TYR   B 1 100 ? -22.117 -30.278 11.064  1.00 36.28  ? 100 TYR   B CG   1 
ATOM   2570 C  CD1  . TYR   B 1 100 ? -20.961 -30.957 10.714  1.00 43.05  ? 100 TYR   B CD1  1 
ATOM   2571 C  CD2  . TYR   B 1 100 ? -21.993 -29.227 11.958  1.00 44.47  ? 100 TYR   B CD2  1 
ATOM   2572 C  CE1  . TYR   B 1 100 ? -19.720 -30.609 11.232  1.00 46.37  ? 100 TYR   B CE1  1 
ATOM   2573 C  CE2  . TYR   B 1 100 ? -20.764 -28.858 12.483  1.00 50.92  ? 100 TYR   B CE2  1 
ATOM   2574 C  CZ   . TYR   B 1 100 ? -19.621 -29.553 12.121  1.00 51.81  ? 100 TYR   B CZ   1 
ATOM   2575 O  OH   . TYR   B 1 100 ? -18.409 -29.188 12.638  1.00 55.71  ? 100 TYR   B OH   1 
ATOM   2576 N  N    . LYS   B 1 101 ? -26.506 -31.165 11.304  1.00 25.87  ? 101 LYS   B N    1 
ATOM   2577 C  CA   . LYS   B 1 101 ? -27.949 -31.458 11.458  1.00 25.75  ? 101 LYS   B CA   1 
ATOM   2578 C  C    . LYS   B 1 101 ? -28.757 -30.167 11.251  1.00 24.63  ? 101 LYS   B C    1 
ATOM   2579 O  O    . LYS   B 1 101 ? -28.264 -29.052 11.555  1.00 23.63  ? 101 LYS   B O    1 
ATOM   2580 C  CB   . LYS   B 1 101 ? -28.197 -32.120 12.824  1.00 27.95  ? 101 LYS   B CB   1 
ATOM   2581 C  CG   . LYS   B 1 101 ? -27.634 -31.365 14.027  1.00 33.74  ? 101 LYS   B CG   1 
ATOM   2582 C  CD   . LYS   B 1 101 ? -27.635 -32.103 15.367  1.00 34.42  ? 101 LYS   B CD   1 
ATOM   2583 C  CE   . LYS   B 1 101 ? -26.348 -32.836 15.685  1.00 36.66  ? 101 LYS   B CE   1 
ATOM   2584 N  NZ   . LYS   B 1 101 ? -25.272 -31.912 16.110  1.00 36.94  ? 101 LYS   B NZ   1 
ATOM   2585 N  N    . GLU   B 1 102 ? -29.959 -30.330 10.706  1.00 22.26  ? 102 GLU   B N    1 
ATOM   2586 C  CA   . GLU   B 1 102 ? -30.984 -29.276 10.560  1.00 21.30  ? 102 GLU   B CA   1 
ATOM   2587 C  C    . GLU   B 1 102 ? -32.349 -29.974 10.585  1.00 20.44  ? 102 GLU   B C    1 
ATOM   2588 O  O    . GLU   B 1 102 ? -32.418 -31.176 10.265  1.00 18.49  ? 102 GLU   B O    1 
ATOM   2589 C  CB   . GLU   B 1 102 ? -30.740 -28.487 9.265   1.00 21.66  ? 102 GLU   B CB   1 
ATOM   2590 C  CG   . GLU   B 1 102 ? -31.060 -29.269 7.988   1.00 21.62  ? 102 GLU   B CG   1 
ATOM   2591 C  CD   . GLU   B 1 102 ? -30.412 -28.809 6.689   1.00 22.86  ? 102 GLU   B CD   1 
ATOM   2592 O  OE1  . GLU   B 1 102 ? -29.366 -28.109 6.753   1.00 25.19  ? 102 GLU   B OE1  1 
ATOM   2593 O  OE2  . GLU   B 1 102 ? -30.923 -29.178 5.589   1.00 22.31  ? 102 GLU   B OE2  1 
ATOM   2594 N  N    . THR   B 1 103 ? -33.393 -29.245 10.957  1.00 20.33  ? 103 THR   B N    1 
ATOM   2595 C  CA   . THR   B 1 103 ? -34.795 -29.625 10.652  1.00 20.56  ? 103 THR   B CA   1 
ATOM   2596 C  C    . THR   B 1 103 ? -34.972 -29.494 9.137   1.00 19.92  ? 103 THR   B C    1 
ATOM   2597 O  O    . THR   B 1 103 ? -34.454 -28.482 8.572   1.00 21.20  ? 103 THR   B O    1 
ATOM   2598 C  CB   . THR   B 1 103 ? -35.807 -28.743 11.402  1.00 20.35  ? 103 THR   B CB   1 
ATOM   2599 O  OG1  . THR   B 1 103 ? -35.597 -27.400 10.965  1.00 20.79  ? 103 THR   B OG1  1 
ATOM   2600 C  CG2  . THR   B 1 103 ? -35.670 -28.821 12.903  1.00 19.50  ? 103 THR   B CG2  1 
ATOM   2601 N  N    . ASN   B 1 104 ? -35.634 -30.462 8.498   1.00 17.62  ? 104 ASN   B N    1 
ATOM   2602 C  CA   . ASN   B 1 104 ? -35.958 -30.393 7.050   1.00 17.89  ? 104 ASN   B CA   1 
ATOM   2603 C  C    . ASN   B 1 104 ? -37.486 -30.433 6.927   1.00 20.01  ? 104 ASN   B C    1 
ATOM   2604 O  O    . ASN   B 1 104 ? -38.046 -31.442 6.471   1.00 20.48  ? 104 ASN   B O    1 
ATOM   2605 C  CB   . ASN   B 1 104 ? -35.217 -31.461 6.246   1.00 17.79  ? 104 ASN   B CB   1 
ATOM   2606 C  CG   . ASN   B 1 104 ? -33.710 -31.298 6.259   1.00 17.33  ? 104 ASN   B CG   1 
ATOM   2607 O  OD1  . ASN   B 1 104 ? -32.993 -32.154 6.802   1.00 19.83  ? 104 ASN   B OD1  1 
ATOM   2608 N  ND2  . ASN   B 1 104 ? -33.224 -30.236 5.648   1.00 14.63  ? 104 ASN   B ND2  1 
ATOM   2609 N  N    . THR   B 1 105 ? -38.125 -29.341 7.336   1.00 20.59  ? 105 THR   B N    1 
ATOM   2610 C  CA   . THR   B 1 105 ? -39.585 -29.230 7.495   1.00 22.80  ? 105 THR   B CA   1 
ATOM   2611 C  C    . THR   B 1 105 ? -40.171 -28.687 6.198   1.00 22.69  ? 105 THR   B C    1 
ATOM   2612 O  O    . THR   B 1 105 ? -39.639 -27.693 5.681   1.00 21.58  ? 105 THR   B O    1 
ATOM   2613 C  CB   . THR   B 1 105 ? -39.922 -28.329 8.683   1.00 23.99  ? 105 THR   B CB   1 
ATOM   2614 O  OG1  . THR   B 1 105 ? -39.130 -28.803 9.778   1.00 25.64  ? 105 THR   B OG1  1 
ATOM   2615 C  CG2  . THR   B 1 105 ? -41.400 -28.334 9.006   1.00 24.80  ? 105 THR   B CG2  1 
ATOM   2616 N  N    . ILE   B 1 106 ? -41.199 -29.348 5.683   1.00 19.62  ? 106 ILE   B N    1 
ATOM   2617 C  CA   . ILE   B 1 106 ? -41.891 -28.918 4.441   1.00 19.47  ? 106 ILE   B CA   1 
ATOM   2618 C  C    . ILE   B 1 106 ? -43.314 -28.488 4.833   1.00 18.43  ? 106 ILE   B C    1 
ATOM   2619 O  O    . ILE   B 1 106 ? -44.063 -29.318 5.375   1.00 17.03  ? 106 ILE   B O    1 
ATOM   2620 C  CB   . ILE   B 1 106 ? -41.872 -30.057 3.410   1.00 18.92  ? 106 ILE   B CB   1 
ATOM   2621 C  CG1  . ILE   B 1 106 ? -40.454 -30.569 3.153   1.00 18.71  ? 106 ILE   B CG1  1 
ATOM   2622 C  CG2  . ILE   B 1 106 ? -42.583 -29.637 2.136   1.00 18.69  ? 106 ILE   B CG2  1 
ATOM   2623 C  CD1  . ILE   B 1 106 ? -39.650 -29.722 2.196   1.00 18.59  ? 106 ILE   B CD1  1 
ATOM   2624 N  N    . LEU   B 1 107 ? -43.649 -27.219 4.608   1.00 18.22  ? 107 LEU   B N    1 
ATOM   2625 C  CA   . LEU   B 1 107 ? -44.919 -26.611 5.068   1.00 19.01  ? 107 LEU   B CA   1 
ATOM   2626 C  C    . LEU   B 1 107 ? -45.978 -26.768 3.983   1.00 19.11  ? 107 LEU   B C    1 
ATOM   2627 O  O    . LEU   B 1 107 ? -47.196 -26.754 4.308   1.00 20.28  ? 107 LEU   B O    1 
ATOM   2628 C  CB   . LEU   B 1 107 ? -44.703 -25.134 5.372   1.00 20.41  ? 107 LEU   B CB   1 
ATOM   2629 C  CG   . LEU   B 1 107 ? -44.103 -24.807 6.731   1.00 22.41  ? 107 LEU   B CG   1 
ATOM   2630 C  CD1  . LEU   B 1 107 ? -42.683 -25.330 6.835   1.00 24.49  ? 107 LEU   B CD1  1 
ATOM   2631 C  CD2  . LEU   B 1 107 ? -44.108 -23.300 6.927   1.00 24.05  ? 107 LEU   B CD2  1 
ATOM   2632 N  N    . SER   B 1 108 ? -45.548 -26.868 2.732   1.00 19.14  ? 108 SER   B N    1 
ATOM   2633 C  CA   . SER   B 1 108 ? -46.458 -27.040 1.582   1.00 18.20  ? 108 SER   B CA   1 
ATOM   2634 C  C    . SER   B 1 108 ? -45.669 -27.523 0.371   1.00 18.04  ? 108 SER   B C    1 
ATOM   2635 O  O    . SER   B 1 108 ? -44.427 -27.409 0.356   1.00 17.52  ? 108 SER   B O    1 
ATOM   2636 C  CB   . SER   B 1 108 ? -47.184 -25.769 1.282   1.00 19.55  ? 108 SER   B CB   1 
ATOM   2637 O  OG   . SER   B 1 108 ? -46.309 -24.813 0.704   1.00 20.28  ? 108 SER   B OG   1 
ATOM   2638 N  N    . TRP   B 1 109 ? -46.382 -28.069 -0.598  1.00 16.79  ? 109 TRP   B N    1 
ATOM   2639 C  CA   . TRP   B 1 109 ? -45.798 -28.693 -1.803  1.00 17.64  ? 109 TRP   B CA   1 
ATOM   2640 C  C    . TRP   B 1 109 ? -46.890 -28.814 -2.848  1.00 18.07  ? 109 TRP   B C    1 
ATOM   2641 O  O    . TRP   B 1 109 ? -47.934 -29.399 -2.532  1.00 19.17  ? 109 TRP   B O    1 
ATOM   2642 C  CB   . TRP   B 1 109 ? -45.206 -30.053 -1.450  1.00 18.08  ? 109 TRP   B CB   1 
ATOM   2643 C  CG   . TRP   B 1 109 ? -44.628 -30.814 -2.604  1.00 18.38  ? 109 TRP   B CG   1 
ATOM   2644 C  CD1  . TRP   B 1 109 ? -44.074 -30.302 -3.738  1.00 18.69  ? 109 TRP   B CD1  1 
ATOM   2645 C  CD2  . TRP   B 1 109 ? -44.492 -32.240 -2.701  1.00 18.87  ? 109 TRP   B CD2  1 
ATOM   2646 N  NE1  . TRP   B 1 109 ? -43.594 -31.303 -4.528  1.00 18.37  ? 109 TRP   B NE1  1 
ATOM   2647 C  CE2  . TRP   B 1 109 ? -43.837 -32.507 -3.922  1.00 19.33  ? 109 TRP   B CE2  1 
ATOM   2648 C  CE3  . TRP   B 1 109 ? -44.845 -33.314 -1.872  1.00 19.15  ? 109 TRP   B CE3  1 
ATOM   2649 C  CZ2  . TRP   B 1 109 ? -43.517 -33.805 -4.328  1.00 19.07  ? 109 TRP   B CZ2  1 
ATOM   2650 C  CZ3  . TRP   B 1 109 ? -44.538 -34.592 -2.280  1.00 18.81  ? 109 TRP   B CZ3  1 
ATOM   2651 C  CH2  . TRP   B 1 109 ? -43.896 -34.833 -3.498  1.00 19.11  ? 109 TRP   B CH2  1 
ATOM   2652 N  N    . SER   B 1 110 ? -46.660 -28.265 -4.037  1.00 18.71  ? 110 SER   B N    1 
ATOM   2653 C  CA   . SER   B 1 110 ? -47.586 -28.407 -5.181  1.00 18.06  ? 110 SER   B CA   1 
ATOM   2654 C  C    . SER   B 1 110 ? -46.798 -28.779 -6.439  1.00 17.86  ? 110 SER   B C    1 
ATOM   2655 O  O    . SER   B 1 110 ? -45.581 -28.531 -6.481  1.00 17.71  ? 110 SER   B O    1 
ATOM   2656 C  CB   . SER   B 1 110 ? -48.384 -27.171 -5.351  1.00 18.39  ? 110 SER   B CB   1 
ATOM   2657 O  OG   . SER   B 1 110 ? -47.611 -26.239 -6.058  1.00 22.29  ? 110 SER   B OG   1 
ATOM   2658 N  N    . PHE   B 1 111 ? -47.471 -29.426 -7.387  1.00 17.84  ? 111 PHE   B N    1 
ATOM   2659 C  CA   . PHE   B 1 111 ? -46.864 -29.997 -8.613  1.00 18.44  ? 111 PHE   B CA   1 
ATOM   2660 C  C    . PHE   B 1 111 ? -47.905 -30.095 -9.735  1.00 18.71  ? 111 PHE   B C    1 
ATOM   2661 O  O    . PHE   B 1 111 ? -49.037 -30.521 -9.510  1.00 17.85  ? 111 PHE   B O    1 
ATOM   2662 C  CB   . PHE   B 1 111 ? -46.253 -31.370 -8.349  1.00 17.67  ? 111 PHE   B CB   1 
ATOM   2663 C  CG   . PHE   B 1 111 ? -45.711 -32.032 -9.590  1.00 17.56  ? 111 PHE   B CG   1 
ATOM   2664 C  CD1  . PHE   B 1 111 ? -44.428 -31.761 -10.034 1.00 18.03  ? 111 PHE   B CD1  1 
ATOM   2665 C  CD2  . PHE   B 1 111 ? -46.495 -32.903 -10.328 1.00 17.10  ? 111 PHE   B CD2  1 
ATOM   2666 C  CE1  . PHE   B 1 111 ? -43.932 -32.352 -11.193 1.00 18.67  ? 111 PHE   B CE1  1 
ATOM   2667 C  CE2  . PHE   B 1 111 ? -46.005 -33.490 -11.482 1.00 18.28  ? 111 PHE   B CE2  1 
ATOM   2668 C  CZ   . PHE   B 1 111 ? -44.718 -33.223 -11.911 1.00 19.08  ? 111 PHE   B CZ   1 
ATOM   2669 N  N    . THR   B 1 112 ? -47.499 -29.690 -10.929 1.00 18.86  ? 112 THR   B N    1 
ATOM   2670 C  CA   . THR   B 1 112 ? -48.326 -29.738 -12.155 1.00 20.77  ? 112 THR   B CA   1 
ATOM   2671 C  C    . THR   B 1 112 ? -47.452 -30.300 -13.265 1.00 22.02  ? 112 THR   B C    1 
ATOM   2672 O  O    . THR   B 1 112 ? -46.292 -29.883 -13.382 1.00 22.25  ? 112 THR   B O    1 
ATOM   2673 C  CB   . THR   B 1 112 ? -48.856 -28.367 -12.591 1.00 19.28  ? 112 THR   B CB   1 
ATOM   2674 O  OG1  . THR   B 1 112 ? -49.586 -27.791 -11.512 1.00 22.15  ? 112 THR   B OG1  1 
ATOM   2675 C  CG2  . THR   B 1 112 ? -49.754 -28.457 -13.803 1.00 20.52  ? 112 THR   B CG2  1 
ATOM   2676 N  N    . SER   B 1 113 ? -48.022 -31.197 -14.039 1.00 24.57  ? 113 SER   B N    1 
ATOM   2677 C  CA   . SER   B 1 113 ? -47.407 -31.826 -15.222 1.00 28.39  ? 113 SER   B CA   1 
ATOM   2678 C  C    . SER   B 1 113 ? -48.434 -31.751 -16.349 1.00 31.52  ? 113 SER   B C    1 
ATOM   2679 O  O    . SER   B 1 113 ? -49.627 -32.090 -16.080 1.00 29.10  ? 113 SER   B O    1 
ATOM   2680 C  CB   . SER   B 1 113 ? -47.032 -33.238 -14.913 1.00 30.54  ? 113 SER   B CB   1 
ATOM   2681 O  OG   . SER   B 1 113 ? -46.226 -33.772 -15.944 1.00 37.46  ? 113 SER   B OG   1 
ATOM   2682 N  N    . LYS   B 1 114 ? -48.003 -31.289 -17.525 1.00 32.44  ? 114 LYS   B N    1 
ATOM   2683 C  CA   . LYS   B 1 114 ? -48.836 -31.178 -18.748 1.00 33.89  ? 114 LYS   B CA   1 
ATOM   2684 C  C    . LYS   B 1 114 ? -48.046 -31.810 -19.893 1.00 32.96  ? 114 LYS   B C    1 
ATOM   2685 O  O    . LYS   B 1 114 ? -46.898 -31.387 -20.137 1.00 29.65  ? 114 LYS   B O    1 
ATOM   2686 C  CB   . LYS   B 1 114 ? -49.223 -29.720 -19.016 1.00 38.60  ? 114 LYS   B CB   1 
ATOM   2687 C  CG   . LYS   B 1 114 ? -50.132 -29.100 -17.955 1.00 44.87  ? 114 LYS   B CG   1 
ATOM   2688 C  CD   . LYS   B 1 114 ? -50.737 -27.751 -18.333 1.00 47.16  ? 114 LYS   B CD   1 
ATOM   2689 C  CE   . LYS   B 1 114 ? -51.976 -27.387 -17.528 1.00 48.28  ? 114 LYS   B CE   1 
ATOM   2690 N  NZ   . LYS   B 1 114 ? -53.199 -28.088 -18.011 1.00 46.31  ? 114 LYS   B NZ   1 
ATOM   2691 N  N    . LEU   B 1 115 ? -48.652 -32.813 -20.521 1.00 32.53  ? 115 LEU   B N    1 
ATOM   2692 C  CA   . LEU   B 1 115 ? -48.095 -33.614 -21.630 1.00 35.05  ? 115 LEU   B CA   1 
ATOM   2693 C  C    . LEU   B 1 115 ? -48.933 -33.333 -22.890 1.00 40.86  ? 115 LEU   B C    1 
ATOM   2694 O  O    . LEU   B 1 115 ? -49.953 -34.032 -23.102 1.00 35.62  ? 115 LEU   B O    1 
ATOM   2695 C  CB   . LEU   B 1 115 ? -48.139 -35.076 -21.179 1.00 32.52  ? 115 LEU   B CB   1 
ATOM   2696 C  CG   . LEU   B 1 115 ? -47.365 -36.070 -22.036 1.00 33.52  ? 115 LEU   B CG   1 
ATOM   2697 C  CD1  . LEU   B 1 115 ? -45.874 -35.749 -22.074 1.00 33.47  ? 115 LEU   B CD1  1 
ATOM   2698 C  CD2  . LEU   B 1 115 ? -47.592 -37.484 -21.526 1.00 33.33  ? 115 LEU   B CD2  1 
ATOM   2699 N  N    . LYS   B 1 116 ? -48.532 -32.306 -23.654 1.00 49.20  ? 116 LYS   B N    1 
ATOM   2700 C  CA   . LYS   B 1 116 ? -49.221 -31.785 -24.867 1.00 58.41  ? 116 LYS   B CA   1 
ATOM   2701 C  C    . LYS   B 1 116 ? -48.819 -32.635 -26.075 1.00 65.31  ? 116 LYS   B C    1 
ATOM   2702 O  O    . LYS   B 1 116 ? -47.708 -32.439 -26.581 1.00 73.75  ? 116 LYS   B O    1 
ATOM   2703 C  CB   . LYS   B 1 116 ? -48.848 -30.315 -25.075 1.00 66.26  ? 116 LYS   B CB   1 
ATOM   2704 C  CG   . LYS   B 1 116 ? -49.485 -29.635 -26.279 1.00 73.07  ? 116 LYS   B CG   1 
ATOM   2705 C  CD   . LYS   B 1 116 ? -50.858 -29.087 -25.994 1.00 80.01  ? 116 LYS   B CD   1 
ATOM   2706 C  CE   . LYS   B 1 116 ? -51.417 -28.242 -27.119 1.00 87.38  ? 116 LYS   B CE   1 
ATOM   2707 N  NZ   . LYS   B 1 116 ? -52.688 -27.594 -26.718 1.00 91.92  ? 116 LYS   B NZ   1 
ATOM   2708 N  N    . SER   B 1 117 ? -49.727 -33.498 -26.541 1.00 79.24  ? 117 SER   B N    1 
ATOM   2709 C  CA   . SER   B 1 117 ? -49.467 -34.667 -27.429 1.00 86.27  ? 117 SER   B CA   1 
ATOM   2710 C  C    . SER   B 1 117 ? -49.268 -34.242 -28.899 1.00 95.66  ? 117 SER   B C    1 
ATOM   2711 O  O    . SER   B 1 117 ? -49.522 -33.060 -29.235 1.00 89.54  ? 117 SER   B O    1 
ATOM   2712 C  CB   . SER   B 1 117 ? -50.579 -35.685 -27.277 1.00 87.07  ? 117 SER   B CB   1 
ATOM   2713 O  OG   . SER   B 1 117 ? -50.111 -37.001 -27.531 1.00 88.21  ? 117 SER   B OG   1 
ATOM   2714 N  N    . ASN   B 1 118 ? -48.868 -35.205 -29.746 1.00 106.06 ? 118 ASN   B N    1 
ATOM   2715 C  CA   . ASN   B 1 118 ? -48.217 -35.021 -31.079 1.00 106.61 ? 118 ASN   B CA   1 
ATOM   2716 C  C    . ASN   B 1 118 ? -49.265 -34.875 -32.200 1.00 110.27 ? 118 ASN   B C    1 
ATOM   2717 O  O    . ASN   B 1 118 ? -49.350 -33.773 -32.793 1.00 95.98  ? 118 ASN   B O    1 
ATOM   2718 C  CB   . ASN   B 1 118 ? -47.274 -36.197 -31.381 1.00 102.51 ? 118 ASN   B CB   1 
ATOM   2719 C  CG   . ASN   B 1 118 ? -45.918 -35.785 -31.912 1.00 97.87  ? 118 ASN   B CG   1 
ATOM   2720 O  OD1  . ASN   B 1 118 ? -45.509 -34.633 -31.774 1.00 96.19  ? 118 ASN   B OD1  1 
ATOM   2721 N  ND2  . ASN   B 1 118 ? -45.205 -36.735 -32.496 1.00 85.80  ? 118 ASN   B ND2  1 
ATOM   2722 N  N    . SER   B 1 119 ? -50.016 -35.952 -32.484 1.00 114.51 ? 119 SER   B N    1 
ATOM   2723 C  CA   . SER   B 1 119 ? -50.974 -36.089 -33.618 1.00 109.13 ? 119 SER   B CA   1 
ATOM   2724 C  C    . SER   B 1 119 ? -52.363 -35.531 -33.255 1.00 106.81 ? 119 SER   B C    1 
ATOM   2725 O  O    . SER   B 1 119 ? -52.991 -34.931 -34.150 1.00 97.92  ? 119 SER   B O    1 
ATOM   2726 C  CB   . SER   B 1 119 ? -51.063 -37.530 -34.069 1.00 107.36 ? 119 SER   B CB   1 
ATOM   2727 O  OG   . SER   B 1 119 ? -49.814 -37.975 -34.578 1.00 103.21 ? 119 SER   B OG   1 
ATOM   2728 N  N    . THR   B 1 120 ? -52.826 -35.729 -32.009 1.00 105.05 ? 120 THR   B N    1 
ATOM   2729 C  CA   . THR   B 1 120 ? -54.178 -35.330 -31.512 1.00 96.68  ? 120 THR   B CA   1 
ATOM   2730 C  C    . THR   B 1 120 ? -54.179 -33.846 -31.112 1.00 94.97  ? 120 THR   B C    1 
ATOM   2731 O  O    . THR   B 1 120 ? -55.241 -33.216 -31.251 1.00 95.07  ? 120 THR   B O    1 
ATOM   2732 C  CB   . THR   B 1 120 ? -54.661 -36.232 -30.363 1.00 95.66  ? 120 THR   B CB   1 
ATOM   2733 O  OG1  . THR   B 1 120 ? -53.792 -36.097 -29.236 1.00 90.56  ? 120 THR   B OG1  1 
ATOM   2734 C  CG2  . THR   B 1 120 ? -54.755 -37.691 -30.761 1.00 94.13  ? 120 THR   B CG2  1 
ATOM   2735 N  N    . HIS   B 1 121 ? -53.044 -33.314 -30.637 1.00 94.21  ? 121 HIS   B N    1 
ATOM   2736 C  CA   . HIS   B 1 121 ? -52.813 -31.873 -30.323 1.00 89.45  ? 121 HIS   B CA   1 
ATOM   2737 C  C    . HIS   B 1 121 ? -53.615 -31.453 -29.073 1.00 83.24  ? 121 HIS   B C    1 
ATOM   2738 O  O    . HIS   B 1 121 ? -54.160 -30.327 -29.078 1.00 91.82  ? 121 HIS   B O    1 
ATOM   2739 C  CB   . HIS   B 1 121 ? -53.094 -30.995 -31.565 1.00 89.53  ? 121 HIS   B CB   1 
ATOM   2740 C  CG   . HIS   B 1 121 ? -51.885 -30.681 -32.389 1.00 93.78  ? 121 HIS   B CG   1 
ATOM   2741 N  ND1  . HIS   B 1 121 ? -51.286 -29.427 -32.390 1.00 93.47  ? 121 HIS   B ND1  1 
ATOM   2742 C  CD2  . HIS   B 1 121 ? -51.159 -31.439 -33.240 1.00 92.96  ? 121 HIS   B CD2  1 
ATOM   2743 C  CE1  . HIS   B 1 121 ? -50.243 -29.435 -33.197 1.00 89.56  ? 121 HIS   B CE1  1 
ATOM   2744 N  NE2  . HIS   B 1 121 ? -50.142 -30.658 -33.729 1.00 89.10  ? 121 HIS   B NE2  1 
ATOM   2745 N  N    . GLU   B 1 122 ? -53.637 -32.292 -28.025 1.00 67.60  ? 122 GLU   B N    1 
ATOM   2746 C  CA   . GLU   B 1 122 ? -54.344 -32.040 -26.731 1.00 63.20  ? 122 GLU   B CA   1 
ATOM   2747 C  C    . GLU   B 1 122 ? -53.481 -32.555 -25.561 1.00 56.21  ? 122 GLU   B C    1 
ATOM   2748 O  O    . GLU   B 1 122 ? -52.423 -33.160 -25.838 1.00 51.99  ? 122 GLU   B O    1 
ATOM   2749 C  CB   . GLU   B 1 122 ? -55.738 -32.675 -26.752 1.00 62.59  ? 122 GLU   B CB   1 
ATOM   2750 C  CG   . GLU   B 1 122 ? -55.764 -34.052 -27.401 1.00 67.79  ? 122 GLU   B CG   1 
ATOM   2751 C  CD   . GLU   B 1 122 ? -57.139 -34.663 -27.624 1.00 66.09  ? 122 GLU   B CD   1 
ATOM   2752 O  OE1  . GLU   B 1 122 ? -58.147 -33.962 -27.400 1.00 66.55  ? 122 GLU   B OE1  1 
ATOM   2753 O  OE2  . GLU   B 1 122 ? -57.196 -35.847 -28.016 1.00 64.20  ? 122 GLU   B OE2  1 
ATOM   2754 N  N    . THR   B 1 123 ? -53.900 -32.314 -24.307 1.00 45.68  ? 123 THR   B N    1 
ATOM   2755 C  CA   . THR   B 1 123 ? -53.047 -32.483 -23.094 1.00 41.53  ? 123 THR   B CA   1 
ATOM   2756 C  C    . THR   B 1 123 ? -53.619 -33.531 -22.123 1.00 34.22  ? 123 THR   B C    1 
ATOM   2757 O  O    . THR   B 1 123 ? -54.834 -33.535 -21.858 1.00 33.83  ? 123 THR   B O    1 
ATOM   2758 C  CB   . THR   B 1 123 ? -52.777 -31.152 -22.363 1.00 43.13  ? 123 THR   B CB   1 
ATOM   2759 O  OG1  . THR   B 1 123 ? -53.750 -30.899 -21.350 1.00 45.93  ? 123 THR   B OG1  1 
ATOM   2760 C  CG2  . THR   B 1 123 ? -52.718 -29.951 -23.281 1.00 42.55  ? 123 THR   B CG2  1 
ATOM   2761 N  N    . ASN   B 1 124 ? -52.731 -34.386 -21.613 1.00 27.95  ? 124 ASN   B N    1 
ATOM   2762 C  CA   . ASN   B 1 124 ? -52.880 -35.116 -20.331 1.00 25.63  ? 124 ASN   B CA   1 
ATOM   2763 C  C    . ASN   B 1 124 ? -52.167 -34.326 -19.235 1.00 25.60  ? 124 ASN   B C    1 
ATOM   2764 O  O    . ASN   B 1 124 ? -51.075 -33.773 -19.499 1.00 23.97  ? 124 ASN   B O    1 
ATOM   2765 C  CB   . ASN   B 1 124 ? -52.336 -36.534 -20.435 1.00 24.90  ? 124 ASN   B CB   1 
ATOM   2766 C  CG   . ASN   B 1 124 ? -53.301 -37.426 -21.172 1.00 24.36  ? 124 ASN   B CG   1 
ATOM   2767 O  OD1  . ASN   B 1 124 ? -54.297 -36.938 -21.717 1.00 23.76  ? 124 ASN   B OD1  1 
ATOM   2768 N  ND2  . ASN   B 1 124 ? -53.017 -38.714 -21.180 1.00 22.03  ? 124 ASN   B ND2  1 
ATOM   2769 N  N    . ALA   B 1 125 ? -52.768 -34.263 -18.049 1.00 24.82  ? 125 ALA   B N    1 
ATOM   2770 C  CA   . ALA   B 1 125 ? -52.293 -33.414 -16.937 1.00 21.94  ? 125 ALA   B CA   1 
ATOM   2771 C  C    . ALA   B 1 125 ? -52.510 -34.127 -15.605 1.00 20.99  ? 125 ALA   B C    1 
ATOM   2772 O  O    . ALA   B 1 125 ? -53.548 -34.827 -15.468 1.00 18.13  ? 125 ALA   B O    1 
ATOM   2773 C  CB   . ALA   B 1 125 ? -53.015 -32.088 -16.974 1.00 22.15  ? 125 ALA   B CB   1 
ATOM   2774 N  N    . LEU   B 1 126 ? -51.561 -33.927 -14.677 1.00 20.74  ? 126 LEU   B N    1 
ATOM   2775 C  CA   . LEU   B 1 126 ? -51.676 -34.216 -13.226 1.00 19.26  ? 126 LEU   B CA   1 
ATOM   2776 C  C    . LEU   B 1 126 ? -51.352 -32.927 -12.471 1.00 20.05  ? 126 LEU   B C    1 
ATOM   2777 O  O    . LEU   B 1 126 ? -50.475 -32.168 -12.908 1.00 23.23  ? 126 LEU   B O    1 
ATOM   2778 C  CB   . LEU   B 1 126 ? -50.705 -35.334 -12.840 1.00 19.14  ? 126 LEU   B CB   1 
ATOM   2779 C  CG   . LEU   B 1 126 ? -50.553 -35.584 -11.335 1.00 19.13  ? 126 LEU   B CG   1 
ATOM   2780 C  CD1  . LEU   B 1 126 ? -51.731 -36.383 -10.802 1.00 19.06  ? 126 LEU   B CD1  1 
ATOM   2781 C  CD2  . LEU   B 1 126 ? -49.261 -36.304 -11.029 1.00 18.16  ? 126 LEU   B CD2  1 
ATOM   2782 N  N    . HIS   B 1 127 ? -52.006 -32.713 -11.345 1.00 19.03  ? 127 HIS   B N    1 
ATOM   2783 C  CA   . HIS   B 1 127 ? -51.737 -31.587 -10.429 1.00 18.62  ? 127 HIS   B CA   1 
ATOM   2784 C  C    . HIS   B 1 127 ? -52.109 -32.009 -9.006  1.00 17.72  ? 127 HIS   B C    1 
ATOM   2785 O  O    . HIS   B 1 127 ? -53.192 -32.608 -8.807  1.00 18.13  ? 127 HIS   B O    1 
ATOM   2786 C  CB   . HIS   B 1 127 ? -52.502 -30.331 -10.877 1.00 20.20  ? 127 HIS   B CB   1 
ATOM   2787 C  CG   . HIS   B 1 127 ? -52.485 -29.265 -9.833  1.00 22.42  ? 127 HIS   B CG   1 
ATOM   2788 N  ND1  . HIS   B 1 127 ? -51.353 -28.521 -9.560  1.00 22.59  ? 127 HIS   B ND1  1 
ATOM   2789 C  CD2  . HIS   B 1 127 ? -53.426 -28.865 -8.955  1.00 22.48  ? 127 HIS   B CD2  1 
ATOM   2790 C  CE1  . HIS   B 1 127 ? -51.614 -27.698 -8.568  1.00 23.53  ? 127 HIS   B CE1  1 
ATOM   2791 N  NE2  . HIS   B 1 127 ? -52.877 -27.899 -8.173  1.00 21.92  ? 127 HIS   B NE2  1 
ATOM   2792 N  N    . PHE   B 1 128 ? -51.241 -31.733 -8.043  1.00 16.68  ? 128 PHE   B N    1 
ATOM   2793 C  CA   . PHE   B 1 128 ? -51.552 -31.938 -6.611  1.00 16.38  ? 128 PHE   B CA   1 
ATOM   2794 C  C    . PHE   B 1 128 ? -51.090 -30.700 -5.859  1.00 17.29  ? 128 PHE   B C    1 
ATOM   2795 O  O    . PHE   B 1 128 ? -50.160 -30.039 -6.322  1.00 17.97  ? 128 PHE   B O    1 
ATOM   2796 C  CB   . PHE   B 1 128 ? -50.998 -33.272 -6.100  1.00 15.67  ? 128 PHE   B CB   1 
ATOM   2797 C  CG   . PHE   B 1 128 ? -49.500 -33.434 -6.070  1.00 15.02  ? 128 PHE   B CG   1 
ATOM   2798 C  CD1  . PHE   B 1 128 ? -48.741 -32.865 -5.055  1.00 14.50  ? 128 PHE   B CD1  1 
ATOM   2799 C  CD2  . PHE   B 1 128 ? -48.862 -34.253 -6.983  1.00 14.17  ? 128 PHE   B CD2  1 
ATOM   2800 C  CE1  . PHE   B 1 128 ? -47.366 -33.063 -4.995  1.00 14.22  ? 128 PHE   B CE1  1 
ATOM   2801 C  CE2  . PHE   B 1 128 ? -47.489 -34.443 -6.917  1.00 14.24  ? 128 PHE   B CE2  1 
ATOM   2802 C  CZ   . PHE   B 1 128 ? -46.744 -33.856 -5.927  1.00 13.76  ? 128 PHE   B CZ   1 
ATOM   2803 N  N    . MET   B 1 129 ? -51.760 -30.411 -4.747  1.00 18.09  ? 129 MET   B N    1 
ATOM   2804 C  CA   . MET   B 1 129 ? -51.464 -29.280 -3.860  1.00 19.15  ? 129 MET   B CA   1 
ATOM   2805 C  C    . MET   B 1 129 ? -51.621 -29.740 -2.411  1.00 18.83  ? 129 MET   B C    1 
ATOM   2806 O  O    . MET   B 1 129 ? -52.752 -30.097 -2.032  1.00 18.61  ? 129 MET   B O    1 
ATOM   2807 C  CB   . MET   B 1 129 ? -52.427 -28.131 -4.162  1.00 21.52  ? 129 MET   B CB   1 
ATOM   2808 C  CG   . MET   B 1 129 ? -52.100 -26.851 -3.436  1.00 23.60  ? 129 MET   B CG   1 
ATOM   2809 S  SD   . MET   B 1 129 ? -53.147 -25.498 -4.022  1.00 29.09  ? 129 MET   B SD   1 
ATOM   2810 C  CE   . MET   B 1 129 ? -52.112 -24.802 -5.317  1.00 31.83  ? 129 MET   B CE   1 
ATOM   2811 N  N    . PHE   B 1 130 ? -50.539 -29.722 -1.632  1.00 17.85  ? 130 PHE   B N    1 
ATOM   2812 C  CA   . PHE   B 1 130 ? -50.582 -29.945 -0.168  1.00 19.36  ? 130 PHE   B CA   1 
ATOM   2813 C  C    . PHE   B 1 130 ? -50.244 -28.635 0.548   1.00 19.45  ? 130 PHE   B C    1 
ATOM   2814 O  O    . PHE   B 1 130 ? -49.072 -28.247 0.503   1.00 18.43  ? 130 PHE   B O    1 
ATOM   2815 C  CB   . PHE   B 1 130 ? -49.589 -31.032 0.254   1.00 20.31  ? 130 PHE   B CB   1 
ATOM   2816 C  CG   . PHE   B 1 130 ? -49.741 -32.349 -0.458  1.00 20.58  ? 130 PHE   B CG   1 
ATOM   2817 C  CD1  . PHE   B 1 130 ? -50.862 -33.134 -0.263  1.00 24.21  ? 130 PHE   B CD1  1 
ATOM   2818 C  CD2  . PHE   B 1 130 ? -48.747 -32.829 -1.290  1.00 21.48  ? 130 PHE   B CD2  1 
ATOM   2819 C  CE1  . PHE   B 1 130 ? -50.998 -34.354 -0.909  1.00 24.24  ? 130 PHE   B CE1  1 
ATOM   2820 C  CE2  . PHE   B 1 130 ? -48.884 -34.042 -1.944  1.00 21.38  ? 130 PHE   B CE2  1 
ATOM   2821 C  CZ   . PHE   B 1 130 ? -50.004 -34.804 -1.747  1.00 22.97  ? 130 PHE   B CZ   1 
ATOM   2822 N  N    . ASN   B 1 131 ? -51.229 -27.996 1.183   1.00 19.23  ? 131 ASN   B N    1 
ATOM   2823 C  CA   . ASN   B 1 131 ? -51.039 -26.811 2.059   1.00 20.46  ? 131 ASN   B CA   1 
ATOM   2824 C  C    . ASN   B 1 131 ? -51.018 -27.267 3.514   1.00 20.69  ? 131 ASN   B C    1 
ATOM   2825 O  O    . ASN   B 1 131 ? -50.503 -26.522 4.342   1.00 21.52  ? 131 ASN   B O    1 
ATOM   2826 C  CB   . ASN   B 1 131 ? -52.095 -25.733 1.799   1.00 21.63  ? 131 ASN   B CB   1 
ATOM   2827 C  CG   . ASN   B 1 131 ? -51.836 -24.983 0.504   1.00 23.87  ? 131 ASN   B CG   1 
ATOM   2828 O  OD1  . ASN   B 1 131 ? -50.727 -24.505 0.295   1.00 28.01  ? 131 ASN   B OD1  1 
ATOM   2829 N  ND2  . ASN   B 1 131 ? -52.828 -24.865 -0.365  1.00 20.29  ? 131 ASN   B ND2  1 
ATOM   2830 N  N    . GLN   B 1 132 ? -51.539 -28.455 3.808   1.00 22.69  ? 132 GLN   B N    1 
ATOM   2831 C  CA   . GLN   B 1 132 ? -51.485 -29.092 5.150   1.00 25.18  ? 132 GLN   B CA   1 
ATOM   2832 C  C    . GLN   B 1 132 ? -51.291 -30.601 4.943   1.00 25.15  ? 132 GLN   B C    1 
ATOM   2833 O  O    . GLN   B 1 132 ? -52.004 -31.194 4.118   1.00 26.48  ? 132 GLN   B O    1 
ATOM   2834 C  CB   . GLN   B 1 132 ? -52.751 -28.846 5.987   1.00 28.53  ? 132 GLN   B CB   1 
ATOM   2835 C  CG   . GLN   B 1 132 ? -53.035 -27.380 6.317   1.00 35.28  ? 132 GLN   B CG   1 
ATOM   2836 C  CD   . GLN   B 1 132 ? -51.980 -26.671 7.152   1.00 38.16  ? 132 GLN   B CD   1 
ATOM   2837 O  OE1  . GLN   B 1 132 ? -51.219 -27.284 7.897   1.00 42.06  ? 132 GLN   B OE1  1 
ATOM   2838 N  NE2  . GLN   B 1 132 ? -51.929 -25.350 7.042   1.00 34.52  ? 132 GLN   B NE2  1 
ATOM   2839 N  N    . PHE   B 1 133 ? -50.364 -31.203 5.672   1.00 21.36  ? 133 PHE   B N    1 
ATOM   2840 C  CA   . PHE   B 1 133 ? -50.107 -32.657 5.643   1.00 22.00  ? 133 PHE   B CA   1 
ATOM   2841 C  C    . PHE   B 1 133 ? -50.832 -33.273 6.847   1.00 23.30  ? 133 PHE   B C    1 
ATOM   2842 O  O    . PHE   B 1 133 ? -50.963 -32.579 7.866   1.00 24.70  ? 133 PHE   B O    1 
ATOM   2843 C  CB   . PHE   B 1 133 ? -48.597 -32.897 5.659   1.00 21.49  ? 133 PHE   B CB   1 
ATOM   2844 C  CG   . PHE   B 1 133 ? -47.846 -32.348 4.471   1.00 21.95  ? 133 PHE   B CG   1 
ATOM   2845 C  CD1  . PHE   B 1 133 ? -47.707 -33.100 3.318   1.00 21.68  ? 133 PHE   B CD1  1 
ATOM   2846 C  CD2  . PHE   B 1 133 ? -47.274 -31.086 4.506   1.00 21.12  ? 133 PHE   B CD2  1 
ATOM   2847 C  CE1  . PHE   B 1 133 ? -47.008 -32.612 2.230   1.00 21.63  ? 133 PHE   B CE1  1 
ATOM   2848 C  CE2  . PHE   B 1 133 ? -46.576 -30.602 3.416   1.00 20.57  ? 133 PHE   B CE2  1 
ATOM   2849 C  CZ   . PHE   B 1 133 ? -46.437 -31.368 2.287   1.00 21.51  ? 133 PHE   B CZ   1 
ATOM   2850 N  N    . SER   B 1 134 ? -51.288 -34.521 6.747   1.00 23.45  ? 134 SER   B N    1 
ATOM   2851 C  CA   . SER   B 1 134 ? -52.035 -35.215 7.829   1.00 26.08  ? 134 SER   B CA   1 
ATOM   2852 C  C    . SER   B 1 134 ? -51.231 -36.419 8.322   1.00 27.91  ? 134 SER   B C    1 
ATOM   2853 O  O    . SER   B 1 134 ? -50.394 -36.915 7.559   1.00 24.52  ? 134 SER   B O    1 
ATOM   2854 C  CB   . SER   B 1 134 ? -53.414 -35.604 7.364   1.00 25.91  ? 134 SER   B CB   1 
ATOM   2855 O  OG   . SER   B 1 134 ? -53.370 -36.043 6.015   1.00 27.34  ? 134 SER   B OG   1 
ATOM   2856 N  N    . LYS   B 1 135 ? -51.535 -36.883 9.537   1.00 35.82  ? 135 LYS   B N    1 
ATOM   2857 C  CA   . LYS   B 1 135 ? -50.834 -37.974 10.277  1.00 43.13  ? 135 LYS   B CA   1 
ATOM   2858 C  C    . LYS   B 1 135 ? -50.896 -39.284 9.485   1.00 42.30  ? 135 LYS   B C    1 
ATOM   2859 O  O    . LYS   B 1 135 ? -49.948 -40.074 9.622   1.00 49.31  ? 135 LYS   B O    1 
ATOM   2860 C  CB   . LYS   B 1 135 ? -51.449 -38.249 11.659  1.00 47.61  ? 135 LYS   B CB   1 
ATOM   2861 C  CG   . LYS   B 1 135 ? -51.293 -37.148 12.711  1.00 51.97  ? 135 LYS   B CG   1 
ATOM   2862 C  CD   . LYS   B 1 135 ? -52.015 -35.819 12.416  1.00 56.62  ? 135 LYS   B CD   1 
ATOM   2863 C  CE   . LYS   B 1 135 ? -53.498 -35.938 12.098  1.00 56.52  ? 135 LYS   B CE   1 
ATOM   2864 N  NZ   . LYS   B 1 135 ? -53.935 -34.965 11.062  1.00 54.51  ? 135 LYS   B NZ   1 
ATOM   2865 N  N    . ASP   B 1 136 ? -51.961 -39.516 8.716   1.00 39.87  ? 136 ASP   B N    1 
ATOM   2866 C  CA   . ASP   B 1 136 ? -52.084 -40.730 7.867   1.00 44.39  ? 136 ASP   B CA   1 
ATOM   2867 C  C    . ASP   B 1 136 ? -52.319 -40.318 6.403   1.00 42.39  ? 136 ASP   B C    1 
ATOM   2868 O  O    . ASP   B 1 136 ? -53.479 -40.364 5.932   1.00 39.26  ? 136 ASP   B O    1 
ATOM   2869 C  CB   . ASP   B 1 136 ? -53.158 -41.666 8.421   1.00 48.11  ? 136 ASP   B CB   1 
ATOM   2870 C  CG   . ASP   B 1 136 ? -53.008 -43.084 7.909   1.00 56.01  ? 136 ASP   B CG   1 
ATOM   2871 O  OD1  . ASP   B 1 136 ? -52.089 -43.320 7.082   1.00 62.10  ? 136 ASP   B OD1  1 
ATOM   2872 O  OD2  . ASP   B 1 136 ? -53.809 -43.939 8.329   1.00 64.49  ? 136 ASP   B OD2  1 
ATOM   2873 N  N    . GLN   B 1 137 ? -51.239 -39.961 5.704   1.00 34.90  ? 137 GLN   B N    1 
ATOM   2874 C  CA   . GLN   B 1 137 ? -51.284 -39.272 4.393   1.00 33.83  ? 137 GLN   B CA   1 
ATOM   2875 C  C    . GLN   B 1 137 ? -51.176 -40.311 3.272   1.00 31.13  ? 137 GLN   B C    1 
ATOM   2876 O  O    . GLN   B 1 137 ? -50.059 -40.528 2.786   1.00 25.86  ? 137 GLN   B O    1 
ATOM   2877 C  CB   . GLN   B 1 137 ? -50.145 -38.258 4.325   1.00 34.70  ? 137 GLN   B CB   1 
ATOM   2878 C  CG   . GLN   B 1 137 ? -50.128 -37.452 3.040   1.00 35.06  ? 137 GLN   B CG   1 
ATOM   2879 C  CD   . GLN   B 1 137 ? -50.908 -36.176 3.156   1.00 34.03  ? 137 GLN   B CD   1 
ATOM   2880 O  OE1  . GLN   B 1 137 ? -50.731 -35.416 4.103   1.00 35.64  ? 137 GLN   B OE1  1 
ATOM   2881 N  NE2  . GLN   B 1 137 ? -51.767 -35.933 2.183   1.00 35.36  ? 137 GLN   B NE2  1 
ATOM   2882 N  N    . LYS   B 1 138 ? -52.310 -40.855 2.814   1.00 28.94  ? 138 LYS   B N    1 
ATOM   2883 C  CA   . LYS   B 1 138 ? -52.330 -42.088 1.983   1.00 27.46  ? 138 LYS   B CA   1 
ATOM   2884 C  C    . LYS   B 1 138 ? -51.911 -41.784 0.535   1.00 22.83  ? 138 LYS   B C    1 
ATOM   2885 O  O    . LYS   B 1 138 ? -51.654 -42.748 -0.209  1.00 18.37  ? 138 LYS   B O    1 
ATOM   2886 C  CB   . LYS   B 1 138 ? -53.688 -42.782 2.114   1.00 30.91  ? 138 LYS   B CB   1 
ATOM   2887 C  CG   . LYS   B 1 138 ? -54.031 -43.172 3.544   1.00 35.84  ? 138 LYS   B CG   1 
ATOM   2888 C  CD   . LYS   B 1 138 ? -55.002 -44.333 3.675   1.00 41.22  ? 138 LYS   B CD   1 
ATOM   2889 C  CE   . LYS   B 1 138 ? -54.883 -45.064 4.997   1.00 43.80  ? 138 LYS   B CE   1 
ATOM   2890 N  NZ   . LYS   B 1 138 ? -53.668 -45.919 5.028   1.00 45.93  ? 138 LYS   B NZ   1 
ATOM   2891 N  N    . ASP   B 1 139 ? -51.799 -40.511 0.131   1.00 20.12  ? 139 ASP   B N    1 
ATOM   2892 C  CA   . ASP   B 1 139 ? -51.326 -40.176 -1.248  1.00 19.44  ? 139 ASP   B CA   1 
ATOM   2893 C  C    . ASP   B 1 139 ? -49.810 -39.898 -1.269  1.00 17.68  ? 139 ASP   B C    1 
ATOM   2894 O  O    . ASP   B 1 139 ? -49.303 -39.488 -2.323  1.00 17.80  ? 139 ASP   B O    1 
ATOM   2895 C  CB   . ASP   B 1 139 ? -52.162 -39.062 -1.893  1.00 19.49  ? 139 ASP   B CB   1 
ATOM   2896 C  CG   . ASP   B 1 139 ? -52.291 -37.793 -1.076  1.00 21.31  ? 139 ASP   B CG   1 
ATOM   2897 O  OD1  . ASP   B 1 139 ? -51.898 -37.800 0.119   1.00 22.93  ? 139 ASP   B OD1  1 
ATOM   2898 O  OD2  . ASP   B 1 139 ? -52.793 -36.817 -1.635  1.00 20.84  ? 139 ASP   B OD2  1 
ATOM   2899 N  N    . LEU   B 1 140 ? -49.110 -40.086 -0.151  1.00 17.77  ? 140 LEU   B N    1 
ATOM   2900 C  CA   . LEU   B 1 140 ? -47.635 -39.974 -0.075  1.00 18.17  ? 140 LEU   B CA   1 
ATOM   2901 C  C    . LEU   B 1 140 ? -47.052 -41.337 0.292   1.00 18.17  ? 140 LEU   B C    1 
ATOM   2902 O  O    . LEU   B 1 140 ? -47.616 -42.030 1.098   1.00 19.90  ? 140 LEU   B O    1 
ATOM   2903 C  CB   . LEU   B 1 140 ? -47.253 -38.958 1.006   1.00 19.36  ? 140 LEU   B CB   1 
ATOM   2904 C  CG   . LEU   B 1 140 ? -47.455 -37.481 0.697   1.00 18.90  ? 140 LEU   B CG   1 
ATOM   2905 C  CD1  . LEU   B 1 140 ? -46.832 -36.636 1.792   1.00 19.89  ? 140 LEU   B CD1  1 
ATOM   2906 C  CD2  . LEU   B 1 140 ? -46.884 -37.075 -0.651  1.00 18.75  ? 140 LEU   B CD2  1 
ATOM   2907 N  N    . ILE   B 1 141 ? -45.934 -41.692 -0.296  1.00 19.86  ? 141 ILE   B N    1 
ATOM   2908 C  CA   . ILE   B 1 141 ? -45.086 -42.826 0.128   1.00 18.97  ? 141 ILE   B CA   1 
ATOM   2909 C  C    . ILE   B 1 141 ? -43.968 -42.215 0.960   1.00 18.14  ? 141 ILE   B C    1 
ATOM   2910 O  O    . ILE   B 1 141 ? -43.098 -41.595 0.369   1.00 17.54  ? 141 ILE   B O    1 
ATOM   2911 C  CB   . ILE   B 1 141 ? -44.554 -43.571 -1.107  1.00 20.83  ? 141 ILE   B CB   1 
ATOM   2912 C  CG1  . ILE   B 1 141 ? -45.694 -44.269 -1.842  1.00 23.71  ? 141 ILE   B CG1  1 
ATOM   2913 C  CG2  . ILE   B 1 141 ? -43.418 -44.534 -0.750  1.00 20.34  ? 141 ILE   B CG2  1 
ATOM   2914 C  CD1  . ILE   B 1 141 ? -45.462 -44.398 -3.334  1.00 25.96  ? 141 ILE   B CD1  1 
ATOM   2915 N  N    . LEU   B 1 142 ? -44.009 -42.382 2.276   1.00 17.83  ? 142 LEU   B N    1 
ATOM   2916 C  CA   . LEU   B 1 142 ? -42.934 -41.915 3.182   1.00 17.75  ? 142 LEU   B CA   1 
ATOM   2917 C  C    . LEU   B 1 142 ? -41.814 -42.963 3.178   1.00 17.50  ? 142 LEU   B C    1 
ATOM   2918 O  O    . LEU   B 1 142 ? -42.129 -44.152 3.245   1.00 16.01  ? 142 LEU   B O    1 
ATOM   2919 C  CB   . LEU   B 1 142 ? -43.518 -41.668 4.575   1.00 17.43  ? 142 LEU   B CB   1 
ATOM   2920 C  CG   . LEU   B 1 142 ? -44.710 -40.709 4.597   1.00 18.78  ? 142 LEU   B CG   1 
ATOM   2921 C  CD1  . LEU   B 1 142 ? -45.260 -40.531 6.008   1.00 19.50  ? 142 LEU   B CD1  1 
ATOM   2922 C  CD2  . LEU   B 1 142 ? -44.329 -39.349 4.012   1.00 20.10  ? 142 LEU   B CD2  1 
ATOM   2923 N  N    . GLN   B 1 143 ? -40.553 -42.524 3.073   1.00 17.24  ? 143 GLN   B N    1 
ATOM   2924 C  CA   . GLN   B 1 143 ? -39.372 -43.427 3.047   1.00 17.02  ? 143 GLN   B CA   1 
ATOM   2925 C  C    . GLN   B 1 143 ? -38.407 -42.968 4.133   1.00 16.80  ? 143 GLN   B C    1 
ATOM   2926 O  O    . GLN   B 1 143 ? -38.348 -41.765 4.412   1.00 17.32  ? 143 GLN   B O    1 
ATOM   2927 C  CB   . GLN   B 1 143 ? -38.745 -43.430 1.643   1.00 16.83  ? 143 GLN   B CB   1 
ATOM   2928 C  CG   . GLN   B 1 143 ? -39.544 -44.206 0.605   1.00 16.14  ? 143 GLN   B CG   1 
ATOM   2929 C  CD   . GLN   B 1 143 ? -38.938 -44.173 -0.773  1.00 17.06  ? 143 GLN   B CD   1 
ATOM   2930 O  OE1  . GLN   B 1 143 ? -38.147 -43.276 -1.118  1.00 17.07  ? 143 GLN   B OE1  1 
ATOM   2931 N  NE2  . GLN   B 1 143 ? -39.325 -45.143 -1.590  1.00 14.64  ? 143 GLN   B NE2  1 
ATOM   2932 N  N    . GLY   B 1 144 ? -37.697 -43.907 4.743   1.00 17.72  ? 144 GLY   B N    1 
ATOM   2933 C  CA   . GLY   B 1 144 ? -36.683 -43.639 5.779   1.00 17.27  ? 144 GLY   B CA   1 
ATOM   2934 C  C    . GLY   B 1 144 ? -37.323 -43.068 7.031   1.00 17.09  ? 144 GLY   B C    1 
ATOM   2935 O  O    . GLY   B 1 144 ? -38.225 -43.686 7.541   1.00 17.62  ? 144 GLY   B O    1 
ATOM   2936 N  N    . ASP   B 1 145 ? -36.885 -41.887 7.458   1.00 18.61  ? 145 ASP   B N    1 
ATOM   2937 C  CA   . ASP   B 1 145 ? -37.279 -41.217 8.718   1.00 18.01  ? 145 ASP   B CA   1 
ATOM   2938 C  C    . ASP   B 1 145 ? -38.414 -40.217 8.492   1.00 17.73  ? 145 ASP   B C    1 
ATOM   2939 O  O    . ASP   B 1 145 ? -38.801 -39.580 9.474   1.00 19.93  ? 145 ASP   B O    1 
ATOM   2940 C  CB   . ASP   B 1 145 ? -36.085 -40.478 9.307   1.00 19.23  ? 145 ASP   B CB   1 
ATOM   2941 C  CG   . ASP   B 1 145 ? -34.949 -41.391 9.746   1.00 20.54  ? 145 ASP   B CG   1 
ATOM   2942 O  OD1  . ASP   B 1 145 ? -35.236 -42.538 10.196  1.00 21.37  ? 145 ASP   B OD1  1 
ATOM   2943 O  OD2  . ASP   B 1 145 ? -33.789 -40.950 9.635   1.00 20.90  ? 145 ASP   B OD2  1 
ATOM   2944 N  N    . ALA   B 1 146 ? -38.924 -40.057 7.272   1.00 16.00  ? 146 ALA   B N    1 
ATOM   2945 C  CA   . ALA   B 1 146 ? -39.918 -39.003 6.942   1.00 17.29  ? 146 ALA   B CA   1 
ATOM   2946 C  C    . ALA   B 1 146 ? -41.237 -39.268 7.691   1.00 17.49  ? 146 ALA   B C    1 
ATOM   2947 O  O    . ALA   B 1 146 ? -41.667 -40.423 7.679   1.00 15.99  ? 146 ALA   B O    1 
ATOM   2948 C  CB   . ALA   B 1 146 ? -40.118 -38.934 5.442   1.00 16.64  ? 146 ALA   B CB   1 
ATOM   2949 N  N    . THR   B 1 147 ? -41.825 -38.244 8.336   1.00 18.44  ? 147 THR   B N    1 
ATOM   2950 C  CA   . THR   B 1 147 ? -43.145 -38.298 9.042   1.00 20.16  ? 147 THR   B CA   1 
ATOM   2951 C  C    . THR   B 1 147 ? -43.991 -37.069 8.667   1.00 22.49  ? 147 THR   B C    1 
ATOM   2952 O  O    . THR   B 1 147 ? -43.403 -36.054 8.226   1.00 20.63  ? 147 THR   B O    1 
ATOM   2953 C  CB   . THR   B 1 147 ? -42.983 -38.415 10.565  1.00 21.00  ? 147 THR   B CB   1 
ATOM   2954 O  OG1  . THR   B 1 147 ? -42.171 -37.339 11.042  1.00 22.88  ? 147 THR   B OG1  1 
ATOM   2955 C  CG2  . THR   B 1 147 ? -42.343 -39.718 10.996  1.00 21.19  ? 147 THR   B CG2  1 
ATOM   2956 N  N    . THR   B 1 148 ? -45.317 -37.197 8.789   1.00 24.32  ? 148 THR   B N    1 
ATOM   2957 C  CA   . THR   B 1 148 ? -46.340 -36.135 8.568   1.00 28.12  ? 148 THR   B CA   1 
ATOM   2958 C  C    . THR   B 1 148 ? -47.195 -36.027 9.832   1.00 32.73  ? 148 THR   B C    1 
ATOM   2959 O  O    . THR   B 1 148 ? -47.230 -37.032 10.569  1.00 33.17  ? 148 THR   B O    1 
ATOM   2960 C  CB   . THR   B 1 148 ? -47.257 -36.423 7.364   1.00 27.23  ? 148 THR   B CB   1 
ATOM   2961 O  OG1  . THR   B 1 148 ? -47.907 -37.687 7.530   1.00 24.94  ? 148 THR   B OG1  1 
ATOM   2962 C  CG2  . THR   B 1 148 ? -46.538 -36.421 6.030   1.00 26.85  ? 148 THR   B CG2  1 
ATOM   2963 N  N    . GLY   B 1 149 ? -47.845 -34.877 10.078  1.00 38.84  ? 149 GLY   B N    1 
ATOM   2964 C  CA   . GLY   B 1 149 ? -48.929 -34.750 11.081  1.00 43.25  ? 149 GLY   B CA   1 
ATOM   2965 C  C    . GLY   B 1 149 ? -48.640 -33.731 12.171  1.00 49.41  ? 149 GLY   B C    1 
ATOM   2966 O  O    . GLY   B 1 149 ? -49.618 -33.140 12.702  1.00 51.84  ? 149 GLY   B O    1 
ATOM   2967 N  N    . THR   B 1 150 ? -47.353 -33.537 12.490  1.00 52.84  ? 150 THR   B N    1 
ATOM   2968 C  CA   . THR   B 1 150 ? -46.815 -32.506 13.424  1.00 50.99  ? 150 THR   B CA   1 
ATOM   2969 C  C    . THR   B 1 150 ? -47.053 -31.111 12.834  1.00 48.41  ? 150 THR   B C    1 
ATOM   2970 O  O    . THR   B 1 150 ? -46.319 -30.762 11.882  1.00 45.59  ? 150 THR   B O    1 
ATOM   2971 C  CB   . THR   B 1 150 ? -45.322 -32.754 13.682  1.00 53.28  ? 150 THR   B CB   1 
ATOM   2972 O  OG1  . THR   B 1 150 ? -45.266 -33.955 14.447  1.00 52.24  ? 150 THR   B OG1  1 
ATOM   2973 C  CG2  . THR   B 1 150 ? -44.620 -31.631 14.419  1.00 55.29  ? 150 THR   B CG2  1 
ATOM   2974 N  N    . ASP   B 1 151 ? -48.060 -30.380 13.348  1.00 46.42  ? 151 ASP   B N    1 
ATOM   2975 C  CA   . ASP   B 1 151 ? -48.408 -28.983 12.955  1.00 45.01  ? 151 ASP   B CA   1 
ATOM   2976 C  C    . ASP   B 1 151 ? -48.826 -28.932 11.475  1.00 36.69  ? 151 ASP   B C    1 
ATOM   2977 O  O    . ASP   B 1 151 ? -48.700 -27.853 10.851  1.00 35.17  ? 151 ASP   B O    1 
ATOM   2978 C  CB   . ASP   B 1 151 ? -47.237 -28.018 13.209  1.00 51.48  ? 151 ASP   B CB   1 
ATOM   2979 C  CG   . ASP   B 1 151 ? -46.930 -27.769 14.680  1.00 57.45  ? 151 ASP   B CG   1 
ATOM   2980 O  OD1  . ASP   B 1 151 ? -47.910 -27.607 15.474  1.00 61.89  ? 151 ASP   B OD1  1 
ATOM   2981 O  OD2  . ASP   B 1 151 ? -45.716 -27.741 15.025  1.00 51.97  ? 151 ASP   B OD2  1 
ATOM   2982 N  N    . GLY   B 1 152 ? -49.306 -30.054 10.931  1.00 30.28  ? 152 GLY   B N    1 
ATOM   2983 C  CA   . GLY   B 1 152 ? -49.744 -30.168 9.534   1.00 24.93  ? 152 GLY   B CA   1 
ATOM   2984 C  C    . GLY   B 1 152 ? -48.560 -30.126 8.599   1.00 23.13  ? 152 GLY   B C    1 
ATOM   2985 O  O    . GLY   B 1 152 ? -48.742 -29.745 7.452   1.00 21.56  ? 152 GLY   B O    1 
ATOM   2986 N  N    . ASN   B 1 153 ? -47.373 -30.501 9.081   1.00 23.40  ? 153 ASN   B N    1 
ATOM   2987 C  CA   . ASN   B 1 153 ? -46.100 -30.377 8.328   1.00 22.14  ? 153 ASN   B CA   1 
ATOM   2988 C  C    . ASN   B 1 153 ? -45.572 -31.755 7.931   1.00 20.90  ? 153 ASN   B C    1 
ATOM   2989 O  O    . ASN   B 1 153 ? -45.994 -32.757 8.536   1.00 19.12  ? 153 ASN   B O    1 
ATOM   2990 C  CB   . ASN   B 1 153 ? -45.034 -29.624 9.120   1.00 22.04  ? 153 ASN   B CB   1 
ATOM   2991 C  CG   . ASN   B 1 153 ? -45.389 -28.176 9.356   1.00 22.11  ? 153 ASN   B CG   1 
ATOM   2992 O  OD1  . ASN   B 1 153 ? -46.048 -27.522 8.538   1.00 20.05  ? 153 ASN   B OD1  1 
ATOM   2993 N  ND2  . ASN   B 1 153 ? -44.938 -27.678 10.486  1.00 22.59  ? 153 ASN   B ND2  1 
ATOM   2994 N  N    . LEU   B 1 154 ? -44.716 -31.765 6.904   1.00 20.00  ? 154 LEU   B N    1 
ATOM   2995 C  CA   . LEU   B 1 154 ? -43.898 -32.928 6.477   1.00 20.10  ? 154 LEU   B CA   1 
ATOM   2996 C  C    . LEU   B 1 154 ? -42.471 -32.752 7.006   1.00 21.54  ? 154 LEU   B C    1 
ATOM   2997 O  O    . LEU   B 1 154 ? -41.779 -31.803 6.536   1.00 23.74  ? 154 LEU   B O    1 
ATOM   2998 C  CB   . LEU   B 1 154 ? -43.921 -32.974 4.950   1.00 19.31  ? 154 LEU   B CB   1 
ATOM   2999 C  CG   . LEU   B 1 154 ? -42.930 -33.923 4.291   1.00 18.62  ? 154 LEU   B CG   1 
ATOM   3000 C  CD1  . LEU   B 1 154 ? -43.160 -35.339 4.776   1.00 18.44  ? 154 LEU   B CD1  1 
ATOM   3001 C  CD2  . LEU   B 1 154 ? -43.028 -33.830 2.771   1.00 18.67  ? 154 LEU   B CD2  1 
ATOM   3002 N  N    . GLU   B 1 155 ? -42.050 -33.624 7.927   1.00 20.84  ? 155 GLU   B N    1 
ATOM   3003 C  CA   . GLU   B 1 155 ? -40.682 -33.656 8.511   1.00 21.08  ? 155 GLU   B CA   1 
ATOM   3004 C  C    . GLU   B 1 155 ? -39.863 -34.747 7.812   1.00 19.73  ? 155 GLU   B C    1 
ATOM   3005 O  O    . GLU   B 1 155 ? -40.020 -35.932 8.146   1.00 20.46  ? 155 GLU   B O    1 
ATOM   3006 C  CB   . GLU   B 1 155 ? -40.725 -33.926 10.016  1.00 22.64  ? 155 GLU   B CB   1 
ATOM   3007 C  CG   . GLU   B 1 155 ? -41.399 -32.823 10.813  1.00 24.90  ? 155 GLU   B CG   1 
ATOM   3008 C  CD   . GLU   B 1 155 ? -40.576 -31.556 10.984  1.00 26.74  ? 155 GLU   B CD   1 
ATOM   3009 O  OE1  . GLU   B 1 155 ? -39.500 -31.432 10.312  1.00 27.53  ? 155 GLU   B OE1  1 
ATOM   3010 O  OE2  . GLU   B 1 155 ? -41.017 -30.689 11.780  1.00 32.10  ? 155 GLU   B OE2  1 
ATOM   3011 N  N    . LEU   B 1 156 ? -39.020 -34.346 6.876   1.00 18.44  ? 156 LEU   B N    1 
ATOM   3012 C  CA   . LEU   B 1 156 ? -38.261 -35.284 6.032   1.00 19.82  ? 156 LEU   B CA   1 
ATOM   3013 C  C    . LEU   B 1 156 ? -37.210 -36.012 6.889   1.00 20.35  ? 156 LEU   B C    1 
ATOM   3014 O  O    . LEU   B 1 156 ? -37.050 -37.211 6.675   1.00 21.07  ? 156 LEU   B O    1 
ATOM   3015 C  CB   . LEU   B 1 156 ? -37.665 -34.519 4.851   1.00 19.46  ? 156 LEU   B CB   1 
ATOM   3016 C  CG   . LEU   B 1 156 ? -38.667 -34.082 3.790   1.00 20.32  ? 156 LEU   B CG   1 
ATOM   3017 C  CD1  . LEU   B 1 156 ? -38.021 -33.176 2.749   1.00 21.32  ? 156 LEU   B CD1  1 
ATOM   3018 C  CD2  . LEU   B 1 156 ? -39.274 -35.292 3.111   1.00 21.11  ? 156 LEU   B CD2  1 
ATOM   3019 N  N    . THR   B 1 157 ? -36.608 -35.359 7.883   1.00 19.58  ? 157 THR   B N    1 
ATOM   3020 C  CA   . THR   B 1 157 ? -35.585 -35.964 8.779   1.00 21.20  ? 157 THR   B CA   1 
ATOM   3021 C  C    . THR   B 1 157 ? -36.103 -35.973 10.222  1.00 22.17  ? 157 THR   B C    1 
ATOM   3022 O  O    . THR   B 1 157 ? -37.076 -35.249 10.507  1.00 20.68  ? 157 THR   B O    1 
ATOM   3023 C  CB   . THR   B 1 157 ? -34.231 -35.268 8.577   1.00 20.55  ? 157 THR   B CB   1 
ATOM   3024 O  OG1  . THR   B 1 157 ? -34.382 -33.844 8.655   1.00 22.90  ? 157 THR   B OG1  1 
ATOM   3025 C  CG2  . THR   B 1 157 ? -33.629 -35.607 7.233   1.00 20.75  ? 157 THR   B CG2  1 
ATOM   3026 N  N    . ARG   B 1 158 ? -35.504 -36.811 11.069  1.00 26.54  ? 158 ARG   B N    1 
ATOM   3027 C  CA   . ARG   B 1 158 ? -35.825 -36.946 12.518  1.00 32.51  ? 158 ARG   B CA   1 
ATOM   3028 C  C    . ARG   B 1 158 ? -35.649 -35.610 13.236  1.00 31.32  ? 158 ARG   B C    1 
ATOM   3029 O  O    . ARG   B 1 158 ? -34.516 -35.075 13.251  1.00 31.05  ? 158 ARG   B O    1 
ATOM   3030 C  CB   . ARG   B 1 158 ? -34.876 -37.894 13.253  1.00 38.37  ? 158 ARG   B CB   1 
ATOM   3031 C  CG   . ARG   B 1 158 ? -35.270 -39.358 13.249  1.00 45.14  ? 158 ARG   B CG   1 
ATOM   3032 C  CD   . ARG   B 1 158 ? -36.612 -39.657 13.902  1.00 51.26  ? 158 ARG   B CD   1 
ATOM   3033 N  NE   . ARG   B 1 158 ? -37.269 -40.876 13.406  1.00 54.53  ? 158 ARG   B NE   1 
ATOM   3034 C  CZ   . ARG   B 1 158 ? -36.678 -42.053 13.161  1.00 59.82  ? 158 ARG   B CZ   1 
ATOM   3035 N  NH1  . ARG   B 1 158 ? -37.420 -43.063 12.733  1.00 62.60  ? 158 ARG   B NH1  1 
ATOM   3036 N  NH2  . ARG   B 1 158 ? -35.376 -42.238 13.349  1.00 57.19  ? 158 ARG   B NH2  1 
ATOM   3037 N  N    . VAL   B 1 159 ? -36.726 -35.136 13.844  1.00 33.14  ? 159 VAL   B N    1 
ATOM   3038 C  CA   . VAL   B 1 159 ? -36.724 -34.052 14.859  1.00 33.91  ? 159 VAL   B CA   1 
ATOM   3039 C  C    . VAL   B 1 159 ? -37.323 -34.654 16.129  1.00 36.50  ? 159 VAL   B C    1 
ATOM   3040 O  O    . VAL   B 1 159 ? -38.347 -35.336 16.000  1.00 37.90  ? 159 VAL   B O    1 
ATOM   3041 C  CB   . VAL   B 1 159 ? -37.508 -32.830 14.362  1.00 35.78  ? 159 VAL   B CB   1 
ATOM   3042 C  CG1  . VAL   B 1 159 ? -37.358 -31.649 15.311  1.00 37.93  ? 159 VAL   B CG1  1 
ATOM   3043 C  CG2  . VAL   B 1 159 ? -37.095 -32.436 12.947  1.00 36.36  ? 159 VAL   B CG2  1 
ATOM   3044 N  N    . SER   B 1 160 ? -36.681 -34.442 17.286  1.00 39.14  ? 160 SER   B N    1 
ATOM   3045 C  CA   . SER   B 1 160 ? -37.207 -34.770 18.643  1.00 37.97  ? 160 SER   B CA   1 
ATOM   3046 C  C    . SER   B 1 160 ? -38.458 -33.938 18.905  1.00 36.59  ? 160 SER   B C    1 
ATOM   3047 O  O    . SER   B 1 160 ? -38.665 -32.941 18.174  1.00 35.47  ? 160 SER   B O    1 
ATOM   3048 C  CB   . SER   B 1 160 ? -36.181 -34.529 19.711  1.00 38.15  ? 160 SER   B CB   1 
ATOM   3049 O  OG   . SER   B 1 160 ? -35.147 -35.498 19.629  1.00 39.27  ? 160 SER   B OG   1 
ATOM   3050 N  N    . SER   B 1 161 ? -39.239 -34.311 19.924  1.00 37.86  ? 161 SER   B N    1 
ATOM   3051 C  CA   . SER   B 1 161 ? -40.490 -33.603 20.308  1.00 37.78  ? 161 SER   B CA   1 
ATOM   3052 C  C    . SER   B 1 161 ? -40.172 -32.137 20.634  1.00 40.25  ? 161 SER   B C    1 
ATOM   3053 O  O    . SER   B 1 161 ? -40.981 -31.255 20.230  1.00 41.95  ? 161 SER   B O    1 
ATOM   3054 C  CB   . SER   B 1 161 ? -41.191 -34.289 21.436  1.00 37.68  ? 161 SER   B CB   1 
ATOM   3055 O  OG   . SER   B 1 161 ? -40.331 -34.441 22.553  1.00 40.57  ? 161 SER   B OG   1 
ATOM   3056 N  N    . ASN   B 1 162 ? -39.025 -31.872 21.277  1.00 39.51  ? 162 ASN   B N    1 
ATOM   3057 C  CA   . ASN   B 1 162 ? -38.611 -30.502 21.697  1.00 41.42  ? 162 ASN   B CA   1 
ATOM   3058 C  C    . ASN   B 1 162 ? -38.018 -29.716 20.522  1.00 43.20  ? 162 ASN   B C    1 
ATOM   3059 O  O    . ASN   B 1 162 ? -37.587 -28.568 20.763  1.00 45.72  ? 162 ASN   B O    1 
ATOM   3060 C  CB   . ASN   B 1 162 ? -37.558 -30.523 22.801  1.00 41.80  ? 162 ASN   B CB   1 
ATOM   3061 C  CG   . ASN   B 1 162 ? -36.184 -30.867 22.279  1.00 41.94  ? 162 ASN   B CG   1 
ATOM   3062 O  OD1  . ASN   B 1 162 ? -36.040 -31.271 21.129  1.00 43.19  ? 162 ASN   B OD1  1 
ATOM   3063 N  ND2  . ASN   B 1 162 ? -35.179 -30.724 23.124  1.00 42.47  ? 162 ASN   B ND2  1 
ATOM   3064 N  N    . GLY   B 1 163 ? -37.909 -30.333 19.338  1.00 40.37  ? 163 GLY   B N    1 
ATOM   3065 C  CA   . GLY   B 1 163 ? -37.592 -29.633 18.077  1.00 38.52  ? 163 GLY   B CA   1 
ATOM   3066 C  C    . GLY   B 1 163 ? -36.125 -29.731 17.690  1.00 35.92  ? 163 GLY   B C    1 
ATOM   3067 O  O    . GLY   B 1 163 ? -35.733 -29.017 16.755  1.00 38.96  ? 163 GLY   B O    1 
ATOM   3068 N  N    . SER   B 1 164 ? -35.348 -30.603 18.334  1.00 31.57  ? 164 SER   B N    1 
ATOM   3069 C  CA   . SER   B 1 164 ? -33.900 -30.797 18.054  1.00 31.56  ? 164 SER   B CA   1 
ATOM   3070 C  C    . SER   B 1 164 ? -33.733 -31.775 16.892  1.00 29.69  ? 164 SER   B C    1 
ATOM   3071 O  O    . SER   B 1 164 ? -34.107 -32.940 16.976  1.00 26.08  ? 164 SER   B O    1 
ATOM   3072 C  CB   . SER   B 1 164 ? -33.167 -31.269 19.281  1.00 32.29  ? 164 SER   B CB   1 
ATOM   3073 O  OG   . SER   B 1 164 ? -33.635 -30.570 20.423  1.00 32.64  ? 164 SER   B OG   1 
ATOM   3074 N  N    . PRO   B 1 165 ? -33.176 -31.334 15.750  1.00 29.62  ? 165 PRO   B N    1 
ATOM   3075 C  CA   . PRO   B 1 165 ? -32.905 -32.252 14.654  1.00 28.87  ? 165 PRO   B CA   1 
ATOM   3076 C  C    . PRO   B 1 165 ? -31.801 -33.214 15.096  1.00 30.07  ? 165 PRO   B C    1 
ATOM   3077 O  O    . PRO   B 1 165 ? -31.024 -32.856 15.959  1.00 33.33  ? 165 PRO   B O    1 
ATOM   3078 C  CB   . PRO   B 1 165 ? -32.464 -31.344 13.509  1.00 28.90  ? 165 PRO   B CB   1 
ATOM   3079 C  CG   . PRO   B 1 165 ? -31.897 -30.119 14.220  1.00 29.74  ? 165 PRO   B CG   1 
ATOM   3080 C  CD   . PRO   B 1 165 ? -32.752 -29.953 15.459  1.00 29.71  ? 165 PRO   B CD   1 
ATOM   3081 N  N    . GLN   B 1 166 ? -31.799 -34.408 14.504  1.00 31.51  ? 166 GLN   B N    1 
ATOM   3082 C  CA   . GLN   B 1 166 ? -30.831 -35.507 14.732  1.00 29.90  ? 166 GLN   B CA   1 
ATOM   3083 C  C    . GLN   B 1 166 ? -29.940 -35.653 13.498  1.00 26.95  ? 166 GLN   B C    1 
ATOM   3084 O  O    . GLN   B 1 166 ? -30.408 -35.416 12.363  1.00 22.72  ? 166 GLN   B O    1 
ATOM   3085 C  CB   . GLN   B 1 166 ? -31.581 -36.807 15.011  1.00 33.41  ? 166 GLN   B CB   1 
ATOM   3086 C  CG   . GLN   B 1 166 ? -32.749 -36.633 15.979  1.00 37.99  ? 166 GLN   B CG   1 
ATOM   3087 C  CD   . GLN   B 1 166 ? -32.326 -36.172 17.354  1.00 39.09  ? 166 GLN   B CD   1 
ATOM   3088 O  OE1  . GLN   B 1 166 ? -31.384 -36.699 17.947  1.00 39.84  ? 166 GLN   B OE1  1 
ATOM   3089 N  NE2  . GLN   B 1 166 ? -33.031 -35.181 17.878  1.00 38.73  ? 166 GLN   B NE2  1 
ATOM   3090 N  N    . GLY   B 1 167 ? -28.682 -36.008 13.729  1.00 27.00  ? 167 GLY   B N    1 
ATOM   3091 C  CA   . GLY   B 1 167 ? -27.702 -36.288 12.667  1.00 24.91  ? 167 GLY   B CA   1 
ATOM   3092 C  C    . GLY   B 1 167 ? -27.921 -37.668 12.095  1.00 22.97  ? 167 GLY   B C    1 
ATOM   3093 O  O    . GLY   B 1 167 ? -28.733 -38.425 12.660  1.00 23.28  ? 167 GLY   B O    1 
ATOM   3094 N  N    . SER   B 1 168 ? -27.213 -37.973 11.008  1.00 22.64  ? 168 SER   B N    1 
ATOM   3095 C  CA   . SER   B 1 168 ? -27.227 -39.286 10.322  1.00 23.41  ? 168 SER   B CA   1 
ATOM   3096 C  C    . SER   B 1 168 ? -28.680 -39.707 10.039  1.00 21.12  ? 168 SER   B C    1 
ATOM   3097 O  O    . SER   B 1 168 ? -29.023 -40.865 10.271  1.00 20.43  ? 168 SER   B O    1 
ATOM   3098 C  CB   . SER   B 1 168 ? -26.444 -40.282 11.159  1.00 25.41  ? 168 SER   B CB   1 
ATOM   3099 O  OG   . SER   B 1 168 ? -25.081 -39.852 11.271  1.00 26.86  ? 168 SER   B OG   1 
ATOM   3100 N  N    . SER   B 1 169 ? -29.508 -38.778 9.562   1.00 18.57  ? 169 SER   B N    1 
ATOM   3101 C  CA   . SER   B 1 169 ? -30.936 -39.014 9.240   1.00 18.90  ? 169 SER   B CA   1 
ATOM   3102 C  C    . SER   B 1 169 ? -31.163 -38.867 7.728   1.00 18.48  ? 169 SER   B C    1 
ATOM   3103 O  O    . SER   B 1 169 ? -30.427 -38.077 7.055   1.00 17.69  ? 169 SER   B O    1 
ATOM   3104 C  CB   . SER   B 1 169 ? -31.832 -38.099 10.043  1.00 19.02  ? 169 SER   B CB   1 
ATOM   3105 O  OG   . SER   B 1 169 ? -33.196 -38.435 9.843   1.00 20.15  ? 169 SER   B OG   1 
ATOM   3106 N  N    . VAL   B 1 170 ? -32.120 -39.623 7.196   1.00 17.51  ? 170 VAL   B N    1 
ATOM   3107 C  CA   . VAL   B 1 170 ? -32.532 -39.527 5.769   1.00 17.85  ? 170 VAL   B CA   1 
ATOM   3108 C  C    . VAL   B 1 170 ? -34.026 -39.857 5.673   1.00 17.77  ? 170 VAL   B C    1 
ATOM   3109 O  O    . VAL   B 1 170 ? -34.506 -40.761 6.369   1.00 17.08  ? 170 VAL   B O    1 
ATOM   3110 C  CB   . VAL   B 1 170 ? -31.674 -40.410 4.846   1.00 18.68  ? 170 VAL   B CB   1 
ATOM   3111 C  CG1  . VAL   B 1 170 ? -31.800 -41.885 5.172   1.00 19.29  ? 170 VAL   B CG1  1 
ATOM   3112 C  CG2  . VAL   B 1 170 ? -32.003 -40.190 3.384   1.00 20.06  ? 170 VAL   B CG2  1 
ATOM   3113 N  N    . GLY   B 1 171 ? -34.737 -39.116 4.839   1.00 18.57  ? 171 GLY   B N    1 
ATOM   3114 C  CA   . GLY   B 1 171 ? -36.188 -39.293 4.646   1.00 19.14  ? 171 GLY   B CA   1 
ATOM   3115 C  C    . GLY   B 1 171 ? -36.634 -38.726 3.314   1.00 18.41  ? 171 GLY   B C    1 
ATOM   3116 O  O    . GLY   B 1 171 ? -35.987 -37.789 2.807   1.00 18.71  ? 171 GLY   B O    1 
ATOM   3117 N  N    . ARG   B 1 172 ? -37.700 -39.277 2.759   1.00 16.92  ? 172 ARG   B N    1 
ATOM   3118 C  CA   . ARG   B 1 172 ? -38.232 -38.850 1.447   1.00 16.89  ? 172 ARG   B CA   1 
ATOM   3119 C  C    . ARG   B 1 172 ? -39.753 -38.959 1.489   1.00 15.72  ? 172 ARG   B C    1 
ATOM   3120 O  O    . ARG   B 1 172 ? -40.276 -39.789 2.241   1.00 15.68  ? 172 ARG   B O    1 
ATOM   3121 C  CB   . ARG   B 1 172 ? -37.651 -39.699 0.307   1.00 16.24  ? 172 ARG   B CB   1 
ATOM   3122 C  CG   . ARG   B 1 172 ? -36.143 -39.867 0.371   1.00 16.74  ? 172 ARG   B CG   1 
ATOM   3123 C  CD   . ARG   B 1 172 ? -35.459 -40.287 -0.912  1.00 17.09  ? 172 ARG   B CD   1 
ATOM   3124 N  NE   . ARG   B 1 172 ? -36.087 -41.383 -1.632  1.00 17.33  ? 172 ARG   B NE   1 
ATOM   3125 C  CZ   . ARG   B 1 172 ? -35.565 -41.978 -2.705  1.00 17.18  ? 172 ARG   B CZ   1 
ATOM   3126 N  NH1  . ARG   B 1 172 ? -34.385 -41.603 -3.160  1.00 16.48  ? 172 ARG   B NH1  1 
ATOM   3127 N  NH2  . ARG   B 1 172 ? -36.228 -42.945 -3.327  1.00 17.88  ? 172 ARG   B NH2  1 
ATOM   3128 N  N    . ALA   B 1 173 ? -40.414 -38.160 0.671   1.00 16.17  ? 173 ALA   B N    1 
ATOM   3129 C  CA   . ALA   B 1 173 ? -41.856 -38.273 0.369   1.00 15.75  ? 173 ALA   B CA   1 
ATOM   3130 C  C    . ALA   B 1 173 ? -42.022 -38.290 -1.144  1.00 16.27  ? 173 ALA   B C    1 
ATOM   3131 O  O    . ALA   B 1 173 ? -41.501 -37.375 -1.801  1.00 16.15  ? 173 ALA   B O    1 
ATOM   3132 C  CB   . ALA   B 1 173 ? -42.592 -37.125 1.010   1.00 16.34  ? 173 ALA   B CB   1 
ATOM   3133 N  N    . LEU   B 1 174 ? -42.673 -39.321 -1.672  1.00 16.31  ? 174 LEU   B N    1 
ATOM   3134 C  CA   . LEU   B 1 174 ? -42.999 -39.408 -3.104  1.00 17.53  ? 174 LEU   B CA   1 
ATOM   3135 C  C    . LEU   B 1 174 ? -44.515 -39.340 -3.257  1.00 18.12  ? 174 LEU   B C    1 
ATOM   3136 O  O    . LEU   B 1 174 ? -45.227 -39.889 -2.407  1.00 17.53  ? 174 LEU   B O    1 
ATOM   3137 C  CB   . LEU   B 1 174 ? -42.446 -40.714 -3.670  1.00 18.69  ? 174 LEU   B CB   1 
ATOM   3138 C  CG   . LEU   B 1 174 ? -40.924 -40.795 -3.668  1.00 19.78  ? 174 LEU   B CG   1 
ATOM   3139 C  CD1  . LEU   B 1 174 ? -40.419 -41.413 -2.360  1.00 20.50  ? 174 LEU   B CD1  1 
ATOM   3140 C  CD2  . LEU   B 1 174 ? -40.432 -41.564 -4.865  1.00 20.07  ? 174 LEU   B CD2  1 
ATOM   3141 N  N    . PHE   B 1 175 ? -44.983 -38.702 -4.318  1.00 17.88  ? 175 PHE   B N    1 
ATOM   3142 C  CA   . PHE   B 1 175 ? -46.423 -38.721 -4.650  1.00 18.58  ? 175 PHE   B CA   1 
ATOM   3143 C  C    . PHE   B 1 175 ? -46.765 -40.147 -5.107  1.00 19.16  ? 175 PHE   B C    1 
ATOM   3144 O  O    . PHE   B 1 175 ? -45.994 -40.750 -5.901  1.00 19.28  ? 175 PHE   B O    1 
ATOM   3145 C  CB   . PHE   B 1 175 ? -46.761 -37.649 -5.682  1.00 17.44  ? 175 PHE   B CB   1 
ATOM   3146 C  CG   . PHE   B 1 175 ? -48.245 -37.501 -5.890  1.00 17.53  ? 175 PHE   B CG   1 
ATOM   3147 C  CD1  . PHE   B 1 175 ? -49.055 -37.060 -4.855  1.00 17.38  ? 175 PHE   B CD1  1 
ATOM   3148 C  CD2  . PHE   B 1 175 ? -48.837 -37.854 -7.095  1.00 18.04  ? 175 PHE   B CD2  1 
ATOM   3149 C  CE1  . PHE   B 1 175 ? -50.431 -36.981 -5.024  1.00 17.68  ? 175 PHE   B CE1  1 
ATOM   3150 C  CE2  . PHE   B 1 175 ? -50.213 -37.745 -7.271  1.00 17.66  ? 175 PHE   B CE2  1 
ATOM   3151 C  CZ   . PHE   B 1 175 ? -51.002 -37.303 -6.235  1.00 17.07  ? 175 PHE   B CZ   1 
ATOM   3152 N  N    . TYR   B 1 176 ? -47.889 -40.660 -4.622  1.00 19.63  ? 176 TYR   B N    1 
ATOM   3153 C  CA   . TYR   B 1 176 ? -48.303 -42.070 -4.788  1.00 22.04  ? 176 TYR   B CA   1 
ATOM   3154 C  C    . TYR   B 1 176 ? -48.391 -42.423 -6.277  1.00 20.69  ? 176 TYR   B C    1 
ATOM   3155 O  O    . TYR   B 1 176 ? -48.004 -43.534 -6.636  1.00 19.96  ? 176 TYR   B O    1 
ATOM   3156 C  CB   . TYR   B 1 176 ? -49.622 -42.351 -4.068  1.00 25.12  ? 176 TYR   B CB   1 
ATOM   3157 C  CG   . TYR   B 1 176 ? -49.788 -43.811 -3.769  1.00 29.08  ? 176 TYR   B CG   1 
ATOM   3158 C  CD1  . TYR   B 1 176 ? -49.174 -44.372 -2.665  1.00 33.65  ? 176 TYR   B CD1  1 
ATOM   3159 C  CD2  . TYR   B 1 176 ? -50.498 -44.640 -4.620  1.00 33.35  ? 176 TYR   B CD2  1 
ATOM   3160 C  CE1  . TYR   B 1 176 ? -49.280 -45.725 -2.395  1.00 37.85  ? 176 TYR   B CE1  1 
ATOM   3161 C  CE2  . TYR   B 1 176 ? -50.616 -45.998 -4.365  1.00 35.04  ? 176 TYR   B CE2  1 
ATOM   3162 C  CZ   . TYR   B 1 176 ? -49.996 -46.539 -3.253  1.00 36.52  ? 176 TYR   B CZ   1 
ATOM   3163 O  OH   . TYR   B 1 176 ? -50.070 -47.870 -2.999  1.00 40.52  ? 176 TYR   B OH   1 
ATOM   3164 N  N    . ALA   B 1 177 ? -48.817 -41.487 -7.125  1.00 20.40  ? 177 ALA   B N    1 
ATOM   3165 C  CA   . ALA   B 1 177 ? -49.148 -41.767 -8.543  1.00 20.43  ? 177 ALA   B CA   1 
ATOM   3166 C  C    . ALA   B 1 177 ? -47.932 -41.540 -9.428  1.00 19.75  ? 177 ALA   B C    1 
ATOM   3167 O  O    . ALA   B 1 177 ? -47.357 -40.463 -9.429  1.00 19.88  ? 177 ALA   B O    1 
ATOM   3168 C  CB   . ALA   B 1 177 ? -50.308 -40.928 -9.008  1.00 20.10  ? 177 ALA   B CB   1 
ATOM   3169 N  N    . PRO   B 1 178 ? -47.572 -42.518 -10.285 1.00 19.80  ? 178 PRO   B N    1 
ATOM   3170 C  CA   . PRO   B 1 178 ? -46.666 -42.252 -11.394 1.00 20.11  ? 178 PRO   B CA   1 
ATOM   3171 C  C    . PRO   B 1 178 ? -47.140 -41.076 -12.267 1.00 20.62  ? 178 PRO   B C    1 
ATOM   3172 O  O    . PRO   B 1 178 ? -48.368 -40.809 -12.380 1.00 20.70  ? 178 PRO   B O    1 
ATOM   3173 C  CB   . PRO   B 1 178 ? -46.666 -43.553 -12.206 1.00 20.23  ? 178 PRO   B CB   1 
ATOM   3174 C  CG   . PRO   B 1 178 ? -47.137 -44.618 -11.228 1.00 20.55  ? 178 PRO   B CG   1 
ATOM   3175 C  CD   . PRO   B 1 178 ? -48.080 -43.900 -10.290 1.00 20.68  ? 178 PRO   B CD   1 
ATOM   3176 N  N    . VAL   B 1 179 ? -46.165 -40.398 -12.867 1.00 20.06  ? 179 VAL   B N    1 
ATOM   3177 C  CA   . VAL   B 1 179 ? -46.382 -39.210 -13.726 1.00 22.35  ? 179 VAL   B CA   1 
ATOM   3178 C  C    . VAL   B 1 179 ? -45.879 -39.572 -15.115 1.00 23.02  ? 179 VAL   B C    1 
ATOM   3179 O  O    . VAL   B 1 179 ? -44.861 -40.251 -15.191 1.00 24.23  ? 179 VAL   B O    1 
ATOM   3180 C  CB   . VAL   B 1 179 ? -45.654 -37.986 -13.151 1.00 23.96  ? 179 VAL   B CB   1 
ATOM   3181 C  CG1  . VAL   B 1 179 ? -46.017 -36.727 -13.917 1.00 24.43  ? 179 VAL   B CG1  1 
ATOM   3182 C  CG2  . VAL   B 1 179 ? -45.938 -37.824 -11.659 1.00 24.62  ? 179 VAL   B CG2  1 
ATOM   3183 N  N    . HIS   B 1 180 ? -46.586 -39.169 -16.161 1.00 24.30  ? 180 HIS   B N    1 
ATOM   3184 C  CA   . HIS   B 1 180 ? -46.180 -39.443 -17.560 1.00 27.74  ? 180 HIS   B CA   1 
ATOM   3185 C  C    . HIS   B 1 180 ? -45.348 -38.251 -18.041 1.00 28.83  ? 180 HIS   B C    1 
ATOM   3186 O  O    . HIS   B 1 180 ? -45.913 -37.165 -18.202 1.00 28.42  ? 180 HIS   B O    1 
ATOM   3187 C  CB   . HIS   B 1 180 ? -47.420 -39.768 -18.401 1.00 28.49  ? 180 HIS   B CB   1 
ATOM   3188 C  CG   . HIS   B 1 180 ? -47.122 -40.565 -19.625 1.00 28.38  ? 180 HIS   B CG   1 
ATOM   3189 N  ND1  . HIS   B 1 180 ? -48.076 -40.809 -20.589 1.00 28.77  ? 180 HIS   B ND1  1 
ATOM   3190 C  CD2  . HIS   B 1 180 ? -45.976 -41.124 -20.071 1.00 28.39  ? 180 HIS   B CD2  1 
ATOM   3191 C  CE1  . HIS   B 1 180 ? -47.539 -41.505 -21.572 1.00 28.18  ? 180 HIS   B CE1  1 
ATOM   3192 N  NE2  . HIS   B 1 180 ? -46.251 -41.713 -21.275 1.00 30.05  ? 180 HIS   B NE2  1 
ATOM   3193 N  N    . ILE   B 1 181 ? -44.038 -38.440 -18.201 1.00 32.52  ? 181 ILE   B N    1 
ATOM   3194 C  CA   . ILE   B 1 181 ? -43.056 -37.316 -18.278 1.00 34.29  ? 181 ILE   B CA   1 
ATOM   3195 C  C    . ILE   B 1 181 ? -42.640 -37.082 -19.739 1.00 34.09  ? 181 ILE   B C    1 
ATOM   3196 O  O    . ILE   B 1 181 ? -42.358 -35.915 -20.069 1.00 33.11  ? 181 ILE   B O    1 
ATOM   3197 C  CB   . ILE   B 1 181 ? -41.880 -37.574 -17.311 1.00 37.58  ? 181 ILE   B CB   1 
ATOM   3198 C  CG1  . ILE   B 1 181 ? -41.465 -36.288 -16.597 1.00 41.87  ? 181 ILE   B CG1  1 
ATOM   3199 C  CG2  . ILE   B 1 181 ? -40.699 -38.257 -17.979 1.00 37.70  ? 181 ILE   B CG2  1 
ATOM   3200 C  CD1  . ILE   B 1 181 ? -42.506 -35.785 -15.621 1.00 41.78  ? 181 ILE   B CD1  1 
ATOM   3201 N  N    . TRP   B 1 182 ? -42.656 -38.121 -20.588 1.00 34.00  ? 182 TRP   B N    1 
ATOM   3202 C  CA   . TRP   B 1 182 ? -42.557 -37.975 -22.066 1.00 36.61  ? 182 TRP   B CA   1 
ATOM   3203 C  C    . TRP   B 1 182 ? -43.206 -39.166 -22.777 1.00 39.19  ? 182 TRP   B C    1 
ATOM   3204 O  O    . TRP   B 1 182 ? -43.440 -40.187 -22.107 1.00 38.34  ? 182 TRP   B O    1 
ATOM   3205 C  CB   . TRP   B 1 182 ? -41.095 -37.796 -22.505 1.00 37.89  ? 182 TRP   B CB   1 
ATOM   3206 C  CG   . TRP   B 1 182 ? -40.144 -38.872 -22.077 1.00 36.22  ? 182 TRP   B CG   1 
ATOM   3207 C  CD1  . TRP   B 1 182 ? -39.371 -38.874 -20.956 1.00 37.12  ? 182 TRP   B CD1  1 
ATOM   3208 C  CD2  . TRP   B 1 182 ? -39.839 -40.095 -22.773 1.00 37.74  ? 182 TRP   B CD2  1 
ATOM   3209 N  NE1  . TRP   B 1 182 ? -38.603 -40.008 -20.905 1.00 37.90  ? 182 TRP   B NE1  1 
ATOM   3210 C  CE2  . TRP   B 1 182 ? -38.867 -40.777 -22.005 1.00 38.35  ? 182 TRP   B CE2  1 
ATOM   3211 C  CE3  . TRP   B 1 182 ? -40.274 -40.674 -23.972 1.00 37.37  ? 182 TRP   B CE3  1 
ATOM   3212 C  CZ2  . TRP   B 1 182 ? -38.349 -42.015 -22.386 1.00 39.15  ? 182 TRP   B CZ2  1 
ATOM   3213 C  CZ3  . TRP   B 1 182 ? -39.747 -41.885 -24.357 1.00 38.96  ? 182 TRP   B CZ3  1 
ATOM   3214 C  CH2  . TRP   B 1 182 ? -38.796 -42.544 -23.577 1.00 40.87  ? 182 TRP   B CH2  1 
ATOM   3215 N  N    . GLU   B 1 183 ? -43.454 -39.021 -24.087 1.00 45.03  ? 183 GLU   B N    1 
ATOM   3216 C  CA   . GLU   B 1 183 ? -44.030 -40.065 -24.985 1.00 52.25  ? 183 GLU   B CA   1 
ATOM   3217 C  C    . GLU   B 1 183 ? -43.062 -40.405 -26.130 1.00 54.50  ? 183 GLU   B C    1 
ATOM   3218 O  O    . GLU   B 1 183 ? -42.916 -41.607 -26.428 1.00 57.46  ? 183 GLU   B O    1 
ATOM   3219 C  CB   . GLU   B 1 183 ? -45.370 -39.626 -25.571 1.00 54.50  ? 183 GLU   B CB   1 
ATOM   3220 C  CG   . GLU   B 1 183 ? -46.552 -39.895 -24.662 1.00 59.90  ? 183 GLU   B CG   1 
ATOM   3221 C  CD   . GLU   B 1 183 ? -47.894 -40.017 -25.368 1.00 67.91  ? 183 GLU   B CD   1 
ATOM   3222 O  OE1  . GLU   B 1 183 ? -47.949 -39.740 -26.596 1.00 67.71  ? 183 GLU   B OE1  1 
ATOM   3223 O  OE2  . GLU   B 1 183 ? -48.887 -40.389 -24.688 1.00 72.78  ? 183 GLU   B OE2  1 
ATOM   3224 N  N    . SER   B 1 184 ? -42.455 -39.401 -26.771 1.00 57.25  ? 184 SER   B N    1 
ATOM   3225 C  CA   . SER   B 1 184 ? -41.355 -39.564 -27.767 1.00 58.61  ? 184 SER   B CA   1 
ATOM   3226 C  C    . SER   B 1 184 ? -40.440 -38.327 -27.724 1.00 60.72  ? 184 SER   B C    1 
ATOM   3227 O  O    . SER   B 1 184 ? -40.650 -37.490 -26.836 1.00 56.58  ? 184 SER   B O    1 
ATOM   3228 C  CB   . SER   B 1 184 ? -41.917 -39.828 -29.157 1.00 57.61  ? 184 SER   B CB   1 
ATOM   3229 O  OG   . SER   B 1 184 ? -42.965 -38.916 -29.487 1.00 57.47  ? 184 SER   B OG   1 
ATOM   3230 N  N    . SER   B 1 185 ? -39.458 -38.211 -28.630 1.00 66.35  ? 185 SER   B N    1 
ATOM   3231 C  CA   . SER   B 1 185 ? -38.634 -36.983 -28.823 1.00 67.25  ? 185 SER   B CA   1 
ATOM   3232 C  C    . SER   B 1 185 ? -39.554 -35.779 -29.061 1.00 64.50  ? 185 SER   B C    1 
ATOM   3233 O  O    . SER   B 1 185 ? -39.227 -34.676 -28.580 1.00 66.68  ? 185 SER   B O    1 
ATOM   3234 C  CB   . SER   B 1 185 ? -37.643 -37.130 -29.958 1.00 70.80  ? 185 SER   B CB   1 
ATOM   3235 O  OG   . SER   B 1 185 ? -36.513 -37.890 -29.550 1.00 75.15  ? 185 SER   B OG   1 
ATOM   3236 N  N    . ALA   B 1 186 ? -40.674 -35.997 -29.755 1.00 59.99  ? 186 ALA   B N    1 
ATOM   3237 C  CA   . ALA   B 1 186 ? -41.602 -34.949 -30.235 1.00 59.18  ? 186 ALA   B CA   1 
ATOM   3238 C  C    . ALA   B 1 186 ? -42.587 -34.502 -29.143 1.00 59.88  ? 186 ALA   B C    1 
ATOM   3239 O  O    . ALA   B 1 186 ? -43.285 -33.496 -29.380 1.00 59.91  ? 186 ALA   B O    1 
ATOM   3240 C  CB   . ALA   B 1 186 ? -42.344 -35.466 -31.438 1.00 59.03  ? 186 ALA   B CB   1 
ATOM   3241 N  N    . VAL   B 1 187 ? -42.672 -35.215 -28.013 1.00 56.48  ? 187 VAL   B N    1 
ATOM   3242 C  CA   . VAL   B 1 187 ? -43.703 -34.971 -26.955 1.00 54.18  ? 187 VAL   B CA   1 
ATOM   3243 C  C    . VAL   B 1 187 ? -43.087 -35.223 -25.571 1.00 50.86  ? 187 VAL   B C    1 
ATOM   3244 O  O    . VAL   B 1 187 ? -43.026 -36.413 -25.147 1.00 47.98  ? 187 VAL   B O    1 
ATOM   3245 C  CB   . VAL   B 1 187 ? -44.962 -35.834 -27.179 1.00 52.35  ? 187 VAL   B CB   1 
ATOM   3246 C  CG1  . VAL   B 1 187 ? -45.954 -35.704 -26.031 1.00 51.62  ? 187 VAL   B CG1  1 
ATOM   3247 C  CG2  . VAL   B 1 187 ? -45.631 -35.497 -28.501 1.00 54.07  ? 187 VAL   B CG2  1 
ATOM   3248 N  N    . VAL   B 1 188 ? -42.692 -34.134 -24.896 1.00 44.54  ? 188 VAL   B N    1 
ATOM   3249 C  CA   . VAL   B 1 188 ? -42.100 -34.124 -23.523 1.00 40.72  ? 188 VAL   B CA   1 
ATOM   3250 C  C    . VAL   B 1 188 ? -42.940 -33.204 -22.614 1.00 36.04  ? 188 VAL   B C    1 
ATOM   3251 O  O    . VAL   B 1 188 ? -43.265 -32.077 -23.010 1.00 32.90  ? 188 VAL   B O    1 
ATOM   3252 C  CB   . VAL   B 1 188 ? -40.612 -33.710 -23.561 1.00 41.59  ? 188 VAL   B CB   1 
ATOM   3253 C  CG1  . VAL   B 1 188 ? -39.950 -33.894 -22.204 1.00 41.24  ? 188 VAL   B CG1  1 
ATOM   3254 C  CG2  . VAL   B 1 188 ? -39.833 -34.472 -24.633 1.00 43.16  ? 188 VAL   B CG2  1 
ATOM   3255 N  N    . ALA   B 1 189 ? -43.256 -33.661 -21.404 1.00 34.48  ? 189 ALA   B N    1 
ATOM   3256 C  CA   . ALA   B 1 189 ? -44.045 -32.904 -20.406 1.00 33.97  ? 189 ALA   B CA   1 
ATOM   3257 C  C    . ALA   B 1 189 ? -43.322 -31.608 -20.028 1.00 31.54  ? 189 ALA   B C    1 
ATOM   3258 O  O    . ALA   B 1 189 ? -42.086 -31.649 -19.814 1.00 33.20  ? 189 ALA   B O    1 
ATOM   3259 C  CB   . ALA   B 1 189 ? -44.279 -33.760 -19.185 1.00 35.86  ? 189 ALA   B CB   1 
ATOM   3260 N  N    . SER   B 1 190 ? -44.059 -30.505 -19.944 1.00 27.74  ? 190 SER   B N    1 
ATOM   3261 C  CA   . SER   B 1 190 ? -43.725 -29.362 -19.055 1.00 28.69  ? 190 SER   B CA   1 
ATOM   3262 C  C    . SER   B 1 190 ? -44.171 -29.694 -17.621 1.00 27.87  ? 190 SER   B C    1 
ATOM   3263 O  O    . SER   B 1 190 ? -45.247 -30.334 -17.442 1.00 25.78  ? 190 SER   B O    1 
ATOM   3264 C  CB   . SER   B 1 190 ? -44.333 -28.073 -19.537 1.00 28.65  ? 190 SER   B CB   1 
ATOM   3265 O  OG   . SER   B 1 190 ? -43.585 -27.557 -20.624 1.00 31.52  ? 190 SER   B OG   1 
ATOM   3266 N  N    . PHE   B 1 191 ? -43.383 -29.309 -16.622 1.00 25.07  ? 191 PHE   B N    1 
ATOM   3267 C  CA   . PHE   B 1 191 ? -43.814 -29.440 -15.214 1.00 23.88  ? 191 PHE   B CA   1 
ATOM   3268 C  C    . PHE   B 1 191 ? -43.312 -28.257 -14.397 1.00 24.33  ? 191 PHE   B C    1 
ATOM   3269 O  O    . PHE   B 1 191 ? -42.421 -27.507 -14.839 1.00 23.17  ? 191 PHE   B O    1 
ATOM   3270 C  CB   . PHE   B 1 191 ? -43.412 -30.793 -14.634 1.00 24.47  ? 191 PHE   B CB   1 
ATOM   3271 C  CG   . PHE   B 1 191 ? -41.932 -31.043 -14.517 1.00 24.53  ? 191 PHE   B CG   1 
ATOM   3272 C  CD1  . PHE   B 1 191 ? -41.190 -30.451 -13.504 1.00 24.09  ? 191 PHE   B CD1  1 
ATOM   3273 C  CD2  . PHE   B 1 191 ? -41.299 -31.913 -15.393 1.00 24.89  ? 191 PHE   B CD2  1 
ATOM   3274 C  CE1  . PHE   B 1 191 ? -39.827 -30.682 -13.400 1.00 24.54  ? 191 PHE   B CE1  1 
ATOM   3275 C  CE2  . PHE   B 1 191 ? -39.940 -32.163 -15.276 1.00 25.43  ? 191 PHE   B CE2  1 
ATOM   3276 C  CZ   . PHE   B 1 191 ? -39.203 -31.531 -14.287 1.00 26.12  ? 191 PHE   B CZ   1 
ATOM   3277 N  N    . GLU   B 1 192 ? -43.947 -28.105 -13.236 1.00 23.41  ? 192 GLU   B N    1 
ATOM   3278 C  CA   . GLU   B 1 192 ? -43.772 -26.998 -12.266 1.00 22.81  ? 192 GLU   B CA   1 
ATOM   3279 C  C    . GLU   B 1 192 ? -43.983 -27.591 -10.864 1.00 20.04  ? 192 GLU   B C    1 
ATOM   3280 O  O    . GLU   B 1 192 ? -44.869 -28.462 -10.678 1.00 17.89  ? 192 GLU   B O    1 
ATOM   3281 C  CB   . GLU   B 1 192 ? -44.730 -25.873 -12.646 1.00 26.26  ? 192 GLU   B CB   1 
ATOM   3282 C  CG   . GLU   B 1 192 ? -44.810 -24.764 -11.626 1.00 30.22  ? 192 GLU   B CG   1 
ATOM   3283 C  CD   . GLU   B 1 192 ? -45.594 -23.550 -12.091 1.00 34.90  ? 192 GLU   B CD   1 
ATOM   3284 O  OE1  . GLU   B 1 192 ? -46.721 -23.744 -12.620 1.00 38.96  ? 192 GLU   B OE1  1 
ATOM   3285 O  OE2  . GLU   B 1 192 ? -45.077 -22.409 -11.937 1.00 37.44  ? 192 GLU   B OE2  1 
ATOM   3286 N  N    . ALA   B 1 193 ? -43.137 -27.215 -9.921  1.00 18.69  ? 193 ALA   B N    1 
ATOM   3287 C  CA   . ALA   B 1 193 ? -43.213 -27.678 -8.523  1.00 18.87  ? 193 ALA   B CA   1 
ATOM   3288 C  C    . ALA   B 1 193 ? -42.917 -26.497 -7.617  1.00 18.41  ? 193 ALA   B C    1 
ATOM   3289 O  O    . ALA   B 1 193 ? -41.989 -25.740 -7.920  1.00 19.21  ? 193 ALA   B O    1 
ATOM   3290 C  CB   . ALA   B 1 193 ? -42.248 -28.810 -8.282  1.00 20.58  ? 193 ALA   B CB   1 
ATOM   3291 N  N    . THR   B 1 194 ? -43.696 -26.336 -6.561  1.00 17.79  ? 194 THR   B N    1 
ATOM   3292 C  CA   . THR   B 1 194 ? -43.449 -25.304 -5.537  1.00 18.27  ? 194 THR   B CA   1 
ATOM   3293 C  C    . THR   B 1 194 ? -43.497 -25.998 -4.186  1.00 17.45  ? 194 THR   B C    1 
ATOM   3294 O  O    . THR   B 1 194 ? -44.332 -26.888 -4.015  1.00 17.96  ? 194 THR   B O    1 
ATOM   3295 C  CB   . THR   B 1 194 ? -44.412 -24.120 -5.706  1.00 18.87  ? 194 THR   B CB   1 
ATOM   3296 O  OG1  . THR   B 1 194 ? -44.253 -23.660 -7.048  1.00 22.21  ? 194 THR   B OG1  1 
ATOM   3297 C  CG2  . THR   B 1 194 ? -44.123 -22.969 -4.769  1.00 19.25  ? 194 THR   B CG2  1 
ATOM   3298 N  N    . PHE   B 1 195 ? -42.605 -25.614 -3.283  1.00 17.85  ? 195 PHE   B N    1 
ATOM   3299 C  CA   . PHE   B 1 195 ? -42.643 -26.033 -1.860  1.00 17.59  ? 195 PHE   B CA   1 
ATOM   3300 C  C    . PHE   B 1 195 ? -42.088 -24.905 -0.977  1.00 18.13  ? 195 PHE   B C    1 
ATOM   3301 O  O    . PHE   B 1 195 ? -41.183 -24.135 -1.409  1.00 19.22  ? 195 PHE   B O    1 
ATOM   3302 C  CB   . PHE   B 1 195 ? -41.976 -27.409 -1.700  1.00 17.76  ? 195 PHE   B CB   1 
ATOM   3303 C  CG   . PHE   B 1 195 ? -40.488 -27.481 -1.917  1.00 17.49  ? 195 PHE   B CG   1 
ATOM   3304 C  CD1  . PHE   B 1 195 ? -39.613 -27.339 -0.856  1.00 18.62  ? 195 PHE   B CD1  1 
ATOM   3305 C  CD2  . PHE   B 1 195 ? -39.961 -27.746 -3.172  1.00 18.69  ? 195 PHE   B CD2  1 
ATOM   3306 C  CE1  . PHE   B 1 195 ? -38.241 -27.440 -1.051  1.00 17.93  ? 195 PHE   B CE1  1 
ATOM   3307 C  CE2  . PHE   B 1 195 ? -38.589 -27.846 -3.363  1.00 17.98  ? 195 PHE   B CE2  1 
ATOM   3308 C  CZ   . PHE   B 1 195 ? -37.738 -27.685 -2.300  1.00 17.29  ? 195 PHE   B CZ   1 
ATOM   3309 N  N    . THR   B 1 196 ? -42.661 -24.779 0.219   1.00 17.78  ? 196 THR   B N    1 
ATOM   3310 C  CA   . THR   B 1 196 ? -42.127 -23.948 1.326   1.00 18.31  ? 196 THR   B CA   1 
ATOM   3311 C  C    . THR   B 1 196 ? -41.451 -24.873 2.343   1.00 17.26  ? 196 THR   B C    1 
ATOM   3312 O  O    . THR   B 1 196 ? -41.924 -26.011 2.547   1.00 15.20  ? 196 THR   B O    1 
ATOM   3313 C  CB   . THR   B 1 196 ? -43.227 -23.085 1.954   1.00 18.43  ? 196 THR   B CB   1 
ATOM   3314 O  OG1  . THR   B 1 196 ? -44.146 -23.985 2.581   1.00 19.97  ? 196 THR   B OG1  1 
ATOM   3315 C  CG2  . THR   B 1 196 ? -43.933 -22.195 0.947   1.00 18.65  ? 196 THR   B CG2  1 
ATOM   3316 N  N    . PHE   B 1 197 ? -40.377 -24.393 2.954   1.00 18.02  ? 197 PHE   B N    1 
ATOM   3317 C  CA   . PHE   B 1 197 ? -39.552 -25.172 3.908   1.00 18.33  ? 197 PHE   B CA   1 
ATOM   3318 C  C    . PHE   B 1 197 ? -39.085 -24.264 5.041   1.00 19.89  ? 197 PHE   B C    1 
ATOM   3319 O  O    . PHE   B 1 197 ? -39.003 -23.009 4.905   1.00 21.21  ? 197 PHE   B O    1 
ATOM   3320 C  CB   . PHE   B 1 197 ? -38.384 -25.813 3.164   1.00 19.00  ? 197 PHE   B CB   1 
ATOM   3321 C  CG   . PHE   B 1 197 ? -37.517 -24.803 2.460   1.00 19.67  ? 197 PHE   B CG   1 
ATOM   3322 C  CD1  . PHE   B 1 197 ? -37.841 -24.367 1.183   1.00 19.35  ? 197 PHE   B CD1  1 
ATOM   3323 C  CD2  . PHE   B 1 197 ? -36.401 -24.257 3.094   1.00 20.29  ? 197 PHE   B CD2  1 
ATOM   3324 C  CE1  . PHE   B 1 197 ? -37.068 -23.409 0.549   1.00 19.32  ? 197 PHE   B CE1  1 
ATOM   3325 C  CE2  . PHE   B 1 197 ? -35.607 -23.318 2.450   1.00 20.18  ? 197 PHE   B CE2  1 
ATOM   3326 C  CZ   . PHE   B 1 197 ? -35.952 -22.892 1.179   1.00 20.71  ? 197 PHE   B CZ   1 
ATOM   3327 N  N    . LEU   B 1 198 ? -38.815 -24.889 6.175   1.00 21.30  ? 198 LEU   B N    1 
ATOM   3328 C  CA   . LEU   B 1 198 ? -38.092 -24.274 7.308   1.00 22.56  ? 198 LEU   B CA   1 
ATOM   3329 C  C    . LEU   B 1 198 ? -36.850 -25.131 7.606   1.00 22.81  ? 198 LEU   B C    1 
ATOM   3330 O  O    . LEU   B 1 198 ? -37.005 -26.297 8.034   1.00 21.50  ? 198 LEU   B O    1 
ATOM   3331 C  CB   . LEU   B 1 198 ? -39.044 -24.184 8.502   1.00 24.06  ? 198 LEU   B CB   1 
ATOM   3332 C  CG   . LEU   B 1 198 ? -38.780 -23.027 9.465   1.00 25.37  ? 198 LEU   B CG   1 
ATOM   3333 C  CD1  . LEU   B 1 198 ? -39.821 -22.998 10.579  1.00 26.86  ? 198 LEU   B CD1  1 
ATOM   3334 C  CD2  . LEU   B 1 198 ? -37.390 -23.144 10.053  1.00 26.72  ? 198 LEU   B CD2  1 
ATOM   3335 N  N    . ILE   B 1 199 ? -35.665 -24.589 7.344   1.00 22.20  ? 199 ILE   B N    1 
ATOM   3336 C  CA   . ILE   B 1 199 ? -34.374 -25.202 7.761   1.00 23.19  ? 199 ILE   B CA   1 
ATOM   3337 C  C    . ILE   B 1 199 ? -33.842 -24.438 8.987   1.00 25.74  ? 199 ILE   B C    1 
ATOM   3338 O  O    . ILE   B 1 199 ? -33.464 -23.266 8.847   1.00 25.54  ? 199 ILE   B O    1 
ATOM   3339 C  CB   . ILE   B 1 199 ? -33.385 -25.229 6.584   1.00 23.26  ? 199 ILE   B CB   1 
ATOM   3340 C  CG1  . ILE   B 1 199 ? -33.972 -25.999 5.398   1.00 21.82  ? 199 ILE   B CG1  1 
ATOM   3341 C  CG2  . ILE   B 1 199 ? -32.043 -25.795 7.043   1.00 23.37  ? 199 ILE   B CG2  1 
ATOM   3342 C  CD1  . ILE   B 1 199 ? -33.143 -25.972 4.139   1.00 22.10  ? 199 ILE   B CD1  1 
ATOM   3343 N  N    . LYS   B 1 200 ? -33.855 -25.095 10.145  1.00 29.36  ? 200 LYS   B N    1 
ATOM   3344 C  CA   . LYS   B 1 200 ? -33.465 -24.566 11.478  1.00 34.91  ? 200 LYS   B CA   1 
ATOM   3345 C  C    . LYS   B 1 200 ? -32.371 -25.471 12.070  1.00 34.83  ? 200 LYS   B C    1 
ATOM   3346 O  O    . LYS   B 1 200 ? -32.502 -26.707 12.021  1.00 33.47  ? 200 LYS   B O    1 
ATOM   3347 C  CB   . LYS   B 1 200 ? -34.694 -24.541 12.392  1.00 39.04  ? 200 LYS   B CB   1 
ATOM   3348 C  CG   . LYS   B 1 200 ? -34.550 -23.802 13.715  1.00 42.15  ? 200 LYS   B CG   1 
ATOM   3349 C  CD   . LYS   B 1 200 ? -35.892 -23.465 14.371  1.00 44.62  ? 200 LYS   B CD   1 
ATOM   3350 C  CE   . LYS   B 1 200 ? -36.887 -24.616 14.456  1.00 48.33  ? 200 LYS   B CE   1 
ATOM   3351 N  NZ   . LYS   B 1 200 ? -36.518 -25.627 15.486  1.00 49.97  ? 200 LYS   B NZ   1 
ATOM   3352 N  N    . SER   B 1 201 ? -31.330 -24.871 12.620  1.00 36.43  ? 201 SER   B N    1 
ATOM   3353 C  CA   . SER   B 1 201 ? -30.171 -25.576 13.214  1.00 38.98  ? 201 SER   B CA   1 
ATOM   3354 C  C    . SER   B 1 201 ? -29.629 -24.744 14.374  1.00 41.35  ? 201 SER   B C    1 
ATOM   3355 O  O    . SER   B 1 201 ? -29.488 -23.533 14.244  1.00 40.14  ? 201 SER   B O    1 
ATOM   3356 C  CB   . SER   B 1 201 ? -29.138 -25.804 12.137  1.00 39.67  ? 201 SER   B CB   1 
ATOM   3357 O  OG   . SER   B 1 201 ? -27.924 -26.305 12.671  1.00 39.54  ? 201 SER   B OG   1 
ATOM   3358 N  N    . PRO   B 1 202 ? -29.344 -25.336 15.555  1.00 51.62  ? 202 PRO   B N    1 
ATOM   3359 C  CA   . PRO   B 1 202 ? -28.536 -24.670 16.582  1.00 55.37  ? 202 PRO   B CA   1 
ATOM   3360 C  C    . PRO   B 1 202 ? -27.018 -24.860 16.393  1.00 61.73  ? 202 PRO   B C    1 
ATOM   3361 O  O    . PRO   B 1 202 ? -26.247 -24.153 17.006  1.00 62.11  ? 202 PRO   B O    1 
ATOM   3362 C  CB   . PRO   B 1 202 ? -29.003 -25.394 17.846  1.00 56.02  ? 202 PRO   B CB   1 
ATOM   3363 C  CG   . PRO   B 1 202 ? -29.216 -26.820 17.371  1.00 54.57  ? 202 PRO   B CG   1 
ATOM   3364 C  CD   . PRO   B 1 202 ? -29.790 -26.675 15.974  1.00 55.61  ? 202 PRO   B CD   1 
ATOM   3365 N  N    . ASP   B 1 203 ? -26.628 -25.839 15.569  1.00 72.23  ? 203 ASP   B N    1 
ATOM   3366 C  CA   . ASP   B 1 203 ? -25.234 -26.058 15.093  1.00 74.60  ? 203 ASP   B CA   1 
ATOM   3367 C  C    . ASP   B 1 203 ? -24.652 -24.760 14.511  1.00 80.36  ? 203 ASP   B C    1 
ATOM   3368 O  O    . ASP   B 1 203 ? -25.430 -23.894 14.036  1.00 75.31  ? 203 ASP   B O    1 
ATOM   3369 C  CB   . ASP   B 1 203 ? -25.169 -27.122 13.990  1.00 77.32  ? 203 ASP   B CB   1 
ATOM   3370 C  CG   . ASP   B 1 203 ? -24.762 -28.526 14.418  1.00 81.73  ? 203 ASP   B CG   1 
ATOM   3371 O  OD1  . ASP   B 1 203 ? -24.329 -28.701 15.580  1.00 85.17  ? 203 ASP   B OD1  1 
ATOM   3372 O  OD2  . ASP   B 1 203 ? -24.860 -29.440 13.565  1.00 69.99  ? 203 ASP   B OD2  1 
ATOM   3373 N  N    . SER   B 1 204 ? -23.318 -24.655 14.532  1.00 82.11  ? 204 SER   B N    1 
ATOM   3374 C  CA   . SER   B 1 204 ? -22.509 -23.703 13.725  1.00 76.34  ? 204 SER   B CA   1 
ATOM   3375 C  C    . SER   B 1 204 ? -22.918 -23.848 12.253  1.00 74.60  ? 204 SER   B C    1 
ATOM   3376 O  O    . SER   B 1 204 ? -23.353 -22.840 11.629  1.00 62.31  ? 204 SER   B O    1 
ATOM   3377 C  CB   . SER   B 1 204 ? -21.033 -23.968 13.917  1.00 71.23  ? 204 SER   B CB   1 
ATOM   3378 O  OG   . SER   B 1 204 ? -20.771 -24.354 15.256  1.00 65.48  ? 204 SER   B OG   1 
ATOM   3379 N  N    . HIS   B 1 205 ? -22.805 -25.080 11.745  1.00 67.54  ? 205 HIS   B N    1 
ATOM   3380 C  CA   . HIS   B 1 205 ? -23.108 -25.464 10.343  1.00 63.94  ? 205 HIS   B CA   1 
ATOM   3381 C  C    . HIS   B 1 205 ? -24.433 -26.235 10.305  1.00 49.17  ? 205 HIS   B C    1 
ATOM   3382 O  O    . HIS   B 1 205 ? -24.591 -27.274 10.940  1.00 44.61  ? 205 HIS   B O    1 
ATOM   3383 C  CB   . HIS   B 1 205 ? -21.935 -26.270 9.745   1.00 72.47  ? 205 HIS   B CB   1 
ATOM   3384 C  CG   . HIS   B 1 205 ? -20.600 -25.583 9.723   1.00 76.09  ? 205 HIS   B CG   1 
ATOM   3385 N  ND1  . HIS   B 1 205 ? -19.748 -25.557 10.826  1.00 84.49  ? 205 HIS   B ND1  1 
ATOM   3386 C  CD2  . HIS   B 1 205 ? -19.930 -24.962 8.721   1.00 76.35  ? 205 HIS   B CD2  1 
ATOM   3387 C  CE1  . HIS   B 1 205 ? -18.634 -24.921 10.511  1.00 80.01  ? 205 HIS   B CE1  1 
ATOM   3388 N  NE2  . HIS   B 1 205 ? -18.721 -24.547 9.223   1.00 80.38  ? 205 HIS   B NE2  1 
ATOM   3389 N  N    . PRO   B 1 206 ? -25.466 -25.748 9.588   1.00 36.26  ? 206 PRO   B N    1 
ATOM   3390 C  CA   . PRO   B 1 206 ? -26.540 -26.634 9.156   1.00 29.87  ? 206 PRO   B CA   1 
ATOM   3391 C  C    . PRO   B 1 206 ? -26.021 -27.638 8.108   1.00 26.42  ? 206 PRO   B C    1 
ATOM   3392 O  O    . PRO   B 1 206 ? -25.092 -27.339 7.394   1.00 24.75  ? 206 PRO   B O    1 
ATOM   3393 C  CB   . PRO   B 1 206 ? -27.583 -25.664 8.582   1.00 31.60  ? 206 PRO   B CB   1 
ATOM   3394 C  CG   . PRO   B 1 206 ? -26.781 -24.444 8.178   1.00 32.59  ? 206 PRO   B CG   1 
ATOM   3395 C  CD   . PRO   B 1 206 ? -25.688 -24.346 9.214   1.00 32.50  ? 206 PRO   B CD   1 
ATOM   3396 N  N    . ALA   B 1 207 ? -26.615 -28.832 8.072   1.00 23.37  ? 207 ALA   B N    1 
ATOM   3397 C  CA   . ALA   B 1 207 ? -26.413 -29.867 7.031   1.00 20.83  ? 207 ALA   B CA   1 
ATOM   3398 C  C    . ALA   B 1 207 ? -27.575 -30.860 7.074   1.00 16.87  ? 207 ALA   B C    1 
ATOM   3399 O  O    . ALA   B 1 207 ? -28.193 -31.045 8.118   1.00 13.97  ? 207 ALA   B O    1 
ATOM   3400 C  CB   . ALA   B 1 207 ? -25.077 -30.540 7.238   1.00 20.84  ? 207 ALA   B CB   1 
ATOM   3401 N  N    . ASP   B 1 208 ? -27.877 -31.505 5.949   1.00 15.83  ? 208 ASP   B N    1 
ATOM   3402 C  CA   . ASP   B 1 208 ? -27.128 -31.456 4.706   1.00 16.23  ? 208 ASP   B CA   1 
ATOM   3403 C  C    . ASP   B 1 208 ? -27.940 -30.818 3.571   1.00 16.25  ? 208 ASP   B C    1 
ATOM   3404 O  O    . ASP   B 1 208 ? -27.313 -30.324 2.593   1.00 17.48  ? 208 ASP   B O    1 
ATOM   3405 C  CB   . ASP   B 1 208 ? -26.701 -32.864 4.277   1.00 16.11  ? 208 ASP   B CB   1 
ATOM   3406 C  CG   . ASP   B 1 208 ? -25.346 -33.223 4.844   1.00 16.79  ? 208 ASP   B CG   1 
ATOM   3407 O  OD1  . ASP   B 1 208 ? -25.335 -33.688 6.005   1.00 17.97  ? 208 ASP   B OD1  1 
ATOM   3408 O  OD2  . ASP   B 1 208 ? -24.325 -32.995 4.140   1.00 15.38  ? 208 ASP   B OD2  1 
ATOM   3409 N  N    . GLY   B 1 209 ? -29.265 -30.849 3.634   1.00 15.62  ? 209 GLY   B N    1 
ATOM   3410 C  CA   . GLY   B 1 209 ? -30.090 -30.199 2.597   1.00 16.36  ? 209 GLY   B CA   1 
ATOM   3411 C  C    . GLY   B 1 209 ? -31.376 -30.935 2.263   1.00 15.92  ? 209 GLY   B C    1 
ATOM   3412 O  O    . GLY   B 1 209 ? -31.623 -32.014 2.824   1.00 15.57  ? 209 GLY   B O    1 
ATOM   3413 N  N    . ILE   B 1 210 ? -32.177 -30.303 1.395   1.00 16.57  ? 210 ILE   B N    1 
ATOM   3414 C  CA   . ILE   B 1 210 ? -33.484 -30.769 0.863   1.00 15.24  ? 210 ILE   B CA   1 
ATOM   3415 C  C    . ILE   B 1 210 ? -33.332 -30.827 -0.650  1.00 15.35  ? 210 ILE   B C    1 
ATOM   3416 O  O    . ILE   B 1 210 ? -32.607 -29.964 -1.216  1.00 16.23  ? 210 ILE   B O    1 
ATOM   3417 C  CB   . ILE   B 1 210 ? -34.625 -29.822 1.278   1.00 16.08  ? 210 ILE   B CB   1 
ATOM   3418 C  CG1  . ILE   B 1 210 ? -34.743 -29.687 2.790   1.00 17.03  ? 210 ILE   B CG1  1 
ATOM   3419 C  CG2  . ILE   B 1 210 ? -35.952 -30.276 0.675   1.00 16.13  ? 210 ILE   B CG2  1 
ATOM   3420 C  CD1  . ILE   B 1 210 ? -35.718 -28.635 3.221   1.00 18.01  ? 210 ILE   B CD1  1 
ATOM   3421 N  N    . ALA   B 1 211 ? -34.003 -31.772 -1.297  1.00 14.65  ? 211 ALA   B N    1 
ATOM   3422 C  CA   . ALA   B 1 211 ? -34.008 -31.886 -2.771  1.00 14.98  ? 211 ALA   B CA   1 
ATOM   3423 C  C    . ALA   B 1 211 ? -35.425 -32.186 -3.259  1.00 14.92  ? 211 ALA   B C    1 
ATOM   3424 O  O    . ALA   B 1 211 ? -36.140 -32.894 -2.569  1.00 15.56  ? 211 ALA   B O    1 
ATOM   3425 C  CB   . ALA   B 1 211 ? -33.015 -32.945 -3.197  1.00 15.36  ? 211 ALA   B CB   1 
ATOM   3426 N  N    . PHE   B 1 212 ? -35.814 -31.589 -4.373  1.00 15.02  ? 212 PHE   B N    1 
ATOM   3427 C  CA   . PHE   B 1 212 ? -36.935 -32.050 -5.207  1.00 16.17  ? 212 PHE   B CA   1 
ATOM   3428 C  C    . PHE   B 1 212 ? -36.348 -32.974 -6.273  1.00 16.89  ? 212 PHE   B C    1 
ATOM   3429 O  O    . PHE   B 1 212 ? -35.395 -32.553 -6.947  1.00 18.04  ? 212 PHE   B O    1 
ATOM   3430 C  CB   . PHE   B 1 212 ? -37.646 -30.868 -5.853  1.00 17.05  ? 212 PHE   B CB   1 
ATOM   3431 C  CG   . PHE   B 1 212 ? -38.641 -31.299 -6.883  1.00 16.97  ? 212 PHE   B CG   1 
ATOM   3432 C  CD1  . PHE   B 1 212 ? -39.887 -31.771 -6.500  1.00 17.87  ? 212 PHE   B CD1  1 
ATOM   3433 C  CD2  . PHE   B 1 212 ? -38.317 -31.277 -8.224  1.00 17.15  ? 212 PHE   B CD2  1 
ATOM   3434 C  CE1  . PHE   B 1 212 ? -40.807 -32.196 -7.452  1.00 17.94  ? 212 PHE   B CE1  1 
ATOM   3435 C  CE2  . PHE   B 1 212 ? -39.244 -31.685 -9.177  1.00 18.41  ? 212 PHE   B CE2  1 
ATOM   3436 C  CZ   . PHE   B 1 212 ? -40.486 -32.146 -8.791  1.00 17.75  ? 212 PHE   B CZ   1 
ATOM   3437 N  N    . PHE   B 1 213 ? -36.872 -34.192 -6.407  1.00 16.67  ? 213 PHE   B N    1 
ATOM   3438 C  CA   . PHE   B 1 213 ? -36.303 -35.201 -7.325  1.00 18.03  ? 213 PHE   B CA   1 
ATOM   3439 C  C    . PHE   B 1 213 ? -37.414 -35.849 -8.153  1.00 18.43  ? 213 PHE   B C    1 
ATOM   3440 O  O    . PHE   B 1 213 ? -38.558 -35.958 -7.698  1.00 18.04  ? 213 PHE   B O    1 
ATOM   3441 C  CB   . PHE   B 1 213 ? -35.439 -36.204 -6.565  1.00 18.45  ? 213 PHE   B CB   1 
ATOM   3442 C  CG   . PHE   B 1 213 ? -36.203 -37.184 -5.723  1.00 18.65  ? 213 PHE   B CG   1 
ATOM   3443 C  CD1  . PHE   B 1 213 ? -36.609 -36.843 -4.450  1.00 18.40  ? 213 PHE   B CD1  1 
ATOM   3444 C  CD2  . PHE   B 1 213 ? -36.553 -38.430 -6.232  1.00 20.29  ? 213 PHE   B CD2  1 
ATOM   3445 C  CE1  . PHE   B 1 213 ? -37.325 -37.741 -3.676  1.00 19.01  ? 213 PHE   B CE1  1 
ATOM   3446 C  CE2  . PHE   B 1 213 ? -37.258 -39.335 -5.452  1.00 20.57  ? 213 PHE   B CE2  1 
ATOM   3447 C  CZ   . PHE   B 1 213 ? -37.645 -38.984 -4.176  1.00 19.86  ? 213 PHE   B CZ   1 
ATOM   3448 N  N    . ILE   B 1 214 ? -37.056 -36.181 -9.389  1.00 20.46  ? 214 ILE   B N    1 
ATOM   3449 C  CA   . ILE   B 1 214 ? -37.789 -37.095 -10.302 1.00 22.22  ? 214 ILE   B CA   1 
ATOM   3450 C  C    . ILE   B 1 214 ? -36.972 -38.383 -10.381 1.00 23.62  ? 214 ILE   B C    1 
ATOM   3451 O  O    . ILE   B 1 214 ? -35.723 -38.316 -10.585 1.00 24.79  ? 214 ILE   B O    1 
ATOM   3452 C  CB   . ILE   B 1 214 ? -37.972 -36.444 -11.681 1.00 23.67  ? 214 ILE   B CB   1 
ATOM   3453 C  CG1  . ILE   B 1 214 ? -38.556 -35.038 -11.570 1.00 24.54  ? 214 ILE   B CG1  1 
ATOM   3454 C  CG2  . ILE   B 1 214 ? -38.820 -37.327 -12.587 1.00 25.81  ? 214 ILE   B CG2  1 
ATOM   3455 C  CD1  . ILE   B 1 214 ? -38.146 -34.134 -12.714 1.00 25.78  ? 214 ILE   B CD1  1 
ATOM   3456 N  N    . SER   B 1 215 ? -37.625 -39.524 -10.195 1.00 24.10  ? 215 SER   B N    1 
ATOM   3457 C  CA   . SER   B 1 215 ? -36.942 -40.837 -10.215 1.00 24.25  ? 215 SER   B CA   1 
ATOM   3458 C  C    . SER   B 1 215 ? -37.753 -41.829 -11.033 1.00 26.12  ? 215 SER   B C    1 
ATOM   3459 O  O    . SER   B 1 215 ? -38.894 -41.474 -11.444 1.00 24.47  ? 215 SER   B O    1 
ATOM   3460 C  CB   . SER   B 1 215 ? -36.733 -41.338 -8.836  1.00 24.91  ? 215 SER   B CB   1 
ATOM   3461 O  OG   . SER   B 1 215 ? -37.986 -41.638 -8.232  1.00 27.02  ? 215 SER   B OG   1 
ATOM   3462 N  N    . ASN   B 1 216 ? -37.160 -43.008 -11.257 1.00 25.17  ? 216 ASN   B N    1 
ATOM   3463 C  CA   . ASN   B 1 216 ? -37.875 -44.253 -11.641 1.00 25.82  ? 216 ASN   B CA   1 
ATOM   3464 C  C    . ASN   B 1 216 ? -38.919 -44.551 -10.553 1.00 25.44  ? 216 ASN   B C    1 
ATOM   3465 O  O    . ASN   B 1 216 ? -38.684 -44.192 -9.364  1.00 22.09  ? 216 ASN   B O    1 
ATOM   3466 C  CB   . ASN   B 1 216 ? -36.885 -45.400 -11.875 1.00 27.41  ? 216 ASN   B CB   1 
ATOM   3467 C  CG   . ASN   B 1 216 ? -35.951 -45.602 -10.697 1.00 30.16  ? 216 ASN   B CG   1 
ATOM   3468 O  OD1  . ASN   B 1 216 ? -35.145 -44.721 -10.379 1.00 29.28  ? 216 ASN   B OD1  1 
ATOM   3469 N  ND2  . ASN   B 1 216 ? -36.076 -46.737 -10.025 1.00 28.01  ? 216 ASN   B ND2  1 
ATOM   3470 N  N    . ILE   B 1 217 ? -40.050 -45.148 -10.954 1.00 25.26  ? 217 ILE   B N    1 
ATOM   3471 C  CA   . ILE   B 1 217 ? -41.276 -45.322 -10.115 1.00 25.40  ? 217 ILE   B CA   1 
ATOM   3472 C  C    . ILE   B 1 217 ? -40.936 -46.159 -8.874  1.00 24.72  ? 217 ILE   B C    1 
ATOM   3473 O  O    . ILE   B 1 217 ? -41.504 -45.875 -7.793  1.00 23.71  ? 217 ILE   B O    1 
ATOM   3474 C  CB   . ILE   B 1 217 ? -42.437 -45.914 -10.943 1.00 26.19  ? 217 ILE   B CB   1 
ATOM   3475 C  CG1  . ILE   B 1 217 ? -42.060 -47.231 -11.623 1.00 28.05  ? 217 ILE   B CG1  1 
ATOM   3476 C  CG2  . ILE   B 1 217 ? -42.926 -44.924 -11.982 1.00 26.79  ? 217 ILE   B CG2  1 
ATOM   3477 C  CD1  . ILE   B 1 217 ? -43.234 -47.923 -12.270 1.00 31.24  ? 217 ILE   B CD1  1 
ATOM   3478 N  N    . ASP   B 1 218 ? -40.017 -47.123 -9.013  1.00 25.71  ? 218 ASP   B N    1 
ATOM   3479 C  CA   . ASP   B 1 218 ? -39.647 -48.112 -7.959  1.00 28.97  ? 218 ASP   B CA   1 
ATOM   3480 C  C    . ASP   B 1 218 ? -38.500 -47.576 -7.068  1.00 27.29  ? 218 ASP   B C    1 
ATOM   3481 O  O    . ASP   B 1 218 ? -37.977 -48.363 -6.273  1.00 25.87  ? 218 ASP   B O    1 
ATOM   3482 C  CB   . ASP   B 1 218 ? -39.319 -49.489 -8.581  1.00 32.26  ? 218 ASP   B CB   1 
ATOM   3483 C  CG   . ASP   B 1 218 ? -38.308 -49.514 -9.738  1.00 36.29  ? 218 ASP   B CG   1 
ATOM   3484 O  OD1  . ASP   B 1 218 ? -38.276 -48.540 -10.534 1.00 43.17  ? 218 ASP   B OD1  1 
ATOM   3485 O  OD2  . ASP   B 1 218 ? -37.560 -50.517 -9.862  1.00 36.03  ? 218 ASP   B OD2  1 
ATOM   3486 N  N    . SER   B 1 219 ? -38.144 -46.291 -7.146  1.00 26.92  ? 219 SER   B N    1 
ATOM   3487 C  CA   . SER   B 1 219 ? -36.999 -45.677 -6.408  1.00 26.91  ? 219 SER   B CA   1 
ATOM   3488 C  C    . SER   B 1 219 ? -37.123 -45.851 -4.884  1.00 25.45  ? 219 SER   B C    1 
ATOM   3489 O  O    . SER   B 1 219 ? -38.213 -45.595 -4.311  1.00 24.06  ? 219 SER   B O    1 
ATOM   3490 C  CB   . SER   B 1 219 ? -36.850 -44.218 -6.747  1.00 28.99  ? 219 SER   B CB   1 
ATOM   3491 O  OG   . SER   B 1 219 ? -35.767 -43.646 -6.008  1.00 33.03  ? 219 SER   B OG   1 
ATOM   3492 N  N    . SER   B 1 220 ? -36.011 -46.201 -4.229  1.00 24.60  ? 220 SER   B N    1 
ATOM   3493 C  CA   . SER   B 1 220 ? -35.893 -46.232 -2.748  1.00 25.39  ? 220 SER   B CA   1 
ATOM   3494 C  C    . SER   B 1 220 ? -34.602 -45.528 -2.309  1.00 24.08  ? 220 SER   B C    1 
ATOM   3495 O  O    . SER   B 1 220 ? -33.747 -45.214 -3.171  1.00 22.61  ? 220 SER   B O    1 
ATOM   3496 C  CB   . SER   B 1 220 ? -35.974 -47.649 -2.222  1.00 27.13  ? 220 SER   B CB   1 
ATOM   3497 O  OG   . SER   B 1 220 ? -35.123 -48.504 -2.969  1.00 31.36  ? 220 SER   B OG   1 
ATOM   3498 N  N    . ILE   B 1 221 ? -34.486 -45.269 -1.005  1.00 22.75  ? 221 ILE   B N    1 
ATOM   3499 C  CA   . ILE   B 1 221 ? -33.298 -44.615 -0.396  1.00 22.73  ? 221 ILE   B CA   1 
ATOM   3500 C  C    . ILE   B 1 221 ? -32.108 -45.544 -0.611  1.00 21.74  ? 221 ILE   B C    1 
ATOM   3501 O  O    . ILE   B 1 221 ? -32.124 -46.651 -0.099  1.00 21.11  ? 221 ILE   B O    1 
ATOM   3502 C  CB   . ILE   B 1 221 ? -33.533 -44.325 1.097   1.00 21.79  ? 221 ILE   B CB   1 
ATOM   3503 C  CG1  . ILE   B 1 221 ? -34.639 -43.283 1.287   1.00 21.93  ? 221 ILE   B CG1  1 
ATOM   3504 C  CG2  . ILE   B 1 221 ? -32.231 -43.903 1.765   1.00 20.33  ? 221 ILE   B CG2  1 
ATOM   3505 C  CD1  . ILE   B 1 221 ? -35.028 -43.014 2.740   1.00 22.09  ? 221 ILE   B CD1  1 
ATOM   3506 N  N    . PRO   B 1 222 ? -31.053 -45.150 -1.358  1.00 22.12  ? 222 PRO   B N    1 
ATOM   3507 C  CA   . PRO   B 1 222 ? -29.871 -46.003 -1.493  1.00 23.55  ? 222 PRO   B CA   1 
ATOM   3508 C  C    . PRO   B 1 222 ? -29.173 -46.175 -0.129  1.00 23.83  ? 222 PRO   B C    1 
ATOM   3509 O  O    . PRO   B 1 222 ? -29.186 -45.276 0.672   1.00 23.21  ? 222 PRO   B O    1 
ATOM   3510 C  CB   . PRO   B 1 222 ? -28.988 -45.286 -2.527  1.00 21.97  ? 222 PRO   B CB   1 
ATOM   3511 C  CG   . PRO   B 1 222 ? -29.905 -44.254 -3.159  1.00 22.03  ? 222 PRO   B CG   1 
ATOM   3512 C  CD   . PRO   B 1 222 ? -30.900 -43.879 -2.084  1.00 21.11  ? 222 PRO   B CD   1 
ATOM   3513 N  N    . SER   B 1 223 ? -28.657 -47.375 0.128   1.00 26.64  ? 223 SER   B N    1 
ATOM   3514 C  CA   . SER   B 1 223 ? -27.731 -47.704 1.242   1.00 27.76  ? 223 SER   B CA   1 
ATOM   3515 C  C    . SER   B 1 223 ? -26.667 -46.592 1.379   1.00 25.41  ? 223 SER   B C    1 
ATOM   3516 O  O    . SER   B 1 223 ? -26.100 -46.170 0.355   1.00 25.28  ? 223 SER   B O    1 
ATOM   3517 C  CB   . SER   B 1 223 ? -27.143 -49.092 0.994   1.00 29.76  ? 223 SER   B CB   1 
ATOM   3518 O  OG   . SER   B 1 223 ? -25.999 -49.337 1.806   1.00 36.96  ? 223 SER   B OG   1 
ATOM   3519 N  N    . GLY   B 1 224 ? -26.456 -46.080 2.592   1.00 23.69  ? 224 GLY   B N    1 
ATOM   3520 C  CA   . GLY   B 1 224 ? -25.364 -45.146 2.911   1.00 24.82  ? 224 GLY   B CA   1 
ATOM   3521 C  C    . GLY   B 1 224 ? -25.534 -43.778 2.259   1.00 25.47  ? 224 GLY   B C    1 
ATOM   3522 O  O    . GLY   B 1 224 ? -24.519 -43.114 2.064   1.00 23.97  ? 224 GLY   B O    1 
ATOM   3523 N  N    . SER   B 1 225 ? -26.772 -43.358 1.949   1.00 23.52  ? 225 SER   B N    1 
ATOM   3524 C  CA   . SER   B 1 225 ? -27.081 -42.078 1.257   1.00 22.56  ? 225 SER   B CA   1 
ATOM   3525 C  C    . SER   B 1 225 ? -27.421 -40.981 2.276   1.00 22.47  ? 225 SER   B C    1 
ATOM   3526 O  O    . SER   B 1 225 ? -27.991 -39.954 1.848   1.00 23.90  ? 225 SER   B O    1 
ATOM   3527 C  CB   . SER   B 1 225 ? -28.199 -42.239 0.235   1.00 21.70  ? 225 SER   B CB   1 
ATOM   3528 O  OG   . SER   B 1 225 ? -29.473 -42.391 0.856   1.00 18.41  ? 225 SER   B OG   1 
ATOM   3529 N  N    . THR   B 1 226 ? -27.126 -41.167 3.563   1.00 20.93  ? 226 THR   B N    1 
ATOM   3530 C  CA   . THR   B 1 226 ? -27.282 -40.074 4.554   1.00 22.73  ? 226 THR   B CA   1 
ATOM   3531 C  C    . THR   B 1 226 ? -26.233 -39.009 4.224   1.00 22.04  ? 226 THR   B C    1 
ATOM   3532 O  O    . THR   B 1 226 ? -25.384 -39.261 3.336   1.00 23.74  ? 226 THR   B O    1 
ATOM   3533 C  CB   . THR   B 1 226 ? -27.246 -40.537 6.025   1.00 24.01  ? 226 THR   B CB   1 
ATOM   3534 O  OG1  . THR   B 1 226 ? -25.927 -40.963 6.352   1.00 23.73  ? 226 THR   B OG1  1 
ATOM   3535 C  CG2  . THR   B 1 226 ? -28.246 -41.634 6.345   1.00 24.12  ? 226 THR   B CG2  1 
ATOM   3536 N  N    . GLY   B 1 227 ? -26.330 -37.860 4.884   1.00 20.69  ? 227 GLY   B N    1 
ATOM   3537 C  CA   . GLY   B 1 227 ? -25.412 -36.714 4.735   1.00 19.97  ? 227 GLY   B CA   1 
ATOM   3538 C  C    . GLY   B 1 227 ? -25.362 -36.176 3.316   1.00 19.03  ? 227 GLY   B C    1 
ATOM   3539 O  O    . GLY   B 1 227 ? -26.418 -35.809 2.755   1.00 17.85  ? 227 GLY   B O    1 
ATOM   3540 N  N    . ARG   B 1 228 ? -24.161 -36.108 2.761   1.00 18.22  ? 228 ARG   B N    1 
ATOM   3541 C  CA   . ARG   B 1 228 ? -23.836 -35.292 1.567   1.00 18.85  ? 228 ARG   B CA   1 
ATOM   3542 C  C    . ARG   B 1 228 ? -24.569 -35.794 0.314   1.00 19.65  ? 228 ARG   B C    1 
ATOM   3543 O  O    . ARG   B 1 228 ? -24.625 -35.054 -0.662  1.00 21.16  ? 228 ARG   B O    1 
ATOM   3544 C  CB   . ARG   B 1 228 ? -22.320 -35.336 1.364   1.00 18.92  ? 228 ARG   B CB   1 
ATOM   3545 C  CG   . ARG   B 1 228 ? -21.737 -36.721 1.115   1.00 18.29  ? 228 ARG   B CG   1 
ATOM   3546 C  CD   . ARG   B 1 228 ? -20.225 -36.591 1.076   1.00 18.55  ? 228 ARG   B CD   1 
ATOM   3547 N  NE   . ARG   B 1 228 ? -19.611 -37.780 0.547   1.00 20.23  ? 228 ARG   B NE   1 
ATOM   3548 C  CZ   . ARG   B 1 228 ? -18.305 -37.990 0.410   1.00 20.31  ? 228 ARG   B CZ   1 
ATOM   3549 N  NH1  . ARG   B 1 228 ? -17.423 -37.063 0.755   1.00 20.04  ? 228 ARG   B NH1  1 
ATOM   3550 N  NH2  . ARG   B 1 228 ? -17.894 -39.144 -0.080  1.00 20.33  ? 228 ARG   B NH2  1 
ATOM   3551 N  N    . LEU   B 1 229 ? -25.067 -37.024 0.332   1.00 19.75  ? 229 LEU   B N    1 
ATOM   3552 C  CA   . LEU   B 1 229 ? -25.689 -37.721 -0.827  1.00 20.67  ? 229 LEU   B CA   1 
ATOM   3553 C  C    . LEU   B 1 229 ? -27.208 -37.501 -0.840  1.00 19.22  ? 229 LEU   B C    1 
ATOM   3554 O  O    . LEU   B 1 229 ? -27.845 -37.981 -1.792  1.00 18.12  ? 229 LEU   B O    1 
ATOM   3555 C  CB   . LEU   B 1 229 ? -25.344 -39.211 -0.714  1.00 21.42  ? 229 LEU   B CB   1 
ATOM   3556 C  CG   . LEU   B 1 229 ? -23.867 -39.562 -0.869  1.00 20.87  ? 229 LEU   B CG   1 
ATOM   3557 C  CD1  . LEU   B 1 229 ? -23.659 -41.076 -0.813  1.00 21.41  ? 229 LEU   B CD1  1 
ATOM   3558 C  CD2  . LEU   B 1 229 ? -23.323 -39.003 -2.169  1.00 21.68  ? 229 LEU   B CD2  1 
ATOM   3559 N  N    . LEU   B 1 230 ? -27.746 -36.852 0.203   1.00 18.71  ? 230 LEU   B N    1 
ATOM   3560 C  CA   . LEU   B 1 230 ? -29.080 -36.192 0.227   1.00 19.30  ? 230 LEU   B CA   1 
ATOM   3561 C  C    . LEU   B 1 230 ? -30.218 -37.205 0.086   1.00 17.81  ? 230 LEU   B C    1 
ATOM   3562 O  O    . LEU   B 1 230 ? -31.325 -36.796 -0.315  1.00 19.06  ? 230 LEU   B O    1 
ATOM   3563 C  CB   . LEU   B 1 230 ? -29.123 -35.151 -0.894  1.00 19.92  ? 230 LEU   B CB   1 
ATOM   3564 C  CG   . LEU   B 1 230 ? -28.234 -33.933 -0.644  1.00 21.79  ? 230 LEU   B CG   1 
ATOM   3565 C  CD1  . LEU   B 1 230 ? -28.162 -33.041 -1.879  1.00 22.01  ? 230 LEU   B CD1  1 
ATOM   3566 C  CD2  . LEU   B 1 230 ? -28.723 -33.149 0.567   1.00 21.27  ? 230 LEU   B CD2  1 
ATOM   3567 N  N    . GLY   B 1 231 ? -29.963 -38.470 0.411   1.00 17.33  ? 231 GLY   B N    1 
ATOM   3568 C  CA   . GLY   B 1 231 ? -30.932 -39.575 0.262   1.00 17.13  ? 231 GLY   B CA   1 
ATOM   3569 C  C    . GLY   B 1 231 ? -31.162 -39.951 -1.187  1.00 16.81  ? 231 GLY   B C    1 
ATOM   3570 O  O    . GLY   B 1 231 ? -32.125 -40.689 -1.442  1.00 17.99  ? 231 GLY   B O    1 
ATOM   3571 N  N    . LEU   B 1 232 ? -30.309 -39.506 -2.114  1.00 18.78  ? 232 LEU   B N    1 
ATOM   3572 C  CA   . LEU   B 1 232 ? -30.584 -39.579 -3.584  1.00 20.50  ? 232 LEU   B CA   1 
ATOM   3573 C  C    . LEU   B 1 232 ? -29.638 -40.551 -4.315  1.00 22.01  ? 232 LEU   B C    1 
ATOM   3574 O  O    . LEU   B 1 232 ? -30.079 -41.168 -5.262  1.00 24.21  ? 232 LEU   B O    1 
ATOM   3575 C  CB   . LEU   B 1 232 ? -30.453 -38.177 -4.187  1.00 20.24  ? 232 LEU   B CB   1 
ATOM   3576 C  CG   . LEU   B 1 232 ? -31.578 -37.192 -3.837  1.00 21.37  ? 232 LEU   B CG   1 
ATOM   3577 C  CD1  . LEU   B 1 232 ? -31.331 -35.840 -4.486  1.00 21.59  ? 232 LEU   B CD1  1 
ATOM   3578 C  CD2  . LEU   B 1 232 ? -32.958 -37.721 -4.230  1.00 21.83  ? 232 LEU   B CD2  1 
ATOM   3579 N  N    . PHE   B 1 233 ? -28.365 -40.611 -3.955  1.00 22.54  ? 233 PHE   B N    1 
ATOM   3580 C  CA   . PHE   B 1 233 ? -27.324 -41.292 -4.754  1.00 23.86  ? 233 PHE   B CA   1 
ATOM   3581 C  C    . PHE   B 1 233 ? -26.606 -42.304 -3.875  1.00 23.20  ? 233 PHE   B C    1 
ATOM   3582 O  O    . PHE   B 1 233 ? -26.509 -42.132 -2.666  1.00 22.00  ? 233 PHE   B O    1 
ATOM   3583 C  CB   . PHE   B 1 233 ? -26.380 -40.260 -5.364  1.00 25.46  ? 233 PHE   B CB   1 
ATOM   3584 C  CG   . PHE   B 1 233 ? -27.066 -39.277 -6.275  1.00 26.32  ? 233 PHE   B CG   1 
ATOM   3585 C  CD1  . PHE   B 1 233 ? -27.446 -39.643 -7.552  1.00 27.80  ? 233 PHE   B CD1  1 
ATOM   3586 C  CD2  . PHE   B 1 233 ? -27.340 -37.989 -5.847  1.00 27.82  ? 233 PHE   B CD2  1 
ATOM   3587 C  CE1  . PHE   B 1 233 ? -28.088 -38.744 -8.388  1.00 27.98  ? 233 PHE   B CE1  1 
ATOM   3588 C  CE2  . PHE   B 1 233 ? -27.971 -37.088 -6.686  1.00 26.82  ? 233 PHE   B CE2  1 
ATOM   3589 C  CZ   . PHE   B 1 233 ? -28.358 -37.473 -7.947  1.00 28.16  ? 233 PHE   B CZ   1 
ATOM   3590 N  N    . PRO   B 1 234 ? -26.171 -43.441 -4.452  1.00 26.66  ? 234 PRO   B N    1 
ATOM   3591 C  CA   . PRO   B 1 234 ? -25.518 -44.487 -3.668  1.00 26.11  ? 234 PRO   B CA   1 
ATOM   3592 C  C    . PRO   B 1 234 ? -24.041 -44.156 -3.405  1.00 28.17  ? 234 PRO   B C    1 
ATOM   3593 O  O    . PRO   B 1 234 ? -23.521 -44.654 -2.423  1.00 30.36  ? 234 PRO   B O    1 
ATOM   3594 C  CB   . PRO   B 1 234 ? -25.701 -45.717 -4.550  1.00 25.36  ? 234 PRO   B CB   1 
ATOM   3595 C  CG   . PRO   B 1 234 ? -25.688 -45.164 -5.969  1.00 27.32  ? 234 PRO   B CG   1 
ATOM   3596 C  CD   . PRO   B 1 234 ? -26.335 -43.794 -5.879  1.00 26.40  ? 234 PRO   B CD   1 
ATOM   3597 N  N    . ASP   B 1 235 ? -23.444 -43.272 -4.221  1.00 28.97  ? 235 ASP   B N    1 
ATOM   3598 C  CA   . ASP   B 1 235 ? -22.035 -42.800 -4.087  1.00 31.22  ? 235 ASP   B CA   1 
ATOM   3599 C  C    . ASP   B 1 235 ? -21.890 -41.359 -4.630  1.00 32.61  ? 235 ASP   B C    1 
ATOM   3600 O  O    . ASP   B 1 235 ? -22.918 -40.770 -5.089  1.00 31.03  ? 235 ASP   B O    1 
ATOM   3601 C  CB   . ASP   B 1 235 ? -21.089 -43.776 -4.796  1.00 31.31  ? 235 ASP   B CB   1 
ATOM   3602 C  CG   . ASP   B 1 235 ? -21.521 -44.012 -6.225  1.00 33.94  ? 235 ASP   B CG   1 
ATOM   3603 O  OD1  . ASP   B 1 235 ? -21.435 -43.061 -7.031  1.00 32.61  ? 235 ASP   B OD1  1 
ATOM   3604 O  OD2  . ASP   B 1 235 ? -22.004 -45.126 -6.498  1.00 42.66  ? 235 ASP   B OD2  1 
ATOM   3605 N  N    . ALA   B 1 236 ? -20.664 -40.809 -4.586  1.00 29.62  ? 236 ALA   B N    1 
ATOM   3606 C  CA   . ALA   B 1 236 ? -20.338 -39.392 -4.879  1.00 31.94  ? 236 ALA   B CA   1 
ATOM   3607 C  C    . ALA   B 1 236 ? -19.758 -39.240 -6.291  1.00 33.80  ? 236 ALA   B C    1 
ATOM   3608 O  O    . ALA   B 1 236 ? -19.146 -38.186 -6.559  1.00 34.89  ? 236 ALA   B O    1 
ATOM   3609 C  CB   . ALA   B 1 236 ? -19.394 -38.843 -3.839  1.00 30.96  ? 236 ALA   B CB   1 
ATOM   3610 N  N    . ASN   B 1 237 ? -19.980 -40.228 -7.164  1.00 38.85  ? 237 ASN   B N    1 
ATOM   3611 C  CA   . ASN   B 1 237 ? -19.639 -40.174 -8.613  1.00 45.62  ? 237 ASN   B CA   1 
ATOM   3612 C  C    . ASN   B 1 237 ? -20.400 -39.018 -9.275  1.00 45.33  ? 237 ASN   B C    1 
ATOM   3613 O  O    . ASN   B 1 237 ? -21.631 -38.858 -9.113  1.00 38.71  ? 237 ASN   B O    1 
ATOM   3614 C  CB   . ASN   B 1 237 ? -19.944 -41.488 -9.340  1.00 48.09  ? 237 ASN   B CB   1 
ATOM   3615 C  CG   . ASN   B 1 237 ? -18.801 -42.480 -9.283  1.00 55.29  ? 237 ASN   B CG   1 
ATOM   3616 O  OD1  . ASN   B 1 237 ? -18.004 -42.479 -8.339  1.00 52.77  ? 237 ASN   B OD1  1 
ATOM   3617 N  ND2  . ASN   B 1 237 ? -18.726 -43.334 -10.295 1.00 60.90  ? 237 ASN   B ND2  1 
ATOM   3618 O  OXT  . ASN   B 1 237 ? -19.748 -38.234 -9.974  1.00 48.67  ? 237 ASN   B OXT  1 
ATOM   3619 N  N    . ALA   C 1 1   ? -13.920 -15.657 -4.045  1.00 46.17  ? 1   ALA   C N    1 
ATOM   3620 C  CA   . ALA   C 1 1   ? -13.982 -15.649 -2.536  1.00 44.51  ? 1   ALA   C CA   1 
ATOM   3621 C  C    . ALA   C 1 1   ? -14.135 -14.199 -2.078  1.00 36.94  ? 1   ALA   C C    1 
ATOM   3622 O  O    . ALA   C 1 1   ? -14.243 -13.305 -2.953  1.00 34.59  ? 1   ALA   C O    1 
ATOM   3623 C  CB   . ALA   C 1 1   ? -12.748 -16.304 -1.944  1.00 45.69  ? 1   ALA   C CB   1 
ATOM   3624 N  N    . ASP   C 1 2   ? -14.147 -13.971 -0.770  1.00 33.94  ? 2   ASP   C N    1 
ATOM   3625 C  CA   . ASP   C 1 2   ? -14.285 -12.611 -0.193  1.00 35.77  ? 2   ASP   C CA   1 
ATOM   3626 C  C    . ASP   C 1 2   ? -13.141 -11.717 -0.703  1.00 32.78  ? 2   ASP   C C    1 
ATOM   3627 O  O    . ASP   C 1 2   ? -12.119 -12.246 -1.187  1.00 33.70  ? 2   ASP   C O    1 
ATOM   3628 C  CB   . ASP   C 1 2   ? -14.349 -12.668 1.334   1.00 36.70  ? 2   ASP   C CB   1 
ATOM   3629 C  CG   . ASP   C 1 2   ? -15.616 -13.310 1.889   1.00 37.31  ? 2   ASP   C CG   1 
ATOM   3630 O  OD1  . ASP   C 1 2   ? -16.494 -13.745 1.069   1.00 40.62  ? 2   ASP   C OD1  1 
ATOM   3631 O  OD2  . ASP   C 1 2   ? -15.737 -13.347 3.135   1.00 33.92  ? 2   ASP   C OD2  1 
ATOM   3632 N  N    . THR   C 1 3   ? -13.385 -10.413 -0.723  1.00 30.65  ? 3   THR   C N    1 
ATOM   3633 C  CA   . THR   C 1 3   ? -12.359 -9.343  -0.711  1.00 30.48  ? 3   THR   C CA   1 
ATOM   3634 C  C    . THR   C 1 3   ? -12.534 -8.620  0.632   1.00 27.51  ? 3   THR   C C    1 
ATOM   3635 O  O    . THR   C 1 3   ? -13.634 -8.137  0.887   1.00 25.55  ? 3   THR   C O    1 
ATOM   3636 C  CB   . THR   C 1 3   ? -12.483 -8.453  -1.952  1.00 33.01  ? 3   THR   C CB   1 
ATOM   3637 O  OG1  . THR   C 1 3   ? -13.775 -7.852  -1.885  1.00 37.99  ? 3   THR   C OG1  1 
ATOM   3638 C  CG2  . THR   C 1 3   ? -12.346 -9.211  -3.256  1.00 33.50  ? 3   THR   C CG2  1 
ATOM   3639 N  N    . ILE   C 1 4   ? -11.518 -8.664  1.494   1.00 25.49  ? 4   ILE   C N    1 
ATOM   3640 C  CA   . ILE   C 1 4   ? -11.516 -8.050  2.847   1.00 23.15  ? 4   ILE   C CA   1 
ATOM   3641 C  C    . ILE   C 1 4   ? -10.505 -6.900  2.881   1.00 22.03  ? 4   ILE   C C    1 
ATOM   3642 O  O    . ILE   C 1 4   ? -9.374  -7.079  2.391   1.00 20.41  ? 4   ILE   C O    1 
ATOM   3643 C  CB   . ILE   C 1 4   ? -11.151 -9.079  3.912   1.00 24.90  ? 4   ILE   C CB   1 
ATOM   3644 C  CG1  . ILE   C 1 4   ? -12.109 -10.268 3.904   1.00 26.40  ? 4   ILE   C CG1  1 
ATOM   3645 C  CG2  . ILE   C 1 4   ? -11.091 -8.393  5.267   1.00 26.43  ? 4   ILE   C CG2  1 
ATOM   3646 C  CD1  . ILE   C 1 4   ? -13.399 -9.995  4.642   1.00 27.82  ? 4   ILE   C CD1  1 
ATOM   3647 N  N    . VAL   C 1 5   ? -10.939 -5.768  3.431   1.00 19.24  ? 5   VAL   C N    1 
ATOM   3648 C  CA   . VAL   C 1 5   ? -10.091 -4.679  3.966   1.00 17.96  ? 5   VAL   C CA   1 
ATOM   3649 C  C    . VAL   C 1 5   ? -10.363 -4.662  5.471   1.00 17.79  ? 5   VAL   C C    1 
ATOM   3650 O  O    . VAL   C 1 5   ? -11.581 -4.642  5.840   1.00 16.93  ? 5   VAL   C O    1 
ATOM   3651 C  CB   . VAL   C 1 5   ? -10.454 -3.336  3.311   1.00 17.81  ? 5   VAL   C CB   1 
ATOM   3652 C  CG1  . VAL   C 1 5   ? -9.719  -2.171  3.951   1.00 17.83  ? 5   VAL   C CG1  1 
ATOM   3653 C  CG2  . VAL   C 1 5   ? -10.216 -3.359  1.809   1.00 17.89  ? 5   VAL   C CG2  1 
ATOM   3654 N  N    . ALA   C 1 6   ? -9.323  -4.680  6.316   1.00 15.04  ? 6   ALA   C N    1 
ATOM   3655 C  CA   . ALA   C 1 6   ? -9.525  -4.587  7.777   1.00 13.88  ? 6   ALA   C CA   1 
ATOM   3656 C  C    . ALA   C 1 6   ? -8.422  -3.808  8.478   1.00 13.25  ? 6   ALA   C C    1 
ATOM   3657 O  O    . ALA   C 1 6   ? -7.280  -3.662  7.929   1.00 12.68  ? 6   ALA   C O    1 
ATOM   3658 C  CB   . ALA   C 1 6   ? -9.661  -5.968  8.367   1.00 14.27  ? 6   ALA   C CB   1 
ATOM   3659 N  N    . VAL   C 1 7   ? -8.772  -3.328  9.665   1.00 12.86  ? 7   VAL   C N    1 
ATOM   3660 C  CA   . VAL   C 1 7   ? -7.788  -2.895  10.687  1.00 14.12  ? 7   VAL   C CA   1 
ATOM   3661 C  C    . VAL   C 1 7   ? -7.746  -3.958  11.775  1.00 13.92  ? 7   VAL   C C    1 
ATOM   3662 O  O    . VAL   C 1 7   ? -8.794  -4.202  12.387  1.00 13.52  ? 7   VAL   C O    1 
ATOM   3663 C  CB   . VAL   C 1 7   ? -8.129  -1.519  11.263  1.00 14.09  ? 7   VAL   C CB   1 
ATOM   3664 C  CG1  . VAL   C 1 7   ? -7.213  -1.177  12.433  1.00 14.32  ? 7   VAL   C CG1  1 
ATOM   3665 C  CG2  . VAL   C 1 7   ? -8.071  -0.476  10.161  1.00 14.13  ? 7   VAL   C CG2  1 
ATOM   3666 N  N    . GLU   C 1 8   ? -6.596  -4.586  11.972  1.00 13.63  ? 8   GLU   C N    1 
ATOM   3667 C  CA   . GLU   C 1 8   ? -6.492  -5.665  12.979  1.00 15.30  ? 8   GLU   C CA   1 
ATOM   3668 C  C    . GLU   C 1 8   ? -5.845  -5.069  14.233  1.00 15.56  ? 8   GLU   C C    1 
ATOM   3669 O  O    . GLU   C 1 8   ? -4.946  -4.209  14.109  1.00 15.13  ? 8   GLU   C O    1 
ATOM   3670 C  CB   . GLU   C 1 8   ? -5.724  -6.865  12.424  1.00 16.61  ? 8   GLU   C CB   1 
ATOM   3671 C  CG   . GLU   C 1 8   ? -4.326  -6.511  11.958  1.00 17.72  ? 8   GLU   C CG   1 
ATOM   3672 C  CD   . GLU   C 1 8   ? -3.415  -7.702  11.714  1.00 19.34  ? 8   GLU   C CD   1 
ATOM   3673 O  OE1  . GLU   C 1 8   ? -3.811  -8.586  10.948  1.00 21.03  ? 8   GLU   C OE1  1 
ATOM   3674 O  OE2  . GLU   C 1 8   ? -2.321  -7.746  12.300  1.00 20.28  ? 8   GLU   C OE2  1 
ATOM   3675 N  N    . LEU   C 1 9   ? -6.373  -5.454  15.391  1.00 15.65  ? 9   LEU   C N    1 
ATOM   3676 C  CA   . LEU   C 1 9   ? -5.747  -5.317  16.722  1.00 15.68  ? 9   LEU   C CA   1 
ATOM   3677 C  C    . LEU   C 1 9   ? -5.244  -6.709  17.084  1.00 16.64  ? 9   LEU   C C    1 
ATOM   3678 O  O    . LEU   C 1 9   ? -6.015  -7.497  17.645  1.00 17.80  ? 9   LEU   C O    1 
ATOM   3679 C  CB   . LEU   C 1 9   ? -6.768  -4.788  17.732  1.00 16.12  ? 9   LEU   C CB   1 
ATOM   3680 C  CG   . LEU   C 1 9   ? -6.992  -3.277  17.688  1.00 17.08  ? 9   LEU   C CG   1 
ATOM   3681 C  CD1  . LEU   C 1 9   ? -7.259  -2.807  16.267  1.00 18.09  ? 9   LEU   C CD1  1 
ATOM   3682 C  CD2  . LEU   C 1 9   ? -8.145  -2.882  18.598  1.00 17.74  ? 9   LEU   C CD2  1 
ATOM   3683 N  N    . ASP   C 1 10  ? -4.002  -6.998  16.712  1.00 16.16  ? 10  ASP   C N    1 
ATOM   3684 C  CA   . ASP   C 1 10  ? -3.415  -8.356  16.719  1.00 16.31  ? 10  ASP   C CA   1 
ATOM   3685 C  C    . ASP   C 1 10  ? -2.674  -8.573  18.054  1.00 17.18  ? 10  ASP   C C    1 
ATOM   3686 O  O    . ASP   C 1 10  ? -1.619  -7.928  18.284  1.00 16.50  ? 10  ASP   C O    1 
ATOM   3687 C  CB   . ASP   C 1 10  ? -2.557  -8.497  15.468  1.00 16.30  ? 10  ASP   C CB   1 
ATOM   3688 C  CG   . ASP   C 1 10  ? -2.121  -9.916  15.189  1.00 16.46  ? 10  ASP   C CG   1 
ATOM   3689 O  OD1  . ASP   C 1 10  ? -2.238  -10.752 16.103  1.00 16.61  ? 10  ASP   C OD1  1 
ATOM   3690 O  OD2  . ASP   C 1 10  ? -1.659  -10.168 14.061  1.00 16.71  ? 10  ASP   C OD2  1 
ATOM   3691 N  N    . THR   C 1 11  ? -3.213  -9.425  18.928  1.00 16.42  ? 11  THR   C N    1 
ATOM   3692 C  CA   . THR   C 1 11  ? -2.692  -9.595  20.308  1.00 17.06  ? 11  THR   C CA   1 
ATOM   3693 C  C    . THR   C 1 11  ? -1.572  -10.639 20.337  1.00 17.56  ? 11  THR   C C    1 
ATOM   3694 O  O    . THR   C 1 11  ? -0.817  -10.595 21.298  1.00 18.56  ? 11  THR   C O    1 
ATOM   3695 C  CB   . THR   C 1 11  ? -3.810  -9.923  21.302  1.00 16.42  ? 11  THR   C CB   1 
ATOM   3696 O  OG1  . THR   C 1 11  ? -4.507  -11.110 20.921  1.00 16.26  ? 11  THR   C OG1  1 
ATOM   3697 C  CG2  . THR   C 1 11  ? -4.792  -8.783  21.433  1.00 16.64  ? 11  THR   C CG2  1 
ATOM   3698 N  N    . TYR   C 1 12  ? -1.423  -11.484 19.309  1.00 18.46  ? 12  TYR   C N    1 
ATOM   3699 C  CA   . TYR   C 1 12  ? -0.551  -12.689 19.366  1.00 19.06  ? 12  TYR   C CA   1 
ATOM   3700 C  C    . TYR   C 1 12  ? 0.401   -12.739 18.181  1.00 17.88  ? 12  TYR   C C    1 
ATOM   3701 O  O    . TYR   C 1 12  ? -0.029  -12.843 17.042  1.00 17.80  ? 12  TYR   C O    1 
ATOM   3702 C  CB   . TYR   C 1 12  ? -1.388  -13.964 19.433  1.00 21.39  ? 12  TYR   C CB   1 
ATOM   3703 C  CG   . TYR   C 1 12  ? -0.540  -15.191 19.598  1.00 23.32  ? 12  TYR   C CG   1 
ATOM   3704 C  CD1  . TYR   C 1 12  ? 0.014   -15.498 20.829  1.00 24.43  ? 12  TYR   C CD1  1 
ATOM   3705 C  CD2  . TYR   C 1 12  ? -0.210  -15.988 18.511  1.00 25.13  ? 12  TYR   C CD2  1 
ATOM   3706 C  CE1  . TYR   C 1 12  ? 0.846   -16.586 20.994  1.00 24.36  ? 12  TYR   C CE1  1 
ATOM   3707 C  CE2  . TYR   C 1 12  ? 0.629   -17.081 18.659  1.00 27.51  ? 12  TYR   C CE2  1 
ATOM   3708 C  CZ   . TYR   C 1 12  ? 1.150   -17.381 19.910  1.00 27.57  ? 12  TYR   C CZ   1 
ATOM   3709 O  OH   . TYR   C 1 12  ? 1.966   -18.464 20.082  1.00 33.34  ? 12  TYR   C OH   1 
ATOM   3710 N  N    . PRO   C 1 13  ? 1.728   -12.694 18.409  1.00 18.36  ? 13  PRO   C N    1 
ATOM   3711 C  CA   . PRO   C 1 13  ? 2.697   -12.668 17.309  1.00 19.12  ? 13  PRO   C CA   1 
ATOM   3712 C  C    . PRO   C 1 13  ? 2.866   -14.024 16.595  1.00 20.41  ? 13  PRO   C C    1 
ATOM   3713 O  O    . PRO   C 1 13  ? 3.331   -14.950 17.223  1.00 19.67  ? 13  PRO   C O    1 
ATOM   3714 C  CB   . PRO   C 1 13  ? 4.022   -12.293 17.981  1.00 19.00  ? 13  PRO   C CB   1 
ATOM   3715 C  CG   . PRO   C 1 13  ? 3.660   -11.933 19.417  1.00 18.98  ? 13  PRO   C CG   1 
ATOM   3716 C  CD   . PRO   C 1 13  ? 2.374   -12.652 19.729  1.00 18.39  ? 13  PRO   C CD   1 
ATOM   3717 N  N    . ASN   C 1 14  ? 2.408   -14.109 15.339  1.00 19.62  ? 14  ASN   C N    1 
ATOM   3718 C  CA   . ASN   C 1 14  ? 2.522   -15.297 14.459  1.00 19.45  ? 14  ASN   C CA   1 
ATOM   3719 C  C    . ASN   C 1 14  ? 3.646   -14.999 13.473  1.00 20.11  ? 14  ASN   C C    1 
ATOM   3720 O  O    . ASN   C 1 14  ? 3.333   -14.635 12.335  1.00 20.61  ? 14  ASN   C O    1 
ATOM   3721 C  CB   . ASN   C 1 14  ? 1.207   -15.593 13.722  1.00 19.48  ? 14  ASN   C CB   1 
ATOM   3722 C  CG   . ASN   C 1 14  ? 0.084   -15.980 14.656  1.00 19.58  ? 14  ASN   C CG   1 
ATOM   3723 O  OD1  . ASN   C 1 14  ? -0.733  -15.142 15.032  1.00 17.61  ? 14  ASN   C OD1  1 
ATOM   3724 N  ND2  . ASN   C 1 14  ? 0.054   -17.246 15.057  1.00 19.56  ? 14  ASN   C ND2  1 
ATOM   3725 N  N    . THR   C 1 15  ? 4.901   -15.098 13.911  1.00 21.65  ? 15  THR   C N    1 
ATOM   3726 C  CA   . THR   C 1 15  ? 6.065   -14.542 13.185  1.00 24.28  ? 15  THR   C CA   1 
ATOM   3727 C  C    . THR   C 1 15  ? 6.324   -15.348 11.914  1.00 26.25  ? 15  THR   C C    1 
ATOM   3728 O  O    . THR   C 1 15  ? 6.959   -14.781 11.014  1.00 26.59  ? 15  THR   C O    1 
ATOM   3729 C  CB   . THR   C 1 15  ? 7.316   -14.474 14.065  1.00 25.42  ? 15  THR   C CB   1 
ATOM   3730 O  OG1  . THR   C 1 15  ? 7.650   -15.798 14.469  1.00 27.79  ? 15  THR   C OG1  1 
ATOM   3731 C  CG2  . THR   C 1 15  ? 7.114   -13.602 15.281  1.00 25.99  ? 15  THR   C CG2  1 
ATOM   3732 N  N    . ASP   C 1 16  ? 5.826   -16.590 11.831  1.00 29.17  ? 16  ASP   C N    1 
ATOM   3733 C  CA   . ASP   C 1 16  ? 5.961   -17.473 10.636  1.00 31.90  ? 16  ASP   C CA   1 
ATOM   3734 C  C    . ASP   C 1 16  ? 5.053   -17.019 9.485   1.00 30.68  ? 16  ASP   C C    1 
ATOM   3735 O  O    . ASP   C 1 16  ? 5.159   -17.618 8.412   1.00 33.55  ? 16  ASP   C O    1 
ATOM   3736 C  CB   . ASP   C 1 16  ? 5.626   -18.930 10.965  1.00 34.57  ? 16  ASP   C CB   1 
ATOM   3737 C  CG   . ASP   C 1 16  ? 4.136   -19.154 11.157  1.00 38.86  ? 16  ASP   C CG   1 
ATOM   3738 O  OD1  . ASP   C 1 16  ? 3.525   -18.430 11.990  1.00 40.40  ? 16  ASP   C OD1  1 
ATOM   3739 O  OD2  . ASP   C 1 16  ? 3.593   -20.028 10.462  1.00 44.80  ? 16  ASP   C OD2  1 
ATOM   3740 N  N    . ILE   C 1 17  ? 4.159   -16.046 9.687   1.00 30.55  ? 17  ILE   C N    1 
ATOM   3741 C  CA   . ILE   C 1 17  ? 3.316   -15.487 8.580   1.00 30.42  ? 17  ILE   C CA   1 
ATOM   3742 C  C    . ILE   C 1 17  ? 3.388   -13.949 8.576   1.00 29.67  ? 17  ILE   C C    1 
ATOM   3743 O  O    . ILE   C 1 17  ? 2.408   -13.298 8.159   1.00 31.50  ? 17  ILE   C O    1 
ATOM   3744 C  CB   . ILE   C 1 17  ? 1.876   -16.021 8.665   1.00 30.08  ? 17  ILE   C CB   1 
ATOM   3745 C  CG1  . ILE   C 1 17  ? 1.192   -15.644 9.984   1.00 30.55  ? 17  ILE   C CG1  1 
ATOM   3746 C  CG2  . ILE   C 1 17  ? 1.872   -17.527 8.425   1.00 30.91  ? 17  ILE   C CG2  1 
ATOM   3747 C  CD1  . ILE   C 1 17  ? -0.298  -15.889 9.997   1.00 31.60  ? 17  ILE   C CD1  1 
ATOM   3748 N  N    . GLY   C 1 18  ? 4.521   -13.385 8.998   1.00 26.30  ? 18  GLY   C N    1 
ATOM   3749 C  CA   . GLY   C 1 18  ? 4.889   -11.989 8.707   1.00 25.04  ? 18  GLY   C CA   1 
ATOM   3750 C  C    . GLY   C 1 18  ? 4.557   -11.031 9.833   1.00 23.00  ? 18  GLY   C C    1 
ATOM   3751 O  O    . GLY   C 1 18  ? 4.826   -9.861  9.660   1.00 24.78  ? 18  GLY   C O    1 
ATOM   3752 N  N    . ASP   C 1 19  ? 3.930   -11.483 10.918  1.00 22.13  ? 19  ASP   C N    1 
ATOM   3753 C  CA   . ASP   C 1 19  ? 3.647   -10.628 12.102  1.00 20.23  ? 19  ASP   C CA   1 
ATOM   3754 C  C    . ASP   C 1 19  ? 4.981   -10.201 12.699  1.00 20.77  ? 19  ASP   C C    1 
ATOM   3755 O  O    . ASP   C 1 19  ? 5.910   -11.007 12.767  1.00 21.29  ? 19  ASP   C O    1 
ATOM   3756 C  CB   . ASP   C 1 19  ? 2.890   -11.363 13.220  1.00 18.37  ? 19  ASP   C CB   1 
ATOM   3757 C  CG   . ASP   C 1 19  ? 1.372   -11.417 13.105  1.00 16.48  ? 19  ASP   C CG   1 
ATOM   3758 O  OD1  . ASP   C 1 19  ? 0.819   -10.757 12.199  1.00 15.73  ? 19  ASP   C OD1  1 
ATOM   3759 O  OD2  . ASP   C 1 19  ? 0.756   -12.127 13.929  1.00 14.60  ? 19  ASP   C OD2  1 
ATOM   3760 N  N    . PRO   C 1 20  ? 5.107   -8.962  13.207  1.00 21.32  ? 20  PRO   C N    1 
ATOM   3761 C  CA   . PRO   C 1 20  ? 6.258   -8.601  14.037  1.00 22.40  ? 20  PRO   C CA   1 
ATOM   3762 C  C    . PRO   C 1 20  ? 6.191   -9.393  15.358  1.00 24.01  ? 20  PRO   C C    1 
ATOM   3763 O  O    . PRO   C 1 20  ? 5.173   -10.033 15.621  1.00 24.86  ? 20  PRO   C O    1 
ATOM   3764 C  CB   . PRO   C 1 20  ? 6.077   -7.089  14.244  1.00 21.79  ? 20  PRO   C CB   1 
ATOM   3765 C  CG   . PRO   C 1 20  ? 4.575   -6.888  14.156  1.00 22.02  ? 20  PRO   C CG   1 
ATOM   3766 C  CD   . PRO   C 1 20  ? 4.127   -7.870  13.092  1.00 21.80  ? 20  PRO   C CD   1 
ATOM   3767 N  N    . SER   C 1 21  ? 7.236   -9.310  16.172  1.00 24.13  ? 21  SER   C N    1 
ATOM   3768 C  CA   . SER   C 1 21  ? 7.448   -10.126 17.392  1.00 27.03  ? 21  SER   C CA   1 
ATOM   3769 C  C    . SER   C 1 21  ? 6.753   -9.509  18.605  1.00 26.90  ? 21  SER   C C    1 
ATOM   3770 O  O    . SER   C 1 21  ? 7.157   -9.838  19.737  1.00 28.98  ? 21  SER   C O    1 
ATOM   3771 C  CB   . SER   C 1 21  ? 8.927   -10.271 17.670  1.00 31.16  ? 21  SER   C CB   1 
ATOM   3772 O  OG   . SER   C 1 21  ? 9.598   -10.739 16.514  1.00 36.40  ? 21  SER   C OG   1 
ATOM   3773 N  N    . TYR   C 1 22  ? 5.764   -8.642  18.401  1.00 25.68  ? 22  TYR   C N    1 
ATOM   3774 C  CA   . TYR   C 1 22  ? 5.006   -7.985  19.501  1.00 22.56  ? 22  TYR   C CA   1 
ATOM   3775 C  C    . TYR   C 1 22  ? 3.532   -7.796  19.102  1.00 20.20  ? 22  TYR   C C    1 
ATOM   3776 O  O    . TYR   C 1 22  ? 3.181   -7.815  17.919  1.00 16.24  ? 22  TYR   C O    1 
ATOM   3777 C  CB   . TYR   C 1 22  ? 5.695   -6.663  19.863  1.00 21.85  ? 22  TYR   C CB   1 
ATOM   3778 C  CG   . TYR   C 1 22  ? 6.157   -5.877  18.665  1.00 22.81  ? 22  TYR   C CG   1 
ATOM   3779 C  CD1  . TYR   C 1 22  ? 5.242   -5.233  17.857  1.00 22.18  ? 22  TYR   C CD1  1 
ATOM   3780 C  CD2  . TYR   C 1 22  ? 7.499   -5.801  18.310  1.00 24.10  ? 22  TYR   C CD2  1 
ATOM   3781 C  CE1  . TYR   C 1 22  ? 5.632   -4.545  16.724  1.00 23.05  ? 22  TYR   C CE1  1 
ATOM   3782 C  CE2  . TYR   C 1 22  ? 7.911   -5.101  17.184  1.00 24.52  ? 22  TYR   C CE2  1 
ATOM   3783 C  CZ   . TYR   C 1 22  ? 6.968   -4.472  16.385  1.00 24.34  ? 22  TYR   C CZ   1 
ATOM   3784 O  OH   . TYR   C 1 22  ? 7.310   -3.778  15.257  1.00 25.62  ? 22  TYR   C OH   1 
ATOM   3785 N  N    . PRO   C 1 23  ? 2.641   -7.551  20.090  1.00 18.17  ? 23  PRO   C N    1 
ATOM   3786 C  CA   . PRO   C 1 23  ? 1.269   -7.123  19.811  1.00 18.60  ? 23  PRO   C CA   1 
ATOM   3787 C  C    . PRO   C 1 23  ? 1.298   -5.837  18.966  1.00 17.91  ? 23  PRO   C C    1 
ATOM   3788 O  O    . PRO   C 1 23  ? 2.138   -4.976  19.214  1.00 17.86  ? 23  PRO   C O    1 
ATOM   3789 C  CB   . PRO   C 1 23  ? 0.648   -6.928  21.205  1.00 17.61  ? 23  PRO   C CB   1 
ATOM   3790 C  CG   . PRO   C 1 23  ? 1.501   -7.809  22.088  1.00 18.36  ? 23  PRO   C CG   1 
ATOM   3791 C  CD   . PRO   C 1 23  ? 2.903   -7.675  21.530  1.00 17.78  ? 23  PRO   C CD   1 
ATOM   3792 N  N    . HIS   C 1 24  ? 0.431   -5.761  17.958  1.00 16.01  ? 24  HIS   C N    1 
ATOM   3793 C  CA   . HIS   C 1 24  ? 0.519   -4.740  16.888  1.00 15.85  ? 24  HIS   C CA   1 
ATOM   3794 C  C    . HIS   C 1 24  ? -0.882  -4.393  16.383  1.00 16.13  ? 24  HIS   C C    1 
ATOM   3795 O  O    . HIS   C 1 24  ? -1.803  -5.151  16.600  1.00 14.52  ? 24  HIS   C O    1 
ATOM   3796 C  CB   . HIS   C 1 24  ? 1.446   -5.206  15.750  1.00 15.44  ? 24  HIS   C CB   1 
ATOM   3797 C  CG   . HIS   C 1 24  ? 1.069   -6.517  15.147  1.00 15.99  ? 24  HIS   C CG   1 
ATOM   3798 N  ND1  . HIS   C 1 24  ? 1.273   -7.710  15.798  1.00 16.09  ? 24  HIS   C ND1  1 
ATOM   3799 C  CD2  . HIS   C 1 24  ? 0.463   -6.824  13.971  1.00 16.63  ? 24  HIS   C CD2  1 
ATOM   3800 C  CE1  . HIS   C 1 24  ? 0.814   -8.707  15.054  1.00 16.35  ? 24  HIS   C CE1  1 
ATOM   3801 N  NE2  . HIS   C 1 24  ? 0.310   -8.192  13.924  1.00 16.61  ? 24  HIS   C NE2  1 
ATOM   3802 N  N    . ILE   C 1 25  ? -1.012  -3.223  15.783  1.00 16.59  ? 25  ILE   C N    1 
ATOM   3803 C  CA   . ILE   C 1 25  ? -2.165  -2.881  14.912  1.00 17.88  ? 25  ILE   C CA   1 
ATOM   3804 C  C    . ILE   C 1 25  ? -1.656  -2.953  13.474  1.00 16.74  ? 25  ILE   C C    1 
ATOM   3805 O  O    . ILE   C 1 25  ? -0.441  -2.701  13.213  1.00 16.05  ? 25  ILE   C O    1 
ATOM   3806 C  CB   . ILE   C 1 25  ? -2.736  -1.499  15.287  1.00 18.69  ? 25  ILE   C CB   1 
ATOM   3807 C  CG1  . ILE   C 1 25  ? -1.676  -0.400  15.191  1.00 18.40  ? 25  ILE   C CG1  1 
ATOM   3808 C  CG2  . ILE   C 1 25  ? -3.315  -1.566  16.678  1.00 19.28  ? 25  ILE   C CG2  1 
ATOM   3809 C  CD1  . ILE   C 1 25  ? -2.222  0.957   15.464  1.00 20.18  ? 25  ILE   C CD1  1 
ATOM   3810 N  N    . GLY   C 1 26  ? -2.543  -3.283  12.558  1.00 15.85  ? 26  GLY   C N    1 
ATOM   3811 C  CA   . GLY   C 1 26  ? -2.148  -3.345  11.147  1.00 16.47  ? 26  GLY   C CA   1 
ATOM   3812 C  C    . GLY   C 1 26  ? -3.304  -3.043  10.246  1.00 16.02  ? 26  GLY   C C    1 
ATOM   3813 O  O    . GLY   C 1 26  ? -4.454  -3.142  10.702  1.00 16.41  ? 26  GLY   C O    1 
ATOM   3814 N  N    . ILE   C 1 27  ? -2.977  -2.709  9.006   1.00 17.09  ? 27  ILE   C N    1 
ATOM   3815 C  CA   . ILE   C 1 27  ? -3.956  -2.579  7.897   1.00 17.48  ? 27  ILE   C CA   1 
ATOM   3816 C  C    . ILE   C 1 27  ? -3.814  -3.805  6.995   1.00 17.13  ? 27  ILE   C C    1 
ATOM   3817 O  O    . ILE   C 1 27  ? -2.712  -4.050  6.471   1.00 16.49  ? 27  ILE   C O    1 
ATOM   3818 C  CB   . ILE   C 1 27  ? -3.782  -1.234  7.176   1.00 17.25  ? 27  ILE   C CB   1 
ATOM   3819 C  CG1  . ILE   C 1 27  ? -4.142  -0.089  8.135   1.00 17.94  ? 27  ILE   C CG1  1 
ATOM   3820 C  CG2  . ILE   C 1 27  ? -4.623  -1.219  5.907   1.00 18.21  ? 27  ILE   C CG2  1 
ATOM   3821 C  CD1  . ILE   C 1 27  ? -3.637  1.277   7.733   1.00 19.03  ? 27  ILE   C CD1  1 
ATOM   3822 N  N    . ASP   C 1 28  ? -4.907  -4.549  6.845   1.00 17.19  ? 28  ASP   C N    1 
ATOM   3823 C  CA   . ASP   C 1 28  ? -4.959  -5.805  6.045   1.00 17.97  ? 28  ASP   C CA   1 
ATOM   3824 C  C    . ASP   C 1 28  ? -5.809  -5.576  4.787   1.00 17.10  ? 28  ASP   C C    1 
ATOM   3825 O  O    . ASP   C 1 28  ? -7.015  -5.296  4.912   1.00 19.05  ? 28  ASP   C O    1 
ATOM   3826 C  CB   . ASP   C 1 28  ? -5.536  -6.946  6.887   1.00 17.76  ? 28  ASP   C CB   1 
ATOM   3827 C  CG   . ASP   C 1 28  ? -4.695  -7.312  8.094   1.00 19.66  ? 28  ASP   C CG   1 
ATOM   3828 O  OD1  . ASP   C 1 28  ? -3.544  -6.810  8.190   1.00 18.32  ? 28  ASP   C OD1  1 
ATOM   3829 O  OD2  . ASP   C 1 28  ? -5.200  -8.128  8.936   1.00 21.28  ? 28  ASP   C OD2  1 
ATOM   3830 N  N    . ILE   C 1 29  ? -5.208  -5.691  3.621   1.00 17.07  ? 29  ILE   C N    1 
ATOM   3831 C  CA   . ILE   C 1 29  ? -5.895  -5.587  2.313   1.00 18.21  ? 29  ILE   C CA   1 
ATOM   3832 C  C    . ILE   C 1 29  ? -5.734  -6.922  1.594   1.00 18.70  ? 29  ILE   C C    1 
ATOM   3833 O  O    . ILE   C 1 29  ? -4.611  -7.220  1.151   1.00 17.29  ? 29  ILE   C O    1 
ATOM   3834 C  CB   . ILE   C 1 29  ? -5.309  -4.444  1.467   1.00 19.19  ? 29  ILE   C CB   1 
ATOM   3835 C  CG1  . ILE   C 1 29  ? -5.073  -3.148  2.256   1.00 19.56  ? 29  ILE   C CG1  1 
ATOM   3836 C  CG2  . ILE   C 1 29  ? -6.186  -4.226  0.243   1.00 18.55  ? 29  ILE   C CG2  1 
ATOM   3837 C  CD1  . ILE   C 1 29  ? -6.315  -2.408  2.630   1.00 20.50  ? 29  ILE   C CD1  1 
ATOM   3838 N  N    . LYS   C 1 30  ? -6.822  -7.683  1.462   1.00 20.87  ? 30  LYS   C N    1 
ATOM   3839 C  CA   . LYS   C 1 30  ? -6.892  -8.915  0.641   1.00 22.22  ? 30  LYS   C CA   1 
ATOM   3840 C  C    . LYS   C 1 30  ? -5.998  -10.026 1.201   1.00 23.21  ? 30  LYS   C C    1 
ATOM   3841 O  O    . LYS   C 1 30  ? -5.757  -10.997 0.456   1.00 24.82  ? 30  LYS   C O    1 
ATOM   3842 C  CB   . LYS   C 1 30  ? -6.442  -8.606  -0.792  1.00 25.18  ? 30  LYS   C CB   1 
ATOM   3843 C  CG   . LYS   C 1 30  ? -7.478  -7.873  -1.628  1.00 26.68  ? 30  LYS   C CG   1 
ATOM   3844 C  CD   . LYS   C 1 30  ? -6.877  -7.039  -2.712  1.00 27.15  ? 30  LYS   C CD   1 
ATOM   3845 C  CE   . LYS   C 1 30  ? -6.278  -7.870  -3.822  1.00 29.20  ? 30  LYS   C CE   1 
ATOM   3846 N  NZ   . LYS   C 1 30  ? -5.656  -6.987  -4.840  1.00 30.81  ? 30  LYS   C NZ   1 
ATOM   3847 N  N    . SER   C 1 31  ? -5.500  -9.887  2.431   1.00 22.56  ? 31  SER   C N    1 
ATOM   3848 C  CA   . SER   C 1 31  ? -4.518  -10.811 3.050   1.00 21.04  ? 31  SER   C CA   1 
ATOM   3849 C  C    . SER   C 1 31  ? -4.334  -10.469 4.521   1.00 21.79  ? 31  SER   C C    1 
ATOM   3850 O  O    . SER   C 1 31  ? -4.307  -9.264  4.849   1.00 23.10  ? 31  SER   C O    1 
ATOM   3851 C  CB   . SER   C 1 31  ? -3.205  -10.756 2.367   1.00 21.01  ? 31  SER   C CB   1 
ATOM   3852 O  OG   . SER   C 1 31  ? -2.231  -11.360 3.196   1.00 21.50  ? 31  SER   C OG   1 
ATOM   3853 N  N    . VAL   C 1 32  ? -4.172  -11.496 5.350   1.00 21.80  ? 32  VAL   C N    1 
ATOM   3854 C  CA   . VAL   C 1 32  ? -3.862  -11.376 6.802   1.00 21.78  ? 32  VAL   C CA   1 
ATOM   3855 C  C    . VAL   C 1 32  ? -2.446  -10.820 7.001   1.00 21.73  ? 32  VAL   C C    1 
ATOM   3856 O  O    . VAL   C 1 32  ? -2.176  -10.354 8.112   1.00 22.22  ? 32  VAL   C O    1 
ATOM   3857 C  CB   . VAL   C 1 32  ? -4.005  -12.730 7.517   1.00 24.18  ? 32  VAL   C CB   1 
ATOM   3858 C  CG1  . VAL   C 1 32  ? -2.757  -13.599 7.355   1.00 23.77  ? 32  VAL   C CG1  1 
ATOM   3859 C  CG2  . VAL   C 1 32  ? -4.346  -12.533 8.993   1.00 26.28  ? 32  VAL   C CG2  1 
ATOM   3860 N  N    . ARG   C 1 33  ? -1.565  -10.897 6.004   1.00 21.02  ? 33  ARG   C N    1 
ATOM   3861 C  CA   . ARG   C 1 33  ? -0.194  -10.331 6.099   1.00 21.54  ? 33  ARG   C CA   1 
ATOM   3862 C  C    . ARG   C 1 33  ? -0.288  -8.827  5.877   1.00 19.90  ? 33  ARG   C C    1 
ATOM   3863 O  O    . ARG   C 1 33  ? -0.308  -8.410  4.704   1.00 18.31  ? 33  ARG   C O    1 
ATOM   3864 C  CB   . ARG   C 1 33  ? 0.766   -10.922 5.061   1.00 24.00  ? 33  ARG   C CB   1 
ATOM   3865 C  CG   . ARG   C 1 33  ? 1.196   -12.340 5.383   1.00 26.79  ? 33  ARG   C CG   1 
ATOM   3866 C  CD   . ARG   C 1 33  ? 2.034   -12.995 4.303   1.00 28.11  ? 33  ARG   C CD   1 
ATOM   3867 N  NE   . ARG   C 1 33  ? 1.939   -14.447 4.464   1.00 30.56  ? 33  ARG   C NE   1 
ATOM   3868 C  CZ   . ARG   C 1 33  ? 2.897   -15.262 4.908   1.00 32.09  ? 33  ARG   C CZ   1 
ATOM   3869 N  NH1  . ARG   C 1 33  ? 4.093   -14.806 5.251   1.00 33.76  ? 33  ARG   C NH1  1 
ATOM   3870 N  NH2  . ARG   C 1 33  ? 2.647   -16.553 4.992   1.00 31.19  ? 33  ARG   C NH2  1 
ATOM   3871 N  N    . SER   C 1 34  ? -0.293  -8.073  6.974   1.00 17.96  ? 34  SER   C N    1 
ATOM   3872 C  CA   . SER   C 1 34  ? -0.580  -6.624  7.017   1.00 18.41  ? 34  SER   C CA   1 
ATOM   3873 C  C    . SER   C 1 34  ? 0.259   -5.875  6.000   1.00 18.15  ? 34  SER   C C    1 
ATOM   3874 O  O    . SER   C 1 34  ? 1.444   -6.169  5.912   1.00 19.63  ? 34  SER   C O    1 
ATOM   3875 C  CB   . SER   C 1 34  ? -0.335  -6.101  8.390   1.00 18.14  ? 34  SER   C CB   1 
ATOM   3876 O  OG   . SER   C 1 34  ? -1.224  -6.730  9.285   1.00 19.33  ? 34  SER   C OG   1 
ATOM   3877 N  N    . LYS   C 1 35  ? -0.326  -4.890  5.328   1.00 18.10  ? 35  LYS   C N    1 
ATOM   3878 C  CA   . LYS   C 1 35  ? 0.418   -3.977  4.427   1.00 19.95  ? 35  LYS   C CA   1 
ATOM   3879 C  C    . LYS   C 1 35  ? 1.226   -2.953  5.248   1.00 19.74  ? 35  LYS   C C    1 
ATOM   3880 O  O    . LYS   C 1 35  ? 2.192   -2.395  4.713   1.00 17.54  ? 35  LYS   C O    1 
ATOM   3881 C  CB   . LYS   C 1 35  ? -0.562  -3.322  3.456   1.00 22.40  ? 35  LYS   C CB   1 
ATOM   3882 C  CG   . LYS   C 1 35  ? -1.373  -4.319  2.630   1.00 23.81  ? 35  LYS   C CG   1 
ATOM   3883 C  CD   . LYS   C 1 35  ? -0.610  -4.834  1.473   1.00 25.01  ? 35  LYS   C CD   1 
ATOM   3884 C  CE   . LYS   C 1 35  ? -1.453  -5.650  0.525   1.00 25.33  ? 35  LYS   C CE   1 
ATOM   3885 N  NZ   . LYS   C 1 35  ? -1.749  -6.990  1.070   1.00 27.17  ? 35  LYS   C NZ   1 
ATOM   3886 N  N    . LYS   C 1 36  ? 0.833   -2.703  6.496   1.00 20.25  ? 36  LYS   C N    1 
ATOM   3887 C  CA   . LYS   C 1 36  ? 1.546   -1.801  7.433   1.00 20.31  ? 36  LYS   C CA   1 
ATOM   3888 C  C    . LYS   C 1 36  ? 1.134   -2.184  8.853   1.00 17.90  ? 36  LYS   C C    1 
ATOM   3889 O  O    . LYS   C 1 36  ? -0.027  -2.559  9.065   1.00 17.33  ? 36  LYS   C O    1 
ATOM   3890 C  CB   . LYS   C 1 36  ? 1.238   -0.346  7.067   1.00 25.04  ? 36  LYS   C CB   1 
ATOM   3891 C  CG   . LYS   C 1 36  ? 2.065   0.712   7.796   1.00 29.83  ? 36  LYS   C CG   1 
ATOM   3892 C  CD   . LYS   C 1 36  ? 3.411   1.075   7.170   1.00 31.78  ? 36  LYS   C CD   1 
ATOM   3893 C  CE   . LYS   C 1 36  ? 3.327   2.106   6.068   1.00 36.69  ? 36  LYS   C CE   1 
ATOM   3894 N  NZ   . LYS   C 1 36  ? 2.954   3.454   6.570   1.00 37.90  ? 36  LYS   C NZ   1 
ATOM   3895 N  N    . THR   C 1 37  ? 2.065   -2.097  9.795   1.00 16.75  ? 37  THR   C N    1 
ATOM   3896 C  CA   . THR   C 1 37  ? 1.865   -2.458  11.212  1.00 15.82  ? 37  THR   C CA   1 
ATOM   3897 C  C    . THR   C 1 37  ? 2.577   -1.455  12.111  1.00 15.64  ? 37  THR   C C    1 
ATOM   3898 O  O    . THR   C 1 37  ? 3.564   -0.805  11.657  1.00 14.89  ? 37  THR   C O    1 
ATOM   3899 C  CB   . THR   C 1 37  ? 2.451   -3.837  11.521  1.00 16.10  ? 37  THR   C CB   1 
ATOM   3900 O  OG1  . THR   C 1 37  ? 3.827   -3.647  11.249  1.00 16.79  ? 37  THR   C OG1  1 
ATOM   3901 C  CG2  . THR   C 1 37  ? 1.883   -4.959  10.678  1.00 16.32  ? 37  THR   C CG2  1 
ATOM   3902 N  N    . ALA   C 1 38  ? 2.129   -1.350  13.356  1.00 14.32  ? 38  ALA   C N    1 
ATOM   3903 C  CA   . ALA   C 1 38  ? 2.841   -0.567  14.378  1.00 15.25  ? 38  ALA   C CA   1 
ATOM   3904 C  C    . ALA   C 1 38  ? 2.681   -1.329  15.689  1.00 15.84  ? 38  ALA   C C    1 
ATOM   3905 O  O    . ALA   C 1 38  ? 1.632   -1.946  15.856  1.00 13.52  ? 38  ALA   C O    1 
ATOM   3906 C  CB   . ALA   C 1 38  ? 2.319   0.856   14.467  1.00 14.39  ? 38  ALA   C CB   1 
ATOM   3907 N  N    . LYS   C 1 39  ? 3.723   -1.303  16.520  1.00 16.78  ? 39  LYS   C N    1 
ATOM   3908 C  CA   . LYS   C 1 39  ? 3.743   -1.883  17.879  1.00 18.46  ? 39  LYS   C CA   1 
ATOM   3909 C  C    . LYS   C 1 39  ? 2.565   -1.331  18.670  1.00 17.35  ? 39  LYS   C C    1 
ATOM   3910 O  O    . LYS   C 1 39  ? 2.322   -0.109  18.606  1.00 14.95  ? 39  LYS   C O    1 
ATOM   3911 C  CB   . LYS   C 1 39  ? 5.052   -1.542  18.599  1.00 21.13  ? 39  LYS   C CB   1 
ATOM   3912 C  CG   . LYS   C 1 39  ? 5.238   -2.239  19.936  1.00 23.43  ? 39  LYS   C CG   1 
ATOM   3913 C  CD   . LYS   C 1 39  ? 6.647   -2.116  20.472  1.00 26.33  ? 39  LYS   C CD   1 
ATOM   3914 C  CE   . LYS   C 1 39  ? 6.736   -2.416  21.955  1.00 30.27  ? 39  LYS   C CE   1 
ATOM   3915 N  NZ   . LYS   C 1 39  ? 6.763   -3.874  22.240  1.00 33.03  ? 39  LYS   C NZ   1 
ATOM   3916 N  N    . TRP   C 1 40  ? 1.905   -2.224  19.410  1.00 18.12  ? 40  TRP   C N    1 
ATOM   3917 C  CA   . TRP   C 1 40  ? 0.726   -1.909  20.245  1.00 19.05  ? 40  TRP   C CA   1 
ATOM   3918 C  C    . TRP   C 1 40  ? 0.955   -2.454  21.645  1.00 19.12  ? 40  TRP   C C    1 
ATOM   3919 O  O    . TRP   C 1 40  ? 1.035   -3.657  21.776  1.00 18.46  ? 40  TRP   C O    1 
ATOM   3920 C  CB   . TRP   C 1 40  ? -0.547  -2.488  19.613  1.00 20.03  ? 40  TRP   C CB   1 
ATOM   3921 C  CG   . TRP   C 1 40  ? -1.791  -2.251  20.412  1.00 20.17  ? 40  TRP   C CG   1 
ATOM   3922 C  CD1  . TRP   C 1 40  ? -2.139  -1.095  21.054  1.00 20.35  ? 40  TRP   C CD1  1 
ATOM   3923 C  CD2  . TRP   C 1 40  ? -2.883  -3.168  20.616  1.00 20.56  ? 40  TRP   C CD2  1 
ATOM   3924 N  NE1  . TRP   C 1 40  ? -3.351  -1.239  21.670  1.00 20.48  ? 40  TRP   C NE1  1 
ATOM   3925 C  CE2  . TRP   C 1 40  ? -3.825  -2.507  21.432  1.00 20.82  ? 40  TRP   C CE2  1 
ATOM   3926 C  CE3  . TRP   C 1 40  ? -3.151  -4.483  20.212  1.00 20.72  ? 40  TRP   C CE3  1 
ATOM   3927 C  CZ2  . TRP   C 1 40  ? -5.026  -3.109  21.814  1.00 20.59  ? 40  TRP   C CZ2  1 
ATOM   3928 C  CZ3  . TRP   C 1 40  ? -4.319  -5.083  20.620  1.00 20.09  ? 40  TRP   C CZ3  1 
ATOM   3929 C  CH2  . TRP   C 1 40  ? -5.245  -4.400  21.399  1.00 20.26  ? 40  TRP   C CH2  1 
ATOM   3930 N  N    . ASN   C 1 41  ? 1.012   -1.583  22.646  1.00 21.83  ? 41  ASN   C N    1 
ATOM   3931 C  CA   . ASN   C 1 41  ? 1.018   -1.979  24.079  1.00 23.97  ? 41  ASN   C CA   1 
ATOM   3932 C  C    . ASN   C 1 41  ? -0.426  -2.214  24.537  1.00 23.95  ? 41  ASN   C C    1 
ATOM   3933 O  O    . ASN   C 1 41  ? -0.995  -1.338  25.222  1.00 23.76  ? 41  ASN   C O    1 
ATOM   3934 C  CB   . ASN   C 1 41  ? 1.758   -0.949  24.923  1.00 25.12  ? 41  ASN   C CB   1 
ATOM   3935 C  CG   . ASN   C 1 41  ? 3.210   -0.848  24.517  1.00 28.60  ? 41  ASN   C CG   1 
ATOM   3936 O  OD1  . ASN   C 1 41  ? 3.837   -1.859  24.182  1.00 33.96  ? 41  ASN   C OD1  1 
ATOM   3937 N  ND2  . ASN   C 1 41  ? 3.737   0.366   24.499  1.00 28.74  ? 41  ASN   C ND2  1 
ATOM   3938 N  N    . MET   C 1 42  ? -0.987  -3.360  24.145  1.00 25.59  ? 42  MET   C N    1 
ATOM   3939 C  CA   . MET   C 1 42  ? -2.267  -3.905  24.669  1.00 28.18  ? 42  MET   C CA   1 
ATOM   3940 C  C    . MET   C 1 42  ? -2.136  -3.973  26.199  1.00 27.28  ? 42  MET   C C    1 
ATOM   3941 O  O    . MET   C 1 42  ? -1.062  -4.378  26.680  1.00 27.72  ? 42  MET   C O    1 
ATOM   3942 C  CB   . MET   C 1 42  ? -2.570  -5.296  24.088  1.00 29.24  ? 42  MET   C CB   1 
ATOM   3943 C  CG   . MET   C 1 42  ? -4.008  -5.767  24.316  1.00 31.54  ? 42  MET   C CG   1 
ATOM   3944 S  SD   . MET   C 1 42  ? -4.332  -6.716  25.868  1.00 34.76  ? 42  MET   C SD   1 
ATOM   3945 C  CE   . MET   C 1 42  ? -3.174  -8.065  25.641  1.00 35.43  ? 42  MET   C CE   1 
ATOM   3946 N  N    . GLN   C 1 43  ? -3.171  -3.547  26.927  1.00 26.03  ? 43  GLN   C N    1 
ATOM   3947 C  CA   . GLN   C 1 43  ? -3.209  -3.536  28.411  1.00 26.13  ? 43  GLN   C CA   1 
ATOM   3948 C  C    . GLN   C 1 43  ? -4.312  -4.494  28.833  1.00 26.82  ? 43  GLN   C C    1 
ATOM   3949 O  O    . GLN   C 1 43  ? -5.522  -4.120  28.707  1.00 27.10  ? 43  GLN   C O    1 
ATOM   3950 C  CB   . GLN   C 1 43  ? -3.485  -2.141  28.978  1.00 27.68  ? 43  GLN   C CB   1 
ATOM   3951 C  CG   . GLN   C 1 43  ? -2.274  -1.229  28.974  1.00 29.34  ? 43  GLN   C CG   1 
ATOM   3952 C  CD   . GLN   C 1 43  ? -2.706  0.175   29.290  1.00 29.79  ? 43  GLN   C CD   1 
ATOM   3953 O  OE1  . GLN   C 1 43  ? -3.503  0.393   30.199  1.00 33.65  ? 43  GLN   C OE1  1 
ATOM   3954 N  NE2  . GLN   C 1 43  ? -2.214  1.127   28.518  1.00 29.01  ? 43  GLN   C NE2  1 
ATOM   3955 N  N    . ASN   C 1 44  ? -3.895  -5.677  29.268  1.00 26.72  ? 44  ASN   C N    1 
ATOM   3956 C  CA   . ASN   C 1 44  ? -4.783  -6.770  29.729  1.00 28.17  ? 44  ASN   C CA   1 
ATOM   3957 C  C    . ASN   C 1 44  ? -5.763  -6.194  30.753  1.00 25.50  ? 44  ASN   C C    1 
ATOM   3958 O  O    . ASN   C 1 44  ? -5.331  -5.593  31.707  1.00 23.68  ? 44  ASN   C O    1 
ATOM   3959 C  CB   . ASN   C 1 44  ? -3.988  -7.943  30.304  1.00 29.81  ? 44  ASN   C CB   1 
ATOM   3960 C  CG   . ASN   C 1 44  ? -4.780  -9.231  30.281  1.00 32.26  ? 44  ASN   C CG   1 
ATOM   3961 O  OD1  . ASN   C 1 44  ? -6.003  -9.220  30.400  1.00 31.82  ? 44  ASN   C OD1  1 
ATOM   3962 N  ND2  . ASN   C 1 44  ? -4.092  -10.346 30.118  1.00 35.65  ? 44  ASN   C ND2  1 
ATOM   3963 N  N    . GLY   C 1 45  ? -7.054  -6.344  30.511  1.00 26.04  ? 45  GLY   C N    1 
ATOM   3964 C  CA   . GLY   C 1 45  ? -8.090  -6.043  31.508  1.00 26.66  ? 45  GLY   C CA   1 
ATOM   3965 C  C    . GLY   C 1 45  ? -8.562  -4.611  31.431  1.00 27.78  ? 45  GLY   C C    1 
ATOM   3966 O  O    . GLY   C 1 45  ? -9.409  -4.262  32.256  1.00 27.53  ? 45  GLY   C O    1 
ATOM   3967 N  N    . LYS   C 1 46  ? -8.103  -3.818  30.454  1.00 30.57  ? 46  LYS   C N    1 
ATOM   3968 C  CA   . LYS   C 1 46  ? -8.469  -2.372  30.396  1.00 31.49  ? 46  LYS   C CA   1 
ATOM   3969 C  C    . LYS   C 1 46  ? -9.271  -2.077  29.115  1.00 26.17  ? 46  LYS   C C    1 
ATOM   3970 O  O    . LYS   C 1 46  ? -9.118  -2.799  28.113  1.00 28.40  ? 46  LYS   C O    1 
ATOM   3971 C  CB   . LYS   C 1 46  ? -7.216  -1.509  30.613  1.00 37.24  ? 46  LYS   C CB   1 
ATOM   3972 C  CG   . LYS   C 1 46  ? -7.472  -0.021  30.881  1.00 46.15  ? 46  LYS   C CG   1 
ATOM   3973 C  CD   . LYS   C 1 46  ? -8.584  0.307   31.919  1.00 53.55  ? 46  LYS   C CD   1 
ATOM   3974 C  CE   . LYS   C 1 46  ? -9.113  1.731   31.844  1.00 55.22  ? 46  LYS   C CE   1 
ATOM   3975 N  NZ   . LYS   C 1 46  ? -9.925  1.976   30.625  1.00 53.80  ? 46  LYS   C NZ   1 
ATOM   3976 N  N    . VAL   C 1 47  ? -10.163 -1.094  29.206  1.00 23.90  ? 47  VAL   C N    1 
ATOM   3977 C  CA   . VAL   C 1 47  ? -11.049 -0.582  28.121  1.00 23.10  ? 47  VAL   C CA   1 
ATOM   3978 C  C    . VAL   C 1 47  ? -10.235 0.381   27.264  1.00 22.48  ? 47  VAL   C C    1 
ATOM   3979 O  O    . VAL   C 1 47  ? -9.801  1.420   27.789  1.00 26.04  ? 47  VAL   C O    1 
ATOM   3980 C  CB   . VAL   C 1 47  ? -12.314 0.121   28.667  1.00 22.35  ? 47  VAL   C CB   1 
ATOM   3981 C  CG1  . VAL   C 1 47  ? -13.187 0.633   27.534  1.00 21.95  ? 47  VAL   C CG1  1 
ATOM   3982 C  CG2  . VAL   C 1 47  ? -13.115 -0.792  29.584  1.00 22.93  ? 47  VAL   C CG2  1 
ATOM   3983 N  N    . GLY   C 1 48  ? -10.043 0.037   25.997  1.00 20.70  ? 48  GLY   C N    1 
ATOM   3984 C  CA   . GLY   C 1 48  ? -9.407  0.896   24.991  1.00 19.02  ? 48  GLY   C CA   1 
ATOM   3985 C  C    . GLY   C 1 48  ? -10.408 1.357   23.954  1.00 18.50  ? 48  GLY   C C    1 
ATOM   3986 O  O    . GLY   C 1 48  ? -11.598 0.894   23.967  1.00 17.25  ? 48  GLY   C O    1 
ATOM   3987 N  N    . THR   C 1 49  ? -9.928  2.231   23.072  1.00 18.71  ? 49  THR   C N    1 
ATOM   3988 C  CA   . THR   C 1 49  ? -10.703 2.913   22.010  1.00 18.21  ? 49  THR   C CA   1 
ATOM   3989 C  C    . THR   C 1 49  ? -9.951  2.785   20.685  1.00 16.23  ? 49  THR   C C    1 
ATOM   3990 O  O    . THR   C 1 49  ? -8.716  3.010   20.640  1.00 14.21  ? 49  THR   C O    1 
ATOM   3991 C  CB   . THR   C 1 49  ? -10.942 4.374   22.393  1.00 21.07  ? 49  THR   C CB   1 
ATOM   3992 O  OG1  . THR   C 1 49  ? -11.561 4.366   23.681  1.00 22.70  ? 49  THR   C OG1  1 
ATOM   3993 C  CG2  . THR   C 1 49  ? -11.804 5.111   21.392  1.00 22.00  ? 49  THR   C CG2  1 
ATOM   3994 N  N    . ALA   C 1 50  ? -10.681 2.398   19.648  1.00 15.45  ? 50  ALA   C N    1 
ATOM   3995 C  CA   . ALA   C 1 50  ? -10.184 2.321   18.271  1.00 15.66  ? 50  ALA   C CA   1 
ATOM   3996 C  C    . ALA   C 1 50  ? -10.918 3.385   17.468  1.00 16.64  ? 50  ALA   C C    1 
ATOM   3997 O  O    . ALA   C 1 50  ? -12.179 3.433   17.511  1.00 17.66  ? 50  ALA   C O    1 
ATOM   3998 C  CB   . ALA   C 1 50  ? -10.396 0.942   17.742  1.00 15.79  ? 50  ALA   C CB   1 
ATOM   3999 N  N    . HIS   C 1 51  ? -10.150 4.203   16.767  1.00 16.76  ? 51  HIS   C N    1 
ATOM   4000 C  CA   . HIS   C 1 51  ? -10.637 5.246   15.850  1.00 16.70  ? 51  HIS   C CA   1 
ATOM   4001 C  C    . HIS   C 1 51  ? -10.055 4.950   14.480  1.00 16.72  ? 51  HIS   C C    1 
ATOM   4002 O  O    . HIS   C 1 51  ? -8.808  4.904   14.385  1.00 16.78  ? 51  HIS   C O    1 
ATOM   4003 C  CB   . HIS   C 1 51  ? -10.236 6.628   16.379  1.00 17.53  ? 51  HIS   C CB   1 
ATOM   4004 C  CG   . HIS   C 1 51  ? -10.949 7.748   15.707  1.00 17.71  ? 51  HIS   C CG   1 
ATOM   4005 N  ND1  . HIS   C 1 51  ? -10.657 9.073   15.964  1.00 18.73  ? 51  HIS   C ND1  1 
ATOM   4006 C  CD2  . HIS   C 1 51  ? -11.940 7.746   14.796  1.00 19.55  ? 51  HIS   C CD2  1 
ATOM   4007 C  CE1  . HIS   C 1 51  ? -11.442 9.843   15.248  1.00 20.12  ? 51  HIS   C CE1  1 
ATOM   4008 N  NE2  . HIS   C 1 51  ? -12.234 9.053   14.503  1.00 19.83  ? 51  HIS   C NE2  1 
ATOM   4009 N  N    . ILE   C 1 52  ? -10.923 4.771   13.482  1.00 16.04  ? 52  ILE   C N    1 
ATOM   4010 C  CA   . ILE   C 1 52  ? -10.544 4.408   12.088  1.00 15.94  ? 52  ILE   C CA   1 
ATOM   4011 C  C    . ILE   C 1 52  ? -11.168 5.417   11.128  1.00 15.41  ? 52  ILE   C C    1 
ATOM   4012 O  O    . ILE   C 1 52  ? -12.403 5.600   11.191  1.00 16.90  ? 52  ILE   C O    1 
ATOM   4013 C  CB   . ILE   C 1 52  ? -11.019 2.978   11.778  1.00 16.44  ? 52  ILE   C CB   1 
ATOM   4014 C  CG1  . ILE   C 1 52  ? -10.326 1.958   12.679  1.00 17.52  ? 52  ILE   C CG1  1 
ATOM   4015 C  CG2  . ILE   C 1 52  ? -10.848 2.645   10.311  1.00 16.26  ? 52  ILE   C CG2  1 
ATOM   4016 C  CD1  . ILE   C 1 52  ? -11.218 0.810   13.076  1.00 18.54  ? 52  ILE   C CD1  1 
ATOM   4017 N  N    . ILE   C 1 53  ? -10.378 5.972   10.215  1.00 14.58  ? 53  ILE   C N    1 
ATOM   4018 C  CA   . ILE   C 1 53  ? -10.875 6.907   9.166   1.00 15.03  ? 53  ILE   C CA   1 
ATOM   4019 C  C    . ILE   C 1 53  ? -10.346 6.436   7.815   1.00 15.63  ? 53  ILE   C C    1 
ATOM   4020 O  O    . ILE   C 1 53  ? -9.136  6.096   7.726   1.00 15.78  ? 53  ILE   C O    1 
ATOM   4021 C  CB   . ILE   C 1 53  ? -10.457 8.362   9.460   1.00 14.86  ? 53  ILE   C CB   1 
ATOM   4022 C  CG1  . ILE   C 1 53  ? -11.027 8.850   10.786  1.00 15.18  ? 53  ILE   C CG1  1 
ATOM   4023 C  CG2  . ILE   C 1 53  ? -10.860 9.280   8.320   1.00 14.91  ? 53  ILE   C CG2  1 
ATOM   4024 C  CD1  . ILE   C 1 53  ? -10.698 10.288  11.112  1.00 15.69  ? 53  ILE   C CD1  1 
ATOM   4025 N  N    . TYR   C 1 54  ? -11.245 6.362   6.832   1.00 15.28  ? 54  TYR   C N    1 
ATOM   4026 C  CA   . TYR   C 1 54  ? -10.920 6.353   5.384   1.00 15.67  ? 54  TYR   C CA   1 
ATOM   4027 C  C    . TYR   C 1 54  ? -11.277 7.732   4.831   1.00 15.41  ? 54  TYR   C C    1 
ATOM   4028 O  O    . TYR   C 1 54  ? -12.464 8.106   4.822   1.00 14.42  ? 54  TYR   C O    1 
ATOM   4029 C  CB   . TYR   C 1 54  ? -11.641 5.258   4.586   1.00 14.68  ? 54  TYR   C CB   1 
ATOM   4030 C  CG   . TYR   C 1 54  ? -11.158 5.211   3.157   1.00 14.55  ? 54  TYR   C CG   1 
ATOM   4031 C  CD1  . TYR   C 1 54  ? -9.851  4.830   2.872   1.00 14.91  ? 54  TYR   C CD1  1 
ATOM   4032 C  CD2  . TYR   C 1 54  ? -11.954 5.621   2.100   1.00 14.91  ? 54  TYR   C CD2  1 
ATOM   4033 C  CE1  . TYR   C 1 54  ? -9.355  4.842   1.586   1.00 13.99  ? 54  TYR   C CE1  1 
ATOM   4034 C  CE2  . TYR   C 1 54  ? -11.480 5.622   0.800   1.00 14.80  ? 54  TYR   C CE2  1 
ATOM   4035 C  CZ   . TYR   C 1 54  ? -10.175 5.229   0.543   1.00 14.67  ? 54  TYR   C CZ   1 
ATOM   4036 O  OH   . TYR   C 1 54  ? -9.678  5.184   -0.719  1.00 13.64  ? 54  TYR   C OH   1 
ATOM   4037 N  N    . ASN   C 1 55  ? -10.261 8.480   4.423   1.00 17.12  ? 55  ASN   C N    1 
ATOM   4038 C  CA   . ASN   C 1 55  ? -10.424 9.830   3.848   1.00 18.52  ? 55  ASN   C CA   1 
ATOM   4039 C  C    . ASN   C 1 55  ? -10.333 9.705   2.319   1.00 20.05  ? 55  ASN   C C    1 
ATOM   4040 O  O    . ASN   C 1 55  ? -9.236  9.427   1.834   1.00 20.90  ? 55  ASN   C O    1 
ATOM   4041 C  CB   . ASN   C 1 55  ? -9.378  10.764  4.450   1.00 18.85  ? 55  ASN   C CB   1 
ATOM   4042 C  CG   . ASN   C 1 55  ? -9.629  12.212  4.087   1.00 18.03  ? 55  ASN   C CG   1 
ATOM   4043 O  OD1  . ASN   C 1 55  ? -10.631 12.514  3.456   1.00 18.32  ? 55  ASN   C OD1  1 
ATOM   4044 N  ND2  . ASN   C 1 55  ? -8.723  13.101  4.451   1.00 17.67  ? 55  ASN   C ND2  1 
ATOM   4045 N  N    . SER   C 1 56  ? -11.442 9.881   1.592   1.00 20.73  ? 56  SER   C N    1 
ATOM   4046 C  CA   . SER   C 1 56  ? -11.493 9.714   0.109   1.00 22.89  ? 56  SER   C CA   1 
ATOM   4047 C  C    . SER   C 1 56  ? -10.646 10.782  -0.592  1.00 22.75  ? 56  SER   C C    1 
ATOM   4048 O  O    . SER   C 1 56  ? -10.145 10.483  -1.666  1.00 23.78  ? 56  SER   C O    1 
ATOM   4049 C  CB   . SER   C 1 56  ? -12.918 9.669   -0.438  1.00 23.63  ? 56  SER   C CB   1 
ATOM   4050 O  OG   . SER   C 1 56  ? -13.699 10.749  0.059   1.00 25.41  ? 56  SER   C OG   1 
ATOM   4051 N  N    . VAL   C 1 57  ? -10.460 11.953  0.017   1.00 25.56  ? 57  VAL   C N    1 
ATOM   4052 C  CA   . VAL   C 1 57  ? -9.651  13.079  -0.544  1.00 28.01  ? 57  VAL   C CA   1 
ATOM   4053 C  C    . VAL   C 1 57  ? -8.202  12.605  -0.735  1.00 28.19  ? 57  VAL   C C    1 
ATOM   4054 O  O    . VAL   C 1 57  ? -7.672  12.828  -1.831  1.00 28.91  ? 57  VAL   C O    1 
ATOM   4055 C  CB   . VAL   C 1 57  ? -9.714  14.345  0.339   1.00 30.40  ? 57  VAL   C CB   1 
ATOM   4056 C  CG1  . VAL   C 1 57  ? -8.864  15.468  -0.241  1.00 31.12  ? 57  VAL   C CG1  1 
ATOM   4057 C  CG2  . VAL   C 1 57  ? -11.143 14.841  0.543   1.00 30.63  ? 57  VAL   C CG2  1 
ATOM   4058 N  N    . ASP   C 1 58  ? -7.629  11.926  0.265   1.00 29.77  ? 58  ASP   C N    1 
ATOM   4059 C  CA   . ASP   C 1 58  ? -6.231  11.409  0.288   1.00 32.43  ? 58  ASP   C CA   1 
ATOM   4060 C  C    . ASP   C 1 58  ? -6.128  9.961   -0.191  1.00 29.22  ? 58  ASP   C C    1 
ATOM   4061 O  O    . ASP   C 1 58  ? -4.995  9.505   -0.413  1.00 27.78  ? 58  ASP   C O    1 
ATOM   4062 C  CB   . ASP   C 1 58  ? -5.667  11.331  1.710   1.00 35.79  ? 58  ASP   C CB   1 
ATOM   4063 C  CG   . ASP   C 1 58  ? -5.202  12.654  2.247   1.00 40.75  ? 58  ASP   C CG   1 
ATOM   4064 O  OD1  . ASP   C 1 58  ? -4.915  13.553  1.396   1.00 43.98  ? 58  ASP   C OD1  1 
ATOM   4065 O  OD2  . ASP   C 1 58  ? -5.150  12.774  3.506   1.00 43.96  ? 58  ASP   C OD2  1 
ATOM   4066 N  N    . LYS   C 1 59  ? -7.226  9.214   -0.206  1.00 28.72  ? 59  LYS   C N    1 
ATOM   4067 C  CA   . LYS   C 1 59  ? -7.193  7.759   -0.505  1.00 27.59  ? 59  LYS   C CA   1 
ATOM   4068 C  C    . LYS   C 1 59  ? -6.374  7.071   0.590   1.00 27.35  ? 59  LYS   C C    1 
ATOM   4069 O  O    . LYS   C 1 59  ? -5.623  6.125   0.279   1.00 29.93  ? 59  LYS   C O    1 
ATOM   4070 C  CB   . LYS   C 1 59  ? -6.607  7.516   -1.899  1.00 28.93  ? 59  LYS   C CB   1 
ATOM   4071 C  CG   . LYS   C 1 59  ? -7.288  8.275   -3.037  1.00 32.72  ? 59  LYS   C CG   1 
ATOM   4072 C  CD   . LYS   C 1 59  ? -8.649  7.709   -3.399  1.00 36.65  ? 59  LYS   C CD   1 
ATOM   4073 C  CE   . LYS   C 1 59  ? -9.090  8.017   -4.815  1.00 39.27  ? 59  LYS   C CE   1 
ATOM   4074 N  NZ   . LYS   C 1 59  ? -10.081 9.114   -4.833  1.00 42.94  ? 59  LYS   C NZ   1 
ATOM   4075 N  N    . ARG   C 1 60  ? -6.542  7.518   1.833   1.00 26.70  ? 60  ARG   C N    1 
ATOM   4076 C  CA   . ARG   C 1 60  ? -5.739  7.092   3.013   1.00 26.31  ? 60  ARG   C CA   1 
ATOM   4077 C  C    . ARG   C 1 60  ? -6.648  6.423   4.047   1.00 23.90  ? 60  ARG   C C    1 
ATOM   4078 O  O    . ARG   C 1 60  ? -7.613  7.071   4.507   1.00 25.05  ? 60  ARG   C O    1 
ATOM   4079 C  CB   . ARG   C 1 60  ? -5.040  8.313   3.614   1.00 29.19  ? 60  ARG   C CB   1 
ATOM   4080 C  CG   . ARG   C 1 60  ? -3.854  7.978   4.502   1.00 34.81  ? 60  ARG   C CG   1 
ATOM   4081 C  CD   . ARG   C 1 60  ? -2.923  9.168   4.664   1.00 39.79  ? 60  ARG   C CD   1 
ATOM   4082 N  NE   . ARG   C 1 60  ? -2.056  9.286   3.509   1.00 43.00  ? 60  ARG   C NE   1 
ATOM   4083 C  CZ   . ARG   C 1 60  ? -1.416  10.384  3.137   1.00 51.35  ? 60  ARG   C CZ   1 
ATOM   4084 N  NH1  . ARG   C 1 60  ? -0.656  10.341  2.056   1.00 52.68  ? 60  ARG   C NH1  1 
ATOM   4085 N  NH2  . ARG   C 1 60  ? -1.519  11.510  3.833   1.00 56.41  ? 60  ARG   C NH2  1 
ATOM   4086 N  N    . LEU   C 1 61  ? -6.355  5.166   4.386   1.00 22.22  ? 61  LEU   C N    1 
ATOM   4087 C  CA   . LEU   C 1 61  ? -6.912  4.430   5.552   1.00 20.49  ? 61  LEU   C CA   1 
ATOM   4088 C  C    . LEU   C 1 61  ? -6.010  4.629   6.765   1.00 20.40  ? 61  LEU   C C    1 
ATOM   4089 O  O    . LEU   C 1 61  ? -4.823  4.294   6.669   1.00 20.82  ? 61  LEU   C O    1 
ATOM   4090 C  CB   . LEU   C 1 61  ? -7.001  2.941   5.224   1.00 19.73  ? 61  LEU   C CB   1 
ATOM   4091 C  CG   . LEU   C 1 61  ? -7.744  2.109   6.257   1.00 19.91  ? 61  LEU   C CG   1 
ATOM   4092 C  CD1  . LEU   C 1 61  ? -9.135  2.656   6.488   1.00 19.63  ? 61  LEU   C CD1  1 
ATOM   4093 C  CD2  . LEU   C 1 61  ? -7.823  0.657   5.804   1.00 21.42  ? 61  LEU   C CD2  1 
ATOM   4094 N  N    . SER   C 1 62  ? -6.584  5.099   7.867   1.00 20.84  ? 62  SER   C N    1 
ATOM   4095 C  CA   . SER   C 1 62  ? -5.882  5.448   9.129   1.00 20.94  ? 62  SER   C CA   1 
ATOM   4096 C  C    . SER   C 1 62  ? -6.560  4.744   10.279  1.00 18.24  ? 62  SER   C C    1 
ATOM   4097 O  O    . SER   C 1 62  ? -7.794  4.707   10.244  1.00 17.42  ? 62  SER   C O    1 
ATOM   4098 C  CB   . SER   C 1 62  ? -5.964  6.920   9.421   1.00 22.07  ? 62  SER   C CB   1 
ATOM   4099 O  OG   . SER   C 1 62  ? -5.056  7.611   8.628   1.00 28.52  ? 62  SER   C OG   1 
ATOM   4100 N  N    . ALA   C 1 63  ? -5.803  4.425   11.321  1.00 16.32  ? 63  ALA   C N    1 
ATOM   4101 C  CA   . ALA   C 1 63  ? -6.337  3.865   12.577  1.00 16.77  ? 63  ALA   C CA   1 
ATOM   4102 C  C    . ALA   C 1 63  ? -5.505  4.348   13.766  1.00 18.26  ? 63  ALA   C C    1 
ATOM   4103 O  O    . ALA   C 1 63  ? -4.244  4.417   13.659  1.00 19.53  ? 63  ALA   C O    1 
ATOM   4104 C  CB   . ALA   C 1 63  ? -6.348  2.368   12.486  1.00 16.43  ? 63  ALA   C CB   1 
ATOM   4105 N  N    . VAL   C 1 64  ? -6.163  4.654   14.874  1.00 17.93  ? 64  VAL   C N    1 
ATOM   4106 C  CA   . VAL   C 1 64  ? -5.468  4.974   16.151  1.00 18.67  ? 64  VAL   C CA   1 
ATOM   4107 C  C    . VAL   C 1 64  ? -6.090  4.116   17.246  1.00 17.38  ? 64  VAL   C C    1 
ATOM   4108 O  O    . VAL   C 1 64  ? -7.359  4.021   17.289  1.00 18.35  ? 64  VAL   C O    1 
ATOM   4109 C  CB   . VAL   C 1 64  ? -5.576  6.473   16.478  1.00 19.72  ? 64  VAL   C CB   1 
ATOM   4110 C  CG1  . VAL   C 1 64  ? -4.834  6.818   17.753  1.00 20.18  ? 64  VAL   C CG1  1 
ATOM   4111 C  CG2  . VAL   C 1 64  ? -5.041  7.304   15.334  1.00 21.48  ? 64  VAL   C CG2  1 
ATOM   4112 N  N    . VAL   C 1 65  ? -5.256  3.499   18.069  1.00 15.96  ? 65  VAL   C N    1 
ATOM   4113 C  CA   . VAL   C 1 65  ? -5.734  2.664   19.213  1.00 17.73  ? 65  VAL   C CA   1 
ATOM   4114 C  C    . VAL   C 1 65  ? -5.111  3.185   20.494  1.00 17.72  ? 65  VAL   C C    1 
ATOM   4115 O  O    . VAL   C 1 65  ? -3.908  3.393   20.546  1.00 17.24  ? 65  VAL   C O    1 
ATOM   4116 C  CB   . VAL   C 1 65  ? -5.474  1.167   19.005  1.00 17.36  ? 65  VAL   C CB   1 
ATOM   4117 C  CG1  . VAL   C 1 65  ? -6.047  0.334   20.141  1.00 17.46  ? 65  VAL   C CG1  1 
ATOM   4118 C  CG2  . VAL   C 1 65  ? -6.070  0.737   17.684  1.00 17.83  ? 65  VAL   C CG2  1 
ATOM   4119 N  N    . SER   C 1 66  ? -5.949  3.471   21.472  1.00 20.62  ? 66  SER   C N    1 
ATOM   4120 C  CA   . SER   C 1 66  ? -5.514  4.172   22.702  1.00 22.07  ? 66  SER   C CA   1 
ATOM   4121 C  C    . SER   C 1 66  ? -6.251  3.645   23.934  1.00 21.77  ? 66  SER   C C    1 
ATOM   4122 O  O    . SER   C 1 66  ? -7.314  2.999   23.803  1.00 20.78  ? 66  SER   C O    1 
ATOM   4123 C  CB   . SER   C 1 66  ? -5.632  5.665   22.535  1.00 23.60  ? 66  SER   C CB   1 
ATOM   4124 O  OG   . SER   C 1 66  ? -6.967  6.066   22.380  1.00 24.29  ? 66  SER   C OG   1 
ATOM   4125 N  N    . TYR   C 1 67  ? -5.620  3.875   25.077  1.00 22.34  ? 67  TYR   C N    1 
ATOM   4126 C  CA   . TYR   C 1 67  ? -6.112  3.660   26.456  1.00 23.14  ? 67  TYR   C CA   1 
ATOM   4127 C  C    . TYR   C 1 67  ? -6.020  5.009   27.169  1.00 24.82  ? 67  TYR   C C    1 
ATOM   4128 O  O    . TYR   C 1 67  ? -5.133  5.807   26.881  1.00 23.80  ? 67  TYR   C O    1 
ATOM   4129 C  CB   . TYR   C 1 67  ? -5.239  2.592   27.121  1.00 22.96  ? 67  TYR   C CB   1 
ATOM   4130 C  CG   . TYR   C 1 67  ? -5.399  1.186   26.598  1.00 22.15  ? 67  TYR   C CG   1 
ATOM   4131 C  CD1  . TYR   C 1 67  ? -6.454  0.401   27.022  1.00 22.54  ? 67  TYR   C CD1  1 
ATOM   4132 C  CD2  . TYR   C 1 67  ? -4.486  0.611   25.724  1.00 22.27  ? 67  TYR   C CD2  1 
ATOM   4133 C  CE1  . TYR   C 1 67  ? -6.625  -0.902  26.585  1.00 22.23  ? 67  TYR   C CE1  1 
ATOM   4134 C  CE2  . TYR   C 1 67  ? -4.659  -0.689  25.251  1.00 23.26  ? 67  TYR   C CE2  1 
ATOM   4135 C  CZ   . TYR   C 1 67  ? -5.727  -1.458  25.695  1.00 22.92  ? 67  TYR   C CZ   1 
ATOM   4136 O  OH   . TYR   C 1 67  ? -5.928  -2.761  25.302  1.00 24.12  ? 67  TYR   C OH   1 
ATOM   4137 N  N    . PRO   C 1 68  ? -6.882  5.323   28.155  1.00 29.18  ? 68  PRO   C N    1 
ATOM   4138 C  CA   . PRO   C 1 68  ? -6.705  6.553   28.929  1.00 32.69  ? 68  PRO   C CA   1 
ATOM   4139 C  C    . PRO   C 1 68  ? -5.287  6.553   29.529  1.00 36.46  ? 68  PRO   C C    1 
ATOM   4140 O  O    . PRO   C 1 68  ? -4.812  5.471   29.855  1.00 36.15  ? 68  PRO   C O    1 
ATOM   4141 C  CB   . PRO   C 1 68  ? -7.797  6.451   30.012  1.00 30.61  ? 68  PRO   C CB   1 
ATOM   4142 C  CG   . PRO   C 1 68  ? -8.819  5.505   29.407  1.00 31.16  ? 68  PRO   C CG   1 
ATOM   4143 C  CD   . PRO   C 1 68  ? -7.991  4.495   28.641  1.00 29.45  ? 68  PRO   C CD   1 
ATOM   4144 N  N    . ASN   C 1 69  ? -4.630  7.719   29.622  1.00 40.85  ? 69  ASN   C N    1 
ATOM   4145 C  CA   . ASN   C 1 69  ? -3.267  7.869   30.223  1.00 48.62  ? 69  ASN   C CA   1 
ATOM   4146 C  C    . ASN   C 1 69  ? -2.255  6.860   29.622  1.00 46.58  ? 69  ASN   C C    1 
ATOM   4147 O  O    . ASN   C 1 69  ? -1.546  6.167   30.410  1.00 46.69  ? 69  ASN   C O    1 
ATOM   4148 C  CB   . ASN   C 1 69  ? -3.278  7.689   31.756  1.00 57.33  ? 69  ASN   C CB   1 
ATOM   4149 C  CG   . ASN   C 1 69  ? -4.233  8.591   32.522  1.00 59.51  ? 69  ASN   C CG   1 
ATOM   4150 O  OD1  . ASN   C 1 69  ? -4.916  9.442   31.947  1.00 63.18  ? 69  ASN   C OD1  1 
ATOM   4151 N  ND2  . ASN   C 1 69  ? -4.289  8.406   33.833  1.00 55.98  ? 69  ASN   C ND2  1 
ATOM   4152 N  N    . ALA   C 1 70  ? -2.165  6.754   28.291  1.00 38.61  ? 70  ALA   C N    1 
ATOM   4153 C  CA   . ALA   C 1 70  ? -1.051  6.079   27.583  1.00 35.33  ? 70  ALA   C CA   1 
ATOM   4154 C  C    . ALA   C 1 70  ? -0.969  6.632   26.162  1.00 33.47  ? 70  ALA   C C    1 
ATOM   4155 O  O    . ALA   C 1 70  ? -1.976  7.165   25.685  1.00 35.71  ? 70  ALA   C O    1 
ATOM   4156 C  CB   . ALA   C 1 70  ? -1.219  4.582   27.584  1.00 33.89  ? 70  ALA   C CB   1 
ATOM   4157 N  N    . ASP   C 1 71  ? 0.191   6.522   25.524  1.00 34.17  ? 71  ASP   C N    1 
ATOM   4158 C  CA   . ASP   C 1 71  ? 0.376   6.961   24.113  1.00 37.37  ? 71  ASP   C CA   1 
ATOM   4159 C  C    . ASP   C 1 71  ? -0.406  6.008   23.206  1.00 31.40  ? 71  ASP   C C    1 
ATOM   4160 O  O    . ASP   C 1 71  ? -0.619  4.844   23.581  1.00 29.79  ? 71  ASP   C O    1 
ATOM   4161 C  CB   . ASP   C 1 71  ? 1.836   6.983   23.648  1.00 43.16  ? 71  ASP   C CB   1 
ATOM   4162 C  CG   . ASP   C 1 71  ? 2.838   7.099   24.769  1.00 48.53  ? 71  ASP   C CG   1 
ATOM   4163 O  OD1  . ASP   C 1 71  ? 2.720   8.070   25.574  1.00 52.02  ? 71  ASP   C OD1  1 
ATOM   4164 O  OD2  . ASP   C 1 71  ? 3.695   6.196   24.848  1.00 50.68  ? 71  ASP   C OD2  1 
ATOM   4165 N  N    . SER   C 1 72  ? -0.838  6.506   22.057  1.00 26.45  ? 72  SER   C N    1 
ATOM   4166 C  CA   . SER   C 1 72  ? -1.629  5.721   21.082  1.00 23.56  ? 72  SER   C CA   1 
ATOM   4167 C  C    . SER   C 1 72  ? -0.649  4.931   20.212  1.00 21.17  ? 72  SER   C C    1 
ATOM   4168 O  O    . SER   C 1 72  ? 0.565   5.201   20.262  1.00 19.56  ? 72  SER   C O    1 
ATOM   4169 C  CB   . SER   C 1 72  ? -2.519  6.611   20.272  1.00 22.67  ? 72  SER   C CB   1 
ATOM   4170 O  OG   . SER   C 1 72  ? -3.270  7.465   21.122  1.00 22.99  ? 72  SER   C OG   1 
ATOM   4171 N  N    . ALA   C 1 73  ? -1.162  3.941   19.507  1.00 19.25  ? 73  ALA   C N    1 
ATOM   4172 C  CA   . ALA   C 1 73  ? -0.489  3.304   18.363  1.00 19.47  ? 73  ALA   C CA   1 
ATOM   4173 C  C    . ALA   C 1 73  ? -1.307  3.679   17.125  1.00 18.91  ? 73  ALA   C C    1 
ATOM   4174 O  O    . ALA   C 1 73  ? -2.573  3.685   17.193  1.00 16.26  ? 73  ALA   C O    1 
ATOM   4175 C  CB   . ALA   C 1 73  ? -0.414  1.812   18.595  1.00 19.93  ? 73  ALA   C CB   1 
ATOM   4176 N  N    . THR   C 1 74  ? -0.616  4.034   16.053  1.00 17.73  ? 74  THR   C N    1 
ATOM   4177 C  CA   . THR   C 1 74  ? -1.266  4.494   14.810  1.00 18.48  ? 74  THR   C CA   1 
ATOM   4178 C  C    . THR   C 1 74  ? -0.574  3.892   13.596  1.00 17.44  ? 74  THR   C C    1 
ATOM   4179 O  O    . THR   C 1 74  ? 0.627   3.609   13.639  1.00 17.37  ? 74  THR   C O    1 
ATOM   4180 C  CB   . THR   C 1 74  ? -1.292  6.025   14.706  1.00 19.40  ? 74  THR   C CB   1 
ATOM   4181 O  OG1  . THR   C 1 74  ? -2.204  6.336   13.645  1.00 18.75  ? 74  THR   C OG1  1 
ATOM   4182 C  CG2  . THR   C 1 74  ? 0.080   6.626   14.451  1.00 18.76  ? 74  THR   C CG2  1 
ATOM   4183 N  N    . VAL   C 1 75  ? -1.330  3.814   12.518  1.00 18.36  ? 75  VAL   C N    1 
ATOM   4184 C  CA   . VAL   C 1 75  ? -0.949  3.110   11.270  1.00 19.49  ? 75  VAL   C CA   1 
ATOM   4185 C  C    . VAL   C 1 75  ? -1.831  3.682   10.157  1.00 20.24  ? 75  VAL   C C    1 
ATOM   4186 O  O    . VAL   C 1 75  ? -3.032  3.946   10.402  1.00 19.93  ? 75  VAL   C O    1 
ATOM   4187 C  CB   . VAL   C 1 75  ? -1.096  1.594   11.494  1.00 20.21  ? 75  VAL   C CB   1 
ATOM   4188 C  CG1  . VAL   C 1 75  ? -2.541  1.137   11.367  1.00 20.78  ? 75  VAL   C CG1  1 
ATOM   4189 C  CG2  . VAL   C 1 75  ? -0.166  0.797   10.606  1.00 21.30  ? 75  VAL   C CG2  1 
ATOM   4190 N  N    . SER   C 1 76  ? -1.233  3.907   8.997   1.00 22.33  ? 76  SER   C N    1 
ATOM   4191 C  CA   . SER   C 1 76  ? -1.826  4.611   7.836   1.00 23.03  ? 76  SER   C CA   1 
ATOM   4192 C  C    . SER   C 1 76  ? -1.324  3.939   6.557   1.00 23.22  ? 76  SER   C C    1 
ATOM   4193 O  O    . SER   C 1 76  ? -0.179  3.436   6.575   1.00 23.88  ? 76  SER   C O    1 
ATOM   4194 C  CB   . SER   C 1 76  ? -1.459  6.067   7.903   1.00 25.26  ? 76  SER   C CB   1 
ATOM   4195 O  OG   . SER   C 1 76  ? -2.152  6.822   6.938   1.00 30.19  ? 76  SER   C OG   1 
ATOM   4196 N  N    . TYR   C 1 77  ? -2.148  3.902   5.503   1.00 23.56  ? 77  TYR   C N    1 
ATOM   4197 C  CA   . TYR   C 1 77  ? -1.828  3.264   4.201   1.00 23.50  ? 77  TYR   C CA   1 
ATOM   4198 C  C    . TYR   C 1 77  ? -2.714  3.853   3.102   1.00 22.82  ? 77  TYR   C C    1 
ATOM   4199 O  O    . TYR   C 1 77  ? -3.940  3.853   3.259   1.00 20.80  ? 77  TYR   C O    1 
ATOM   4200 C  CB   . TYR   C 1 77  ? -1.985  1.737   4.274   1.00 23.77  ? 77  TYR   C CB   1 
ATOM   4201 C  CG   . TYR   C 1 77  ? -1.257  1.004   3.164   1.00 25.31  ? 77  TYR   C CG   1 
ATOM   4202 C  CD1  . TYR   C 1 77  ? 0.130   0.926   3.146   1.00 25.66  ? 77  TYR   C CD1  1 
ATOM   4203 C  CD2  . TYR   C 1 77  ? -1.945  0.414   2.115   1.00 25.45  ? 77  TYR   C CD2  1 
ATOM   4204 C  CE1  . TYR   C 1 77  ? 0.813   0.282   2.131   1.00 26.32  ? 77  TYR   C CE1  1 
ATOM   4205 C  CE2  . TYR   C 1 77  ? -1.277  -0.231  1.086   1.00 25.73  ? 77  TYR   C CE2  1 
ATOM   4206 C  CZ   . TYR   C 1 77  ? 0.101   -0.309  1.104   1.00 28.04  ? 77  TYR   C CZ   1 
ATOM   4207 O  OH   . TYR   C 1 77  ? 0.761   -0.958  0.101   1.00 36.06  ? 77  TYR   C OH   1 
ATOM   4208 N  N    . ASP   C 1 78  ? -2.103  4.310   2.014   1.00 23.90  ? 78  ASP   C N    1 
ATOM   4209 C  CA   . ASP   C 1 78  ? -2.819  4.836   0.819   1.00 25.79  ? 78  ASP   C CA   1 
ATOM   4210 C  C    . ASP   C 1 78  ? -3.376  3.631   0.070   1.00 24.53  ? 78  ASP   C C    1 
ATOM   4211 O  O    . ASP   C 1 78  ? -2.622  2.695   -0.128  1.00 26.38  ? 78  ASP   C O    1 
ATOM   4212 C  CB   . ASP   C 1 78  ? -1.918  5.708   -0.060  1.00 27.47  ? 78  ASP   C CB   1 
ATOM   4213 C  CG   . ASP   C 1 78  ? -1.376  6.936   0.656   1.00 31.35  ? 78  ASP   C CG   1 
ATOM   4214 O  OD1  . ASP   C 1 78  ? -1.834  7.202   1.791   1.00 32.00  ? 78  ASP   C OD1  1 
ATOM   4215 O  OD2  . ASP   C 1 78  ? -0.470  7.605   0.091   1.00 36.37  ? 78  ASP   C OD2  1 
ATOM   4216 N  N    . VAL   C 1 79  ? -4.675  3.621   -0.213  1.00 25.14  ? 79  VAL   C N    1 
ATOM   4217 C  CA   . VAL   C 1 79  ? -5.351  2.553   -1.007  1.00 27.00  ? 79  VAL   C CA   1 
ATOM   4218 C  C    . VAL   C 1 79  ? -6.606  3.173   -1.637  1.00 29.06  ? 79  VAL   C C    1 
ATOM   4219 O  O    . VAL   C 1 79  ? -7.338  3.895   -0.921  1.00 25.16  ? 79  VAL   C O    1 
ATOM   4220 C  CB   . VAL   C 1 79  ? -5.680  1.308   -0.152  1.00 27.02  ? 79  VAL   C CB   1 
ATOM   4221 C  CG1  . VAL   C 1 79  ? -6.373  1.648   1.158   1.00 27.76  ? 79  VAL   C CG1  1 
ATOM   4222 C  CG2  . VAL   C 1 79  ? -6.527  0.305   -0.913  1.00 26.99  ? 79  VAL   C CG2  1 
ATOM   4223 N  N    . ASP   C 1 80  ? -6.804  2.948   -2.940  1.00 32.71  ? 80  ASP   C N    1 
ATOM   4224 C  CA   . ASP   C 1 80  ? -8.064  3.272   -3.666  1.00 34.53  ? 80  ASP   C CA   1 
ATOM   4225 C  C    . ASP   C 1 80  ? -9.051  2.120   -3.455  1.00 30.39  ? 80  ASP   C C    1 
ATOM   4226 O  O    . ASP   C 1 80  ? -8.799  1.050   -4.029  1.00 27.20  ? 80  ASP   C O    1 
ATOM   4227 C  CB   . ASP   C 1 80  ? -7.833  3.451   -5.169  1.00 37.18  ? 80  ASP   C CB   1 
ATOM   4228 C  CG   . ASP   C 1 80  ? -6.956  4.627   -5.564  1.00 42.92  ? 80  ASP   C CG   1 
ATOM   4229 O  OD1  . ASP   C 1 80  ? -6.335  5.235   -4.651  1.00 44.75  ? 80  ASP   C OD1  1 
ATOM   4230 O  OD2  . ASP   C 1 80  ? -6.900  4.923   -6.797  1.00 42.82  ? 80  ASP   C OD2  1 
ATOM   4231 N  N    . LEU   C 1 81  ? -10.131 2.334   -2.696  1.00 28.77  ? 81  LEU   C N    1 
ATOM   4232 C  CA   . LEU   C 1 81  ? -11.101 1.265   -2.332  1.00 28.43  ? 81  LEU   C CA   1 
ATOM   4233 C  C    . LEU   C 1 81  ? -11.738 0.660   -3.588  1.00 26.97  ? 81  LEU   C C    1 
ATOM   4234 O  O    . LEU   C 1 81  ? -12.017 -0.559  -3.576  1.00 26.41  ? 81  LEU   C O    1 
ATOM   4235 C  CB   . LEU   C 1 81  ? -12.165 1.824   -1.383  1.00 30.67  ? 81  LEU   C CB   1 
ATOM   4236 C  CG   . LEU   C 1 81  ? -11.667 2.225   0.007   1.00 32.55  ? 81  LEU   C CG   1 
ATOM   4237 C  CD1  . LEU   C 1 81  ? -12.815 2.301   0.994   1.00 34.58  ? 81  LEU   C CD1  1 
ATOM   4238 C  CD2  . LEU   C 1 81  ? -10.614 1.276   0.540   1.00 32.00  ? 81  LEU   C CD2  1 
ATOM   4239 N  N    . ASP   C 1 82  ? -11.910 1.432   -4.662  1.00 26.72  ? 82  ASP   C N    1 
ATOM   4240 C  CA   . ASP   C 1 82  ? -12.507 0.922   -5.933  1.00 28.80  ? 82  ASP   C CA   1 
ATOM   4241 C  C    . ASP   C 1 82  ? -11.594 -0.111  -6.631  1.00 28.63  ? 82  ASP   C C    1 
ATOM   4242 O  O    . ASP   C 1 82  ? -12.075 -0.762  -7.563  1.00 29.24  ? 82  ASP   C O    1 
ATOM   4243 C  CB   . ASP   C 1 82  ? -12.868 2.069   -6.872  1.00 30.54  ? 82  ASP   C CB   1 
ATOM   4244 C  CG   . ASP   C 1 82  ? -11.740 3.062   -7.083  1.00 31.61  ? 82  ASP   C CG   1 
ATOM   4245 O  OD1  . ASP   C 1 82  ? -11.279 3.674   -6.088  1.00 36.23  ? 82  ASP   C OD1  1 
ATOM   4246 O  OD2  . ASP   C 1 82  ? -11.315 3.190   -8.226  1.00 34.53  ? 82  ASP   C OD2  1 
ATOM   4247 N  N    . ASN   C 1 83  ? -10.343 -0.284  -6.195  1.00 28.62  ? 83  ASN   C N    1 
ATOM   4248 C  CA   . ASN   C 1 83  ? -9.378  -1.288  -6.730  1.00 29.47  ? 83  ASN   C CA   1 
ATOM   4249 C  C    . ASN   C 1 83  ? -9.420  -2.593  -5.919  1.00 29.09  ? 83  ASN   C C    1 
ATOM   4250 O  O    . ASN   C 1 83  ? -8.841  -3.564  -6.388  1.00 28.12  ? 83  ASN   C O    1 
ATOM   4251 C  CB   . ASN   C 1 83  ? -7.938  -0.767  -6.728  1.00 28.31  ? 83  ASN   C CB   1 
ATOM   4252 C  CG   . ASN   C 1 83  ? -7.686  0.279   -7.790  1.00 31.19  ? 83  ASN   C CG   1 
ATOM   4253 O  OD1  . ASN   C 1 83  ? -8.375  0.296   -8.811  1.00 33.56  ? 83  ASN   C OD1  1 
ATOM   4254 N  ND2  . ASN   C 1 83  ? -6.691  1.134   -7.569  1.00 33.14  ? 83  ASN   C ND2  1 
ATOM   4255 N  N    . VAL   C 1 84  ? -10.084 -2.614  -4.760  1.00 29.25  ? 84  VAL   C N    1 
ATOM   4256 C  CA   . VAL   C 1 84  ? -10.023 -3.738  -3.781  1.00 29.80  ? 84  VAL   C CA   1 
ATOM   4257 C  C    . VAL   C 1 84  ? -11.424 -4.344  -3.578  1.00 28.85  ? 84  VAL   C C    1 
ATOM   4258 O  O    . VAL   C 1 84  ? -11.569 -5.572  -3.737  1.00 30.30  ? 84  VAL   C O    1 
ATOM   4259 C  CB   . VAL   C 1 84  ? -9.411  -3.215  -2.468  1.00 33.08  ? 84  VAL   C CB   1 
ATOM   4260 C  CG1  . VAL   C 1 84  ? -9.383  -4.280  -1.388  1.00 37.22  ? 84  VAL   C CG1  1 
ATOM   4261 C  CG2  . VAL   C 1 84  ? -8.015  -2.649  -2.685  1.00 32.62  ? 84  VAL   C CG2  1 
ATOM   4262 N  N    . LEU   C 1 85  ? -12.428 -3.512  -3.271  1.00 28.92  ? 85  LEU   C N    1 
ATOM   4263 C  CA   . LEU   C 1 85  ? -13.773 -3.925  -2.772  1.00 26.25  ? 85  LEU   C CA   1 
ATOM   4264 C  C    . LEU   C 1 85  ? -14.817 -3.728  -3.864  1.00 23.13  ? 85  LEU   C C    1 
ATOM   4265 O  O    . LEU   C 1 85  ? -14.634 -2.901  -4.744  1.00 21.61  ? 85  LEU   C O    1 
ATOM   4266 C  CB   . LEU   C 1 85  ? -14.151 -3.072  -1.556  1.00 26.87  ? 85  LEU   C CB   1 
ATOM   4267 C  CG   . LEU   C 1 85  ? -13.360 -3.289  -0.267  1.00 26.34  ? 85  LEU   C CG   1 
ATOM   4268 C  CD1  . LEU   C 1 85  ? -13.676 -2.185  0.740   1.00 26.75  ? 85  LEU   C CD1  1 
ATOM   4269 C  CD2  . LEU   C 1 85  ? -13.656 -4.649  0.337   1.00 26.85  ? 85  LEU   C CD2  1 
ATOM   4270 N  N    . PRO   C 1 86  ? -15.969 -4.430  -3.792  1.00 21.39  ? 86  PRO   C N    1 
ATOM   4271 C  CA   . PRO   C 1 86  ? -17.126 -4.112  -4.632  1.00 21.83  ? 86  PRO   C CA   1 
ATOM   4272 C  C    . PRO   C 1 86  ? -17.774 -2.777  -4.210  1.00 21.24  ? 86  PRO   C C    1 
ATOM   4273 O  O    . PRO   C 1 86  ? -17.453 -2.262  -3.146  1.00 18.26  ? 86  PRO   C O    1 
ATOM   4274 C  CB   . PRO   C 1 86  ? -18.071 -5.308  -4.427  1.00 20.78  ? 86  PRO   C CB   1 
ATOM   4275 C  CG   . PRO   C 1 86  ? -17.706 -5.870  -3.070  1.00 20.61  ? 86  PRO   C CG   1 
ATOM   4276 C  CD   . PRO   C 1 86  ? -16.244 -5.534  -2.866  1.00 21.83  ? 86  PRO   C CD   1 
ATOM   4277 N  N    . GLU   C 1 87  ? -18.633 -2.247  -5.083  1.00 23.63  ? 87  GLU   C N    1 
ATOM   4278 C  CA   . GLU   C 1 87  ? -19.404 -0.979  -4.926  1.00 24.42  ? 87  GLU   C CA   1 
ATOM   4279 C  C    . GLU   C 1 87  ? -20.160 -0.972  -3.596  1.00 21.52  ? 87  GLU   C C    1 
ATOM   4280 O  O    . GLU   C 1 87  ? -20.227 0.098   -2.974  1.00 19.67  ? 87  GLU   C O    1 
ATOM   4281 C  CB   . GLU   C 1 87  ? -20.434 -0.835  -6.046  1.00 28.55  ? 87  GLU   C CB   1 
ATOM   4282 C  CG   . GLU   C 1 87  ? -19.915 -0.109  -7.273  1.00 34.48  ? 87  GLU   C CG   1 
ATOM   4283 C  CD   . GLU   C 1 87  ? -21.008 0.234   -8.285  1.00 38.59  ? 87  GLU   C CD   1 
ATOM   4284 O  OE1  . GLU   C 1 87  ? -20.875 -0.174  -9.473  1.00 40.45  ? 87  GLU   C OE1  1 
ATOM   4285 O  OE2  . GLU   C 1 87  ? -21.987 0.921   -7.886  1.00 37.52  ? 87  GLU   C OE2  1 
ATOM   4286 N  N    . TRP   C 1 88  ? -20.735 -2.118  -3.212  1.00 18.37  ? 88  TRP   C N    1 
ATOM   4287 C  CA   . TRP   C 1 88  ? -21.546 -2.302  -1.990  1.00 17.29  ? 88  TRP   C CA   1 
ATOM   4288 C  C    . TRP   C 1 88  ? -20.827 -3.295  -1.086  1.00 16.56  ? 88  TRP   C C    1 
ATOM   4289 O  O    . TRP   C 1 88  ? -20.314 -4.278  -1.621  1.00 16.25  ? 88  TRP   C O    1 
ATOM   4290 C  CB   . TRP   C 1 88  ? -22.956 -2.797  -2.329  1.00 17.34  ? 88  TRP   C CB   1 
ATOM   4291 C  CG   . TRP   C 1 88  ? -23.799 -1.745  -2.954  1.00 18.47  ? 88  TRP   C CG   1 
ATOM   4292 C  CD1  . TRP   C 1 88  ? -23.950 -1.504  -4.284  1.00 19.13  ? 88  TRP   C CD1  1 
ATOM   4293 C  CD2  . TRP   C 1 88  ? -24.617 -0.776  -2.267  1.00 18.04  ? 88  TRP   C CD2  1 
ATOM   4294 N  NE1  . TRP   C 1 88  ? -24.807 -0.448  -4.471  1.00 19.00  ? 88  TRP   C NE1  1 
ATOM   4295 C  CE2  . TRP   C 1 88  ? -25.235 0.013   -3.252  1.00 18.41  ? 88  TRP   C CE2  1 
ATOM   4296 C  CE3  . TRP   C 1 88  ? -24.909 -0.519  -0.926  1.00 18.71  ? 88  TRP   C CE3  1 
ATOM   4297 C  CZ2  . TRP   C 1 88  ? -26.095 1.067   -2.933  1.00 18.93  ? 88  TRP   C CZ2  1 
ATOM   4298 C  CZ3  . TRP   C 1 88  ? -25.754 0.528   -0.609  1.00 20.22  ? 88  TRP   C CZ3  1 
ATOM   4299 C  CH2  . TRP   C 1 88  ? -26.347 1.312   -1.602  1.00 19.51  ? 88  TRP   C CH2  1 
ATOM   4300 N  N    . VAL   C 1 89  ? -20.888 -3.061  0.228   1.00 15.42  ? 89  VAL   C N    1 
ATOM   4301 C  CA   . VAL   C 1 89  ? -20.151 -3.823  1.267   1.00 15.68  ? 89  VAL   C CA   1 
ATOM   4302 C  C    . VAL   C 1 89  ? -21.004 -3.914  2.526   1.00 15.57  ? 89  VAL   C C    1 
ATOM   4303 O  O    . VAL   C 1 89  ? -21.953 -3.133  2.684   1.00 15.42  ? 89  VAL   C O    1 
ATOM   4304 C  CB   . VAL   C 1 89  ? -18.793 -3.170  1.589   1.00 15.69  ? 89  VAL   C CB   1 
ATOM   4305 C  CG1  . VAL   C 1 89  ? -17.853 -3.230  0.404   1.00 16.07  ? 89  VAL   C CG1  1 
ATOM   4306 C  CG2  . VAL   C 1 89  ? -18.962 -1.742  2.041   1.00 15.86  ? 89  VAL   C CG2  1 
ATOM   4307 N  N    . ARG   C 1 90  ? -20.641 -4.837  3.398   1.00 15.54  ? 90  ARG   C N    1 
ATOM   4308 C  CA   . ARG   C 1 90  ? -21.054 -4.803  4.814   1.00 16.54  ? 90  ARG   C CA   1 
ATOM   4309 C  C    . ARG   C 1 90  ? -19.824 -4.465  5.661   1.00 16.35  ? 90  ARG   C C    1 
ATOM   4310 O  O    . ARG   C 1 90  ? -18.693 -4.811  5.273   1.00 14.40  ? 90  ARG   C O    1 
ATOM   4311 C  CB   . ARG   C 1 90  ? -21.721 -6.119  5.212   1.00 17.94  ? 90  ARG   C CB   1 
ATOM   4312 C  CG   . ARG   C 1 90  ? -23.165 -6.214  4.737   1.00 20.48  ? 90  ARG   C CG   1 
ATOM   4313 C  CD   . ARG   C 1 90  ? -24.005 -7.045  5.681   1.00 22.36  ? 90  ARG   C CD   1 
ATOM   4314 N  NE   . ARG   C 1 90  ? -25.430 -6.849  5.468   1.00 24.10  ? 90  ARG   C NE   1 
ATOM   4315 C  CZ   . ARG   C 1 90  ? -26.197 -7.614  4.699   1.00 25.51  ? 90  ARG   C CZ   1 
ATOM   4316 N  NH1  . ARG   C 1 90  ? -25.696 -8.638  4.030   1.00 26.53  ? 90  ARG   C NH1  1 
ATOM   4317 N  NH2  . ARG   C 1 90  ? -27.479 -7.348  4.602   1.00 26.69  ? 90  ARG   C NH2  1 
ATOM   4318 N  N    . VAL   C 1 91  ? -20.061 -3.751  6.749   1.00 16.15  ? 91  VAL   C N    1 
ATOM   4319 C  CA   . VAL   C 1 91  ? -19.024 -3.411  7.752   1.00 17.23  ? 91  VAL   C CA   1 
ATOM   4320 C  C    . VAL   C 1 91  ? -19.332 -4.253  8.988   1.00 16.65  ? 91  VAL   C C    1 
ATOM   4321 O  O    . VAL   C 1 91  ? -20.522 -4.477  9.262   1.00 16.78  ? 91  VAL   C O    1 
ATOM   4322 C  CB   . VAL   C 1 91  ? -19.011 -1.906  8.065   1.00 17.21  ? 91  VAL   C CB   1 
ATOM   4323 C  CG1  . VAL   C 1 91  ? -18.837 -1.092  6.800   1.00 17.97  ? 91  VAL   C CG1  1 
ATOM   4324 C  CG2  . VAL   C 1 91  ? -20.261 -1.477  8.822   1.00 17.36  ? 91  VAL   C CG2  1 
ATOM   4325 N  N    . GLY   C 1 92  ? -18.299 -4.633  9.725   1.00 15.26  ? 92  GLY   C N    1 
ATOM   4326 C  CA   . GLY   C 1 92  ? -18.463 -5.411  10.955  1.00 15.37  ? 92  GLY   C CA   1 
ATOM   4327 C  C    . GLY   C 1 92  ? -17.208 -5.486  11.803  1.00 15.64  ? 92  GLY   C C    1 
ATOM   4328 O  O    . GLY   C 1 92  ? -16.136 -4.907  11.425  1.00 15.43  ? 92  GLY   C O    1 
ATOM   4329 N  N    . LEU   C 1 93  ? -17.348 -6.192  12.926  1.00 16.04  ? 93  LEU   C N    1 
ATOM   4330 C  CA   . LEU   C 1 93  ? -16.269 -6.498  13.892  1.00 16.52  ? 93  LEU   C CA   1 
ATOM   4331 C  C    . LEU   C 1 93  ? -16.085 -8.015  13.871  1.00 17.06  ? 93  LEU   C C    1 
ATOM   4332 O  O    . LEU   C 1 93  ? -17.084 -8.746  13.698  1.00 16.35  ? 93  LEU   C O    1 
ATOM   4333 C  CB   . LEU   C 1 93  ? -16.650 -5.947  15.276  1.00 16.20  ? 93  LEU   C CB   1 
ATOM   4334 C  CG   . LEU   C 1 93  ? -16.871 -4.426  15.337  1.00 16.47  ? 93  LEU   C CG   1 
ATOM   4335 C  CD1  . LEU   C 1 93  ? -17.441 -3.990  16.667  1.00 16.74  ? 93  LEU   C CD1  1 
ATOM   4336 C  CD2  . LEU   C 1 93  ? -15.590 -3.661  15.095  1.00 15.95  ? 93  LEU   C CD2  1 
ATOM   4337 N  N    . SER   C 1 94  ? -14.834 -8.453  13.923  1.00 17.42  ? 94  SER   C N    1 
ATOM   4338 C  CA   . SER   C 1 94  ? -14.415 -9.875  13.978  1.00 18.81  ? 94  SER   C CA   1 
ATOM   4339 C  C    . SER   C 1 94  ? -13.486 -10.055 15.185  1.00 18.90  ? 94  SER   C C    1 
ATOM   4340 O  O    . SER   C 1 94  ? -12.771 -9.093  15.540  1.00 17.44  ? 94  SER   C O    1 
ATOM   4341 C  CB   . SER   C 1 94  ? -13.736 -10.281 12.698  1.00 19.69  ? 94  SER   C CB   1 
ATOM   4342 O  OG   . SER   C 1 94  ? -13.671 -11.698 12.573  1.00 22.33  ? 94  SER   C OG   1 
ATOM   4343 N  N    . ALA   C 1 95  ? -13.483 -11.238 15.786  1.00 18.09  ? 95  ALA   C N    1 
ATOM   4344 C  CA   . ALA   C 1 95  ? -12.475 -11.629 16.790  1.00 18.61  ? 95  ALA   C CA   1 
ATOM   4345 C  C    . ALA   C 1 95  ? -12.303 -13.137 16.747  1.00 19.92  ? 95  ALA   C C    1 
ATOM   4346 O  O    . ALA   C 1 95  ? -13.178 -13.841 16.204  1.00 19.77  ? 95  ALA   C O    1 
ATOM   4347 C  CB   . ALA   C 1 95  ? -12.865 -11.167 18.161  1.00 18.35  ? 95  ALA   C CB   1 
ATOM   4348 N  N    . SER   C 1 96  ? -11.172 -13.608 17.244  1.00 20.07  ? 96  SER   C N    1 
ATOM   4349 C  CA   . SER   C 1 96  ? -10.881 -15.052 17.286  1.00 21.30  ? 96  SER   C CA   1 
ATOM   4350 C  C    . SER   C 1 96  ? -9.881  -15.344 18.405  1.00 22.89  ? 96  SER   C C    1 
ATOM   4351 O  O    . SER   C 1 96  ? -9.096  -14.439 18.751  1.00 21.07  ? 96  SER   C O    1 
ATOM   4352 C  CB   . SER   C 1 96  ? -10.393 -15.552 15.957  1.00 22.61  ? 96  SER   C CB   1 
ATOM   4353 O  OG   . SER   C 1 96  ? -9.060  -15.126 15.742  1.00 24.29  ? 96  SER   C OG   1 
ATOM   4354 N  N    . THR   C 1 97  ? -9.983  -16.564 18.960  1.00 23.26  ? 97  THR   C N    1 
ATOM   4355 C  CA   . THR   C 1 97  ? -9.015  -17.223 19.867  1.00 21.34  ? 97  THR   C CA   1 
ATOM   4356 C  C    . THR   C 1 97  ? -8.520  -18.503 19.185  1.00 21.70  ? 97  THR   C C    1 
ATOM   4357 O  O    . THR   C 1 97  ? -9.149  -18.947 18.199  1.00 19.16  ? 97  THR   C O    1 
ATOM   4358 C  CB   . THR   C 1 97  ? -9.657  -17.466 21.237  1.00 20.51  ? 97  THR   C CB   1 
ATOM   4359 O  OG1  . THR   C 1 97  ? -10.667 -18.477 21.131  1.00 18.69  ? 97  THR   C OG1  1 
ATOM   4360 C  CG2  . THR   C 1 97  ? -10.235 -16.202 21.832  1.00 19.11  ? 97  THR   C CG2  1 
ATOM   4361 N  N    . GLY   C 1 98  ? -7.422  -19.067 19.687  1.00 22.77  ? 98  GLY   C N    1 
ATOM   4362 C  CA   . GLY   C 1 98  ? -6.729  -20.215 19.056  1.00 23.94  ? 98  GLY   C CA   1 
ATOM   4363 C  C    . GLY   C 1 98  ? -6.364  -21.254 20.098  1.00 23.45  ? 98  GLY   C C    1 
ATOM   4364 O  O    . GLY   C 1 98  ? -7.242  -21.598 20.879  1.00 21.70  ? 98  GLY   C O    1 
ATOM   4365 N  N    . LEU   C 1 99  ? -5.094  -21.673 20.162  1.00 24.69  ? 99  LEU   C N    1 
ATOM   4366 C  CA   . LEU   C 1 99  ? -4.562  -22.388 21.356  1.00 25.49  ? 99  LEU   C CA   1 
ATOM   4367 C  C    . LEU   C 1 99  ? -4.637  -21.450 22.566  1.00 24.14  ? 99  LEU   C C    1 
ATOM   4368 O  O    . LEU   C 1 99  ? -5.024  -21.904 23.645  1.00 25.60  ? 99  LEU   C O    1 
ATOM   4369 C  CB   . LEU   C 1 99  ? -3.131  -22.841 21.085  1.00 27.08  ? 99  LEU   C CB   1 
ATOM   4370 C  CG   . LEU   C 1 99  ? -2.345  -23.296 22.312  1.00 28.57  ? 99  LEU   C CG   1 
ATOM   4371 C  CD1  . LEU   C 1 99  ? -2.994  -24.529 22.939  1.00 30.28  ? 99  LEU   C CD1  1 
ATOM   4372 C  CD2  . LEU   C 1 99  ? -0.898  -23.565 21.917  1.00 28.22  ? 99  LEU   C CD2  1 
ATOM   4373 N  N    . TYR   C 1 100 ? -4.308  -20.177 22.372  1.00 24.64  ? 100 TYR   C N    1 
ATOM   4374 C  CA   . TYR   C 1 100 ? -4.417  -19.102 23.390  1.00 25.03  ? 100 TYR   C CA   1 
ATOM   4375 C  C    . TYR   C 1 100 ? -5.705  -18.292 23.165  1.00 25.79  ? 100 TYR   C C    1 
ATOM   4376 O  O    . TYR   C 1 100 ? -6.278  -18.322 22.048  1.00 27.78  ? 100 TYR   C O    1 
ATOM   4377 C  CB   . TYR   C 1 100 ? -3.127  -18.282 23.353  1.00 26.20  ? 100 TYR   C CB   1 
ATOM   4378 C  CG   . TYR   C 1 100 ? -1.897  -19.112 23.638  1.00 28.24  ? 100 TYR   C CG   1 
ATOM   4379 C  CD1  . TYR   C 1 100 ? -1.793  -19.896 24.785  1.00 30.09  ? 100 TYR   C CD1  1 
ATOM   4380 C  CD2  . TYR   C 1 100 ? -0.833  -19.130 22.754  1.00 31.34  ? 100 TYR   C CD2  1 
ATOM   4381 C  CE1  . TYR   C 1 100 ? -0.648  -20.636 25.061  1.00 29.76  ? 100 TYR   C CE1  1 
ATOM   4382 C  CE2  . TYR   C 1 100 ? 0.306   -19.880 23.002  1.00 31.57  ? 100 TYR   C CE2  1 
ATOM   4383 C  CZ   . TYR   C 1 100 ? 0.397   -20.635 24.157  1.00 30.80  ? 100 TYR   C CZ   1 
ATOM   4384 O  OH   . TYR   C 1 100 ? 1.526   -21.370 24.369  1.00 36.83  ? 100 TYR   C OH   1 
ATOM   4385 N  N    . LYS   C 1 101 ? -6.117  -17.540 24.186  1.00 25.87  ? 101 LYS   C N    1 
ATOM   4386 C  CA   . LYS   C 1 101 ? -7.486  -16.988 24.316  1.00 27.16  ? 101 LYS   C CA   1 
ATOM   4387 C  C    . LYS   C 1 101 ? -7.484  -15.653 25.090  1.00 25.87  ? 101 LYS   C C    1 
ATOM   4388 O  O    . LYS   C 1 101 ? -6.497  -15.342 25.813  1.00 23.40  ? 101 LYS   C O    1 
ATOM   4389 C  CB   . LYS   C 1 101 ? -8.346  -18.038 25.024  1.00 29.92  ? 101 LYS   C CB   1 
ATOM   4390 C  CG   . LYS   C 1 101 ? -7.921  -18.322 26.464  1.00 35.03  ? 101 LYS   C CG   1 
ATOM   4391 C  CD   . LYS   C 1 101 ? -8.523  -19.562 27.059  1.00 38.80  ? 101 LYS   C CD   1 
ATOM   4392 C  CE   . LYS   C 1 101 ? -7.691  -20.807 26.821  1.00 41.40  ? 101 LYS   C CE   1 
ATOM   4393 N  NZ   . LYS   C 1 101 ? -6.593  -20.909 27.810  1.00 44.02  ? 101 LYS   C NZ   1 
ATOM   4394 N  N    . GLU   C 1 102 ? -8.588  -14.918 24.944  1.00 23.58  ? 102 GLU   C N    1 
ATOM   4395 C  CA   . GLU   C 1 102 ? -8.883  -13.586 25.542  1.00 24.44  ? 102 GLU   C CA   1 
ATOM   4396 C  C    . GLU   C 1 102 ? -10.389 -13.319 25.377  1.00 22.94  ? 102 GLU   C C    1 
ATOM   4397 O  O    . GLU   C 1 102 ? -11.009 -13.904 24.453  1.00 20.89  ? 102 GLU   C O    1 
ATOM   4398 C  CB   . GLU   C 1 102 ? -8.059  -12.471 24.877  1.00 24.43  ? 102 GLU   C CB   1 
ATOM   4399 C  CG   . GLU   C 1 102 ? -8.534  -12.062 23.471  1.00 23.43  ? 102 GLU   C CG   1 
ATOM   4400 C  CD   . GLU   C 1 102 ? -7.507  -11.469 22.499  1.00 24.63  ? 102 GLU   C CD   1 
ATOM   4401 O  OE1  . GLU   C 1 102 ? -6.266  -11.481 22.797  1.00 20.53  ? 102 GLU   C OE1  1 
ATOM   4402 O  OE2  . GLU   C 1 102 ? -7.941  -11.021 21.402  1.00 24.82  ? 102 GLU   C OE2  1 
ATOM   4403 N  N    . THR   C 1 103 ? -10.952 -12.483 26.245  1.00 22.94  ? 103 THR   C N    1 
ATOM   4404 C  CA   . THR   C 1 103 ? -12.291 -11.876 26.035  1.00 24.19  ? 103 THR   C CA   1 
ATOM   4405 C  C    . THR   C 1 103 ? -12.126 -10.876 24.899  1.00 22.55  ? 103 THR   C C    1 
ATOM   4406 O  O    . THR   C 1 103 ? -11.085 -10.212 24.881  1.00 20.60  ? 103 THR   C O    1 
ATOM   4407 C  CB   . THR   C 1 103 ? -12.858 -11.206 27.293  1.00 24.91  ? 103 THR   C CB   1 
ATOM   4408 O  OG1  . THR   C 1 103 ? -12.030 -10.079 27.580  1.00 22.71  ? 103 THR   C OG1  1 
ATOM   4409 C  CG2  . THR   C 1 103 ? -12.955 -12.157 28.464  1.00 25.48  ? 103 THR   C CG2  1 
ATOM   4410 N  N    . ASN   C 1 104 ? -13.080 -10.843 23.971  1.00 21.58  ? 104 ASN   C N    1 
ATOM   4411 C  CA   . ASN   C 1 104 ? -13.131 -9.863  22.851  1.00 20.49  ? 104 ASN   C CA   1 
ATOM   4412 C  C    . ASN   C 1 104 ? -14.444 -9.077  22.991  1.00 20.22  ? 104 ASN   C C    1 
ATOM   4413 O  O    . ASN   C 1 104 ? -15.351 -9.200  22.135  1.00 20.28  ? 104 ASN   C O    1 
ATOM   4414 C  CB   . ASN   C 1 104 ? -12.902 -10.570 21.513  1.00 19.79  ? 104 ASN   C CB   1 
ATOM   4415 C  CG   . ASN   C 1 104 ? -11.553 -11.263 21.426  1.00 20.53  ? 104 ASN   C CG   1 
ATOM   4416 O  OD1  . ASN   C 1 104 ? -11.475 -12.476 21.247  1.00 25.10  ? 104 ASN   C OD1  1 
ATOM   4417 N  ND2  . ASN   C 1 104 ? -10.468 -10.518 21.505  1.00 19.66  ? 104 ASN   C ND2  1 
ATOM   4418 N  N    . THR   C 1 105 ? -14.550 -8.309  24.069  1.00 20.56  ? 105 THR   C N    1 
ATOM   4419 C  CA   . THR   C 1 105 ? -15.780 -7.599  24.486  1.00 21.34  ? 105 THR   C CA   1 
ATOM   4420 C  C    . THR   C 1 105 ? -15.823 -6.211  23.839  1.00 21.88  ? 105 THR   C C    1 
ATOM   4421 O  O    . THR   C 1 105 ? -14.904 -5.411  24.070  1.00 21.13  ? 105 THR   C O    1 
ATOM   4422 C  CB   . THR   C 1 105 ? -15.829 -7.497  26.017  1.00 23.42  ? 105 THR   C CB   1 
ATOM   4423 O  OG1  . THR   C 1 105 ? -15.487 -8.783  26.539  1.00 24.15  ? 105 THR   C OG1  1 
ATOM   4424 C  CG2  . THR   C 1 105 ? -17.177 -7.051  26.544  1.00 21.99  ? 105 THR   C CG2  1 
ATOM   4425 N  N    . ILE   C 1 106 ? -16.876 -5.937  23.072  1.00 22.54  ? 106 ILE   C N    1 
ATOM   4426 C  CA   . ILE   C 1 106 ? -17.176 -4.600  22.495  1.00 22.35  ? 106 ILE   C CA   1 
ATOM   4427 C  C    . ILE   C 1 106 ? -18.204 -3.901  23.403  1.00 22.72  ? 106 ILE   C C    1 
ATOM   4428 O  O    . ILE   C 1 106 ? -19.303 -4.473  23.622  1.00 22.97  ? 106 ILE   C O    1 
ATOM   4429 C  CB   . ILE   C 1 106 ? -17.676 -4.763  21.041  1.00 22.88  ? 106 ILE   C CB   1 
ATOM   4430 C  CG1  . ILE   C 1 106 ? -16.721 -5.589  20.169  1.00 23.15  ? 106 ILE   C CG1  1 
ATOM   4431 C  CG2  . ILE   C 1 106 ? -17.967 -3.401  20.423  1.00 23.22  ? 106 ILE   C CG2  1 
ATOM   4432 C  CD1  . ILE   C 1 106 ? -15.291 -5.071  20.111  1.00 23.20  ? 106 ILE   C CD1  1 
ATOM   4433 N  N    . LEU   C 1 107 ? -17.887 -2.698  23.891  1.00 24.06  ? 107 LEU   C N    1 
ATOM   4434 C  CA   . LEU   C 1 107 ? -18.767 -1.897  24.793  1.00 25.00  ? 107 LEU   C CA   1 
ATOM   4435 C  C    . LEU   C 1 107 ? -19.575 -0.891  23.972  1.00 23.50  ? 107 LEU   C C    1 
ATOM   4436 O  O    . LEU   C 1 107 ? -20.667 -0.519  24.439  1.00 22.38  ? 107 LEU   C O    1 
ATOM   4437 C  CB   . LEU   C 1 107 ? -17.940 -1.175  25.859  1.00 26.23  ? 107 LEU   C CB   1 
ATOM   4438 C  CG   . LEU   C 1 107 ? -17.438 -2.062  26.995  1.00 29.15  ? 107 LEU   C CG   1 
ATOM   4439 C  CD1  . LEU   C 1 107 ? -16.215 -2.841  26.557  1.00 30.36  ? 107 LEU   C CD1  1 
ATOM   4440 C  CD2  . LEU   C 1 107 ? -17.109 -1.236  28.233  1.00 28.34  ? 107 LEU   C CD2  1 
ATOM   4441 N  N    . SER   C 1 108 ? -19.051 -0.469  22.813  1.00 21.03  ? 108 SER   C N    1 
ATOM   4442 C  CA   . SER   C 1 108 ? -19.687 0.534   21.928  1.00 19.97  ? 108 SER   C CA   1 
ATOM   4443 C  C    . SER   C 1 108 ? -19.052 0.484   20.546  1.00 18.41  ? 108 SER   C C    1 
ATOM   4444 O  O    . SER   C 1 108 ? -17.913 0.000   20.432  1.00 18.22  ? 108 SER   C O    1 
ATOM   4445 C  CB   . SER   C 1 108 ? -19.622 1.903   22.516  1.00 20.64  ? 108 SER   C CB   1 
ATOM   4446 O  OG   . SER   C 1 108 ? -18.274 2.311   22.644  1.00 22.95  ? 108 SER   C OG   1 
ATOM   4447 N  N    . TRP   C 1 109 ? -19.814 0.905   19.537  1.00 17.12  ? 109 TRP   C N    1 
ATOM   4448 C  CA   . TRP   C 1 109 ? -19.431 0.858   18.110  1.00 17.42  ? 109 TRP   C CA   1 
ATOM   4449 C  C    . TRP   C 1 109 ? -20.256 1.872   17.340  1.00 17.09  ? 109 TRP   C C    1 
ATOM   4450 O  O    . TRP   C 1 109 ? -21.489 1.775   17.382  1.00 18.92  ? 109 TRP   C O    1 
ATOM   4451 C  CB   . TRP   C 1 109 ? -19.597 -0.563  17.545  1.00 17.58  ? 109 TRP   C CB   1 
ATOM   4452 C  CG   . TRP   C 1 109 ? -19.232 -0.704  16.098  1.00 17.53  ? 109 TRP   C CG   1 
ATOM   4453 C  CD1  . TRP   C 1 109 ? -18.295 0.009   15.409  1.00 18.43  ? 109 TRP   C CD1  1 
ATOM   4454 C  CD2  . TRP   C 1 109 ? -19.791 -1.636  15.156  1.00 16.98  ? 109 TRP   C CD2  1 
ATOM   4455 N  NE1  . TRP   C 1 109 ? -18.239 -0.409  14.106  1.00 18.96  ? 109 TRP   C NE1  1 
ATOM   4456 C  CE2  . TRP   C 1 109 ? -19.142 -1.423  13.924  1.00 18.30  ? 109 TRP   C CE2  1 
ATOM   4457 C  CE3  . TRP   C 1 109 ? -20.762 -2.630  15.241  1.00 17.67  ? 109 TRP   C CE3  1 
ATOM   4458 C  CZ2  . TRP   C 1 109 ? -19.438 -2.162  12.781  1.00 18.28  ? 109 TRP   C CZ2  1 
ATOM   4459 C  CZ3  . TRP   C 1 109 ? -21.054 -3.364  14.116  1.00 18.11  ? 109 TRP   C CZ3  1 
ATOM   4460 C  CH2  . TRP   C 1 109 ? -20.423 -3.114  12.899  1.00 18.54  ? 109 TRP   C CH2  1 
ATOM   4461 N  N    . SER   C 1 110 ? -19.600 2.796   16.648  1.00 17.66  ? 110 SER   C N    1 
ATOM   4462 C  CA   . SER   C 1 110 ? -20.282 3.796   15.790  1.00 17.81  ? 110 SER   C CA   1 
ATOM   4463 C  C    . SER   C 1 110 ? -19.579 3.847   14.429  1.00 16.95  ? 110 SER   C C    1 
ATOM   4464 O  O    . SER   C 1 110 ? -18.372 3.544   14.364  1.00 16.12  ? 110 SER   C O    1 
ATOM   4465 C  CB   . SER   C 1 110 ? -20.365 5.148   16.455  1.00 18.36  ? 110 SER   C CB   1 
ATOM   4466 O  OG   . SER   C 1 110 ? -19.109 5.809   16.393  1.00 22.17  ? 110 SER   C OG   1 
ATOM   4467 N  N    . PHE   C 1 111 ? -20.323 4.216   13.391  1.00 15.69  ? 111 PHE   C N    1 
ATOM   4468 C  CA   . PHE   C 1 111 ? -19.864 4.183   11.989  1.00 16.74  ? 111 PHE   C CA   1 
ATOM   4469 C  C    . PHE   C 1 111 ? -20.624 5.212   11.162  1.00 17.13  ? 111 PHE   C C    1 
ATOM   4470 O  O    . PHE   C 1 111 ? -21.899 5.271   11.279  1.00 18.75  ? 111 PHE   C O    1 
ATOM   4471 C  CB   . PHE   C 1 111 ? -20.068 2.791   11.388  1.00 16.14  ? 111 PHE   C CB   1 
ATOM   4472 C  CG   . PHE   C 1 111 ? -19.731 2.711   9.924   1.00 16.20  ? 111 PHE   C CG   1 
ATOM   4473 C  CD1  . PHE   C 1 111 ? -18.434 2.504   9.504   1.00 15.85  ? 111 PHE   C CD1  1 
ATOM   4474 C  CD2  . PHE   C 1 111 ? -20.718 2.878   8.963   1.00 16.27  ? 111 PHE   C CD2  1 
ATOM   4475 C  CE1  . PHE   C 1 111 ? -18.122 2.428   8.158   1.00 15.60  ? 111 PHE   C CE1  1 
ATOM   4476 C  CE2  . PHE   C 1 111 ? -20.403 2.812   7.619   1.00 15.70  ? 111 PHE   C CE2  1 
ATOM   4477 C  CZ   . PHE   C 1 111 ? -19.110 2.580   7.222   1.00 15.72  ? 111 PHE   C CZ   1 
ATOM   4478 N  N    . THR   C 1 112 ? -19.892 5.951   10.325  1.00 15.55  ? 112 THR   C N    1 
ATOM   4479 C  CA   . THR   C 1 112 ? -20.471 6.913   9.354   1.00 16.11  ? 112 THR   C CA   1 
ATOM   4480 C  C    . THR   C 1 112 ? -19.801 6.746   7.998   1.00 16.28  ? 112 THR   C C    1 
ATOM   4481 O  O    . THR   C 1 112 ? -18.558 6.756   7.953   1.00 16.01  ? 112 THR   C O    1 
ATOM   4482 C  CB   . THR   C 1 112 ? -20.333 8.374   9.818   1.00 16.14  ? 112 THR   C CB   1 
ATOM   4483 O  OG1  . THR   C 1 112 ? -20.964 8.491   11.085  1.00 16.88  ? 112 THR   C OG1  1 
ATOM   4484 C  CG2  . THR   C 1 112 ? -21.008 9.373   8.908   1.00 16.32  ? 112 THR   C CG2  1 
ATOM   4485 N  N    . SER   C 1 113 ? -20.603 6.663   6.940   1.00 17.69  ? 113 SER   C N    1 
ATOM   4486 C  CA   . SER   C 1 113 ? -20.126 6.692   5.536   1.00 19.55  ? 113 SER   C CA   1 
ATOM   4487 C  C    . SER   C 1 113 ? -20.782 7.853   4.801   1.00 18.78  ? 113 SER   C C    1 
ATOM   4488 O  O    . SER   C 1 113 ? -21.971 8.064   4.988   1.00 18.84  ? 113 SER   C O    1 
ATOM   4489 C  CB   . SER   C 1 113 ? -20.394 5.384   4.844   1.00 20.20  ? 113 SER   C CB   1 
ATOM   4490 O  OG   . SER   C 1 113 ? -21.794 5.168   4.716   1.00 24.44  ? 113 SER   C OG   1 
ATOM   4491 N  N    . LYS   C 1 114 ? -20.018 8.518   3.969   1.00 19.18  ? 114 LYS   C N    1 
ATOM   4492 C  CA   . LYS   C 1 114 ? -20.490 9.653   3.155   1.00 20.09  ? 114 LYS   C CA   1 
ATOM   4493 C  C    . LYS   C 1 114 ? -20.004 9.461   1.721   1.00 19.98  ? 114 LYS   C C    1 
ATOM   4494 O  O    . LYS   C 1 114 ? -18.827 9.320   1.538   1.00 18.52  ? 114 LYS   C O    1 
ATOM   4495 C  CB   . LYS   C 1 114 ? -20.072 10.977  3.792   1.00 21.50  ? 114 LYS   C CB   1 
ATOM   4496 C  CG   . LYS   C 1 114 ? -20.964 11.393  4.943   1.00 26.61  ? 114 LYS   C CG   1 
ATOM   4497 C  CD   . LYS   C 1 114 ? -20.464 12.472  5.853   1.00 30.22  ? 114 LYS   C CD   1 
ATOM   4498 C  CE   . LYS   C 1 114 ? -20.088 13.738  5.122   1.00 34.68  ? 114 LYS   C CE   1 
ATOM   4499 N  NZ   . LYS   C 1 114 ? -19.036 14.513  5.826   1.00 36.87  ? 114 LYS   C NZ   1 
ATOM   4500 N  N    . LEU   C 1 115 ? -20.932 9.361   0.780   1.00 20.92  ? 115 LEU   C N    1 
ATOM   4501 C  CA   . LEU   C 1 115 ? -20.612 9.222   -0.662  1.00 26.19  ? 115 LEU   C CA   1 
ATOM   4502 C  C    . LEU   C 1 115 ? -21.072 10.509  -1.348  1.00 30.33  ? 115 LEU   C C    1 
ATOM   4503 O  O    . LEU   C 1 115 ? -22.295 10.709  -1.518  1.00 27.17  ? 115 LEU   C O    1 
ATOM   4504 C  CB   . LEU   C 1 115 ? -21.312 7.980   -1.218  1.00 26.35  ? 115 LEU   C CB   1 
ATOM   4505 C  CG   . LEU   C 1 115 ? -20.957 7.570   -2.646  1.00 25.50  ? 115 LEU   C CG   1 
ATOM   4506 C  CD1  . LEU   C 1 115 ? -19.461 7.366   -2.812  1.00 25.56  ? 115 LEU   C CD1  1 
ATOM   4507 C  CD2  . LEU   C 1 115 ? -21.710 6.305   -3.004  1.00 26.96  ? 115 LEU   C CD2  1 
ATOM   4508 N  N    . LYS   C 1 116 ? -20.104 11.372  -1.625  1.00 38.49  ? 116 LYS   C N    1 
ATOM   4509 C  CA   . LYS   C 1 116 ? -20.295 12.767  -2.074  1.00 49.33  ? 116 LYS   C CA   1 
ATOM   4510 C  C    . LYS   C 1 116 ? -19.939 12.781  -3.552  1.00 54.53  ? 116 LYS   C C    1 
ATOM   4511 O  O    . LYS   C 1 116 ? -18.751 12.914  -3.885  1.00 58.92  ? 116 LYS   C O    1 
ATOM   4512 C  CB   . LYS   C 1 116 ? -19.431 13.714  -1.230  1.00 55.34  ? 116 LYS   C CB   1 
ATOM   4513 C  CG   . LYS   C 1 116 ? -19.474 15.182  -1.636  1.00 64.03  ? 116 LYS   C CG   1 
ATOM   4514 C  CD   . LYS   C 1 116 ? -18.559 16.090  -0.821  1.00 71.28  ? 116 LYS   C CD   1 
ATOM   4515 C  CE   . LYS   C 1 116 ? -19.084 16.389  0.571   1.00 78.83  ? 116 LYS   C CE   1 
ATOM   4516 N  NZ   . LYS   C 1 116 ? -18.793 17.787  0.982   1.00 80.88  ? 116 LYS   C NZ   1 
ATOM   4517 N  N    . SER   C 1 117 ? -20.939 12.562  -4.393  1.00 67.10  ? 117 SER   C N    1 
ATOM   4518 C  CA   . SER   C 1 117 ? -20.811 12.646  -5.866  1.00 82.57  ? 117 SER   C CA   1 
ATOM   4519 C  C    . SER   C 1 117 ? -20.310 14.050  -6.254  1.00 87.09  ? 117 SER   C C    1 
ATOM   4520 O  O    . SER   C 1 117 ? -20.710 15.031  -5.602  1.00 86.31  ? 117 SER   C O    1 
ATOM   4521 C  CB   . SER   C 1 117 ? -22.128 12.276  -6.507  1.00 87.02  ? 117 SER   C CB   1 
ATOM   4522 O  OG   . SER   C 1 117 ? -22.805 11.269  -5.750  1.00 80.74  ? 117 SER   C OG   1 
ATOM   4523 N  N    . ASN   C 1 118 ? -19.390 14.137  -7.215  1.00 99.11  ? 118 ASN   C N    1 
ATOM   4524 C  CA   . ASN   C 1 118 ? -18.980 15.416  -7.853  1.00 113.17 ? 118 ASN   C CA   1 
ATOM   4525 C  C    . ASN   C 1 118 ? -19.741 15.567  -9.180  1.00 127.82 ? 118 ASN   C C    1 
ATOM   4526 O  O    . ASN   C 1 118 ? -19.994 16.729  -9.578  1.00 117.56 ? 118 ASN   C O    1 
ATOM   4527 C  CB   . ASN   C 1 118 ? -17.464 15.493  -8.047  1.00 108.67 ? 118 ASN   C CB   1 
ATOM   4528 C  CG   . ASN   C 1 118 ? -17.006 16.902  -8.350  1.00 107.80 ? 118 ASN   C CG   1 
ATOM   4529 O  OD1  . ASN   C 1 118 ? -17.515 17.853  -7.759  1.00 103.04 ? 118 ASN   C OD1  1 
ATOM   4530 N  ND2  . ASN   C 1 118 ? -16.057 17.041  -9.263  1.00 106.22 ? 118 ASN   C ND2  1 
ATOM   4531 N  N    . SER   C 1 119 ? -20.110 14.436  -9.811  1.00 141.31 ? 119 SER   C N    1 
ATOM   4532 C  CA   . SER   C 1 119 ? -20.795 14.338  -11.132 1.00 139.69 ? 119 SER   C CA   1 
ATOM   4533 C  C    . SER   C 1 119 ? -22.326 14.392  -10.971 1.00 143.87 ? 119 SER   C C    1 
ATOM   4534 O  O    . SER   C 1 119 ? -22.957 15.118  -11.769 1.00 139.96 ? 119 SER   C O    1 
ATOM   4535 C  CB   . SER   C 1 119 ? -20.349 13.109  -11.899 1.00 130.73 ? 119 SER   C CB   1 
ATOM   4536 O  OG   . SER   C 1 119 ? -20.600 11.922  -11.162 1.00 125.43 ? 119 SER   C OG   1 
ATOM   4537 N  N    . THR   C 1 120 ? -22.911 13.674  -9.995  1.00 143.39 ? 120 THR   C N    1 
ATOM   4538 C  CA   . THR   C 1 120 ? -24.348 13.816  -9.595  1.00 130.63 ? 120 THR   C CA   1 
ATOM   4539 C  C    . THR   C 1 120 ? -24.462 15.024  -8.639  1.00 124.63 ? 120 THR   C C    1 
ATOM   4540 O  O    . THR   C 1 120 ? -25.535 15.658  -8.620  1.00 115.24 ? 120 THR   C O    1 
ATOM   4541 C  CB   . THR   C 1 120 ? -24.961 12.499  -9.071  1.00 123.51 ? 120 THR   C CB   1 
ATOM   4542 O  OG1  . THR   C 1 120 ? -24.757 12.350  -7.665  1.00 119.18 ? 120 THR   C OG1  1 
ATOM   4543 C  CG2  . THR   C 1 120 ? -24.442 11.260  -9.774  1.00 118.16 ? 120 THR   C CG2  1 
ATOM   4544 N  N    . HIS   C 1 121 ? -23.373 15.339  -7.916  1.00 124.22 ? 121 HIS   C N    1 
ATOM   4545 C  CA   . HIS   C 1 121 ? -23.137 16.526  -7.036  1.00 117.37 ? 121 HIS   C CA   1 
ATOM   4546 C  C    . HIS   C 1 121 ? -24.100 16.571  -5.835  1.00 114.48 ? 121 HIS   C C    1 
ATOM   4547 O  O    . HIS   C 1 121 ? -24.737 17.626  -5.636  1.00 123.59 ? 121 HIS   C O    1 
ATOM   4548 C  CB   . HIS   C 1 121 ? -23.159 17.844  -7.827  1.00 112.37 ? 121 HIS   C CB   1 
ATOM   4549 C  CG   . HIS   C 1 121 ? -22.826 19.023  -6.969  1.00 112.57 ? 121 HIS   C CG   1 
ATOM   4550 N  ND1  . HIS   C 1 121 ? -21.716 19.044  -6.135  1.00 104.92 ? 121 HIS   C ND1  1 
ATOM   4551 C  CD2  . HIS   C 1 121 ? -23.470 20.196  -6.770  1.00 111.08 ? 121 HIS   C CD2  1 
ATOM   4552 C  CE1  . HIS   C 1 121 ? -21.683 20.186  -5.477  1.00 103.19 ? 121 HIS   C CE1  1 
ATOM   4553 N  NE2  . HIS   C 1 121 ? -22.748 20.910  -5.848  1.00 109.77 ? 121 HIS   C NE2  1 
ATOM   4554 N  N    . GLU   C 1 122 ? -24.149 15.501  -5.028  1.00 100.95 ? 122 GLU   C N    1 
ATOM   4555 C  CA   . GLU   C 1 122 ? -24.941 15.406  -3.764  1.00 84.52  ? 122 GLU   C CA   1 
ATOM   4556 C  C    . GLU   C 1 122 ? -24.279 14.396  -2.810  1.00 65.55  ? 122 GLU   C C    1 
ATOM   4557 O  O    . GLU   C 1 122 ? -23.513 13.532  -3.304  1.00 64.99  ? 122 GLU   C O    1 
ATOM   4558 C  CB   . GLU   C 1 122 ? -26.380 14.972  -4.066  1.00 89.45  ? 122 GLU   C CB   1 
ATOM   4559 C  CG   . GLU   C 1 122 ? -27.314 16.097  -4.498  1.00 86.80  ? 122 GLU   C CG   1 
ATOM   4560 C  CD   . GLU   C 1 122 ? -27.754 17.050  -3.391  1.00 90.23  ? 122 GLU   C CD   1 
ATOM   4561 O  OE1  . GLU   C 1 122 ? -27.031 17.176  -2.371  1.00 85.96  ? 122 GLU   C OE1  1 
ATOM   4562 O  OE2  . GLU   C 1 122 ? -28.835 17.662  -3.539  1.00 87.91  ? 122 GLU   C OE2  1 
ATOM   4563 N  N    . THR   C 1 123 ? -24.589 14.459  -1.509  1.00 45.46  ? 123 THR   C N    1 
ATOM   4564 C  CA   . THR   C 1 123 ? -24.063 13.498  -0.493  1.00 39.19  ? 123 THR   C CA   1 
ATOM   4565 C  C    . THR   C 1 123 ? -25.162 12.495  -0.079  1.00 31.11  ? 123 THR   C C    1 
ATOM   4566 O  O    . THR   C 1 123 ? -26.301 12.932  0.198   1.00 28.97  ? 123 THR   C O    1 
ATOM   4567 C  CB   . THR   C 1 123 ? -23.382 14.224  0.679   1.00 38.97  ? 123 THR   C CB   1 
ATOM   4568 O  OG1  . THR   C 1 123 ? -23.171 13.250  1.708   1.00 37.66  ? 123 THR   C OG1  1 
ATOM   4569 C  CG2  . THR   C 1 123 ? -24.166 15.408  1.209   1.00 41.67  ? 123 THR   C CG2  1 
ATOM   4570 N  N    . ASN   C 1 124 ? -24.835 11.192  -0.112  1.00 24.24  ? 124 ASN   C N    1 
ATOM   4571 C  CA   . ASN   C 1 124 ? -25.583 10.084  0.544   1.00 21.27  ? 124 ASN   C CA   1 
ATOM   4572 C  C    . ASN   C 1 124 ? -24.812 9.621   1.794   1.00 19.72  ? 124 ASN   C C    1 
ATOM   4573 O  O    . ASN   C 1 124 ? -23.560 9.611   1.783   1.00 19.13  ? 124 ASN   C O    1 
ATOM   4574 C  CB   . ASN   C 1 124 ? -25.857 8.942   -0.434  1.00 20.73  ? 124 ASN   C CB   1 
ATOM   4575 C  CG   . ASN   C 1 124 ? -26.912 9.266   -1.477  1.00 21.29  ? 124 ASN   C CG   1 
ATOM   4576 O  OD1  . ASN   C 1 124 ? -27.511 10.335  -1.501  1.00 19.92  ? 124 ASN   C OD1  1 
ATOM   4577 N  ND2  . ASN   C 1 124 ? -27.179 8.321   -2.343  1.00 21.36  ? 124 ASN   C ND2  1 
ATOM   4578 N  N    . ALA   C 1 125 ? -25.522 9.244   2.854   1.00 17.77  ? 125 ALA   C N    1 
ATOM   4579 C  CA   . ALA   C 1 125 ? -24.913 8.968   4.173   1.00 16.98  ? 125 ALA   C CA   1 
ATOM   4580 C  C    . ALA   C 1 125 ? -25.637 7.834   4.899   1.00 16.10  ? 125 ALA   C C    1 
ATOM   4581 O  O    . ALA   C 1 125 ? -26.880 7.687   4.778   1.00 14.76  ? 125 ALA   C O    1 
ATOM   4582 C  CB   . ALA   C 1 125 ? -24.900 10.224  5.014   1.00 16.30  ? 125 ALA   C CB   1 
ATOM   4583 N  N    . LEU   C 1 126 ? -24.858 7.077   5.665   1.00 15.49  ? 126 LEU   C N    1 
ATOM   4584 C  CA   . LEU   C 1 126 ? -25.355 6.134   6.702   1.00 14.88  ? 126 LEU   C CA   1 
ATOM   4585 C  C    . LEU   C 1 126 ? -24.599 6.397   8.005   1.00 14.46  ? 126 LEU   C C    1 
ATOM   4586 O  O    . LEU   C 1 126 ? -23.358 6.567   7.965   1.00 14.04  ? 126 LEU   C O    1 
ATOM   4587 C  CB   . LEU   C 1 126 ? -25.144 4.701   6.212   1.00 14.10  ? 126 LEU   C CB   1 
ATOM   4588 C  CG   . LEU   C 1 126 ? -25.345 3.636   7.278   1.00 14.28  ? 126 LEU   C CG   1 
ATOM   4589 C  CD1  . LEU   C 1 126 ? -26.827 3.470   7.617   1.00 14.57  ? 126 LEU   C CD1  1 
ATOM   4590 C  CD2  . LEU   C 1 126 ? -24.755 2.349   6.800   1.00 15.34  ? 126 LEU   C CD2  1 
ATOM   4591 N  N    . HIS   C 1 127 ? -25.309 6.409   9.122   1.00 14.26  ? 127 HIS   C N    1 
ATOM   4592 C  CA   . HIS   C 1 127 ? -24.675 6.519   10.459  1.00 15.44  ? 127 HIS   C CA   1 
ATOM   4593 C  C    . HIS   C 1 127 ? -25.398 5.573   11.416  1.00 15.09  ? 127 HIS   C C    1 
ATOM   4594 O  O    . HIS   C 1 127 ? -26.643 5.552   11.399  1.00 14.16  ? 127 HIS   C O    1 
ATOM   4595 C  CB   . HIS   C 1 127 ? -24.634 7.988   10.931  1.00 16.07  ? 127 HIS   C CB   1 
ATOM   4596 C  CG   . HIS   C 1 127 ? -24.305 8.139   12.370  1.00 17.62  ? 127 HIS   C CG   1 
ATOM   4597 N  ND1  . HIS   C 1 127 ? -23.006 8.140   12.823  1.00 19.05  ? 127 HIS   C ND1  1 
ATOM   4598 C  CD2  . HIS   C 1 127 ? -25.099 8.274   13.460  1.00 18.90  ? 127 HIS   C CD2  1 
ATOM   4599 C  CE1  . HIS   C 1 127 ? -23.004 8.239   14.143  1.00 19.31  ? 127 HIS   C CE1  1 
ATOM   4600 N  NE2  . HIS   C 1 127 ? -24.279 8.324   14.558  1.00 20.29  ? 127 HIS   C NE2  1 
ATOM   4601 N  N    . PHE   C 1 128 ? -24.641 4.817   12.206  1.00 14.82  ? 128 PHE   C N    1 
ATOM   4602 C  CA   . PHE   C 1 128 ? -25.208 4.046   13.331  1.00 15.87  ? 128 PHE   C CA   1 
ATOM   4603 C  C    . PHE   C 1 128 ? -24.316 4.256   14.542  1.00 16.93  ? 128 PHE   C C    1 
ATOM   4604 O  O    . PHE   C 1 128 ? -23.115 4.519   14.429  1.00 16.75  ? 128 PHE   C O    1 
ATOM   4605 C  CB   . PHE   C 1 128 ? -25.465 2.587   12.942  1.00 16.00  ? 128 PHE   C CB   1 
ATOM   4606 C  CG   . PHE   C 1 128 ? -24.257 1.753   12.589  1.00 16.06  ? 128 PHE   C CG   1 
ATOM   4607 C  CD1  . PHE   C 1 128 ? -23.458 1.207   13.583  1.00 16.17  ? 128 PHE   C CD1  1 
ATOM   4608 C  CD2  . PHE   C 1 128 ? -23.932 1.500   11.266  1.00 16.13  ? 128 PHE   C CD2  1 
ATOM   4609 C  CE1  . PHE   C 1 128 ? -22.333 0.459   13.265  1.00 16.37  ? 128 PHE   C CE1  1 
ATOM   4610 C  CE2  . PHE   C 1 128 ? -22.818 0.738   10.945  1.00 16.63  ? 128 PHE   C CE2  1 
ATOM   4611 C  CZ   . PHE   C 1 128 ? -22.025 0.208   11.945  1.00 16.36  ? 128 PHE   C CZ   1 
ATOM   4612 N  N    . MET   C 1 129 ? -24.926 4.208   15.704  1.00 19.97  ? 129 MET   C N    1 
ATOM   4613 C  CA   . MET   C 1 129 ? -24.188 4.299   16.986  1.00 24.04  ? 129 MET   C CA   1 
ATOM   4614 C  C    . MET   C 1 129 ? -24.807 3.310   17.972  1.00 22.11  ? 129 MET   C C    1 
ATOM   4615 O  O    . MET   C 1 129 ? -26.041 3.367   18.165  1.00 20.59  ? 129 MET   C O    1 
ATOM   4616 C  CB   . MET   C 1 129 ? -24.261 5.730   17.529  1.00 27.55  ? 129 MET   C CB   1 
ATOM   4617 C  CG   . MET   C 1 129 ? -23.407 5.981   18.748  1.00 30.69  ? 129 MET   C CG   1 
ATOM   4618 S  SD   . MET   C 1 129 ? -23.640 7.659   19.420  1.00 39.80  ? 129 MET   C SD   1 
ATOM   4619 C  CE   . MET   C 1 129 ? -23.893 8.626   17.926  1.00 39.12  ? 129 MET   C CE   1 
ATOM   4620 N  N    . PHE   C 1 130 ? -23.982 2.427   18.538  1.00 23.10  ? 130 PHE   C N    1 
ATOM   4621 C  CA   . PHE   C 1 130 ? -24.345 1.535   19.666  1.00 24.04  ? 130 PHE   C CA   1 
ATOM   4622 C  C    . PHE   C 1 130 ? -23.505 1.917   20.880  1.00 24.93  ? 130 PHE   C C    1 
ATOM   4623 O  O    . PHE   C 1 130 ? -22.284 1.710   20.833  1.00 23.60  ? 130 PHE   C O    1 
ATOM   4624 C  CB   . PHE   C 1 130 ? -24.117 0.071   19.305  1.00 25.15  ? 130 PHE   C CB   1 
ATOM   4625 C  CG   . PHE   C 1 130 ? -24.763 -0.369  18.020  1.00 26.71  ? 130 PHE   C CG   1 
ATOM   4626 C  CD1  . PHE   C 1 130 ? -26.143 -0.351  17.882  1.00 31.47  ? 130 PHE   C CD1  1 
ATOM   4627 C  CD2  . PHE   C 1 130 ? -24.000 -0.811  16.952  1.00 26.36  ? 130 PHE   C CD2  1 
ATOM   4628 C  CE1  . PHE   C 1 130 ? -26.742 -0.778  16.704  1.00 29.51  ? 130 PHE   C CE1  1 
ATOM   4629 C  CE2  . PHE   C 1 130 ? -24.599 -1.219  15.769  1.00 27.28  ? 130 PHE   C CE2  1 
ATOM   4630 C  CZ   . PHE   C 1 130 ? -25.966 -1.212  15.651  1.00 27.73  ? 130 PHE   C CZ   1 
ATOM   4631 N  N    . ASN   C 1 131 ? -24.149 2.447   21.923  1.00 27.61  ? 131 ASN   C N    1 
ATOM   4632 C  CA   . ASN   C 1 131 ? -23.570 2.608   23.287  1.00 30.94  ? 131 ASN   C CA   1 
ATOM   4633 C  C    . ASN   C 1 131 ? -23.960 1.428   24.192  1.00 31.83  ? 131 ASN   C C    1 
ATOM   4634 O  O    . ASN   C 1 131 ? -23.210 1.153   25.138  1.00 33.86  ? 131 ASN   C O    1 
ATOM   4635 C  CB   . ASN   C 1 131 ? -23.963 3.941   23.915  1.00 32.33  ? 131 ASN   C CB   1 
ATOM   4636 C  CG   . ASN   C 1 131 ? -23.163 5.088   23.341  1.00 35.52  ? 131 ASN   C CG   1 
ATOM   4637 O  OD1  . ASN   C 1 131 ? -22.024 4.904   22.904  1.00 36.80  ? 131 ASN   C OD1  1 
ATOM   4638 N  ND2  . ASN   C 1 131 ? -23.751 6.272   23.344  1.00 34.40  ? 131 ASN   C ND2  1 
ATOM   4639 N  N    . GLN   C 1 132 ? -25.087 0.771   23.929  1.00 31.13  ? 132 GLN   C N    1 
ATOM   4640 C  CA   . GLN   C 1 132 ? -25.477 -0.517  24.557  1.00 34.03  ? 132 GLN   C CA   1 
ATOM   4641 C  C    . GLN   C 1 132 ? -25.978 -1.450  23.455  1.00 32.54  ? 132 GLN   C C    1 
ATOM   4642 O  O    . GLN   C 1 132 ? -26.656 -0.977  22.523  1.00 38.50  ? 132 GLN   C O    1 
ATOM   4643 C  CB   . GLN   C 1 132 ? -26.581 -0.342  25.605  1.00 37.04  ? 132 GLN   C CB   1 
ATOM   4644 C  CG   . GLN   C 1 132 ? -26.225 0.602   26.746  1.00 44.22  ? 132 GLN   C CG   1 
ATOM   4645 C  CD   . GLN   C 1 132 ? -25.012 0.185   27.553  1.00 47.39  ? 132 GLN   C CD   1 
ATOM   4646 O  OE1  . GLN   C 1 132 ? -24.686 -0.991  27.666  1.00 48.66  ? 132 GLN   C OE1  1 
ATOM   4647 N  NE2  . GLN   C 1 132 ? -24.338 1.160   28.147  1.00 46.43  ? 132 GLN   C NE2  1 
ATOM   4648 N  N    . PHE   C 1 133 ? -25.671 -2.730  23.573  1.00 30.22  ? 133 PHE   C N    1 
ATOM   4649 C  CA   . PHE   C 1 133 ? -26.223 -3.811  22.730  1.00 30.86  ? 133 PHE   C CA   1 
ATOM   4650 C  C    . PHE   C 1 133 ? -27.275 -4.517  23.576  1.00 32.39  ? 133 PHE   C C    1 
ATOM   4651 O  O    . PHE   C 1 133 ? -27.082 -4.563  24.778  1.00 32.75  ? 133 PHE   C O    1 
ATOM   4652 C  CB   . PHE   C 1 133 ? -25.104 -4.750  22.266  1.00 27.47  ? 133 PHE   C CB   1 
ATOM   4653 C  CG   . PHE   C 1 133 ? -23.983 -4.086  21.516  1.00 23.29  ? 133 PHE   C CG   1 
ATOM   4654 C  CD1  . PHE   C 1 133 ? -22.913 -3.525  22.197  1.00 22.27  ? 133 PHE   C CD1  1 
ATOM   4655 C  CD2  . PHE   C 1 133 ? -23.974 -4.057  20.126  1.00 21.87  ? 133 PHE   C CD2  1 
ATOM   4656 C  CE1  . PHE   C 1 133 ? -21.873 -2.921  21.507  1.00 21.44  ? 133 PHE   C CE1  1 
ATOM   4657 C  CE2  . PHE   C 1 133 ? -22.933 -3.454  19.437  1.00 20.46  ? 133 PHE   C CE2  1 
ATOM   4658 C  CZ   . PHE   C 1 133 ? -21.889 -2.881  20.128  1.00 21.18  ? 133 PHE   C CZ   1 
ATOM   4659 N  N    . SER   C 1 134 ? -28.340 -5.038  22.968  1.00 36.57  ? 134 SER   C N    1 
ATOM   4660 C  CA   . SER   C 1 134 ? -29.455 -5.707  23.690  1.00 37.06  ? 134 SER   C CA   1 
ATOM   4661 C  C    . SER   C 1 134 ? -29.551 -7.166  23.239  1.00 36.25  ? 134 SER   C C    1 
ATOM   4662 O  O    . SER   C 1 134 ? -28.839 -7.517  22.281  1.00 33.28  ? 134 SER   C O    1 
ATOM   4663 C  CB   . SER   C 1 134 ? -30.747 -4.944  23.516  1.00 40.21  ? 134 SER   C CB   1 
ATOM   4664 O  OG   . SER   C 1 134 ? -31.057 -4.786  22.145  1.00 40.00  ? 134 SER   C OG   1 
ATOM   4665 N  N    . LYS   C 1 135 ? -30.408 -7.955  23.905  1.00 43.11  ? 135 LYS   C N    1 
ATOM   4666 C  CA   . LYS   C 1 135 ? -30.430 -9.450  23.906  1.00 46.88  ? 135 LYS   C CA   1 
ATOM   4667 C  C    . LYS   C 1 135 ? -30.785 -9.993  22.517  1.00 47.80  ? 135 LYS   C C    1 
ATOM   4668 O  O    . LYS   C 1 135 ? -30.337 -11.118 22.203  1.00 52.23  ? 135 LYS   C O    1 
ATOM   4669 C  CB   . LYS   C 1 135 ? -31.449 -10.004 24.910  1.00 53.93  ? 135 LYS   C CB   1 
ATOM   4670 C  CG   . LYS   C 1 135 ? -31.110 -9.814  26.387  1.00 63.36  ? 135 LYS   C CG   1 
ATOM   4671 C  CD   . LYS   C 1 135 ? -30.951 -8.349  26.854  1.00 66.10  ? 135 LYS   C CD   1 
ATOM   4672 C  CE   . LYS   C 1 135 ? -32.207 -7.504  26.711  1.00 66.38  ? 135 LYS   C CE   1 
ATOM   4673 N  NZ   . LYS   C 1 135 ? -31.910 -6.053  26.621  1.00 62.00  ? 135 LYS   C NZ   1 
ATOM   4674 N  N    . ASP   C 1 136 ? -31.589 -9.256  21.743  1.00 44.51  ? 136 ASP   C N    1 
ATOM   4675 C  CA   . ASP   C 1 136 ? -31.953 -9.610  20.346  1.00 45.29  ? 136 ASP   C CA   1 
ATOM   4676 C  C    . ASP   C 1 136 ? -31.814 -8.335  19.505  1.00 41.53  ? 136 ASP   C C    1 
ATOM   4677 O  O    . ASP   C 1 136 ? -32.750 -7.516  19.456  1.00 40.46  ? 136 ASP   C O    1 
ATOM   4678 C  CB   . ASP   C 1 136 ? -33.336 -10.264 20.285  1.00 49.71  ? 136 ASP   C CB   1 
ATOM   4679 C  CG   . ASP   C 1 136 ? -33.755 -10.693 18.890  1.00 55.23  ? 136 ASP   C CG   1 
ATOM   4680 O  OD1  . ASP   C 1 136 ? -32.868 -11.072 18.095  1.00 58.86  ? 136 ASP   C OD1  1 
ATOM   4681 O  OD2  . ASP   C 1 136 ? -34.969 -10.619 18.600  1.00 61.22  ? 136 ASP   C OD2  1 
ATOM   4682 N  N    . GLN   C 1 137 ? -30.640 -8.171  18.909  1.00 35.87  ? 137 GLN   C N    1 
ATOM   4683 C  CA   . GLN   C 1 137 ? -30.171 -6.939  18.245  1.00 33.05  ? 137 GLN   C CA   1 
ATOM   4684 C  C    . GLN   C 1 137 ? -30.375 -7.161  16.748  1.00 29.38  ? 137 GLN   C C    1 
ATOM   4685 O  O    . GLN   C 1 137 ? -29.455 -7.642  16.081  1.00 26.82  ? 137 GLN   C O    1 
ATOM   4686 C  CB   . GLN   C 1 137 ? -28.725 -6.678  18.685  1.00 34.95  ? 137 GLN   C CB   1 
ATOM   4687 C  CG   . GLN   C 1 137 ? -28.144 -5.362  18.188  1.00 38.03  ? 137 GLN   C CG   1 
ATOM   4688 C  CD   . GLN   C 1 137 ? -28.425 -4.190  19.089  1.00 39.40  ? 137 GLN   C CD   1 
ATOM   4689 O  OE1  . GLN   C 1 137 ? -28.339 -4.291  20.310  1.00 44.66  ? 137 GLN   C OE1  1 
ATOM   4690 N  NE2  . GLN   C 1 137 ? -28.741 -3.056  18.483  1.00 40.84  ? 137 GLN   C NE2  1 
ATOM   4691 N  N    . LYS   C 1 138 ? -31.573 -6.849  16.257  1.00 29.03  ? 138 LYS   C N    1 
ATOM   4692 C  CA   . LYS   C 1 138 ? -32.023 -7.197  14.887  1.00 28.20  ? 138 LYS   C CA   1 
ATOM   4693 C  C    . LYS   C 1 138 ? -31.317 -6.347  13.806  1.00 25.72  ? 138 LYS   C C    1 
ATOM   4694 O  O    . LYS   C 1 138 ? -31.406 -6.753  12.655  1.00 25.06  ? 138 LYS   C O    1 
ATOM   4695 C  CB   . LYS   C 1 138 ? -33.548 -7.083  14.810  1.00 29.43  ? 138 LYS   C CB   1 
ATOM   4696 C  CG   . LYS   C 1 138 ? -34.313 -8.038  15.726  1.00 31.96  ? 138 LYS   C CG   1 
ATOM   4697 C  CD   . LYS   C 1 138 ? -35.806 -8.159  15.399  1.00 33.26  ? 138 LYS   C CD   1 
ATOM   4698 C  CE   . LYS   C 1 138 ? -36.636 -8.863  16.459  1.00 34.02  ? 138 LYS   C CE   1 
ATOM   4699 N  NZ   . LYS   C 1 138 ? -36.416 -10.331 16.443  1.00 36.50  ? 138 LYS   C NZ   1 
ATOM   4700 N  N    . ASP   C 1 139 ? -30.619 -5.249  14.139  1.00 22.73  ? 139 ASP   C N    1 
ATOM   4701 C  CA   . ASP   C 1 139 ? -29.813 -4.455  13.161  1.00 22.39  ? 139 ASP   C CA   1 
ATOM   4702 C  C    . ASP   C 1 139 ? -28.370 -4.997  13.057  1.00 22.02  ? 139 ASP   C C    1 
ATOM   4703 O  O    . ASP   C 1 139 ? -27.579 -4.416  12.287  1.00 20.57  ? 139 ASP   C O    1 
ATOM   4704 C  CB   . ASP   C 1 139 ? -29.843 -2.950  13.481  1.00 23.14  ? 139 ASP   C CB   1 
ATOM   4705 C  CG   . ASP   C 1 139 ? -29.547 -2.553  14.928  1.00 24.87  ? 139 ASP   C CG   1 
ATOM   4706 O  OD1  . ASP   C 1 139 ? -29.285 -3.468  15.776  1.00 25.00  ? 139 ASP   C OD1  1 
ATOM   4707 O  OD2  . ASP   C 1 139 ? -29.606 -1.325  15.216  1.00 24.69  ? 139 ASP   C OD2  1 
ATOM   4708 N  N    . LEU   C 1 140 ? -28.032 -6.072  13.776  1.00 20.20  ? 140 LEU   C N    1 
ATOM   4709 C  CA   . LEU   C 1 140 ? -26.714 -6.757  13.693  1.00 22.17  ? 140 LEU   C CA   1 
ATOM   4710 C  C    . LEU   C 1 140 ? -26.904 -8.183  13.192  1.00 22.65  ? 140 LEU   C C    1 
ATOM   4711 O  O    . LEU   C 1 140 ? -27.796 -8.871  13.704  1.00 24.28  ? 140 LEU   C O    1 
ATOM   4712 C  CB   . LEU   C 1 140 ? -26.048 -6.801  15.071  1.00 23.01  ? 140 LEU   C CB   1 
ATOM   4713 C  CG   . LEU   C 1 140 ? -25.511 -5.479  15.612  1.00 23.66  ? 140 LEU   C CG   1 
ATOM   4714 C  CD1  . LEU   C 1 140 ? -24.772 -5.711  16.920  1.00 25.00  ? 140 LEU   C CD1  1 
ATOM   4715 C  CD2  . LEU   C 1 140 ? -24.608 -4.807  14.592  1.00 23.32  ? 140 LEU   C CD2  1 
ATOM   4716 N  N    . ILE   C 1 141 ? -26.092 -8.597  12.232  1.00 22.38  ? 141 ILE   C N    1 
ATOM   4717 C  CA   . ILE   C 1 141 ? -25.962 -10.013 11.806  1.00 21.00  ? 141 ILE   C CA   1 
ATOM   4718 C  C    . ILE   C 1 141 ? -24.842 -10.605 12.643  1.00 20.88  ? 141 ILE   C C    1 
ATOM   4719 O  O    . ILE   C 1 141 ? -23.718 -10.128 12.525  1.00 19.53  ? 141 ILE   C O    1 
ATOM   4720 C  CB   . ILE   C 1 141 ? -25.657 -10.109 10.302  1.00 21.33  ? 141 ILE   C CB   1 
ATOM   4721 C  CG1  . ILE   C 1 141 ? -26.772 -9.463  9.470   1.00 23.00  ? 141 ILE   C CG1  1 
ATOM   4722 C  CG2  . ILE   C 1 141 ? -25.404 -11.557 9.901   1.00 21.26  ? 141 ILE   C CG2  1 
ATOM   4723 C  CD1  . ILE   C 1 141 ? -26.361 -9.060  8.060   1.00 22.33  ? 141 ILE   C CD1  1 
ATOM   4724 N  N    . LEU   C 1 142 ? -25.152 -11.607 13.455  1.00 21.91  ? 142 LEU   C N    1 
ATOM   4725 C  CA   . LEU   C 1 142 ? -24.163 -12.298 14.319  1.00 20.36  ? 142 LEU   C CA   1 
ATOM   4726 C  C    . LEU   C 1 142 ? -23.791 -13.619 13.655  1.00 20.92  ? 142 LEU   C C    1 
ATOM   4727 O  O    . LEU   C 1 142 ? -24.710 -14.356 13.291  1.00 20.39  ? 142 LEU   C O    1 
ATOM   4728 C  CB   . LEU   C 1 142 ? -24.774 -12.500 15.710  1.00 20.87  ? 142 LEU   C CB   1 
ATOM   4729 C  CG   . LEU   C 1 142 ? -25.252 -11.226 16.416  1.00 19.87  ? 142 LEU   C CG   1 
ATOM   4730 C  CD1  . LEU   C 1 142 ? -25.855 -11.576 17.768  1.00 19.47  ? 142 LEU   C CD1  1 
ATOM   4731 C  CD2  . LEU   C 1 142 ? -24.116 -10.213 16.564  1.00 18.63  ? 142 LEU   C CD2  1 
ATOM   4732 N  N    . GLN   C 1 143 ? -22.480 -13.873 13.511  1.00 20.68  ? 143 GLN   C N    1 
ATOM   4733 C  CA   . GLN   C 1 143 ? -21.875 -15.082 12.914  1.00 18.55  ? 143 GLN   C CA   1 
ATOM   4734 C  C    . GLN   C 1 143 ? -20.962 -15.751 13.950  1.00 19.41  ? 143 GLN   C C    1 
ATOM   4735 O  O    . GLN   C 1 143 ? -20.337 -15.009 14.733  1.00 19.85  ? 143 GLN   C O    1 
ATOM   4736 C  CB   . GLN   C 1 143 ? -21.104 -14.657 11.678  1.00 19.49  ? 143 GLN   C CB   1 
ATOM   4737 C  CG   . GLN   C 1 143 ? -21.945 -13.855 10.681  1.00 19.83  ? 143 GLN   C CG   1 
ATOM   4738 C  CD   . GLN   C 1 143 ? -21.191 -13.569 9.404   1.00 18.38  ? 143 GLN   C CD   1 
ATOM   4739 O  OE1  . GLN   C 1 143 ? -19.973 -13.382 9.416   1.00 18.27  ? 143 GLN   C OE1  1 
ATOM   4740 N  NE2  . GLN   C 1 143 ? -21.902 -13.550 8.288   1.00 16.37  ? 143 GLN   C NE2  1 
ATOM   4741 N  N    . GLY   C 1 144 ? -20.877 -17.094 13.941  1.00 19.21  ? 144 GLY   C N    1 
ATOM   4742 C  CA   . GLY   C 1 144 ? -20.063 -17.907 14.863  1.00 18.48  ? 144 GLY   C CA   1 
ATOM   4743 C  C    . GLY   C 1 144 ? -20.491 -17.705 16.304  1.00 19.25  ? 144 GLY   C C    1 
ATOM   4744 O  O    . GLY   C 1 144 ? -21.685 -17.714 16.546  1.00 18.21  ? 144 GLY   C O    1 
ATOM   4745 N  N    . ASP   C 1 145 ? -19.557 -17.462 17.230  1.00 20.31  ? 145 ASP   C N    1 
ATOM   4746 C  CA   . ASP   C 1 145 ? -19.815 -17.534 18.698  1.00 21.09  ? 145 ASP   C CA   1 
ATOM   4747 C  C    . ASP   C 1 145 ? -20.258 -16.180 19.259  1.00 22.33  ? 145 ASP   C C    1 
ATOM   4748 O  O    . ASP   C 1 145 ? -20.415 -16.077 20.501  1.00 21.45  ? 145 ASP   C O    1 
ATOM   4749 C  CB   . ASP   C 1 145 ? -18.581 -18.072 19.424  1.00 22.25  ? 145 ASP   C CB   1 
ATOM   4750 C  CG   . ASP   C 1 145 ? -18.160 -19.409 18.846  1.00 23.17  ? 145 ASP   C CG   1 
ATOM   4751 O  OD1  . ASP   C 1 145 ? -19.077 -20.118 18.374  1.00 22.16  ? 145 ASP   C OD1  1 
ATOM   4752 O  OD2  . ASP   C 1 145 ? -16.922 -19.707 18.826  1.00 24.41  ? 145 ASP   C OD2  1 
ATOM   4753 N  N    . ALA   C 1 146 ? -20.489 -15.195 18.389  1.00 21.77  ? 146 ALA   C N    1 
ATOM   4754 C  CA   . ALA   C 1 146 ? -20.828 -13.811 18.771  1.00 21.44  ? 146 ALA   C CA   1 
ATOM   4755 C  C    . ALA   C 1 146 ? -22.219 -13.769 19.398  1.00 22.47  ? 146 ALA   C C    1 
ATOM   4756 O  O    . ALA   C 1 146 ? -23.152 -14.288 18.785  1.00 21.47  ? 146 ALA   C O    1 
ATOM   4757 C  CB   . ALA   C 1 146 ? -20.731 -12.929 17.552  1.00 20.91  ? 146 ALA   C CB   1 
ATOM   4758 N  N    . THR   C 1 147 ? -22.343 -13.165 20.584  1.00 25.22  ? 147 THR   C N    1 
ATOM   4759 C  CA   . THR   C 1 147 ? -23.642 -12.904 21.262  1.00 25.59  ? 147 THR   C CA   1 
ATOM   4760 C  C    . THR   C 1 147 ? -23.687 -11.457 21.763  1.00 24.64  ? 147 THR   C C    1 
ATOM   4761 O  O    . THR   C 1 147 ? -22.627 -10.823 21.873  1.00 24.38  ? 147 THR   C O    1 
ATOM   4762 C  CB   . THR   C 1 147 ? -23.876 -13.861 22.439  1.00 26.78  ? 147 THR   C CB   1 
ATOM   4763 O  OG1  . THR   C 1 147 ? -22.825 -13.685 23.390  1.00 29.00  ? 147 THR   C OG1  1 
ATOM   4764 C  CG2  . THR   C 1 147 ? -23.934 -15.313 22.020  1.00 27.40  ? 147 THR   C CG2  1 
ATOM   4765 N  N    . THR   C 1 148 ? -24.881 -10.993 22.105  1.00 25.56  ? 148 THR   C N    1 
ATOM   4766 C  CA   . THR   C 1 148 ? -25.154 -9.661  22.694  1.00 28.34  ? 148 THR   C CA   1 
ATOM   4767 C  C    . THR   C 1 148 ? -25.982 -9.838  23.967  1.00 32.62  ? 148 THR   C C    1 
ATOM   4768 O  O    . THR   C 1 148 ? -26.487 -10.951 24.190  1.00 32.49  ? 148 THR   C O    1 
ATOM   4769 C  CB   . THR   C 1 148 ? -25.907 -8.775  21.695  1.00 27.79  ? 148 THR   C CB   1 
ATOM   4770 O  OG1  . THR   C 1 148 ? -27.054 -9.494  21.245  1.00 25.99  ? 148 THR   C OG1  1 
ATOM   4771 C  CG2  . THR   C 1 148 ? -25.078 -8.383  20.492  1.00 28.37  ? 148 THR   C CG2  1 
ATOM   4772 N  N    . GLY   C 1 149 ? -26.085 -8.777  24.771  1.00 38.67  ? 149 GLY   C N    1 
ATOM   4773 C  CA   . GLY   C 1 149 ? -27.138 -8.598  25.793  1.00 43.76  ? 149 GLY   C CA   1 
ATOM   4774 C  C    . GLY   C 1 149 ? -26.623 -8.710  27.216  1.00 45.75  ? 149 GLY   C C    1 
ATOM   4775 O  O    . GLY   C 1 149 ? -27.217 -8.058  28.112  1.00 46.47  ? 149 GLY   C O    1 
ATOM   4776 N  N    . THR   C 1 150 ? -25.574 -9.509  27.428  1.00 48.72  ? 150 THR   C N    1 
ATOM   4777 C  CA   . THR   C 1 150 ? -25.008 -9.785  28.775  1.00 51.15  ? 150 THR   C CA   1 
ATOM   4778 C  C    . THR   C 1 150 ? -24.238 -8.526  29.198  1.00 48.70  ? 150 THR   C C    1 
ATOM   4779 O  O    . THR   C 1 150 ? -23.169 -8.230  28.615  1.00 40.83  ? 150 THR   C O    1 
ATOM   4780 C  CB   . THR   C 1 150 ? -24.239 -11.116 28.788  1.00 53.87  ? 150 THR   C CB   1 
ATOM   4781 O  OG1  . THR   C 1 150 ? -23.447 -11.223 27.602  1.00 55.38  ? 150 THR   C OG1  1 
ATOM   4782 C  CG2  . THR   C 1 150 ? -25.157 -12.319 28.865  1.00 54.40  ? 150 THR   C CG2  1 
ATOM   4783 N  N    . ASP   C 1 151 ? -24.843 -7.753  30.102  1.00 45.57  ? 151 ASP   C N    1 
ATOM   4784 C  CA   . ASP   C 1 151 ? -24.291 -6.476  30.615  1.00 45.60  ? 151 ASP   C CA   1 
ATOM   4785 C  C    . ASP   C 1 151 ? -24.290 -5.435  29.489  1.00 38.75  ? 151 ASP   C C    1 
ATOM   4786 O  O    . ASP   C 1 151 ? -23.581 -4.448  29.621  1.00 39.53  ? 151 ASP   C O    1 
ATOM   4787 C  CB   . ASP   C 1 151 ? -22.899 -6.695  31.227  1.00 52.22  ? 151 ASP   C CB   1 
ATOM   4788 C  CG   . ASP   C 1 151 ? -22.442 -5.566  32.147  1.00 58.32  ? 151 ASP   C CG   1 
ATOM   4789 O  OD1  . ASP   C 1 151 ? -23.276 -5.092  32.978  1.00 52.59  ? 151 ASP   C OD1  1 
ATOM   4790 O  OD2  . ASP   C 1 151 ? -21.256 -5.155  32.021  1.00 59.47  ? 151 ASP   C OD2  1 
ATOM   4791 N  N    . GLY   C 1 152 ? -25.085 -5.630  28.434  1.00 34.24  ? 152 GLY   C N    1 
ATOM   4792 C  CA   . GLY   C 1 152 ? -25.216 -4.667  27.322  1.00 31.63  ? 152 GLY   C CA   1 
ATOM   4793 C  C    . GLY   C 1 152 ? -23.973 -4.592  26.437  1.00 29.38  ? 152 GLY   C C    1 
ATOM   4794 O  O    . GLY   C 1 152 ? -23.776 -3.544  25.754  1.00 26.75  ? 152 GLY   C O    1 
ATOM   4795 N  N    . ASN   C 1 153 ? -23.164 -5.657  26.423  1.00 25.45  ? 153 ASN   C N    1 
ATOM   4796 C  CA   . ASN   C 1 153 ? -21.937 -5.735  25.596  1.00 23.49  ? 153 ASN   C CA   1 
ATOM   4797 C  C    . ASN   C 1 153 ? -22.154 -6.709  24.444  1.00 22.29  ? 153 ASN   C C    1 
ATOM   4798 O  O    . ASN   C 1 153 ? -23.144 -7.452  24.438  1.00 22.14  ? 153 ASN   C O    1 
ATOM   4799 C  CB   . ASN   C 1 153 ? -20.704 -6.106  26.415  1.00 23.76  ? 153 ASN   C CB   1 
ATOM   4800 C  CG   . ASN   C 1 153 ? -20.431 -5.090  27.501  1.00 24.47  ? 153 ASN   C CG   1 
ATOM   4801 O  OD1  . ASN   C 1 153 ? -20.699 -3.902  27.318  1.00 25.33  ? 153 ASN   C OD1  1 
ATOM   4802 N  ND2  . ASN   C 1 153 ? -19.940 -5.552  28.634  1.00 23.09  ? 153 ASN   C ND2  1 
ATOM   4803 N  N    . LEU   C 1 154 ? -21.280 -6.607  23.458  1.00 21.35  ? 154 LEU   C N    1 
ATOM   4804 C  CA   . LEU   C 1 154 ? -21.147 -7.555  22.347  1.00 22.54  ? 154 LEU   C CA   1 
ATOM   4805 C  C    . LEU   C 1 154 ? -19.900 -8.376  22.676  1.00 24.15  ? 154 LEU   C C    1 
ATOM   4806 O  O    . LEU   C 1 154 ? -18.837 -7.762  22.847  1.00 22.32  ? 154 LEU   C O    1 
ATOM   4807 C  CB   . LEU   C 1 154 ? -21.034 -6.740  21.058  1.00 22.99  ? 154 LEU   C CB   1 
ATOM   4808 C  CG   . LEU   C 1 154 ? -20.509 -7.473  19.833  1.00 23.83  ? 154 LEU   C CG   1 
ATOM   4809 C  CD1  . LEU   C 1 154 ? -21.413 -8.639  19.468  1.00 25.53  ? 154 LEU   C CD1  1 
ATOM   4810 C  CD2  . LEU   C 1 154 ? -20.379 -6.512  18.675  1.00 23.68  ? 154 LEU   C CD2  1 
ATOM   4811 N  N    . GLU   C 1 155 ? -20.056 -9.695  22.870  1.00 26.62  ? 155 GLU   C N    1 
ATOM   4812 C  CA   . GLU   C 1 155 ? -18.920 -10.637 23.085  1.00 26.82  ? 155 GLU   C CA   1 
ATOM   4813 C  C    . GLU   C 1 155 ? -18.695 -11.335 21.756  1.00 25.65  ? 155 GLU   C C    1 
ATOM   4814 O  O    . GLU   C 1 155 ? -19.596 -12.076 21.327  1.00 27.89  ? 155 GLU   C O    1 
ATOM   4815 C  CB   . GLU   C 1 155 ? -19.202 -11.640 24.203  1.00 27.67  ? 155 GLU   C CB   1 
ATOM   4816 C  CG   . GLU   C 1 155 ? -19.527 -10.988 25.529  1.00 29.83  ? 155 GLU   C CG   1 
ATOM   4817 C  CD   . GLU   C 1 155 ? -18.348 -10.537 26.374  1.00 33.01  ? 155 GLU   C CD   1 
ATOM   4818 O  OE1  . GLU   C 1 155 ? -17.188 -10.740 25.946  1.00 37.87  ? 155 GLU   C OE1  1 
ATOM   4819 O  OE2  . GLU   C 1 155 ? -18.601 -9.981  27.463  1.00 33.21  ? 155 GLU   C OE2  1 
ATOM   4820 N  N    . LEU   C 1 156 ? -17.595 -11.021 21.079  1.00 23.48  ? 156 LEU   C N    1 
ATOM   4821 C  CA   . LEU   C 1 156 ? -17.357 -11.561 19.720  1.00 22.42  ? 156 LEU   C CA   1 
ATOM   4822 C  C    . LEU   C 1 156 ? -16.964 -13.037 19.827  1.00 22.10  ? 156 LEU   C C    1 
ATOM   4823 O  O    . LEU   C 1 156 ? -17.292 -13.790 18.913  1.00 21.45  ? 156 LEU   C O    1 
ATOM   4824 C  CB   . LEU   C 1 156 ? -16.288 -10.723 19.030  1.00 20.43  ? 156 LEU   C CB   1 
ATOM   4825 C  CG   . LEU   C 1 156 ? -16.759 -9.350  18.565  1.00 20.15  ? 156 LEU   C CG   1 
ATOM   4826 C  CD1  . LEU   C 1 156 ? -15.563 -8.490  18.196  1.00 19.35  ? 156 LEU   C CD1  1 
ATOM   4827 C  CD2  . LEU   C 1 156 ? -17.726 -9.467  17.388  1.00 19.72  ? 156 LEU   C CD2  1 
ATOM   4828 N  N    . THR   C 1 157 ? -16.294 -13.436 20.910  1.00 23.12  ? 157 THR   C N    1 
ATOM   4829 C  CA   . THR   C 1 157 ? -15.844 -14.840 21.102  1.00 24.58  ? 157 THR   C CA   1 
ATOM   4830 C  C    . THR   C 1 157 ? -16.475 -15.412 22.363  1.00 25.81  ? 157 THR   C C    1 
ATOM   4831 O  O    . THR   C 1 157 ? -16.947 -14.636 23.217  1.00 22.29  ? 157 THR   C O    1 
ATOM   4832 C  CB   . THR   C 1 157 ? -14.318 -14.999 21.077  1.00 24.88  ? 157 THR   C CB   1 
ATOM   4833 O  OG1  . THR   C 1 157 ? -13.725 -14.181 22.080  1.00 25.61  ? 157 THR   C OG1  1 
ATOM   4834 C  CG2  . THR   C 1 157 ? -13.730 -14.664 19.724  1.00 25.40  ? 157 THR   C CG2  1 
ATOM   4835 N  N    . ARG   C 1 158 ? -16.496 -16.743 22.419  1.00 30.66  ? 158 ARG   C N    1 
ATOM   4836 C  CA   . ARG   C 1 158 ? -17.250 -17.530 23.426  1.00 36.83  ? 158 ARG   C CA   1 
ATOM   4837 C  C    . ARG   C 1 158 ? -16.636 -17.241 24.795  1.00 33.85  ? 158 ARG   C C    1 
ATOM   4838 O  O    . ARG   C 1 158 ? -15.409 -17.374 24.916  1.00 33.45  ? 158 ARG   C O    1 
ATOM   4839 C  CB   . ARG   C 1 158 ? -17.220 -19.020 23.056  1.00 44.31  ? 158 ARG   C CB   1 
ATOM   4840 C  CG   . ARG   C 1 158 ? -17.987 -19.915 24.020  1.00 52.52  ? 158 ARG   C CG   1 
ATOM   4841 C  CD   . ARG   C 1 158 ? -19.277 -20.498 23.465  1.00 61.14  ? 158 ARG   C CD   1 
ATOM   4842 N  NE   . ARG   C 1 158 ? -19.129 -21.923 23.151  1.00 69.02  ? 158 ARG   C NE   1 
ATOM   4843 C  CZ   . ARG   C 1 158 ? -20.110 -22.830 23.174  1.00 73.95  ? 158 ARG   C CZ   1 
ATOM   4844 N  NH1  . ARG   C 1 158 ? -19.836 -24.091 22.876  1.00 73.47  ? 158 ARG   C NH1  1 
ATOM   4845 N  NH2  . ARG   C 1 158 ? -21.350 -22.486 23.503  1.00 75.23  ? 158 ARG   C NH2  1 
ATOM   4846 N  N    . VAL   C 1 159 ? -17.467 -16.810 25.744  1.00 35.55  ? 159 VAL   C N    1 
ATOM   4847 C  CA   . VAL   C 1 159 ? -17.138 -16.615 27.188  1.00 38.65  ? 159 VAL   C CA   1 
ATOM   4848 C  C    . VAL   C 1 159 ? -17.985 -17.605 28.012  1.00 42.36  ? 159 VAL   C C    1 
ATOM   4849 O  O    . VAL   C 1 159 ? -19.154 -17.843 27.655  1.00 41.87  ? 159 VAL   C O    1 
ATOM   4850 C  CB   . VAL   C 1 159 ? -17.393 -15.157 27.621  1.00 41.29  ? 159 VAL   C CB   1 
ATOM   4851 C  CG1  . VAL   C 1 159 ? -17.173 -14.968 29.114  1.00 43.76  ? 159 VAL   C CG1  1 
ATOM   4852 C  CG2  . VAL   C 1 159 ? -16.555 -14.156 26.835  1.00 41.73  ? 159 VAL   C CG2  1 
ATOM   4853 N  N    . SER   C 1 160 ? -17.418 -18.164 29.083  1.00 45.25  ? 160 SER   C N    1 
ATOM   4854 C  CA   . SER   C 1 160 ? -18.078 -19.145 29.986  1.00 47.96  ? 160 SER   C CA   1 
ATOM   4855 C  C    . SER   C 1 160 ? -19.074 -18.426 30.892  1.00 54.01  ? 160 SER   C C    1 
ATOM   4856 O  O    . SER   C 1 160 ? -19.060 -17.176 30.922  1.00 51.23  ? 160 SER   C O    1 
ATOM   4857 C  CB   . SER   C 1 160 ? -17.066 -19.884 30.802  1.00 45.70  ? 160 SER   C CB   1 
ATOM   4858 O  OG   . SER   C 1 160 ? -16.294 -20.738 29.972  1.00 49.25  ? 160 SER   C OG   1 
ATOM   4859 N  N    . SER   C 1 161 ? -19.893 -19.192 31.619  1.00 62.30  ? 161 SER   C N    1 
ATOM   4860 C  CA   . SER   C 1 161 ? -20.793 -18.677 32.686  1.00 63.72  ? 161 SER   C CA   1 
ATOM   4861 C  C    . SER   C 1 161 ? -19.978 -17.859 33.704  1.00 65.73  ? 161 SER   C C    1 
ATOM   4862 O  O    . SER   C 1 161 ? -20.463 -16.783 34.105  1.00 67.57  ? 161 SER   C O    1 
ATOM   4863 C  CB   . SER   C 1 161 ? -21.584 -19.793 33.332  1.00 63.94  ? 161 SER   C CB   1 
ATOM   4864 O  OG   . SER   C 1 161 ? -20.811 -20.979 33.447  1.00 67.47  ? 161 SER   C OG   1 
ATOM   4865 N  N    . ASN   C 1 162 ? -18.757 -18.298 34.046  1.00 68.22  ? 162 ASN   C N    1 
ATOM   4866 C  CA   . ASN   C 1 162 ? -17.879 -17.658 35.074  1.00 68.05  ? 162 ASN   C CA   1 
ATOM   4867 C  C    . ASN   C 1 162 ? -17.102 -16.462 34.491  1.00 65.62  ? 162 ASN   C C    1 
ATOM   4868 O  O    . ASN   C 1 162 ? -16.321 -15.850 35.251  1.00 65.10  ? 162 ASN   C O    1 
ATOM   4869 C  CB   . ASN   C 1 162 ? -16.925 -18.672 35.723  1.00 69.55  ? 162 ASN   C CB   1 
ATOM   4870 C  CG   . ASN   C 1 162 ? -16.206 -19.559 34.725  1.00 70.29  ? 162 ASN   C CG   1 
ATOM   4871 O  OD1  . ASN   C 1 162 ? -16.195 -19.271 33.532  1.00 71.82  ? 162 ASN   C OD1  1 
ATOM   4872 N  ND2  . ASN   C 1 162 ? -15.614 -20.645 35.197  1.00 67.68  ? 162 ASN   C ND2  1 
ATOM   4873 N  N    . GLY   C 1 163 ? -17.294 -16.135 33.207  1.00 62.00  ? 163 GLY   C N    1 
ATOM   4874 C  CA   . GLY   C 1 163 ? -16.688 -14.960 32.543  1.00 58.81  ? 163 GLY   C CA   1 
ATOM   4875 C  C    . GLY   C 1 163 ? -15.337 -15.276 31.910  1.00 53.11  ? 163 GLY   C C    1 
ATOM   4876 O  O    . GLY   C 1 163 ? -14.630 -14.323 31.491  1.00 50.23  ? 163 GLY   C O    1 
ATOM   4877 N  N    . SER   C 1 164 ? -15.002 -16.562 31.799  1.00 43.35  ? 164 SER   C N    1 
ATOM   4878 C  CA   . SER   C 1 164 ? -13.684 -17.060 31.336  1.00 42.65  ? 164 SER   C CA   1 
ATOM   4879 C  C    . SER   C 1 164 ? -13.727 -17.341 29.838  1.00 39.37  ? 164 SER   C C    1 
ATOM   4880 O  O    . SER   C 1 164 ? -14.667 -17.971 29.340  1.00 33.66  ? 164 SER   C O    1 
ATOM   4881 C  CB   . SER   C 1 164 ? -13.274 -18.279 32.113  1.00 46.04  ? 164 SER   C CB   1 
ATOM   4882 O  OG   . SER   C 1 164 ? -13.251 -17.981 33.499  1.00 47.67  ? 164 SER   C OG   1 
ATOM   4883 N  N    . PRO   C 1 165 ? -12.716 -16.869 29.070  1.00 35.90  ? 165 PRO   C N    1 
ATOM   4884 C  CA   . PRO   C 1 165 ? -12.740 -17.003 27.614  1.00 34.22  ? 165 PRO   C CA   1 
ATOM   4885 C  C    . PRO   C 1 165 ? -12.356 -18.429 27.212  1.00 34.63  ? 165 PRO   C C    1 
ATOM   4886 O  O    . PRO   C 1 165 ? -11.559 -19.001 27.905  1.00 33.36  ? 165 PRO   C O    1 
ATOM   4887 C  CB   . PRO   C 1 165 ? -11.710 -15.990 27.120  1.00 33.59  ? 165 PRO   C CB   1 
ATOM   4888 C  CG   . PRO   C 1 165 ? -10.741 -15.853 28.292  1.00 35.42  ? 165 PRO   C CG   1 
ATOM   4889 C  CD   . PRO   C 1 165 ? -11.541 -16.132 29.552  1.00 34.86  ? 165 PRO   C CD   1 
ATOM   4890 N  N    . GLN   C 1 166 ? -12.954 -18.946 26.132  1.00 34.86  ? 166 GLN   C N    1 
ATOM   4891 C  CA   . GLN   C 1 166 ? -12.659 -20.276 25.538  1.00 35.48  ? 166 GLN   C CA   1 
ATOM   4892 C  C    . GLN   C 1 166 ? -11.700 -20.108 24.345  1.00 31.24  ? 166 GLN   C C    1 
ATOM   4893 O  O    . GLN   C 1 166 ? -11.704 -19.040 23.690  1.00 30.48  ? 166 GLN   C O    1 
ATOM   4894 C  CB   . GLN   C 1 166 ? -13.949 -20.978 25.090  1.00 42.62  ? 166 GLN   C CB   1 
ATOM   4895 C  CG   . GLN   C 1 166 ? -14.846 -21.492 26.222  1.00 49.54  ? 166 GLN   C CG   1 
ATOM   4896 C  CD   . GLN   C 1 166 ? -15.672 -22.697 25.808  1.00 55.83  ? 166 GLN   C CD   1 
ATOM   4897 O  OE1  . GLN   C 1 166 ? -15.996 -22.897 24.632  1.00 55.11  ? 166 GLN   C OE1  1 
ATOM   4898 N  NE2  . GLN   C 1 166 ? -16.013 -23.537 26.776  1.00 58.60  ? 166 GLN   C NE2  1 
ATOM   4899 N  N    . GLY   C 1 167 ? -10.914 -21.143 24.066  1.00 25.34  ? 167 GLY   C N    1 
ATOM   4900 C  CA   . GLY   C 1 167 ? -10.050 -21.226 22.881  1.00 23.98  ? 167 GLY   C CA   1 
ATOM   4901 C  C    . GLY   C 1 167 ? -10.845 -21.629 21.660  1.00 24.02  ? 167 GLY   C C    1 
ATOM   4902 O  O    . GLY   C 1 167 ? -12.062 -21.901 21.823  1.00 25.50  ? 167 GLY   C O    1 
ATOM   4903 N  N    . SER   C 1 168 ? -10.193 -21.648 20.491  1.00 22.27  ? 168 SER   C N    1 
ATOM   4904 C  CA   . SER   C 1 168 ? -10.734 -22.117 19.188  1.00 23.19  ? 168 SER   C CA   1 
ATOM   4905 C  C    . SER   C 1 168 ? -12.135 -21.541 18.962  1.00 22.73  ? 168 SER   C C    1 
ATOM   4906 O  O    . SER   C 1 168 ? -13.026 -22.277 18.563  1.00 21.14  ? 168 SER   C O    1 
ATOM   4907 C  CB   . SER   C 1 168 ? -10.707 -23.622 19.130  1.00 23.52  ? 168 SER   C CB   1 
ATOM   4908 O  OG   . SER   C 1 168 ? -9.363  -24.076 18.994  1.00 24.62  ? 168 SER   C OG   1 
ATOM   4909 N  N    . SER   C 1 169 ? -12.290 -20.248 19.227  1.00 24.67  ? 169 SER   C N    1 
ATOM   4910 C  CA   . SER   C 1 169 ? -13.545 -19.476 19.068  1.00 25.50  ? 169 SER   C CA   1 
ATOM   4911 C  C    . SER   C 1 169 ? -13.369 -18.395 17.994  1.00 26.01  ? 169 SER   C C    1 
ATOM   4912 O  O    . SER   C 1 169 ? -12.278 -17.769 17.938  1.00 24.90  ? 169 SER   C O    1 
ATOM   4913 C  CB   . SER   C 1 169 ? -13.964 -18.873 20.368  1.00 26.96  ? 169 SER   C CB   1 
ATOM   4914 O  OG   . SER   C 1 169 ? -15.263 -18.325 20.232  1.00 29.79  ? 169 SER   C OG   1 
ATOM   4915 N  N    . VAL   C 1 170 ? -14.405 -18.181 17.175  1.00 24.09  ? 170 VAL   C N    1 
ATOM   4916 C  CA   . VAL   C 1 170 ? -14.450 -17.084 16.173  1.00 22.80  ? 170 VAL   C CA   1 
ATOM   4917 C  C    . VAL   C 1 170 ? -15.883 -16.535 16.129  1.00 23.69  ? 170 VAL   C C    1 
ATOM   4918 O  O    . VAL   C 1 170 ? -16.872 -17.329 16.171  1.00 22.15  ? 170 VAL   C O    1 
ATOM   4919 C  CB   . VAL   C 1 170 ? -13.941 -17.558 14.797  1.00 23.57  ? 170 VAL   C CB   1 
ATOM   4920 C  CG1  . VAL   C 1 170 ? -14.710 -18.771 14.289  1.00 24.58  ? 170 VAL   C CG1  1 
ATOM   4921 C  CG2  . VAL   C 1 170 ? -13.946 -16.450 13.741  1.00 22.83  ? 170 VAL   C CG2  1 
ATOM   4922 N  N    . GLY   C 1 171 ? -15.999 -15.209 16.063  1.00 23.36  ? 171 GLY   C N    1 
ATOM   4923 C  CA   . GLY   C 1 171 ? -17.297 -14.497 16.072  1.00 23.48  ? 171 GLY   C CA   1 
ATOM   4924 C  C    . GLY   C 1 171 ? -17.199 -13.167 15.341  1.00 21.73  ? 171 GLY   C C    1 
ATOM   4925 O  O    . GLY   C 1 171 ? -16.149 -12.504 15.450  1.00 18.30  ? 171 GLY   C O    1 
ATOM   4926 N  N    . ARG   C 1 172 ? -18.226 -12.843 14.557  1.00 20.81  ? 172 ARG   C N    1 
ATOM   4927 C  CA   . ARG   C 1 172 ? -18.328 -11.539 13.857  1.00 20.31  ? 172 ARG   C CA   1 
ATOM   4928 C  C    . ARG   C 1 172 ? -19.715 -10.943 14.097  1.00 20.52  ? 172 ARG   C C    1 
ATOM   4929 O  O    . ARG   C 1 172 ? -20.663 -11.707 14.431  1.00 19.71  ? 172 ARG   C O    1 
ATOM   4930 C  CB   . ARG   C 1 172 ? -18.009 -11.712 12.373  1.00 18.81  ? 172 ARG   C CB   1 
ATOM   4931 C  CG   . ARG   C 1 172 ? -16.753 -12.533 12.142  1.00 18.04  ? 172 ARG   C CG   1 
ATOM   4932 C  CD   . ARG   C 1 172 ? -16.230 -12.450 10.736  1.00 17.61  ? 172 ARG   C CD   1 
ATOM   4933 N  NE   . ARG   C 1 172 ? -17.236 -12.558 9.691   1.00 16.02  ? 172 ARG   C NE   1 
ATOM   4934 C  CZ   . ARG   C 1 172 ? -16.953 -12.619 8.398   1.00 16.46  ? 172 ARG   C CZ   1 
ATOM   4935 N  NH1  . ARG   C 1 172 ? -15.692 -12.629 7.987   1.00 15.93  ? 172 ARG   C NH1  1 
ATOM   4936 N  NH2  . ARG   C 1 172 ? -17.939 -12.687 7.516   1.00 17.36  ? 172 ARG   C NH2  1 
ATOM   4937 N  N    . ALA   C 1 173 ? -19.785 -9.617  13.993  1.00 18.87  ? 173 ALA   C N    1 
ATOM   4938 C  CA   . ALA   C 1 173 ? -21.017 -8.810  14.038  1.00 18.11  ? 173 ALA   C CA   1 
ATOM   4939 C  C    . ALA   C 1 173 ? -20.987 -7.889  12.818  1.00 18.41  ? 173 ALA   C C    1 
ATOM   4940 O  O    . ALA   C 1 173 ? -20.017 -7.144  12.704  1.00 18.76  ? 173 ALA   C O    1 
ATOM   4941 C  CB   . ALA   C 1 173 ? -21.060 -8.049  15.334  1.00 17.76  ? 173 ALA   C CB   1 
ATOM   4942 N  N    . LEU   C 1 174 ? -21.940 -8.008  11.894  1.00 18.03  ? 174 LEU   C N    1 
ATOM   4943 C  CA   . LEU   C 1 174 ? -22.024 -7.130  10.699  1.00 18.56  ? 174 LEU   C CA   1 
ATOM   4944 C  C    . LEU   C 1 174 ? -23.284 -6.263  10.790  1.00 18.17  ? 174 LEU   C C    1 
ATOM   4945 O  O    . LEU   C 1 174 ? -24.340 -6.777  11.202  1.00 17.78  ? 174 LEU   C O    1 
ATOM   4946 C  CB   . LEU   C 1 174 ? -22.080 -7.994  9.447   1.00 20.08  ? 174 LEU   C CB   1 
ATOM   4947 C  CG   . LEU   C 1 174 ? -20.802 -8.738  9.084   1.00 20.30  ? 174 LEU   C CG   1 
ATOM   4948 C  CD1  . LEU   C 1 174 ? -20.690 -10.019 9.881   1.00 22.16  ? 174 LEU   C CD1  1 
ATOM   4949 C  CD2  . LEU   C 1 174 ? -20.796 -9.060  7.603   1.00 20.51  ? 174 LEU   C CD2  1 
ATOM   4950 N  N    . PHE   C 1 175 ? -23.193 -4.993  10.428  1.00 16.35  ? 175 PHE   C N    1 
ATOM   4951 C  CA   . PHE   C 1 175 ? -24.373 -4.108  10.449  1.00 17.21  ? 175 PHE   C CA   1 
ATOM   4952 C  C    . PHE   C 1 175 ? -25.304 -4.596  9.334   1.00 17.52  ? 175 PHE   C C    1 
ATOM   4953 O  O    . PHE   C 1 175 ? -24.821 -5.063  8.271   1.00 16.32  ? 175 PHE   C O    1 
ATOM   4954 C  CB   . PHE   C 1 175 ? -23.967 -2.635  10.326  1.00 18.29  ? 175 PHE   C CB   1 
ATOM   4955 C  CG   . PHE   C 1 175 ? -25.152 -1.723  10.437  1.00 18.12  ? 175 PHE   C CG   1 
ATOM   4956 C  CD1  . PHE   C 1 175 ? -25.776 -1.544  11.652  1.00 18.62  ? 175 PHE   C CD1  1 
ATOM   4957 C  CD2  . PHE   C 1 175 ? -25.700 -1.139  9.315   1.00 18.75  ? 175 PHE   C CD2  1 
ATOM   4958 C  CE1  . PHE   C 1 175 ? -26.918 -0.766  11.745  1.00 20.31  ? 175 PHE   C CE1  1 
ATOM   4959 C  CE2  . PHE   C 1 175 ? -26.825 -0.343  9.416   1.00 19.37  ? 175 PHE   C CE2  1 
ATOM   4960 C  CZ   . PHE   C 1 175 ? -27.448 -0.183  10.621  1.00 19.94  ? 175 PHE   C CZ   1 
ATOM   4961 N  N    . TYR   C 1 176 ? -26.609 -4.538  9.573   1.00 19.37  ? 176 TYR   C N    1 
ATOM   4962 C  CA   . TYR   C 1 176 ? -27.627 -5.160  8.687   1.00 20.58  ? 176 TYR   C CA   1 
ATOM   4963 C  C    . TYR   C 1 176 ? -27.591 -4.499  7.305   1.00 19.04  ? 176 TYR   C C    1 
ATOM   4964 O  O    . TYR   C 1 176 ? -27.564 -5.212  6.312   1.00 17.90  ? 176 TYR   C O    1 
ATOM   4965 C  CB   . TYR   C 1 176 ? -29.010 -5.110  9.327   1.00 23.43  ? 176 TYR   C CB   1 
ATOM   4966 C  CG   . TYR   C 1 176 ? -29.939 -6.177  8.821   1.00 27.51  ? 176 TYR   C CG   1 
ATOM   4967 C  CD1  . TYR   C 1 176 ? -30.730 -5.938  7.717   1.00 31.00  ? 176 TYR   C CD1  1 
ATOM   4968 C  CD2  . TYR   C 1 176 ? -30.041 -7.411  9.441   1.00 31.41  ? 176 TYR   C CD2  1 
ATOM   4969 C  CE1  . TYR   C 1 176 ? -31.616 -6.887  7.247   1.00 33.91  ? 176 TYR   C CE1  1 
ATOM   4970 C  CE2  . TYR   C 1 176 ? -30.900 -8.393  8.962   1.00 32.56  ? 176 TYR   C CE2  1 
ATOM   4971 C  CZ   . TYR   C 1 176 ? -31.698 -8.127  7.859   1.00 36.61  ? 176 TYR   C CZ   1 
ATOM   4972 O  OH   . TYR   C 1 176 ? -32.573 -9.051  7.332   1.00 39.93  ? 176 TYR   C OH   1 
ATOM   4973 N  N    . ALA   C 1 177 ? -27.574 -3.173  7.225   1.00 18.67  ? 177 ALA   C N    1 
ATOM   4974 C  CA   . ALA   C 1 177 ? -27.725 -2.488  5.921   1.00 18.97  ? 177 ALA   C CA   1 
ATOM   4975 C  C    . ALA   C 1 177 ? -26.398 -2.535  5.177   1.00 19.47  ? 177 ALA   C C    1 
ATOM   4976 O  O    . ALA   C 1 177 ? -25.350 -2.184  5.724   1.00 18.54  ? 177 ALA   C O    1 
ATOM   4977 C  CB   . ALA   C 1 177 ? -28.188 -1.065  6.106   1.00 19.77  ? 177 ALA   C CB   1 
ATOM   4978 N  N    . PRO   C 1 178 ? -26.386 -2.915  3.889   1.00 18.37  ? 178 PRO   C N    1 
ATOM   4979 C  CA   . PRO   C 1 178 ? -25.197 -2.699  3.082   1.00 18.31  ? 178 PRO   C CA   1 
ATOM   4980 C  C    . PRO   C 1 178 ? -24.856 -1.204  3.036   1.00 17.32  ? 178 PRO   C C    1 
ATOM   4981 O  O    . PRO   C 1 178 ? -25.740 -0.383  3.223   1.00 16.36  ? 178 PRO   C O    1 
ATOM   4982 C  CB   . PRO   C 1 178 ? -25.563 -3.227  1.681   1.00 18.68  ? 178 PRO   C CB   1 
ATOM   4983 C  CG   . PRO   C 1 178 ? -26.793 -4.080  1.901   1.00 19.58  ? 178 PRO   C CG   1 
ATOM   4984 C  CD   . PRO   C 1 178 ? -27.485 -3.510  3.124   1.00 19.27  ? 178 PRO   C CD   1 
ATOM   4985 N  N    . VAL   C 1 179 ? -23.588 -0.921  2.734   1.00 16.98  ? 179 VAL   C N    1 
ATOM   4986 C  CA   . VAL   C 1 179 ? -22.973 0.423   2.623   1.00 15.91  ? 179 VAL   C CA   1 
ATOM   4987 C  C    . VAL   C 1 179 ? -22.491 0.613   1.187   1.00 17.07  ? 179 VAL   C C    1 
ATOM   4988 O  O    . VAL   C 1 179 ? -21.789 -0.315  0.662   1.00 14.83  ? 179 VAL   C O    1 
ATOM   4989 C  CB   . VAL   C 1 179 ? -21.798 0.540   3.594   1.00 16.98  ? 179 VAL   C CB   1 
ATOM   4990 C  CG1  . VAL   C 1 179 ? -21.146 1.906   3.481   1.00 17.44  ? 179 VAL   C CG1  1 
ATOM   4991 C  CG2  . VAL   C 1 179 ? -22.212 0.224   5.040   1.00 17.39  ? 179 VAL   C CG2  1 
ATOM   4992 N  N    . HIS   C 1 180 ? -22.795 1.780   0.598   1.00 17.12  ? 180 HIS   C N    1 
ATOM   4993 C  CA   . HIS   C 1 180 ? -22.348 2.165   -0.761  1.00 17.79  ? 180 HIS   C CA   1 
ATOM   4994 C  C    . HIS   C 1 180 ? -20.970 2.827   -0.617  1.00 19.15  ? 180 HIS   C C    1 
ATOM   4995 O  O    . HIS   C 1 180 ? -20.907 3.990   -0.208  1.00 18.84  ? 180 HIS   C O    1 
ATOM   4996 C  CB   . HIS   C 1 180 ? -23.406 3.032   -1.471  1.00 18.22  ? 180 HIS   C CB   1 
ATOM   4997 C  CG   . HIS   C 1 180 ? -23.297 3.026   -2.963  1.00 18.59  ? 180 HIS   C CG   1 
ATOM   4998 N  ND1  . HIS   C 1 180 ? -24.120 3.785   -3.774  1.00 21.04  ? 180 HIS   C ND1  1 
ATOM   4999 C  CD2  . HIS   C 1 180 ? -22.477 2.362   -3.806  1.00 20.25  ? 180 HIS   C CD2  1 
ATOM   5000 C  CE1  . HIS   C 1 180 ? -23.815 3.585   -5.040  1.00 20.71  ? 180 HIS   C CE1  1 
ATOM   5001 N  NE2  . HIS   C 1 180 ? -22.795 2.733   -5.090  1.00 20.03  ? 180 HIS   C NE2  1 
ATOM   5002 N  N    . ILE   C 1 181 ? -19.905 2.113   -0.969  1.00 20.46  ? 181 ILE   C N    1 
ATOM   5003 C  CA   . ILE   C 1 181 ? -18.500 2.527   -0.680  1.00 24.13  ? 181 ILE   C CA   1 
ATOM   5004 C  C    . ILE   C 1 181 ? -17.910 3.279   -1.887  1.00 23.68  ? 181 ILE   C C    1 
ATOM   5005 O  O    . ILE   C 1 181 ? -17.010 4.091   -1.676  1.00 24.10  ? 181 ILE   C O    1 
ATOM   5006 C  CB   . ILE   C 1 181 ? -17.699 1.290   -0.216  1.00 26.91  ? 181 ILE   C CB   1 
ATOM   5007 C  CG1  . ILE   C 1 181 ? -16.806 1.606   0.981   1.00 31.57  ? 181 ILE   C CG1  1 
ATOM   5008 C  CG2  . ILE   C 1 181 ? -16.922 0.630   -1.332  1.00 26.69  ? 181 ILE   C CG2  1 
ATOM   5009 C  CD1  . ILE   C 1 181 ? -17.564 1.889   2.257   1.00 31.29  ? 181 ILE   C CD1  1 
ATOM   5010 N  N    . TRP   C 1 182 ? -18.408 3.058   -3.109  1.00 24.89  ? 182 TRP   C N    1 
ATOM   5011 C  CA   . TRP   C 1 182 ? -18.024 3.886   -4.287  1.00 26.64  ? 182 TRP   C CA   1 
ATOM   5012 C  C    . TRP   C 1 182 ? -18.965 3.674   -5.470  1.00 27.91  ? 182 TRP   C C    1 
ATOM   5013 O  O    . TRP   C 1 182 ? -19.630 2.638   -5.544  1.00 30.90  ? 182 TRP   C O    1 
ATOM   5014 C  CB   . TRP   C 1 182 ? -16.579 3.603   -4.709  1.00 25.61  ? 182 TRP   C CB   1 
ATOM   5015 C  CG   . TRP   C 1 182 ? -16.305 2.178   -5.084  1.00 26.08  ? 182 TRP   C CG   1 
ATOM   5016 C  CD1  . TRP   C 1 182 ? -15.836 1.192   -4.266  1.00 25.68  ? 182 TRP   C CD1  1 
ATOM   5017 C  CD2  . TRP   C 1 182 ? -16.437 1.576   -6.385  1.00 25.78  ? 182 TRP   C CD2  1 
ATOM   5018 N  NE1  . TRP   C 1 182 ? -15.685 0.024   -4.956  1.00 25.35  ? 182 TRP   C NE1  1 
ATOM   5019 C  CE2  . TRP   C 1 182 ? -16.027 0.229   -6.264  1.00 26.34  ? 182 TRP   C CE2  1 
ATOM   5020 C  CE3  . TRP   C 1 182 ? -16.856 2.035   -7.633  1.00 25.07  ? 182 TRP   C CE3  1 
ATOM   5021 C  CZ2  . TRP   C 1 182 ? -16.034 -0.658  -7.340  1.00 25.46  ? 182 TRP   C CZ2  1 
ATOM   5022 C  CZ3  . TRP   C 1 182 ? -16.857 1.159   -8.698  1.00 26.83  ? 182 TRP   C CZ3  1 
ATOM   5023 C  CH2  . TRP   C 1 182 ? -16.461 -0.170  -8.552  1.00 24.85  ? 182 TRP   C CH2  1 
ATOM   5024 N  N    . GLU   C 1 183 ? -18.938 4.614   -6.406  1.00 31.34  ? 183 GLU   C N    1 
ATOM   5025 C  CA   . GLU   C 1 183 ? -19.824 4.659   -7.599  1.00 35.62  ? 183 GLU   C CA   1 
ATOM   5026 C  C    . GLU   C 1 183 ? -18.953 4.692   -8.853  1.00 31.53  ? 183 GLU   C C    1 
ATOM   5027 O  O    . GLU   C 1 183 ? -19.400 4.242   -9.898  1.00 34.27  ? 183 GLU   C O    1 
ATOM   5028 C  CB   . GLU   C 1 183 ? -20.741 5.883   -7.516  1.00 40.01  ? 183 GLU   C CB   1 
ATOM   5029 C  CG   . GLU   C 1 183 ? -21.981 5.803   -8.401  1.00 45.12  ? 183 GLU   C CG   1 
ATOM   5030 C  CD   . GLU   C 1 183 ? -22.625 7.157   -8.686  1.00 50.51  ? 183 GLU   C CD   1 
ATOM   5031 O  OE1  . GLU   C 1 183 ? -22.450 8.088   -7.863  1.00 53.55  ? 183 GLU   C OE1  1 
ATOM   5032 O  OE2  . GLU   C 1 183 ? -23.288 7.296   -9.744  1.00 56.69  ? 183 GLU   C OE2  1 
ATOM   5033 N  N    . SER   C 1 184 ? -17.762 5.257   -8.749  1.00 33.31  ? 184 SER   C N    1 
ATOM   5034 C  CA   . SER   C 1 184 ? -16.761 5.314   -9.840  1.00 33.39  ? 184 SER   C CA   1 
ATOM   5035 C  C    . SER   C 1 184 ? -15.409 5.664   -9.223  1.00 34.84  ? 184 SER   C C    1 
ATOM   5036 O  O    . SER   C 1 184 ? -15.367 5.937   -8.010  1.00 34.96  ? 184 SER   C O    1 
ATOM   5037 C  CB   . SER   C 1 184 ? -17.155 6.314   -10.873 1.00 31.92  ? 184 SER   C CB   1 
ATOM   5038 O  OG   . SER   C 1 184 ? -16.780 7.611   -10.442 1.00 37.43  ? 184 SER   C OG   1 
ATOM   5039 N  N    . SER   C 1 185 ? -14.371 5.676   -10.051 1.00 38.44  ? 185 SER   C N    1 
ATOM   5040 C  CA   . SER   C 1 185 ? -12.974 6.050   -9.717  1.00 41.05  ? 185 SER   C CA   1 
ATOM   5041 C  C    . SER   C 1 185 ? -12.953 7.375   -8.943  1.00 39.81  ? 185 SER   C C    1 
ATOM   5042 O  O    . SER   C 1 185 ? -12.173 7.505   -7.972  1.00 38.49  ? 185 SER   C O    1 
ATOM   5043 C  CB   . SER   C 1 185 ? -12.167 6.129   -10.992 1.00 43.94  ? 185 SER   C CB   1 
ATOM   5044 O  OG   . SER   C 1 185 ? -11.025 6.946   -10.819 1.00 50.29  ? 185 SER   C OG   1 
ATOM   5045 N  N    . ALA   C 1 186 ? -13.809 8.315   -9.346  1.00 39.26  ? 186 ALA   C N    1 
ATOM   5046 C  CA   . ALA   C 1 186 ? -13.787 9.723   -8.897  1.00 35.84  ? 186 ALA   C CA   1 
ATOM   5047 C  C    . ALA   C 1 186 ? -14.796 9.935   -7.770  1.00 32.30  ? 186 ALA   C C    1 
ATOM   5048 O  O    . ALA   C 1 186 ? -14.784 11.025  -7.192  1.00 33.97  ? 186 ALA   C O    1 
ATOM   5049 C  CB   . ALA   C 1 186 ? -14.080 10.625  -10.069 1.00 37.30  ? 186 ALA   C CB   1 
ATOM   5050 N  N    . VAL   C 1 187 ? -15.651 8.953   -7.488  1.00 30.45  ? 187 VAL   C N    1 
ATOM   5051 C  CA   . VAL   C 1 187 ? -16.707 9.077   -6.438  1.00 28.49  ? 187 VAL   C CA   1 
ATOM   5052 C  C    . VAL   C 1 187 ? -16.521 7.917   -5.467  1.00 25.62  ? 187 VAL   C C    1 
ATOM   5053 O  O    . VAL   C 1 187 ? -17.114 6.847   -5.687  1.00 26.21  ? 187 VAL   C O    1 
ATOM   5054 C  CB   . VAL   C 1 187 ? -18.126 9.137   -7.041  1.00 29.18  ? 187 VAL   C CB   1 
ATOM   5055 C  CG1  . VAL   C 1 187 ? -19.215 9.257   -5.978  1.00 30.75  ? 187 VAL   C CG1  1 
ATOM   5056 C  CG2  . VAL   C 1 187 ? -18.261 10.274  -8.031  1.00 29.83  ? 187 VAL   C CG2  1 
ATOM   5057 N  N    . VAL   C 1 188 ? -15.689 8.104   -4.443  1.00 23.89  ? 188 VAL   C N    1 
ATOM   5058 C  CA   . VAL   C 1 188 ? -15.488 7.053   -3.419  1.00 23.07  ? 188 VAL   C CA   1 
ATOM   5059 C  C    . VAL   C 1 188 ? -15.867 7.595   -2.041  1.00 20.34  ? 188 VAL   C C    1 
ATOM   5060 O  O    . VAL   C 1 188 ? -15.745 8.808   -1.793  1.00 22.25  ? 188 VAL   C O    1 
ATOM   5061 C  CB   . VAL   C 1 188 ? -14.081 6.437   -3.515  1.00 25.97  ? 188 VAL   C CB   1 
ATOM   5062 C  CG1  . VAL   C 1 188 ? -13.618 6.417   -4.967  1.00 26.96  ? 188 VAL   C CG1  1 
ATOM   5063 C  CG2  . VAL   C 1 188 ? -13.068 7.121   -2.630  1.00 28.56  ? 188 VAL   C CG2  1 
ATOM   5064 N  N    . ALA   C 1 189 ? -16.390 6.719   -1.196  1.00 17.49  ? 189 ALA   C N    1 
ATOM   5065 C  CA   . ALA   C 1 189 ? -16.928 7.085   0.126   1.00 18.24  ? 189 ALA   C CA   1 
ATOM   5066 C  C    . ALA   C 1 189 ? -15.766 7.470   1.056   1.00 16.86  ? 189 ALA   C C    1 
ATOM   5067 O  O    . ALA   C 1 189 ? -14.682 6.908   0.905   1.00 16.17  ? 189 ALA   C O    1 
ATOM   5068 C  CB   . ALA   C 1 189 ? -17.746 5.950   0.684   1.00 17.67  ? 189 ALA   C CB   1 
ATOM   5069 N  N    . SER   C 1 190 ? -15.987 8.444   1.938   1.00 15.62  ? 190 SER   C N    1 
ATOM   5070 C  CA   . SER   C 1 190 ? -15.241 8.598   3.204   1.00 15.85  ? 190 SER   C CA   1 
ATOM   5071 C  C    . SER   C 1 190 ? -16.014 7.876   4.311   1.00 15.55  ? 190 SER   C C    1 
ATOM   5072 O  O    . SER   C 1 190 ? -17.283 7.780   4.222   1.00 15.84  ? 190 SER   C O    1 
ATOM   5073 C  CB   . SER   C 1 190 ? -15.010 10.050  3.537   1.00 16.30  ? 190 SER   C CB   1 
ATOM   5074 O  OG   . SER   C 1 190 ? -14.042 10.591  2.666   1.00 16.25  ? 190 SER   C OG   1 
ATOM   5075 N  N    . PHE   C 1 191 ? -15.301 7.397   5.326   1.00 14.98  ? 191 PHE   C N    1 
ATOM   5076 C  CA   . PHE   C 1 191 ? -15.940 6.737   6.488   1.00 14.96  ? 191 PHE   C CA   1 
ATOM   5077 C  C    . PHE   C 1 191 ? -15.089 6.910   7.750   1.00 14.87  ? 191 PHE   C C    1 
ATOM   5078 O  O    . PHE   C 1 191 ? -13.882 7.219   7.699   1.00 13.54  ? 191 PHE   C O    1 
ATOM   5079 C  CB   . PHE   C 1 191 ? -16.361 5.302   6.148   1.00 14.95  ? 191 PHE   C CB   1 
ATOM   5080 C  CG   . PHE   C 1 191 ? -15.282 4.268   6.006   1.00 15.41  ? 191 PHE   C CG   1 
ATOM   5081 C  CD1  . PHE   C 1 191 ? -14.618 3.772   7.116   1.00 16.33  ? 191 PHE   C CD1  1 
ATOM   5082 C  CD2  . PHE   C 1 191 ? -14.948 3.771   4.755   1.00 16.80  ? 191 PHE   C CD2  1 
ATOM   5083 C  CE1  . PHE   C 1 191 ? -13.625 2.821   6.975   1.00 16.49  ? 191 PHE   C CE1  1 
ATOM   5084 C  CE2  . PHE   C 1 191 ? -13.964 2.804   4.616   1.00 16.11  ? 191 PHE   C CE2  1 
ATOM   5085 C  CZ   . PHE   C 1 191 ? -13.314 2.331   5.732   1.00 16.90  ? 191 PHE   C CZ   1 
ATOM   5086 N  N    . GLU   C 1 192 ? -15.789 6.764   8.872   1.00 14.97  ? 192 GLU   C N    1 
ATOM   5087 C  CA   . GLU   C 1 192 ? -15.258 6.894   10.243  1.00 16.30  ? 192 GLU   C CA   1 
ATOM   5088 C  C    . GLU   C 1 192 ? -15.942 5.815   11.070  1.00 15.79  ? 192 GLU   C C    1 
ATOM   5089 O  O    . GLU   C 1 192 ? -17.179 5.655   10.956  1.00 14.45  ? 192 GLU   C O    1 
ATOM   5090 C  CB   . GLU   C 1 192 ? -15.535 8.283   10.836  1.00 18.07  ? 192 GLU   C CB   1 
ATOM   5091 C  CG   . GLU   C 1 192 ? -14.921 8.507   12.217  1.00 18.93  ? 192 GLU   C CG   1 
ATOM   5092 C  CD   . GLU   C 1 192 ? -14.977 9.964   12.656  1.00 20.88  ? 192 GLU   C CD   1 
ATOM   5093 O  OE1  . GLU   C 1 192 ? -15.797 10.691  12.053  1.00 21.92  ? 192 GLU   C OE1  1 
ATOM   5094 O  OE2  . GLU   C 1 192 ? -14.208 10.383  13.593  1.00 21.07  ? 192 GLU   C OE2  1 
ATOM   5095 N  N    . ALA   C 1 193 ? -15.138 5.084   11.825  1.00 15.09  ? 193 ALA   C N    1 
ATOM   5096 C  CA   . ALA   C 1 193 ? -15.614 4.083   12.798  1.00 15.23  ? 193 ALA   C CA   1 
ATOM   5097 C  C    . ALA   C 1 193 ? -14.890 4.317   14.110  1.00 14.02  ? 193 ALA   C C    1 
ATOM   5098 O  O    . ALA   C 1 193 ? -13.747 4.763   14.102  1.00 13.71  ? 193 ALA   C O    1 
ATOM   5099 C  CB   . ALA   C 1 193 ? -15.423 2.684   12.263  1.00 15.61  ? 193 ALA   C CB   1 
ATOM   5100 N  N    . THR   C 1 194 ? -15.596 4.100   15.191  1.00 15.62  ? 194 THR   C N    1 
ATOM   5101 C  CA   . THR   C 1 194 ? -15.031 4.038   16.555  1.00 18.46  ? 194 THR   C CA   1 
ATOM   5102 C  C    . THR   C 1 194 ? -15.653 2.847   17.275  1.00 16.70  ? 194 THR   C C    1 
ATOM   5103 O  O    . THR   C 1 194 ? -16.843 2.551   17.031  1.00 16.30  ? 194 THR   C O    1 
ATOM   5104 C  CB   . THR   C 1 194 ? -15.275 5.340   17.329  1.00 20.21  ? 194 THR   C CB   1 
ATOM   5105 O  OG1  . THR   C 1 194 ? -16.691 5.418   17.500  1.00 22.31  ? 194 THR   C OG1  1 
ATOM   5106 C  CG2  . THR   C 1 194 ? -14.765 6.554   16.590  1.00 20.97  ? 194 THR   C CG2  1 
ATOM   5107 N  N    . PHE   C 1 195 ? -14.866 2.199   18.119  1.00 16.25  ? 195 PHE   C N    1 
ATOM   5108 C  CA   . PHE   C 1 195 ? -15.356 1.149   19.024  1.00 17.36  ? 195 PHE   C CA   1 
ATOM   5109 C  C    . PHE   C 1 195 ? -14.520 1.159   20.292  1.00 18.41  ? 195 PHE   C C    1 
ATOM   5110 O  O    . PHE   C 1 195 ? -13.319 1.471   20.250  1.00 16.85  ? 195 PHE   C O    1 
ATOM   5111 C  CB   . PHE   C 1 195 ? -15.406 -0.214  18.322  1.00 18.20  ? 195 PHE   C CB   1 
ATOM   5112 C  CG   . PHE   C 1 195 ? -14.105 -0.810  17.836  1.00 18.28  ? 195 PHE   C CG   1 
ATOM   5113 C  CD1  . PHE   C 1 195 ? -13.374 -1.675  18.649  1.00 17.75  ? 195 PHE   C CD1  1 
ATOM   5114 C  CD2  . PHE   C 1 195 ? -13.666 -0.590  16.536  1.00 18.02  ? 195 PHE   C CD2  1 
ATOM   5115 C  CE1  . PHE   C 1 195 ? -12.218 -2.274  18.180  1.00 18.25  ? 195 PHE   C CE1  1 
ATOM   5116 C  CE2  . PHE   C 1 195 ? -12.496 -1.180  16.077  1.00 19.13  ? 195 PHE   C CE2  1 
ATOM   5117 C  CZ   . PHE   C 1 195 ? -11.771 -2.012  16.901  1.00 19.23  ? 195 PHE   C CZ   1 
ATOM   5118 N  N    . THR   C 1 196 ? -15.180 0.858   21.407  1.00 20.13  ? 196 THR   C N    1 
ATOM   5119 C  CA   . THR   C 1 196 ? -14.502 0.612   22.701  1.00 21.89  ? 196 THR   C CA   1 
ATOM   5120 C  C    . THR   C 1 196 ? -14.518 -0.892  22.910  1.00 19.99  ? 196 THR   C C    1 
ATOM   5121 O  O    . THR   C 1 196 ? -15.492 -1.518  22.508  1.00 19.03  ? 196 THR   C O    1 
ATOM   5122 C  CB   . THR   C 1 196 ? -15.109 1.462   23.818  1.00 23.65  ? 196 THR   C CB   1 
ATOM   5123 O  OG1  . THR   C 1 196 ? -16.427 0.990   24.096  1.00 27.20  ? 196 THR   C OG1  1 
ATOM   5124 C  CG2  . THR   C 1 196 ? -15.142 2.928   23.430  1.00 24.06  ? 196 THR   C CG2  1 
ATOM   5125 N  N    . PHE   C 1 197 ? -13.426 -1.422  23.438  1.00 18.93  ? 197 PHE   C N    1 
ATOM   5126 C  CA   . PHE   C 1 197 ? -13.192 -2.871  23.580  1.00 19.73  ? 197 PHE   C CA   1 
ATOM   5127 C  C    . PHE   C 1 197 ? -12.535 -3.137  24.933  1.00 21.67  ? 197 PHE   C C    1 
ATOM   5128 O  O    . PHE   C 1 197 ? -11.830 -2.276  25.457  1.00 20.32  ? 197 PHE   C O    1 
ATOM   5129 C  CB   . PHE   C 1 197 ? -12.305 -3.363  22.440  1.00 18.61  ? 197 PHE   C CB   1 
ATOM   5130 C  CG   . PHE   C 1 197 ? -10.937 -2.725  22.434  1.00 17.66  ? 197 PHE   C CG   1 
ATOM   5131 C  CD1  . PHE   C 1 197 ? -9.912  -3.246  23.209  1.00 17.57  ? 197 PHE   C CD1  1 
ATOM   5132 C  CD2  . PHE   C 1 197 ? -10.684 -1.606  21.664  1.00 17.58  ? 197 PHE   C CD2  1 
ATOM   5133 C  CE1  . PHE   C 1 197 ? -8.656  -2.666  23.195  1.00 18.00  ? 197 PHE   C CE1  1 
ATOM   5134 C  CE2  . PHE   C 1 197 ? -9.430  -1.025  21.653  1.00 17.68  ? 197 PHE   C CE2  1 
ATOM   5135 C  CZ   . PHE   C 1 197 ? -8.425  -1.545  22.432  1.00 18.17  ? 197 PHE   C CZ   1 
ATOM   5136 N  N    . LEU   C 1 198 ? -12.778 -4.331  25.465  1.00 24.67  ? 198 LEU   C N    1 
ATOM   5137 C  CA   . LEU   C 1 198 ? -12.105 -4.866  26.663  1.00 23.93  ? 198 LEU   C CA   1 
ATOM   5138 C  C    . LEU   C 1 198 ? -11.560 -6.242  26.285  1.00 23.80  ? 198 LEU   C C    1 
ATOM   5139 O  O    . LEU   C 1 198 ? -12.377 -7.119  25.944  1.00 22.80  ? 198 LEU   C O    1 
ATOM   5140 C  CB   . LEU   C 1 198 ? -13.111 -4.924  27.812  1.00 25.32  ? 198 LEU   C CB   1 
ATOM   5141 C  CG   . LEU   C 1 198 ? -12.501 -4.877  29.210  1.00 26.14  ? 198 LEU   C CG   1 
ATOM   5142 C  CD1  . LEU   C 1 198 ? -13.581 -4.883  30.284  1.00 28.60  ? 198 LEU   C CD1  1 
ATOM   5143 C  CD2  . LEU   C 1 198 ? -11.546 -6.023  29.409  1.00 25.63  ? 198 LEU   C CD2  1 
ATOM   5144 N  N    . ILE   C 1 199 ? -10.231 -6.361  26.242  1.00 22.87  ? 199 ILE   C N    1 
ATOM   5145 C  CA   . ILE   C 1 199 ? -9.495  -7.638  26.085  1.00 23.65  ? 199 ILE   C CA   1 
ATOM   5146 C  C    . ILE   C 1 199 ? -8.872  -8.008  27.433  1.00 25.87  ? 199 ILE   C C    1 
ATOM   5147 O  O    . ILE   C 1 199 ? -7.974  -7.268  27.880  1.00 24.49  ? 199 ILE   C O    1 
ATOM   5148 C  CB   . ILE   C 1 199 ? -8.458  -7.537  24.963  1.00 23.40  ? 199 ILE   C CB   1 
ATOM   5149 C  CG1  . ILE   C 1 199 ? -9.150  -7.362  23.610  1.00 23.42  ? 199 ILE   C CG1  1 
ATOM   5150 C  CG2  . ILE   C 1 199 ? -7.545  -8.753  24.984  1.00 23.32  ? 199 ILE   C CG2  1 
ATOM   5151 C  CD1  . ILE   C 1 199 ? -8.267  -6.793  22.528  1.00 24.29  ? 199 ILE   C CD1  1 
ATOM   5152 N  N    . LYS   C 1 200 ? -9.358  -9.117  28.014  1.00 26.11  ? 200 LYS   C N    1 
ATOM   5153 C  CA   . LYS   C 1 200 ? -9.018  -9.673  29.347  1.00 29.73  ? 200 LYS   C CA   1 
ATOM   5154 C  C    . LYS   C 1 200 ? -8.581  -11.119 29.109  1.00 30.38  ? 200 LYS   C C    1 
ATOM   5155 O  O    . LYS   C 1 200 ? -9.264  -11.830 28.355  1.00 29.58  ? 200 LYS   C O    1 
ATOM   5156 C  CB   . LYS   C 1 200 ? -10.217 -9.591  30.309  1.00 32.59  ? 200 LYS   C CB   1 
ATOM   5157 C  CG   . LYS   C 1 200 ? -9.867  -9.516  31.796  1.00 37.53  ? 200 LYS   C CG   1 
ATOM   5158 C  CD   . LYS   C 1 200 ? -11.041 -9.325  32.784  1.00 40.84  ? 200 LYS   C CD   1 
ATOM   5159 C  CE   . LYS   C 1 200 ? -11.812 -8.021  32.641  1.00 44.00  ? 200 LYS   C CE   1 
ATOM   5160 N  NZ   . LYS   C 1 200 ? -11.155 -6.878  33.334  1.00 45.44  ? 200 LYS   C NZ   1 
ATOM   5161 N  N    . SER   C 1 201 ? -7.467  -11.533 29.702  1.00 32.18  ? 201 SER   C N    1 
ATOM   5162 C  CA   . SER   C 1 201 ? -6.909  -12.899 29.545  1.00 37.70  ? 201 SER   C CA   1 
ATOM   5163 C  C    . SER   C 1 201 ? -6.311  -13.376 30.868  1.00 38.39  ? 201 SER   C C    1 
ATOM   5164 O  O    . SER   C 1 201 ? -5.604  -12.625 31.519  1.00 34.10  ? 201 SER   C O    1 
ATOM   5165 C  CB   . SER   C 1 201 ? -5.890  -12.922 28.433  1.00 37.07  ? 201 SER   C CB   1 
ATOM   5166 O  OG   . SER   C 1 201 ? -5.426  -14.240 28.192  1.00 39.96  ? 201 SER   C OG   1 
ATOM   5167 N  N    . PRO   C 1 202 ? -6.536  -14.644 31.281  1.00 49.45  ? 202 PRO   C N    1 
ATOM   5168 C  CA   . PRO   C 1 202 ? -5.827  -15.221 32.427  1.00 52.82  ? 202 PRO   C CA   1 
ATOM   5169 C  C    . PRO   C 1 202 ? -4.394  -15.625 32.037  1.00 54.01  ? 202 PRO   C C    1 
ATOM   5170 O  O    . PRO   C 1 202 ? -3.523  -15.574 32.864  1.00 54.58  ? 202 PRO   C O    1 
ATOM   5171 C  CB   . PRO   C 1 202 ? -6.699  -16.433 32.774  1.00 54.18  ? 202 PRO   C CB   1 
ATOM   5172 C  CG   . PRO   C 1 202 ? -7.225  -16.896 31.423  1.00 54.70  ? 202 PRO   C CG   1 
ATOM   5173 C  CD   . PRO   C 1 202 ? -7.436  -15.617 30.630  1.00 53.11  ? 202 PRO   C CD   1 
ATOM   5174 N  N    . ASP   C 1 203 ? -4.182  -15.999 30.773  1.00 62.77  ? 203 ASP   C N    1 
ATOM   5175 C  CA   . ASP   C 1 203 ? -2.836  -16.222 30.179  1.00 68.52  ? 203 ASP   C CA   1 
ATOM   5176 C  C    . ASP   C 1 203 ? -2.030  -14.911 30.272  1.00 69.11  ? 203 ASP   C C    1 
ATOM   5177 O  O    . ASP   C 1 203 ? -2.634  -13.822 30.315  1.00 63.73  ? 203 ASP   C O    1 
ATOM   5178 C  CB   . ASP   C 1 203 ? -2.909  -16.696 28.714  1.00 68.31  ? 203 ASP   C CB   1 
ATOM   5179 C  CG   . ASP   C 1 203 ? -3.750  -17.935 28.405  1.00 69.62  ? 203 ASP   C CG   1 
ATOM   5180 O  OD1  . ASP   C 1 203 ? -3.678  -18.915 29.183  1.00 72.76  ? 203 ASP   C OD1  1 
ATOM   5181 O  OD2  . ASP   C 1 203 ? -4.457  -17.925 27.357  1.00 60.53  ? 203 ASP   C OD2  1 
ATOM   5182 N  N    . SER   C 1 204 ? -0.701  -15.018 30.315  1.00 73.03  ? 204 SER   C N    1 
ATOM   5183 C  CA   . SER   C 1 204 ? 0.261   -13.913 30.054  1.00 68.12  ? 204 SER   C CA   1 
ATOM   5184 C  C    . SER   C 1 204 ? 0.588   -13.900 28.554  1.00 61.02  ? 204 SER   C C    1 
ATOM   5185 O  O    . SER   C 1 204 ? 1.449   -13.100 28.144  1.00 57.18  ? 204 SER   C O    1 
ATOM   5186 C  CB   . SER   C 1 204 ? 1.512   -14.044 30.915  1.00 71.36  ? 204 SER   C CB   1 
ATOM   5187 O  OG   . SER   C 1 204 ? 2.182   -15.285 30.688  1.00 64.29  ? 204 SER   C OG   1 
ATOM   5188 N  N    . HIS   C 1 205 ? -0.039  -14.803 27.785  1.00 59.49  ? 205 HIS   C N    1 
ATOM   5189 C  CA   . HIS   C 1 205 ? -0.091  -14.807 26.294  1.00 56.19  ? 205 HIS   C CA   1 
ATOM   5190 C  C    . HIS   C 1 205 ? -1.562  -14.798 25.848  1.00 46.57  ? 205 HIS   C C    1 
ATOM   5191 O  O    . HIS   C 1 205 ? -2.183  -15.841 25.656  1.00 43.53  ? 205 HIS   C O    1 
ATOM   5192 C  CB   . HIS   C 1 205 ? 0.749   -15.977 25.740  1.00 60.74  ? 205 HIS   C CB   1 
ATOM   5193 C  CG   . HIS   C 1 205 ? 2.175   -15.640 25.412  1.00 69.20  ? 205 HIS   C CG   1 
ATOM   5194 N  ND1  . HIS   C 1 205 ? 2.986   -16.491 24.661  1.00 71.35  ? 205 HIS   C ND1  1 
ATOM   5195 C  CD2  . HIS   C 1 205 ? 2.939   -14.559 25.702  1.00 71.21  ? 205 HIS   C CD2  1 
ATOM   5196 C  CE1  . HIS   C 1 205 ? 4.182   -15.954 24.520  1.00 71.12  ? 205 HIS   C CE1  1 
ATOM   5197 N  NE2  . HIS   C 1 205 ? 4.177   -14.766 25.146  1.00 73.86  ? 205 HIS   C NE2  1 
ATOM   5198 N  N    . PRO   C 1 206 ? -2.216  -13.616 25.758  1.00 36.39  ? 206 PRO   C N    1 
ATOM   5199 C  CA   . PRO   C 1 206 ? -3.524  -13.520 25.106  1.00 30.18  ? 206 PRO   C CA   1 
ATOM   5200 C  C    . PRO   C 1 206 ? -3.474  -13.732 23.587  1.00 25.95  ? 206 PRO   C C    1 
ATOM   5201 O  O    . PRO   C 1 206 ? -2.434  -13.568 22.994  1.00 25.71  ? 206 PRO   C O    1 
ATOM   5202 C  CB   . PRO   C 1 206 ? -3.986  -12.094 25.414  1.00 32.41  ? 206 PRO   C CB   1 
ATOM   5203 C  CG   . PRO   C 1 206 ? -2.720  -11.338 25.775  1.00 33.29  ? 206 PRO   C CG   1 
ATOM   5204 C  CD   . PRO   C 1 206 ? -1.774  -12.354 26.368  1.00 31.47  ? 206 PRO   C CD   1 
ATOM   5205 N  N    . ALA   C 1 207 ? -4.608  -14.101 22.989  1.00 23.84  ? 207 ALA   C N    1 
ATOM   5206 C  CA   . ALA   C 1 207 ? -4.763  -14.323 21.530  1.00 21.91  ? 207 ALA   C CA   1 
ATOM   5207 C  C    . ALA   C 1 207 ? -6.248  -14.390 21.187  1.00 20.91  ? 207 ALA   C C    1 
ATOM   5208 O  O    . ALA   C 1 207 ? -7.029  -14.702 22.064  1.00 22.56  ? 207 ALA   C O    1 
ATOM   5209 C  CB   . ALA   C 1 207 ? -4.049  -15.594 21.140  1.00 21.61  ? 207 ALA   C CB   1 
ATOM   5210 N  N    . ASP   C 1 208 ? -6.650  -14.116 19.937  1.00 20.12  ? 208 ASP   C N    1 
ATOM   5211 C  CA   . ASP   C 1 208 ? -5.771  -13.734 18.843  1.00 20.04  ? 208 ASP   C CA   1 
ATOM   5212 C  C    . ASP   C 1 208 ? -5.961  -12.257 18.439  1.00 21.09  ? 208 ASP   C C    1 
ATOM   5213 O  O    . ASP   C 1 208 ? -5.024  -11.672 17.824  1.00 20.69  ? 208 ASP   C O    1 
ATOM   5214 C  CB   . ASP   C 1 208 ? -5.983  -14.666 17.661  1.00 19.61  ? 208 ASP   C CB   1 
ATOM   5215 C  CG   . ASP   C 1 208 ? -5.121  -15.911 17.707  1.00 20.45  ? 208 ASP   C CG   1 
ATOM   5216 O  OD1  . ASP   C 1 208 ? -5.538  -16.870 18.374  1.00 20.71  ? 208 ASP   C OD1  1 
ATOM   5217 O  OD2  . ASP   C 1 208 ? -4.064  -15.925 17.030  1.00 19.34  ? 208 ASP   C OD2  1 
ATOM   5218 N  N    . GLY   C 1 209 ? -7.109  -11.646 18.740  1.00 20.64  ? 209 GLY   C N    1 
ATOM   5219 C  CA   . GLY   C 1 209 ? -7.299  -10.210 18.479  1.00 20.13  ? 209 GLY   C CA   1 
ATOM   5220 C  C    . GLY   C 1 209 ? -8.698  -9.859  18.024  1.00 18.74  ? 209 GLY   C C    1 
ATOM   5221 O  O    . GLY   C 1 209 ? -9.537  -10.747 17.936  1.00 20.95  ? 209 GLY   C O    1 
ATOM   5222 N  N    . ILE   C 1 210 ? -8.911  -8.572  17.773  1.00 18.36  ? 210 ILE   C N    1 
ATOM   5223 C  CA   . ILE   C 1 210 ? -10.157 -7.981  17.206  1.00 17.41  ? 210 ILE   C CA   1 
ATOM   5224 C  C    . ILE   C 1 210 ? -9.787  -7.319  15.868  1.00 16.60  ? 210 ILE   C C    1 
ATOM   5225 O  O    . ILE   C 1 210 ? -8.655  -6.825  15.773  1.00 15.48  ? 210 ILE   C O    1 
ATOM   5226 C  CB   . ILE   C 1 210 ? -10.729 -6.984  18.221  1.00 16.82  ? 210 ILE   C CB   1 
ATOM   5227 C  CG1  . ILE   C 1 210 ? -11.017 -7.694  19.545  1.00 17.34  ? 210 ILE   C CG1  1 
ATOM   5228 C  CG2  . ILE   C 1 210 ? -11.948 -6.278  17.659  1.00 17.66  ? 210 ILE   C CG2  1 
ATOM   5229 C  CD1  . ILE   C 1 210 ? -11.630 -6.828  20.603  1.00 17.99  ? 210 ILE   C CD1  1 
ATOM   5230 N  N    . ALA   C 1 211 ? -10.691 -7.310  14.886  1.00 14.86  ? 211 ALA   C N    1 
ATOM   5231 C  CA   . ALA   C 1 211 ? -10.559 -6.539  13.630  1.00 14.27  ? 211 ALA   C CA   1 
ATOM   5232 C  C    . ALA   C 1 211 ? -11.861 -5.796  13.334  1.00 14.72  ? 211 ALA   C C    1 
ATOM   5233 O  O    . ALA   C 1 211 ? -12.939 -6.401  13.520  1.00 15.12  ? 211 ALA   C O    1 
ATOM   5234 C  CB   . ALA   C 1 211 ? -10.203 -7.431  12.474  1.00 13.44  ? 211 ALA   C CB   1 
ATOM   5235 N  N    . PHE   C 1 212 ? -11.747 -4.553  12.857  1.00 14.29  ? 212 PHE   C N    1 
ATOM   5236 C  CA   . PHE   C 1 212 ? -12.800 -3.843  12.090  1.00 14.94  ? 212 PHE   C CA   1 
ATOM   5237 C  C    . PHE   C 1 212 ? -12.599 -4.182  10.621  1.00 15.00  ? 212 PHE   C C    1 
ATOM   5238 O  O    . PHE   C 1 212 ? -11.464 -4.098  10.191  1.00 15.29  ? 212 PHE   C O    1 
ATOM   5239 C  CB   . PHE   C 1 212 ? -12.743 -2.324  12.252  1.00 14.80  ? 212 PHE   C CB   1 
ATOM   5240 C  CG   . PHE   C 1 212 ? -13.668 -1.584  11.320  1.00 14.36  ? 212 PHE   C CG   1 
ATOM   5241 C  CD1  . PHE   C 1 212 ? -15.019 -1.489  11.586  1.00 15.13  ? 212 PHE   C CD1  1 
ATOM   5242 C  CD2  . PHE   C 1 212 ? -13.189 -1.007  10.164  1.00 15.08  ? 212 PHE   C CD2  1 
ATOM   5243 C  CE1  . PHE   C 1 212 ? -15.863 -0.811  10.721  1.00 16.14  ? 212 PHE   C CE1  1 
ATOM   5244 C  CE2  . PHE   C 1 212 ? -14.030 -0.334  9.294   1.00 16.10  ? 212 PHE   C CE2  1 
ATOM   5245 C  CZ   . PHE   C 1 212 ? -15.367 -0.223  9.580   1.00 15.90  ? 212 PHE   C CZ   1 
ATOM   5246 N  N    . PHE   C 1 213 ? -13.656 -4.537  9.892   1.00 15.36  ? 213 PHE   C N    1 
ATOM   5247 C  CA   . PHE   C 1 213 ? -13.511 -5.026  8.507   1.00 16.33  ? 213 PHE   C CA   1 
ATOM   5248 C  C    . PHE   C 1 213 ? -14.668 -4.569  7.621   1.00 17.05  ? 213 PHE   C C    1 
ATOM   5249 O  O    . PHE   C 1 213 ? -15.769 -4.200  8.093   1.00 16.24  ? 213 PHE   C O    1 
ATOM   5250 C  CB   . PHE   C 1 213 ? -13.340 -6.541  8.513   1.00 17.45  ? 213 PHE   C CB   1 
ATOM   5251 C  CG   . PHE   C 1 213 ? -14.612 -7.329  8.650   1.00 19.00  ? 213 PHE   C CG   1 
ATOM   5252 C  CD1  . PHE   C 1 213 ? -15.131 -7.626  9.897   1.00 19.92  ? 213 PHE   C CD1  1 
ATOM   5253 C  CD2  . PHE   C 1 213 ? -15.267 -7.799  7.527   1.00 19.84  ? 213 PHE   C CD2  1 
ATOM   5254 C  CE1  . PHE   C 1 213 ? -16.310 -8.340  10.016  1.00 21.58  ? 213 PHE   C CE1  1 
ATOM   5255 C  CE2  . PHE   C 1 213 ? -16.438 -8.527  7.649   1.00 21.97  ? 213 PHE   C CE2  1 
ATOM   5256 C  CZ   . PHE   C 1 213 ? -16.954 -8.804  8.890   1.00 21.83  ? 213 PHE   C CZ   1 
ATOM   5257 N  N    . ILE   C 1 214 ? -14.367 -4.584  6.328   1.00 17.69  ? 214 ILE   C N    1 
ATOM   5258 C  CA   . ILE   C 1 214 ? -15.290 -4.294  5.203   1.00 18.98  ? 214 ILE   C CA   1 
ATOM   5259 C  C    . ILE   C 1 214 ? -15.158 -5.448  4.210   1.00 18.57  ? 214 ILE   C C    1 
ATOM   5260 O  O    . ILE   C 1 214 ? -14.035 -5.849  3.942   1.00 18.79  ? 214 ILE   C O    1 
ATOM   5261 C  CB   . ILE   C 1 214 ? -14.903 -2.950  4.569   1.00 21.65  ? 214 ILE   C CB   1 
ATOM   5262 C  CG1  . ILE   C 1 214 ? -14.529 -1.923  5.644   1.00 23.28  ? 214 ILE   C CG1  1 
ATOM   5263 C  CG2  . ILE   C 1 214 ? -15.996 -2.438  3.631   1.00 21.46  ? 214 ILE   C CG2  1 
ATOM   5264 C  CD1  . ILE   C 1 214 ? -13.977 -0.648  5.082   1.00 23.49  ? 214 ILE   C CD1  1 
ATOM   5265 N  N    . SER   C 1 215 ? -16.263 -5.938  3.669   1.00 19.26  ? 215 SER   C N    1 
ATOM   5266 C  CA   . SER   C 1 215 ? -16.302 -7.132  2.790   1.00 21.47  ? 215 SER   C CA   1 
ATOM   5267 C  C    . SER   C 1 215 ? -17.545 -7.111  1.911   1.00 20.62  ? 215 SER   C C    1 
ATOM   5268 O  O    . SER   C 1 215 ? -18.481 -6.365  2.215   1.00 18.56  ? 215 SER   C O    1 
ATOM   5269 C  CB   . SER   C 1 215 ? -16.334 -8.367  3.612   1.00 24.94  ? 215 SER   C CB   1 
ATOM   5270 O  OG   . SER   C 1 215 ? -17.576 -8.411  4.313   1.00 29.65  ? 215 SER   C OG   1 
ATOM   5271 N  N    . ASN   C 1 216 ? -17.559 -7.961  0.893   1.00 22.47  ? 216 ASN   C N    1 
ATOM   5272 C  CA   . ASN   C 1 216 ? -18.771 -8.263  0.081   1.00 23.99  ? 216 ASN   C CA   1 
ATOM   5273 C  C    . ASN   C 1 216 ? -19.941 -8.470  1.045   1.00 22.68  ? 216 ASN   C C    1 
ATOM   5274 O  O    . ASN   C 1 216 ? -19.700 -8.896  2.208   1.00 20.94  ? 216 ASN   C O    1 
ATOM   5275 C  CB   . ASN   C 1 216 ? -18.541 -9.442  -0.867  1.00 28.72  ? 216 ASN   C CB   1 
ATOM   5276 C  CG   . ASN   C 1 216 ? -17.823 -10.593 -0.191  1.00 33.12  ? 216 ASN   C CG   1 
ATOM   5277 O  OD1  . ASN   C 1 216 ? -16.767 -10.400 0.420   1.00 35.22  ? 216 ASN   C OD1  1 
ATOM   5278 N  ND2  . ASN   C 1 216 ? -18.373 -11.793 -0.307  1.00 40.24  ? 216 ASN   C ND2  1 
ATOM   5279 N  N    . ILE   C 1 217 ? -21.152 -8.121  0.593   1.00 20.90  ? 217 ILE   C N    1 
ATOM   5280 C  CA   . ILE   C 1 217 ? -22.372 -8.048  1.444   1.00 20.86  ? 217 ILE   C CA   1 
ATOM   5281 C  C    . ILE   C 1 217 ? -22.691 -9.446  1.984   1.00 20.13  ? 217 ILE   C C    1 
ATOM   5282 O  O    . ILE   C 1 217 ? -23.242 -9.515  3.085   1.00 20.72  ? 217 ILE   C O    1 
ATOM   5283 C  CB   . ILE   C 1 217 ? -23.588 -7.389  0.723   1.00 21.78  ? 217 ILE   C CB   1 
ATOM   5284 C  CG1  . ILE   C 1 217 ? -24.151 -8.233  -0.418  1.00 23.69  ? 217 ILE   C CG1  1 
ATOM   5285 C  CG2  . ILE   C 1 217 ? -23.273 -5.988  0.220   1.00 21.63  ? 217 ILE   C CG2  1 
ATOM   5286 C  CD1  . ILE   C 1 217 ? -25.360 -7.611  -1.107  1.00 24.57  ? 217 ILE   C CD1  1 
ATOM   5287 N  N    . ASP   C 1 218 ? -22.360 -10.514 1.260   1.00 22.11  ? 218 ASP   C N    1 
ATOM   5288 C  CA   . ASP   C 1 218 ? -22.734 -11.919 1.613   1.00 23.57  ? 218 ASP   C CA   1 
ATOM   5289 C  C    . ASP   C 1 218 ? -21.578 -12.611 2.354   1.00 24.34  ? 218 ASP   C C    1 
ATOM   5290 O  O    . ASP   C 1 218 ? -21.639 -13.839 2.532   1.00 25.52  ? 218 ASP   C O    1 
ATOM   5291 C  CB   . ASP   C 1 218 ? -23.141 -12.715 0.368   1.00 25.51  ? 218 ASP   C CB   1 
ATOM   5292 C  CG   . ASP   C 1 218 ? -22.121 -12.697 -0.779  1.00 31.39  ? 218 ASP   C CG   1 
ATOM   5293 O  OD1  . ASP   C 1 218 ? -21.327 -11.709 -0.894  1.00 33.91  ? 218 ASP   C OD1  1 
ATOM   5294 O  OD2  . ASP   C 1 218 ? -22.126 -13.660 -1.580  1.00 33.02  ? 218 ASP   C OD2  1 
ATOM   5295 N  N    . SER   C 1 219 ? -20.583 -11.865 2.833   1.00 22.05  ? 219 SER   C N    1 
ATOM   5296 C  CA   . SER   C 1 219 ? -19.420 -12.432 3.552   1.00 21.68  ? 219 SER   C CA   1 
ATOM   5297 C  C    . SER   C 1 219 ? -19.893 -13.300 4.722   1.00 21.34  ? 219 SER   C C    1 
ATOM   5298 O  O    . SER   C 1 219 ? -20.678 -12.830 5.526   1.00 20.70  ? 219 SER   C O    1 
ATOM   5299 C  CB   . SER   C 1 219 ? -18.495 -11.345 4.026   1.00 21.58  ? 219 SER   C CB   1 
ATOM   5300 O  OG   . SER   C 1 219 ? -17.416 -11.887 4.764   1.00 21.71  ? 219 SER   C OG   1 
ATOM   5301 N  N    . SER   C 1 220 ? -19.366 -14.518 4.839   1.00 23.52  ? 220 SER   C N    1 
ATOM   5302 C  CA   . SER   C 1 220 ? -19.504 -15.371 6.050   1.00 24.01  ? 220 SER   C CA   1 
ATOM   5303 C  C    . SER   C 1 220 ? -18.113 -15.747 6.597   1.00 21.54  ? 220 SER   C C    1 
ATOM   5304 O  O    . SER   C 1 220 ? -17.099 -15.574 5.873   1.00 20.41  ? 220 SER   C O    1 
ATOM   5305 C  CB   . SER   C 1 220 ? -20.395 -16.558 5.748   1.00 27.29  ? 220 SER   C CB   1 
ATOM   5306 O  OG   . SER   C 1 220 ? -19.653 -17.629 5.195   1.00 31.11  ? 220 SER   C OG   1 
ATOM   5307 N  N    . ILE   C 1 221 ? -18.042 -16.205 7.844   1.00 20.06  ? 221 ILE   C N    1 
ATOM   5308 C  CA   . ILE   C 1 221 ? -16.763 -16.643 8.460   1.00 20.57  ? 221 ILE   C CA   1 
ATOM   5309 C  C    . ILE   C 1 221 ? -16.136 -17.724 7.584   1.00 20.50  ? 221 ILE   C C    1 
ATOM   5310 O  O    . ILE   C 1 221 ? -16.701 -18.797 7.445   1.00 18.90  ? 221 ILE   C O    1 
ATOM   5311 C  CB   . ILE   C 1 221 ? -16.960 -17.129 9.907   1.00 21.69  ? 221 ILE   C CB   1 
ATOM   5312 C  CG1  . ILE   C 1 221 ? -17.316 -15.978 10.852  1.00 21.96  ? 221 ILE   C CG1  1 
ATOM   5313 C  CG2  . ILE   C 1 221 ? -15.704 -17.852 10.374  1.00 21.92  ? 221 ILE   C CG2  1 
ATOM   5314 C  CD1  . ILE   C 1 221 ? -17.949 -16.439 12.145  1.00 22.60  ? 221 ILE   C CD1  1 
ATOM   5315 N  N    . PRO   C 1 222 ? -14.932 -17.507 6.996   1.00 22.11  ? 222 PRO   C N    1 
ATOM   5316 C  CA   . PRO   C 1 222 ? -14.294 -18.525 6.158   1.00 21.71  ? 222 PRO   C CA   1 
ATOM   5317 C  C    . PRO   C 1 222 ? -13.942 -19.783 6.966   1.00 23.23  ? 222 PRO   C C    1 
ATOM   5318 O  O    . PRO   C 1 222 ? -13.593 -19.637 8.105   1.00 22.43  ? 222 PRO   C O    1 
ATOM   5319 C  CB   . PRO   C 1 222 ? -12.985 -17.878 5.687   1.00 21.43  ? 222 PRO   C CB   1 
ATOM   5320 C  CG   . PRO   C 1 222 ? -13.186 -16.395 5.939   1.00 21.05  ? 222 PRO   C CG   1 
ATOM   5321 C  CD   . PRO   C 1 222 ? -14.098 -16.305 7.142   1.00 20.61  ? 222 PRO   C CD   1 
ATOM   5322 N  N    . SER   C 1 223 ? -14.037 -20.974 6.371   1.00 25.07  ? 223 SER   C N    1 
ATOM   5323 C  CA   . SER   C 1 223 ? -13.721 -22.246 7.065   1.00 26.54  ? 223 SER   C CA   1 
ATOM   5324 C  C    . SER   C 1 223 ? -12.275 -22.223 7.569   1.00 26.13  ? 223 SER   C C    1 
ATOM   5325 O  O    . SER   C 1 223 ? -11.388 -21.825 6.804   1.00 27.65  ? 223 SER   C O    1 
ATOM   5326 C  CB   . SER   C 1 223 ? -13.957 -23.437 6.185   1.00 30.46  ? 223 SER   C CB   1 
ATOM   5327 O  OG   . SER   C 1 223 ? -14.020 -24.614 6.987   1.00 34.50  ? 223 SER   C OG   1 
ATOM   5328 N  N    . GLY   C 1 224 ? -12.067 -22.617 8.826   1.00 27.65  ? 224 GLY   C N    1 
ATOM   5329 C  CA   . GLY   C 1 224 ? -10.746 -22.785 9.464   1.00 26.52  ? 224 GLY   C CA   1 
ATOM   5330 C  C    . GLY   C 1 224 ? -10.069 -21.454 9.732   1.00 27.06  ? 224 GLY   C C    1 
ATOM   5331 O  O    . GLY   C 1 224 ? -8.835  -21.407 9.713   1.00 27.85  ? 224 GLY   C O    1 
ATOM   5332 N  N    . SER   C 1 225 ? -10.837 -20.389 9.973   1.00 26.52  ? 225 SER   C N    1 
ATOM   5333 C  CA   . SER   C 1 225 ? -10.300 -19.016 10.189  1.00 23.43  ? 225 SER   C CA   1 
ATOM   5334 C  C    . SER   C 1 225 ? -10.325 -18.658 11.682  1.00 21.77  ? 225 SER   C C    1 
ATOM   5335 O  O    . SER   C 1 225 ? -10.377 -17.454 11.988  1.00 24.75  ? 225 SER   C O    1 
ATOM   5336 C  CB   . SER   C 1 225 ? -11.058 -18.000 9.347   1.00 23.20  ? 225 SER   C CB   1 
ATOM   5337 O  OG   . SER   C 1 225 ? -12.368 -17.792 9.856   1.00 21.98  ? 225 SER   C OG   1 
ATOM   5338 N  N    . THR   C 1 226 ? -10.314 -19.639 12.593  1.00 20.45  ? 226 THR   C N    1 
ATOM   5339 C  CA   . THR   C 1 226 ? -10.023 -19.393 14.035  1.00 20.38  ? 226 THR   C CA   1 
ATOM   5340 C  C    . THR   C 1 226 ? -8.538  -19.029 14.190  1.00 19.31  ? 226 THR   C C    1 
ATOM   5341 O  O    . THR   C 1 226 ? -7.768  -19.131 13.216  1.00 19.66  ? 226 THR   C O    1 
ATOM   5342 C  CB   . THR   C 1 226 ? -10.397 -20.569 14.952  1.00 21.18  ? 226 THR   C CB   1 
ATOM   5343 O  OG1  . THR   C 1 226 ? -9.683  -21.733 14.535  1.00 22.91  ? 226 THR   C OG1  1 
ATOM   5344 C  CG2  . THR   C 1 226 ? -11.875 -20.866 14.953  1.00 21.31  ? 226 THR   C CG2  1 
ATOM   5345 N  N    . GLY   C 1 227 ? -8.158  -18.549 15.370  1.00 19.08  ? 227 GLY   C N    1 
ATOM   5346 C  CA   . GLY   C 1 227 ? -6.764  -18.206 15.707  1.00 19.09  ? 227 GLY   C CA   1 
ATOM   5347 C  C    . GLY   C 1 227 ? -6.237  -17.041 14.897  1.00 18.02  ? 227 GLY   C C    1 
ATOM   5348 O  O    . GLY   C 1 227 ? -6.874  -16.001 14.859  1.00 17.05  ? 227 GLY   C O    1 
ATOM   5349 N  N    . ARG   C 1 228 ? -5.111  -17.239 14.235  1.00 18.91  ? 228 ARG   C N    1 
ATOM   5350 C  CA   . ARG   C 1 228 ? -4.303  -16.154 13.623  1.00 19.34  ? 228 ARG   C CA   1 
ATOM   5351 C  C    . ARG   C 1 228 ? -5.034  -15.523 12.426  1.00 19.72  ? 228 ARG   C C    1 
ATOM   5352 O  O    . ARG   C 1 228 ? -4.547  -14.474 11.959  1.00 18.14  ? 228 ARG   C O    1 
ATOM   5353 C  CB   . ARG   C 1 228 ? -2.933  -16.703 13.206  1.00 18.88  ? 228 ARG   C CB   1 
ATOM   5354 C  CG   . ARG   C 1 228 ? -3.013  -17.766 12.128  1.00 19.92  ? 228 ARG   C CG   1 
ATOM   5355 C  CD   . ARG   C 1 228 ? -1.757  -18.589 12.105  1.00 20.80  ? 228 ARG   C CD   1 
ATOM   5356 N  NE   . ARG   C 1 228 ? -1.686  -19.399 10.892  1.00 22.64  ? 228 ARG   C NE   1 
ATOM   5357 C  CZ   . ARG   C 1 228 ? -0.595  -20.027 10.443  1.00 21.96  ? 228 ARG   C CZ   1 
ATOM   5358 N  NH1  . ARG   C 1 228 ? 0.544   -19.988 11.114  1.00 23.06  ? 228 ARG   C NH1  1 
ATOM   5359 N  NH2  . ARG   C 1 228 ? -0.659  -20.708 9.321   1.00 22.46  ? 228 ARG   C NH2  1 
ATOM   5360 N  N    . LEU   C 1 229 ? -6.094  -16.148 11.897  1.00 20.06  ? 229 LEU   C N    1 
ATOM   5361 C  CA   . LEU   C 1 229 ? -6.792  -15.639 10.682  1.00 19.99  ? 229 LEU   C CA   1 
ATOM   5362 C  C    . LEU   C 1 229 ? -7.938  -14.703 11.101  1.00 19.19  ? 229 LEU   C C    1 
ATOM   5363 O  O    . LEU   C 1 229 ? -8.564  -14.108 10.204  1.00 18.29  ? 229 LEU   C O    1 
ATOM   5364 C  CB   . LEU   C 1 229 ? -7.275  -16.802 9.808   1.00 20.85  ? 229 LEU   C CB   1 
ATOM   5365 C  CG   . LEU   C 1 229 ? -6.177  -17.737 9.294   1.00 21.41  ? 229 LEU   C CG   1 
ATOM   5366 C  CD1  . LEU   C 1 229 ? -6.744  -18.782 8.360   1.00 22.30  ? 229 LEU   C CD1  1 
ATOM   5367 C  CD2  . LEU   C 1 229 ? -5.064  -16.971 8.599   1.00 22.90  ? 229 LEU   C CD2  1 
ATOM   5368 N  N    . LEU   C 1 230 ? -8.209  -14.586 12.403  1.00 17.98  ? 230 LEU   C N    1 
ATOM   5369 C  CA   . LEU   C 1 230 ? -9.054  -13.514 12.989  1.00 19.20  ? 230 LEU   C CA   1 
ATOM   5370 C  C    . LEU   C 1 230 ? -10.502 -13.548 12.460  1.00 21.19  ? 230 LEU   C C    1 
ATOM   5371 O  O    . LEU   C 1 230 ? -11.182 -12.509 12.542  1.00 19.77  ? 230 LEU   C O    1 
ATOM   5372 C  CB   . LEU   C 1 230 ? -8.366  -12.194 12.636  1.00 20.31  ? 230 LEU   C CB   1 
ATOM   5373 C  CG   . LEU   C 1 230 ? -7.027  -11.969 13.340  1.00 21.14  ? 230 LEU   C CG   1 
ATOM   5374 C  CD1  . LEU   C 1 230 ? -6.307  -10.778 12.752  1.00 22.48  ? 230 LEU   C CD1  1 
ATOM   5375 C  CD2  . LEU   C 1 230 ? -7.246  -11.761 14.827  1.00 21.01  ? 230 LEU   C CD2  1 
ATOM   5376 N  N    . GLY   C 1 231 ? -10.973 -14.696 11.953  1.00 20.38  ? 231 GLY   C N    1 
ATOM   5377 C  CA   . GLY   C 1 231 ? -12.320 -14.845 11.386  1.00 20.65  ? 231 GLY   C CA   1 
ATOM   5378 C  C    . GLY   C 1 231 ? -12.464 -14.196 10.017  1.00 20.51  ? 231 GLY   C C    1 
ATOM   5379 O  O    . GLY   C 1 231 ? -13.590 -14.153 9.511   1.00 21.03  ? 231 GLY   C O    1 
ATOM   5380 N  N    . LEU   C 1 232 ? -11.363 -13.779 9.399   1.00 21.09  ? 232 LEU   C N    1 
ATOM   5381 C  CA   . LEU   C 1 232 ? -11.380 -12.890 8.211   1.00 21.59  ? 232 LEU   C CA   1 
ATOM   5382 C  C    . LEU   C 1 232 ? -10.901 -13.606 6.953   1.00 22.36  ? 232 LEU   C C    1 
ATOM   5383 O  O    . LEU   C 1 232 ? -11.402 -13.232 5.898   1.00 23.65  ? 232 LEU   C O    1 
ATOM   5384 C  CB   . LEU   C 1 232 ? -10.462 -11.695 8.454   1.00 20.81  ? 232 LEU   C CB   1 
ATOM   5385 C  CG   . LEU   C 1 232 ? -10.961 -10.689 9.476   1.00 21.73  ? 232 LEU   C CG   1 
ATOM   5386 C  CD1  . LEU   C 1 232 ? -9.986  -9.549  9.534   1.00 22.21  ? 232 LEU   C CD1  1 
ATOM   5387 C  CD2  . LEU   C 1 232 ? -12.365 -10.194 9.150   1.00 22.72  ? 232 LEU   C CD2  1 
ATOM   5388 N  N    . PHE   C 1 233 ? -9.883  -14.467 7.033   1.00 21.25  ? 233 PHE   C N    1 
ATOM   5389 C  CA   . PHE   C 1 233 ? -9.184  -14.993 5.832   1.00 22.11  ? 233 PHE   C CA   1 
ATOM   5390 C  C    . PHE   C 1 233 ? -9.256  -16.520 5.814   1.00 22.42  ? 233 PHE   C C    1 
ATOM   5391 O  O    . PHE   C 1 233 ? -9.267  -17.151 6.874   1.00 20.95  ? 233 PHE   C O    1 
ATOM   5392 C  CB   . PHE   C 1 233 ? -7.743  -14.483 5.787   1.00 22.04  ? 233 PHE   C CB   1 
ATOM   5393 C  CG   . PHE   C 1 233 ? -7.651  -12.982 5.724   1.00 22.48  ? 233 PHE   C CG   1 
ATOM   5394 C  CD1  . PHE   C 1 233 ? -7.942  -12.306 4.552   1.00 22.61  ? 233 PHE   C CD1  1 
ATOM   5395 C  CD2  . PHE   C 1 233 ? -7.333  -12.246 6.855   1.00 23.41  ? 233 PHE   C CD2  1 
ATOM   5396 C  CE1  . PHE   C 1 233 ? -7.917  -10.920 4.521   1.00 23.57  ? 233 PHE   C CE1  1 
ATOM   5397 C  CE2  . PHE   C 1 233 ? -7.298  -10.863 6.818   1.00 22.21  ? 233 PHE   C CE2  1 
ATOM   5398 C  CZ   . PHE   C 1 233 ? -7.598  -10.207 5.655   1.00 22.15  ? 233 PHE   C CZ   1 
ATOM   5399 N  N    . PRO   C 1 234 ? -9.351  -17.141 4.611   1.00 23.35  ? 234 PRO   C N    1 
ATOM   5400 C  CA   . PRO   C 1 234 ? -9.327  -18.601 4.481   1.00 25.16  ? 234 PRO   C CA   1 
ATOM   5401 C  C    . PRO   C 1 234 ? -7.927  -19.230 4.564   1.00 28.23  ? 234 PRO   C C    1 
ATOM   5402 O  O    . PRO   C 1 234 ? -7.844  -20.408 4.790   1.00 31.28  ? 234 PRO   C O    1 
ATOM   5403 C  CB   . PRO   C 1 234 ? -9.886  -18.825 3.073   1.00 24.23  ? 234 PRO   C CB   1 
ATOM   5404 C  CG   . PRO   C 1 234 ? -9.483  -17.583 2.302   1.00 23.84  ? 234 PRO   C CG   1 
ATOM   5405 C  CD   . PRO   C 1 234 ? -9.545  -16.460 3.314   1.00 23.09  ? 234 PRO   C CD   1 
ATOM   5406 N  N    . ASP   C 1 235 ? -6.872  -18.439 4.369   1.00 28.50  ? 235 ASP   C N    1 
ATOM   5407 C  CA   . ASP   C 1 235 ? -5.457  -18.903 4.359   1.00 28.75  ? 235 ASP   C CA   1 
ATOM   5408 C  C    . ASP   C 1 235 ? -4.549  -17.763 4.833   1.00 27.86  ? 235 ASP   C C    1 
ATOM   5409 O  O    . ASP   C 1 235 ? -4.981  -16.585 4.820   1.00 24.76  ? 235 ASP   C O    1 
ATOM   5410 C  CB   . ASP   C 1 235 ? -5.044  -19.394 2.968   1.00 30.20  ? 235 ASP   C CB   1 
ATOM   5411 C  CG   . ASP   C 1 235 ? -5.264  -18.378 1.851   1.00 33.36  ? 235 ASP   C CG   1 
ATOM   5412 O  OD1  . ASP   C 1 235 ? -4.530  -17.365 1.809   1.00 35.13  ? 235 ASP   C OD1  1 
ATOM   5413 O  OD2  . ASP   C 1 235 ? -6.191  -18.587 1.037   1.00 34.95  ? 235 ASP   C OD2  1 
ATOM   5414 N  N    . ALA   C 1 236 ? -3.330  -18.112 5.242   1.00 29.19  ? 236 ALA   C N    1 
ATOM   5415 C  CA   . ALA   C 1 236 ? -2.319  -17.190 5.805   1.00 33.03  ? 236 ALA   C CA   1 
ATOM   5416 C  C    . ALA   C 1 236 ? -1.465  -16.557 4.703   1.00 29.57  ? 236 ALA   C C    1 
ATOM   5417 O  O    . ALA   C 1 236 ? -0.442  -15.981 5.034   1.00 34.49  ? 236 ALA   C O    1 
ATOM   5418 C  CB   . ALA   C 1 236 ? -1.453  -17.931 6.807   1.00 34.77  ? 236 ALA   C CB   1 
ATOM   5419 N  N    . ASN   C 1 237 ? -1.840  -16.663 3.439   1.00 30.56  ? 237 ASN   C N    1 
ATOM   5420 C  CA   . ASN   C 1 237 ? -0.998  -16.126 2.335   1.00 36.45  ? 237 ASN   C CA   1 
ATOM   5421 C  C    . ASN   C 1 237 ? -1.424  -14.678 2.056   1.00 38.94  ? 237 ASN   C C    1 
ATOM   5422 O  O    . ASN   C 1 237 ? -2.569  -14.269 2.233   1.00 40.06  ? 237 ASN   C O    1 
ATOM   5423 C  CB   . ASN   C 1 237 ? -1.023  -17.037 1.105   1.00 36.73  ? 237 ASN   C CB   1 
ATOM   5424 C  CG   . ASN   C 1 237 ? -0.824  -18.490 1.484   1.00 36.73  ? 237 ASN   C CG   1 
ATOM   5425 O  OD1  . ASN   C 1 237 ? -1.740  -19.300 1.332   1.00 38.04  ? 237 ASN   C OD1  1 
ATOM   5426 N  ND2  . ASN   C 1 237 ? 0.331   -18.806 2.049   1.00 30.84  ? 237 ASN   C ND2  1 
ATOM   5427 O  OXT  . ASN   C 1 237 ? -0.574  -13.885 1.667   1.00 44.89  ? 237 ASN   C OXT  1 
ATOM   5428 N  N    . ALA   D 1 1   ? -16.793 -9.261  -53.108 1.00 52.55  ? 1   ALA   D N    1 
ATOM   5429 C  CA   . ALA   D 1 1   ? -17.545 -10.328 -52.357 1.00 53.15  ? 1   ALA   D CA   1 
ATOM   5430 C  C    . ALA   D 1 1   ? -16.574 -11.247 -51.596 1.00 49.24  ? 1   ALA   D C    1 
ATOM   5431 O  O    . ALA   D 1 1   ? -15.347 -11.180 -51.819 1.00 46.16  ? 1   ALA   D O    1 
ATOM   5432 C  CB   . ALA   D 1 1   ? -18.422 -11.120 -53.309 1.00 53.35  ? 1   ALA   D CB   1 
ATOM   5433 N  N    . ASP   D 1 2   ? -17.128 -12.101 -50.734 1.00 48.02  ? 2   ASP   D N    1 
ATOM   5434 C  CA   . ASP   D 1 2   ? -16.379 -13.109 -49.935 1.00 46.79  ? 2   ASP   D CA   1 
ATOM   5435 C  C    . ASP   D 1 2   ? -15.636 -14.056 -50.896 1.00 45.13  ? 2   ASP   D C    1 
ATOM   5436 O  O    . ASP   D 1 2   ? -16.097 -14.247 -52.043 1.00 47.24  ? 2   ASP   D O    1 
ATOM   5437 C  CB   . ASP   D 1 2   ? -17.307 -13.886 -48.981 1.00 45.47  ? 2   ASP   D CB   1 
ATOM   5438 C  CG   . ASP   D 1 2   ? -18.082 -13.054 -47.958 1.00 42.99  ? 2   ASP   D CG   1 
ATOM   5439 O  OD1  . ASP   D 1 2   ? -17.784 -11.852 -47.815 1.00 37.26  ? 2   ASP   D OD1  1 
ATOM   5440 O  OD2  . ASP   D 1 2   ? -18.992 -13.620 -47.307 1.00 41.48  ? 2   ASP   D OD2  1 
ATOM   5441 N  N    . THR   D 1 3   ? -14.499 -14.598 -50.461 1.00 42.25  ? 3   THR   D N    1 
ATOM   5442 C  CA   . THR   D 1 3   ? -13.858 -15.780 -51.074 1.00 42.54  ? 3   THR   D CA   1 
ATOM   5443 C  C    . THR   D 1 3   ? -14.215 -17.008 -50.227 1.00 44.45  ? 3   THR   D C    1 
ATOM   5444 O  O    . THR   D 1 3   ? -13.939 -17.006 -49.000 1.00 42.68  ? 3   THR   D O    1 
ATOM   5445 C  CB   . THR   D 1 3   ? -12.351 -15.579 -51.241 1.00 43.62  ? 3   THR   D CB   1 
ATOM   5446 O  OG1  . THR   D 1 3   ? -12.190 -14.343 -51.935 1.00 48.32  ? 3   THR   D OG1  1 
ATOM   5447 C  CG2  . THR   D 1 3   ? -11.694 -16.694 -52.026 1.00 42.26  ? 3   THR   D CG2  1 
ATOM   5448 N  N    . ILE   D 1 4   ? -14.828 -18.006 -50.868 1.00 42.06  ? 4   ILE   D N    1 
ATOM   5449 C  CA   . ILE   D 1 4   ? -15.225 -19.300 -50.249 1.00 39.49  ? 4   ILE   D CA   1 
ATOM   5450 C  C    . ILE   D 1 4   ? -14.449 -20.440 -50.916 1.00 37.01  ? 4   ILE   D C    1 
ATOM   5451 O  O    . ILE   D 1 4   ? -14.318 -20.437 -52.156 1.00 38.81  ? 4   ILE   D O    1 
ATOM   5452 C  CB   . ILE   D 1 4   ? -16.745 -19.502 -50.356 1.00 40.60  ? 4   ILE   D CB   1 
ATOM   5453 C  CG1  . ILE   D 1 4   ? -17.506 -18.366 -49.671 1.00 42.25  ? 4   ILE   D CG1  1 
ATOM   5454 C  CG2  . ILE   D 1 4   ? -17.156 -20.866 -49.820 1.00 40.89  ? 4   ILE   D CG2  1 
ATOM   5455 C  CD1  . ILE   D 1 4   ? -17.258 -18.257 -48.179 1.00 44.00  ? 4   ILE   D CD1  1 
ATOM   5456 N  N    . VAL   D 1 5   ? -13.924 -21.339 -50.080 1.00 33.43  ? 5   VAL   D N    1 
ATOM   5457 C  CA   . VAL   D 1 5   ? -13.572 -22.753 -50.386 1.00 30.87  ? 5   VAL   D CA   1 
ATOM   5458 C  C    . VAL   D 1 5   ? -14.413 -23.634 -49.449 1.00 31.02  ? 5   VAL   D C    1 
ATOM   5459 O  O    . VAL   D 1 5   ? -14.440 -23.359 -48.234 1.00 34.31  ? 5   VAL   D O    1 
ATOM   5460 C  CB   . VAL   D 1 5   ? -12.062 -22.980 -50.218 1.00 30.73  ? 5   VAL   D CB   1 
ATOM   5461 C  CG1  . VAL   D 1 5   ? -11.678 -24.432 -50.477 1.00 30.99  ? 5   VAL   D CG1  1 
ATOM   5462 C  CG2  . VAL   D 1 5   ? -11.264 -22.052 -51.113 1.00 29.37  ? 5   VAL   D CG2  1 
ATOM   5463 N  N    . ALA   D 1 6   ? -15.161 -24.595 -49.980 1.00 28.96  ? 6   ALA   D N    1 
ATOM   5464 C  CA   . ALA   D 1 6   ? -16.155 -25.350 -49.194 1.00 28.04  ? 6   ALA   D CA   1 
ATOM   5465 C  C    . ALA   D 1 6   ? -16.229 -26.796 -49.676 1.00 28.58  ? 6   ALA   D C    1 
ATOM   5466 O  O    . ALA   D 1 6   ? -16.051 -27.056 -50.881 1.00 29.62  ? 6   ALA   D O    1 
ATOM   5467 C  CB   . ALA   D 1 6   ? -17.500 -24.684 -49.278 1.00 26.74  ? 6   ALA   D CB   1 
ATOM   5468 N  N    . VAL   D 1 7   ? -16.489 -27.689 -48.734 1.00 27.71  ? 7   VAL   D N    1 
ATOM   5469 C  CA   . VAL   D 1 7   ? -16.908 -29.091 -48.989 1.00 27.64  ? 7   VAL   D CA   1 
ATOM   5470 C  C    . VAL   D 1 7   ? -18.403 -29.138 -48.665 1.00 28.41  ? 7   VAL   D C    1 
ATOM   5471 O  O    . VAL   D 1 7   ? -18.777 -28.791 -47.521 1.00 27.37  ? 7   VAL   D O    1 
ATOM   5472 C  CB   . VAL   D 1 7   ? -16.078 -30.087 -48.159 1.00 26.56  ? 7   VAL   D CB   1 
ATOM   5473 C  CG1  . VAL   D 1 7   ? -16.658 -31.499 -48.227 1.00 28.67  ? 7   VAL   D CG1  1 
ATOM   5474 C  CG2  . VAL   D 1 7   ? -14.628 -30.076 -48.606 1.00 24.78  ? 7   VAL   D CG2  1 
ATOM   5475 N  N    . GLU   D 1 8   ? -19.231 -29.487 -49.650 1.00 27.23  ? 8   GLU   D N    1 
ATOM   5476 C  CA   . GLU   D 1 8   ? -20.703 -29.484 -49.481 1.00 27.66  ? 8   GLU   D CA   1 
ATOM   5477 C  C    . GLU   D 1 8   ? -21.235 -30.917 -49.350 1.00 25.77  ? 8   GLU   D C    1 
ATOM   5478 O  O    . GLU   D 1 8   ? -20.731 -31.838 -50.044 1.00 27.13  ? 8   GLU   D O    1 
ATOM   5479 C  CB   . GLU   D 1 8   ? -21.383 -28.702 -50.602 1.00 28.90  ? 8   GLU   D CB   1 
ATOM   5480 C  CG   . GLU   D 1 8   ? -21.028 -29.155 -51.997 1.00 28.84  ? 8   GLU   D CG   1 
ATOM   5481 C  CD   . GLU   D 1 8   ? -22.024 -28.630 -53.011 1.00 30.68  ? 8   GLU   D CD   1 
ATOM   5482 O  OE1  . GLU   D 1 8   ? -22.025 -27.390 -53.259 1.00 30.22  ? 8   GLU   D OE1  1 
ATOM   5483 O  OE2  . GLU   D 1 8   ? -22.820 -29.454 -53.517 1.00 30.80  ? 8   GLU   D OE2  1 
ATOM   5484 N  N    . LEU   D 1 9   ? -22.146 -31.080 -48.396 1.00 24.19  ? 9   LEU   D N    1 
ATOM   5485 C  CA   . LEU   D 1 9   ? -23.075 -32.224 -48.243 1.00 25.06  ? 9   LEU   D CA   1 
ATOM   5486 C  C    . LEU   D 1 9   ? -24.405 -31.752 -48.818 1.00 24.92  ? 9   LEU   D C    1 
ATOM   5487 O  O    . LEU   D 1 9   ? -25.175 -31.126 -48.073 1.00 26.29  ? 9   LEU   D O    1 
ATOM   5488 C  CB   . LEU   D 1 9   ? -23.211 -32.600 -46.760 1.00 24.19  ? 9   LEU   D CB   1 
ATOM   5489 C  CG   . LEU   D 1 9   ? -22.059 -33.406 -46.151 1.00 24.67  ? 9   LEU   D CG   1 
ATOM   5490 C  CD1  . LEU   D 1 9   ? -20.697 -32.798 -46.454 1.00 22.53  ? 9   LEU   D CD1  1 
ATOM   5491 C  CD2  . LEU   D 1 9   ? -22.252 -33.550 -44.637 1.00 24.78  ? 9   LEU   D CD2  1 
ATOM   5492 N  N    . ASP   D 1 10  ? -24.612 -31.953 -50.121 1.00 26.13  ? 10  ASP   D N    1 
ATOM   5493 C  CA   . ASP   D 1 10  ? -25.765 -31.388 -50.875 1.00 24.86  ? 10  ASP   D CA   1 
ATOM   5494 C  C    . ASP   D 1 10  ? -26.856 -32.455 -50.945 1.00 26.84  ? 10  ASP   D C    1 
ATOM   5495 O  O    . ASP   D 1 10  ? -26.662 -33.452 -51.667 1.00 30.42  ? 10  ASP   D O    1 
ATOM   5496 C  CB   . ASP   D 1 10  ? -25.318 -30.924 -52.262 1.00 24.29  ? 10  ASP   D CB   1 
ATOM   5497 C  CG   . ASP   D 1 10  ? -26.348 -30.093 -53.006 1.00 23.96  ? 10  ASP   D CG   1 
ATOM   5498 O  OD1  . ASP   D 1 10  ? -27.533 -30.078 -52.578 1.00 23.18  ? 10  ASP   D OD1  1 
ATOM   5499 O  OD2  . ASP   D 1 10  ? -25.959 -29.463 -54.002 1.00 22.64  ? 10  ASP   D OD2  1 
ATOM   5500 N  N    . THR   D 1 11  ? -27.949 -32.247 -50.216 1.00 27.20  ? 11  THR   D N    1 
ATOM   5501 C  CA   . THR   D 1 11  ? -29.066 -33.206 -50.068 1.00 29.83  ? 11  THR   D CA   1 
ATOM   5502 C  C    . THR   D 1 11  ? -30.164 -33.001 -51.129 1.00 32.90  ? 11  THR   D C    1 
ATOM   5503 O  O    . THR   D 1 11  ? -31.190 -33.717 -51.043 1.00 29.71  ? 11  THR   D O    1 
ATOM   5504 C  CB   . THR   D 1 11  ? -29.641 -33.088 -48.659 1.00 29.38  ? 11  THR   D CB   1 
ATOM   5505 O  OG1  . THR   D 1 11  ? -30.177 -31.775 -48.501 1.00 30.04  ? 11  THR   D OG1  1 
ATOM   5506 C  CG2  . THR   D 1 11  ? -28.590 -33.358 -47.606 1.00 32.31  ? 11  THR   D CG2  1 
ATOM   5507 N  N    . TYR   D 1 12  ? -30.024 -32.041 -52.054 1.00 36.62  ? 12  TYR   D N    1 
ATOM   5508 C  CA   . TYR   D 1 12  ? -31.122 -31.700 -53.001 1.00 38.71  ? 12  TYR   D CA   1 
ATOM   5509 C  C    . TYR   D 1 12  ? -30.576 -31.348 -54.376 1.00 41.27  ? 12  TYR   D C    1 
ATOM   5510 O  O    . TYR   D 1 12  ? -29.859 -30.363 -54.529 1.00 43.78  ? 12  TYR   D O    1 
ATOM   5511 C  CB   . TYR   D 1 12  ? -32.013 -30.584 -52.466 1.00 38.49  ? 12  TYR   D CB   1 
ATOM   5512 C  CG   . TYR   D 1 12  ? -33.198 -30.313 -53.357 1.00 42.41  ? 12  TYR   D CG   1 
ATOM   5513 C  CD1  . TYR   D 1 12  ? -34.391 -30.991 -53.182 1.00 42.91  ? 12  TYR   D CD1  1 
ATOM   5514 C  CD2  . TYR   D 1 12  ? -33.116 -29.406 -54.407 1.00 43.22  ? 12  TYR   D CD2  1 
ATOM   5515 C  CE1  . TYR   D 1 12  ? -35.482 -30.759 -54.002 1.00 43.06  ? 12  TYR   D CE1  1 
ATOM   5516 C  CE2  . TYR   D 1 12  ? -34.199 -29.156 -55.232 1.00 43.80  ? 12  TYR   D CE2  1 
ATOM   5517 C  CZ   . TYR   D 1 12  ? -35.391 -29.830 -55.024 1.00 44.18  ? 12  TYR   D CZ   1 
ATOM   5518 O  OH   . TYR   D 1 12  ? -36.462 -29.609 -55.841 1.00 47.27  ? 12  TYR   D OH   1 
ATOM   5519 N  N    . PRO   D 1 13  ? -30.929 -32.128 -55.426 1.00 48.87  ? 13  PRO   D N    1 
ATOM   5520 C  CA   . PRO   D 1 13  ? -30.449 -31.846 -56.778 1.00 51.10  ? 13  PRO   D CA   1 
ATOM   5521 C  C    . PRO   D 1 13  ? -31.043 -30.524 -57.294 1.00 46.64  ? 13  PRO   D C    1 
ATOM   5522 O  O    . PRO   D 1 13  ? -32.242 -30.402 -57.342 1.00 52.62  ? 13  PRO   D O    1 
ATOM   5523 C  CB   . PRO   D 1 13  ? -30.908 -33.056 -57.612 1.00 52.16  ? 13  PRO   D CB   1 
ATOM   5524 C  CG   . PRO   D 1 13  ? -31.332 -34.101 -56.595 1.00 51.89  ? 13  PRO   D CG   1 
ATOM   5525 C  CD   . PRO   D 1 13  ? -31.796 -33.316 -55.387 1.00 51.21  ? 13  PRO   D CD   1 
ATOM   5526 N  N    . ASN   D 1 14  ? -30.182 -29.547 -57.566 1.00 42.50  ? 14  ASN   D N    1 
ATOM   5527 C  CA   . ASN   D 1 14  ? -30.511 -28.280 -58.265 1.00 40.22  ? 14  ASN   D CA   1 
ATOM   5528 C  C    . ASN   D 1 14  ? -29.924 -28.386 -59.679 1.00 42.41  ? 14  ASN   D C    1 
ATOM   5529 O  O    . ASN   D 1 14  ? -28.856 -27.781 -59.932 1.00 45.29  ? 14  ASN   D O    1 
ATOM   5530 C  CB   . ASN   D 1 14  ? -30.011 -27.072 -57.462 1.00 36.49  ? 14  ASN   D CB   1 
ATOM   5531 C  CG   . ASN   D 1 14  ? -30.675 -26.918 -56.105 1.00 35.24  ? 14  ASN   D CG   1 
ATOM   5532 O  OD1  . ASN   D 1 14  ? -30.084 -27.222 -55.064 1.00 36.74  ? 14  ASN   D OD1  1 
ATOM   5533 N  ND2  . ASN   D 1 14  ? -31.896 -26.417 -56.087 1.00 29.24  ? 14  ASN   D ND2  1 
ATOM   5534 N  N    . THR   D 1 15  ? -30.577 -29.157 -60.560 1.00 45.31  ? 15  THR   D N    1 
ATOM   5535 C  CA   . THR   D 1 15  ? -30.026 -29.606 -61.880 1.00 46.15  ? 15  THR   D CA   1 
ATOM   5536 C  C    . THR   D 1 15  ? -29.868 -28.404 -62.835 1.00 44.14  ? 15  THR   D C    1 
ATOM   5537 O  O    . THR   D 1 15  ? -28.960 -28.445 -63.684 1.00 38.54  ? 15  THR   D O    1 
ATOM   5538 C  CB   . THR   D 1 15  ? -30.869 -30.743 -62.476 1.00 45.48  ? 15  THR   D CB   1 
ATOM   5539 O  OG1  . THR   D 1 15  ? -32.155 -30.266 -62.873 1.00 45.91  ? 15  THR   D OG1  1 
ATOM   5540 C  CG2  . THR   D 1 15  ? -31.067 -31.885 -61.503 1.00 48.26  ? 15  THR   D CG2  1 
ATOM   5541 N  N    . ASP   D 1 16  ? -30.674 -27.349 -62.658 1.00 44.60  ? 16  ASP   D N    1 
ATOM   5542 C  CA   . ASP   D 1 16  ? -30.582 -26.086 -63.438 1.00 46.27  ? 16  ASP   D CA   1 
ATOM   5543 C  C    . ASP   D 1 16  ? -29.368 -25.234 -63.030 1.00 47.06  ? 16  ASP   D C    1 
ATOM   5544 O  O    . ASP   D 1 16  ? -29.215 -24.160 -63.636 1.00 45.68  ? 16  ASP   D O    1 
ATOM   5545 C  CB   . ASP   D 1 16  ? -31.860 -25.252 -63.315 1.00 49.88  ? 16  ASP   D CB   1 
ATOM   5546 C  CG   . ASP   D 1 16  ? -32.214 -24.829 -61.900 1.00 55.95  ? 16  ASP   D CG   1 
ATOM   5547 O  OD1  . ASP   D 1 16  ? -31.942 -25.619 -60.965 1.00 61.61  ? 16  ASP   D OD1  1 
ATOM   5548 O  OD2  . ASP   D 1 16  ? -32.778 -23.718 -61.744 1.00 55.80  ? 16  ASP   D OD2  1 
ATOM   5549 N  N    . ILE   D 1 17  ? -28.532 -25.653 -62.065 1.00 49.07  ? 17  ILE   D N    1 
ATOM   5550 C  CA   . ILE   D 1 17  ? -27.305 -24.881 -61.673 1.00 46.76  ? 17  ILE   D CA   1 
ATOM   5551 C  C    . ILE   D 1 17  ? -26.102 -25.815 -61.435 1.00 47.28  ? 17  ILE   D C    1 
ATOM   5552 O  O    . ILE   D 1 17  ? -25.222 -25.432 -60.653 1.00 52.33  ? 17  ILE   D O    1 
ATOM   5553 C  CB   . ILE   D 1 17  ? -27.581 -23.953 -60.461 1.00 44.11  ? 17  ILE   D CB   1 
ATOM   5554 C  CG1  . ILE   D 1 17  ? -27.829 -24.727 -59.164 1.00 43.41  ? 17  ILE   D CG1  1 
ATOM   5555 C  CG2  . ILE   D 1 17  ? -28.728 -22.986 -60.752 1.00 42.76  ? 17  ILE   D CG2  1 
ATOM   5556 C  CD1  . ILE   D 1 17  ? -27.835 -23.867 -57.916 1.00 43.00  ? 17  ILE   D CD1  1 
ATOM   5557 N  N    . GLY   D 1 18  ? -26.020 -26.962 -62.117 1.00 45.68  ? 18  GLY   D N    1 
ATOM   5558 C  CA   . GLY   D 1 18  ? -24.792 -27.784 -62.191 1.00 40.73  ? 18  GLY   D CA   1 
ATOM   5559 C  C    . GLY   D 1 18  ? -24.808 -28.999 -61.267 1.00 38.37  ? 18  GLY   D C    1 
ATOM   5560 O  O    . GLY   D 1 18  ? -23.860 -29.804 -61.339 1.00 37.59  ? 18  GLY   D O    1 
ATOM   5561 N  N    . ASP   D 1 19  ? -25.816 -29.138 -60.404 1.00 36.49  ? 19  ASP   D N    1 
ATOM   5562 C  CA   . ASP   D 1 19  ? -25.908 -30.291 -59.474 1.00 38.60  ? 19  ASP   D CA   1 
ATOM   5563 C  C    . ASP   D 1 19  ? -26.111 -31.545 -60.317 1.00 43.62  ? 19  ASP   D C    1 
ATOM   5564 O  O    . ASP   D 1 19  ? -26.902 -31.529 -61.254 1.00 48.34  ? 19  ASP   D O    1 
ATOM   5565 C  CB   . ASP   D 1 19  ? -27.037 -30.128 -58.444 1.00 37.71  ? 19  ASP   D CB   1 
ATOM   5566 C  CG   . ASP   D 1 19  ? -26.661 -29.322 -57.200 1.00 35.15  ? 19  ASP   D CG   1 
ATOM   5567 O  OD1  . ASP   D 1 19  ? -25.522 -28.855 -57.151 1.00 34.64  ? 19  ASP   D OD1  1 
ATOM   5568 O  OD2  . ASP   D 1 19  ? -27.512 -29.171 -56.289 1.00 30.42  ? 19  ASP   D OD2  1 
ATOM   5569 N  N    . PRO   D 1 20  ? -25.424 -32.667 -60.013 1.00 44.26  ? 20  PRO   D N    1 
ATOM   5570 C  CA   . PRO   D 1 20  ? -25.898 -33.986 -60.448 1.00 42.82  ? 20  PRO   D CA   1 
ATOM   5571 C  C    . PRO   D 1 20  ? -27.357 -34.197 -59.992 1.00 42.40  ? 20  PRO   D C    1 
ATOM   5572 O  O    . PRO   D 1 20  ? -27.791 -33.446 -59.134 1.00 44.79  ? 20  PRO   D O    1 
ATOM   5573 C  CB   . PRO   D 1 20  ? -24.942 -34.969 -59.748 1.00 44.84  ? 20  PRO   D CB   1 
ATOM   5574 C  CG   . PRO   D 1 20  ? -23.700 -34.147 -59.396 1.00 45.94  ? 20  PRO   D CG   1 
ATOM   5575 C  CD   . PRO   D 1 20  ? -24.179 -32.719 -59.229 1.00 43.81  ? 20  PRO   D CD   1 
ATOM   5576 N  N    . SER   D 1 21  ? -28.069 -35.202 -60.529 1.00 42.77  ? 21  SER   D N    1 
ATOM   5577 C  CA   . SER   D 1 21  ? -29.509 -35.500 -60.250 1.00 41.10  ? 21  SER   D CA   1 
ATOM   5578 C  C    . SER   D 1 21  ? -29.688 -36.438 -59.037 1.00 42.27  ? 21  SER   D C    1 
ATOM   5579 O  O    . SER   D 1 21  ? -30.799 -36.983 -58.869 1.00 41.87  ? 21  SER   D O    1 
ATOM   5580 C  CB   . SER   D 1 21  ? -30.204 -36.044 -61.478 1.00 40.68  ? 21  SER   D CB   1 
ATOM   5581 O  OG   . SER   D 1 21  ? -29.334 -36.889 -62.221 1.00 41.38  ? 21  SER   D OG   1 
ATOM   5582 N  N    . TYR   D 1 22  ? -28.666 -36.575 -58.181 1.00 40.42  ? 22  TYR   D N    1 
ATOM   5583 C  CA   . TYR   D 1 22  ? -28.712 -37.311 -56.882 1.00 39.61  ? 22  TYR   D CA   1 
ATOM   5584 C  C    . TYR   D 1 22  ? -28.126 -36.423 -55.777 1.00 39.34  ? 22  TYR   D C    1 
ATOM   5585 O  O    . TYR   D 1 22  ? -27.374 -35.489 -56.067 1.00 40.83  ? 22  TYR   D O    1 
ATOM   5586 C  CB   . TYR   D 1 22  ? -27.944 -38.632 -57.008 1.00 34.93  ? 22  TYR   D CB   1 
ATOM   5587 C  CG   . TYR   D 1 22  ? -26.716 -38.548 -57.882 1.00 33.76  ? 22  TYR   D CG   1 
ATOM   5588 C  CD1  . TYR   D 1 22  ? -25.509 -38.087 -57.378 1.00 35.24  ? 22  TYR   D CD1  1 
ATOM   5589 C  CD2  . TYR   D 1 22  ? -26.763 -38.872 -59.232 1.00 33.21  ? 22  TYR   D CD2  1 
ATOM   5590 C  CE1  . TYR   D 1 22  ? -24.378 -37.973 -58.176 1.00 33.80  ? 22  TYR   D CE1  1 
ATOM   5591 C  CE2  . TYR   D 1 22  ? -25.640 -38.770 -60.044 1.00 32.81  ? 22  TYR   D CE2  1 
ATOM   5592 C  CZ   . TYR   D 1 22  ? -24.439 -38.324 -59.512 1.00 34.81  ? 22  TYR   D CZ   1 
ATOM   5593 O  OH   . TYR   D 1 22  ? -23.318 -38.211 -60.287 1.00 37.79  ? 22  TYR   D OH   1 
ATOM   5594 N  N    . PRO   D 1 23  ? -28.443 -36.663 -54.483 1.00 34.67  ? 23  PRO   D N    1 
ATOM   5595 C  CA   . PRO   D 1 23  ? -27.578 -36.207 -53.394 1.00 34.09  ? 23  PRO   D CA   1 
ATOM   5596 C  C    . PRO   D 1 23  ? -26.091 -36.482 -53.675 1.00 33.29  ? 23  PRO   D C    1 
ATOM   5597 O  O    . PRO   D 1 23  ? -25.768 -37.508 -54.257 1.00 30.98  ? 23  PRO   D O    1 
ATOM   5598 C  CB   . PRO   D 1 23  ? -28.097 -37.014 -52.202 1.00 33.59  ? 23  PRO   D CB   1 
ATOM   5599 C  CG   . PRO   D 1 23  ? -29.576 -37.123 -52.492 1.00 34.39  ? 23  PRO   D CG   1 
ATOM   5600 C  CD   . PRO   D 1 23  ? -29.659 -37.324 -53.993 1.00 33.84  ? 23  PRO   D CD   1 
ATOM   5601 N  N    . HIS   D 1 24  ? -25.221 -35.542 -53.300 1.00 31.30  ? 24  HIS   D N    1 
ATOM   5602 C  CA   . HIS   D 1 24  ? -23.774 -35.586 -53.624 1.00 32.64  ? 24  HIS   D CA   1 
ATOM   5603 C  C    . HIS   D 1 24  ? -22.953 -34.765 -52.621 1.00 32.30  ? 24  HIS   D C    1 
ATOM   5604 O  O    . HIS   D 1 24  ? -23.488 -33.840 -52.025 1.00 30.88  ? 24  HIS   D O    1 
ATOM   5605 C  CB   . HIS   D 1 24  ? -23.543 -35.057 -55.043 1.00 33.76  ? 24  HIS   D CB   1 
ATOM   5606 C  CG   . HIS   D 1 24  ? -24.099 -33.684 -55.230 1.00 35.23  ? 24  HIS   D CG   1 
ATOM   5607 N  ND1  . HIS   D 1 24  ? -25.462 -33.432 -55.210 1.00 34.91  ? 24  HIS   D ND1  1 
ATOM   5608 C  CD2  . HIS   D 1 24  ? -23.495 -32.490 -55.408 1.00 34.38  ? 24  HIS   D CD2  1 
ATOM   5609 C  CE1  . HIS   D 1 24  ? -25.670 -32.144 -55.399 1.00 34.68  ? 24  HIS   D CE1  1 
ATOM   5610 N  NE2  . HIS   D 1 24  ? -24.482 -31.545 -55.517 1.00 34.65  ? 24  HIS   D NE2  1 
ATOM   5611 N  N    . ILE   D 1 25  ? -21.681 -35.122 -52.490 1.00 33.39  ? 25  ILE   D N    1 
ATOM   5612 C  CA   . ILE   D 1 25  ? -20.623 -34.319 -51.831 1.00 37.09  ? 25  ILE   D CA   1 
ATOM   5613 C  C    . ILE   D 1 25  ? -19.807 -33.666 -52.949 1.00 36.34  ? 25  ILE   D C    1 
ATOM   5614 O  O    . ILE   D 1 25  ? -19.588 -34.329 -53.981 1.00 32.57  ? 25  ILE   D O    1 
ATOM   5615 C  CB   . ILE   D 1 25  ? -19.784 -35.196 -50.878 1.00 39.58  ? 25  ILE   D CB   1 
ATOM   5616 C  CG1  . ILE   D 1 25  ? -19.027 -36.308 -51.611 1.00 41.73  ? 25  ILE   D CG1  1 
ATOM   5617 C  CG2  . ILE   D 1 25  ? -20.680 -35.758 -49.782 1.00 39.21  ? 25  ILE   D CG2  1 
ATOM   5618 C  CD1  . ILE   D 1 25  ? -18.098 -37.110 -50.731 1.00 43.23  ? 25  ILE   D CD1  1 
ATOM   5619 N  N    . GLY   D 1 26  ? -19.425 -32.402 -52.756 1.00 37.30  ? 26  GLY   D N    1 
ATOM   5620 C  CA   . GLY   D 1 26  ? -18.694 -31.593 -53.750 1.00 36.10  ? 26  GLY   D CA   1 
ATOM   5621 C  C    . GLY   D 1 26  ? -17.649 -30.702 -53.097 1.00 36.73  ? 26  GLY   D C    1 
ATOM   5622 O  O    . GLY   D 1 26  ? -17.837 -30.333 -51.918 1.00 35.76  ? 26  GLY   D O    1 
ATOM   5623 N  N    . ILE   D 1 27  ? -16.584 -30.398 -53.842 1.00 34.10  ? 27  ILE   D N    1 
ATOM   5624 C  CA   . ILE   D 1 27  ? -15.526 -29.407 -53.505 1.00 35.30  ? 27  ILE   D CA   1 
ATOM   5625 C  C    . ILE   D 1 27  ? -15.785 -28.124 -54.308 1.00 37.88  ? 27  ILE   D C    1 
ATOM   5626 O  O    . ILE   D 1 27  ? -15.694 -28.162 -55.558 1.00 37.02  ? 27  ILE   D O    1 
ATOM   5627 C  CB   . ILE   D 1 27  ? -14.138 -30.006 -53.782 1.00 36.80  ? 27  ILE   D CB   1 
ATOM   5628 C  CG1  . ILE   D 1 27  ? -13.849 -31.167 -52.828 1.00 36.32  ? 27  ILE   D CG1  1 
ATOM   5629 C  CG2  . ILE   D 1 27  ? -13.061 -28.932 -53.712 1.00 37.77  ? 27  ILE   D CG2  1 
ATOM   5630 C  CD1  . ILE   D 1 27  ? -12.650 -31.989 -53.220 1.00 36.83  ? 27  ILE   D CD1  1 
ATOM   5631 N  N    . ASP   D 1 28  ? -16.128 -27.043 -53.602 1.00 37.34  ? 28  ASP   D N    1 
ATOM   5632 C  CA   . ASP   D 1 28  ? -16.529 -25.732 -54.167 1.00 34.12  ? 28  ASP   D CA   1 
ATOM   5633 C  C    . ASP   D 1 28  ? -15.378 -24.742 -54.008 1.00 36.58  ? 28  ASP   D C    1 
ATOM   5634 O  O    . ASP   D 1 28  ? -15.108 -24.346 -52.846 1.00 36.73  ? 28  ASP   D O    1 
ATOM   5635 C  CB   . ASP   D 1 28  ? -17.767 -25.199 -53.457 1.00 32.64  ? 28  ASP   D CB   1 
ATOM   5636 C  CG   . ASP   D 1 28  ? -18.975 -26.090 -53.632 1.00 33.73  ? 28  ASP   D CG   1 
ATOM   5637 O  OD1  . ASP   D 1 28  ? -18.819 -27.141 -54.300 1.00 34.67  ? 28  ASP   D OD1  1 
ATOM   5638 O  OD2  . ASP   D 1 28  ? -20.047 -25.744 -53.076 1.00 32.52  ? 28  ASP   D OD2  1 
ATOM   5639 N  N    . ILE   D 1 29  ? -14.741 -24.365 -55.121 1.00 34.35  ? 29  ILE   D N    1 
ATOM   5640 C  CA   . ILE   D 1 29  ? -13.752 -23.252 -55.179 1.00 37.34  ? 29  ILE   D CA   1 
ATOM   5641 C  C    . ILE   D 1 29  ? -14.442 -22.022 -55.770 1.00 39.85  ? 29  ILE   D C    1 
ATOM   5642 O  O    . ILE   D 1 29  ? -14.517 -21.938 -57.012 1.00 44.87  ? 29  ILE   D O    1 
ATOM   5643 C  CB   . ILE   D 1 29  ? -12.495 -23.633 -55.984 1.00 37.02  ? 29  ILE   D CB   1 
ATOM   5644 C  CG1  . ILE   D 1 29  ? -11.966 -25.025 -55.630 1.00 36.54  ? 29  ILE   D CG1  1 
ATOM   5645 C  CG2  . ILE   D 1 29  ? -11.432 -22.562 -55.800 1.00 37.44  ? 29  ILE   D CG2  1 
ATOM   5646 C  CD1  . ILE   D 1 29  ? -11.726 -25.223 -54.155 1.00 38.08  ? 29  ILE   D CD1  1 
ATOM   5647 N  N    . LYS   D 1 30  ? -14.929 -21.128 -54.902 1.00 39.65  ? 30  LYS   D N    1 
ATOM   5648 C  CA   . LYS   D 1 30  ? -15.418 -19.760 -55.233 1.00 39.71  ? 30  LYS   D CA   1 
ATOM   5649 C  C    . LYS   D 1 30  ? -16.747 -19.807 -56.010 1.00 39.10  ? 30  LYS   D C    1 
ATOM   5650 O  O    . LYS   D 1 30  ? -17.121 -18.766 -56.584 1.00 44.56  ? 30  LYS   D O    1 
ATOM   5651 C  CB   . LYS   D 1 30  ? -14.367 -18.982 -56.036 1.00 42.05  ? 30  LYS   D CB   1 
ATOM   5652 C  CG   . LYS   D 1 30  ? -13.019 -18.774 -55.355 1.00 45.69  ? 30  LYS   D CG   1 
ATOM   5653 C  CD   . LYS   D 1 30  ? -11.944 -18.111 -56.225 1.00 46.88  ? 30  LYS   D CD   1 
ATOM   5654 C  CE   . LYS   D 1 30  ? -12.320 -16.730 -56.733 1.00 51.88  ? 30  LYS   D CE   1 
ATOM   5655 N  NZ   . LYS   D 1 30  ? -12.373 -15.722 -55.646 1.00 53.92  ? 30  LYS   D NZ   1 
ATOM   5656 N  N    . SER   D 1 31  ? -17.477 -20.921 -55.979 1.00 36.82  ? 31  SER   D N    1 
ATOM   5657 C  CA   . SER   D 1 31  ? -18.717 -21.139 -56.771 1.00 34.64  ? 31  SER   D CA   1 
ATOM   5658 C  C    . SER   D 1 31  ? -19.501 -22.334 -56.213 1.00 33.96  ? 31  SER   D C    1 
ATOM   5659 O  O    . SER   D 1 31  ? -18.846 -23.365 -55.974 1.00 38.24  ? 31  SER   D O    1 
ATOM   5660 C  CB   . SER   D 1 31  ? -18.352 -21.353 -58.237 1.00 34.61  ? 31  SER   D CB   1 
ATOM   5661 O  OG   . SER   D 1 31  ? -19.451 -21.869 -58.980 1.00 31.43  ? 31  SER   D OG   1 
ATOM   5662 N  N    . VAL   D 1 32  ? -20.831 -22.210 -56.076 1.00 33.71  ? 32  VAL   D N    1 
ATOM   5663 C  CA   . VAL   D 1 32  ? -21.806 -23.301 -55.735 1.00 37.62  ? 32  VAL   D CA   1 
ATOM   5664 C  C    . VAL   D 1 32  ? -21.776 -24.436 -56.786 1.00 39.52  ? 32  VAL   D C    1 
ATOM   5665 O  O    . VAL   D 1 32  ? -22.282 -25.527 -56.468 1.00 38.35  ? 32  VAL   D O    1 
ATOM   5666 C  CB   . VAL   D 1 32  ? -23.237 -22.739 -55.594 1.00 37.84  ? 32  VAL   D CB   1 
ATOM   5667 C  CG1  . VAL   D 1 32  ? -23.873 -22.449 -56.949 1.00 38.90  ? 32  VAL   D CG1  1 
ATOM   5668 C  CG2  . VAL   D 1 32  ? -24.140 -23.654 -54.783 1.00 37.26  ? 32  VAL   D CG2  1 
ATOM   5669 N  N    . ARG   D 1 33  ? -21.233 -24.189 -57.992 1.00 40.83  ? 33  ARG   D N    1 
ATOM   5670 C  CA   . ARG   D 1 33  ? -21.001 -25.201 -59.062 1.00 39.72  ? 33  ARG   D CA   1 
ATOM   5671 C  C    . ARG   D 1 33  ? -19.695 -25.939 -58.768 1.00 37.33  ? 33  ARG   D C    1 
ATOM   5672 O  O    . ARG   D 1 33  ? -18.631 -25.447 -59.171 1.00 34.94  ? 33  ARG   D O    1 
ATOM   5673 C  CB   . ARG   D 1 33  ? -20.941 -24.560 -60.455 1.00 41.50  ? 33  ARG   D CB   1 
ATOM   5674 C  CG   . ARG   D 1 33  ? -22.285 -24.046 -60.959 1.00 46.79  ? 33  ARG   D CG   1 
ATOM   5675 C  CD   . ARG   D 1 33  ? -22.196 -23.032 -62.099 1.00 50.00  ? 33  ARG   D CD   1 
ATOM   5676 N  NE   . ARG   D 1 33  ? -23.400 -22.207 -62.151 1.00 50.91  ? 33  ARG   D NE   1 
ATOM   5677 C  CZ   . ARG   D 1 33  ? -24.451 -22.409 -62.949 1.00 53.42  ? 33  ARG   D CZ   1 
ATOM   5678 N  NH1  . ARG   D 1 33  ? -24.467 -23.415 -63.812 1.00 52.36  ? 33  ARG   D NH1  1 
ATOM   5679 N  NH2  . ARG   D 1 33  ? -25.485 -21.584 -62.883 1.00 52.07  ? 33  ARG   D NH2  1 
ATOM   5680 N  N    . SER   D 1 34  ? -19.796 -27.100 -58.124 1.00 38.82  ? 34  SER   D N    1 
ATOM   5681 C  CA   . SER   D 1 34  ? -18.650 -27.908 -57.631 1.00 40.10  ? 34  SER   D CA   1 
ATOM   5682 C  C    . SER   D 1 34  ? -17.646 -28.156 -58.764 1.00 42.99  ? 34  SER   D C    1 
ATOM   5683 O  O    . SER   D 1 34  ? -18.083 -28.445 -59.897 1.00 44.64  ? 34  SER   D O    1 
ATOM   5684 C  CB   . SER   D 1 34  ? -19.135 -29.205 -57.041 1.00 38.64  ? 34  SER   D CB   1 
ATOM   5685 O  OG   . SER   D 1 34  ? -20.172 -28.979 -56.097 1.00 40.06  ? 34  SER   D OG   1 
ATOM   5686 N  N    . LYS   D 1 35  ? -16.349 -28.069 -58.464 1.00 44.08  ? 35  LYS   D N    1 
ATOM   5687 C  CA   . LYS   D 1 35  ? -15.266 -28.484 -59.390 1.00 46.98  ? 35  LYS   D CA   1 
ATOM   5688 C  C    . LYS   D 1 35  ? -15.305 -30.008 -59.549 1.00 44.15  ? 35  LYS   D C    1 
ATOM   5689 O  O    . LYS   D 1 35  ? -15.090 -30.463 -60.660 1.00 49.42  ? 35  LYS   D O    1 
ATOM   5690 C  CB   . LYS   D 1 35  ? -13.889 -28.038 -58.889 1.00 50.86  ? 35  LYS   D CB   1 
ATOM   5691 C  CG   . LYS   D 1 35  ? -13.711 -26.540 -58.689 1.00 54.65  ? 35  LYS   D CG   1 
ATOM   5692 C  CD   . LYS   D 1 35  ? -13.848 -25.710 -59.949 1.00 56.95  ? 35  LYS   D CD   1 
ATOM   5693 C  CE   . LYS   D 1 35  ? -13.980 -24.234 -59.637 1.00 59.74  ? 35  LYS   D CE   1 
ATOM   5694 N  NZ   . LYS   D 1 35  ? -14.298 -23.440 -60.845 1.00 60.33  ? 35  LYS   D NZ   1 
ATOM   5695 N  N    . LYS   D 1 36  ? -15.526 -30.760 -58.467 1.00 44.36  ? 36  LYS   D N    1 
ATOM   5696 C  CA   . LYS   D 1 36  ? -15.704 -32.241 -58.498 1.00 45.73  ? 36  LYS   D CA   1 
ATOM   5697 C  C    . LYS   D 1 36  ? -16.801 -32.664 -57.508 1.00 41.76  ? 36  LYS   D C    1 
ATOM   5698 O  O    . LYS   D 1 36  ? -16.988 -31.976 -56.482 1.00 40.71  ? 36  LYS   D O    1 
ATOM   5699 C  CB   . LYS   D 1 36  ? -14.394 -32.985 -58.214 1.00 49.97  ? 36  LYS   D CB   1 
ATOM   5700 C  CG   . LYS   D 1 36  ? -14.495 -34.487 -58.458 1.00 54.54  ? 36  LYS   D CG   1 
ATOM   5701 C  CD   . LYS   D 1 36  ? -13.180 -35.237 -58.454 1.00 57.03  ? 36  LYS   D CD   1 
ATOM   5702 C  CE   . LYS   D 1 36  ? -12.675 -35.634 -59.824 1.00 54.85  ? 36  LYS   D CE   1 
ATOM   5703 N  NZ   . LYS   D 1 36  ? -11.731 -36.770 -59.712 1.00 51.28  ? 36  LYS   D NZ   1 
ATOM   5704 N  N    . THR   D 1 37  ? -17.541 -33.721 -57.850 1.00 37.95  ? 37  THR   D N    1 
ATOM   5705 C  CA   . THR   D 1 37  ? -18.668 -34.276 -57.057 1.00 36.78  ? 37  THR   D CA   1 
ATOM   5706 C  C    . THR   D 1 37  ? -18.522 -35.797 -56.961 1.00 38.89  ? 37  THR   D C    1 
ATOM   5707 O  O    . THR   D 1 37  ? -17.773 -36.393 -57.766 1.00 39.65  ? 37  THR   D O    1 
ATOM   5708 C  CB   . THR   D 1 37  ? -20.038 -33.945 -57.662 1.00 38.56  ? 37  THR   D CB   1 
ATOM   5709 O  OG1  . THR   D 1 37  ? -20.140 -34.605 -58.924 1.00 37.11  ? 37  THR   D OG1  1 
ATOM   5710 C  CG2  . THR   D 1 37  ? -20.275 -32.461 -57.838 1.00 39.26  ? 37  THR   D CG2  1 
ATOM   5711 N  N    . ALA   D 1 38  ? -19.202 -36.388 -55.981 1.00 37.16  ? 38  ALA   D N    1 
ATOM   5712 C  CA   . ALA   D 1 38  ? -19.386 -37.846 -55.827 1.00 34.76  ? 38  ALA   D CA   1 
ATOM   5713 C  C    . ALA   D 1 38  ? -20.809 -38.076 -55.325 1.00 35.52  ? 38  ALA   D C    1 
ATOM   5714 O  O    . ALA   D 1 38  ? -21.277 -37.302 -54.463 1.00 34.91  ? 38  ALA   D O    1 
ATOM   5715 C  CB   . ALA   D 1 38  ? -18.352 -38.422 -54.885 1.00 32.44  ? 38  ALA   D CB   1 
ATOM   5716 N  N    . LYS   D 1 39  ? -21.481 -39.086 -55.871 1.00 37.86  ? 39  LYS   D N    1 
ATOM   5717 C  CA   . LYS   D 1 39  ? -22.802 -39.556 -55.389 1.00 39.04  ? 39  LYS   D CA   1 
ATOM   5718 C  C    . LYS   D 1 39  ? -22.690 -39.828 -53.886 1.00 37.97  ? 39  LYS   D C    1 
ATOM   5719 O  O    . LYS   D 1 39  ? -21.639 -40.348 -53.451 1.00 35.64  ? 39  LYS   D O    1 
ATOM   5720 C  CB   . LYS   D 1 39  ? -23.216 -40.819 -56.148 1.00 41.51  ? 39  LYS   D CB   1 
ATOM   5721 C  CG   . LYS   D 1 39  ? -24.626 -41.302 -55.849 1.00 44.06  ? 39  LYS   D CG   1 
ATOM   5722 C  CD   . LYS   D 1 39  ? -24.961 -42.607 -56.531 1.00 47.58  ? 39  LYS   D CD   1 
ATOM   5723 C  CE   . LYS   D 1 39  ? -26.401 -43.009 -56.304 1.00 47.97  ? 39  LYS   D CE   1 
ATOM   5724 N  NZ   . LYS   D 1 39  ? -27.323 -42.243 -57.172 1.00 48.42  ? 39  LYS   D NZ   1 
ATOM   5725 N  N    . TRP   D 1 40  ? -23.741 -39.509 -53.136 1.00 36.40  ? 40  TRP   D N    1 
ATOM   5726 C  CA   . TRP   D 1 40  ? -23.781 -39.646 -51.661 1.00 36.56  ? 40  TRP   D CA   1 
ATOM   5727 C  C    . TRP   D 1 40  ? -25.156 -40.161 -51.240 1.00 36.94  ? 40  TRP   D C    1 
ATOM   5728 O  O    . TRP   D 1 40  ? -26.141 -39.436 -51.433 1.00 41.61  ? 40  TRP   D O    1 
ATOM   5729 C  CB   . TRP   D 1 40  ? -23.444 -38.303 -50.988 1.00 37.79  ? 40  TRP   D CB   1 
ATOM   5730 C  CG   . TRP   D 1 40  ? -23.603 -38.315 -49.499 1.00 35.82  ? 40  TRP   D CG   1 
ATOM   5731 C  CD1  . TRP   D 1 40  ? -23.206 -39.301 -48.644 1.00 34.60  ? 40  TRP   D CD1  1 
ATOM   5732 C  CD2  . TRP   D 1 40  ? -24.225 -37.306 -48.685 1.00 37.89  ? 40  TRP   D CD2  1 
ATOM   5733 N  NE1  . TRP   D 1 40  ? -23.551 -38.981 -47.362 1.00 35.92  ? 40  TRP   D NE1  1 
ATOM   5734 C  CE2  . TRP   D 1 40  ? -24.153 -37.754 -47.349 1.00 37.00  ? 40  TRP   D CE2  1 
ATOM   5735 C  CE3  . TRP   D 1 40  ? -24.801 -36.054 -48.943 1.00 37.38  ? 40  TRP   D CE3  1 
ATOM   5736 C  CZ2  . TRP   D 1 40  ? -24.647 -37.000 -46.283 1.00 38.65  ? 40  TRP   D CZ2  1 
ATOM   5737 C  CZ3  . TRP   D 1 40  ? -25.295 -35.315 -47.891 1.00 36.43  ? 40  TRP   D CZ3  1 
ATOM   5738 C  CH2  . TRP   D 1 40  ? -25.209 -35.778 -46.578 1.00 36.86  ? 40  TRP   D CH2  1 
ATOM   5739 N  N    . ASN   D 1 41  ? -25.212 -41.361 -50.671 1.00 38.16  ? 41  ASN   D N    1 
ATOM   5740 C  CA   . ASN   D 1 41  ? -26.480 -41.990 -50.223 1.00 41.94  ? 41  ASN   D CA   1 
ATOM   5741 C  C    . ASN   D 1 41  ? -26.721 -41.477 -48.808 1.00 40.60  ? 41  ASN   D C    1 
ATOM   5742 O  O    . ASN   D 1 41  ? -26.272 -42.115 -47.860 1.00 41.78  ? 41  ASN   D O    1 
ATOM   5743 C  CB   . ASN   D 1 41  ? -26.458 -43.512 -50.413 1.00 43.23  ? 41  ASN   D CB   1 
ATOM   5744 C  CG   . ASN   D 1 41  ? -26.143 -43.888 -51.850 1.00 47.50  ? 41  ASN   D CG   1 
ATOM   5745 O  OD1  . ASN   D 1 41  ? -25.082 -44.434 -52.131 1.00 50.28  ? 41  ASN   D OD1  1 
ATOM   5746 N  ND2  . ASN   D 1 41  ? -27.024 -43.552 -52.785 1.00 47.68  ? 41  ASN   D ND2  1 
ATOM   5747 N  N    . MET   D 1 42  ? -27.322 -40.293 -48.715 1.00 41.74  ? 42  MET   D N    1 
ATOM   5748 C  CA   . MET   D 1 42  ? -27.693 -39.643 -47.440 1.00 43.49  ? 42  MET   D CA   1 
ATOM   5749 C  C    . MET   D 1 42  ? -28.701 -40.554 -46.733 1.00 40.96  ? 42  MET   D C    1 
ATOM   5750 O  O    . MET   D 1 42  ? -29.593 -41.068 -47.408 1.00 41.17  ? 42  MET   D O    1 
ATOM   5751 C  CB   . MET   D 1 42  ? -28.303 -38.258 -47.700 1.00 46.23  ? 42  MET   D CB   1 
ATOM   5752 C  CG   . MET   D 1 42  ? -28.290 -37.349 -46.494 1.00 46.10  ? 42  MET   D CG   1 
ATOM   5753 S  SD   . MET   D 1 42  ? -29.631 -37.660 -45.312 1.00 53.45  ? 42  MET   D SD   1 
ATOM   5754 C  CE   . MET   D 1 42  ? -31.053 -37.078 -46.240 1.00 50.92  ? 42  MET   D CE   1 
ATOM   5755 N  N    . GLN   D 1 43  ? -28.564 -40.742 -45.422 1.00 40.06  ? 43  GLN   D N    1 
ATOM   5756 C  CA   . GLN   D 1 43  ? -29.495 -41.574 -44.625 1.00 42.06  ? 43  GLN   D CA   1 
ATOM   5757 C  C    . GLN   D 1 43  ? -30.246 -40.683 -43.645 1.00 39.86  ? 43  GLN   D C    1 
ATOM   5758 O  O    . GLN   D 1 43  ? -29.634 -40.229 -42.666 1.00 46.49  ? 43  GLN   D O    1 
ATOM   5759 C  CB   . GLN   D 1 43  ? -28.720 -42.714 -43.984 1.00 42.61  ? 43  GLN   D CB   1 
ATOM   5760 C  CG   . GLN   D 1 43  ? -27.960 -43.486 -45.049 1.00 43.81  ? 43  GLN   D CG   1 
ATOM   5761 C  CD   . GLN   D 1 43  ? -27.646 -44.896 -44.637 1.00 43.73  ? 43  GLN   D CD   1 
ATOM   5762 O  OE1  . GLN   D 1 43  ? -28.366 -45.491 -43.837 1.00 44.79  ? 43  GLN   D OE1  1 
ATOM   5763 N  NE2  . GLN   D 1 43  ? -26.556 -45.424 -45.179 1.00 44.26  ? 43  GLN   D NE2  1 
ATOM   5764 N  N    . ASN   D 1 44  ? -31.520 -40.452 -43.947 1.00 35.45  ? 44  ASN   D N    1 
ATOM   5765 C  CA   . ASN   D 1 44  ? -32.452 -39.602 -43.178 1.00 35.94  ? 44  ASN   D CA   1 
ATOM   5766 C  C    . ASN   D 1 44  ? -32.509 -40.134 -41.750 1.00 36.57  ? 44  ASN   D C    1 
ATOM   5767 O  O    . ASN   D 1 44  ? -32.693 -41.352 -41.584 1.00 38.62  ? 44  ASN   D O    1 
ATOM   5768 C  CB   . ASN   D 1 44  ? -33.828 -39.571 -43.850 1.00 38.65  ? 44  ASN   D CB   1 
ATOM   5769 C  CG   . ASN   D 1 44  ? -34.784 -38.566 -43.241 1.00 39.46  ? 44  ASN   D CG   1 
ATOM   5770 O  OD1  . ASN   D 1 44  ? -34.918 -38.472 -42.027 1.00 43.64  ? 44  ASN   D OD1  1 
ATOM   5771 N  ND2  . ASN   D 1 44  ? -35.498 -37.837 -44.079 1.00 43.20  ? 44  ASN   D ND2  1 
ATOM   5772 N  N    . GLY   D 1 45  ? -32.322 -39.251 -40.769 1.00 35.66  ? 45  GLY   D N    1 
ATOM   5773 C  CA   . GLY   D 1 45  ? -32.519 -39.541 -39.333 1.00 37.34  ? 45  GLY   D CA   1 
ATOM   5774 C  C    . GLY   D 1 45  ? -31.303 -40.179 -38.665 1.00 34.37  ? 45  GLY   D C    1 
ATOM   5775 O  O    . GLY   D 1 45  ? -31.387 -40.389 -37.447 1.00 36.26  ? 45  GLY   D O    1 
ATOM   5776 N  N    . LYS   D 1 46  ? -30.219 -40.453 -39.405 1.00 33.10  ? 46  LYS   D N    1 
ATOM   5777 C  CA   . LYS   D 1 46  ? -29.024 -41.218 -38.930 1.00 34.73  ? 46  LYS   D CA   1 
ATOM   5778 C  C    . LYS   D 1 46  ? -27.810 -40.294 -38.750 1.00 34.41  ? 46  LYS   D C    1 
ATOM   5779 O  O    . LYS   D 1 46  ? -27.513 -39.476 -39.675 1.00 33.65  ? 46  LYS   D O    1 
ATOM   5780 C  CB   . LYS   D 1 46  ? -28.579 -42.294 -39.932 1.00 37.80  ? 46  LYS   D CB   1 
ATOM   5781 C  CG   . LYS   D 1 46  ? -29.615 -43.326 -40.368 1.00 43.40  ? 46  LYS   D CG   1 
ATOM   5782 C  CD   . LYS   D 1 46  ? -30.176 -44.214 -39.261 1.00 46.23  ? 46  LYS   D CD   1 
ATOM   5783 C  CE   . LYS   D 1 46  ? -31.547 -43.767 -38.789 1.00 50.88  ? 46  LYS   D CE   1 
ATOM   5784 N  NZ   . LYS   D 1 46  ? -32.260 -44.830 -38.037 1.00 53.09  ? 46  LYS   D NZ   1 
ATOM   5785 N  N    . VAL   D 1 47  ? -27.062 -40.473 -37.656 1.00 30.75  ? 47  VAL   D N    1 
ATOM   5786 C  CA   . VAL   D 1 47  ? -25.822 -39.687 -37.399 1.00 27.68  ? 47  VAL   D CA   1 
ATOM   5787 C  C    . VAL   D 1 47  ? -24.756 -40.107 -38.417 1.00 26.78  ? 47  VAL   D C    1 
ATOM   5788 O  O    . VAL   D 1 47  ? -24.483 -41.311 -38.521 1.00 28.13  ? 47  VAL   D O    1 
ATOM   5789 C  CB   . VAL   D 1 47  ? -25.337 -39.853 -35.949 1.00 27.82  ? 47  VAL   D CB   1 
ATOM   5790 C  CG1  . VAL   D 1 47  ? -23.964 -39.216 -35.725 1.00 26.26  ? 47  VAL   D CG1  1 
ATOM   5791 C  CG2  . VAL   D 1 47  ? -26.367 -39.298 -34.964 1.00 28.55  ? 47  VAL   D CG2  1 
ATOM   5792 N  N    . GLY   D 1 48  ? -24.175 -39.140 -39.132 1.00 25.46  ? 48  GLY   D N    1 
ATOM   5793 C  CA   . GLY   D 1 48  ? -23.067 -39.351 -40.093 1.00 26.96  ? 48  GLY   D CA   1 
ATOM   5794 C  C    . GLY   D 1 48  ? -21.787 -38.626 -39.671 1.00 26.72  ? 48  GLY   D C    1 
ATOM   5795 O  O    . GLY   D 1 48  ? -21.849 -37.813 -38.730 1.00 26.55  ? 48  GLY   D O    1 
ATOM   5796 N  N    . THR   D 1 49  ? -20.673 -38.905 -40.351 1.00 24.35  ? 49  THR   D N    1 
ATOM   5797 C  CA   . THR   D 1 49  ? -19.334 -38.360 -40.051 1.00 26.17  ? 49  THR   D CA   1 
ATOM   5798 C  C    . THR   D 1 49  ? -18.741 -37.836 -41.347 1.00 27.17  ? 49  THR   D C    1 
ATOM   5799 O  O    . THR   D 1 49  ? -18.721 -38.615 -42.307 1.00 28.51  ? 49  THR   D O    1 
ATOM   5800 C  CB   . THR   D 1 49  ? -18.395 -39.407 -39.424 1.00 25.80  ? 49  THR   D CB   1 
ATOM   5801 O  OG1  . THR   D 1 49  ? -18.938 -39.815 -38.174 1.00 25.69  ? 49  THR   D OG1  1 
ATOM   5802 C  CG2  . THR   D 1 49  ? -17.004 -38.885 -39.152 1.00 25.96  ? 49  THR   D CG2  1 
ATOM   5803 N  N    . ALA   D 1 50  ? -18.264 -36.586 -41.332 1.00 26.82  ? 50  ALA   D N    1 
ATOM   5804 C  CA   . ALA   D 1 50  ? -17.487 -35.940 -42.407 1.00 29.26  ? 50  ALA   D CA   1 
ATOM   5805 C  C    . ALA   D 1 50  ? -16.042 -35.722 -41.941 1.00 30.66  ? 50  ALA   D C    1 
ATOM   5806 O  O    . ALA   D 1 50  ? -15.833 -35.250 -40.806 1.00 35.12  ? 50  ALA   D O    1 
ATOM   5807 C  CB   . ALA   D 1 50  ? -18.140 -34.635 -42.789 1.00 31.76  ? 50  ALA   D CB   1 
ATOM   5808 N  N    . HIS   D 1 51  ? -15.085 -36.071 -42.786 1.00 29.71  ? 51  HIS   D N    1 
ATOM   5809 C  CA   . HIS   D 1 51  ? -13.632 -35.905 -42.561 1.00 32.08  ? 51  HIS   D CA   1 
ATOM   5810 C  C    . HIS   D 1 51  ? -13.088 -35.202 -43.803 1.00 31.38  ? 51  HIS   D C    1 
ATOM   5811 O  O    . HIS   D 1 51  ? -13.196 -35.799 -44.879 1.00 33.46  ? 51  HIS   D O    1 
ATOM   5812 C  CB   . HIS   D 1 51  ? -12.999 -37.279 -42.290 1.00 36.90  ? 51  HIS   D CB   1 
ATOM   5813 C  CG   . HIS   D 1 51  ? -11.580 -37.243 -41.822 1.00 41.26  ? 51  HIS   D CG   1 
ATOM   5814 N  ND1  . HIS   D 1 51  ? -10.680 -38.257 -42.105 1.00 44.41  ? 51  HIS   D ND1  1 
ATOM   5815 C  CD2  . HIS   D 1 51  ? -10.902 -36.344 -41.072 1.00 46.27  ? 51  HIS   D CD2  1 
ATOM   5816 C  CE1  . HIS   D 1 51  ? -9.513  -37.982 -41.557 1.00 45.45  ? 51  HIS   D CE1  1 
ATOM   5817 N  NE2  . HIS   D 1 51  ? -9.620  -36.815 -40.914 1.00 44.63  ? 51  HIS   D NE2  1 
ATOM   5818 N  N    . ILE   D 1 52  ? -12.644 -33.948 -43.671 1.00 30.54  ? 52  ILE   D N    1 
ATOM   5819 C  CA   . ILE   D 1 52  ? -11.977 -33.165 -44.746 1.00 29.38  ? 52  ILE   D CA   1 
ATOM   5820 C  C    . ILE   D 1 52  ? -10.478 -33.144 -44.426 1.00 31.14  ? 52  ILE   D C    1 
ATOM   5821 O  O    . ILE   D 1 52  ? -10.119 -33.033 -43.236 1.00 31.65  ? 52  ILE   D O    1 
ATOM   5822 C  CB   . ILE   D 1 52  ? -12.574 -31.746 -44.869 1.00 30.66  ? 52  ILE   D CB   1 
ATOM   5823 C  CG1  . ILE   D 1 52  ? -14.044 -31.738 -45.310 1.00 32.46  ? 52  ILE   D CG1  1 
ATOM   5824 C  CG2  . ILE   D 1 52  ? -11.729 -30.901 -45.809 1.00 30.83  ? 52  ILE   D CG2  1 
ATOM   5825 C  CD1  . ILE   D 1 52  ? -15.054 -31.780 -44.190 1.00 33.24  ? 52  ILE   D CD1  1 
ATOM   5826 N  N    . ILE   D 1 53  ? -9.629  -33.293 -45.437 1.00 29.33  ? 53  ILE   D N    1 
ATOM   5827 C  CA   . ILE   D 1 53  ? -8.158  -33.155 -45.283 1.00 30.54  ? 53  ILE   D CA   1 
ATOM   5828 C  C    . ILE   D 1 53  ? -7.654  -32.333 -46.457 1.00 30.99  ? 53  ILE   D C    1 
ATOM   5829 O  O    . ILE   D 1 53  ? -8.171  -32.510 -47.558 1.00 34.60  ? 53  ILE   D O    1 
ATOM   5830 C  CB   . ILE   D 1 53  ? -7.454  -34.525 -45.188 1.00 31.76  ? 53  ILE   D CB   1 
ATOM   5831 C  CG1  . ILE   D 1 53  ? -7.521  -35.093 -43.770 1.00 33.33  ? 53  ILE   D CG1  1 
ATOM   5832 C  CG2  . ILE   D 1 53  ? -6.013  -34.421 -45.667 1.00 34.60  ? 53  ILE   D CG2  1 
ATOM   5833 C  CD1  . ILE   D 1 53  ? -7.195  -36.567 -43.668 1.00 35.75  ? 53  ILE   D CD1  1 
ATOM   5834 N  N    . TYR   D 1 54  ? -6.707  -31.444 -46.199 1.00 32.49  ? 54  TYR   D N    1 
ATOM   5835 C  CA   . TYR   D 1 54  ? -5.918  -30.728 -47.221 1.00 35.69  ? 54  TYR   D CA   1 
ATOM   5836 C  C    . TYR   D 1 54  ? -4.463  -30.914 -46.825 1.00 38.80  ? 54  TYR   D C    1 
ATOM   5837 O  O    . TYR   D 1 54  ? -4.124  -30.600 -45.668 1.00 37.33  ? 54  TYR   D O    1 
ATOM   5838 C  CB   . TYR   D 1 54  ? -6.284  -29.242 -47.317 1.00 34.55  ? 54  TYR   D CB   1 
ATOM   5839 C  CG   . TYR   D 1 54  ? -5.477  -28.492 -48.349 1.00 35.13  ? 54  TYR   D CG   1 
ATOM   5840 C  CD1  . TYR   D 1 54  ? -5.843  -28.511 -49.686 1.00 36.46  ? 54  TYR   D CD1  1 
ATOM   5841 C  CD2  . TYR   D 1 54  ? -4.330  -27.793 -48.008 1.00 35.79  ? 54  TYR   D CD2  1 
ATOM   5842 C  CE1  . TYR   D 1 54  ? -5.115  -27.832 -50.650 1.00 35.43  ? 54  TYR   D CE1  1 
ATOM   5843 C  CE2  . TYR   D 1 54  ? -3.583  -27.113 -48.959 1.00 35.78  ? 54  TYR   D CE2  1 
ATOM   5844 C  CZ   . TYR   D 1 54  ? -3.975  -27.136 -50.290 1.00 35.93  ? 54  TYR   D CZ   1 
ATOM   5845 O  OH   . TYR   D 1 54  ? -3.260  -26.477 -51.249 1.00 33.62  ? 54  TYR   D OH   1 
ATOM   5846 N  N    . ASN   D 1 55  ? -3.679  -31.338 -47.806 1.00 44.09  ? 55  ASN   D N    1 
ATOM   5847 C  CA   . ASN   D 1 55  ? -2.253  -31.693 -47.672 1.00 49.05  ? 55  ASN   D CA   1 
ATOM   5848 C  C    . ASN   D 1 55  ? -1.460  -30.687 -48.508 1.00 54.59  ? 55  ASN   D C    1 
ATOM   5849 O  O    . ASN   D 1 55  ? -1.567  -30.740 -49.720 1.00 58.57  ? 55  ASN   D O    1 
ATOM   5850 C  CB   . ASN   D 1 55  ? -2.133  -33.159 -48.085 1.00 50.97  ? 55  ASN   D CB   1 
ATOM   5851 C  CG   . ASN   D 1 55  ? -0.723  -33.625 -48.315 1.00 47.74  ? 55  ASN   D CG   1 
ATOM   5852 O  OD1  . ASN   D 1 55  ? 0.144   -32.857 -48.678 1.00 47.56  ? 55  ASN   D OD1  1 
ATOM   5853 N  ND2  . ASN   D 1 55  ? -0.492  -34.888 -48.082 1.00 50.32  ? 55  ASN   D ND2  1 
ATOM   5854 N  N    . SER   D 1 56  ? -0.660  -29.841 -47.870 1.00 58.10  ? 56  SER   D N    1 
ATOM   5855 C  CA   . SER   D 1 56  ? 0.056   -28.752 -48.579 1.00 59.08  ? 56  SER   D CA   1 
ATOM   5856 C  C    . SER   D 1 56  ? 1.207   -29.292 -49.441 1.00 55.18  ? 56  SER   D C    1 
ATOM   5857 O  O    . SER   D 1 56  ? 1.856   -28.472 -50.103 1.00 51.83  ? 56  SER   D O    1 
ATOM   5858 C  CB   . SER   D 1 56  ? 0.567   -27.755 -47.566 1.00 59.77  ? 56  SER   D CB   1 
ATOM   5859 O  OG   . SER   D 1 56  ? 1.125   -28.422 -46.443 1.00 61.00  ? 56  SER   D OG   1 
ATOM   5860 N  N    . VAL   D 1 57  ? 1.503   -30.594 -49.391 1.00 55.47  ? 57  VAL   D N    1 
ATOM   5861 C  CA   . VAL   D 1 57  ? 2.617   -31.192 -50.184 1.00 59.07  ? 57  VAL   D CA   1 
ATOM   5862 C  C    . VAL   D 1 57  ? 2.009   -31.760 -51.473 1.00 56.60  ? 57  VAL   D C    1 
ATOM   5863 O  O    . VAL   D 1 57  ? 2.456   -31.336 -52.548 1.00 59.73  ? 57  VAL   D O    1 
ATOM   5864 C  CB   . VAL   D 1 57  ? 3.427   -32.219 -49.365 1.00 61.81  ? 57  VAL   D CB   1 
ATOM   5865 C  CG1  . VAL   D 1 57  ? 4.454   -32.953 -50.220 1.00 64.00  ? 57  VAL   D CG1  1 
ATOM   5866 C  CG2  . VAL   D 1 57  ? 4.113   -31.560 -48.175 1.00 57.87  ? 57  VAL   D CG2  1 
ATOM   5867 N  N    . ASP   D 1 58  ? 0.976   -32.605 -51.368 1.00 55.51  ? 58  ASP   D N    1 
ATOM   5868 C  CA   . ASP   D 1 58  ? 0.191   -33.140 -52.520 1.00 51.06  ? 58  ASP   D CA   1 
ATOM   5869 C  C    . ASP   D 1 58  ? -0.682  -32.030 -53.129 1.00 48.60  ? 58  ASP   D C    1 
ATOM   5870 O  O    . ASP   D 1 58  ? -1.042  -32.170 -54.299 1.00 50.69  ? 58  ASP   D O    1 
ATOM   5871 C  CB   . ASP   D 1 58  ? -0.670  -34.347 -52.121 1.00 51.29  ? 58  ASP   D CB   1 
ATOM   5872 C  CG   . ASP   D 1 58  ? 0.074   -35.449 -51.366 1.00 55.08  ? 58  ASP   D CG   1 
ATOM   5873 O  OD1  . ASP   D 1 58  ? 1.245   -35.231 -50.975 1.00 51.86  ? 58  ASP   D OD1  1 
ATOM   5874 O  OD2  . ASP   D 1 58  ? -0.527  -36.522 -51.157 1.00 54.56  ? 58  ASP   D OD2  1 
ATOM   5875 N  N    . LYS   D 1 59  ? -1.013  -30.978 -52.366 1.00 50.83  ? 59  LYS   D N    1 
ATOM   5876 C  CA   . LYS   D 1 59  ? -1.898  -29.834 -52.757 1.00 49.51  ? 59  LYS   D CA   1 
ATOM   5877 C  C    . LYS   D 1 59  ? -3.282  -30.364 -53.161 1.00 46.03  ? 59  LYS   D C    1 
ATOM   5878 O  O    . LYS   D 1 59  ? -3.875  -29.844 -54.125 1.00 43.04  ? 59  LYS   D O    1 
ATOM   5879 C  CB   . LYS   D 1 59  ? -1.260  -28.983 -53.861 1.00 49.54  ? 59  LYS   D CB   1 
ATOM   5880 C  CG   . LYS   D 1 59  ? 0.072   -28.333 -53.503 1.00 52.53  ? 59  LYS   D CG   1 
ATOM   5881 C  CD   . LYS   D 1 59  ? -0.039  -27.261 -52.434 1.00 58.00  ? 59  LYS   D CD   1 
ATOM   5882 C  CE   . LYS   D 1 59  ? 1.240   -26.474 -52.217 1.00 60.34  ? 59  LYS   D CE   1 
ATOM   5883 N  NZ   . LYS   D 1 59  ? 1.731   -25.832 -53.457 1.00 65.67  ? 59  LYS   D NZ   1 
ATOM   5884 N  N    . ARG   D 1 60  ? -3.788  -31.331 -52.399 1.00 46.87  ? 60  ARG   D N    1 
ATOM   5885 C  CA   . ARG   D 1 60  ? -5.031  -32.093 -52.674 1.00 48.19  ? 60  ARG   D CA   1 
ATOM   5886 C  C    . ARG   D 1 60  ? -6.020  -31.872 -51.528 1.00 43.22  ? 60  ARG   D C    1 
ATOM   5887 O  O    . ARG   D 1 60  ? -5.608  -32.006 -50.368 1.00 39.81  ? 60  ARG   D O    1 
ATOM   5888 C  CB   . ARG   D 1 60  ? -4.678  -33.577 -52.788 1.00 59.52  ? 60  ARG   D CB   1 
ATOM   5889 C  CG   . ARG   D 1 60  ? -5.799  -34.469 -53.302 1.00 66.88  ? 60  ARG   D CG   1 
ATOM   5890 C  CD   . ARG   D 1 60  ? -5.356  -35.921 -53.372 1.00 71.17  ? 60  ARG   D CD   1 
ATOM   5891 N  NE   . ARG   D 1 60  ? -5.653  -36.492 -54.679 1.00 76.29  ? 60  ARG   D NE   1 
ATOM   5892 C  CZ   . ARG   D 1 60  ? -4.751  -36.886 -55.578 1.00 77.86  ? 60  ARG   D CZ   1 
ATOM   5893 N  NH1  . ARG   D 1 60  ? -5.164  -37.382 -56.733 1.00 82.40  ? 60  ARG   D NH1  1 
ATOM   5894 N  NH2  . ARG   D 1 60  ? -3.454  -36.801 -55.328 1.00 74.22  ? 60  ARG   D NH2  1 
ATOM   5895 N  N    . LEU   D 1 61  ? -7.270  -31.538 -51.848 1.00 38.71  ? 61  LEU   D N    1 
ATOM   5896 C  CA   . LEU   D 1 61  ? -8.376  -31.407 -50.869 1.00 36.55  ? 61  LEU   D CA   1 
ATOM   5897 C  C    . LEU   D 1 61  ? -9.302  -32.611 -51.047 1.00 35.77  ? 61  LEU   D C    1 
ATOM   5898 O  O    . LEU   D 1 61  ? -9.920  -32.712 -52.105 1.00 34.91  ? 61  LEU   D O    1 
ATOM   5899 C  CB   . LEU   D 1 61  ? -9.112  -30.081 -51.095 1.00 36.74  ? 61  LEU   D CB   1 
ATOM   5900 C  CG   . LEU   D 1 61  ? -10.292 -29.789 -50.167 1.00 36.32  ? 61  LEU   D CG   1 
ATOM   5901 C  CD1  . LEU   D 1 61  ? -9.843  -29.637 -48.722 1.00 38.55  ? 61  LEU   D CD1  1 
ATOM   5902 C  CD2  . LEU   D 1 61  ? -11.013 -28.530 -50.609 1.00 36.83  ? 61  LEU   D CD2  1 
ATOM   5903 N  N    . SER   D 1 62  ? -9.389  -33.458 -50.021 1.00 35.52  ? 62  SER   D N    1 
ATOM   5904 C  CA   . SER   D 1 62  ? -10.195 -34.703 -49.955 1.00 35.89  ? 62  SER   D CA   1 
ATOM   5905 C  C    . SER   D 1 62  ? -11.275 -34.549 -48.889 1.00 35.00  ? 62  SER   D C    1 
ATOM   5906 O  O    . SER   D 1 62  ? -11.065 -33.770 -47.957 1.00 40.32  ? 62  SER   D O    1 
ATOM   5907 C  CB   . SER   D 1 62  ? -9.314  -35.875 -49.633 1.00 37.44  ? 62  SER   D CB   1 
ATOM   5908 O  OG   . SER   D 1 62  ? -8.003  -35.653 -50.140 1.00 45.34  ? 62  SER   D OG   1 
ATOM   5909 N  N    . ALA   D 1 63  ? -12.354 -35.307 -49.011 1.00 33.35  ? 63  ALA   D N    1 
ATOM   5910 C  CA   . ALA   D 1 63  ? -13.452 -35.402 -48.033 1.00 34.16  ? 63  ALA   D CA   1 
ATOM   5911 C  C    . ALA   D 1 63  ? -14.019 -36.824 -48.076 1.00 38.95  ? 63  ALA   D C    1 
ATOM   5912 O  O    . ALA   D 1 63  ? -14.022 -37.427 -49.166 1.00 42.18  ? 63  ALA   D O    1 
ATOM   5913 C  CB   . ALA   D 1 63  ? -14.509 -34.390 -48.357 1.00 35.85  ? 63  ALA   D CB   1 
ATOM   5914 N  N    . VAL   D 1 64  ? -14.463 -37.333 -46.925 1.00 40.50  ? 64  VAL   D N    1 
ATOM   5915 C  CA   . VAL   D 1 64  ? -15.071 -38.683 -46.751 1.00 37.33  ? 64  VAL   D CA   1 
ATOM   5916 C  C    . VAL   D 1 64  ? -16.316 -38.496 -45.885 1.00 37.15  ? 64  VAL   D C    1 
ATOM   5917 O  O    . VAL   D 1 64  ? -16.182 -38.107 -44.709 1.00 39.89  ? 64  VAL   D O    1 
ATOM   5918 C  CB   . VAL   D 1 64  ? -14.097 -39.689 -46.100 1.00 37.83  ? 64  VAL   D CB   1 
ATOM   5919 C  CG1  . VAL   D 1 64  ? -14.720 -41.072 -45.967 1.00 36.88  ? 64  VAL   D CG1  1 
ATOM   5920 C  CG2  . VAL   D 1 64  ? -12.761 -39.758 -46.828 1.00 39.91  ? 64  VAL   D CG2  1 
ATOM   5921 N  N    . VAL   D 1 65  ? -17.490 -38.733 -46.447 1.00 33.25  ? 65  VAL   D N    1 
ATOM   5922 C  CA   . VAL   D 1 65  ? -18.747 -38.758 -45.660 1.00 32.22  ? 65  VAL   D CA   1 
ATOM   5923 C  C    . VAL   D 1 65  ? -19.190 -40.220 -45.569 1.00 32.61  ? 65  VAL   D C    1 
ATOM   5924 O  O    . VAL   D 1 65  ? -19.151 -40.933 -46.589 1.00 31.14  ? 65  VAL   D O    1 
ATOM   5925 C  CB   . VAL   D 1 65  ? -19.816 -37.842 -46.273 1.00 31.88  ? 65  VAL   D CB   1 
ATOM   5926 C  CG1  . VAL   D 1 65  ? -20.995 -37.685 -45.326 1.00 31.53  ? 65  VAL   D CG1  1 
ATOM   5927 C  CG2  . VAL   D 1 65  ? -19.226 -36.484 -46.646 1.00 31.76  ? 65  VAL   D CG2  1 
ATOM   5928 N  N    . SER   D 1 66  ? -19.555 -40.639 -44.367 1.00 33.09  ? 66  SER   D N    1 
ATOM   5929 C  CA   . SER   D 1 66  ? -19.758 -42.055 -43.999 1.00 37.51  ? 66  SER   D CA   1 
ATOM   5930 C  C    . SER   D 1 66  ? -20.870 -42.146 -42.962 1.00 36.73  ? 66  SER   D C    1 
ATOM   5931 O  O    . SER   D 1 66  ? -21.245 -41.109 -42.376 1.00 34.78  ? 66  SER   D O    1 
ATOM   5932 C  CB   . SER   D 1 66  ? -18.467 -42.681 -43.514 1.00 40.42  ? 66  SER   D CB   1 
ATOM   5933 O  OG   . SER   D 1 66  ? -17.783 -41.812 -42.626 1.00 42.26  ? 66  SER   D OG   1 
ATOM   5934 N  N    . TYR   D 1 67  ? -21.402 -43.356 -42.817 1.00 37.08  ? 67  TYR   D N    1 
ATOM   5935 C  CA   . TYR   D 1 67  ? -22.527 -43.724 -41.928 1.00 35.56  ? 67  TYR   D CA   1 
ATOM   5936 C  C    . TYR   D 1 67  ? -22.228 -45.095 -41.322 1.00 36.26  ? 67  TYR   D C    1 
ATOM   5937 O  O    . TYR   D 1 67  ? -21.519 -45.894 -41.929 1.00 29.99  ? 67  TYR   D O    1 
ATOM   5938 C  CB   . TYR   D 1 67  ? -23.811 -43.747 -42.751 1.00 36.01  ? 67  TYR   D CB   1 
ATOM   5939 C  CG   . TYR   D 1 67  ? -24.460 -42.413 -43.000 1.00 36.00  ? 67  TYR   D CG   1 
ATOM   5940 C  CD1  . TYR   D 1 67  ? -25.142 -41.779 -41.978 1.00 34.66  ? 67  TYR   D CD1  1 
ATOM   5941 C  CD2  . TYR   D 1 67  ? -24.455 -41.820 -44.258 1.00 35.12  ? 67  TYR   D CD2  1 
ATOM   5942 C  CE1  . TYR   D 1 67  ? -25.767 -40.566 -42.181 1.00 34.67  ? 67  TYR   D CE1  1 
ATOM   5943 C  CE2  . TYR   D 1 67  ? -25.097 -40.612 -44.482 1.00 34.50  ? 67  TYR   D CE2  1 
ATOM   5944 C  CZ   . TYR   D 1 67  ? -25.754 -39.987 -43.436 1.00 33.95  ? 67  TYR   D CZ   1 
ATOM   5945 O  OH   . TYR   D 1 67  ? -26.414 -38.807 -43.584 1.00 34.41  ? 67  TYR   D OH   1 
ATOM   5946 N  N    . PRO   D 1 68  ? -22.724 -45.410 -40.103 1.00 42.44  ? 68  PRO   D N    1 
ATOM   5947 C  CA   . PRO   D 1 68  ? -22.510 -46.736 -39.512 1.00 44.23  ? 68  PRO   D CA   1 
ATOM   5948 C  C    . PRO   D 1 68  ? -23.055 -47.846 -40.429 1.00 44.22  ? 68  PRO   D C    1 
ATOM   5949 O  O    . PRO   D 1 68  ? -24.197 -47.742 -40.849 1.00 44.25  ? 68  PRO   D O    1 
ATOM   5950 C  CB   . PRO   D 1 68  ? -23.283 -46.703 -38.178 1.00 43.96  ? 68  PRO   D CB   1 
ATOM   5951 C  CG   . PRO   D 1 68  ? -23.479 -45.218 -37.881 1.00 46.96  ? 68  PRO   D CG   1 
ATOM   5952 C  CD   . PRO   D 1 68  ? -23.521 -44.527 -39.232 1.00 43.61  ? 68  PRO   D CD   1 
ATOM   5953 N  N    . ASN   D 1 69  ? -22.216 -48.840 -40.757 1.00 47.64  ? 69  ASN   D N    1 
ATOM   5954 C  CA   . ASN   D 1 69  ? -22.585 -50.079 -41.511 1.00 47.47  ? 69  ASN   D CA   1 
ATOM   5955 C  C    . ASN   D 1 69  ? -23.169 -49.710 -42.890 1.00 50.77  ? 69  ASN   D C    1 
ATOM   5956 O  O    . ASN   D 1 69  ? -24.212 -50.296 -43.281 1.00 49.79  ? 69  ASN   D O    1 
ATOM   5957 C  CB   . ASN   D 1 69  ? -23.525 -50.964 -40.684 1.00 43.16  ? 69  ASN   D CB   1 
ATOM   5958 C  CG   . ASN   D 1 69  ? -22.862 -51.593 -39.474 1.00 40.61  ? 69  ASN   D CG   1 
ATOM   5959 O  OD1  . ASN   D 1 69  ? -21.630 -51.593 -39.355 1.00 34.92  ? 69  ASN   D OD1  1 
ATOM   5960 N  ND2  . ASN   D 1 69  ? -23.676 -52.144 -38.580 1.00 37.58  ? 69  ASN   D ND2  1 
ATOM   5961 N  N    . ALA   D 1 70  ? -22.509 -48.773 -43.592 1.00 50.83  ? 70  ALA   D N    1 
ATOM   5962 C  CA   . ALA   D 1 70  ? -22.837 -48.298 -44.958 1.00 50.33  ? 70  ALA   D CA   1 
ATOM   5963 C  C    . ALA   D 1 70  ? -21.541 -47.869 -45.669 1.00 52.00  ? 70  ALA   D C    1 
ATOM   5964 O  O    . ALA   D 1 70  ? -20.477 -47.815 -45.006 1.00 49.16  ? 70  ALA   D O    1 
ATOM   5965 C  CB   . ALA   D 1 70  ? -23.860 -47.190 -44.882 1.00 48.24  ? 70  ALA   D CB   1 
ATOM   5966 N  N    . ASP   D 1 71  ? -21.599 -47.613 -46.979 1.00 57.75  ? 71  ASP   D N    1 
ATOM   5967 C  CA   . ASP   D 1 71  ? -20.400 -47.263 -47.797 1.00 63.31  ? 71  ASP   D CA   1 
ATOM   5968 C  C    . ASP   D 1 71  ? -20.053 -45.777 -47.615 1.00 60.27  ? 71  ASP   D C    1 
ATOM   5969 O  O    . ASP   D 1 71  ? -20.921 -44.990 -47.168 1.00 53.69  ? 71  ASP   D O    1 
ATOM   5970 C  CB   . ASP   D 1 71  ? -20.592 -47.607 -49.280 1.00 68.50  ? 71  ASP   D CB   1 
ATOM   5971 C  CG   . ASP   D 1 71  ? -20.128 -49.005 -49.666 1.00 71.64  ? 71  ASP   D CG   1 
ATOM   5972 O  OD1  . ASP   D 1 71  ? -19.608 -49.724 -48.783 1.00 72.37  ? 71  ASP   D OD1  1 
ATOM   5973 O  OD2  . ASP   D 1 71  ? -20.276 -49.361 -50.855 1.00 71.71  ? 71  ASP   D OD2  1 
ATOM   5974 N  N    . SER   D 1 72  ? -18.812 -45.422 -47.946 1.00 58.55  ? 72  SER   D N    1 
ATOM   5975 C  CA   . SER   D 1 72  ? -18.243 -44.060 -47.795 1.00 55.68  ? 72  SER   D CA   1 
ATOM   5976 C  C    . SER   D 1 72  ? -18.148 -43.392 -49.164 1.00 53.57  ? 72  SER   D C    1 
ATOM   5977 O  O    . SER   D 1 72  ? -17.414 -43.910 -50.034 1.00 54.42  ? 72  SER   D O    1 
ATOM   5978 C  CB   . SER   D 1 72  ? -16.901 -44.110 -47.135 1.00 50.07  ? 72  SER   D CB   1 
ATOM   5979 O  OG   . SER   D 1 72  ? -17.014 -44.785 -45.898 1.00 53.97  ? 72  SER   D OG   1 
ATOM   5980 N  N    . ALA   D 1 73  ? -18.851 -42.275 -49.332 1.00 48.27  ? 73  ALA   D N    1 
ATOM   5981 C  CA   . ALA   D 1 73  ? -18.651 -41.344 -50.462 1.00 46.52  ? 73  ALA   D CA   1 
ATOM   5982 C  C    . ALA   D 1 73  ? -17.386 -40.541 -50.168 1.00 43.49  ? 73  ALA   D C    1 
ATOM   5983 O  O    . ALA   D 1 73  ? -17.253 -40.069 -49.023 1.00 44.25  ? 73  ALA   D O    1 
ATOM   5984 C  CB   . ALA   D 1 73  ? -19.867 -40.466 -50.633 1.00 45.94  ? 73  ALA   D CB   1 
ATOM   5985 N  N    . THR   D 1 74  ? -16.473 -40.453 -51.136 1.00 42.65  ? 74  THR   D N    1 
ATOM   5986 C  CA   . THR   D 1 74  ? -15.246 -39.617 -51.067 1.00 44.95  ? 74  THR   D CA   1 
ATOM   5987 C  C    . THR   D 1 74  ? -15.108 -38.809 -52.353 1.00 44.10  ? 74  THR   D C    1 
ATOM   5988 O  O    . THR   D 1 74  ? -15.548 -39.288 -53.408 1.00 45.49  ? 74  THR   D O    1 
ATOM   5989 C  CB   . THR   D 1 74  ? -13.963 -40.433 -50.849 1.00 47.60  ? 74  THR   D CB   1 
ATOM   5990 O  OG1  . THR   D 1 74  ? -13.681 -41.142 -52.051 1.00 53.72  ? 74  THR   D OG1  1 
ATOM   5991 C  CG2  . THR   D 1 74  ? -14.060 -41.406 -49.696 1.00 49.79  ? 74  THR   D CG2  1 
ATOM   5992 N  N    . VAL   D 1 75  ? -14.490 -37.633 -52.257 1.00 44.64  ? 75  VAL   D N    1 
ATOM   5993 C  CA   . VAL   D 1 75  ? -14.237 -36.735 -53.417 1.00 42.87  ? 75  VAL   D CA   1 
ATOM   5994 C  C    . VAL   D 1 75  ? -12.886 -36.050 -53.202 1.00 43.82  ? 75  VAL   D C    1 
ATOM   5995 O  O    . VAL   D 1 75  ? -12.559 -35.786 -52.036 1.00 45.38  ? 75  VAL   D O    1 
ATOM   5996 C  CB   . VAL   D 1 75  ? -15.413 -35.750 -53.572 1.00 44.85  ? 75  VAL   D CB   1 
ATOM   5997 C  CG1  . VAL   D 1 75  ? -15.435 -34.685 -52.481 1.00 46.60  ? 75  VAL   D CG1  1 
ATOM   5998 C  CG2  . VAL   D 1 75  ? -15.433 -35.112 -54.947 1.00 45.80  ? 75  VAL   D CG2  1 
ATOM   5999 N  N    . SER   D 1 76  ? -12.130 -35.809 -54.280 1.00 46.50  ? 76  SER   D N    1 
ATOM   6000 C  CA   . SER   D 1 76  ? -10.782 -35.172 -54.281 1.00 46.47  ? 76  SER   D CA   1 
ATOM   6001 C  C    . SER   D 1 76  ? -10.729 -34.041 -55.308 1.00 46.56  ? 76  SER   D C    1 
ATOM   6002 O  O    . SER   D 1 76  ? -11.595 -34.011 -56.183 1.00 52.60  ? 76  SER   D O    1 
ATOM   6003 C  CB   . SER   D 1 76  ? -9.703  -36.163 -54.584 1.00 45.52  ? 76  SER   D CB   1 
ATOM   6004 O  OG   . SER   D 1 76  ? -9.635  -37.142 -53.572 1.00 49.52  ? 76  SER   D OG   1 
ATOM   6005 N  N    . TYR   D 1 77  ? -9.734  -33.162 -55.199 1.00 45.98  ? 77  TYR   D N    1 
ATOM   6006 C  CA   . TYR   D 1 77  ? -9.434  -32.080 -56.171 1.00 50.31  ? 77  TYR   D CA   1 
ATOM   6007 C  C    . TYR   D 1 77  ? -8.100  -31.424 -55.799 1.00 52.36  ? 77  TYR   D C    1 
ATOM   6008 O  O    . TYR   D 1 77  ? -7.993  -30.880 -54.678 1.00 56.06  ? 77  TYR   D O    1 
ATOM   6009 C  CB   . TYR   D 1 77  ? -10.549 -31.026 -56.238 1.00 50.85  ? 77  TYR   D CB   1 
ATOM   6010 C  CG   . TYR   D 1 77  ? -10.352 -30.040 -57.366 1.00 56.94  ? 77  TYR   D CG   1 
ATOM   6011 C  CD1  . TYR   D 1 77  ? -10.317 -30.478 -58.684 1.00 59.03  ? 77  TYR   D CD1  1 
ATOM   6012 C  CD2  . TYR   D 1 77  ? -10.140 -28.687 -57.131 1.00 57.26  ? 77  TYR   D CD2  1 
ATOM   6013 C  CE1  . TYR   D 1 77  ? -10.097 -29.603 -59.736 1.00 58.91  ? 77  TYR   D CE1  1 
ATOM   6014 C  CE2  . TYR   D 1 77  ? -9.922  -27.798 -58.176 1.00 57.45  ? 77  TYR   D CE2  1 
ATOM   6015 C  CZ   . TYR   D 1 77  ? -9.899  -28.255 -59.487 1.00 59.43  ? 77  TYR   D CZ   1 
ATOM   6016 O  OH   . TYR   D 1 77  ? -9.675  -27.410 -60.545 1.00 53.79  ? 77  TYR   D OH   1 
ATOM   6017 N  N    . ASP   D 1 78  ? -7.123  -31.474 -56.711 1.00 51.47  ? 78  ASP   D N    1 
ATOM   6018 C  CA   . ASP   D 1 78  ? -5.813  -30.786 -56.573 1.00 52.44  ? 78  ASP   D CA   1 
ATOM   6019 C  C    . ASP   D 1 78  ? -6.047  -29.289 -56.754 1.00 50.02  ? 78  ASP   D C    1 
ATOM   6020 O  O    . ASP   D 1 78  ? -6.520  -28.904 -57.824 1.00 55.27  ? 78  ASP   D O    1 
ATOM   6021 C  CB   . ASP   D 1 78  ? -4.786  -31.271 -57.599 1.00 53.22  ? 78  ASP   D CB   1 
ATOM   6022 C  CG   . ASP   D 1 78  ? -4.580  -32.774 -57.608 1.00 57.08  ? 78  ASP   D CG   1 
ATOM   6023 O  OD1  . ASP   D 1 78  ? -5.166  -33.456 -56.741 1.00 52.86  ? 78  ASP   D OD1  1 
ATOM   6024 O  OD2  . ASP   D 1 78  ? -3.819  -33.249 -58.480 1.00 64.27  ? 78  ASP   D OD2  1 
ATOM   6025 N  N    . VAL   D 1 79  ? -5.748  -28.482 -55.741 1.00 50.08  ? 79  VAL   D N    1 
ATOM   6026 C  CA   . VAL   D 1 79  ? -5.810  -26.993 -55.846 1.00 54.28  ? 79  VAL   D CA   1 
ATOM   6027 C  C    . VAL   D 1 79  ? -4.686  -26.401 -54.989 1.00 52.68  ? 79  VAL   D C    1 
ATOM   6028 O  O    . VAL   D 1 79  ? -4.278  -27.034 -53.996 1.00 52.13  ? 79  VAL   D O    1 
ATOM   6029 C  CB   . VAL   D 1 79  ? -7.205  -26.440 -55.479 1.00 52.58  ? 79  VAL   D CB   1 
ATOM   6030 C  CG1  . VAL   D 1 79  ? -7.706  -26.964 -54.142 1.00 50.97  ? 79  VAL   D CG1  1 
ATOM   6031 C  CG2  . VAL   D 1 79  ? -7.246  -24.920 -55.519 1.00 52.24  ? 79  VAL   D CG2  1 
ATOM   6032 N  N    . ASP   D 1 80  ? -4.181  -25.249 -55.412 1.00 55.47  ? 80  ASP   D N    1 
ATOM   6033 C  CA   . ASP   D 1 80  ? -3.040  -24.532 -54.789 1.00 58.99  ? 80  ASP   D CA   1 
ATOM   6034 C  C    . ASP   D 1 80  ? -3.643  -23.342 -54.027 1.00 57.06  ? 80  ASP   D C    1 
ATOM   6035 O  O    . ASP   D 1 80  ? -3.860  -22.294 -54.664 1.00 55.55  ? 80  ASP   D O    1 
ATOM   6036 C  CB   . ASP   D 1 80  ? -2.034  -24.173 -55.888 1.00 62.55  ? 80  ASP   D CB   1 
ATOM   6037 C  CG   . ASP   D 1 80  ? -0.660  -23.764 -55.398 1.00 72.48  ? 80  ASP   D CG   1 
ATOM   6038 O  OD1  . ASP   D 1 80  ? -0.275  -24.201 -54.289 1.00 81.82  ? 80  ASP   D OD1  1 
ATOM   6039 O  OD2  . ASP   D 1 80  ? 0.015   -23.010 -56.133 1.00 75.94  ? 80  ASP   D OD2  1 
ATOM   6040 N  N    . LEU   D 1 81  ? -3.951  -23.513 -52.734 1.00 50.64  ? 81  LEU   D N    1 
ATOM   6041 C  CA   . LEU   D 1 81  ? -4.910  -22.648 -51.985 1.00 48.87  ? 81  LEU   D CA   1 
ATOM   6042 C  C    . LEU   D 1 81  ? -4.329  -21.249 -51.758 1.00 47.07  ? 81  LEU   D C    1 
ATOM   6043 O  O    . LEU   D 1 81  ? -5.116  -20.342 -51.445 1.00 42.91  ? 81  LEU   D O    1 
ATOM   6044 C  CB   . LEU   D 1 81  ? -5.305  -23.312 -50.660 1.00 49.06  ? 81  LEU   D CB   1 
ATOM   6045 C  CG   . LEU   D 1 81  ? -6.350  -24.427 -50.761 1.00 47.78  ? 81  LEU   D CG   1 
ATOM   6046 C  CD1  . LEU   D 1 81  ? -6.660  -24.998 -49.388 1.00 49.08  ? 81  LEU   D CD1  1 
ATOM   6047 C  CD2  . LEU   D 1 81  ? -7.628  -23.937 -51.427 1.00 47.87  ? 81  LEU   D CD2  1 
ATOM   6048 N  N    . ASP   D 1 82  ? -3.017  -21.078 -51.928 1.00 50.06  ? 82  ASP   D N    1 
ATOM   6049 C  CA   . ASP   D 1 82  ? -2.347  -19.749 -51.949 1.00 54.99  ? 82  ASP   D CA   1 
ATOM   6050 C  C    . ASP   D 1 82  ? -2.785  -18.952 -53.189 1.00 57.07  ? 82  ASP   D C    1 
ATOM   6051 O  O    . ASP   D 1 82  ? -2.649  -17.710 -53.147 1.00 59.40  ? 82  ASP   D O    1 
ATOM   6052 C  CB   . ASP   D 1 82  ? -0.820  -19.860 -51.848 1.00 59.79  ? 82  ASP   D CB   1 
ATOM   6053 C  CG   . ASP   D 1 82  ? -0.182  -21.088 -52.485 1.00 65.61  ? 82  ASP   D CG   1 
ATOM   6054 O  OD1  . ASP   D 1 82  ? -0.900  -22.101 -52.683 1.00 65.47  ? 82  ASP   D OD1  1 
ATOM   6055 O  OD2  . ASP   D 1 82  ? 1.047   -21.038 -52.743 1.00 70.04  ? 82  ASP   D OD2  1 
ATOM   6056 N  N    . ASN   D 1 83  ? -3.297  -19.627 -54.230 1.00 56.44  ? 83  ASN   D N    1 
ATOM   6057 C  CA   . ASN   D 1 83  ? -3.870  -19.007 -55.460 1.00 55.53  ? 83  ASN   D CA   1 
ATOM   6058 C  C    . ASN   D 1 83  ? -5.288  -18.487 -55.200 1.00 52.34  ? 83  ASN   D C    1 
ATOM   6059 O  O    . ASN   D 1 83  ? -5.744  -17.680 -56.025 1.00 62.44  ? 83  ASN   D O    1 
ATOM   6060 C  CB   . ASN   D 1 83  ? -3.987  -19.976 -56.647 1.00 58.05  ? 83  ASN   D CB   1 
ATOM   6061 C  CG   . ASN   D 1 83  ? -2.668  -20.410 -57.260 1.00 60.48  ? 83  ASN   D CG   1 
ATOM   6062 O  OD1  . ASN   D 1 83  ? -1.619  -19.827 -56.986 1.00 61.75  ? 83  ASN   D OD1  1 
ATOM   6063 N  ND2  . ASN   D 1 83  ? -2.717  -21.427 -58.110 1.00 54.97  ? 83  ASN   D ND2  1 
ATOM   6064 N  N    . VAL   D 1 84  ? -5.968  -18.936 -54.135 1.00 46.57  ? 84  VAL   D N    1 
ATOM   6065 C  CA   . VAL   D 1 84  ? -7.453  -18.817 -53.985 1.00 44.46  ? 84  VAL   D CA   1 
ATOM   6066 C  C    . VAL   D 1 84  ? -7.821  -17.939 -52.777 1.00 45.16  ? 84  VAL   D C    1 
ATOM   6067 O  O    . VAL   D 1 84  ? -8.568  -16.947 -52.961 1.00 45.60  ? 84  VAL   D O    1 
ATOM   6068 C  CB   . VAL   D 1 84  ? -8.096  -20.210 -53.842 1.00 45.54  ? 84  VAL   D CB   1 
ATOM   6069 C  CG1  . VAL   D 1 84  ? -9.606  -20.138 -53.941 1.00 49.13  ? 84  VAL   D CG1  1 
ATOM   6070 C  CG2  . VAL   D 1 84  ? -7.550  -21.203 -54.852 1.00 44.75  ? 84  VAL   D CG2  1 
ATOM   6071 N  N    . LEU   D 1 85  ? -7.366  -18.338 -51.584 1.00 41.12  ? 85  LEU   D N    1 
ATOM   6072 C  CA   . LEU   D 1 85  ? -7.784  -17.788 -50.267 1.00 38.99  ? 85  LEU   D CA   1 
ATOM   6073 C  C    . LEU   D 1 85  ? -6.817  -16.680 -49.844 1.00 37.40  ? 85  LEU   D C    1 
ATOM   6074 O  O    . LEU   D 1 85  ? -5.666  -16.667 -50.262 1.00 36.28  ? 85  LEU   D O    1 
ATOM   6075 C  CB   . LEU   D 1 85  ? -7.812  -18.934 -49.240 1.00 38.26  ? 85  LEU   D CB   1 
ATOM   6076 C  CG   . LEU   D 1 85  ? -8.987  -19.914 -49.344 1.00 36.87  ? 85  LEU   D CG   1 
ATOM   6077 C  CD1  . LEU   D 1 85  ? -8.753  -21.154 -48.500 1.00 36.96  ? 85  LEU   D CD1  1 
ATOM   6078 C  CD2  . LEU   D 1 85  ? -10.300 -19.254 -48.947 1.00 35.89  ? 85  LEU   D CD2  1 
ATOM   6079 N  N    . PRO   D 1 86  ? -7.245  -15.705 -49.004 1.00 36.80  ? 86  PRO   D N    1 
ATOM   6080 C  CA   . PRO   D 1 86  ? -6.312  -14.763 -48.384 1.00 36.19  ? 86  PRO   D CA   1 
ATOM   6081 C  C    . PRO   D 1 86  ? -5.373  -15.477 -47.395 1.00 39.24  ? 86  PRO   D C    1 
ATOM   6082 O  O    . PRO   D 1 86  ? -5.621  -16.644 -47.061 1.00 40.47  ? 86  PRO   D O    1 
ATOM   6083 C  CB   . PRO   D 1 86  ? -7.217  -13.760 -47.666 1.00 35.15  ? 86  PRO   D CB   1 
ATOM   6084 C  CG   . PRO   D 1 86  ? -8.493  -14.536 -47.409 1.00 37.21  ? 86  PRO   D CG   1 
ATOM   6085 C  CD   . PRO   D 1 86  ? -8.637  -15.454 -48.603 1.00 37.51  ? 86  PRO   D CD   1 
ATOM   6086 N  N    . GLU   D 1 87  ? -4.313  -14.785 -46.964 1.00 37.31  ? 87  GLU   D N    1 
ATOM   6087 C  CA   . GLU   D 1 87  ? -3.304  -15.318 -46.013 1.00 35.82  ? 87  GLU   D CA   1 
ATOM   6088 C  C    . GLU   D 1 87  ? -4.009  -15.793 -44.730 1.00 32.79  ? 87  GLU   D C    1 
ATOM   6089 O  O    . GLU   D 1 87  ? -3.661  -16.888 -44.226 1.00 31.98  ? 87  GLU   D O    1 
ATOM   6090 C  CB   . GLU   D 1 87  ? -2.246  -14.252 -45.738 1.00 39.49  ? 87  GLU   D CB   1 
ATOM   6091 C  CG   . GLU   D 1 87  ? -0.924  -14.854 -45.319 1.00 45.02  ? 87  GLU   D CG   1 
ATOM   6092 C  CD   . GLU   D 1 87  ? 0.154   -13.859 -44.925 1.00 50.25  ? 87  GLU   D CD   1 
ATOM   6093 O  OE1  . GLU   D 1 87  ? -0.077  -12.641 -45.109 1.00 50.19  ? 87  GLU   D OE1  1 
ATOM   6094 O  OE2  . GLU   D 1 87  ? 1.223   -14.310 -44.440 1.00 48.33  ? 87  GLU   D OE2  1 
ATOM   6095 N  N    . TRP   D 1 88  ? -4.983  -15.019 -44.238 1.00 27.93  ? 88  TRP   D N    1 
ATOM   6096 C  CA   . TRP   D 1 88  ? -5.769  -15.304 -43.012 1.00 26.19  ? 88  TRP   D CA   1 
ATOM   6097 C  C    . TRP   D 1 88  ? -7.226  -15.576 -43.390 1.00 26.08  ? 88  TRP   D C    1 
ATOM   6098 O  O    . TRP   D 1 88  ? -7.769  -14.840 -44.250 1.00 24.91  ? 88  TRP   D O    1 
ATOM   6099 C  CB   . TRP   D 1 88  ? -5.661  -14.140 -42.011 1.00 26.92  ? 88  TRP   D CB   1 
ATOM   6100 C  CG   . TRP   D 1 88  ? -4.310  -14.054 -41.382 1.00 25.98  ? 88  TRP   D CG   1 
ATOM   6101 C  CD1  . TRP   D 1 88  ? -3.211  -13.456 -41.919 1.00 25.54  ? 88  TRP   D CD1  1 
ATOM   6102 C  CD2  . TRP   D 1 88  ? -3.881  -14.669 -40.153 1.00 25.60  ? 88  TRP   D CD2  1 
ATOM   6103 N  NE1  . TRP   D 1 88  ? -2.138  -13.616 -41.087 1.00 25.53  ? 88  TRP   D NE1  1 
ATOM   6104 C  CE2  . TRP   D 1 88  ? -2.514  -14.353 -39.993 1.00 26.24  ? 88  TRP   D CE2  1 
ATOM   6105 C  CE3  . TRP   D 1 88  ? -4.510  -15.433 -39.166 1.00 25.17  ? 88  TRP   D CE3  1 
ATOM   6106 C  CZ2  . TRP   D 1 88  ? -1.770  -14.783 -38.897 1.00 25.33  ? 88  TRP   D CZ2  1 
ATOM   6107 C  CZ3  . TRP   D 1 88  ? -3.782  -15.844 -38.072 1.00 26.23  ? 88  TRP   D CZ3  1 
ATOM   6108 C  CH2  . TRP   D 1 88  ? -2.428  -15.524 -37.943 1.00 27.55  ? 88  TRP   D CH2  1 
ATOM   6109 N  N    . VAL   D 1 89  ? -7.850  -16.546 -42.707 1.00 24.87  ? 89  VAL   D N    1 
ATOM   6110 C  CA   . VAL   D 1 89  ? -9.242  -16.999 -42.989 1.00 24.48  ? 89  VAL   D CA   1 
ATOM   6111 C  C    . VAL   D 1 89  ? -9.981  -17.311 -41.682 1.00 23.82  ? 89  VAL   D C    1 
ATOM   6112 O  O    . VAL   D 1 89  ? -9.343  -17.451 -40.649 1.00 24.70  ? 89  VAL   D O    1 
ATOM   6113 C  CB   . VAL   D 1 89  ? -9.196  -18.239 -43.896 1.00 23.46  ? 89  VAL   D CB   1 
ATOM   6114 C  CG1  . VAL   D 1 89  ? -8.513  -17.939 -45.220 1.00 24.09  ? 89  VAL   D CG1  1 
ATOM   6115 C  CG2  . VAL   D 1 89  ? -8.512  -19.399 -43.199 1.00 24.19  ? 89  VAL   D CG2  1 
ATOM   6116 N  N    . ARG   D 1 90  ? -11.296 -17.451 -41.750 1.00 23.84  ? 90  ARG   D N    1 
ATOM   6117 C  CA   . ARG   D 1 90  ? -12.066 -18.180 -40.725 1.00 24.83  ? 90  ARG   D CA   1 
ATOM   6118 C  C    . ARG   D 1 90  ? -12.612 -19.471 -41.329 1.00 24.90  ? 90  ARG   D C    1 
ATOM   6119 O  O    . ARG   D 1 90  ? -12.943 -19.498 -42.527 1.00 25.38  ? 90  ARG   D O    1 
ATOM   6120 C  CB   . ARG   D 1 90  ? -13.163 -17.308 -40.128 1.00 24.08  ? 90  ARG   D CB   1 
ATOM   6121 C  CG   . ARG   D 1 90  ? -12.673 -16.532 -38.916 1.00 25.37  ? 90  ARG   D CG   1 
ATOM   6122 C  CD   . ARG   D 1 90  ? -13.745 -15.595 -38.427 1.00 26.09  ? 90  ARG   D CD   1 
ATOM   6123 N  NE   . ARG   D 1 90  ? -13.365 -15.017 -37.158 1.00 27.49  ? 90  ARG   D NE   1 
ATOM   6124 C  CZ   . ARG   D 1 90  ? -13.251 -13.713 -36.919 1.00 30.56  ? 90  ARG   D CZ   1 
ATOM   6125 N  NH1  . ARG   D 1 90  ? -13.500 -12.824 -37.870 1.00 30.35  ? 90  ARG   D NH1  1 
ATOM   6126 N  NH2  . ARG   D 1 90  ? -12.926 -13.302 -35.703 1.00 30.30  ? 90  ARG   D NH2  1 
ATOM   6127 N  N    . VAL   D 1 91  ? -12.661 -20.501 -40.498 1.00 23.81  ? 91  VAL   D N    1 
ATOM   6128 C  CA   . VAL   D 1 91  ? -13.267 -21.819 -40.820 1.00 24.55  ? 91  VAL   D CA   1 
ATOM   6129 C  C    . VAL   D 1 91  ? -14.640 -21.876 -40.144 1.00 23.73  ? 91  VAL   D C    1 
ATOM   6130 O  O    . VAL   D 1 91  ? -14.822 -21.264 -39.061 1.00 21.52  ? 91  VAL   D O    1 
ATOM   6131 C  CB   . VAL   D 1 91  ? -12.322 -22.951 -40.382 1.00 25.77  ? 91  VAL   D CB   1 
ATOM   6132 C  CG1  . VAL   D 1 91  ? -10.960 -22.777 -41.036 1.00 25.98  ? 91  VAL   D CG1  1 
ATOM   6133 C  CG2  . VAL   D 1 91  ? -12.191 -23.053 -38.863 1.00 24.67  ? 91  VAL   D CG2  1 
ATOM   6134 N  N    . GLY   D 1 92  ? -15.581 -22.575 -40.767 1.00 23.36  ? 92  GLY   D N    1 
ATOM   6135 C  CA   . GLY   D 1 92  ? -16.979 -22.576 -40.322 1.00 22.73  ? 92  GLY   D CA   1 
ATOM   6136 C  C    . GLY   D 1 92  ? -17.788 -23.702 -40.929 1.00 21.72  ? 92  GLY   D C    1 
ATOM   6137 O  O    . GLY   D 1 92  ? -17.299 -24.415 -41.842 1.00 19.94  ? 92  GLY   D O    1 
ATOM   6138 N  N    . LEU   D 1 93  ? -19.010 -23.801 -40.427 1.00 20.91  ? 93  LEU   D N    1 
ATOM   6139 C  CA   . LEU   D 1 93  ? -20.079 -24.719 -40.860 1.00 20.48  ? 93  LEU   D CA   1 
ATOM   6140 C  C    . LEU   D 1 93  ? -21.292 -23.870 -41.257 1.00 21.76  ? 93  LEU   D C    1 
ATOM   6141 O  O    . LEU   D 1 93  ? -21.618 -22.921 -40.513 1.00 20.32  ? 93  LEU   D O    1 
ATOM   6142 C  CB   . LEU   D 1 93  ? -20.423 -25.659 -39.696 1.00 19.78  ? 93  LEU   D CB   1 
ATOM   6143 C  CG   . LEU   D 1 93  ? -19.321 -26.627 -39.282 1.00 20.46  ? 93  LEU   D CG   1 
ATOM   6144 C  CD1  . LEU   D 1 93  ? -19.709 -27.388 -38.030 1.00 19.99  ? 93  LEU   D CD1  1 
ATOM   6145 C  CD2  . LEU   D 1 93  ? -19.000 -27.584 -40.411 1.00 20.82  ? 93  LEU   D CD2  1 
ATOM   6146 N  N    . SER   D 1 94  ? -21.933 -24.237 -42.369 1.00 22.46  ? 94  SER   D N    1 
ATOM   6147 C  CA   . SER   D 1 94  ? -23.087 -23.548 -42.990 1.00 23.73  ? 94  SER   D CA   1 
ATOM   6148 C  C    . SER   D 1 94  ? -24.183 -24.572 -43.298 1.00 24.85  ? 94  SER   D C    1 
ATOM   6149 O  O    . SER   D 1 94  ? -23.851 -25.709 -43.616 1.00 26.68  ? 94  SER   D O    1 
ATOM   6150 C  CB   . SER   D 1 94  ? -22.644 -22.813 -44.245 1.00 23.22  ? 94  SER   D CB   1 
ATOM   6151 O  OG   . SER   D 1 94  ? -23.674 -21.953 -44.707 1.00 22.90  ? 94  SER   D OG   1 
ATOM   6152 N  N    . ALA   D 1 95  ? -25.450 -24.182 -43.204 1.00 26.08  ? 95  ALA   D N    1 
ATOM   6153 C  CA   . ALA   D 1 95  ? -26.582 -24.960 -43.746 1.00 25.91  ? 95  ALA   D CA   1 
ATOM   6154 C  C    . ALA   D 1 95  ? -27.743 -24.020 -44.054 1.00 25.50  ? 95  ALA   D C    1 
ATOM   6155 O  O    . ALA   D 1 95  ? -27.795 -22.902 -43.515 1.00 25.10  ? 95  ALA   D O    1 
ATOM   6156 C  CB   . ALA   D 1 95  ? -27.011 -26.059 -42.795 1.00 26.52  ? 95  ALA   D CB   1 
ATOM   6157 N  N    . SER   D 1 96  ? -28.623 -24.499 -44.918 1.00 26.08  ? 96  SER   D N    1 
ATOM   6158 C  CA   . SER   D 1 96  ? -29.791 -23.778 -45.474 1.00 27.12  ? 96  SER   D CA   1 
ATOM   6159 C  C    . SER   D 1 96  ? -30.881 -24.802 -45.782 1.00 28.68  ? 96  SER   D C    1 
ATOM   6160 O  O    . SER   D 1 96  ? -30.522 -25.956 -46.092 1.00 27.15  ? 96  SER   D O    1 
ATOM   6161 C  CB   . SER   D 1 96  ? -29.404 -23.025 -46.694 1.00 27.94  ? 96  SER   D CB   1 
ATOM   6162 O  OG   . SER   D 1 96  ? -28.767 -23.892 -47.630 1.00 29.47  ? 96  SER   D OG   1 
ATOM   6163 N  N    . THR   D 1 97  ? -32.132 -24.387 -45.597 1.00 29.54  ? 97  THR   D N    1 
ATOM   6164 C  CA   . THR   D 1 97  ? -33.376 -24.981 -46.124 1.00 28.99  ? 97  THR   D CA   1 
ATOM   6165 C  C    . THR   D 1 97  ? -34.028 -23.933 -47.030 1.00 32.47  ? 97  THR   D C    1 
ATOM   6166 O  O    . THR   D 1 97  ? -33.720 -22.714 -46.852 1.00 30.96  ? 97  THR   D O    1 
ATOM   6167 C  CB   . THR   D 1 97  ? -34.283 -25.378 -44.951 1.00 29.27  ? 97  THR   D CB   1 
ATOM   6168 O  OG1  . THR   D 1 97  ? -34.657 -24.182 -44.264 1.00 27.86  ? 97  THR   D OG1  1 
ATOM   6169 C  CG2  . THR   D 1 97  ? -33.608 -26.314 -43.972 1.00 29.22  ? 97  THR   D CG2  1 
ATOM   6170 N  N    . GLY   D 1 98  ? -34.910 -24.378 -47.935 1.00 36.46  ? 98  GLY   D N    1 
ATOM   6171 C  CA   . GLY   D 1 98  ? -35.612 -23.544 -48.936 1.00 36.38  ? 98  GLY   D CA   1 
ATOM   6172 C  C    . GLY   D 1 98  ? -37.112 -23.810 -48.932 1.00 35.92  ? 98  GLY   D C    1 
ATOM   6173 O  O    . GLY   D 1 98  ? -37.752 -23.627 -47.888 1.00 34.49  ? 98  GLY   D O    1 
ATOM   6174 N  N    . LEU   D 1 99  ? -37.670 -24.247 -50.058 1.00 39.65  ? 99  LEU   D N    1 
ATOM   6175 C  CA   . LEU   D 1 99  ? -39.061 -24.770 -50.107 1.00 39.15  ? 99  LEU   D CA   1 
ATOM   6176 C  C    . LEU   D 1 99  ? -39.107 -26.093 -49.330 1.00 39.74  ? 99  LEU   D C    1 
ATOM   6177 O  O    . LEU   D 1 99  ? -39.972 -26.232 -48.445 1.00 39.57  ? 99  LEU   D O    1 
ATOM   6178 C  CB   . LEU   D 1 99  ? -39.471 -24.961 -51.568 1.00 39.49  ? 99  LEU   D CB   1 
ATOM   6179 C  CG   . LEU   D 1 99  ? -40.882 -25.505 -51.776 1.00 39.40  ? 99  LEU   D CG   1 
ATOM   6180 C  CD1  . LEU   D 1 99  ? -41.941 -24.499 -51.329 1.00 36.84  ? 99  LEU   D CD1  1 
ATOM   6181 C  CD2  . LEU   D 1 99  ? -41.065 -25.901 -53.231 1.00 40.20  ? 99  LEU   D CD2  1 
ATOM   6182 N  N    . TYR   D 1 100 ? -38.184 -27.011 -49.624 1.00 40.21  ? 100 TYR   D N    1 
ATOM   6183 C  CA   . TYR   D 1 100 ? -37.997 -28.283 -48.877 1.00 45.15  ? 100 TYR   D CA   1 
ATOM   6184 C  C    . TYR   D 1 100 ? -36.971 -28.079 -47.747 1.00 48.92  ? 100 TYR   D C    1 
ATOM   6185 O  O    . TYR   D 1 100 ? -36.100 -27.176 -47.844 1.00 42.05  ? 100 TYR   D O    1 
ATOM   6186 C  CB   . TYR   D 1 100 ? -37.622 -29.418 -49.831 1.00 49.09  ? 100 TYR   D CB   1 
ATOM   6187 C  CG   . TYR   D 1 100 ? -38.663 -29.725 -50.882 1.00 52.72  ? 100 TYR   D CG   1 
ATOM   6188 C  CD1  . TYR   D 1 100 ? -39.996 -29.936 -50.549 1.00 54.31  ? 100 TYR   D CD1  1 
ATOM   6189 C  CD2  . TYR   D 1 100 ? -38.312 -29.806 -52.218 1.00 56.74  ? 100 TYR   D CD2  1 
ATOM   6190 C  CE1  . TYR   D 1 100 ? -40.950 -30.213 -51.518 1.00 57.92  ? 100 TYR   D CE1  1 
ATOM   6191 C  CE2  . TYR   D 1 100 ? -39.251 -30.083 -53.200 1.00 62.21  ? 100 TYR   D CE2  1 
ATOM   6192 C  CZ   . TYR   D 1 100 ? -40.574 -30.294 -52.849 1.00 63.06  ? 100 TYR   D CZ   1 
ATOM   6193 O  OH   . TYR   D 1 100 ? -41.493 -30.568 -53.822 1.00 67.52  ? 100 TYR   D OH   1 
ATOM   6194 N  N    . LYS   D 1 101 ? -37.068 -28.922 -46.707 1.00 47.84  ? 101 LYS   D N    1 
ATOM   6195 C  CA   . LYS   D 1 101 ? -36.520 -28.665 -45.351 1.00 45.72  ? 101 LYS   D CA   1 
ATOM   6196 C  C    . LYS   D 1 101 ? -35.999 -29.955 -44.698 1.00 47.86  ? 101 LYS   D C    1 
ATOM   6197 O  O    . LYS   D 1 101 ? -36.589 -31.043 -44.961 1.00 46.74  ? 101 LYS   D O    1 
ATOM   6198 C  CB   . LYS   D 1 101 ? -37.598 -28.008 -44.485 1.00 47.92  ? 101 LYS   D CB   1 
ATOM   6199 C  CG   . LYS   D 1 101 ? -39.031 -28.468 -44.732 1.00 49.58  ? 101 LYS   D CG   1 
ATOM   6200 C  CD   . LYS   D 1 101 ? -40.071 -27.390 -44.443 1.00 50.62  ? 101 LYS   D CD   1 
ATOM   6201 C  CE   . LYS   D 1 101 ? -41.495 -27.899 -44.460 1.00 50.77  ? 101 LYS   D CE   1 
ATOM   6202 N  NZ   . LYS   D 1 101 ? -41.715 -28.922 -43.408 1.00 48.96  ? 101 LYS   D NZ   1 
ATOM   6203 N  N    . GLU   D 1 102 ? -34.956 -29.799 -43.857 1.00 41.01  ? 102 GLU   D N    1 
ATOM   6204 C  CA   . GLU   D 1 102 ? -34.239 -30.854 -43.083 1.00 36.50  ? 102 GLU   D CA   1 
ATOM   6205 C  C    . GLU   D 1 102 ? -33.644 -30.244 -41.803 1.00 34.59  ? 102 GLU   D C    1 
ATOM   6206 O  O    . GLU   D 1 102 ? -33.319 -29.039 -41.803 1.00 34.56  ? 102 GLU   D O    1 
ATOM   6207 C  CB   . GLU   D 1 102 ? -33.124 -31.481 -43.934 1.00 35.12  ? 102 GLU   D CB   1 
ATOM   6208 C  CG   . GLU   D 1 102 ? -31.867 -30.619 -44.074 1.00 34.19  ? 102 GLU   D CG   1 
ATOM   6209 C  CD   . GLU   D 1 102 ? -30.945 -30.958 -45.241 1.00 34.39  ? 102 GLU   D CD   1 
ATOM   6210 O  OE1  . GLU   D 1 102 ? -31.379 -31.677 -46.178 1.00 34.37  ? 102 GLU   D OE1  1 
ATOM   6211 O  OE2  . GLU   D 1 102 ? -29.795 -30.482 -45.233 1.00 32.41  ? 102 GLU   D OE2  1 
ATOM   6212 N  N    . THR   D 1 103 ? -33.487 -31.033 -40.737 1.00 32.71  ? 103 THR   D N    1 
ATOM   6213 C  CA   . THR   D 1 103 ? -32.684 -30.632 -39.550 1.00 30.78  ? 103 THR   D CA   1 
ATOM   6214 C  C    . THR   D 1 103 ? -31.235 -30.607 -40.022 1.00 30.73  ? 103 THR   D C    1 
ATOM   6215 O  O    . THR   D 1 103 ? -30.883 -31.473 -40.866 1.00 30.84  ? 103 THR   D O    1 
ATOM   6216 C  CB   . THR   D 1 103 ? -32.878 -31.549 -38.335 1.00 32.85  ? 103 THR   D CB   1 
ATOM   6217 O  OG1  . THR   D 1 103 ? -32.370 -32.857 -38.625 1.00 32.43  ? 103 THR   D OG1  1 
ATOM   6218 C  CG2  . THR   D 1 103 ? -34.323 -31.615 -37.884 1.00 32.70  ? 103 THR   D CG2  1 
ATOM   6219 N  N    . ASN   D 1 104 ? -30.459 -29.614 -39.596 1.00 27.87  ? 104 ASN   D N    1 
ATOM   6220 C  CA   . ASN   D 1 104 ? -29.003 -29.565 -39.903 1.00 28.32  ? 104 ASN   D CA   1 
ATOM   6221 C  C    . ASN   D 1 104 ? -28.263 -29.500 -38.556 1.00 28.52  ? 104 ASN   D C    1 
ATOM   6222 O  O    . ASN   D 1 104 ? -27.659 -28.464 -38.236 1.00 25.75  ? 104 ASN   D O    1 
ATOM   6223 C  CB   . ASN   D 1 104 ? -28.694 -28.454 -40.903 1.00 26.77  ? 104 ASN   D CB   1 
ATOM   6224 C  CG   . ASN   D 1 104 ? -29.324 -28.655 -42.268 1.00 26.39  ? 104 ASN   D CG   1 
ATOM   6225 O  OD1  . ASN   D 1 104 ? -30.261 -27.950 -42.639 1.00 30.24  ? 104 ASN   D OD1  1 
ATOM   6226 N  ND2  . ASN   D 1 104 ? -28.784 -29.564 -43.056 1.00 25.42  ? 104 ASN   D ND2  1 
ATOM   6227 N  N    . THR   D 1 105 ? -28.394 -30.578 -37.777 1.00 29.23  ? 105 THR   D N    1 
ATOM   6228 C  CA   . THR   D 1 105 ? -27.853 -30.725 -36.408 1.00 28.28  ? 105 THR   D CA   1 
ATOM   6229 C  C    . THR   D 1 105 ? -26.403 -31.179 -36.504 1.00 27.91  ? 105 THR   D C    1 
ATOM   6230 O  O    . THR   D 1 105 ? -26.150 -32.179 -37.190 1.00 27.41  ? 105 THR   D O    1 
ATOM   6231 C  CB   . THR   D 1 105 ? -28.679 -31.712 -35.582 1.00 31.37  ? 105 THR   D CB   1 
ATOM   6232 O  OG1  . THR   D 1 105 ? -30.067 -31.516 -35.892 1.00 35.07  ? 105 THR   D OG1  1 
ATOM   6233 C  CG2  . THR   D 1 105 ? -28.428 -31.556 -34.098 1.00 30.39  ? 105 THR   D CG2  1 
ATOM   6234 N  N    . ILE   D 1 106 ? -25.499 -30.409 -35.895 1.00 26.28  ? 106 ILE   D N    1 
ATOM   6235 C  CA   . ILE   D 1 106 ? -24.058 -30.745 -35.712 1.00 24.69  ? 106 ILE   D CA   1 
ATOM   6236 C  C    . ILE   D 1 106 ? -23.866 -31.156 -34.255 1.00 23.35  ? 106 ILE   D C    1 
ATOM   6237 O  O    . ILE   D 1 106 ? -24.268 -30.381 -33.351 1.00 21.14  ? 106 ILE   D O    1 
ATOM   6238 C  CB   . ILE   D 1 106 ? -23.158 -29.566 -36.106 1.00 24.63  ? 106 ILE   D CB   1 
ATOM   6239 C  CG1  . ILE   D 1 106 ? -23.428 -29.148 -37.554 1.00 25.42  ? 106 ILE   D CG1  1 
ATOM   6240 C  CG2  . ILE   D 1 106 ? -21.693 -29.899 -35.865 1.00 23.88  ? 106 ILE   D CG2  1 
ATOM   6241 C  CD1  . ILE   D 1 106 ? -22.871 -30.098 -38.594 1.00 24.49  ? 106 ILE   D CD1  1 
ATOM   6242 N  N    . LEU   D 1 107 ? -23.363 -32.375 -34.058 1.00 23.48  ? 107 LEU   D N    1 
ATOM   6243 C  CA   . LEU   D 1 107 ? -23.182 -33.000 -32.718 1.00 24.61  ? 107 LEU   D CA   1 
ATOM   6244 C  C    . LEU   D 1 107 ? -21.724 -32.845 -32.280 1.00 21.03  ? 107 LEU   D C    1 
ATOM   6245 O  O    . LEU   D 1 107 ? -21.499 -32.834 -31.087 1.00 21.61  ? 107 LEU   D O    1 
ATOM   6246 C  CB   . LEU   D 1 107 ? -23.608 -34.478 -32.753 1.00 26.12  ? 107 LEU   D CB   1 
ATOM   6247 C  CG   . LEU   D 1 107 ? -25.108 -34.701 -32.968 1.00 29.80  ? 107 LEU   D CG   1 
ATOM   6248 C  CD1  . LEU   D 1 107 ? -25.398 -35.096 -34.417 1.00 30.73  ? 107 LEU   D CD1  1 
ATOM   6249 C  CD2  . LEU   D 1 107 ? -25.677 -35.736 -32.005 1.00 31.00  ? 107 LEU   D CD2  1 
ATOM   6250 N  N    . SER   D 1 108 ? -20.780 -32.740 -33.207 1.00 19.77  ? 108 SER   D N    1 
ATOM   6251 C  CA   . SER   D 1 108 ? -19.345 -32.574 -32.884 1.00 21.14  ? 108 SER   D CA   1 
ATOM   6252 C  C    . SER   D 1 108 ? -18.640 -31.872 -34.039 1.00 20.41  ? 108 SER   D C    1 
ATOM   6253 O  O    . SER   D 1 108 ? -19.116 -31.979 -35.179 1.00 22.78  ? 108 SER   D O    1 
ATOM   6254 C  CB   . SER   D 1 108 ? -18.678 -33.901 -32.554 1.00 22.26  ? 108 SER   D CB   1 
ATOM   6255 O  OG   . SER   D 1 108 ? -18.618 -34.752 -33.695 1.00 23.75  ? 108 SER   D OG   1 
ATOM   6256 N  N    . TRP   D 1 109 ? -17.550 -31.184 -33.739 1.00 19.02  ? 109 TRP   D N    1 
ATOM   6257 C  CA   . TRP   D 1 109 ? -16.710 -30.511 -34.751 1.00 19.94  ? 109 TRP   D CA   1 
ATOM   6258 C  C    . TRP   D 1 109 ? -15.294 -30.349 -34.205 1.00 21.18  ? 109 TRP   D C    1 
ATOM   6259 O  O    . TRP   D 1 109 ? -15.129 -29.874 -33.059 1.00 21.57  ? 109 TRP   D O    1 
ATOM   6260 C  CB   . TRP   D 1 109 ? -17.356 -29.182 -35.134 1.00 20.07  ? 109 TRP   D CB   1 
ATOM   6261 C  CG   . TRP   D 1 109 ? -16.651 -28.391 -36.183 1.00 18.52  ? 109 TRP   D CG   1 
ATOM   6262 C  CD1  . TRP   D 1 109 ? -15.866 -28.849 -37.199 1.00 19.89  ? 109 TRP   D CD1  1 
ATOM   6263 C  CD2  . TRP   D 1 109 ? -16.697 -26.969 -36.323 1.00 18.55  ? 109 TRP   D CD2  1 
ATOM   6264 N  NE1  . TRP   D 1 109 ? -15.413 -27.804 -37.961 1.00 19.77  ? 109 TRP   D NE1  1 
ATOM   6265 C  CE2  . TRP   D 1 109 ? -15.912 -26.639 -37.448 1.00 18.94  ? 109 TRP   D CE2  1 
ATOM   6266 C  CE3  . TRP   D 1 109 ? -17.333 -25.946 -35.616 1.00 19.38  ? 109 TRP   D CE3  1 
ATOM   6267 C  CZ2  . TRP   D 1 109 ? -15.735 -25.324 -37.865 1.00 19.41  ? 109 TRP   D CZ2  1 
ATOM   6268 C  CZ3  . TRP   D 1 109 ? -17.150 -24.646 -36.031 1.00 18.91  ? 109 TRP   D CZ3  1 
ATOM   6269 C  CH2  . TRP   D 1 109 ? -16.359 -24.343 -37.130 1.00 18.34  ? 109 TRP   D CH2  1 
ATOM   6270 N  N    . SER   D 1 110 ? -14.305 -30.755 -34.997 1.00 20.73  ? 110 SER   D N    1 
ATOM   6271 C  CA   . SER   D 1 110 ? -12.877 -30.575 -34.668 1.00 21.69  ? 110 SER   D CA   1 
ATOM   6272 C  C    . SER   D 1 110 ? -12.134 -30.108 -35.914 1.00 20.73  ? 110 SER   D C    1 
ATOM   6273 O  O    . SER   D 1 110 ? -12.609 -30.359 -37.014 1.00 21.58  ? 110 SER   D O    1 
ATOM   6274 C  CB   . SER   D 1 110 ? -12.290 -31.828 -34.092 1.00 22.69  ? 110 SER   D CB   1 
ATOM   6275 O  OG   . SER   D 1 110 ? -12.321 -32.828 -35.075 1.00 25.46  ? 110 SER   D OG   1 
ATOM   6276 N  N    . PHE   D 1 111 ? -11.047 -29.377 -35.707 1.00 20.12  ? 111 PHE   D N    1 
ATOM   6277 C  CA   . PHE   D 1 111 ? -10.243 -28.758 -36.777 1.00 20.63  ? 111 PHE   D CA   1 
ATOM   6278 C  C    . PHE   D 1 111 ? -8.802  -28.668 -36.283 1.00 21.35  ? 111 PHE   D C    1 
ATOM   6279 O  O    . PHE   D 1 111 ? -8.590  -28.331 -35.101 1.00 21.52  ? 111 PHE   D O    1 
ATOM   6280 C  CB   . PHE   D 1 111 ? -10.844 -27.411 -37.182 1.00 20.22  ? 111 PHE   D CB   1 
ATOM   6281 C  CG   . PHE   D 1 111 ? -9.984  -26.608 -38.116 1.00 21.01  ? 111 PHE   D CG   1 
ATOM   6282 C  CD1  . PHE   D 1 111 ? -9.042  -25.716 -37.623 1.00 22.31  ? 111 PHE   D CD1  1 
ATOM   6283 C  CD2  . PHE   D 1 111 ? -10.105 -26.741 -39.486 1.00 22.12  ? 111 PHE   D CD2  1 
ATOM   6284 C  CE1  . PHE   D 1 111 ? -8.220  -25.006 -38.484 1.00 22.27  ? 111 PHE   D CE1  1 
ATOM   6285 C  CE2  . PHE   D 1 111 ? -9.286  -26.020 -40.343 1.00 21.88  ? 111 PHE   D CE2  1 
ATOM   6286 C  CZ   . PHE   D 1 111 ? -8.348  -25.154 -39.844 1.00 22.40  ? 111 PHE   D CZ   1 
ATOM   6287 N  N    . THR   D 1 112 ? -7.861  -28.995 -37.166 1.00 21.28  ? 112 THR   D N    1 
ATOM   6288 C  CA   . THR   D 1 112 ? -6.413  -28.814 -36.964 1.00 23.72  ? 112 THR   D CA   1 
ATOM   6289 C  C    . THR   D 1 112 ? -5.814  -28.168 -38.220 1.00 24.78  ? 112 THR   D C    1 
ATOM   6290 O  O    . THR   D 1 112 ? -6.181  -28.549 -39.323 1.00 26.29  ? 112 THR   D O    1 
ATOM   6291 C  CB   . THR   D 1 112 ? -5.743  -30.142 -36.591 1.00 23.65  ? 112 THR   D CB   1 
ATOM   6292 O  OG1  . THR   D 1 112 ? -6.366  -30.633 -35.406 1.00 22.18  ? 112 THR   D OG1  1 
ATOM   6293 C  CG2  . THR   D 1 112 ? -4.255  -29.999 -36.359 1.00 24.20  ? 112 THR   D CG2  1 
ATOM   6294 N  N    . SER   D 1 113 ? -4.921  -27.212 -38.019 1.00 25.99  ? 113 SER   D N    1 
ATOM   6295 C  CA   . SER   D 1 113 ? -4.187  -26.465 -39.055 1.00 28.49  ? 113 SER   D CA   1 
ATOM   6296 C  C    . SER   D 1 113 ? -2.716  -26.531 -38.675 1.00 29.26  ? 113 SER   D C    1 
ATOM   6297 O  O    . SER   D 1 113 ? -2.460  -26.446 -37.473 1.00 28.94  ? 113 SER   D O    1 
ATOM   6298 C  CB   . SER   D 1 113 ? -4.683  -25.063 -39.112 1.00 30.43  ? 113 SER   D CB   1 
ATOM   6299 O  OG   . SER   D 1 113 ? -3.876  -24.287 -39.976 1.00 38.52  ? 113 SER   D OG   1 
ATOM   6300 N  N    . LYS   D 1 114 ? -1.819  -26.717 -39.643 1.00 32.14  ? 114 LYS   D N    1 
ATOM   6301 C  CA   . LYS   D 1 114 ? -0.353  -26.816 -39.406 1.00 38.66  ? 114 LYS   D CA   1 
ATOM   6302 C  C    . LYS   D 1 114 ? 0.381   -26.180 -40.575 1.00 40.34  ? 114 LYS   D C    1 
ATOM   6303 O  O    . LYS   D 1 114 ? 0.127   -26.580 -41.715 1.00 45.70  ? 114 LYS   D O    1 
ATOM   6304 C  CB   . LYS   D 1 114 ? 0.111   -28.264 -39.238 1.00 43.23  ? 114 LYS   D CB   1 
ATOM   6305 C  CG   . LYS   D 1 114 ? -0.224  -28.879 -37.889 1.00 47.91  ? 114 LYS   D CG   1 
ATOM   6306 C  CD   . LYS   D 1 114 ? 0.166   -30.338 -37.757 1.00 53.30  ? 114 LYS   D CD   1 
ATOM   6307 C  CE   . LYS   D 1 114 ? -0.120  -30.884 -36.370 1.00 59.98  ? 114 LYS   D CE   1 
ATOM   6308 N  NZ   . LYS   D 1 114 ? 0.158   -32.338 -36.282 1.00 63.25  ? 114 LYS   D NZ   1 
ATOM   6309 N  N    . LEU   D 1 115 ? 1.264   -25.241 -40.262 1.00 40.42  ? 115 LEU   D N    1 
ATOM   6310 C  CA   . LEU   D 1 115 ? 1.961   -24.357 -41.217 1.00 42.76  ? 115 LEU   D CA   1 
ATOM   6311 C  C    . LEU   D 1 115 ? 3.459   -24.395 -40.879 1.00 50.05  ? 115 LEU   D C    1 
ATOM   6312 O  O    . LEU   D 1 115 ? 3.840   -23.781 -39.852 1.00 44.49  ? 115 LEU   D O    1 
ATOM   6313 C  CB   . LEU   D 1 115 ? 1.336   -22.968 -41.050 1.00 40.14  ? 115 LEU   D CB   1 
ATOM   6314 C  CG   . LEU   D 1 115 ? 1.902   -21.833 -41.907 1.00 43.00  ? 115 LEU   D CG   1 
ATOM   6315 C  CD1  . LEU   D 1 115 ? 1.500   -21.967 -43.373 1.00 42.86  ? 115 LEU   D CD1  1 
ATOM   6316 C  CD2  . LEU   D 1 115 ? 1.438   -20.490 -41.367 1.00 44.05  ? 115 LEU   D CD2  1 
ATOM   6317 N  N    . LYS   D 1 116 ? 4.251   -25.147 -41.663 1.00 61.83  ? 116 LYS   D N    1 
ATOM   6318 C  CA   . LYS   D 1 116 ? 5.728   -25.302 -41.516 1.00 69.88  ? 116 LYS   D CA   1 
ATOM   6319 C  C    . LYS   D 1 116 ? 6.435   -24.144 -42.227 1.00 76.79  ? 116 LYS   D C    1 
ATOM   6320 O  O    . LYS   D 1 116 ? 6.337   -24.082 -43.465 1.00 72.06  ? 116 LYS   D O    1 
ATOM   6321 C  CB   . LYS   D 1 116 ? 6.238   -26.618 -42.117 1.00 77.25  ? 116 LYS   D CB   1 
ATOM   6322 C  CG   . LYS   D 1 116 ? 5.841   -27.893 -41.381 1.00 85.10  ? 116 LYS   D CG   1 
ATOM   6323 C  CD   . LYS   D 1 116 ? 6.553   -29.139 -41.894 1.00 89.34  ? 116 LYS   D CD   1 
ATOM   6324 C  CE   . LYS   D 1 116 ? 6.252   -30.382 -41.081 1.00 95.18  ? 116 LYS   D CE   1 
ATOM   6325 N  NZ   . LYS   D 1 116 ? 4.795   -30.634 -40.973 1.00 96.25  ? 116 LYS   D NZ   1 
ATOM   6326 N  N    . SER   D 1 117 ? 7.132   -23.289 -41.461 1.00 89.71  ? 117 SER   D N    1 
ATOM   6327 C  CA   . SER   D 1 117 ? 7.936   -22.123 -41.927 1.00 94.99  ? 117 SER   D CA   1 
ATOM   6328 C  C    . SER   D 1 117 ? 9.090   -22.599 -42.830 1.00 99.56  ? 117 SER   D C    1 
ATOM   6329 O  O    . SER   D 1 117 ? 9.365   -23.820 -42.846 1.00 101.98 ? 117 SER   D O    1 
ATOM   6330 C  CB   . SER   D 1 117 ? 8.430   -21.321 -40.740 1.00 94.57  ? 117 SER   D CB   1 
ATOM   6331 O  OG   . SER   D 1 117 ? 9.059   -20.118 -41.150 1.00 94.11  ? 117 SER   D OG   1 
ATOM   6332 N  N    . ASN   D 1 118 ? 9.736   -21.678 -43.559 1.00 103.60 ? 118 ASN   D N    1 
ATOM   6333 C  CA   . ASN   D 1 118 ? 10.739  -21.989 -44.620 1.00 106.88 ? 118 ASN   D CA   1 
ATOM   6334 C  C    . ASN   D 1 118 ? 12.149  -21.551 -44.188 1.00 113.32 ? 118 ASN   D C    1 
ATOM   6335 O  O    . ASN   D 1 118 ? 13.085  -22.368 -44.331 1.00 115.08 ? 118 ASN   D O    1 
ATOM   6336 C  CB   . ASN   D 1 118 ? 10.369  -21.341 -45.958 1.00 100.79 ? 118 ASN   D CB   1 
ATOM   6337 C  CG   . ASN   D 1 118 ? 11.018  -22.022 -47.146 1.00 97.76  ? 118 ASN   D CG   1 
ATOM   6338 O  OD1  . ASN   D 1 118 ? 10.887  -23.231 -47.325 1.00 93.30  ? 118 ASN   D OD1  1 
ATOM   6339 N  ND2  . ASN   D 1 118 ? 11.719  -21.255 -47.966 1.00 95.45  ? 118 ASN   D ND2  1 
ATOM   6340 N  N    . SER   D 1 119 ? 12.301  -20.310 -43.708 1.00 113.40 ? 119 SER   D N    1 
ATOM   6341 C  CA   . SER   D 1 119 ? 13.599  -19.694 -43.314 1.00 108.96 ? 119 SER   D CA   1 
ATOM   6342 C  C    . SER   D 1 119 ? 14.151  -20.359 -42.044 1.00 118.60 ? 119 SER   D C    1 
ATOM   6343 O  O    . SER   D 1 119 ? 15.390  -20.335 -41.876 1.00 122.69 ? 119 SER   D O    1 
ATOM   6344 C  CB   . SER   D 1 119 ? 13.471  -18.195 -43.131 1.00 100.57 ? 119 SER   D CB   1 
ATOM   6345 O  OG   . SER   D 1 119 ? 13.088  -17.861 -41.803 1.00 88.48  ? 119 SER   D OG   1 
ATOM   6346 N  N    . THR   D 1 120 ? 13.273  -20.905 -41.186 1.00 124.36 ? 120 THR   D N    1 
ATOM   6347 C  CA   . THR   D 1 120 ? 13.611  -21.457 -39.839 1.00 124.65 ? 120 THR   D CA   1 
ATOM   6348 C  C    . THR   D 1 120 ? 13.025  -22.868 -39.616 1.00 119.01 ? 120 THR   D C    1 
ATOM   6349 O  O    . THR   D 1 120 ? 13.490  -23.526 -38.666 1.00 116.53 ? 120 THR   D O    1 
ATOM   6350 C  CB   . THR   D 1 120 ? 13.177  -20.484 -38.732 1.00 127.49 ? 120 THR   D CB   1 
ATOM   6351 O  OG1  . THR   D 1 120 ? 11.815  -20.119 -38.964 1.00 135.92 ? 120 THR   D OG1  1 
ATOM   6352 C  CG2  . THR   D 1 120 ? 14.036  -19.238 -38.660 1.00 121.40 ? 120 THR   D CG2  1 
ATOM   6353 N  N    . HIS   D 1 121 ? 12.040  -23.314 -40.412 1.00 115.99 ? 121 HIS   D N    1 
ATOM   6354 C  CA   . HIS   D 1 121 ? 11.521  -24.717 -40.477 1.00 112.88 ? 121 HIS   D CA   1 
ATOM   6355 C  C    . HIS   D 1 121 ? 10.803  -25.153 -39.186 1.00 108.82 ? 121 HIS   D C    1 
ATOM   6356 O  O    . HIS   D 1 121 ? 10.736  -26.386 -38.940 1.00 96.74  ? 121 HIS   D O    1 
ATOM   6357 C  CB   . HIS   D 1 121 ? 12.645  -25.702 -40.849 1.00 111.98 ? 121 HIS   D CB   1 
ATOM   6358 C  CG   . HIS   D 1 121 ? 12.727  -25.986 -42.311 1.00 112.64 ? 121 HIS   D CG   1 
ATOM   6359 N  ND1  . HIS   D 1 121 ? 13.094  -25.021 -43.228 1.00 111.08 ? 121 HIS   D ND1  1 
ATOM   6360 C  CD2  . HIS   D 1 121 ? 12.488  -27.113 -43.018 1.00 110.24 ? 121 HIS   D CD2  1 
ATOM   6361 C  CE1  . HIS   D 1 121 ? 13.079  -25.540 -44.438 1.00 109.06 ? 121 HIS   D CE1  1 
ATOM   6362 N  NE2  . HIS   D 1 121 ? 12.712  -26.826 -44.337 1.00 107.87 ? 121 HIS   D NE2  1 
ATOM   6363 N  N    . GLU   D 1 122 ? 10.255  -24.211 -38.407 1.00 104.81 ? 122 GLU   D N    1 
ATOM   6364 C  CA   . GLU   D 1 122 ? 9.387   -24.513 -37.232 1.00 97.00  ? 122 GLU   D CA   1 
ATOM   6365 C  C    . GLU   D 1 122 ? 7.921   -24.308 -37.633 1.00 85.23  ? 122 GLU   D C    1 
ATOM   6366 O  O    . GLU   D 1 122 ? 7.665   -23.435 -38.502 1.00 84.83  ? 122 GLU   D O    1 
ATOM   6367 C  CB   . GLU   D 1 122 ? 9.734   -23.644 -36.021 1.00 99.39  ? 122 GLU   D CB   1 
ATOM   6368 C  CG   . GLU   D 1 122 ? 11.083  -23.954 -35.391 1.00 102.21 ? 122 GLU   D CG   1 
ATOM   6369 C  CD   . GLU   D 1 122 ? 12.135  -22.869 -35.544 1.00 108.15 ? 122 GLU   D CD   1 
ATOM   6370 O  OE1  . GLU   D 1 122 ? 11.819  -21.822 -36.148 1.00 108.94 ? 122 GLU   D OE1  1 
ATOM   6371 O  OE2  . GLU   D 1 122 ? 13.265  -23.073 -35.047 1.00 114.99 ? 122 GLU   D OE2  1 
ATOM   6372 N  N    . THR   D 1 123 ? 7.004   -25.059 -37.000 1.00 67.81  ? 123 THR   D N    1 
ATOM   6373 C  CA   . THR   D 1 123 ? 5.554   -25.108 -37.347 1.00 57.58  ? 123 THR   D CA   1 
ATOM   6374 C  C    . THR   D 1 123 ? 4.719   -24.291 -36.342 1.00 44.04  ? 123 THR   D C    1 
ATOM   6375 O  O    . THR   D 1 123 ? 5.020   -24.297 -35.144 1.00 41.01  ? 123 THR   D O    1 
ATOM   6376 C  CB   . THR   D 1 123 ? 5.046   -26.551 -37.499 1.00 57.45  ? 123 THR   D CB   1 
ATOM   6377 O  OG1  . THR   D 1 123 ? 4.349   -26.927 -36.313 1.00 52.64  ? 123 THR   D OG1  1 
ATOM   6378 C  CG2  . THR   D 1 123 ? 6.144   -27.552 -37.800 1.00 59.50  ? 123 THR   D CG2  1 
ATOM   6379 N  N    . ASN   D 1 124 ? 3.733   -23.560 -36.856 1.00 36.26  ? 124 ASN   D N    1 
ATOM   6380 C  CA   . ASN   D 1 124 ? 2.643   -22.924 -36.076 1.00 32.96  ? 124 ASN   D CA   1 
ATOM   6381 C  C    . ASN   D 1 124 ? 1.409   -23.810 -36.252 1.00 27.55  ? 124 ASN   D C    1 
ATOM   6382 O  O    . ASN   D 1 124 ? 1.278   -24.411 -37.340 1.00 30.58  ? 124 ASN   D O    1 
ATOM   6383 C  CB   . ASN   D 1 124 ? 2.400   -21.471 -36.511 1.00 32.61  ? 124 ASN   D CB   1 
ATOM   6384 C  CG   . ASN   D 1 124 ? 3.526   -20.512 -36.170 1.00 32.07  ? 124 ASN   D CG   1 
ATOM   6385 O  OD1  . ASN   D 1 124 ? 4.539   -20.874 -35.567 1.00 30.66  ? 124 ASN   D OD1  1 
ATOM   6386 N  ND2  . ASN   D 1 124 ? 3.351   -19.261 -36.554 1.00 31.55  ? 124 ASN   D ND2  1 
ATOM   6387 N  N    . ALA   D 1 125 ? 0.542   -23.911 -35.249 1.00 23.51  ? 125 ALA   D N    1 
ATOM   6388 C  CA   . ALA   D 1 125 ? -0.638  -24.800 -35.309 1.00 22.20  ? 125 ALA   D CA   1 
ATOM   6389 C  C    . ALA   D 1 125 ? -1.818  -24.224 -34.518 1.00 22.65  ? 125 ALA   D C    1 
ATOM   6390 O  O    . ALA   D 1 125 ? -1.588  -23.583 -33.485 1.00 23.98  ? 125 ALA   D O    1 
ATOM   6391 C  CB   . ALA   D 1 125 ? -0.249  -26.181 -34.833 1.00 21.32  ? 125 ALA   D CB   1 
ATOM   6392 N  N    . LEU   D 1 126 ? -3.041  -24.469 -35.004 1.00 22.47  ? 126 LEU   D N    1 
ATOM   6393 C  CA   . LEU   D 1 126 ? -4.317  -24.304 -34.265 1.00 21.41  ? 126 LEU   D CA   1 
ATOM   6394 C  C    . LEU   D 1 126 ? -5.085  -25.639 -34.267 1.00 20.84  ? 126 LEU   D C    1 
ATOM   6395 O  O    . LEU   D 1 126 ? -5.119  -26.323 -35.301 1.00 19.22  ? 126 LEU   D O    1 
ATOM   6396 C  CB   . LEU   D 1 126 ? -5.140  -23.201 -34.935 1.00 22.86  ? 126 LEU   D CB   1 
ATOM   6397 C  CG   . LEU   D 1 126 ? -6.502  -22.933 -34.306 1.00 23.34  ? 126 LEU   D CG   1 
ATOM   6398 C  CD1  . LEU   D 1 126 ? -6.373  -22.041 -33.085 1.00 24.25  ? 126 LEU   D CD1  1 
ATOM   6399 C  CD2  . LEU   D 1 126 ? -7.434  -22.311 -35.311 1.00 24.72  ? 126 LEU   D CD2  1 
ATOM   6400 N  N    . HIS   D 1 127 ? -5.659  -26.018 -33.124 1.00 19.61  ? 127 HIS   D N    1 
ATOM   6401 C  CA   . HIS   D 1 127 ? -6.598  -27.157 -33.008 1.00 19.67  ? 127 HIS   D CA   1 
ATOM   6402 C  C    . HIS   D 1 127 ? -7.744  -26.730 -32.112 1.00 18.43  ? 127 HIS   D C    1 
ATOM   6403 O  O    . HIS   D 1 127 ? -7.488  -26.041 -31.104 1.00 18.64  ? 127 HIS   D O    1 
ATOM   6404 C  CB   . HIS   D 1 127 ? -5.878  -28.418 -32.501 1.00 20.91  ? 127 HIS   D CB   1 
ATOM   6405 C  CG   . HIS   D 1 127 ? -6.775  -29.498 -31.994 1.00 22.09  ? 127 HIS   D CG   1 
ATOM   6406 N  ND1  . HIS   D 1 127 ? -7.434  -30.367 -32.830 1.00 23.79  ? 127 HIS   D ND1  1 
ATOM   6407 C  CD2  . HIS   D 1 127 ? -7.090  -29.878 -30.737 1.00 23.21  ? 127 HIS   D CD2  1 
ATOM   6408 C  CE1  . HIS   D 1 127 ? -8.140  -31.216 -32.113 1.00 24.64  ? 127 HIS   D CE1  1 
ATOM   6409 N  NE2  . HIS   D 1 127 ? -7.961  -30.929 -30.834 1.00 24.20  ? 127 HIS   D NE2  1 
ATOM   6410 N  N    . PHE   D 1 128 ? -8.957  -27.117 -32.464 1.00 17.76  ? 128 PHE   D N    1 
ATOM   6411 C  CA   . PHE   D 1 128 ? -10.084 -27.077 -31.504 1.00 19.08  ? 128 PHE   D CA   1 
ATOM   6412 C  C    . PHE   D 1 128 ? -10.942 -28.319 -31.694 1.00 18.15  ? 128 PHE   D C    1 
ATOM   6413 O  O    . PHE   D 1 128 ? -10.851 -28.968 -32.753 1.00 18.41  ? 128 PHE   D O    1 
ATOM   6414 C  CB   . PHE   D 1 128 ? -10.843 -25.755 -31.633 1.00 19.46  ? 128 PHE   D CB   1 
ATOM   6415 C  CG   . PHE   D 1 128 ? -11.508 -25.550 -32.968 1.00 19.62  ? 128 PHE   D CG   1 
ATOM   6416 C  CD1  . PHE   D 1 128 ? -12.691 -26.206 -33.272 1.00 18.91  ? 128 PHE   D CD1  1 
ATOM   6417 C  CD2  . PHE   D 1 128 ? -10.962 -24.681 -33.905 1.00 19.48  ? 128 PHE   D CD2  1 
ATOM   6418 C  CE1  . PHE   D 1 128 ? -13.310 -25.993 -34.498 1.00 20.90  ? 128 PHE   D CE1  1 
ATOM   6419 C  CE2  . PHE   D 1 128 ? -11.584 -24.476 -35.129 1.00 20.00  ? 128 PHE   D CE2  1 
ATOM   6420 C  CZ   . PHE   D 1 128 ? -12.765 -25.115 -35.421 1.00 18.77  ? 128 PHE   D CZ   1 
ATOM   6421 N  N    . MET   D 1 129 ? -11.759 -28.610 -30.691 1.00 19.19  ? 129 MET   D N    1 
ATOM   6422 C  CA   . MET   D 1 129 ? -12.647 -29.802 -30.639 1.00 22.13  ? 129 MET   D CA   1 
ATOM   6423 C  C    . MET   D 1 129 ? -13.847 -29.465 -29.757 1.00 21.41  ? 129 MET   D C    1 
ATOM   6424 O  O    . MET   D 1 129 ? -13.650 -29.198 -28.563 1.00 19.72  ? 129 MET   D O    1 
ATOM   6425 C  CB   . MET   D 1 129 ? -11.887 -30.992 -30.046 1.00 25.19  ? 129 MET   D CB   1 
ATOM   6426 C  CG   . MET   D 1 129 ? -12.499 -32.335 -30.312 1.00 28.73  ? 129 MET   D CG   1 
ATOM   6427 S  SD   . MET   D 1 129 ? -11.780 -33.605 -29.251 1.00 34.81  ? 129 MET   D SD   1 
ATOM   6428 C  CE   . MET   D 1 129 ? -10.024 -33.246 -29.298 1.00 36.45  ? 129 MET   D CE   1 
ATOM   6429 N  N    . PHE   D 1 130 ? -15.041 -29.463 -30.333 1.00 22.12  ? 130 PHE   D N    1 
ATOM   6430 C  CA   . PHE   D 1 130 ? -16.314 -29.389 -29.583 1.00 23.24  ? 130 PHE   D CA   1 
ATOM   6431 C  C    . PHE   D 1 130 ? -17.020 -30.745 -29.697 1.00 24.17  ? 130 PHE   D C    1 
ATOM   6432 O  O    . PHE   D 1 130 ? -17.378 -31.157 -30.824 1.00 21.40  ? 130 PHE   D O    1 
ATOM   6433 C  CB   . PHE   D 1 130 ? -17.222 -28.300 -30.145 1.00 23.32  ? 130 PHE   D CB   1 
ATOM   6434 C  CG   . PHE   D 1 130 ? -16.564 -26.969 -30.360 1.00 22.22  ? 130 PHE   D CG   1 
ATOM   6435 C  CD1  . PHE   D 1 130 ? -16.394 -26.093 -29.309 1.00 24.10  ? 130 PHE   D CD1  1 
ATOM   6436 C  CD2  . PHE   D 1 130 ? -16.178 -26.568 -31.619 1.00 21.76  ? 130 PHE   D CD2  1 
ATOM   6437 C  CE1  . PHE   D 1 130 ? -15.840 -24.839 -29.509 1.00 23.20  ? 130 PHE   D CE1  1 
ATOM   6438 C  CE2  . PHE   D 1 130 ? -15.605 -25.325 -31.816 1.00 22.36  ? 130 PHE   D CE2  1 
ATOM   6439 C  CZ   . PHE   D 1 130 ? -15.442 -24.462 -30.761 1.00 21.87  ? 130 PHE   D CZ   1 
ATOM   6440 N  N    . ASN   D 1 131 ? -17.211 -31.415 -28.564 1.00 24.89  ? 131 ASN   D N    1 
ATOM   6441 C  CA   . ASN   D 1 131 ? -18.025 -32.653 -28.464 1.00 26.71  ? 131 ASN   D CA   1 
ATOM   6442 C  C    . ASN   D 1 131 ? -19.398 -32.275 -27.911 1.00 28.90  ? 131 ASN   D C    1 
ATOM   6443 O  O    . ASN   D 1 131 ? -20.313 -33.099 -27.997 1.00 27.45  ? 131 ASN   D O    1 
ATOM   6444 C  CB   . ASN   D 1 131 ? -17.312 -33.715 -27.634 1.00 26.23  ? 131 ASN   D CB   1 
ATOM   6445 C  CG   . ASN   D 1 131 ? -16.217 -34.401 -28.422 1.00 28.43  ? 131 ASN   D CG   1 
ATOM   6446 O  OD1  . ASN   D 1 131 ? -16.477 -34.887 -29.513 1.00 30.07  ? 131 ASN   D OD1  1 
ATOM   6447 N  ND2  . ASN   D 1 131 ? -15.001 -34.464 -27.887 1.00 26.17  ? 131 ASN   D ND2  1 
ATOM   6448 N  N    . GLN   D 1 132 ? -19.520 -31.079 -27.332 1.00 31.31  ? 132 GLN   D N    1 
ATOM   6449 C  CA   . GLN   D 1 132 ? -20.825 -30.496 -26.945 1.00 34.69  ? 132 GLN   D CA   1 
ATOM   6450 C  C    . GLN   D 1 132 ? -20.725 -28.978 -27.083 1.00 32.74  ? 132 GLN   D C    1 
ATOM   6451 O  O    . GLN   D 1 132 ? -19.641 -28.398 -26.878 1.00 32.38  ? 132 GLN   D O    1 
ATOM   6452 C  CB   . GLN   D 1 132 ? -21.276 -30.934 -25.546 1.00 42.83  ? 132 GLN   D CB   1 
ATOM   6453 C  CG   . GLN   D 1 132 ? -20.385 -30.458 -24.401 1.00 52.14  ? 132 GLN   D CG   1 
ATOM   6454 C  CD   . GLN   D 1 132 ? -21.114 -29.785 -23.252 1.00 65.21  ? 132 GLN   D CD   1 
ATOM   6455 O  OE1  . GLN   D 1 132 ? -22.082 -29.031 -23.443 1.00 74.65  ? 132 GLN   D OE1  1 
ATOM   6456 N  NE2  . GLN   D 1 132 ? -20.613 -30.003 -22.034 1.00 69.72  ? 132 GLN   D NE2  1 
ATOM   6457 N  N    . PHE   D 1 133 ? -21.825 -28.369 -27.487 1.00 30.22  ? 133 PHE   D N    1 
ATOM   6458 C  CA   . PHE   D 1 133 ? -21.977 -26.909 -27.612 1.00 28.29  ? 133 PHE   D CA   1 
ATOM   6459 C  C    . PHE   D 1 133 ? -22.812 -26.481 -26.411 1.00 30.08  ? 133 PHE   D C    1 
ATOM   6460 O  O    . PHE   D 1 133 ? -23.708 -27.231 -26.054 1.00 30.89  ? 133 PHE   D O    1 
ATOM   6461 C  CB   . PHE   D 1 133 ? -22.615 -26.594 -28.965 1.00 26.49  ? 133 PHE   D CB   1 
ATOM   6462 C  CG   . PHE   D 1 133 ? -21.869 -27.160 -30.143 1.00 24.32  ? 133 PHE   D CG   1 
ATOM   6463 C  CD1  . PHE   D 1 133 ? -22.099 -28.451 -30.568 1.00 24.85  ? 133 PHE   D CD1  1 
ATOM   6464 C  CD2  . PHE   D 1 133 ? -20.927 -26.404 -30.805 1.00 23.42  ? 133 PHE   D CD2  1 
ATOM   6465 C  CE1  . PHE   D 1 133 ? -21.406 -28.969 -31.646 1.00 25.00  ? 133 PHE   D CE1  1 
ATOM   6466 C  CE2  . PHE   D 1 133 ? -20.222 -26.923 -31.874 1.00 24.17  ? 133 PHE   D CE2  1 
ATOM   6467 C  CZ   . PHE   D 1 133 ? -20.466 -28.205 -32.295 1.00 26.07  ? 133 PHE   D CZ   1 
ATOM   6468 N  N    . SER   D 1 134 ? -22.503 -25.349 -25.792 1.00 34.70  ? 134 SER   D N    1 
ATOM   6469 C  CA   . SER   D 1 134 ? -23.386 -24.713 -24.785 1.00 38.96  ? 134 SER   D CA   1 
ATOM   6470 C  C    . SER   D 1 134 ? -24.046 -23.482 -25.417 1.00 37.44  ? 134 SER   D C    1 
ATOM   6471 O  O    . SER   D 1 134 ? -23.691 -23.132 -26.555 1.00 34.87  ? 134 SER   D O    1 
ATOM   6472 C  CB   . SER   D 1 134 ? -22.645 -24.408 -23.489 1.00 40.86  ? 134 SER   D CB   1 
ATOM   6473 O  OG   . SER   D 1 134 ? -21.701 -23.361 -23.657 1.00 45.69  ? 134 SER   D OG   1 
ATOM   6474 N  N    . LYS   D 1 135 ? -24.912 -22.822 -24.653 1.00 41.13  ? 135 LYS   D N    1 
ATOM   6475 C  CA   . LYS   D 1 135 ? -25.941 -21.858 -25.115 1.00 47.67  ? 135 LYS   D CA   1 
ATOM   6476 C  C    . LYS   D 1 135 ? -25.277 -20.517 -25.449 1.00 46.01  ? 135 LYS   D C    1 
ATOM   6477 O  O    . LYS   D 1 135 ? -25.717 -19.861 -26.411 1.00 47.66  ? 135 LYS   D O    1 
ATOM   6478 C  CB   . LYS   D 1 135 ? -27.019 -21.709 -24.036 1.00 54.90  ? 135 LYS   D CB   1 
ATOM   6479 C  CG   . LYS   D 1 135 ? -27.749 -22.996 -23.645 1.00 64.56  ? 135 LYS   D CG   1 
ATOM   6480 C  CD   . LYS   D 1 135 ? -26.899 -24.140 -23.025 1.00 67.60  ? 135 LYS   D CD   1 
ATOM   6481 C  CE   . LYS   D 1 135 ? -26.311 -23.837 -21.655 1.00 73.86  ? 135 LYS   D CE   1 
ATOM   6482 N  NZ   . LYS   D 1 135 ? -25.706 -25.033 -21.012 1.00 71.54  ? 135 LYS   D NZ   1 
ATOM   6483 N  N    . ASP   D 1 136 ? -24.255 -20.122 -24.690 1.00 43.90  ? 136 ASP   D N    1 
ATOM   6484 C  CA   . ASP   D 1 136 ? -23.388 -18.969 -25.048 1.00 44.31  ? 136 ASP   D CA   1 
ATOM   6485 C  C    . ASP   D 1 136 ? -21.957 -19.494 -25.229 1.00 43.45  ? 136 ASP   D C    1 
ATOM   6486 O  O    . ASP   D 1 136 ? -21.181 -19.589 -24.236 1.00 44.24  ? 136 ASP   D O    1 
ATOM   6487 C  CB   . ASP   D 1 136 ? -23.508 -17.837 -24.029 1.00 49.70  ? 136 ASP   D CB   1 
ATOM   6488 C  CG   . ASP   D 1 136 ? -22.581 -16.673 -24.340 1.00 54.12  ? 136 ASP   D CG   1 
ATOM   6489 O  OD1  . ASP   D 1 136 ? -22.427 -16.333 -25.547 1.00 53.00  ? 136 ASP   D OD1  1 
ATOM   6490 O  OD2  . ASP   D 1 136 ? -21.998 -16.135 -23.377 1.00 55.47  ? 136 ASP   D OD2  1 
ATOM   6491 N  N    . GLN   D 1 137 ? -21.644 -19.867 -26.464 1.00 34.29  ? 137 GLN   D N    1 
ATOM   6492 C  CA   . GLN   D 1 137 ? -20.371 -20.502 -26.855 1.00 31.11  ? 137 GLN   D CA   1 
ATOM   6493 C  C    . GLN   D 1 137 ? -19.472 -19.382 -27.382 1.00 27.69  ? 137 GLN   D C    1 
ATOM   6494 O  O    . GLN   D 1 137 ? -19.536 -19.080 -28.575 1.00 24.10  ? 137 GLN   D O    1 
ATOM   6495 C  CB   . GLN   D 1 137 ? -20.697 -21.612 -27.854 1.00 32.15  ? 137 GLN   D CB   1 
ATOM   6496 C  CG   . GLN   D 1 137 ? -19.507 -22.439 -28.297 1.00 32.92  ? 137 GLN   D CG   1 
ATOM   6497 C  CD   . GLN   D 1 137 ? -19.098 -23.477 -27.291 1.00 34.71  ? 137 GLN   D CD   1 
ATOM   6498 O  OE1  . GLN   D 1 137 ? -19.910 -24.292 -26.853 1.00 38.95  ? 137 GLN   D OE1  1 
ATOM   6499 N  NE2  . GLN   D 1 137 ? -17.818 -23.466 -26.949 1.00 32.67  ? 137 GLN   D NE2  1 
ATOM   6500 N  N    . LYS   D 1 138 ? -18.677 -18.763 -26.505 1.00 25.96  ? 138 LYS   D N    1 
ATOM   6501 C  CA   . LYS   D 1 138 ? -17.984 -17.488 -26.827 1.00 23.41  ? 138 LYS   D CA   1 
ATOM   6502 C  C    . LYS   D 1 138 ? -16.840 -17.714 -27.824 1.00 21.87  ? 138 LYS   D C    1 
ATOM   6503 O  O    . LYS   D 1 138 ? -16.313 -16.686 -28.308 1.00 21.19  ? 138 LYS   D O    1 
ATOM   6504 C  CB   . LYS   D 1 138 ? -17.467 -16.797 -25.569 1.00 23.44  ? 138 LYS   D CB   1 
ATOM   6505 C  CG   . LYS   D 1 138 ? -18.534 -16.286 -24.623 1.00 24.13  ? 138 LYS   D CG   1 
ATOM   6506 C  CD   . LYS   D 1 138 ? -18.020 -15.148 -23.767 1.00 26.28  ? 138 LYS   D CD   1 
ATOM   6507 C  CE   . LYS   D 1 138 ? -18.831 -14.887 -22.513 1.00 26.96  ? 138 LYS   D CE   1 
ATOM   6508 N  NZ   . LYS   D 1 138 ? -20.209 -14.446 -22.827 1.00 28.65  ? 138 LYS   D NZ   1 
ATOM   6509 N  N    . ASP   D 1 139 ? -16.469 -18.963 -28.150 1.00 19.04  ? 139 ASP   D N    1 
ATOM   6510 C  CA   . ASP   D 1 139 ? -15.440 -19.222 -29.197 1.00 20.79  ? 139 ASP   D CA   1 
ATOM   6511 C  C    . ASP   D 1 139 ? -16.105 -19.469 -30.557 1.00 20.29  ? 139 ASP   D C    1 
ATOM   6512 O  O    . ASP   D 1 139 ? -15.362 -19.808 -31.491 1.00 21.44  ? 139 ASP   D O    1 
ATOM   6513 C  CB   . ASP   D 1 139 ? -14.451 -20.338 -28.813 1.00 22.07  ? 139 ASP   D CB   1 
ATOM   6514 C  CG   . ASP   D 1 139 ? -15.106 -21.591 -28.272 1.00 22.78  ? 139 ASP   D CG   1 
ATOM   6515 O  OD1  . ASP   D 1 139 ? -16.354 -21.659 -28.352 1.00 28.70  ? 139 ASP   D OD1  1 
ATOM   6516 O  OD2  . ASP   D 1 139 ? -14.387 -22.481 -27.759 1.00 21.78  ? 139 ASP   D OD2  1 
ATOM   6517 N  N    . LEU   D 1 140 ? -17.426 -19.282 -30.685 1.00 19.88  ? 140 LEU   D N    1 
ATOM   6518 C  CA   . LEU   D 1 140 ? -18.174 -19.449 -31.957 1.00 19.99  ? 140 LEU   D CA   1 
ATOM   6519 C  C    . LEU   D 1 140 ? -18.847 -18.118 -32.338 1.00 19.88  ? 140 LEU   D C    1 
ATOM   6520 O  O    . LEU   D 1 140 ? -19.417 -17.461 -31.479 1.00 19.43  ? 140 LEU   D O    1 
ATOM   6521 C  CB   . LEU   D 1 140 ? -19.219 -20.566 -31.801 1.00 20.80  ? 140 LEU   D CB   1 
ATOM   6522 C  CG   . LEU   D 1 140 ? -18.714 -22.020 -31.808 1.00 21.24  ? 140 LEU   D CG   1 
ATOM   6523 C  CD1  . LEU   D 1 140 ? -19.887 -22.976 -31.911 1.00 21.66  ? 140 LEU   D CD1  1 
ATOM   6524 C  CD2  . LEU   D 1 140 ? -17.734 -22.288 -32.949 1.00 20.48  ? 140 LEU   D CD2  1 
ATOM   6525 N  N    . ILE   D 1 141 ? -18.779 -17.741 -33.603 1.00 19.22  ? 141 ILE   D N    1 
ATOM   6526 C  CA   . ILE   D 1 141 ? -19.601 -16.644 -34.177 1.00 20.09  ? 141 ILE   D CA   1 
ATOM   6527 C  C    . ILE   D 1 141 ? -20.813 -17.300 -34.827 1.00 19.98  ? 141 ILE   D C    1 
ATOM   6528 O  O    . ILE   D 1 141 ? -20.625 -18.000 -35.811 1.00 20.19  ? 141 ILE   D O    1 
ATOM   6529 C  CB   . ILE   D 1 141 ? -18.792 -15.819 -35.192 1.00 19.25  ? 141 ILE   D CB   1 
ATOM   6530 C  CG1  . ILE   D 1 141 ? -17.548 -15.223 -34.540 1.00 19.88  ? 141 ILE   D CG1  1 
ATOM   6531 C  CG2  . ILE   D 1 141 ? -19.655 -14.747 -35.841 1.00 20.44  ? 141 ILE   D CG2  1 
ATOM   6532 C  CD1  . ILE   D 1 141 ? -16.548 -14.709 -35.540 1.00 21.04  ? 141 ILE   D CD1  1 
ATOM   6533 N  N    . LEU   D 1 142 ? -21.987 -17.129 -34.245 1.00 20.25  ? 142 LEU   D N    1 
ATOM   6534 C  CA   . LEU   D 1 142 ? -23.252 -17.640 -34.836 1.00 21.72  ? 142 LEU   D CA   1 
ATOM   6535 C  C    . LEU   D 1 142 ? -23.845 -16.563 -35.749 1.00 21.75  ? 142 LEU   D C    1 
ATOM   6536 O  O    . LEU   D 1 142 ? -23.936 -15.419 -35.324 1.00 22.78  ? 142 LEU   D O    1 
ATOM   6537 C  CB   . LEU   D 1 142 ? -24.220 -18.017 -33.710 1.00 22.25  ? 142 LEU   D CB   1 
ATOM   6538 C  CG   . LEU   D 1 142 ? -23.729 -19.121 -32.772 1.00 22.17  ? 142 LEU   D CG   1 
ATOM   6539 C  CD1  . LEU   D 1 142 ? -24.849 -19.584 -31.856 1.00 23.77  ? 142 LEU   D CD1  1 
ATOM   6540 C  CD2  . LEU   D 1 142 ? -23.171 -20.295 -33.560 1.00 22.50  ? 142 LEU   D CD2  1 
ATOM   6541 N  N    . GLN   D 1 143 ? -24.217 -16.948 -36.966 1.00 21.48  ? 143 GLN   D N    1 
ATOM   6542 C  CA   . GLN   D 1 143 ? -24.814 -16.077 -37.993 1.00 20.22  ? 143 GLN   D CA   1 
ATOM   6543 C  C    . GLN   D 1 143 ? -26.167 -16.671 -38.388 1.00 21.01  ? 143 GLN   D C    1 
ATOM   6544 O  O    . GLN   D 1 143 ? -26.315 -17.903 -38.335 1.00 21.40  ? 143 GLN   D O    1 
ATOM   6545 C  CB   . GLN   D 1 143 ? -23.827 -15.968 -39.148 1.00 20.17  ? 143 GLN   D CB   1 
ATOM   6546 C  CG   . GLN   D 1 143 ? -22.538 -15.237 -38.778 1.00 19.54  ? 143 GLN   D CG   1 
ATOM   6547 C  CD   . GLN   D 1 143 ? -21.543 -15.257 -39.908 1.00 20.11  ? 143 GLN   D CD   1 
ATOM   6548 O  OE1  . GLN   D 1 143 ? -21.584 -16.138 -40.758 1.00 21.87  ? 143 GLN   D OE1  1 
ATOM   6549 N  NE2  . GLN   D 1 143 ? -20.629 -14.297 -39.946 1.00 19.95  ? 143 GLN   D NE2  1 
ATOM   6550 N  N    . GLY   D 1 144 ? -27.124 -15.814 -38.748 1.00 21.86  ? 144 GLY   D N    1 
ATOM   6551 C  CA   . GLY   D 1 144 ? -28.437 -16.205 -39.278 1.00 21.90  ? 144 GLY   D CA   1 
ATOM   6552 C  C    . GLY   D 1 144 ? -29.230 -16.935 -38.222 1.00 24.67  ? 144 GLY   D C    1 
ATOM   6553 O  O    . GLY   D 1 144 ? -29.311 -16.403 -37.097 1.00 24.76  ? 144 GLY   D O    1 
ATOM   6554 N  N    . ASP   D 1 145 ? -29.728 -18.136 -38.544 1.00 26.13  ? 145 ASP   D N    1 
ATOM   6555 C  CA   . ASP   D 1 145 ? -30.663 -18.914 -37.692 1.00 28.33  ? 145 ASP   D CA   1 
ATOM   6556 C  C    . ASP   D 1 145 ? -29.904 -19.892 -36.771 1.00 27.96  ? 145 ASP   D C    1 
ATOM   6557 O  O    . ASP   D 1 145 ? -30.567 -20.524 -35.927 1.00 29.77  ? 145 ASP   D O    1 
ATOM   6558 C  CB   . ASP   D 1 145 ? -31.674 -19.668 -38.564 1.00 34.23  ? 145 ASP   D CB   1 
ATOM   6559 C  CG   . ASP   D 1 145 ? -32.627 -18.803 -39.397 1.00 36.03  ? 145 ASP   D CG   1 
ATOM   6560 O  OD1  . ASP   D 1 145 ? -32.352 -17.597 -39.567 1.00 39.87  ? 145 ASP   D OD1  1 
ATOM   6561 O  OD2  . ASP   D 1 145 ? -33.637 -19.356 -39.898 1.00 35.29  ? 145 ASP   D OD2  1 
ATOM   6562 N  N    . ALA   D 1 146 ? -28.581 -20.019 -36.895 1.00 26.16  ? 146 ALA   D N    1 
ATOM   6563 C  CA   . ALA   D 1 146 ? -27.761 -20.982 -36.116 1.00 25.49  ? 146 ALA   D CA   1 
ATOM   6564 C  C    . ALA   D 1 146 ? -27.935 -20.731 -34.618 1.00 26.86  ? 146 ALA   D C    1 
ATOM   6565 O  O    . ALA   D 1 146 ? -27.878 -19.565 -34.223 1.00 29.03  ? 146 ALA   D O    1 
ATOM   6566 C  CB   . ALA   D 1 146 ? -26.321 -20.864 -36.509 1.00 24.90  ? 146 ALA   D CB   1 
ATOM   6567 N  N    . THR   D 1 147 ? -28.155 -21.785 -33.824 1.00 27.29  ? 147 THR   D N    1 
ATOM   6568 C  CA   . THR   D 1 147 ? -28.180 -21.740 -32.336 1.00 29.99  ? 147 THR   D CA   1 
ATOM   6569 C  C    . THR   D 1 147 ? -27.413 -22.935 -31.749 1.00 30.10  ? 147 THR   D C    1 
ATOM   6570 O  O    . THR   D 1 147 ? -27.231 -23.938 -32.481 1.00 29.09  ? 147 THR   D O    1 
ATOM   6571 C  CB   . THR   D 1 147 ? -29.616 -21.701 -31.830 1.00 33.37  ? 147 THR   D CB   1 
ATOM   6572 O  OG1  . THR   D 1 147 ? -30.196 -22.945 -32.224 1.00 38.11  ? 147 THR   D OG1  1 
ATOM   6573 C  CG2  . THR   D 1 147 ? -30.397 -20.534 -32.395 1.00 35.06  ? 147 THR   D CG2  1 
ATOM   6574 N  N    . THR   D 1 148 ? -26.975 -22.812 -30.490 1.00 30.98  ? 148 THR   D N    1 
ATOM   6575 C  CA   . THR   D 1 148 ? -26.126 -23.795 -29.751 1.00 32.59  ? 148 THR   D CA   1 
ATOM   6576 C  C    . THR   D 1 148 ? -26.782 -24.145 -28.412 1.00 34.33  ? 148 THR   D C    1 
ATOM   6577 O  O    . THR   D 1 148 ? -27.415 -23.251 -27.821 1.00 33.95  ? 148 THR   D O    1 
ATOM   6578 C  CB   . THR   D 1 148 ? -24.695 -23.282 -29.485 1.00 33.15  ? 148 THR   D CB   1 
ATOM   6579 O  OG1  . THR   D 1 148 ? -24.698 -22.044 -28.764 1.00 31.20  ? 148 THR   D OG1  1 
ATOM   6580 C  CG2  . THR   D 1 148 ? -23.870 -23.111 -30.745 1.00 33.35  ? 148 THR   D CG2  1 
ATOM   6581 N  N    . GLY   D 1 149 ? -26.646 -25.400 -27.965 1.00 36.18  ? 149 GLY   D N    1 
ATOM   6582 C  CA   . GLY   D 1 149 ? -26.988 -25.821 -26.589 1.00 40.86  ? 149 GLY   D CA   1 
ATOM   6583 C  C    . GLY   D 1 149 ? -28.245 -26.680 -26.478 1.00 43.48  ? 149 GLY   D C    1 
ATOM   6584 O  O    . GLY   D 1 149 ? -28.403 -27.336 -25.421 1.00 42.43  ? 149 GLY   D O    1 
ATOM   6585 N  N    . THR   D 1 150 ? -29.122 -26.664 -27.487 1.00 43.43  ? 150 THR   D N    1 
ATOM   6586 C  CA   . THR   D 1 150 ? -30.274 -27.599 -27.604 1.00 43.87  ? 150 THR   D CA   1 
ATOM   6587 C  C    . THR   D 1 150 ? -29.705 -29.011 -27.764 1.00 43.34  ? 150 THR   D C    1 
ATOM   6588 O  O    . THR   D 1 150 ? -29.165 -29.277 -28.860 1.00 44.25  ? 150 THR   D O    1 
ATOM   6589 C  CB   . THR   D 1 150 ? -31.202 -27.201 -28.768 1.00 46.59  ? 150 THR   D CB   1 
ATOM   6590 O  OG1  . THR   D 1 150 ? -31.579 -25.835 -28.589 1.00 45.06  ? 150 THR   D OG1  1 
ATOM   6591 C  CG2  . THR   D 1 150 ? -32.456 -28.048 -28.863 1.00 45.51  ? 150 THR   D CG2  1 
ATOM   6592 N  N    . ASP   D 1 151 ? -29.797 -29.846 -26.713 1.00 45.00  ? 151 ASP   D N    1 
ATOM   6593 C  CA   . ASP   D 1 151 ? -29.308 -31.259 -26.643 1.00 48.60  ? 151 ASP   D CA   1 
ATOM   6594 C  C    . ASP   D 1 151 ? -27.776 -31.285 -26.552 1.00 43.11  ? 151 ASP   D C    1 
ATOM   6595 O  O    . ASP   D 1 151 ? -27.173 -32.350 -26.798 1.00 39.51  ? 151 ASP   D O    1 
ATOM   6596 C  CB   . ASP   D 1 151 ? -29.764 -32.098 -27.845 1.00 56.21  ? 151 ASP   D CB   1 
ATOM   6597 C  CG   . ASP   D 1 151 ? -31.151 -32.700 -27.701 1.00 66.36  ? 151 ASP   D CG   1 
ATOM   6598 O  OD1  . ASP   D 1 151 ? -31.319 -33.543 -26.799 1.00 72.85  ? 151 ASP   D OD1  1 
ATOM   6599 O  OD2  . ASP   D 1 151 ? -32.049 -32.325 -28.498 1.00 71.89  ? 151 ASP   D OD2  1 
ATOM   6600 N  N    . GLY   D 1 152 ? -27.167 -30.148 -26.223 1.00 40.92  ? 152 GLY   D N    1 
ATOM   6601 C  CA   . GLY   D 1 152 ? -25.707 -29.959 -26.318 1.00 36.31  ? 152 GLY   D CA   1 
ATOM   6602 C  C    . GLY   D 1 152 ? -25.246 -29.905 -27.759 1.00 32.12  ? 152 GLY   D C    1 
ATOM   6603 O  O    . GLY   D 1 152 ? -24.059 -30.163 -27.987 1.00 27.86  ? 152 GLY   D O    1 
ATOM   6604 N  N    . ASN   D 1 153 ? -26.134 -29.527 -28.690 1.00 31.26  ? 153 ASN   D N    1 
ATOM   6605 C  CA   . ASN   D 1 153 ? -25.893 -29.577 -30.161 1.00 28.91  ? 153 ASN   D CA   1 
ATOM   6606 C  C    . ASN   D 1 153 ? -25.855 -28.167 -30.769 1.00 27.77  ? 153 ASN   D C    1 
ATOM   6607 O  O    . ASN   D 1 153 ? -26.369 -27.223 -30.147 1.00 28.20  ? 153 ASN   D O    1 
ATOM   6608 C  CB   . ASN   D 1 153 ? -26.966 -30.401 -30.877 1.00 30.47  ? 153 ASN   D CB   1 
ATOM   6609 C  CG   . ASN   D 1 153 ? -26.914 -31.888 -30.576 1.00 31.98  ? 153 ASN   D CG   1 
ATOM   6610 O  OD1  . ASN   D 1 153 ? -25.835 -32.488 -30.512 1.00 33.98  ? 153 ASN   D OD1  1 
ATOM   6611 N  ND2  . ASN   D 1 153 ? -28.077 -32.502 -30.445 1.00 26.89  ? 153 ASN   D ND2  1 
ATOM   6612 N  N    . LEU   D 1 154 ? -25.266 -28.061 -31.962 1.00 26.63  ? 154 LEU   D N    1 
ATOM   6613 C  CA   . LEU   D 1 154 ? -25.287 -26.878 -32.860 1.00 26.50  ? 154 LEU   D CA   1 
ATOM   6614 C  C    . LEU   D 1 154 ? -26.385 -27.088 -33.916 1.00 26.45  ? 154 LEU   D C    1 
ATOM   6615 O  O    . LEU   D 1 154 ? -26.189 -27.926 -34.785 1.00 28.36  ? 154 LEU   D O    1 
ATOM   6616 C  CB   . LEU   D 1 154 ? -23.880 -26.736 -33.472 1.00 25.89  ? 154 LEU   D CB   1 
ATOM   6617 C  CG   . LEU   D 1 154 ? -23.699 -25.730 -34.609 1.00 25.56  ? 154 LEU   D CG   1 
ATOM   6618 C  CD1  . LEU   D 1 154 ? -24.145 -24.337 -34.201 1.00 27.95  ? 154 LEU   D CD1  1 
ATOM   6619 C  CD2  . LEU   D 1 154 ? -22.251 -25.696 -35.075 1.00 25.89  ? 154 LEU   D CD2  1 
ATOM   6620 N  N    . GLU   D 1 155 ? -27.516 -26.376 -33.815 1.00 29.07  ? 155 GLU   D N    1 
ATOM   6621 C  CA   . GLU   D 1 155 ? -28.607 -26.375 -34.831 1.00 29.53  ? 155 GLU   D CA   1 
ATOM   6622 C  C    . GLU   D 1 155 ? -28.340 -25.286 -35.870 1.00 27.01  ? 155 GLU   D C    1 
ATOM   6623 O  O    . GLU   D 1 155 ? -28.590 -24.123 -35.581 1.00 26.33  ? 155 GLU   D O    1 
ATOM   6624 C  CB   . GLU   D 1 155 ? -29.968 -26.132 -34.176 1.00 33.34  ? 155 GLU   D CB   1 
ATOM   6625 C  CG   . GLU   D 1 155 ? -30.405 -27.250 -33.253 1.00 35.61  ? 155 GLU   D CG   1 
ATOM   6626 C  CD   . GLU   D 1 155 ? -30.691 -28.598 -33.904 1.00 36.90  ? 155 GLU   D CD   1 
ATOM   6627 O  OE1  . GLU   D 1 155 ? -30.651 -28.712 -35.170 1.00 33.09  ? 155 GLU   D OE1  1 
ATOM   6628 O  OE2  . GLU   D 1 155 ? -30.947 -29.544 -33.133 1.00 39.26  ? 155 GLU   D OE2  1 
ATOM   6629 N  N    . LEU   D 1 156 ? -27.804 -25.649 -37.029 1.00 27.85  ? 156 LEU   D N    1 
ATOM   6630 C  CA   . LEU   D 1 156 ? -27.420 -24.656 -38.067 1.00 27.93  ? 156 LEU   D CA   1 
ATOM   6631 C  C    . LEU   D 1 156 ? -28.660 -23.949 -38.642 1.00 28.37  ? 156 LEU   D C    1 
ATOM   6632 O  O    . LEU   D 1 156 ? -28.555 -22.730 -38.884 1.00 25.53  ? 156 LEU   D O    1 
ATOM   6633 C  CB   . LEU   D 1 156 ? -26.589 -25.333 -39.155 1.00 26.67  ? 156 LEU   D CB   1 
ATOM   6634 C  CG   . LEU   D 1 156 ? -25.160 -25.660 -38.738 1.00 27.55  ? 156 LEU   D CG   1 
ATOM   6635 C  CD1  . LEU   D 1 156 ? -24.452 -26.450 -39.824 1.00 27.87  ? 156 LEU   D CD1  1 
ATOM   6636 C  CD2  . LEU   D 1 156 ? -24.392 -24.386 -38.411 1.00 28.48  ? 156 LEU   D CD2  1 
ATOM   6637 N  N    . THR   D 1 157 ? -29.784 -24.660 -38.828 1.00 29.14  ? 157 THR   D N    1 
ATOM   6638 C  CA   . THR   D 1 157 ? -31.040 -24.104 -39.421 1.00 29.71  ? 157 THR   D CA   1 
ATOM   6639 C  C    . THR   D 1 157 ? -32.153 -24.224 -38.380 1.00 32.42  ? 157 THR   D C    1 
ATOM   6640 O  O    . THR   D 1 157 ? -32.035 -25.076 -37.478 1.00 35.64  ? 157 THR   D O    1 
ATOM   6641 C  CB   . THR   D 1 157 ? -31.369 -24.701 -40.805 1.00 27.68  ? 157 THR   D CB   1 
ATOM   6642 O  OG1  . THR   D 1 157 ? -31.436 -26.132 -40.818 1.00 24.89  ? 157 THR   D OG1  1 
ATOM   6643 C  CG2  . THR   D 1 157 ? -30.370 -24.281 -41.864 1.00 26.59  ? 157 THR   D CG2  1 
ATOM   6644 N  N    . ARG   D 1 158 ? -33.156 -23.353 -38.495 1.00 36.23  ? 158 ARG   D N    1 
ATOM   6645 C  CA   . ARG   D 1 158 ? -34.304 -23.213 -37.566 1.00 40.54  ? 158 ARG   D CA   1 
ATOM   6646 C  C    . ARG   D 1 158 ? -35.029 -24.561 -37.457 1.00 39.41  ? 158 ARG   D C    1 
ATOM   6647 O  O    . ARG   D 1 158 ? -35.178 -25.248 -38.492 1.00 36.66  ? 158 ARG   D O    1 
ATOM   6648 C  CB   . ARG   D 1 158 ? -35.217 -22.085 -38.056 1.00 44.70  ? 158 ARG   D CB   1 
ATOM   6649 C  CG   . ARG   D 1 158 ? -36.308 -21.668 -37.082 1.00 50.52  ? 158 ARG   D CG   1 
ATOM   6650 C  CD   . ARG   D 1 158 ? -36.867 -20.293 -37.444 1.00 57.70  ? 158 ARG   D CD   1 
ATOM   6651 N  NE   . ARG   D 1 158 ? -35.980 -19.238 -36.962 1.00 62.49  ? 158 ARG   D NE   1 
ATOM   6652 C  CZ   . ARG   D 1 158 ? -35.891 -18.844 -35.691 1.00 67.05  ? 158 ARG   D CZ   1 
ATOM   6653 N  NH1  . ARG   D 1 158 ? -36.657 -19.398 -34.761 1.00 67.22  ? 158 ARG   D NH1  1 
ATOM   6654 N  NH2  . ARG   D 1 158 ? -35.037 -17.892 -35.350 1.00 66.29  ? 158 ARG   D NH2  1 
ATOM   6655 N  N    . VAL   D 1 159 ? -35.391 -24.914 -36.223 1.00 40.54  ? 159 VAL   D N    1 
ATOM   6656 C  CA   . VAL   D 1 159 ? -36.113 -26.150 -35.805 1.00 45.41  ? 159 VAL   D CA   1 
ATOM   6657 C  C    . VAL   D 1 159 ? -37.134 -25.745 -34.737 1.00 46.84  ? 159 VAL   D C    1 
ATOM   6658 O  O    . VAL   D 1 159 ? -36.832 -24.822 -33.968 1.00 42.08  ? 159 VAL   D O    1 
ATOM   6659 C  CB   . VAL   D 1 159 ? -35.138 -27.219 -35.273 1.00 47.19  ? 159 VAL   D CB   1 
ATOM   6660 C  CG1  . VAL   D 1 159 ? -35.868 -28.470 -34.793 1.00 47.47  ? 159 VAL   D CG1  1 
ATOM   6661 C  CG2  . VAL   D 1 159 ? -34.086 -27.569 -36.312 1.00 44.33  ? 159 VAL   D CG2  1 
ATOM   6662 N  N    . SER   D 1 160 ? -38.305 -26.393 -34.736 1.00 52.14  ? 160 SER   D N    1 
ATOM   6663 C  CA   . SER   D 1 160 ? -39.437 -26.178 -33.791 1.00 55.62  ? 160 SER   D CA   1 
ATOM   6664 C  C    . SER   D 1 160 ? -39.168 -26.949 -32.491 1.00 57.01  ? 160 SER   D C    1 
ATOM   6665 O  O    . SER   D 1 160 ? -38.221 -27.752 -32.488 1.00 58.59  ? 160 SER   D O    1 
ATOM   6666 C  CB   . SER   D 1 160 ? -40.724 -26.627 -34.425 1.00 53.27  ? 160 SER   D CB   1 
ATOM   6667 O  OG   . SER   D 1 160 ? -40.718 -28.039 -34.584 1.00 52.37  ? 160 SER   D OG   1 
ATOM   6668 N  N    . SER   D 1 161 ? -39.975 -26.741 -31.443 1.00 59.63  ? 161 SER   D N    1 
ATOM   6669 C  CA   . SER   D 1 161 ? -39.865 -27.451 -30.132 1.00 61.98  ? 161 SER   D CA   1 
ATOM   6670 C  C    . SER   D 1 161 ? -40.107 -28.966 -30.305 1.00 65.66  ? 161 SER   D C    1 
ATOM   6671 O  O    . SER   D 1 161 ? -39.415 -29.762 -29.610 1.00 56.71  ? 161 SER   D O    1 
ATOM   6672 C  CB   . SER   D 1 161 ? -40.811 -26.864 -29.105 1.00 60.72  ? 161 SER   D CB   1 
ATOM   6673 O  OG   . SER   D 1 161 ? -42.109 -26.665 -29.659 1.00 64.52  ? 161 SER   D OG   1 
ATOM   6674 N  N    . ASN   D 1 162 ? -41.047 -29.343 -31.192 1.00 63.40  ? 162 ASN   D N    1 
ATOM   6675 C  CA   . ASN   D 1 162 ? -41.454 -30.749 -31.485 1.00 62.26  ? 162 ASN   D CA   1 
ATOM   6676 C  C    . ASN   D 1 162 ? -40.328 -31.472 -32.238 1.00 60.33  ? 162 ASN   D C    1 
ATOM   6677 O  O    . ASN   D 1 162 ? -40.291 -32.716 -32.157 1.00 62.64  ? 162 ASN   D O    1 
ATOM   6678 C  CB   . ASN   D 1 162 ? -42.801 -30.830 -32.229 1.00 64.24  ? 162 ASN   D CB   1 
ATOM   6679 C  CG   . ASN   D 1 162 ? -42.779 -30.338 -33.667 1.00 63.38  ? 162 ASN   D CG   1 
ATOM   6680 O  OD1  . ASN   D 1 162 ? -42.342 -31.054 -34.565 1.00 63.68  ? 162 ASN   D OD1  1 
ATOM   6681 N  ND2  . ASN   D 1 162 ? -43.301 -29.143 -33.909 1.00 56.89  ? 162 ASN   D ND2  1 
ATOM   6682 N  N    . GLY   D 1 163 ? -39.455 -30.723 -32.929 1.00 54.93  ? 163 GLY   D N    1 
ATOM   6683 C  CA   . GLY   D 1 163 ? -38.276 -31.235 -33.659 1.00 51.27  ? 163 GLY   D CA   1 
ATOM   6684 C  C    . GLY   D 1 163 ? -38.451 -31.166 -35.175 1.00 51.31  ? 163 GLY   D C    1 
ATOM   6685 O  O    . GLY   D 1 163 ? -37.683 -31.856 -35.901 1.00 50.35  ? 163 GLY   D O    1 
ATOM   6686 N  N    . SER   D 1 164 ? -39.409 -30.368 -35.663 1.00 45.58  ? 164 SER   D N    1 
ATOM   6687 C  CA   . SER   D 1 164 ? -39.722 -30.258 -37.113 1.00 46.30  ? 164 SER   D CA   1 
ATOM   6688 C  C    . SER   D 1 164 ? -38.907 -29.122 -37.728 1.00 42.33  ? 164 SER   D C    1 
ATOM   6689 O  O    . SER   D 1 164 ? -38.977 -27.972 -37.273 1.00 39.13  ? 164 SER   D O    1 
ATOM   6690 C  CB   . SER   D 1 164 ? -41.199 -30.088 -37.362 1.00 46.37  ? 164 SER   D CB   1 
ATOM   6691 O  OG   . SER   D 1 164 ? -41.622 -28.777 -37.022 1.00 49.13  ? 164 SER   D OG   1 
ATOM   6692 N  N    . PRO   D 1 165 ? -38.107 -29.406 -38.782 1.00 39.01  ? 165 PRO   D N    1 
ATOM   6693 C  CA   . PRO   D 1 165 ? -37.326 -28.360 -39.438 1.00 39.25  ? 165 PRO   D CA   1 
ATOM   6694 C  C    . PRO   D 1 165 ? -38.273 -27.328 -40.053 1.00 40.82  ? 165 PRO   D C    1 
ATOM   6695 O  O    . PRO   D 1 165 ? -39.459 -27.595 -40.134 1.00 42.93  ? 165 PRO   D O    1 
ATOM   6696 C  CB   . PRO   D 1 165 ? -36.513 -29.088 -40.517 1.00 40.30  ? 165 PRO   D CB   1 
ATOM   6697 C  CG   . PRO   D 1 165 ? -37.249 -30.404 -40.731 1.00 38.87  ? 165 PRO   D CG   1 
ATOM   6698 C  CD   . PRO   D 1 165 ? -37.916 -30.725 -39.405 1.00 37.46  ? 165 PRO   D CD   1 
ATOM   6699 N  N    . GLN   D 1 166 ? -37.730 -26.186 -40.466 1.00 43.24  ? 166 GLN   D N    1 
ATOM   6700 C  CA   . GLN   D 1 166 ? -38.495 -25.121 -41.155 1.00 42.65  ? 166 GLN   D CA   1 
ATOM   6701 C  C    . GLN   D 1 166 ? -37.730 -24.655 -42.400 1.00 40.71  ? 166 GLN   D C    1 
ATOM   6702 O  O    . GLN   D 1 166 ? -36.471 -24.689 -42.400 1.00 36.55  ? 166 GLN   D O    1 
ATOM   6703 C  CB   . GLN   D 1 166 ? -38.829 -24.031 -40.142 1.00 47.80  ? 166 GLN   D CB   1 
ATOM   6704 C  CG   . GLN   D 1 166 ? -40.007 -24.440 -39.262 1.00 57.35  ? 166 GLN   D CG   1 
ATOM   6705 C  CD   . GLN   D 1 166 ? -40.753 -23.259 -38.698 1.00 62.08  ? 166 GLN   D CD   1 
ATOM   6706 O  OE1  . GLN   D 1 166 ? -40.155 -22.286 -38.229 1.00 65.32  ? 166 GLN   D OE1  1 
ATOM   6707 N  NE2  . GLN   D 1 166 ? -42.074 -23.348 -38.752 1.00 62.44  ? 166 GLN   D NE2  1 
ATOM   6708 N  N    . GLY   D 1 167 ? -38.486 -24.301 -43.443 1.00 36.30  ? 167 GLY   D N    1 
ATOM   6709 C  CA   . GLY   D 1 167 ? -37.958 -23.854 -44.743 1.00 34.46  ? 167 GLY   D CA   1 
ATOM   6710 C  C    . GLY   D 1 167 ? -37.515 -22.406 -44.684 1.00 32.38  ? 167 GLY   D C    1 
ATOM   6711 O  O    . GLY   D 1 167 ? -37.797 -21.730 -43.668 1.00 29.68  ? 167 GLY   D O    1 
ATOM   6712 N  N    . SER   D 1 168 ? -36.833 -21.934 -45.730 1.00 33.86  ? 168 SER   D N    1 
ATOM   6713 C  CA   . SER   D 1 168 ? -36.377 -20.525 -45.864 1.00 37.31  ? 168 SER   D CA   1 
ATOM   6714 C  C    . SER   D 1 168 ? -35.564 -20.153 -44.617 1.00 38.08  ? 168 SER   D C    1 
ATOM   6715 O  O    . SER   D 1 168 ? -35.835 -19.096 -44.006 1.00 40.83  ? 168 SER   D O    1 
ATOM   6716 C  CB   . SER   D 1 168 ? -37.554 -19.606 -46.084 1.00 36.62  ? 168 SER   D CB   1 
ATOM   6717 O  OG   . SER   D 1 168 ? -38.225 -19.988 -47.270 1.00 37.67  ? 168 SER   D OG   1 
ATOM   6718 N  N    . SER   D 1 169 ? -34.650 -21.052 -44.235 1.00 37.37  ? 169 SER   D N    1 
ATOM   6719 C  CA   . SER   D 1 169 ? -33.777 -20.967 -43.039 1.00 34.07  ? 169 SER   D CA   1 
ATOM   6720 C  C    . SER   D 1 169 ? -32.327 -21.005 -43.512 1.00 30.38  ? 169 SER   D C    1 
ATOM   6721 O  O    . SER   D 1 169 ? -32.053 -21.654 -44.528 1.00 27.97  ? 169 SER   D O    1 
ATOM   6722 C  CB   . SER   D 1 169 ? -34.086 -22.067 -42.050 1.00 35.97  ? 169 SER   D CB   1 
ATOM   6723 O  OG   . SER   D 1 169 ? -33.263 -21.964 -40.897 1.00 37.79  ? 169 SER   D OG   1 
ATOM   6724 N  N    . VAL   D 1 170 ? -31.446 -20.280 -42.833 1.00 29.33  ? 170 VAL   D N    1 
ATOM   6725 C  CA   . VAL   D 1 170 ? -29.991 -20.285 -43.151 1.00 28.46  ? 170 VAL   D CA   1 
ATOM   6726 C  C    . VAL   D 1 170 ? -29.234 -19.871 -41.891 1.00 27.57  ? 170 VAL   D C    1 
ATOM   6727 O  O    . VAL   D 1 170 ? -29.726 -18.979 -41.158 1.00 28.82  ? 170 VAL   D O    1 
ATOM   6728 C  CB   . VAL   D 1 170 ? -29.669 -19.374 -44.347 1.00 28.39  ? 170 VAL   D CB   1 
ATOM   6729 C  CG1  . VAL   D 1 170 ? -29.947 -17.906 -44.049 1.00 29.48  ? 170 VAL   D CG1  1 
ATOM   6730 C  CG2  . VAL   D 1 170 ? -28.234 -19.558 -44.802 1.00 30.88  ? 170 VAL   D CG2  1 
ATOM   6731 N  N    . GLY   D 1 171 ? -28.101 -20.521 -41.641 1.00 25.94  ? 171 GLY   D N    1 
ATOM   6732 C  CA   . GLY   D 1 171 ? -27.295 -20.312 -40.429 1.00 23.46  ? 171 GLY   D CA   1 
ATOM   6733 C  C    . GLY   D 1 171 ? -25.880 -20.830 -40.589 1.00 23.06  ? 171 GLY   D C    1 
ATOM   6734 O  O    . GLY   D 1 171 ? -25.648 -21.796 -41.360 1.00 20.27  ? 171 GLY   D O    1 
ATOM   6735 N  N    . ARG   D 1 172 ? -24.944 -20.209 -39.878 1.00 23.44  ? 172 ARG   D N    1 
ATOM   6736 C  CA   . ARG   D 1 172 ? -23.518 -20.610 -39.913 1.00 23.99  ? 172 ARG   D CA   1 
ATOM   6737 C  C    . ARG   D 1 172 ? -22.939 -20.486 -38.512 1.00 22.70  ? 172 ARG   D C    1 
ATOM   6738 O  O    . ARG   D 1 172 ? -23.590 -19.870 -37.654 1.00 24.72  ? 172 ARG   D O    1 
ATOM   6739 C  CB   . ARG   D 1 172 ? -22.745 -19.761 -40.923 1.00 25.44  ? 172 ARG   D CB   1 
ATOM   6740 C  CG   . ARG   D 1 172 ? -23.481 -19.559 -42.237 1.00 26.76  ? 172 ARG   D CG   1 
ATOM   6741 C  CD   . ARG   D 1 172 ? -22.627 -19.076 -43.405 1.00 28.12  ? 172 ARG   D CD   1 
ATOM   6742 N  NE   . ARG   D 1 172 ? -21.789 -17.919 -43.116 1.00 28.06  ? 172 ARG   D NE   1 
ATOM   6743 C  CZ   . ARG   D 1 172 ? -21.085 -17.239 -44.017 1.00 26.69  ? 172 ARG   D CZ   1 
ATOM   6744 N  NH1  . ARG   D 1 172 ? -21.133 -17.569 -45.293 1.00 25.78  ? 172 ARG   D NH1  1 
ATOM   6745 N  NH2  . ARG   D 1 172 ? -20.310 -16.247 -43.624 1.00 26.17  ? 172 ARG   D NH2  1 
ATOM   6746 N  N    . ALA   D 1 173 ? -21.806 -21.145 -38.295 1.00 21.36  ? 173 ALA   D N    1 
ATOM   6747 C  CA   . ALA   D 1 173 ? -20.973 -21.026 -37.089 1.00 20.20  ? 173 ALA   D CA   1 
ATOM   6748 C  C    . ALA   D 1 173 ? -19.536 -20.961 -37.569 1.00 20.36  ? 173 ALA   D C    1 
ATOM   6749 O  O    . ALA   D 1 173 ? -19.139 -21.842 -38.333 1.00 21.25  ? 173 ALA   D O    1 
ATOM   6750 C  CB   . ALA   D 1 173 ? -21.191 -22.180 -36.154 1.00 21.63  ? 173 ALA   D CB   1 
ATOM   6751 N  N    . LEU   D 1 174 ? -18.816 -19.919 -37.164 1.00 21.13  ? 174 LEU   D N    1 
ATOM   6752 C  CA   . LEU   D 1 174 ? -17.383 -19.736 -37.490 1.00 22.07  ? 174 LEU   D CA   1 
ATOM   6753 C  C    . LEU   D 1 174 ? -16.602 -19.812 -36.186 1.00 20.63  ? 174 LEU   D C    1 
ATOM   6754 O  O    . LEU   D 1 174 ? -17.078 -19.275 -35.184 1.00 20.45  ? 174 LEU   D O    1 
ATOM   6755 C  CB   . LEU   D 1 174 ? -17.161 -18.397 -38.209 1.00 23.68  ? 174 LEU   D CB   1 
ATOM   6756 C  CG   . LEU   D 1 174 ? -17.730 -18.322 -39.626 1.00 26.18  ? 174 LEU   D CG   1 
ATOM   6757 C  CD1  . LEU   D 1 174 ? -19.210 -17.989 -39.595 1.00 27.29  ? 174 LEU   D CD1  1 
ATOM   6758 C  CD2  . LEU   D 1 174 ? -16.968 -17.319 -40.476 1.00 28.21  ? 174 LEU   D CD2  1 
ATOM   6759 N  N    . PHE   D 1 175 ? -15.456 -20.486 -36.210 1.00 20.13  ? 175 PHE   D N    1 
ATOM   6760 C  CA   . PHE   D 1 175 ? -14.502 -20.452 -35.084 1.00 20.56  ? 175 PHE   D CA   1 
ATOM   6761 C  C    . PHE   D 1 175 ? -13.992 -19.001 -34.970 1.00 20.68  ? 175 PHE   D C    1 
ATOM   6762 O  O    . PHE   D 1 175 ? -13.680 -18.354 -36.008 1.00 19.17  ? 175 PHE   D O    1 
ATOM   6763 C  CB   . PHE   D 1 175 ? -13.417 -21.516 -35.251 1.00 19.37  ? 175 PHE   D CB   1 
ATOM   6764 C  CG   . PHE   D 1 175 ? -12.580 -21.627 -34.007 1.00 19.96  ? 175 PHE   D CG   1 
ATOM   6765 C  CD1  . PHE   D 1 175 ? -13.133 -22.135 -32.840 1.00 19.64  ? 175 PHE   D CD1  1 
ATOM   6766 C  CD2  . PHE   D 1 175 ? -11.283 -21.133 -33.968 1.00 19.71  ? 175 PHE   D CD2  1 
ATOM   6767 C  CE1  . PHE   D 1 175 ? -12.379 -22.178 -31.674 1.00 19.07  ? 175 PHE   D CE1  1 
ATOM   6768 C  CE2  . PHE   D 1 175 ? -10.537 -21.188 -32.798 1.00 18.42  ? 175 PHE   D CE2  1 
ATOM   6769 C  CZ   . PHE   D 1 175 ? -11.084 -21.708 -31.656 1.00 17.62  ? 175 PHE   D CZ   1 
ATOM   6770 N  N    . TYR   D 1 176 ? -13.945 -18.502 -33.740 1.00 22.25  ? 176 TYR   D N    1 
ATOM   6771 C  CA   . TYR   D 1 176 ? -13.703 -17.078 -33.391 1.00 24.21  ? 176 TYR   D CA   1 
ATOM   6772 C  C    . TYR   D 1 176 ? -12.267 -16.666 -33.758 1.00 23.85  ? 176 TYR   D C    1 
ATOM   6773 O  O    . TYR   D 1 176 ? -12.109 -15.565 -34.272 1.00 26.34  ? 176 TYR   D O    1 
ATOM   6774 C  CB   . TYR   D 1 176 ? -14.051 -16.821 -31.920 1.00 25.90  ? 176 TYR   D CB   1 
ATOM   6775 C  CG   . TYR   D 1 176 ? -14.213 -15.366 -31.553 1.00 29.71  ? 176 TYR   D CG   1 
ATOM   6776 C  CD1  . TYR   D 1 176 ? -15.424 -14.707 -31.706 1.00 33.41  ? 176 TYR   D CD1  1 
ATOM   6777 C  CD2  . TYR   D 1 176 ? -13.140 -14.634 -31.083 1.00 32.19  ? 176 TYR   D CD2  1 
ATOM   6778 C  CE1  . TYR   D 1 176 ? -15.572 -13.370 -31.374 1.00 36.48  ? 176 TYR   D CE1  1 
ATOM   6779 C  CE2  . TYR   D 1 176 ? -13.266 -13.296 -30.751 1.00 34.88  ? 176 TYR   D CE2  1 
ATOM   6780 C  CZ   . TYR   D 1 176 ? -14.483 -12.661 -30.895 1.00 37.86  ? 176 TYR   D CZ   1 
ATOM   6781 O  OH   . TYR   D 1 176 ? -14.572 -11.339 -30.568 1.00 40.82  ? 176 TYR   D OH   1 
ATOM   6782 N  N    . ALA   D 1 177 ? -11.257 -17.505 -33.532 1.00 23.59  ? 177 ALA   D N    1 
ATOM   6783 C  CA   . ALA   D 1 177 ? -9.849  -17.175 -33.857 1.00 24.39  ? 177 ALA   D CA   1 
ATOM   6784 C  C    . ALA   D 1 177 ? -9.645  -17.345 -35.354 1.00 27.19  ? 177 ALA   D C    1 
ATOM   6785 O  O    . ALA   D 1 177 ? -9.933  -18.412 -35.887 1.00 28.30  ? 177 ALA   D O    1 
ATOM   6786 C  CB   . ALA   D 1 177 ? -8.879  -18.044 -33.093 1.00 23.26  ? 177 ALA   D CB   1 
ATOM   6787 N  N    . PRO   D 1 178 ? -9.121  -16.330 -36.077 1.00 27.54  ? 178 PRO   D N    1 
ATOM   6788 C  CA   . PRO   D 1 178 ? -8.690  -16.540 -37.450 1.00 27.97  ? 178 PRO   D CA   1 
ATOM   6789 C  C    . PRO   D 1 178 ? -7.455  -17.455 -37.530 1.00 27.10  ? 178 PRO   D C    1 
ATOM   6790 O  O    . PRO   D 1 178 ? -6.710  -17.523 -36.565 1.00 24.71  ? 178 PRO   D O    1 
ATOM   6791 C  CB   . PRO   D 1 178 ? -8.390  -15.125 -37.962 1.00 29.38  ? 178 PRO   D CB   1 
ATOM   6792 C  CG   . PRO   D 1 178 ? -8.068  -14.344 -36.719 1.00 30.57  ? 178 PRO   D CG   1 
ATOM   6793 C  CD   . PRO   D 1 178 ? -8.927  -14.946 -35.628 1.00 29.69  ? 178 PRO   D CD   1 
ATOM   6794 N  N    . VAL   D 1 179 ? -7.269  -18.069 -38.707 1.00 25.64  ? 179 VAL   D N    1 
ATOM   6795 C  CA   . VAL   D 1 179 ? -6.295  -19.151 -39.015 1.00 26.68  ? 179 VAL   D CA   1 
ATOM   6796 C  C    . VAL   D 1 179 ? -5.376  -18.693 -40.147 1.00 27.89  ? 179 VAL   D C    1 
ATOM   6797 O  O    . VAL   D 1 179 ? -5.885  -18.093 -41.130 1.00 28.46  ? 179 VAL   D O    1 
ATOM   6798 C  CB   . VAL   D 1 179 ? -7.014  -20.444 -39.423 1.00 27.02  ? 179 VAL   D CB   1 
ATOM   6799 C  CG1  . VAL   D 1 179 ? -6.042  -21.614 -39.504 1.00 28.45  ? 179 VAL   D CG1  1 
ATOM   6800 C  CG2  . VAL   D 1 179 ? -8.187  -20.743 -38.506 1.00 26.21  ? 179 VAL   D CG2  1 
ATOM   6801 N  N    . HIS   D 1 180 ? -4.087  -18.985 -40.005 1.00 27.97  ? 180 HIS   D N    1 
ATOM   6802 C  CA   . HIS   D 1 180 ? -3.020  -18.642 -40.973 1.00 30.54  ? 180 HIS   D CA   1 
ATOM   6803 C  C    . HIS   D 1 180 ? -2.867  -19.832 -41.927 1.00 32.91  ? 180 HIS   D C    1 
ATOM   6804 O  O    . HIS   D 1 180 ? -2.317  -20.876 -41.517 1.00 31.37  ? 180 HIS   D O    1 
ATOM   6805 C  CB   . HIS   D 1 180 ? -1.735  -18.269 -40.218 1.00 30.08  ? 180 HIS   D CB   1 
ATOM   6806 C  CG   . HIS   D 1 180 ? -0.786  -17.416 -40.991 1.00 31.08  ? 180 HIS   D CG   1 
ATOM   6807 N  ND1  . HIS   D 1 180 ? 0.526   -17.201 -40.581 1.00 32.71  ? 180 HIS   D ND1  1 
ATOM   6808 C  CD2  . HIS   D 1 180 ? -0.938  -16.726 -42.141 1.00 32.00  ? 180 HIS   D CD2  1 
ATOM   6809 C  CE1  . HIS   D 1 180 ? 1.133   -16.413 -41.442 1.00 32.47  ? 180 HIS   D CE1  1 
ATOM   6810 N  NE2  . HIS   D 1 180 ? 0.255   -16.101 -42.411 1.00 33.71  ? 180 HIS   D NE2  1 
ATOM   6811 N  N    . ILE   D 1 181 ? -3.350  -19.685 -43.158 1.00 36.38  ? 181 ILE   D N    1 
ATOM   6812 C  CA   . ILE   D 1 181 ? -3.484  -20.814 -44.121 1.00 38.35  ? 181 ILE   D CA   1 
ATOM   6813 C  C    . ILE   D 1 181 ? -2.289  -20.855 -45.088 1.00 39.45  ? 181 ILE   D C    1 
ATOM   6814 O  O    . ILE   D 1 181 ? -1.994  -21.986 -45.525 1.00 37.10  ? 181 ILE   D O    1 
ATOM   6815 C  CB   . ILE   D 1 181 ? -4.844  -20.754 -44.840 1.00 41.17  ? 181 ILE   D CB   1 
ATOM   6816 C  CG1  . ILE   D 1 181 ? -5.315  -22.155 -45.233 1.00 46.61  ? 181 ILE   D CG1  1 
ATOM   6817 C  CG2  . ILE   D 1 181 ? -4.812  -19.816 -46.027 1.00 40.25  ? 181 ILE   D CG2  1 
ATOM   6818 C  CD1  . ILE   D 1 181 ? -5.815  -22.972 -44.061 1.00 47.63  ? 181 ILE   D CD1  1 
ATOM   6819 N  N    . TRP   D 1 182 ? -1.613  -19.726 -45.394 1.00 40.21  ? 182 TRP   D N    1 
ATOM   6820 C  CA   . TRP   D 1 182 ? -0.376  -19.722 -46.234 1.00 43.07  ? 182 TRP   D CA   1 
ATOM   6821 C  C    . TRP   D 1 182 ? 0.587   -18.559 -45.938 1.00 45.06  ? 182 TRP   D C    1 
ATOM   6822 O  O    . TRP   D 1 182 ? 0.127   -17.482 -45.544 1.00 42.63  ? 182 TRP   D O    1 
ATOM   6823 C  CB   . TRP   D 1 182 ? -0.718  -19.777 -47.732 1.00 42.11  ? 182 TRP   D CB   1 
ATOM   6824 C  CG   . TRP   D 1 182 ? -1.490  -18.625 -48.301 1.00 39.44  ? 182 TRP   D CG   1 
ATOM   6825 C  CD1  . TRP   D 1 182 ? -2.832  -18.592 -48.545 1.00 40.62  ? 182 TRP   D CD1  1 
ATOM   6826 C  CD2  . TRP   D 1 182 ? -0.971  -17.377 -48.796 1.00 41.01  ? 182 TRP   D CD2  1 
ATOM   6827 N  NE1  . TRP   D 1 182 ? -3.189  -17.398 -49.111 1.00 40.60  ? 182 TRP   D NE1  1 
ATOM   6828 C  CE2  . TRP   D 1 182 ? -2.069  -16.630 -49.275 1.00 41.11  ? 182 TRP   D CE2  1 
ATOM   6829 C  CE3  . TRP   D 1 182 ? 0.303   -16.799 -48.849 1.00 43.30  ? 182 TRP   D CE3  1 
ATOM   6830 C  CZ2  . TRP   D 1 182 ? -1.925  -15.357 -49.822 1.00 42.22  ? 182 TRP   D CZ2  1 
ATOM   6831 C  CZ3  . TRP   D 1 182 ? 0.443   -15.532 -49.372 1.00 43.66  ? 182 TRP   D CZ3  1 
ATOM   6832 C  CH2  . TRP   D 1 182 ? -0.658  -14.824 -49.858 1.00 44.42  ? 182 TRP   D CH2  1 
ATOM   6833 N  N    . GLU   D 1 183 ? 1.866   -18.846 -46.136 1.00 56.54  ? 183 GLU   D N    1 
ATOM   6834 C  CA   . GLU   D 1 183 ? 3.004   -17.887 -46.100 1.00 64.28  ? 183 GLU   D CA   1 
ATOM   6835 C  C    . GLU   D 1 183 ? 3.342   -17.553 -47.557 1.00 67.13  ? 183 GLU   D C    1 
ATOM   6836 O  O    . GLU   D 1 183 ? 3.074   -18.378 -48.423 1.00 66.98  ? 183 GLU   D O    1 
ATOM   6837 C  CB   . GLU   D 1 183 ? 4.133   -18.429 -45.237 1.00 65.07  ? 183 GLU   D CB   1 
ATOM   6838 C  CG   . GLU   D 1 183 ? 3.762   -18.364 -43.782 1.00 67.47  ? 183 GLU   D CG   1 
ATOM   6839 C  CD   . GLU   D 1 183 ? 4.908   -18.097 -42.833 1.00 68.72  ? 183 GLU   D CD   1 
ATOM   6840 O  OE1  . GLU   D 1 183 ? 5.794   -18.965 -42.711 1.00 65.45  ? 183 GLU   D OE1  1 
ATOM   6841 O  OE2  . GLU   D 1 183 ? 4.895   -17.028 -42.223 1.00 67.90  ? 183 GLU   D OE2  1 
ATOM   6842 N  N    . SER   D 1 184 ? 4.069   -16.480 -47.811 1.00 80.09  ? 184 SER   D N    1 
ATOM   6843 C  CA   . SER   D 1 184 ? 4.114   -15.941 -49.200 1.00 89.54  ? 184 SER   D CA   1 
ATOM   6844 C  C    . SER   D 1 184 ? 4.548   -16.882 -50.334 1.00 97.77  ? 184 SER   D C    1 
ATOM   6845 O  O    . SER   D 1 184 ? 3.853   -16.806 -51.387 1.00 89.93  ? 184 SER   D O    1 
ATOM   6846 C  CB   . SER   D 1 184 ? 4.775   -14.584 -49.295 1.00 87.09  ? 184 SER   D CB   1 
ATOM   6847 O  OG   . SER   D 1 184 ? 3.818   -13.577 -49.620 1.00 83.59  ? 184 SER   D OG   1 
ATOM   6848 N  N    . SER   D 1 185 ? 5.587   -17.723 -50.203 1.00 98.86  ? 185 SER   D N    1 
ATOM   6849 C  CA   . SER   D 1 185 ? 5.934   -18.478 -51.443 1.00 92.34  ? 185 SER   D CA   1 
ATOM   6850 C  C    . SER   D 1 185 ? 5.904   -19.990 -51.259 1.00 84.22  ? 185 SER   D C    1 
ATOM   6851 O  O    . SER   D 1 185 ? 6.886   -20.550 -50.766 1.00 81.96  ? 185 SER   D O    1 
ATOM   6852 C  CB   . SER   D 1 185 ? 7.216   -17.995 -52.083 1.00 92.25  ? 185 SER   D CB   1 
ATOM   6853 O  OG   . SER   D 1 185 ? 8.347   -18.749 -51.661 1.00 90.29  ? 185 SER   D OG   1 
ATOM   6854 N  N    . ALA   D 1 186 ? 4.797   -20.605 -51.657 1.00 78.83  ? 186 ALA   D N    1 
ATOM   6855 C  CA   . ALA   D 1 186 ? 4.643   -22.071 -51.580 1.00 80.28  ? 186 ALA   D CA   1 
ATOM   6856 C  C    . ALA   D 1 186 ? 5.028   -22.606 -50.199 1.00 87.07  ? 186 ALA   D C    1 
ATOM   6857 O  O    . ALA   D 1 186 ? 5.936   -23.450 -50.134 1.00 90.92  ? 186 ALA   D O    1 
ATOM   6858 C  CB   . ALA   D 1 186 ? 5.339   -22.774 -52.704 1.00 79.39  ? 186 ALA   D CB   1 
ATOM   6859 N  N    . VAL   D 1 187 ? 4.465   -21.988 -49.153 1.00 84.60  ? 187 VAL   D N    1 
ATOM   6860 C  CA   . VAL   D 1 187 ? 4.507   -22.418 -47.725 1.00 71.71  ? 187 VAL   D CA   1 
ATOM   6861 C  C    . VAL   D 1 187 ? 3.058   -22.275 -47.253 1.00 64.20  ? 187 VAL   D C    1 
ATOM   6862 O  O    . VAL   D 1 187 ? 2.675   -21.205 -46.792 1.00 56.63  ? 187 VAL   D O    1 
ATOM   6863 C  CB   . VAL   D 1 187 ? 5.483   -21.644 -46.829 1.00 72.84  ? 187 VAL   D CB   1 
ATOM   6864 C  CG1  . VAL   D 1 187 ? 5.263   -22.038 -45.379 1.00 72.08  ? 187 VAL   D CG1  1 
ATOM   6865 C  CG2  . VAL   D 1 187 ? 6.917   -21.934 -47.213 1.00 71.94  ? 187 VAL   D CG2  1 
ATOM   6866 N  N    . VAL   D 1 188 ? 2.272   -23.299 -47.528 1.00 56.33  ? 188 VAL   D N    1 
ATOM   6867 C  CA   . VAL   D 1 188 ? 0.822   -23.298 -47.218 1.00 52.07  ? 188 VAL   D CA   1 
ATOM   6868 C  C    . VAL   D 1 188 ? 0.575   -24.309 -46.096 1.00 45.89  ? 188 VAL   D C    1 
ATOM   6869 O  O    . VAL   D 1 188 ? 1.326   -25.243 -45.957 1.00 42.15  ? 188 VAL   D O    1 
ATOM   6870 C  CB   . VAL   D 1 188 ? 0.052   -23.639 -48.509 1.00 51.76  ? 188 VAL   D CB   1 
ATOM   6871 C  CG1  . VAL   D 1 188 ? 0.527   -24.955 -49.080 1.00 50.98  ? 188 VAL   D CG1  1 
ATOM   6872 C  CG2  . VAL   D 1 188 ? -1.466  -23.600 -48.371 1.00 48.86  ? 188 VAL   D CG2  1 
ATOM   6873 N  N    . ALA   D 1 189 ? -0.467  -24.075 -45.327 1.00 41.71  ? 189 ALA   D N    1 
ATOM   6874 C  CA   . ALA   D 1 189 ? -0.864  -24.946 -44.200 1.00 43.10  ? 189 ALA   D CA   1 
ATOM   6875 C  C    . ALA   D 1 189 ? -1.477  -26.230 -44.758 1.00 41.02  ? 189 ALA   D C    1 
ATOM   6876 O  O    . ALA   D 1 189 ? -2.141  -26.179 -45.814 1.00 41.13  ? 189 ALA   D O    1 
ATOM   6877 C  CB   . ALA   D 1 189 ? -1.830  -24.230 -43.271 1.00 41.77  ? 189 ALA   D CB   1 
ATOM   6878 N  N    . SER   D 1 190 ? -1.264  -27.345 -44.068 1.00 37.05  ? 190 SER   D N    1 
ATOM   6879 C  CA   . SER   D 1 190 ? -2.149  -28.524 -44.185 1.00 37.01  ? 190 SER   D CA   1 
ATOM   6880 C  C    . SER   D 1 190 ? -3.202  -28.395 -43.074 1.00 33.69  ? 190 SER   D C    1 
ATOM   6881 O  O    . SER   D 1 190 ? -2.914  -27.719 -42.057 1.00 32.97  ? 190 SER   D O    1 
ATOM   6882 C  CB   . SER   D 1 190 ? -1.360  -29.812 -44.157 1.00 36.41  ? 190 SER   D CB   1 
ATOM   6883 O  OG   . SER   D 1 190 ? -0.994  -30.154 -42.832 1.00 42.90  ? 190 SER   D OG   1 
ATOM   6884 N  N    . PHE   D 1 191 ? -4.404  -28.923 -43.295 1.00 31.55  ? 191 PHE   D N    1 
ATOM   6885 C  CA   . PHE   D 1 191 ? -5.498  -28.900 -42.294 1.00 32.28  ? 191 PHE   D CA   1 
ATOM   6886 C  C    . PHE   D 1 191 ? -6.389  -30.139 -42.442 1.00 31.79  ? 191 PHE   D C    1 
ATOM   6887 O  O    . PHE   D 1 191 ? -6.353  -30.860 -43.466 1.00 28.52  ? 191 PHE   D O    1 
ATOM   6888 C  CB   . PHE   D 1 191 ? -6.289  -27.583 -42.340 1.00 32.38  ? 191 PHE   D CB   1 
ATOM   6889 C  CG   . PHE   D 1 191 ? -7.063  -27.301 -43.609 1.00 32.46  ? 191 PHE   D CG   1 
ATOM   6890 C  CD1  . PHE   D 1 191 ? -8.367  -27.750 -43.768 1.00 31.70  ? 191 PHE   D CD1  1 
ATOM   6891 C  CD2  . PHE   D 1 191 ? -6.500  -26.557 -44.637 1.00 31.87  ? 191 PHE   D CD2  1 
ATOM   6892 C  CE1  . PHE   D 1 191 ? -9.082  -27.469 -44.926 1.00 30.68  ? 191 PHE   D CE1  1 
ATOM   6893 C  CE2  . PHE   D 1 191 ? -7.217  -26.284 -45.797 1.00 30.78  ? 191 PHE   D CE2  1 
ATOM   6894 C  CZ   . PHE   D 1 191 ? -8.505  -26.743 -45.938 1.00 29.21  ? 191 PHE   D CZ   1 
ATOM   6895 N  N    . GLU   D 1 192 ? -7.161  -30.367 -41.384 1.00 29.09  ? 192 GLU   D N    1 
ATOM   6896 C  CA   . GLU   D 1 192 ? -8.093  -31.494 -41.211 1.00 28.16  ? 192 GLU   D CA   1 
ATOM   6897 C  C    . GLU   D 1 192 ? -9.290  -30.962 -40.425 1.00 26.85  ? 192 GLU   D C    1 
ATOM   6898 O  O    . GLU   D 1 192 ? -9.095  -30.210 -39.450 1.00 27.06  ? 192 GLU   D O    1 
ATOM   6899 C  CB   . GLU   D 1 192 ? -7.347  -32.621 -40.503 1.00 32.32  ? 192 GLU   D CB   1 
ATOM   6900 C  CG   . GLU   D 1 192 ? -8.221  -33.751 -40.010 1.00 34.94  ? 192 GLU   D CG   1 
ATOM   6901 C  CD   . GLU   D 1 192 ? -7.406  -34.826 -39.313 1.00 39.16  ? 192 GLU   D CD   1 
ATOM   6902 O  OE1  . GLU   D 1 192 ? -6.624  -34.450 -38.419 1.00 39.79  ? 192 GLU   D OE1  1 
ATOM   6903 O  OE2  . GLU   D 1 192 ? -7.533  -36.027 -39.682 1.00 41.53  ? 192 GLU   D OE2  1 
ATOM   6904 N  N    . ALA   D 1 193 ? -10.494 -31.300 -40.852 1.00 23.98  ? 193 ALA   D N    1 
ATOM   6905 C  CA   . ALA   D 1 193 ? -11.732 -30.996 -40.128 1.00 23.41  ? 193 ALA   D CA   1 
ATOM   6906 C  C    . ALA   D 1 193 ? -12.523 -32.292 -40.026 1.00 25.36  ? 193 ALA   D C    1 
ATOM   6907 O  O    . ALA   D 1 193 ? -12.374 -33.154 -40.908 1.00 25.43  ? 193 ALA   D O    1 
ATOM   6908 C  CB   . ALA   D 1 193 ? -12.495 -29.911 -40.843 1.00 24.91  ? 193 ALA   D CB   1 
ATOM   6909 N  N    . THR   D 1 194 ? -13.288 -32.427 -38.951 1.00 25.43  ? 194 THR   D N    1 
ATOM   6910 C  CA   . THR   D 1 194 ? -14.174 -33.569 -38.689 1.00 25.98  ? 194 THR   D CA   1 
ATOM   6911 C  C    . THR   D 1 194 ? -15.424 -32.973 -38.060 1.00 25.02  ? 194 THR   D C    1 
ATOM   6912 O  O    . THR   D 1 194 ? -15.273 -32.123 -37.167 1.00 23.94  ? 194 THR   D O    1 
ATOM   6913 C  CB   . THR   D 1 194 ? -13.480 -34.622 -37.807 1.00 29.10  ? 194 THR   D CB   1 
ATOM   6914 O  OG1  . THR   D 1 194 ? -12.191 -34.954 -38.333 1.00 30.96  ? 194 THR   D OG1  1 
ATOM   6915 C  CG2  . THR   D 1 194 ? -14.265 -35.907 -37.702 1.00 30.42  ? 194 THR   D CG2  1 
ATOM   6916 N  N    . PHE   D 1 195 ? -16.611 -33.372 -38.520 1.00 24.37  ? 195 PHE   D N    1 
ATOM   6917 C  CA   . PHE   D 1 195 ? -17.863 -33.124 -37.769 1.00 23.32  ? 195 PHE   D CA   1 
ATOM   6918 C  C    . PHE   D 1 195 ? -18.783 -34.335 -37.917 1.00 24.17  ? 195 PHE   D C    1 
ATOM   6919 O  O    . PHE   D 1 195 ? -18.648 -35.107 -38.889 1.00 26.46  ? 195 PHE   D O    1 
ATOM   6920 C  CB   . PHE   D 1 195 ? -18.503 -31.797 -38.195 1.00 23.39  ? 195 PHE   D CB   1 
ATOM   6921 C  CG   . PHE   D 1 195 ? -18.885 -31.690 -39.651 1.00 21.91  ? 195 PHE   D CG   1 
ATOM   6922 C  CD1  . PHE   D 1 195 ? -17.948 -31.333 -40.610 1.00 22.14  ? 195 PHE   D CD1  1 
ATOM   6923 C  CD2  . PHE   D 1 195 ? -20.189 -31.920 -40.053 1.00 21.54  ? 195 PHE   D CD2  1 
ATOM   6924 C  CE1  . PHE   D 1 195 ? -18.309 -31.210 -41.940 1.00 21.35  ? 195 PHE   D CE1  1 
ATOM   6925 C  CE2  . PHE   D 1 195 ? -20.549 -31.790 -41.387 1.00 20.50  ? 195 PHE   D CE2  1 
ATOM   6926 C  CZ   . PHE   D 1 195 ? -19.603 -31.452 -42.325 1.00 20.40  ? 195 PHE   D CZ   1 
ATOM   6927 N  N    . THR   D 1 196 ? -19.666 -34.493 -36.935 1.00 22.41  ? 196 THR   D N    1 
ATOM   6928 C  CA   . THR   D 1 196 ? -20.787 -35.451 -36.932 1.00 22.59  ? 196 THR   D CA   1 
ATOM   6929 C  C    . THR   D 1 196 ? -22.079 -34.646 -37.007 1.00 22.96  ? 196 THR   D C    1 
ATOM   6930 O  O    . THR   D 1 196 ? -22.187 -33.583 -36.328 1.00 22.66  ? 196 THR   D O    1 
ATOM   6931 C  CB   . THR   D 1 196 ? -20.757 -36.375 -35.710 1.00 20.87  ? 196 THR   D CB   1 
ATOM   6932 O  OG1  . THR   D 1 196 ? -20.750 -35.544 -34.552 1.00 23.30  ? 196 THR   D OG1  1 
ATOM   6933 C  CG2  . THR   D 1 196 ? -19.560 -37.289 -35.695 1.00 20.77  ? 196 THR   D CG2  1 
ATOM   6934 N  N    . PHE   D 1 197 ? -23.028 -35.158 -37.779 1.00 24.98  ? 197 PHE   D N    1 
ATOM   6935 C  CA   . PHE   D 1 197 ? -24.269 -34.446 -38.169 1.00 26.42  ? 197 PHE   D CA   1 
ATOM   6936 C  C    . PHE   D 1 197 ? -25.428 -35.451 -38.218 1.00 29.56  ? 197 PHE   D C    1 
ATOM   6937 O  O    . PHE   D 1 197 ? -25.200 -36.652 -38.436 1.00 27.81  ? 197 PHE   D O    1 
ATOM   6938 C  CB   . PHE   D 1 197 ? -24.030 -33.734 -39.499 1.00 24.98  ? 197 PHE   D CB   1 
ATOM   6939 C  CG   . PHE   D 1 197 ? -23.782 -34.685 -40.636 1.00 25.27  ? 197 PHE   D CG   1 
ATOM   6940 C  CD1  . PHE   D 1 197 ? -24.846 -35.226 -41.345 1.00 25.19  ? 197 PHE   D CD1  1 
ATOM   6941 C  CD2  . PHE   D 1 197 ? -22.491 -35.094 -40.950 1.00 26.57  ? 197 PHE   D CD2  1 
ATOM   6942 C  CE1  . PHE   D 1 197 ? -24.621 -36.136 -42.366 1.00 24.77  ? 197 PHE   D CE1  1 
ATOM   6943 C  CE2  . PHE   D 1 197 ? -22.267 -36.011 -41.968 1.00 26.49  ? 197 PHE   D CE2  1 
ATOM   6944 C  CZ   . PHE   D 1 197 ? -23.336 -36.533 -42.670 1.00 25.46  ? 197 PHE   D CZ   1 
ATOM   6945 N  N    . LEU   D 1 198 ? -26.634 -34.942 -37.975 1.00 31.56  ? 198 LEU   D N    1 
ATOM   6946 C  CA   . LEU   D 1 198 ? -27.928 -35.636 -38.119 1.00 31.70  ? 198 LEU   D CA   1 
ATOM   6947 C  C    . LEU   D 1 198 ? -28.816 -34.767 -39.018 1.00 31.52  ? 198 LEU   D C    1 
ATOM   6948 O  O    . LEU   D 1 198 ? -29.368 -33.784 -38.503 1.00 32.16  ? 198 LEU   D O    1 
ATOM   6949 C  CB   . LEU   D 1 198 ? -28.511 -35.802 -36.712 1.00 34.26  ? 198 LEU   D CB   1 
ATOM   6950 C  CG   . LEU   D 1 198 ? -29.701 -36.749 -36.567 1.00 32.78  ? 198 LEU   D CG   1 
ATOM   6951 C  CD1  . LEU   D 1 198 ? -29.811 -37.255 -35.141 1.00 33.78  ? 198 LEU   D CD1  1 
ATOM   6952 C  CD2  . LEU   D 1 198 ? -30.993 -36.068 -36.971 1.00 34.73  ? 198 LEU   D CD2  1 
ATOM   6953 N  N    . ILE   D 1 199 ? -28.881 -35.078 -40.320 1.00 32.06  ? 199 ILE   D N    1 
ATOM   6954 C  CA   . ILE   D 1 199 ? -29.890 -34.519 -41.269 1.00 31.16  ? 199 ILE   D CA   1 
ATOM   6955 C  C    . ILE   D 1 199 ? -31.123 -35.424 -41.239 1.00 32.53  ? 199 ILE   D C    1 
ATOM   6956 O  O    . ILE   D 1 199 ? -30.970 -36.608 -41.549 1.00 33.74  ? 199 ILE   D O    1 
ATOM   6957 C  CB   . ILE   D 1 199 ? -29.334 -34.386 -42.701 1.00 31.73  ? 199 ILE   D CB   1 
ATOM   6958 C  CG1  . ILE   D 1 199 ? -28.076 -33.516 -42.772 1.00 30.71  ? 199 ILE   D CG1  1 
ATOM   6959 C  CG2  . ILE   D 1 199 ? -30.423 -33.858 -43.636 1.00 32.70  ? 199 ILE   D CG2  1 
ATOM   6960 C  CD1  . ILE   D 1 199 ? -27.353 -33.582 -44.111 1.00 30.83  ? 199 ILE   D CD1  1 
ATOM   6961 N  N    . LYS   D 1 200 ? -32.289 -34.850 -40.933 1.00 37.20  ? 200 LYS   D N    1 
ATOM   6962 C  CA   . LYS   D 1 200 ? -33.595 -35.518 -40.648 1.00 40.51  ? 200 LYS   D CA   1 
ATOM   6963 C  C    . LYS   D 1 200 ? -34.694 -34.763 -41.410 1.00 42.34  ? 200 LYS   D C    1 
ATOM   6964 O  O    . LYS   D 1 200 ? -34.541 -33.553 -41.593 1.00 44.94  ? 200 LYS   D O    1 
ATOM   6965 C  CB   . LYS   D 1 200 ? -33.862 -35.462 -39.139 1.00 44.21  ? 200 LYS   D CB   1 
ATOM   6966 C  CG   . LYS   D 1 200 ? -35.197 -36.003 -38.647 1.00 45.97  ? 200 LYS   D CG   1 
ATOM   6967 C  CD   . LYS   D 1 200 ? -35.163 -37.483 -38.341 1.00 51.28  ? 200 LYS   D CD   1 
ATOM   6968 C  CE   . LYS   D 1 200 ? -36.285 -37.930 -37.427 1.00 54.43  ? 200 LYS   D CE   1 
ATOM   6969 N  NZ   . LYS   D 1 200 ? -36.150 -37.351 -36.069 1.00 57.35  ? 200 LYS   D NZ   1 
ATOM   6970 N  N    . SER   D 1 201 ? -35.776 -35.425 -41.811 1.00 45.19  ? 201 SER   D N    1 
ATOM   6971 C  CA   . SER   D 1 201 ? -36.880 -34.796 -42.584 1.00 48.63  ? 201 SER   D CA   1 
ATOM   6972 C  C    . SER   D 1 201 ? -38.151 -35.622 -42.477 1.00 49.36  ? 201 SER   D C    1 
ATOM   6973 O  O    . SER   D 1 201 ? -38.070 -36.842 -42.498 1.00 47.46  ? 201 SER   D O    1 
ATOM   6974 C  CB   . SER   D 1 201 ? -36.484 -34.644 -44.022 1.00 50.95  ? 201 SER   D CB   1 
ATOM   6975 O  OG   . SER   D 1 201 ? -37.469 -33.919 -44.727 1.00 51.81  ? 201 SER   D OG   1 
ATOM   6976 N  N    . PRO   D 1 202 ? -39.345 -34.997 -42.363 1.00 56.21  ? 202 PRO   D N    1 
ATOM   6977 C  CA   . PRO   D 1 202 ? -40.608 -35.701 -42.617 1.00 58.30  ? 202 PRO   D CA   1 
ATOM   6978 C  C    . PRO   D 1 202 ? -40.902 -35.909 -44.117 1.00 61.18  ? 202 PRO   D C    1 
ATOM   6979 O  O    . PRO   D 1 202 ? -41.687 -36.762 -44.415 1.00 63.59  ? 202 PRO   D O    1 
ATOM   6980 C  CB   . PRO   D 1 202 ? -41.661 -34.801 -41.956 1.00 55.58  ? 202 PRO   D CB   1 
ATOM   6981 C  CG   . PRO   D 1 202 ? -41.052 -33.404 -42.005 1.00 55.51  ? 202 PRO   D CG   1 
ATOM   6982 C  CD   . PRO   D 1 202 ? -39.548 -33.596 -41.954 1.00 56.74  ? 202 PRO   D CD   1 
ATOM   6983 N  N    . ASP   D 1 203 ? -40.265 -35.141 -45.014 1.00 71.79  ? 203 ASP   D N    1 
ATOM   6984 C  CA   . ASP   D 1 203 ? -40.333 -35.305 -46.497 1.00 72.38  ? 203 ASP   D CA   1 
ATOM   6985 C  C    . ASP   D 1 203 ? -39.633 -36.606 -46.916 1.00 75.46  ? 203 ASP   D C    1 
ATOM   6986 O  O    . ASP   D 1 203 ? -39.136 -37.329 -46.034 1.00 73.43  ? 203 ASP   D O    1 
ATOM   6987 C  CB   . ASP   D 1 203 ? -39.648 -34.148 -47.237 1.00 73.39  ? 203 ASP   D CB   1 
ATOM   6988 C  CG   . ASP   D 1 203 ? -40.377 -32.817 -47.188 1.00 80.97  ? 203 ASP   D CG   1 
ATOM   6989 O  OD1  . ASP   D 1 203 ? -41.592 -32.823 -46.862 1.00 76.25  ? 203 ASP   D OD1  1 
ATOM   6990 O  OD2  . ASP   D 1 203 ? -39.720 -31.777 -47.482 1.00 76.57  ? 203 ASP   D OD2  1 
ATOM   6991 N  N    . SER   D 1 204 ? -39.622 -36.893 -48.222 1.00 72.04  ? 204 SER   D N    1 
ATOM   6992 C  CA   . SER   D 1 204 ? -38.688 -37.835 -48.896 1.00 68.62  ? 204 SER   D CA   1 
ATOM   6993 C  C    . SER   D 1 204 ? -37.786 -37.056 -49.870 1.00 67.27  ? 204 SER   D C    1 
ATOM   6994 O  O    . SER   D 1 204 ? -36.833 -37.663 -50.403 1.00 56.92  ? 204 SER   D O    1 
ATOM   6995 C  CB   . SER   D 1 204 ? -39.435 -38.961 -49.579 1.00 67.68  ? 204 SER   D CB   1 
ATOM   6996 O  OG   . SER   D 1 204 ? -40.449 -38.456 -50.433 1.00 63.94  ? 204 SER   D OG   1 
ATOM   6997 N  N    . HIS   D 1 205 ? -38.091 -35.771 -50.110 1.00 69.51  ? 205 HIS   D N    1 
ATOM   6998 C  CA   . HIS   D 1 205 ? -37.163 -34.744 -50.665 1.00 72.94  ? 205 HIS   D CA   1 
ATOM   6999 C  C    . HIS   D 1 205 ? -36.708 -33.832 -49.518 1.00 62.18  ? 205 HIS   D C    1 
ATOM   7000 O  O    . HIS   D 1 205 ? -37.372 -32.841 -49.220 1.00 65.05  ? 205 HIS   D O    1 
ATOM   7001 C  CB   . HIS   D 1 205 ? -37.833 -33.956 -51.818 1.00 83.71  ? 205 HIS   D CB   1 
ATOM   7002 C  CG   . HIS   D 1 205 ? -37.620 -34.489 -53.209 1.00 90.07  ? 205 HIS   D CG   1 
ATOM   7003 N  ND1  . HIS   D 1 205 ? -38.654 -35.024 -53.970 1.00 90.99  ? 205 HIS   D ND1  1 
ATOM   7004 C  CD2  . HIS   D 1 205 ? -36.527 -34.516 -54.009 1.00 89.65  ? 205 HIS   D CD2  1 
ATOM   7005 C  CE1  . HIS   D 1 205 ? -38.197 -35.387 -55.154 1.00 89.08  ? 205 HIS   D CE1  1 
ATOM   7006 N  NE2  . HIS   D 1 205 ? -36.896 -35.083 -55.205 1.00 90.26  ? 205 HIS   D NE2  1 
ATOM   7007 N  N    . PRO   D 1 206 ? -35.629 -34.172 -48.770 1.00 49.77  ? 206 PRO   D N    1 
ATOM   7008 C  CA   . PRO   D 1 206 ? -34.983 -33.216 -47.866 1.00 44.40  ? 206 PRO   D CA   1 
ATOM   7009 C  C    . PRO   D 1 206 ? -34.090 -32.191 -48.589 1.00 37.69  ? 206 PRO   D C    1 
ATOM   7010 O  O    . PRO   D 1 206 ? -33.538 -32.488 -49.654 1.00 36.46  ? 206 PRO   D O    1 
ATOM   7011 C  CB   . PRO   D 1 206 ? -34.124 -34.114 -46.959 1.00 45.50  ? 206 PRO   D CB   1 
ATOM   7012 C  CG   . PRO   D 1 206 ? -33.769 -35.281 -47.849 1.00 45.53  ? 206 PRO   D CG   1 
ATOM   7013 C  CD   . PRO   D 1 206 ? -35.015 -35.509 -48.684 1.00 47.00  ? 206 PRO   D CD   1 
ATOM   7014 N  N    . ALA   D 1 207 ? -33.937 -31.012 -47.984 1.00 31.79  ? 207 ALA   D N    1 
ATOM   7015 C  CA   . ALA   D 1 207 ? -33.111 -29.902 -48.523 1.00 29.24  ? 207 ALA   D CA   1 
ATOM   7016 C  C    . ALA   D 1 207 ? -32.658 -28.993 -47.378 1.00 24.14  ? 207 ALA   D C    1 
ATOM   7017 O  O    . ALA   D 1 207 ? -33.333 -28.893 -46.354 1.00 21.52  ? 207 ALA   D O    1 
ATOM   7018 C  CB   . ALA   D 1 207 ? -33.885 -29.137 -49.582 1.00 26.15  ? 207 ALA   D CB   1 
ATOM   7019 N  N    . ASP   D 1 208 ? -31.525 -28.323 -47.563 1.00 21.54  ? 208 ASP   D N    1 
ATOM   7020 C  CA   . ASP   D 1 208 ? -30.801 -28.238 -48.825 1.00 23.53  ? 208 ASP   D CA   1 
ATOM   7021 C  C    . ASP   D 1 208 ? -29.360 -28.731 -48.697 1.00 24.97  ? 208 ASP   D C    1 
ATOM   7022 O  O    . ASP   D 1 208 ? -28.759 -29.022 -49.745 1.00 27.75  ? 208 ASP   D O    1 
ATOM   7023 C  CB   . ASP   D 1 208 ? -30.746 -26.795 -49.335 1.00 24.22  ? 208 ASP   D CB   1 
ATOM   7024 C  CG   . ASP   D 1 208 ? -31.839 -26.465 -50.322 1.00 23.10  ? 208 ASP   D CG   1 
ATOM   7025 O  OD1  . ASP   D 1 208 ? -31.600 -26.699 -51.526 1.00 24.71  ? 208 ASP   D OD1  1 
ATOM   7026 O  OD2  . ASP   D 1 208 ? -32.929 -26.036 -49.867 1.00 22.32  ? 208 ASP   D OD2  1 
ATOM   7027 N  N    . GLY   D 1 209 ? -28.780 -28.749 -47.494 1.00 28.18  ? 209 GLY   D N    1 
ATOM   7028 C  CA   . GLY   D 1 209 ? -27.393 -29.230 -47.305 1.00 27.30  ? 209 GLY   D CA   1 
ATOM   7029 C  C    . GLY   D 1 209 ? -26.696 -28.627 -46.099 1.00 25.88  ? 209 GLY   D C    1 
ATOM   7030 O  O    . GLY   D 1 209 ? -27.296 -27.799 -45.418 1.00 25.82  ? 209 GLY   D O    1 
ATOM   7031 N  N    . ILE   D 1 210 ? -25.481 -29.115 -45.846 1.00 25.84  ? 210 ILE   D N    1 
ATOM   7032 C  CA   . ILE   D 1 210 ? -24.509 -28.656 -44.820 1.00 22.85  ? 210 ILE   D CA   1 
ATOM   7033 C  C    . ILE   D 1 210 ? -23.190 -28.489 -45.571 1.00 22.87  ? 210 ILE   D C    1 
ATOM   7034 O  O    . ILE   D 1 210 ? -22.974 -29.200 -46.542 1.00 23.65  ? 210 ILE   D O    1 
ATOM   7035 C  CB   . ILE   D 1 210 ? -24.402 -29.672 -43.662 1.00 23.16  ? 210 ILE   D CB   1 
ATOM   7036 C  CG1  . ILE   D 1 210 ? -25.697 -29.740 -42.860 1.00 23.13  ? 210 ILE   D CG1  1 
ATOM   7037 C  CG2  . ILE   D 1 210 ? -23.212 -29.362 -42.757 1.00 24.02  ? 210 ILE   D CG2  1 
ATOM   7038 C  CD1  . ILE   D 1 210 ? -25.754 -30.898 -41.894 1.00 24.37  ? 210 ILE   D CD1  1 
ATOM   7039 N  N    . ALA   D 1 211 ? -22.351 -27.559 -45.161 1.00 23.12  ? 211 ALA   D N    1 
ATOM   7040 C  CA   . ALA   D 1 211 ? -21.032 -27.342 -45.778 1.00 23.04  ? 211 ALA   D CA   1 
ATOM   7041 C  C    . ALA   D 1 211 ? -20.033 -26.966 -44.691 1.00 22.41  ? 211 ALA   D C    1 
ATOM   7042 O  O    . ALA   D 1 211 ? -20.426 -26.256 -43.760 1.00 22.65  ? 211 ALA   D O    1 
ATOM   7043 C  CB   . ALA   D 1 211 ? -21.135 -26.284 -46.831 1.00 23.65  ? 211 ALA   D CB   1 
ATOM   7044 N  N    . PHE   D 1 212 ? -18.832 -27.518 -44.787 1.00 22.65  ? 212 PHE   D N    1 
ATOM   7045 C  CA   . PHE   D 1 212 ? -17.601 -26.980 -44.170 1.00 23.79  ? 212 PHE   D CA   1 
ATOM   7046 C  C    . PHE   D 1 212 ? -16.997 -25.932 -45.106 1.00 22.95  ? 212 PHE   D C    1 
ATOM   7047 O  O    . PHE   D 1 212 ? -16.705 -26.276 -46.256 1.00 21.42  ? 212 PHE   D O    1 
ATOM   7048 C  CB   . PHE   D 1 212 ? -16.576 -28.086 -43.932 1.00 23.61  ? 212 PHE   D CB   1 
ATOM   7049 C  CG   . PHE   D 1 212 ? -15.274 -27.560 -43.394 1.00 24.96  ? 212 PHE   D CG   1 
ATOM   7050 C  CD1  . PHE   D 1 212 ? -15.129 -27.279 -42.044 1.00 25.47  ? 212 PHE   D CD1  1 
ATOM   7051 C  CD2  . PHE   D 1 212 ? -14.218 -27.291 -44.248 1.00 25.04  ? 212 PHE   D CD2  1 
ATOM   7052 C  CE1  . PHE   D 1 212 ? -13.930 -26.782 -41.550 1.00 25.28  ? 212 PHE   D CE1  1 
ATOM   7053 C  CE2  . PHE   D 1 212 ? -13.025 -26.791 -43.757 1.00 26.15  ? 212 PHE   D CE2  1 
ATOM   7054 C  CZ   . PHE   D 1 212 ? -12.881 -26.541 -42.406 1.00 26.00  ? 212 PHE   D CZ   1 
ATOM   7055 N  N    . PHE   D 1 213 ? -16.764 -24.710 -44.625 1.00 22.57  ? 213 PHE   D N    1 
ATOM   7056 C  CA   . PHE   D 1 213 ? -16.255 -23.611 -45.489 1.00 23.71  ? 213 PHE   D CA   1 
ATOM   7057 C  C    . PHE   D 1 213 ? -15.079 -22.896 -44.818 1.00 24.72  ? 213 PHE   D C    1 
ATOM   7058 O  O    . PHE   D 1 213 ? -14.966 -22.910 -43.578 1.00 23.11  ? 213 PHE   D O    1 
ATOM   7059 C  CB   . PHE   D 1 213 ? -17.390 -22.671 -45.903 1.00 22.35  ? 213 PHE   D CB   1 
ATOM   7060 C  CG   . PHE   D 1 213 ? -17.926 -21.757 -44.831 1.00 22.33  ? 213 PHE   D CG   1 
ATOM   7061 C  CD1  . PHE   D 1 213 ? -18.933 -22.178 -43.983 1.00 20.10  ? 213 PHE   D CD1  1 
ATOM   7062 C  CD2  . PHE   D 1 213 ? -17.445 -20.456 -44.702 1.00 22.61  ? 213 PHE   D CD2  1 
ATOM   7063 C  CE1  . PHE   D 1 213 ? -19.425 -21.327 -43.009 1.00 20.72  ? 213 PHE   D CE1  1 
ATOM   7064 C  CE2  . PHE   D 1 213 ? -17.933 -19.610 -43.721 1.00 20.90  ? 213 PHE   D CE2  1 
ATOM   7065 C  CZ   . PHE   D 1 213 ? -18.931 -20.047 -42.882 1.00 20.98  ? 213 PHE   D CZ   1 
ATOM   7066 N  N    . ILE   D 1 214 ? -14.209 -22.349 -45.665 1.00 26.10  ? 214 ILE   D N    1 
ATOM   7067 C  CA   . ILE   D 1 214 ? -13.092 -21.424 -45.326 1.00 27.34  ? 214 ILE   D CA   1 
ATOM   7068 C  C    . ILE   D 1 214 ? -13.380 -20.103 -46.026 1.00 27.94  ? 214 ILE   D C    1 
ATOM   7069 O  O    . ILE   D 1 214 ? -13.693 -20.151 -47.220 1.00 29.10  ? 214 ILE   D O    1 
ATOM   7070 C  CB   . ILE   D 1 214 ? -11.755 -22.025 -45.771 1.00 27.17  ? 214 ILE   D CB   1 
ATOM   7071 C  CG1  . ILE   D 1 214 ? -11.666 -23.491 -45.355 1.00 28.03  ? 214 ILE   D CG1  1 
ATOM   7072 C  CG2  . ILE   D 1 214 ? -10.584 -21.212 -45.247 1.00 28.06  ? 214 ILE   D CG2  1 
ATOM   7073 C  CD1  . ILE   D 1 214 ? -10.467 -24.200 -45.907 1.00 29.04  ? 214 ILE   D CD1  1 
ATOM   7074 N  N    . SER   D 1 215 ? -13.342 -18.981 -45.306 1.00 28.47  ? 215 SER   D N    1 
ATOM   7075 C  CA   . SER   D 1 215 ? -13.711 -17.642 -45.843 1.00 29.88  ? 215 SER   D CA   1 
ATOM   7076 C  C    . SER   D 1 215 ? -12.742 -16.570 -45.350 1.00 30.94  ? 215 SER   D C    1 
ATOM   7077 O  O    . SER   D 1 215 ? -12.014 -16.815 -44.370 1.00 32.12  ? 215 SER   D O    1 
ATOM   7078 C  CB   . SER   D 1 215 ? -15.139 -17.278 -45.497 1.00 31.07  ? 215 SER   D CB   1 
ATOM   7079 O  OG   . SER   D 1 215 ? -15.295 -17.007 -44.103 1.00 28.74  ? 215 SER   D OG   1 
ATOM   7080 N  N    . ASN   D 1 216 ? -12.753 -15.417 -46.013 1.00 30.85  ? 216 ASN   D N    1 
ATOM   7081 C  CA   . ASN   D 1 216 ? -12.172 -14.153 -45.494 1.00 32.38  ? 216 ASN   D CA   1 
ATOM   7082 C  C    . ASN   D 1 216 ? -12.725 -13.937 -44.073 1.00 31.72  ? 216 ASN   D C    1 
ATOM   7083 O  O    . ASN   D 1 216 ? -13.902 -14.240 -43.862 1.00 31.49  ? 216 ASN   D O    1 
ATOM   7084 C  CB   . ASN   D 1 216 ? -12.475 -12.998 -46.453 1.00 34.90  ? 216 ASN   D CB   1 
ATOM   7085 C  CG   . ASN   D 1 216 ? -13.934 -12.983 -46.872 1.00 40.24  ? 216 ASN   D CG   1 
ATOM   7086 O  OD1  . ASN   D 1 216 ? -14.359 -13.833 -47.655 1.00 45.74  ? 216 ASN   D OD1  1 
ATOM   7087 N  ND2  . ASN   D 1 216 ? -14.720 -12.059 -46.338 1.00 41.14  ? 216 ASN   D ND2  1 
ATOM   7088 N  N    . ILE   D 1 217 ? -11.918 -13.393 -43.154 1.00 31.06  ? 217 ILE   D N    1 
ATOM   7089 C  CA   . ILE   D 1 217 ? -12.205 -13.246 -41.688 1.00 31.55  ? 217 ILE   D CA   1 
ATOM   7090 C  C    . ILE   D 1 217 ? -13.569 -12.581 -41.454 1.00 32.43  ? 217 ILE   D C    1 
ATOM   7091 O  O    . ILE   D 1 217 ? -14.236 -12.932 -40.466 1.00 28.98  ? 217 ILE   D O    1 
ATOM   7092 C  CB   . ILE   D 1 217 ? -11.068 -12.461 -40.985 1.00 33.25  ? 217 ILE   D CB   1 
ATOM   7093 C  CG1  . ILE   D 1 217 ? -10.924 -11.037 -41.544 1.00 37.90  ? 217 ILE   D CG1  1 
ATOM   7094 C  CG2  . ILE   D 1 217 ? -9.748  -13.218 -41.054 1.00 30.74  ? 217 ILE   D CG2  1 
ATOM   7095 C  CD1  . ILE   D 1 217 ? -9.970  -10.126 -40.776 1.00 39.72  ? 217 ILE   D CD1  1 
ATOM   7096 N  N    . ASP   D 1 218 ? -13.950 -11.629 -42.314 1.00 38.50  ? 218 ASP   D N    1 
ATOM   7097 C  CA   . ASP   D 1 218 ? -15.106 -10.701 -42.138 1.00 41.20  ? 218 ASP   D CA   1 
ATOM   7098 C  C    . ASP   D 1 218 ? -16.381 -11.272 -42.795 1.00 40.57  ? 218 ASP   D C    1 
ATOM   7099 O  O    . ASP   D 1 218 ? -17.452 -10.638 -42.634 1.00 40.34  ? 218 ASP   D O    1 
ATOM   7100 C  CB   . ASP   D 1 218 ? -14.767 -9.307  -42.692 1.00 47.53  ? 218 ASP   D CB   1 
ATOM   7101 C  CG   . ASP   D 1 218 ? -14.117 -9.305  -44.079 1.00 54.58  ? 218 ASP   D CG   1 
ATOM   7102 O  OD1  . ASP   D 1 218 ? -14.860 -9.364  -45.084 1.00 64.11  ? 218 ASP   D OD1  1 
ATOM   7103 O  OD2  . ASP   D 1 218 ? -12.863 -9.251  -44.151 1.00 66.71  ? 218 ASP   D OD2  1 
ATOM   7104 N  N    . SER   D 1 219 ? -16.293 -12.434 -43.458 1.00 37.89  ? 219 SER   D N    1 
ATOM   7105 C  CA   . SER   D 1 219 ? -17.388 -13.098 -44.223 1.00 35.04  ? 219 SER   D CA   1 
ATOM   7106 C  C    . SER   D 1 219 ? -18.682 -13.139 -43.414 1.00 31.67  ? 219 SER   D C    1 
ATOM   7107 O  O    . SER   D 1 219 ? -18.623 -13.428 -42.208 1.00 33.52  ? 219 SER   D O    1 
ATOM   7108 C  CB   . SER   D 1 219 ? -17.011 -14.496 -44.638 1.00 36.41  ? 219 SER   D CB   1 
ATOM   7109 O  OG   . SER   D 1 219 ? -18.174 -15.262 -44.924 1.00 38.25  ? 219 SER   D OG   1 
ATOM   7110 N  N    . SER   D 1 220 ? -19.811 -12.918 -44.086 1.00 29.30  ? 220 SER   D N    1 
ATOM   7111 C  CA   . SER   D 1 220 ? -21.180 -13.021 -43.520 1.00 28.08  ? 220 SER   D CA   1 
ATOM   7112 C  C    . SER   D 1 220 ? -22.104 -13.679 -44.553 1.00 25.64  ? 220 SER   D C    1 
ATOM   7113 O  O    . SER   D 1 220 ? -21.663 -13.879 -45.695 1.00 22.94  ? 220 SER   D O    1 
ATOM   7114 C  CB   . SER   D 1 220 ? -21.694 -11.680 -43.081 1.00 28.83  ? 220 SER   D CB   1 
ATOM   7115 O  OG   . SER   D 1 220 ? -21.627 -10.767 -44.156 1.00 31.57  ? 220 SER   D OG   1 
ATOM   7116 N  N    . ILE   D 1 221 ? -23.310 -14.054 -44.122 1.00 25.36  ? 221 ILE   D N    1 
ATOM   7117 C  CA   . ILE   D 1 221 ? -24.324 -14.759 -44.956 1.00 27.97  ? 221 ILE   D CA   1 
ATOM   7118 C  C    . ILE   D 1 221 ? -24.667 -13.817 -46.100 1.00 28.73  ? 221 ILE   D C    1 
ATOM   7119 O  O    . ILE   D 1 221 ? -25.152 -12.719 -45.839 1.00 28.50  ? 221 ILE   D O    1 
ATOM   7120 C  CB   . ILE   D 1 221 ? -25.564 -15.153 -44.128 1.00 27.29  ? 221 ILE   D CB   1 
ATOM   7121 C  CG1  . ILE   D 1 221 ? -25.234 -16.257 -43.121 1.00 26.48  ? 221 ILE   D CG1  1 
ATOM   7122 C  CG2  . ILE   D 1 221 ? -26.720 -15.566 -45.023 1.00 27.31  ? 221 ILE   D CG2  1 
ATOM   7123 C  CD1  . ILE   D 1 221 ? -26.310 -16.476 -42.089 1.00 25.74  ? 221 ILE   D CD1  1 
ATOM   7124 N  N    . PRO   D 1 222 ? -24.330 -14.175 -47.364 1.00 28.41  ? 222 PRO   D N    1 
ATOM   7125 C  CA   . PRO   D 1 222 ? -24.747 -13.391 -48.524 1.00 29.63  ? 222 PRO   D CA   1 
ATOM   7126 C  C    . PRO   D 1 222 ? -26.275 -13.261 -48.610 1.00 31.78  ? 222 PRO   D C    1 
ATOM   7127 O  O    . PRO   D 1 222 ? -26.987 -14.184 -48.207 1.00 28.93  ? 222 PRO   D O    1 
ATOM   7128 C  CB   . PRO   D 1 222 ? -24.184 -14.155 -49.728 1.00 28.12  ? 222 PRO   D CB   1 
ATOM   7129 C  CG   . PRO   D 1 222 ? -23.021 -14.934 -49.146 1.00 28.17  ? 222 PRO   D CG   1 
ATOM   7130 C  CD   . PRO   D 1 222 ? -23.487 -15.315 -47.754 1.00 28.23  ? 222 PRO   D CD   1 
ATOM   7131 N  N    . SER   D 1 223 ? -26.732 -12.102 -49.091 1.00 34.48  ? 223 SER   D N    1 
ATOM   7132 C  CA   . SER   D 1 223 ? -28.169 -11.761 -49.259 1.00 38.83  ? 223 SER   D CA   1 
ATOM   7133 C  C    . SER   D 1 223 ? -28.816 -12.746 -50.241 1.00 36.03  ? 223 SER   D C    1 
ATOM   7134 O  O    . SER   D 1 223 ? -28.238 -12.947 -51.330 1.00 40.98  ? 223 SER   D O    1 
ATOM   7135 C  CB   . SER   D 1 223 ? -28.335 -10.325 -49.699 1.00 39.83  ? 223 SER   D CB   1 
ATOM   7136 O  OG   . SER   D 1 223 ? -29.537 -9.805  -49.162 1.00 42.74  ? 223 SER   D OG   1 
ATOM   7137 N  N    . GLY   D 1 224 ? -29.940 -13.364 -49.853 1.00 36.15  ? 224 GLY   D N    1 
ATOM   7138 C  CA   . GLY   D 1 224 ? -30.693 -14.340 -50.676 1.00 34.37  ? 224 GLY   D CA   1 
ATOM   7139 C  C    . GLY   D 1 224 ? -29.898 -15.617 -50.914 1.00 34.86  ? 224 GLY   D C    1 
ATOM   7140 O  O    . GLY   D 1 224 ? -29.820 -16.085 -52.078 1.00 33.99  ? 224 GLY   D O    1 
ATOM   7141 N  N    . SER   D 1 225 ? -29.267 -16.140 -49.858 1.00 34.18  ? 225 SER   D N    1 
ATOM   7142 C  CA   . SER   D 1 225 ? -28.377 -17.328 -49.905 1.00 33.54  ? 225 SER   D CA   1 
ATOM   7143 C  C    . SER   D 1 225 ? -29.050 -18.497 -49.171 1.00 32.50  ? 225 SER   D C    1 
ATOM   7144 O  O    . SER   D 1 225 ? -28.341 -19.431 -48.776 1.00 32.49  ? 225 SER   D O    1 
ATOM   7145 C  CB   . SER   D 1 225 ? -26.992 -17.024 -49.353 1.00 34.37  ? 225 SER   D CB   1 
ATOM   7146 O  OG   . SER   D 1 225 ? -27.007 -16.894 -47.926 1.00 34.33  ? 225 SER   D OG   1 
ATOM   7147 N  N    . THR   D 1 226 ? -30.371 -18.460 -48.998 1.00 31.87  ? 226 THR   D N    1 
ATOM   7148 C  CA   . THR   D 1 226 ? -31.141 -19.601 -48.445 1.00 33.23  ? 226 THR   D CA   1 
ATOM   7149 C  C    . THR   D 1 226 ? -31.236 -20.688 -49.523 1.00 31.37  ? 226 THR   D C    1 
ATOM   7150 O  O    . THR   D 1 226 ? -30.675 -20.479 -50.623 1.00 30.94  ? 226 THR   D O    1 
ATOM   7151 C  CB   . THR   D 1 226 ? -32.520 -19.169 -47.944 1.00 33.84  ? 226 THR   D CB   1 
ATOM   7152 O  OG1  . THR   D 1 226 ? -33.202 -18.710 -49.108 1.00 34.26  ? 226 THR   D OG1  1 
ATOM   7153 C  CG2  . THR   D 1 226 ? -32.459 -18.094 -46.882 1.00 35.91  ? 226 THR   D CG2  1 
ATOM   7154 N  N    . GLY   D 1 227 ? -31.843 -21.827 -49.178 1.00 28.71  ? 227 GLY   D N    1 
ATOM   7155 C  CA   . GLY   D 1 227 ? -31.987 -22.993 -50.068 1.00 29.44  ? 227 GLY   D CA   1 
ATOM   7156 C  C    . GLY   D 1 227 ? -30.680 -23.371 -50.734 1.00 29.78  ? 227 GLY   D C    1 
ATOM   7157 O  O    . GLY   D 1 227 ? -29.683 -23.642 -50.005 1.00 31.10  ? 227 GLY   D O    1 
ATOM   7158 N  N    . ARG   D 1 228 ? -30.659 -23.341 -52.065 1.00 29.28  ? 228 ARG   D N    1 
ATOM   7159 C  CA   . ARG   D 1 228 ? -29.613 -23.983 -52.905 1.00 30.11  ? 228 ARG   D CA   1 
ATOM   7160 C  C    . ARG   D 1 228 ? -28.254 -23.294 -52.784 1.00 29.65  ? 228 ARG   D C    1 
ATOM   7161 O  O    . ARG   D 1 228 ? -27.287 -23.831 -53.336 1.00 32.73  ? 228 ARG   D O    1 
ATOM   7162 C  CB   . ARG   D 1 228 ? -30.025 -23.969 -54.378 1.00 32.71  ? 228 ARG   D CB   1 
ATOM   7163 C  CG   . ARG   D 1 228 ? -30.212 -22.588 -54.998 1.00 34.69  ? 228 ARG   D CG   1 
ATOM   7164 C  CD   . ARG   D 1 228 ? -30.910 -22.699 -56.353 1.00 37.58  ? 228 ARG   D CD   1 
ATOM   7165 N  NE   . ARG   D 1 228 ? -30.840 -21.476 -57.150 1.00 39.95  ? 228 ARG   D NE   1 
ATOM   7166 C  CZ   . ARG   D 1 228 ? -31.140 -21.374 -58.444 1.00 39.65  ? 228 ARG   D CZ   1 
ATOM   7167 N  NH1  . ARG   D 1 228 ? -31.533 -22.429 -59.138 1.00 38.69  ? 228 ARG   D NH1  1 
ATOM   7168 N  NH2  . ARG   D 1 228 ? -31.026 -20.205 -59.045 1.00 39.14  ? 228 ARG   D NH2  1 
ATOM   7169 N  N    . LEU   D 1 229 ? -28.162 -22.121 -52.167 1.00 32.33  ? 229 LEU   D N    1 
ATOM   7170 C  CA   . LEU   D 1 229 ? -26.877 -21.366 -52.138 1.00 34.08  ? 229 LEU   D CA   1 
ATOM   7171 C  C    . LEU   D 1 229 ? -26.087 -21.690 -50.853 1.00 33.71  ? 229 LEU   D C    1 
ATOM   7172 O  O    . LEU   D 1 229 ? -24.899 -21.262 -50.767 1.00 34.63  ? 229 LEU   D O    1 
ATOM   7173 C  CB   . LEU   D 1 229 ? -27.184 -19.869 -52.295 1.00 35.50  ? 229 LEU   D CB   1 
ATOM   7174 C  CG   . LEU   D 1 229 ? -27.739 -19.459 -53.666 1.00 35.49  ? 229 LEU   D CG   1 
ATOM   7175 C  CD1  . LEU   D 1 229 ? -27.920 -17.945 -53.758 1.00 34.06  ? 229 LEU   D CD1  1 
ATOM   7176 C  CD2  . LEU   D 1 229 ? -26.855 -19.974 -54.798 1.00 32.97  ? 229 LEU   D CD2  1 
ATOM   7177 N  N    . LEU   D 1 230 ? -26.701 -22.416 -49.902 1.00 33.11  ? 230 LEU   D N    1 
ATOM   7178 C  CA   . LEU   D 1 230 ? -26.014 -23.063 -48.738 1.00 32.52  ? 230 LEU   D CA   1 
ATOM   7179 C  C    . LEU   D 1 230 ? -25.439 -22.027 -47.758 1.00 30.83  ? 230 LEU   D C    1 
ATOM   7180 O  O    . LEU   D 1 230 ? -24.487 -22.375 -47.012 1.00 28.77  ? 230 LEU   D O    1 
ATOM   7181 C  CB   . LEU   D 1 230 ? -24.907 -23.966 -49.289 1.00 31.38  ? 230 LEU   D CB   1 
ATOM   7182 C  CG   . LEU   D 1 230 ? -25.387 -25.094 -50.200 1.00 31.43  ? 230 LEU   D CG   1 
ATOM   7183 C  CD1  . LEU   D 1 230 ? -24.210 -25.866 -50.766 1.00 31.14  ? 230 LEU   D CD1  1 
ATOM   7184 C  CD2  . LEU   D 1 230 ? -26.313 -26.026 -49.449 1.00 30.01  ? 230 LEU   D CD2  1 
ATOM   7185 N  N    . GLY   D 1 231 ? -25.987 -20.803 -47.753 1.00 31.05  ? 231 GLY   D N    1 
ATOM   7186 C  CA   . GLY   D 1 231 ? -25.524 -19.679 -46.910 1.00 29.23  ? 231 GLY   D CA   1 
ATOM   7187 C  C    . GLY   D 1 231 ? -24.077 -19.310 -47.210 1.00 27.75  ? 231 GLY   D C    1 
ATOM   7188 O  O    . GLY   D 1 231 ? -23.463 -18.627 -46.379 1.00 28.77  ? 231 GLY   D O    1 
ATOM   7189 N  N    . LEU   D 1 232 ? -23.579 -19.697 -48.385 1.00 27.29  ? 232 LEU   D N    1 
ATOM   7190 C  CA   . LEU   D 1 232 ? -22.167 -19.557 -48.813 1.00 29.92  ? 232 LEU   D CA   1 
ATOM   7191 C  C    . LEU   D 1 232 ? -22.006 -18.513 -49.928 1.00 31.70  ? 232 LEU   D C    1 
ATOM   7192 O  O    . LEU   D 1 232 ? -20.914 -17.905 -49.996 1.00 31.32  ? 232 LEU   D O    1 
ATOM   7193 C  CB   . LEU   D 1 232 ? -21.689 -20.916 -49.335 1.00 30.25  ? 232 LEU   D CB   1 
ATOM   7194 C  CG   . LEU   D 1 232 ? -21.283 -21.945 -48.281 1.00 31.62  ? 232 LEU   D CG   1 
ATOM   7195 C  CD1  . LEU   D 1 232 ? -20.574 -23.105 -48.952 1.00 31.63  ? 232 LEU   D CD1  1 
ATOM   7196 C  CD2  . LEU   D 1 232 ? -20.398 -21.336 -47.194 1.00 31.51  ? 232 LEU   D CD2  1 
ATOM   7197 N  N    . PHE   D 1 233 ? -22.976 -18.399 -50.844 1.00 32.14  ? 233 PHE   D N    1 
ATOM   7198 C  CA   . PHE   D 1 233 ? -22.809 -17.681 -52.137 1.00 34.05  ? 233 PHE   D CA   1 
ATOM   7199 C  C    . PHE   D 1 233 ? -23.955 -16.712 -52.373 1.00 32.74  ? 233 PHE   D C    1 
ATOM   7200 O  O    . PHE   D 1 233 ? -25.076 -16.986 -51.960 1.00 35.26  ? 233 PHE   D O    1 
ATOM   7201 C  CB   . PHE   D 1 233 ? -22.698 -18.678 -53.290 1.00 32.38  ? 233 PHE   D CB   1 
ATOM   7202 C  CG   . PHE   D 1 233 ? -21.453 -19.514 -53.235 1.00 31.65  ? 233 PHE   D CG   1 
ATOM   7203 C  CD1  . PHE   D 1 233 ? -20.220 -18.949 -53.488 1.00 34.12  ? 233 PHE   D CD1  1 
ATOM   7204 C  CD2  . PHE   D 1 233 ? -21.515 -20.866 -52.940 1.00 33.36  ? 233 PHE   D CD2  1 
ATOM   7205 C  CE1  . PHE   D 1 233 ? -19.064 -19.720 -53.423 1.00 35.85  ? 233 PHE   D CE1  1 
ATOM   7206 C  CE2  . PHE   D 1 233 ? -20.361 -21.632 -52.871 1.00 32.81  ? 233 PHE   D CE2  1 
ATOM   7207 C  CZ   . PHE   D 1 233 ? -19.139 -21.058 -53.116 1.00 32.99  ? 233 PHE   D CZ   1 
ATOM   7208 N  N    . PRO   D 1 234 ? -23.702 -15.571 -53.057 1.00 36.12  ? 234 PRO   D N    1 
ATOM   7209 C  CA   . PRO   D 1 234 ? -24.754 -14.596 -53.380 1.00 36.27  ? 234 PRO   D CA   1 
ATOM   7210 C  C    . PRO   D 1 234 ? -25.554 -14.934 -54.655 1.00 39.36  ? 234 PRO   D C    1 
ATOM   7211 O  O    . PRO   D 1 234 ? -26.758 -14.684 -54.706 1.00 37.16  ? 234 PRO   D O    1 
ATOM   7212 C  CB   . PRO   D 1 234 ? -23.921 -13.324 -53.596 1.00 34.03  ? 234 PRO   D CB   1 
ATOM   7213 C  CG   . PRO   D 1 234 ? -22.640 -13.831 -54.253 1.00 33.57  ? 234 PRO   D CG   1 
ATOM   7214 C  CD   . PRO   D 1 234 ? -22.379 -15.165 -53.578 1.00 35.84  ? 234 PRO   D CD   1 
ATOM   7215 N  N    . ASP   D 1 235 ? -24.854 -15.476 -55.657 1.00 40.81  ? 235 ASP   D N    1 
ATOM   7216 C  CA   . ASP   D 1 235 ? -25.372 -15.816 -57.007 1.00 42.35  ? 235 ASP   D CA   1 
ATOM   7217 C  C    . ASP   D 1 235 ? -24.915 -17.243 -57.325 1.00 44.45  ? 235 ASP   D C    1 
ATOM   7218 O  O    . ASP   D 1 235 ? -24.047 -17.760 -56.589 1.00 41.56  ? 235 ASP   D O    1 
ATOM   7219 C  CB   . ASP   D 1 235 ? -24.915 -14.776 -58.039 1.00 43.42  ? 235 ASP   D CB   1 
ATOM   7220 C  CG   . ASP   D 1 235 ? -23.422 -14.780 -58.349 1.00 45.53  ? 235 ASP   D CG   1 
ATOM   7221 O  OD1  . ASP   D 1 235 ? -22.909 -15.860 -58.713 1.00 47.73  ? 235 ASP   D OD1  1 
ATOM   7222 O  OD2  . ASP   D 1 235 ? -22.778 -13.696 -58.244 1.00 43.66  ? 235 ASP   D OD2  1 
ATOM   7223 N  N    . ALA   D 1 236 ? -25.476 -17.852 -58.375 1.00 48.54  ? 236 ALA   D N    1 
ATOM   7224 C  CA   . ALA   D 1 236 ? -25.242 -19.258 -58.769 1.00 47.46  ? 236 ALA   D CA   1 
ATOM   7225 C  C    . ALA   D 1 236 ? -24.166 -19.348 -59.860 1.00 49.11  ? 236 ALA   D C    1 
ATOM   7226 O  O    . ALA   D 1 236 ? -24.074 -20.425 -60.474 1.00 48.43  ? 236 ALA   D O    1 
ATOM   7227 C  CB   . ALA   D 1 236 ? -26.550 -19.870 -59.224 1.00 49.07  ? 236 ALA   D CB   1 
ATOM   7228 N  N    . ASN   D 1 237 ? -23.357 -18.301 -60.080 1.00 53.78  ? 237 ASN   D N    1 
ATOM   7229 C  CA   . ASN   D 1 237 ? -22.266 -18.310 -61.104 1.00 61.06  ? 237 ASN   D CA   1 
ATOM   7230 C  C    . ASN   D 1 237 ? -21.183 -19.320 -60.699 1.00 64.10  ? 237 ASN   D C    1 
ATOM   7231 O  O    . ASN   D 1 237 ? -21.228 -19.910 -59.610 1.00 60.38  ? 237 ASN   D O    1 
ATOM   7232 C  CB   . ASN   D 1 237 ? -21.630 -16.933 -61.338 1.00 62.00  ? 237 ASN   D CB   1 
ATOM   7233 C  CG   . ASN   D 1 237 ? -22.514 -15.991 -62.129 1.00 61.01  ? 237 ASN   D CG   1 
ATOM   7234 O  OD1  . ASN   D 1 237 ? -23.610 -15.641 -61.690 1.00 55.89  ? 237 ASN   D OD1  1 
ATOM   7235 N  ND2  . ASN   D 1 237 ? -22.042 -15.574 -63.295 1.00 57.58  ? 237 ASN   D ND2  1 
ATOM   7236 O  OXT  . ASN   D 1 237 ? -20.235 -19.557 -61.463 1.00 66.71  ? 237 ASN   D OXT  1 
HETATM 7237 MN MN   . MN    E 2 .   ? 7.161   -10.371 -7.459  1.00 14.48  ? 301 MN    A MN   1 
HETATM 7238 CA CA   . CA    F 3 .   ? 9.109   -7.025  -8.904  1.00 12.42  ? 302 CA    A CA   1 
HETATM 7239 C  C1   . A1EAW G 4 .   ? -9.118  -36.273 2.887   1.00 36.04  ? 301 A1EAW B C1   1 
HETATM 7240 C  C5   . A1EAW G 4 .   ? -11.066 -36.919 4.157   1.00 33.45  ? 301 A1EAW B C5   1 
HETATM 7241 C  C6   . A1EAW G 4 .   ? -9.058  -34.166 1.724   1.00 34.42  ? 301 A1EAW B C6   1 
HETATM 7242 C  C3   . A1EAW G 4 .   ? -11.008 -34.822 3.038   1.00 34.40  ? 301 A1EAW B C3   1 
HETATM 7243 C  C2   . A1EAW G 4 .   ? -9.725  -35.078 2.545   1.00 34.78  ? 301 A1EAW B C2   1 
HETATM 7244 N  N    . A1EAW G 4 .   ? -11.650 -35.752 3.822   1.00 35.19  ? 301 A1EAW B N    1 
HETATM 7245 C  C    . A1EAW G 4 .   ? -9.786  -37.185 3.684   1.00 32.76  ? 301 A1EAW B C    1 
HETATM 7246 O  O    . A1EAW G 4 .   ? -10.908 -38.628 5.747   1.00 33.74  ? 301 A1EAW B O    1 
HETATM 7247 C  C10  . A1EAW G 4 .   ? -11.573 -31.463 1.539   1.00 33.73  ? 301 A1EAW B C10  1 
HETATM 7248 C  C11  . A1EAW G 4 .   ? -12.863 -31.213 2.028   1.00 32.73  ? 301 A1EAW B C11  1 
HETATM 7249 C  C12  . A1EAW G 4 .   ? -13.493 -32.163 2.852   1.00 33.39  ? 301 A1EAW B C12  1 
HETATM 7250 C  C13  . A1EAW G 4 .   ? -14.886 -31.917 3.374   1.00 31.80  ? 301 A1EAW B C13  1 
HETATM 7251 C  C15  . A1EAW G 4 .   ? -11.653 -38.001 5.018   1.00 32.96  ? 301 A1EAW B C15  1 
HETATM 7252 C  C7   . A1EAW G 4 .   ? -9.663  -32.947 1.398   1.00 33.54  ? 301 A1EAW B C7   1 
HETATM 7253 C  C8   . A1EAW G 4 .   ? -10.945 -32.671 1.876   1.00 34.00  ? 301 A1EAW B C8   1 
HETATM 7254 C  C9   . A1EAW G 4 .   ? -11.624 -33.609 2.692   1.00 33.28  ? 301 A1EAW B C9   1 
HETATM 7255 N  N1   . A1EAW G 4 .   ? -12.870 -33.338 3.155   1.00 31.40  ? 301 A1EAW B N1   1 
HETATM 7256 O  O7   . A1EAW G 4 .   ? -15.557 -31.068 2.840   1.00 30.97  ? 301 A1EAW B O7   1 
HETATM 7257 C  C33  . A1EAW G 4 .   ? -12.102 -36.450 9.021   1.00 22.37  ? 301 A1EAW B C33  1 
HETATM 7258 C  C20  . A1EAW G 4 .   ? -13.019 -37.486 8.374   1.00 22.85  ? 301 A1EAW B C20  1 
HETATM 7259 C  C18  . A1EAW G 4 .   ? -14.654 -37.608 6.566   1.00 29.18  ? 301 A1EAW B C18  1 
HETATM 7260 C  C17  . A1EAW G 4 .   ? -14.048 -37.545 5.155   1.00 31.98  ? 301 A1EAW B C17  1 
HETATM 7261 N  N2   . A1EAW G 4 .   ? -12.897 -38.364 5.197   1.00 33.45  ? 301 A1EAW B N2   1 
HETATM 7262 O  O1   . A1EAW G 4 .   ? -13.918 -36.793 7.503   1.00 25.97  ? 301 A1EAW B O1   1 
HETATM 7263 O  O1M2 . A1EAW G 4 .   ? -10.866 -37.049 9.325   1.00 18.82  ? 301 A1EAW B O1M2 1 
HETATM 7264 C  C1M2 . A1EAW G 4 .   ? -10.662 -37.161 10.727  1.00 16.85  ? 301 A1EAW B C1M2 1 
HETATM 7265 C  C2M2 . A1EAW G 4 .   ? -9.210  -37.588 10.950  1.00 15.71  ? 301 A1EAW B C2M2 1 
HETATM 7266 C  C3M2 . A1EAW G 4 .   ? -8.999  -38.964 10.316  1.00 15.81  ? 301 A1EAW B C3M2 1 
HETATM 7267 C  C4M2 . A1EAW G 4 .   ? -9.924  -40.008 10.970  1.00 16.04  ? 301 A1EAW B C4M2 1 
HETATM 7268 C  C5M2 . A1EAW G 4 .   ? -11.361 -39.490 10.870  1.00 15.33  ? 301 A1EAW B C5M2 1 
HETATM 7269 C  C6M2 . A1EAW G 4 .   ? -12.289 -40.380 11.646  1.00 15.91  ? 301 A1EAW B C6M2 1 
HETATM 7270 O  O2M2 . A1EAW G 4 .   ? -9.040  -37.636 12.350  1.00 15.18  ? 301 A1EAW B O2M2 1 
HETATM 7271 O  O3M2 . A1EAW G 4 .   ? -7.668  -39.407 10.390  1.00 16.63  ? 301 A1EAW B O3M2 1 
HETATM 7272 O  O4M2 . A1EAW G 4 .   ? -9.753  -41.315 10.374  1.00 15.71  ? 301 A1EAW B O4M2 1 
HETATM 7273 O  O5M2 . A1EAW G 4 .   ? -11.545 -38.119 11.331  1.00 16.17  ? 301 A1EAW B O5M2 1 
HETATM 7274 O  O6M2 . A1EAW G 4 .   ? -12.094 -40.397 13.081  1.00 16.26  ? 301 A1EAW B O6M2 1 
HETATM 7275 C  C21  . A1EAW G 4 .   ? -17.949 -35.775 7.311   1.00 28.31  ? 301 A1EAW B C21  1 
HETATM 7276 C  C22  . A1EAW G 4 .   ? -16.929 -34.737 7.757   1.00 27.73  ? 301 A1EAW B C22  1 
HETATM 7277 C  C19  . A1EAW G 4 .   ? -16.840 -32.826 6.324   1.00 29.38  ? 301 A1EAW B C19  1 
HETATM 7278 C  C16  . A1EAW G 4 .   ? -16.749 -32.542 4.830   1.00 28.89  ? 301 A1EAW B C16  1 
HETATM 7279 N  N3   . A1EAW G 4 .   ? -15.376 -32.661 4.360   1.00 30.41  ? 301 A1EAW B N3   1 
HETATM 7280 O  O8   . A1EAW G 4 .   ? -16.444 -34.181 6.554   1.00 28.51  ? 301 A1EAW B O8   1 
HETATM 7281 O  O1M  . A1EAW G 4 .   ? -19.095 -35.130 7.745   1.00 25.66  ? 301 A1EAW B O1M  1 
HETATM 7282 C  C1M  . A1EAW G 4 .   ? -20.257 -35.892 7.842   1.00 20.98  ? 301 A1EAW B C1M  1 
HETATM 7283 C  C2M  . A1EAW G 4 .   ? -20.674 -36.743 6.668   1.00 19.72  ? 301 A1EAW B C2M  1 
HETATM 7284 C  C3M  . A1EAW G 4 .   ? -20.968 -35.988 5.394   1.00 18.17  ? 301 A1EAW B C3M  1 
HETATM 7285 C  C4M  . A1EAW G 4 .   ? -21.885 -34.804 5.643   1.00 17.83  ? 301 A1EAW B C4M  1 
HETATM 7286 C  C5M  . A1EAW G 4 .   ? -21.398 -34.004 6.817   1.00 18.76  ? 301 A1EAW B C5M  1 
HETATM 7287 C  C6M  . A1EAW G 4 .   ? -22.404 -32.910 7.198   1.00 18.66  ? 301 A1EAW B C6M  1 
HETATM 7288 O  O2M  . A1EAW G 4 .   ? -21.915 -37.331 7.042   1.00 18.63  ? 301 A1EAW B O2M  1 
HETATM 7289 O  O3M  . A1EAW G 4 .   ? -21.595 -36.888 4.472   1.00 16.85  ? 301 A1EAW B O3M  1 
HETATM 7290 O  O4M  . A1EAW G 4 .   ? -21.872 -33.959 4.484   1.00 17.91  ? 301 A1EAW B O4M  1 
HETATM 7291 O  O5M  . A1EAW G 4 .   ? -21.177 -34.827 7.972   1.00 20.52  ? 301 A1EAW B O5M  1 
HETATM 7292 O  O6M  . A1EAW G 4 .   ? -23.504 -33.508 7.907   1.00 18.12  ? 301 A1EAW B O6M  1 
HETATM 7293 MN MN   . MN    H 2 .   ? -24.071 -29.620 -3.695  1.00 15.40  ? 302 MN    B MN   1 
HETATM 7294 CA CA   . CA    I 3 .   ? -23.280 -30.655 0.287   1.00 18.66  ? 303 CA    B CA   1 
HETATM 7295 C  C1   . A1EAW J 4 .   ? 6.293   -27.585 14.087  1.00 78.25  ? 301 A1EAW C C1   1 
HETATM 7296 C  C5   . A1EAW J 4 .   ? 5.995   -26.879 16.388  1.00 73.83  ? 301 A1EAW C C5   1 
HETATM 7297 C  C6   . A1EAW J 4 .   ? 5.613   -26.096 12.275  1.00 78.91  ? 301 A1EAW C C6   1 
HETATM 7298 C  C3   . A1EAW J 4 .   ? 5.327   -25.449 14.605  1.00 78.20  ? 301 A1EAW C C3   1 
HETATM 7299 C  C2   . A1EAW J 4 .   ? 5.741   -26.381 13.643  1.00 77.71  ? 301 A1EAW C C2   1 
HETATM 7300 N  N    . A1EAW J 4 .   ? 5.462   -25.717 15.939  1.00 76.40  ? 301 A1EAW C N    1 
HETATM 7301 C  C    . A1EAW J 4 .   ? 6.418   -27.835 15.464  1.00 77.21  ? 301 A1EAW C C    1 
HETATM 7302 O  O    . A1EAW J 4 .   ? 7.219   -27.205 18.389  1.00 68.51  ? 301 A1EAW C O    1 
HETATM 7303 C  C10  . A1EAW J 4 .   ? 4.063   -22.719 12.450  1.00 74.29  ? 301 A1EAW C C10  1 
HETATM 7304 C  C11  . A1EAW J 4 .   ? 3.659   -21.815 13.438  1.00 70.53  ? 301 A1EAW C C11  1 
HETATM 7305 C  C12  . A1EAW J 4 .   ? 3.818   -22.148 14.788  1.00 71.28  ? 301 A1EAW C C12  1 
HETATM 7306 C  C13  . A1EAW J 4 .   ? 3.406   -21.228 15.912  1.00 67.90  ? 301 A1EAW C C13  1 
HETATM 7307 C  C15  . A1EAW J 4 .   ? 6.110   -27.125 17.867  1.00 72.45  ? 301 A1EAW C C15  1 
HETATM 7308 C  C7   . A1EAW J 4 .   ? 5.053   -24.878 11.864  1.00 79.35  ? 301 A1EAW C C7   1 
HETATM 7309 C  C8   . A1EAW J 4 .   ? 4.626   -23.945 12.823  1.00 77.87  ? 301 A1EAW C C8   1 
HETATM 7310 C  C9   . A1EAW J 4 .   ? 4.768   -24.235 14.190  1.00 76.15  ? 301 A1EAW C C9   1 
HETATM 7311 N  N1   . A1EAW J 4 .   ? 4.363   -23.342 15.124  1.00 72.26  ? 301 A1EAW C N1   1 
HETATM 7312 O  O7   . A1EAW J 4 .   ? 2.550   -20.371 15.717  1.00 65.73  ? 301 A1EAW C O7   1 
HETATM 7313 C  C33  . A1EAW J 4 .   ? 2.854   -24.537 23.036  1.00 46.27  ? 301 A1EAW C C33  1 
HETATM 7314 C  C20  . A1EAW J 4 .   ? 2.708   -24.899 21.575  1.00 48.51  ? 301 A1EAW C C20  1 
HETATM 7315 C  C18  . A1EAW J 4 .   ? 4.614   -26.054 20.659  1.00 59.28  ? 301 A1EAW C C18  1 
HETATM 7316 C  C17  . A1EAW J 4 .   ? 4.891   -27.401 19.985  1.00 61.70  ? 301 A1EAW C C17  1 
HETATM 7317 N  N2   . A1EAW J 4 .   ? 4.963   -27.239 18.545  1.00 66.10  ? 301 A1EAW C N2   1 
HETATM 7318 O  O1   . A1EAW J 4 .   ? 3.380   -26.144 21.376  1.00 55.00  ? 301 A1EAW C O1   1 
HETATM 7319 O  O1M2 . A1EAW J 4 .   ? 4.150   -23.977 23.240  1.00 40.02  ? 301 A1EAW C O1M2 1 
HETATM 7320 C  C1M2 . A1EAW J 4 .   ? 4.372   -23.672 24.630  1.00 41.12  ? 301 A1EAW C C1M2 1 
HETATM 7321 C  C2M2 . A1EAW J 4 .   ? 5.626   -22.801 24.704  1.00 38.73  ? 301 A1EAW C C2M2 1 
HETATM 7322 C  C3M2 . A1EAW J 4 .   ? 6.813   -23.606 24.263  1.00 35.26  ? 301 A1EAW C C3M2 1 
HETATM 7323 C  C4M2 . A1EAW J 4 .   ? 6.997   -24.810 25.176  1.00 35.13  ? 301 A1EAW C C4M2 1 
HETATM 7324 C  C5M2 . A1EAW J 4 .   ? 5.717   -25.650 25.215  1.00 35.86  ? 301 A1EAW C C5M2 1 
HETATM 7325 C  C6M2 . A1EAW J 4 .   ? 5.852   -26.789 26.243  1.00 34.17  ? 301 A1EAW C C6M2 1 
HETATM 7326 O  O2M2 . A1EAW J 4 .   ? 5.863   -22.374 26.033  1.00 40.10  ? 301 A1EAW C O2M2 1 
HETATM 7327 O  O3M2 . A1EAW J 4 .   ? 7.921   -22.736 24.283  1.00 39.73  ? 301 A1EAW C O3M2 1 
HETATM 7328 O  O4M2 . A1EAW J 4 .   ? 8.095   -25.598 24.699  1.00 32.79  ? 301 A1EAW C O4M2 1 
HETATM 7329 O  O5M2 . A1EAW J 4 .   ? 4.537   -24.838 25.467  1.00 36.65  ? 301 A1EAW C O5M2 1 
HETATM 7330 O  O6M2 . A1EAW J 4 .   ? 5.333   -26.377 27.511  1.00 35.22  ? 301 A1EAW C O6M2 1 
HETATM 7331 C  C21  . A1EAW J 4 .   ? -0.287  -22.647 18.080  1.00 38.64  ? 301 A1EAW C C21  1 
HETATM 7332 C  C22  . A1EAW J 4 .   ? 1.061   -21.948 17.971  1.00 40.90  ? 301 A1EAW C C22  1 
HETATM 7333 C  C19  . A1EAW J 4 .   ? 3.015   -21.584 19.395  1.00 53.78  ? 301 A1EAW C C19  1 
HETATM 7334 C  C16  . A1EAW J 4 .   ? 3.663   -20.685 18.331  1.00 58.41  ? 301 A1EAW C C16  1 
HETATM 7335 N  N3   . A1EAW J 4 .   ? 3.987   -21.420 17.110  1.00 62.69  ? 301 A1EAW C N3   1 
HETATM 7336 O  O8   . A1EAW J 4 .   ? 2.062   -22.511 18.830  1.00 48.03  ? 301 A1EAW C O8   1 
HETATM 7337 O  O1M  . A1EAW J 4 .   ? -1.181  -21.958 17.204  1.00 28.68  ? 301 A1EAW C O1M  1 
HETATM 7338 C  C1M  . A1EAW J 4 .   ? -2.512  -21.923 17.655  1.00 25.85  ? 301 A1EAW C C1M  1 
HETATM 7339 C  C2M  . A1EAW J 4 .   ? -3.364  -21.647 16.419  1.00 25.37  ? 301 A1EAW C C2M  1 
HETATM 7340 C  C3M  . A1EAW J 4 .   ? -2.998  -20.243 15.857  1.00 24.42  ? 301 A1EAW C C3M  1 
HETATM 7341 C  C4M  . A1EAW J 4 .   ? -3.133  -19.133 16.917  1.00 22.23  ? 301 A1EAW C C4M  1 
HETATM 7342 C  C5M  . A1EAW J 4 .   ? -2.397  -19.523 18.197  1.00 21.32  ? 301 A1EAW C C5M  1 
HETATM 7343 C  C6M  . A1EAW J 4 .   ? -2.705  -18.551 19.317  1.00 19.62  ? 301 A1EAW C C6M  1 
HETATM 7344 O  O2M  . A1EAW J 4 .   ? -4.713  -21.717 16.878  1.00 24.23  ? 301 A1EAW C O2M  1 
HETATM 7345 O  O3M  . A1EAW J 4 .   ? -3.786  -19.939 14.716  1.00 25.03  ? 301 A1EAW C O3M  1 
HETATM 7346 O  O4M  . A1EAW J 4 .   ? -2.576  -17.903 16.396  1.00 23.48  ? 301 A1EAW C O4M  1 
HETATM 7347 O  O5M  . A1EAW J 4 .   ? -2.715  -20.874 18.624  1.00 23.91  ? 301 A1EAW C O5M  1 
HETATM 7348 O  O6M  . A1EAW J 4 .   ? -4.047  -18.716 19.775  1.00 18.31  ? 301 A1EAW C O6M  1 
HETATM 7349 MN MN   . MN    K 2 .   ? -0.877  -9.318  12.484  1.00 17.14  ? 302 MN    C MN   1 
HETATM 7350 CA CA   . CA    L 3 .   ? -1.375  -12.638 15.014  1.00 18.21  ? 303 CA    C CA   1 
HETATM 7351 MN MN   . MN    M 2 .   ? -24.274 -29.265 -55.232 1.00 30.24  ? 301 MN    D MN   1 
HETATM 7352 CA CA   . CA    N 3 .   ? -28.312 -28.448 -54.107 1.00 30.62  ? 302 CA    D CA   1 
HETATM 7353 O  O    . HOH   O 5 .   ? 9.290   -0.992  -5.200  1.00 16.48  ? 401 HOH   A O    1 
HETATM 7354 O  O    . HOH   O 5 .   ? 19.748  -20.238 -13.726 1.00 19.42  ? 402 HOH   A O    1 
HETATM 7355 O  O    . HOH   O 5 .   ? -14.763 -23.927 -5.564  1.00 31.30  ? 403 HOH   A O    1 
HETATM 7356 O  O    . HOH   O 5 .   ? -1.990  -5.819  -7.043  1.00 10.73  ? 404 HOH   A O    1 
HETATM 7357 O  O    . HOH   O 5 .   ? 8.737   -29.311 -17.605 1.00 24.93  ? 405 HOH   A O    1 
HETATM 7358 O  O    . HOH   O 5 .   ? 9.290   -6.132  -11.090 1.00 7.79   ? 406 HOH   A O    1 
HETATM 7359 O  O    . HOH   O 5 .   ? -1.408  -11.413 -1.978  1.00 20.57  ? 407 HOH   A O    1 
HETATM 7360 O  O    . HOH   O 5 .   ? -1.810  -35.246 -9.365  1.00 18.93  ? 408 HOH   A O    1 
HETATM 7361 O  O    . HOH   O 5 .   ? 5.505   -9.345  -7.916  1.00 12.42  ? 409 HOH   A O    1 
HETATM 7362 O  O    . HOH   O 5 .   ? -4.794  1.765   -4.633  1.00 21.72  ? 410 HOH   A O    1 
HETATM 7363 O  O    . HOH   O 5 .   ? 6.020   -11.461 -6.076  1.00 14.74  ? 411 HOH   A O    1 
HETATM 7364 O  O    . HOH   O 5 .   ? -14.487 -12.925 -19.128 1.00 11.78  ? 412 HOH   A O    1 
HETATM 7365 O  O    . HOH   O 5 .   ? 6.734   -6.945  -9.027  1.00 9.86   ? 413 HOH   A O    1 
HETATM 7366 O  O    . HOH   O 5 .   ? -4.263  -34.652 -14.755 1.00 20.96  ? 414 HOH   A O    1 
HETATM 7367 O  O    . HOH   O 5 .   ? -3.582  -6.628  -32.017 1.00 19.97  ? 415 HOH   A O    1 
HETATM 7368 O  O    . HOH   O 5 .   ? -7.270  -9.247  -10.538 1.00 17.94  ? 416 HOH   A O    1 
HETATM 7369 O  O    . HOH   O 5 .   ? 12.607  -24.025 -7.124  1.00 12.66  ? 417 HOH   A O    1 
HETATM 7370 O  O    . HOH   O 5 .   ? -5.267  -6.501  -16.268 1.00 14.72  ? 418 HOH   A O    1 
HETATM 7371 O  O    . HOH   O 5 .   ? -4.737  -2.313  -23.161 1.00 17.02  ? 419 HOH   A O    1 
HETATM 7372 O  O    . HOH   O 5 .   ? -13.205 -31.061 -12.609 1.00 22.53  ? 420 HOH   A O    1 
HETATM 7373 O  O    . HOH   O 5 .   ? -7.868  -3.961  -14.404 1.00 23.40  ? 421 HOH   A O    1 
HETATM 7374 O  O    . HOH   O 5 .   ? 13.135  -20.468 -3.199  1.00 16.99  ? 422 HOH   A O    1 
HETATM 7375 O  O    . HOH   O 5 .   ? 5.276   -28.673 -13.595 1.00 31.68  ? 423 HOH   A O    1 
HETATM 7376 O  O    . HOH   P 5 .   ? -23.625 -29.352 -5.649  1.00 13.10  ? 401 HOH   B O    1 
HETATM 7377 O  O    . HOH   P 5 .   ? -23.397 -39.203 -7.393  1.00 18.68  ? 402 HOH   B O    1 
HETATM 7378 O  O    . HOH   P 5 .   ? -14.962 -36.013 3.179   1.00 16.24  ? 403 HOH   B O    1 
HETATM 7379 O  O    . HOH   P 5 .   ? -17.474 -34.620 1.801   1.00 10.20  ? 404 HOH   B O    1 
HETATM 7380 O  O    . HOH   P 5 .   ? -20.357 -39.035 3.925   1.00 21.44  ? 405 HOH   B O    1 
HETATM 7381 O  O    . HOH   P 5 .   ? -48.180 -26.766 6.699   1.00 22.06  ? 406 HOH   B O    1 
HETATM 7382 O  O    . HOH   P 5 .   ? -23.591 -32.706 -1.230  1.00 14.52  ? 407 HOH   B O    1 
HETATM 7383 O  O    . HOH   P 5 .   ? -24.251 -31.795 -4.032  1.00 13.06  ? 408 HOH   B O    1 
HETATM 7384 O  O    . HOH   P 5 .   ? -24.737 -31.481 1.969   1.00 10.65  ? 409 HOH   B O    1 
HETATM 7385 O  O    . HOH   P 5 .   ? -37.276 -32.652 9.428   1.00 17.33  ? 410 HOH   B O    1 
HETATM 7386 O  O    . HOH   P 5 .   ? -13.368 -34.611 6.021   1.00 20.62  ? 411 HOH   B O    1 
HETATM 7387 O  O    . HOH   P 5 .   ? -36.397 -46.427 0.605   1.00 22.75  ? 412 HOH   B O    1 
HETATM 7388 O  O    . HOH   P 5 .   ? -21.215 -32.172 -5.221  1.00 23.69  ? 413 HOH   B O    1 
HETATM 7389 O  O    . HOH   P 5 .   ? -32.834 -42.743 -5.292  1.00 28.76  ? 414 HOH   B O    1 
HETATM 7390 O  O    . HOH   P 5 .   ? -17.063 -35.746 4.218   1.00 20.24  ? 415 HOH   B O    1 
HETATM 7391 O  O    . HOH   Q 5 .   ? -22.023 -1.322  26.383  1.00 26.38  ? 401 HOH   C O    1 
HETATM 7392 O  O    . HOH   Q 5 .   ? 1.522   -19.052 13.789  1.00 21.29  ? 402 HOH   C O    1 
HETATM 7393 O  O    . HOH   Q 5 .   ? -20.339 -14.753 22.690  1.00 19.63  ? 403 HOH   C O    1 
HETATM 7394 O  O    . HOH   Q 5 .   ? 0.339   -8.594  2.209   1.00 20.09  ? 404 HOH   C O    1 
HETATM 7395 O  O    . HOH   Q 5 .   ? -0.835  1.103   26.084  1.00 19.08  ? 405 HOH   C O    1 
HETATM 7396 O  O    . HOH   Q 5 .   ? -2.009  -10.499 11.012  1.00 17.65  ? 406 HOH   C O    1 
HETATM 7397 O  O    . HOH   Q 5 .   ? -17.229 10.968  -1.138  1.00 19.95  ? 407 HOH   C O    1 
HETATM 7398 O  O    . HOH   Q 5 .   ? -8.600  15.801  4.496   1.00 16.01  ? 408 HOH   C O    1 
HETATM 7399 O  O    . HOH   Q 5 .   ? 0.057   -8.450  10.985  1.00 10.40  ? 409 HOH   C O    1 
HETATM 7400 O  O    . HOH   Q 5 .   ? -2.464  -12.953 12.864  1.00 19.29  ? 410 HOH   C O    1 
HETATM 7401 O  O    . HOH   Q 5 .   ? 2.735   3.724   11.870  1.00 16.16  ? 411 HOH   C O    1 
HETATM 7402 O  O    . HOH   Q 5 .   ? 4.456   1.808   11.701  1.00 19.08  ? 412 HOH   C O    1 
HETATM 7403 O  O    . HOH   Q 5 .   ? -15.742 -12.167 23.790  1.00 17.47  ? 413 HOH   C O    1 
HETATM 7404 O  O    . HOH   Q 5 .   ? -3.278  -13.382 16.055  1.00 17.09  ? 414 HOH   C O    1 
HETATM 7405 O  O    . HOH   Q 5 .   ? -20.392 -17.230 9.067   1.00 15.80  ? 415 HOH   C O    1 
HETATM 7406 O  O    . HOH   Q 5 .   ? -20.755 -7.053  -2.045  1.00 19.87  ? 416 HOH   C O    1 
HETATM 7407 O  O    . HOH   Q 5 .   ? 2.197   3.028   21.468  1.00 28.12  ? 417 HOH   C O    1 
HETATM 7408 O  O    . HOH   Q 5 .   ? 2.342   4.397   16.508  1.00 11.23  ? 418 HOH   C O    1 
HETATM 7409 O  O    . HOH   Q 5 .   ? 0.565   1.423   22.176  1.00 14.00  ? 419 HOH   C O    1 
HETATM 7410 O  O    . HOH   Q 5 .   ? 2.694   7.359   17.810  1.00 25.71  ? 420 HOH   C O    1 
HETATM 7411 O  O    . HOH   Q 5 .   ? 3.328   8.426   20.601  1.00 24.57  ? 421 HOH   C O    1 
HETATM 7412 O  O    . HOH   R 5 .   ? -29.441 -27.893 -52.133 1.00 24.65  ? 401 HOH   D O    1 
HETATM 7413 O  O    . HOH   R 5 .   ? -23.780 -19.702 -28.349 1.00 26.25  ? 402 HOH   D O    1 
HETATM 7414 O  O    . HOH   R 5 .   ? -25.077 -44.163 -46.879 1.00 22.50  ? 403 HOH   D O    1 
HETATM 7415 O  O    . HOH   R 5 .   ? -22.737 -29.321 -56.339 1.00 21.70  ? 404 HOH   D O    1 
HETATM 7416 O  O    . HOH   R 5 .   ? -30.842 -27.623 -37.728 1.00 19.75  ? 405 HOH   D O    1 
HETATM 7417 O  O    . HOH   R 5 .   ? -26.302 -26.685 -54.643 1.00 31.14  ? 406 HOH   D O    1 
# 
