data_9CH5
# 
_entry.id   9CH5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_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   9CH5         pdb_00009ch5 10.2210/pdb9ch5/pdb 
WWPDB D_1000285508 ?            ?                   
# 
_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       2025-01-29 
# 
_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                        9CH5 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-01 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex (bound to SAH)' 9CH3 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex' 9CH2 unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAM)' 9CH1 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (bound to SAH)' 9CH0 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-I65W) heteromeric complex (no cofactor)' 9CGW 
unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTE unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y58F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTF unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant Y93F) and RiPP precursor (SonA) heteromeric complex (no cofactor)' 
7LTH unspecified 
PDB 
;Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)
;
7LTR unspecified 
PDB 'Structure of the alpha-N-methyltransferase (SonM mutant R67A) and RiPP precursor (SonA) heteromeric complex (with SAH)' 7LTS 
unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAM)' 
8T1T unspecified 
PDB 
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAH)' 
8T1S unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              mffreema@umn.edu 
_pdbx_contact_author.name_first         Michael 
_pdbx_contact_author.name_last          Freeman 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0491-9618 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Crone, K.K.'   1 ? 
'Labonte, J.W.' 2 ? 
'Elias, M.'     3 ? 
'Freeman, M.F.' 4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Protein Sci.' 
_citation.journal_id_ASTM           PRCIEI 
_citation.journal_id_CSD            0795 
_citation.journal_id_ISSN           1469-896X 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            34 
_citation.language                  ? 
_citation.page_first                e70021 
_citation.page_last                 e70021 
_citation.title                     
'alpha-N-Methyltransferase regiospecificity is mediated by proximal, redundant enzyme-substrate interactions.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/pro.70021 
_citation.pdbx_database_id_PubMed   39840790 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Crone, K.K.'   1 0000-0001-9888-4710 
primary 'Labonte, J.W.' 2 ?                   
primary 'Elias, M.H.'   3 0000-0003-0406-7539 
primary 'Freeman, M.F.' 4 0000-0002-0491-9618 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'TP-methylase family protein'                                                      29068.326 2   ? ?    ? ? 
2 polymer     man 'Extradiol ring-cleavage dioxygenase LigAB LigA subunit domain-containing protein' 8784.607  2   ? L63D ? ? 
3 non-polymer man S-ADENOSYL-L-HOMOCYSTEINE                                                          384.411   2   ? ?    ? ? 
4 water       nat water                                                                              18.015    487 ? ?    ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
A,C ? 
2 'polypeptide(L)' no no MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYDVISHGNGD 
MHHHHHHMSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYDVISHGNGD B,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 S-ADENOSYL-L-HOMOCYSTEINE SAH 
4 water                     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   LEU n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   GLY n 
1 9   THR n 
1 10  GLY n 
1 11  LEU n 
1 12  GLN n 
1 13  LEU n 
1 14  ALA n 
1 15  GLY n 
1 16  GLN n 
1 17  ILE n 
1 18  SER n 
1 19  VAL n 
1 20  LEU n 
1 21  SER n 
1 22  ARG n 
1 23  SER n 
1 24  TYR n 
1 25  ILE n 
1 26  GLU n 
1 27  HIS n 
1 28  ALA n 
1 29  ASP n 
1 30  ILE n 
1 31  VAL n 
1 32  PHE n 
1 33  SER n 
1 34  LEU n 
1 35  LEU n 
1 36  PRO n 
1 37  ASP n 
1 38  GLY n 
1 39  PHE n 
1 40  SER n 
1 41  GLN n 
1 42  ARG n 
1 43  TRP n 
1 44  LEU n 
1 45  THR n 
1 46  LYS n 
1 47  LEU n 
1 48  ASN n 
1 49  PRO n 
1 50  ASN n 
1 51  VAL n 
1 52  ILE n 
1 53  ASN n 
1 54  LEU n 
1 55  GLN n 
1 56  GLN n 
1 57  PHE n 
1 58  TYR n 
1 59  ALA n 
1 60  GLN n 
1 61  ASN n 
1 62  GLY n 
1 63  GLU n 
1 64  VAL n 
1 65  LYS n 
1 66  ASN n 
1 67  ARG n 
1 68  ARG n 
1 69  ASP n 
1 70  THR n 
1 71  TYR n 
1 72  GLU n 
1 73  GLN n 
1 74  MET n 
1 75  VAL n 
1 76  ASN n 
1 77  ALA n 
1 78  ILE n 
1 79  LEU n 
1 80  ASP n 
1 81  ALA n 
1 82  VAL n 
1 83  ARG n 
1 84  ALA n 
1 85  GLY n 
1 86  LYS n 
1 87  LYS n 
1 88  THR n 
1 89  VAL n 
1 90  CYS n 
1 91  ALA n 
1 92  LEU n 
1 93  TYR n 
1 94  GLY n 
1 95  HIS n 
1 96  PRO n 
1 97  GLY n 
1 98  VAL n 
1 99  PHE n 
1 100 ALA n 
1 101 CYS n 
1 102 VAL n 
1 103 SER n 
1 104 HIS n 
1 105 MET n 
1 106 ALA n 
1 107 ILE n 
1 108 THR n 
1 109 ARG n 
1 110 ALA n 
1 111 LYS n 
1 112 ALA n 
1 113 GLU n 
1 114 GLY n 
1 115 PHE n 
1 116 SER n 
1 117 ALA n 
1 118 LYS n 
1 119 MET n 
1 120 GLU n 
1 121 PRO n 
1 122 GLY n 
1 123 ILE n 
1 124 SER n 
1 125 ALA n 
1 126 GLU n 
1 127 ALA n 
1 128 CYS n 
1 129 LEU n 
1 130 TRP n 
1 131 ALA n 
1 132 ASP n 
1 133 LEU n 
1 134 GLY n 
1 135 ILE n 
1 136 ASP n 
1 137 PRO n 
1 138 GLY n 
1 139 ASN n 
1 140 SER n 
1 141 GLY n 
1 142 HIS n 
1 143 GLN n 
1 144 SER n 
1 145 PHE n 
1 146 GLU n 
1 147 ALA n 
1 148 SER n 
1 149 GLN n 
1 150 PHE n 
1 151 MET n 
1 152 PHE n 
1 153 PHE n 
1 154 ASN n 
1 155 HIS n 
1 156 VAL n 
1 157 PRO n 
1 158 ASP n 
1 159 PRO n 
1 160 THR n 
1 161 THR n 
1 162 HIS n 
1 163 LEU n 
1 164 LEU n 
1 165 LEU n 
1 166 TRP n 
1 167 GLN n 
1 168 ILE n 
1 169 ALA n 
1 170 ILE n 
1 171 ALA n 
1 172 GLY n 
1 173 GLU n 
1 174 HIS n 
1 175 THR n 
1 176 LEU n 
1 177 THR n 
1 178 GLN n 
1 179 PHE n 
1 180 HIS n 
1 181 THR n 
1 182 SER n 
1 183 SER n 
1 184 ASP n 
1 185 ARG n 
1 186 LEU n 
1 187 GLN n 
1 188 ILE n 
1 189 LEU n 
1 190 VAL n 
1 191 GLU n 
1 192 GLN n 
1 193 LEU n 
1 194 ASN n 
1 195 GLN n 
1 196 TRP n 
1 197 TYR n 
1 198 PRO n 
1 199 LEU n 
1 200 ASP n 
1 201 HIS n 
1 202 GLU n 
1 203 VAL n 
1 204 VAL n 
1 205 ILE n 
1 206 TYR n 
1 207 GLU n 
1 208 ALA n 
1 209 ALA n 
1 210 ASN n 
1 211 LEU n 
1 212 PRO n 
1 213 ILE n 
1 214 GLN n 
1 215 ALA n 
1 216 PRO n 
1 217 ARG n 
1 218 ILE n 
1 219 GLU n 
1 220 ARG n 
1 221 LEU n 
1 222 PRO n 
1 223 LEU n 
1 224 ALA n 
1 225 ASN n 
1 226 LEU n 
1 227 PRO n 
1 228 GLN n 
1 229 ALA n 
1 230 HIS n 
1 231 LEU n 
1 232 MET n 
1 233 PRO n 
1 234 ILE n 
1 235 SER n 
1 236 THR n 
1 237 LEU n 
1 238 LEU n 
1 239 ILE n 
1 240 PRO n 
1 241 PRO n 
1 242 ALA n 
1 243 LYS n 
1 244 LYS n 
1 245 LEU n 
1 246 GLU n 
1 247 TYR n 
1 248 ASN n 
1 249 TYR n 
1 250 ALA n 
1 251 ILE n 
1 252 LEU n 
1 253 ALA n 
1 254 LYS n 
1 255 LEU n 
1 256 GLY n 
1 257 ILE n 
1 258 GLY n 
1 259 PRO n 
1 260 GLU n 
1 261 ASP n 
1 262 LEU n 
1 263 GLY n 
2 1   MET n 
2 2   HIS n 
2 3   HIS n 
2 4   HIS n 
2 5   HIS n 
2 6   HIS n 
2 7   HIS n 
2 8   MET n 
2 9   SER n 
2 10  GLY n 
2 11  LEU n 
2 12  SER n 
2 13  ASP n 
2 14  PHE n 
2 15  PHE n 
2 16  THR n 
2 17  GLN n 
2 18  LEU n 
2 19  GLY n 
2 20  GLN n 
2 21  ASP n 
2 22  ALA n 
2 23  GLN n 
2 24  LEU n 
2 25  MET n 
2 26  GLU n 
2 27  ASP n 
2 28  TYR n 
2 29  LYS n 
2 30  GLN n 
2 31  ASN n 
2 32  PRO n 
2 33  GLU n 
2 34  ALA n 
2 35  VAL n 
2 36  MET n 
2 37  ARG n 
2 38  ALA n 
2 39  HIS n 
2 40  GLY n 
2 41  LEU n 
2 42  THR n 
2 43  ASP n 
2 44  GLU n 
2 45  GLN n 
2 46  ILE n 
2 47  ASN n 
2 48  ALA n 
2 49  VAL n 
2 50  MET n 
2 51  THR n 
2 52  GLY n 
2 53  ASP n 
2 54  MET n 
2 55  GLU n 
2 56  LYS n 
2 57  LEU n 
2 58  LYS n 
2 59  THR n 
2 60  LEU n 
2 61  SER n 
2 62  GLY n 
2 63  ASP n 
2 64  SER n 
2 65  SER n 
2 66  TYR n 
2 67  GLN n 
2 68  SER n 
2 69  TYR n 
2 70  ASP n 
2 71  VAL n 
2 72  ILE n 
2 73  SER n 
2 74  HIS n 
2 75  GLY n 
2 76  ASN n 
2 77  GLY n 
2 78  ASP n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 78  ? ? SO_1479 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 263 ? ? SO_1478 ? ? ? ? ? ? 'Shewanella oneidensis' 70863 ? ? ? ? ? ? ? ? 'Escherichia coli' 
562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                   ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE                  ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE                ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'           ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE                  ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE                 ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'           ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE                   ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE                 ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                     ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE                ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE                   ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE                    ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE                ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE             ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE                   ? 'C5 H9 N O2'      115.130 
SAH non-polymer         . S-ADENOSYL-L-HOMOCYSTEINE ? 'C14 H20 N6 O5 S' 384.411 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  GLN 12  12  12  GLN GLN A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  GLN 16  16  16  GLN GLN A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  LEU 20  20  20  LEU LEU A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  ILE 25  25  25  ILE ILE A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  HIS 27  27  27  HIS HIS A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  ASP 29  29  29  ASP ASP A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  PHE 32  32  32  PHE PHE A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  ASP 37  37  37  ASP ASP A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  SER 40  40  40  SER SER A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  ASN 50  50  50  ASN ASN A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  ILE 52  52  52  ILE ILE A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLN 55  55  55  GLN GLN A . n 
A 1 56  GLN 56  56  56  GLN GLN A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  TYR 58  58  58  TYR TYR A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  ARG 67  67  67  ARG ARG A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ASP 69  69  69  ASP ASP A . n 
A 1 70  THR 70  70  70  THR THR A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  MET 74  74  74  MET MET A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ASN 76  76  76  ASN ASN A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ALA 84  84  84  ALA ALA A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LYS 86  86  86  LYS LYS A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  CYS 90  90  90  CYS CYS A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  TYR 93  93  93  TYR TYR A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  HIS 95  95  95  HIS HIS A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  PHE 99  99  99  PHE PHE A . n 
A 1 100 ALA 100 100 100 ALA ALA A . n 
A 1 101 CYS 101 101 101 CYS CYS A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 MET 105 105 105 MET MET A . n 
A 1 106 ALA 106 106 106 ALA ALA A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 PHE 115 115 115 PHE PHE A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 LYS 118 118 118 LYS LYS A . n 
A 1 119 MET 119 119 119 MET MET A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 PRO 121 121 121 PRO PRO A . n 
A 1 122 GLY 122 122 122 GLY GLY A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 GLU 126 126 126 GLU GLU A . n 
A 1 127 ALA 127 127 127 ALA ALA A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 TRP 130 130 130 TRP TRP A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 ILE 135 135 135 ILE ILE A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 HIS 142 142 142 HIS HIS A . n 
A 1 143 GLN 143 143 143 GLN GLN A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 PHE 145 145 145 PHE PHE A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 MET 151 151 151 MET MET A . n 
A 1 152 PHE 152 152 152 PHE PHE A . n 
A 1 153 PHE 153 153 153 PHE PHE A . n 
A 1 154 ASN 154 154 154 ASN ASN A . n 
A 1 155 HIS 155 155 155 HIS HIS A . n 
A 1 156 VAL 156 156 156 VAL VAL A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 PRO 159 159 159 PRO PRO A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 HIS 162 162 162 HIS HIS A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 LEU 165 165 165 LEU LEU A . n 
A 1 166 TRP 166 166 166 TRP TRP A . n 
A 1 167 GLN 167 167 167 GLN GLN A . n 
A 1 168 ILE 168 168 168 ILE ILE A . n 
A 1 169 ALA 169 169 169 ALA ALA A . n 
A 1 170 ILE 170 170 170 ILE ILE A . n 
A 1 171 ALA 171 171 171 ALA ALA A . n 
A 1 172 GLY 172 172 172 GLY GLY A . n 
A 1 173 GLU 173 173 173 GLU GLU A . n 
A 1 174 HIS 174 174 174 HIS HIS A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 LEU 176 176 176 LEU LEU A . n 
A 1 177 THR 177 177 177 THR THR A . n 
A 1 178 GLN 178 178 178 GLN GLN A . n 
A 1 179 PHE 179 179 179 PHE PHE A . n 
A 1 180 HIS 180 180 180 HIS HIS A . n 
A 1 181 THR 181 181 181 THR THR A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 ARG 185 185 185 ARG ARG A . n 
A 1 186 LEU 186 186 186 LEU LEU A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 LEU 189 189 189 LEU LEU A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 GLU 191 191 191 GLU GLU A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLN 195 195 195 GLN GLN A . n 
A 1 196 TRP 196 196 196 TRP TRP A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 ILE 205 205 205 ILE ILE A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 ASN 210 210 210 ASN ASN A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 PRO 212 212 212 PRO PRO A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 GLN 214 214 214 GLN GLN A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 PRO 216 216 216 PRO PRO A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 GLU 219 219 219 GLU GLU A . n 
A 1 220 ARG 220 220 220 ARG ARG A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 ASN 225 225 225 ASN ASN A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 PRO 227 227 227 PRO PRO A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 HIS 230 230 230 HIS HIS A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 MET 232 232 232 MET MET A . n 
A 1 233 PRO 233 233 233 PRO PRO A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 SER 235 235 235 SER SER A . n 
A 1 236 THR 236 236 236 THR THR A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 ILE 239 239 239 ILE ILE A . n 
A 1 240 PRO 240 240 240 PRO PRO A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 LYS 243 243 243 LYS LYS A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 TYR 247 247 247 TYR TYR A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 LYS 254 254 254 LYS LYS A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 GLY 256 256 256 GLY GLY A . n 
A 1 257 ILE 257 257 257 ILE ILE A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 PRO 259 259 259 PRO PRO A . n 
A 1 260 GLU 260 260 260 GLU GLU A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
B 2 1   MET 1   -6  ?   ?   ?   B . n 
B 2 2   HIS 2   -5  ?   ?   ?   B . n 
B 2 3   HIS 3   -4  ?   ?   ?   B . n 
B 2 4   HIS 4   -3  ?   ?   ?   B . n 
B 2 5   HIS 5   -2  ?   ?   ?   B . n 
B 2 6   HIS 6   -1  ?   ?   ?   B . n 
B 2 7   HIS 7   0   ?   ?   ?   B . n 
B 2 8   MET 8   1   ?   ?   ?   B . n 
B 2 9   SER 9   2   ?   ?   ?   B . n 
B 2 10  GLY 10  3   3   GLY GLY B . n 
B 2 11  LEU 11  4   4   LEU LEU B . n 
B 2 12  SER 12  5   5   SER SER B . n 
B 2 13  ASP 13  6   6   ASP ASP B . n 
B 2 14  PHE 14  7   7   PHE PHE B . n 
B 2 15  PHE 15  8   8   PHE PHE B . n 
B 2 16  THR 16  9   9   THR THR B . n 
B 2 17  GLN 17  10  10  GLN GLN B . n 
B 2 18  LEU 18  11  11  LEU LEU B . n 
B 2 19  GLY 19  12  12  GLY GLY B . n 
B 2 20  GLN 20  13  13  GLN GLN B . n 
B 2 21  ASP 21  14  14  ASP ASP B . n 
B 2 22  ALA 22  15  15  ALA ALA B . n 
B 2 23  GLN 23  16  16  GLN GLN B . n 
B 2 24  LEU 24  17  17  LEU LEU B . n 
B 2 25  MET 25  18  18  MET MET B . n 
B 2 26  GLU 26  19  19  GLU GLU B . n 
B 2 27  ASP 27  20  20  ASP ASP B . n 
B 2 28  TYR 28  21  21  TYR TYR B . n 
B 2 29  LYS 29  22  22  LYS LYS B . n 
B 2 30  GLN 30  23  23  GLN GLN B . n 
B 2 31  ASN 31  24  24  ASN ASN B . n 
B 2 32  PRO 32  25  25  PRO PRO B . n 
B 2 33  GLU 33  26  26  GLU GLU B . n 
B 2 34  ALA 34  27  27  ALA ALA B . n 
B 2 35  VAL 35  28  28  VAL VAL B . n 
B 2 36  MET 36  29  29  MET MET B . n 
B 2 37  ARG 37  30  30  ARG ARG B . n 
B 2 38  ALA 38  31  31  ALA ALA B . n 
B 2 39  HIS 39  32  32  HIS HIS B . n 
B 2 40  GLY 40  33  33  GLY GLY B . n 
B 2 41  LEU 41  34  34  LEU LEU B . n 
B 2 42  THR 42  35  35  THR THR B . n 
B 2 43  ASP 43  36  36  ASP ASP B . n 
B 2 44  GLU 44  37  37  GLU GLU B . n 
B 2 45  GLN 45  38  38  GLN GLN B . n 
B 2 46  ILE 46  39  39  ILE ILE B . n 
B 2 47  ASN 47  40  40  ASN ASN B . n 
B 2 48  ALA 48  41  41  ALA ALA B . n 
B 2 49  VAL 49  42  42  VAL VAL B . n 
B 2 50  MET 50  43  43  MET MET B . n 
B 2 51  THR 51  44  44  THR THR B . n 
B 2 52  GLY 52  45  45  GLY GLY B . n 
B 2 53  ASP 53  46  46  ASP ASP B . n 
B 2 54  MET 54  47  47  MET MET B . n 
B 2 55  GLU 55  48  48  GLU GLU B . n 
B 2 56  LYS 56  49  49  LYS LYS B . n 
B 2 57  LEU 57  50  50  LEU LEU B . n 
B 2 58  LYS 58  51  51  LYS LYS B . n 
B 2 59  THR 59  52  52  THR THR B . n 
B 2 60  LEU 60  53  53  LEU LEU B . n 
B 2 61  SER 61  54  ?   ?   ?   B . n 
B 2 62  GLY 62  55  ?   ?   ?   B . n 
B 2 63  ASP 63  56  ?   ?   ?   B . n 
B 2 64  SER 64  57  ?   ?   ?   B . n 
B 2 65  SER 65  58  ?   ?   ?   B . n 
B 2 66  TYR 66  59  ?   ?   ?   B . n 
B 2 67  GLN 67  60  ?   ?   ?   B . n 
B 2 68  SER 68  61  ?   ?   ?   B . n 
B 2 69  TYR 69  62  ?   ?   ?   B . n 
B 2 70  ASP 70  63  ?   ?   ?   B . n 
B 2 71  VAL 71  64  ?   ?   ?   B . n 
B 2 72  ILE 72  65  ?   ?   ?   B . n 
B 2 73  SER 73  66  ?   ?   ?   B . n 
B 2 74  HIS 74  67  ?   ?   ?   B . n 
B 2 75  GLY 75  68  ?   ?   ?   B . n 
B 2 76  ASN 76  69  ?   ?   ?   B . n 
B 2 77  GLY 77  70  ?   ?   ?   B . n 
B 2 78  ASP 78  71  ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   GLY 2   2   2   GLY GLY C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   LEU 4   4   4   LEU LEU C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   THR 9   9   9   THR THR C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  LEU 11  11  11  LEU LEU C . n 
C 1 12  GLN 12  12  12  GLN GLN C . n 
C 1 13  LEU 13  13  13  LEU LEU C . n 
C 1 14  ALA 14  14  14  ALA ALA C . n 
C 1 15  GLY 15  15  15  GLY GLY C . n 
C 1 16  GLN 16  16  16  GLN GLN C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  SER 18  18  18  SER SER C . n 
C 1 19  VAL 19  19  19  VAL VAL C . n 
C 1 20  LEU 20  20  20  LEU LEU C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  ARG 22  22  22  ARG ARG C . n 
C 1 23  SER 23  23  23  SER SER C . n 
C 1 24  TYR 24  24  24  TYR TYR C . n 
C 1 25  ILE 25  25  25  ILE ILE C . n 
C 1 26  GLU 26  26  26  GLU GLU C . n 
C 1 27  HIS 27  27  27  HIS HIS C . n 
C 1 28  ALA 28  28  28  ALA ALA C . n 
C 1 29  ASP 29  29  29  ASP ASP C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  PHE 32  32  32  PHE PHE C . n 
C 1 33  SER 33  33  33  SER SER C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  LEU 35  35  35  LEU LEU C . n 
C 1 36  PRO 36  36  36  PRO PRO C . n 
C 1 37  ASP 37  37  37  ASP ASP C . n 
C 1 38  GLY 38  38  38  GLY GLY C . n 
C 1 39  PHE 39  39  39  PHE PHE C . n 
C 1 40  SER 40  40  40  SER SER C . n 
C 1 41  GLN 41  41  41  GLN GLN C . n 
C 1 42  ARG 42  42  42  ARG ARG C . n 
C 1 43  TRP 43  43  43  TRP TRP C . n 
C 1 44  LEU 44  44  44  LEU LEU C . n 
C 1 45  THR 45  45  45  THR THR C . n 
C 1 46  LYS 46  46  46  LYS LYS C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  ASN 48  48  48  ASN ASN C . n 
C 1 49  PRO 49  49  49  PRO PRO C . n 
C 1 50  ASN 50  50  50  ASN ASN C . n 
C 1 51  VAL 51  51  51  VAL VAL C . n 
C 1 52  ILE 52  52  52  ILE ILE C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  GLN 55  55  55  GLN GLN C . n 
C 1 56  GLN 56  56  56  GLN GLN C . n 
C 1 57  PHE 57  57  57  PHE PHE C . n 
C 1 58  TYR 58  58  58  TYR TYR C . n 
C 1 59  ALA 59  59  59  ALA ALA C . n 
C 1 60  GLN 60  60  60  GLN GLN C . n 
C 1 61  ASN 61  61  61  ASN ASN C . n 
C 1 62  GLY 62  62  62  GLY GLY C . n 
C 1 63  GLU 63  63  63  GLU GLU C . n 
C 1 64  VAL 64  64  64  VAL VAL C . n 
C 1 65  LYS 65  65  65  LYS LYS C . n 
C 1 66  ASN 66  66  66  ASN ASN C . n 
C 1 67  ARG 67  67  67  ARG ARG C . n 
C 1 68  ARG 68  68  68  ARG ARG C . n 
C 1 69  ASP 69  69  69  ASP ASP C . n 
C 1 70  THR 70  70  70  THR THR C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  GLU 72  72  72  GLU GLU C . n 
C 1 73  GLN 73  73  73  GLN GLN C . n 
C 1 74  MET 74  74  74  MET MET C . n 
C 1 75  VAL 75  75  75  VAL VAL C . n 
C 1 76  ASN 76  76  76  ASN ASN C . n 
C 1 77  ALA 77  77  77  ALA ALA C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  LEU 79  79  79  LEU LEU C . n 
C 1 80  ASP 80  80  80  ASP ASP C . n 
C 1 81  ALA 81  81  81  ALA ALA C . n 
C 1 82  VAL 82  82  82  VAL VAL C . n 
C 1 83  ARG 83  83  83  ARG ARG C . n 
C 1 84  ALA 84  84  84  ALA ALA C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  LYS 86  86  86  LYS LYS C . n 
C 1 87  LYS 87  87  87  LYS LYS C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  VAL 89  89  89  VAL VAL C . n 
C 1 90  CYS 90  90  90  CYS CYS C . n 
C 1 91  ALA 91  91  91  ALA ALA C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  TYR 93  93  93  TYR TYR C . n 
C 1 94  GLY 94  94  94  GLY GLY C . n 
C 1 95  HIS 95  95  95  HIS HIS C . n 
C 1 96  PRO 96  96  96  PRO PRO C . n 
C 1 97  GLY 97  97  97  GLY GLY C . n 
C 1 98  VAL 98  98  98  VAL VAL C . n 
C 1 99  PHE 99  99  99  PHE PHE C . n 
C 1 100 ALA 100 100 100 ALA ALA C . n 
C 1 101 CYS 101 101 101 CYS CYS C . n 
C 1 102 VAL 102 102 102 VAL VAL C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 HIS 104 104 104 HIS HIS C . n 
C 1 105 MET 105 105 105 MET MET C . n 
C 1 106 ALA 106 106 106 ALA ALA C . n 
C 1 107 ILE 107 107 107 ILE ILE C . n 
C 1 108 THR 108 108 108 THR THR C . n 
C 1 109 ARG 109 109 109 ARG ARG C . n 
C 1 110 ALA 110 110 110 ALA ALA C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 ALA 112 112 112 ALA ALA C . n 
C 1 113 GLU 113 113 113 GLU GLU C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 PHE 115 115 115 PHE PHE C . n 
C 1 116 SER 116 116 116 SER SER C . n 
C 1 117 ALA 117 117 117 ALA ALA C . n 
C 1 118 LYS 118 118 118 LYS LYS C . n 
C 1 119 MET 119 119 119 MET MET C . n 
C 1 120 GLU 120 120 120 GLU GLU C . n 
C 1 121 PRO 121 121 121 PRO PRO C . n 
C 1 122 GLY 122 122 122 GLY GLY C . n 
C 1 123 ILE 123 123 123 ILE ILE C . n 
C 1 124 SER 124 124 124 SER SER C . n 
C 1 125 ALA 125 125 125 ALA ALA C . n 
C 1 126 GLU 126 126 126 GLU GLU C . n 
C 1 127 ALA 127 127 127 ALA ALA C . n 
C 1 128 CYS 128 128 128 CYS CYS C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 TRP 130 130 130 TRP TRP C . n 
C 1 131 ALA 131 131 131 ALA ALA C . n 
C 1 132 ASP 132 132 132 ASP ASP C . n 
C 1 133 LEU 133 133 133 LEU LEU C . n 
C 1 134 GLY 134 134 134 GLY GLY C . n 
C 1 135 ILE 135 135 135 ILE ILE C . n 
C 1 136 ASP 136 136 136 ASP ASP C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 HIS 142 142 142 HIS HIS C . n 
C 1 143 GLN 143 143 143 GLN GLN C . n 
C 1 144 SER 144 144 144 SER SER C . n 
C 1 145 PHE 145 145 145 PHE PHE C . n 
C 1 146 GLU 146 146 146 GLU GLU C . n 
C 1 147 ALA 147 147 147 ALA ALA C . n 
C 1 148 SER 148 148 148 SER SER C . n 
C 1 149 GLN 149 149 149 GLN GLN C . n 
C 1 150 PHE 150 150 150 PHE PHE C . n 
C 1 151 MET 151 151 151 MET MET C . n 
C 1 152 PHE 152 152 152 PHE PHE C . n 
C 1 153 PHE 153 153 153 PHE PHE C . n 
C 1 154 ASN 154 154 154 ASN ASN C . n 
C 1 155 HIS 155 155 155 HIS HIS C . n 
C 1 156 VAL 156 156 156 VAL VAL C . n 
C 1 157 PRO 157 157 157 PRO PRO C . n 
C 1 158 ASP 158 158 158 ASP ASP C . n 
C 1 159 PRO 159 159 159 PRO PRO C . n 
C 1 160 THR 160 160 160 THR THR C . n 
C 1 161 THR 161 161 161 THR THR C . n 
C 1 162 HIS 162 162 162 HIS HIS C . n 
C 1 163 LEU 163 163 163 LEU LEU C . n 
C 1 164 LEU 164 164 164 LEU LEU C . n 
C 1 165 LEU 165 165 165 LEU LEU C . n 
C 1 166 TRP 166 166 166 TRP TRP C . n 
C 1 167 GLN 167 167 167 GLN GLN C . n 
C 1 168 ILE 168 168 168 ILE ILE C . n 
C 1 169 ALA 169 169 169 ALA ALA C . n 
C 1 170 ILE 170 170 170 ILE ILE C . n 
C 1 171 ALA 171 171 171 ALA ALA C . n 
C 1 172 GLY 172 172 172 GLY GLY C . n 
C 1 173 GLU 173 173 173 GLU GLU C . n 
C 1 174 HIS 174 174 174 HIS HIS C . n 
C 1 175 THR 175 175 175 THR THR C . n 
C 1 176 LEU 176 176 176 LEU LEU C . n 
C 1 177 THR 177 177 177 THR THR C . n 
C 1 178 GLN 178 178 178 GLN GLN C . n 
C 1 179 PHE 179 179 179 PHE PHE C . n 
C 1 180 HIS 180 180 180 HIS HIS C . n 
C 1 181 THR 181 181 181 THR THR C . n 
C 1 182 SER 182 182 182 SER SER C . n 
C 1 183 SER 183 183 183 SER SER C . n 
C 1 184 ASP 184 184 184 ASP ASP C . n 
C 1 185 ARG 185 185 185 ARG ARG C . n 
C 1 186 LEU 186 186 186 LEU LEU C . n 
C 1 187 GLN 187 187 187 GLN GLN C . n 
C 1 188 ILE 188 188 188 ILE ILE C . n 
C 1 189 LEU 189 189 189 LEU LEU C . n 
C 1 190 VAL 190 190 190 VAL VAL C . n 
C 1 191 GLU 191 191 191 GLU GLU C . n 
C 1 192 GLN 192 192 192 GLN GLN C . n 
C 1 193 LEU 193 193 193 LEU LEU C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 GLN 195 195 195 GLN GLN C . n 
C 1 196 TRP 196 196 196 TRP TRP C . n 
C 1 197 TYR 197 197 197 TYR TYR C . n 
C 1 198 PRO 198 198 198 PRO PRO C . n 
C 1 199 LEU 199 199 199 LEU LEU C . n 
C 1 200 ASP 200 200 200 ASP ASP C . n 
C 1 201 HIS 201 201 201 HIS HIS C . n 
C 1 202 GLU 202 202 202 GLU GLU C . n 
C 1 203 VAL 203 203 203 VAL VAL C . n 
C 1 204 VAL 204 204 204 VAL VAL C . n 
C 1 205 ILE 205 205 205 ILE ILE C . n 
C 1 206 TYR 206 206 206 TYR TYR C . n 
C 1 207 GLU 207 207 207 GLU GLU C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 ALA 209 209 209 ALA ALA C . n 
C 1 210 ASN 210 210 210 ASN ASN C . n 
C 1 211 LEU 211 211 211 LEU LEU C . n 
C 1 212 PRO 212 212 212 PRO PRO C . n 
C 1 213 ILE 213 213 213 ILE ILE C . n 
C 1 214 GLN 214 214 214 GLN GLN C . n 
C 1 215 ALA 215 215 215 ALA ALA C . n 
C 1 216 PRO 216 216 216 PRO PRO C . n 
C 1 217 ARG 217 217 217 ARG ARG C . n 
C 1 218 ILE 218 218 218 ILE ILE C . n 
C 1 219 GLU 219 219 219 GLU GLU C . n 
C 1 220 ARG 220 220 220 ARG ARG C . n 
C 1 221 LEU 221 221 221 LEU LEU C . n 
C 1 222 PRO 222 222 222 PRO PRO C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 ASN 225 225 225 ASN ASN C . n 
C 1 226 LEU 226 226 226 LEU LEU C . n 
C 1 227 PRO 227 227 227 PRO PRO C . n 
C 1 228 GLN 228 228 228 GLN GLN C . n 
C 1 229 ALA 229 229 229 ALA ALA C . n 
C 1 230 HIS 230 230 230 HIS HIS C . n 
C 1 231 LEU 231 231 231 LEU LEU C . n 
C 1 232 MET 232 232 232 MET MET C . n 
C 1 233 PRO 233 233 233 PRO PRO C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 SER 235 235 235 SER SER C . n 
C 1 236 THR 236 236 236 THR THR C . n 
C 1 237 LEU 237 237 237 LEU LEU C . n 
C 1 238 LEU 238 238 238 LEU LEU C . n 
C 1 239 ILE 239 239 239 ILE ILE C . n 
C 1 240 PRO 240 240 240 PRO PRO C . n 
C 1 241 PRO 241 241 241 PRO PRO C . n 
C 1 242 ALA 242 242 242 ALA ALA C . n 
C 1 243 LYS 243 243 243 LYS LYS C . n 
C 1 244 LYS 244 244 244 LYS LYS C . n 
C 1 245 LEU 245 245 245 LEU LEU C . n 
C 1 246 GLU 246 246 246 GLU GLU C . n 
C 1 247 TYR 247 247 247 TYR TYR C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 TYR 249 249 249 TYR TYR C . n 
C 1 250 ALA 250 250 250 ALA ALA C . n 
C 1 251 ILE 251 251 251 ILE ILE C . n 
C 1 252 LEU 252 252 252 LEU LEU C . n 
C 1 253 ALA 253 253 253 ALA ALA C . n 
C 1 254 LYS 254 254 254 LYS LYS C . n 
C 1 255 LEU 255 255 255 LEU LEU C . n 
C 1 256 GLY 256 256 256 GLY GLY C . n 
C 1 257 ILE 257 257 257 ILE ILE C . n 
C 1 258 GLY 258 258 258 GLY GLY C . n 
C 1 259 PRO 259 259 259 PRO PRO C . n 
C 1 260 GLU 260 260 260 GLU GLU C . n 
C 1 261 ASP 261 261 261 ASP ASP C . n 
C 1 262 LEU 262 262 262 LEU LEU C . n 
C 1 263 GLY 263 263 263 GLY GLY C . n 
D 2 1   MET 1   -6  ?   ?   ?   D . n 
D 2 2   HIS 2   -5  ?   ?   ?   D . n 
D 2 3   HIS 3   -4  ?   ?   ?   D . n 
D 2 4   HIS 4   -3  ?   ?   ?   D . n 
D 2 5   HIS 5   -2  ?   ?   ?   D . n 
D 2 6   HIS 6   -1  ?   ?   ?   D . n 
D 2 7   HIS 7   0   ?   ?   ?   D . n 
D 2 8   MET 8   1   ?   ?   ?   D . n 
D 2 9   SER 9   2   ?   ?   ?   D . n 
D 2 10  GLY 10  3   ?   ?   ?   D . n 
D 2 11  LEU 11  4   4   LEU LEU D . n 
D 2 12  SER 12  5   5   SER SER D . n 
D 2 13  ASP 13  6   6   ASP ASP D . n 
D 2 14  PHE 14  7   7   PHE PHE D . n 
D 2 15  PHE 15  8   8   PHE PHE D . n 
D 2 16  THR 16  9   9   THR THR D . n 
D 2 17  GLN 17  10  10  GLN GLN D . n 
D 2 18  LEU 18  11  11  LEU LEU D . n 
D 2 19  GLY 19  12  12  GLY GLY D . n 
D 2 20  GLN 20  13  13  GLN GLN D . n 
D 2 21  ASP 21  14  14  ASP ASP D . n 
D 2 22  ALA 22  15  15  ALA ALA D . n 
D 2 23  GLN 23  16  16  GLN GLN D . n 
D 2 24  LEU 24  17  17  LEU LEU D . n 
D 2 25  MET 25  18  18  MET MET D . n 
D 2 26  GLU 26  19  19  GLU GLU D . n 
D 2 27  ASP 27  20  20  ASP ASP D . n 
D 2 28  TYR 28  21  21  TYR TYR D . n 
D 2 29  LYS 29  22  22  LYS LYS D . n 
D 2 30  GLN 30  23  23  GLN GLN D . n 
D 2 31  ASN 31  24  24  ASN ASN D . n 
D 2 32  PRO 32  25  25  PRO PRO D . n 
D 2 33  GLU 33  26  26  GLU GLU D . n 
D 2 34  ALA 34  27  27  ALA ALA D . n 
D 2 35  VAL 35  28  28  VAL VAL D . n 
D 2 36  MET 36  29  29  MET MET D . n 
D 2 37  ARG 37  30  30  ARG ARG D . n 
D 2 38  ALA 38  31  31  ALA ALA D . n 
D 2 39  HIS 39  32  32  HIS HIS D . n 
D 2 40  GLY 40  33  33  GLY GLY D . n 
D 2 41  LEU 41  34  34  LEU LEU D . n 
D 2 42  THR 42  35  35  THR THR D . n 
D 2 43  ASP 43  36  36  ASP ASP D . n 
D 2 44  GLU 44  37  37  GLU GLU D . n 
D 2 45  GLN 45  38  38  GLN GLN D . n 
D 2 46  ILE 46  39  39  ILE ILE D . n 
D 2 47  ASN 47  40  40  ASN ASN D . n 
D 2 48  ALA 48  41  41  ALA ALA D . n 
D 2 49  VAL 49  42  42  VAL VAL D . n 
D 2 50  MET 50  43  43  MET MET D . n 
D 2 51  THR 51  44  44  THR THR D . n 
D 2 52  GLY 52  45  45  GLY GLY D . n 
D 2 53  ASP 53  46  46  ASP ASP D . n 
D 2 54  MET 54  47  47  MET MET D . n 
D 2 55  GLU 55  48  48  GLU GLU D . n 
D 2 56  LYS 56  49  49  LYS LYS D . n 
D 2 57  LEU 57  50  50  LEU LEU D . n 
D 2 58  LYS 58  51  51  LYS LYS D . n 
D 2 59  THR 59  52  52  THR THR D . n 
D 2 60  LEU 60  53  53  LEU LEU D . n 
D 2 61  SER 61  54  54  SER SER D . n 
D 2 62  GLY 62  55  ?   ?   ?   D . n 
D 2 63  ASP 63  56  ?   ?   ?   D . n 
D 2 64  SER 64  57  ?   ?   ?   D . n 
D 2 65  SER 65  58  ?   ?   ?   D . n 
D 2 66  TYR 66  59  ?   ?   ?   D . n 
D 2 67  GLN 67  60  ?   ?   ?   D . n 
D 2 68  SER 68  61  ?   ?   ?   D . n 
D 2 69  TYR 69  62  62  TYR TYR D . n 
D 2 70  ASP 70  63  63  ASP ASP D . n 
D 2 71  VAL 71  64  64  VAL VAL D . n 
D 2 72  ILE 72  65  65  ILE ILE D . n 
D 2 73  SER 73  66  ?   ?   ?   D . n 
D 2 74  HIS 74  67  ?   ?   ?   D . n 
D 2 75  GLY 75  68  ?   ?   ?   D . n 
D 2 76  ASN 76  69  ?   ?   ?   D . n 
D 2 77  GLY 77  70  ?   ?   ?   D . n 
D 2 78  ASP 78  71  ?   ?   ?   D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 SAH 1   301 301 SAH SAH A . 
F 3 SAH 1   301 301 SAH SAH C . 
G 4 HOH 1   401 14  HOH HOH A . 
G 4 HOH 2   402 52  HOH HOH A . 
G 4 HOH 3   403 336 HOH HOH A . 
G 4 HOH 4   404 422 HOH HOH A . 
G 4 HOH 5   405 460 HOH HOH A . 
G 4 HOH 6   406 349 HOH HOH A . 
G 4 HOH 7   407 367 HOH HOH A . 
G 4 HOH 8   408 340 HOH HOH A . 
G 4 HOH 9   409 249 HOH HOH A . 
G 4 HOH 10  410 382 HOH HOH A . 
G 4 HOH 11  411 292 HOH HOH A . 
G 4 HOH 12  412 144 HOH HOH A . 
G 4 HOH 13  413 102 HOH HOH A . 
G 4 HOH 14  414 133 HOH HOH A . 
G 4 HOH 15  415 373 HOH HOH A . 
G 4 HOH 16  416 202 HOH HOH A . 
G 4 HOH 17  417 470 HOH HOH A . 
G 4 HOH 18  418 171 HOH HOH A . 
G 4 HOH 19  419 166 HOH HOH A . 
G 4 HOH 20  420 327 HOH HOH A . 
G 4 HOH 21  421 337 HOH HOH A . 
G 4 HOH 22  422 69  HOH HOH A . 
G 4 HOH 23  423 25  HOH HOH A . 
G 4 HOH 24  424 199 HOH HOH A . 
G 4 HOH 25  425 115 HOH HOH A . 
G 4 HOH 26  426 250 HOH HOH A . 
G 4 HOH 27  427 132 HOH HOH A . 
G 4 HOH 28  428 220 HOH HOH A . 
G 4 HOH 29  429 2   HOH HOH A . 
G 4 HOH 30  430 88  HOH HOH A . 
G 4 HOH 31  431 226 HOH HOH A . 
G 4 HOH 32  432 230 HOH HOH A . 
G 4 HOH 33  433 426 HOH HOH A . 
G 4 HOH 34  434 252 HOH HOH A . 
G 4 HOH 35  435 63  HOH HOH A . 
G 4 HOH 36  436 62  HOH HOH A . 
G 4 HOH 37  437 21  HOH HOH A . 
G 4 HOH 38  438 288 HOH HOH A . 
G 4 HOH 39  439 47  HOH HOH A . 
G 4 HOH 40  440 28  HOH HOH A . 
G 4 HOH 41  441 244 HOH HOH A . 
G 4 HOH 42  442 408 HOH HOH A . 
G 4 HOH 43  443 68  HOH HOH A . 
G 4 HOH 44  444 57  HOH HOH A . 
G 4 HOH 45  445 259 HOH HOH A . 
G 4 HOH 46  446 372 HOH HOH A . 
G 4 HOH 47  447 210 HOH HOH A . 
G 4 HOH 48  448 234 HOH HOH A . 
G 4 HOH 49  449 148 HOH HOH A . 
G 4 HOH 50  450 42  HOH HOH A . 
G 4 HOH 51  451 177 HOH HOH A . 
G 4 HOH 52  452 124 HOH HOH A . 
G 4 HOH 53  453 316 HOH HOH A . 
G 4 HOH 54  454 241 HOH HOH A . 
G 4 HOH 55  455 72  HOH HOH A . 
G 4 HOH 56  456 4   HOH HOH A . 
G 4 HOH 57  457 104 HOH HOH A . 
G 4 HOH 58  458 6   HOH HOH A . 
G 4 HOH 59  459 168 HOH HOH A . 
G 4 HOH 60  460 147 HOH HOH A . 
G 4 HOH 61  461 46  HOH HOH A . 
G 4 HOH 62  462 213 HOH HOH A . 
G 4 HOH 63  463 89  HOH HOH A . 
G 4 HOH 64  464 268 HOH HOH A . 
G 4 HOH 65  465 350 HOH HOH A . 
G 4 HOH 66  466 294 HOH HOH A . 
G 4 HOH 67  467 342 HOH HOH A . 
G 4 HOH 68  468 486 HOH HOH A . 
G 4 HOH 69  469 117 HOH HOH A . 
G 4 HOH 70  470 172 HOH HOH A . 
G 4 HOH 71  471 33  HOH HOH A . 
G 4 HOH 72  472 78  HOH HOH A . 
G 4 HOH 73  473 169 HOH HOH A . 
G 4 HOH 74  474 129 HOH HOH A . 
G 4 HOH 75  475 16  HOH HOH A . 
G 4 HOH 76  476 61  HOH HOH A . 
G 4 HOH 77  477 296 HOH HOH A . 
G 4 HOH 78  478 24  HOH HOH A . 
G 4 HOH 79  479 86  HOH HOH A . 
G 4 HOH 80  480 26  HOH HOH A . 
G 4 HOH 81  481 322 HOH HOH A . 
G 4 HOH 82  482 343 HOH HOH A . 
G 4 HOH 83  483 355 HOH HOH A . 
G 4 HOH 84  484 93  HOH HOH A . 
G 4 HOH 85  485 251 HOH HOH A . 
G 4 HOH 86  486 92  HOH HOH A . 
G 4 HOH 87  487 22  HOH HOH A . 
G 4 HOH 88  488 365 HOH HOH A . 
G 4 HOH 89  489 156 HOH HOH A . 
G 4 HOH 90  490 487 HOH HOH A . 
G 4 HOH 91  491 125 HOH HOH A . 
G 4 HOH 92  492 496 HOH HOH A . 
G 4 HOH 93  493 35  HOH HOH A . 
G 4 HOH 94  494 208 HOH HOH A . 
G 4 HOH 95  495 498 HOH HOH A . 
G 4 HOH 96  496 362 HOH HOH A . 
G 4 HOH 97  497 179 HOH HOH A . 
G 4 HOH 98  498 76  HOH HOH A . 
G 4 HOH 99  499 232 HOH HOH A . 
G 4 HOH 100 500 221 HOH HOH A . 
G 4 HOH 101 501 312 HOH HOH A . 
G 4 HOH 102 502 9   HOH HOH A . 
G 4 HOH 103 503 83  HOH HOH A . 
G 4 HOH 104 504 39  HOH HOH A . 
G 4 HOH 105 505 98  HOH HOH A . 
G 4 HOH 106 506 266 HOH HOH A . 
G 4 HOH 107 507 196 HOH HOH A . 
G 4 HOH 108 508 58  HOH HOH A . 
G 4 HOH 109 509 116 HOH HOH A . 
G 4 HOH 110 510 183 HOH HOH A . 
G 4 HOH 111 511 11  HOH HOH A . 
G 4 HOH 112 512 499 HOH HOH A . 
G 4 HOH 113 513 154 HOH HOH A . 
G 4 HOH 114 514 82  HOH HOH A . 
G 4 HOH 115 515 447 HOH HOH A . 
G 4 HOH 116 516 323 HOH HOH A . 
G 4 HOH 117 517 262 HOH HOH A . 
G 4 HOH 118 518 31  HOH HOH A . 
G 4 HOH 119 519 246 HOH HOH A . 
G 4 HOH 120 520 371 HOH HOH A . 
G 4 HOH 121 521 55  HOH HOH A . 
G 4 HOH 122 522 30  HOH HOH A . 
G 4 HOH 123 523 128 HOH HOH A . 
G 4 HOH 124 524 107 HOH HOH A . 
G 4 HOH 125 525 71  HOH HOH A . 
G 4 HOH 126 526 305 HOH HOH A . 
G 4 HOH 127 527 65  HOH HOH A . 
G 4 HOH 128 528 417 HOH HOH A . 
G 4 HOH 129 529 222 HOH HOH A . 
G 4 HOH 130 530 200 HOH HOH A . 
G 4 HOH 131 531 310 HOH HOH A . 
G 4 HOH 132 532 151 HOH HOH A . 
G 4 HOH 133 533 149 HOH HOH A . 
G 4 HOH 134 534 257 HOH HOH A . 
G 4 HOH 135 535 97  HOH HOH A . 
G 4 HOH 136 536 145 HOH HOH A . 
G 4 HOH 137 537 403 HOH HOH A . 
G 4 HOH 138 538 80  HOH HOH A . 
G 4 HOH 139 539 204 HOH HOH A . 
G 4 HOH 140 540 95  HOH HOH A . 
G 4 HOH 141 541 481 HOH HOH A . 
G 4 HOH 142 542 264 HOH HOH A . 
G 4 HOH 143 543 297 HOH HOH A . 
G 4 HOH 144 544 184 HOH HOH A . 
G 4 HOH 145 545 318 HOH HOH A . 
G 4 HOH 146 546 142 HOH HOH A . 
G 4 HOH 147 547 284 HOH HOH A . 
G 4 HOH 148 548 409 HOH HOH A . 
G 4 HOH 149 549 265 HOH HOH A . 
G 4 HOH 150 550 488 HOH HOH A . 
G 4 HOH 151 551 415 HOH HOH A . 
G 4 HOH 152 552 405 HOH HOH A . 
G 4 HOH 153 553 67  HOH HOH A . 
G 4 HOH 154 554 418 HOH HOH A . 
G 4 HOH 155 555 56  HOH HOH A . 
G 4 HOH 156 556 242 HOH HOH A . 
G 4 HOH 157 557 291 HOH HOH A . 
G 4 HOH 158 558 303 HOH HOH A . 
G 4 HOH 159 559 173 HOH HOH A . 
G 4 HOH 160 560 191 HOH HOH A . 
G 4 HOH 161 561 96  HOH HOH A . 
G 4 HOH 162 562 193 HOH HOH A . 
G 4 HOH 163 563 361 HOH HOH A . 
G 4 HOH 164 564 413 HOH HOH A . 
G 4 HOH 165 565 136 HOH HOH A . 
G 4 HOH 166 566 332 HOH HOH A . 
G 4 HOH 167 567 70  HOH HOH A . 
G 4 HOH 168 568 492 HOH HOH A . 
G 4 HOH 169 569 258 HOH HOH A . 
G 4 HOH 170 570 333 HOH HOH A . 
G 4 HOH 171 571 198 HOH HOH A . 
G 4 HOH 172 572 379 HOH HOH A . 
G 4 HOH 173 573 157 HOH HOH A . 
G 4 HOH 174 574 467 HOH HOH A . 
G 4 HOH 175 575 260 HOH HOH A . 
G 4 HOH 176 576 276 HOH HOH A . 
G 4 HOH 177 577 432 HOH HOH A . 
G 4 HOH 178 578 141 HOH HOH A . 
G 4 HOH 179 579 354 HOH HOH A . 
G 4 HOH 180 580 279 HOH HOH A . 
G 4 HOH 181 581 416 HOH HOH A . 
G 4 HOH 182 582 445 HOH HOH A . 
G 4 HOH 183 583 420 HOH HOH A . 
G 4 HOH 184 584 135 HOH HOH A . 
G 4 HOH 185 585 283 HOH HOH A . 
G 4 HOH 186 586 423 HOH HOH A . 
G 4 HOH 187 587 500 HOH HOH A . 
G 4 HOH 188 588 451 HOH HOH A . 
G 4 HOH 189 589 155 HOH HOH A . 
G 4 HOH 190 590 277 HOH HOH A . 
G 4 HOH 191 591 440 HOH HOH A . 
G 4 HOH 192 592 458 HOH HOH A . 
G 4 HOH 193 593 459 HOH HOH A . 
G 4 HOH 194 594 399 HOH HOH A . 
G 4 HOH 195 595 455 HOH HOH A . 
G 4 HOH 196 596 414 HOH HOH A . 
G 4 HOH 197 597 37  HOH HOH A . 
G 4 HOH 198 598 374 HOH HOH A . 
G 4 HOH 199 599 443 HOH HOH A . 
G 4 HOH 200 600 452 HOH HOH A . 
G 4 HOH 201 601 401 HOH HOH A . 
G 4 HOH 202 602 368 HOH HOH A . 
G 4 HOH 203 603 453 HOH HOH A . 
G 4 HOH 204 604 438 HOH HOH A . 
G 4 HOH 205 605 161 HOH HOH A . 
G 4 HOH 206 606 464 HOH HOH A . 
G 4 HOH 207 607 320 HOH HOH A . 
H 4 HOH 1   101 484 HOH HOH B . 
H 4 HOH 2   102 328 HOH HOH B . 
H 4 HOH 3   103 302 HOH HOH B . 
H 4 HOH 4   104 348 HOH HOH B . 
H 4 HOH 5   105 314 HOH HOH B . 
H 4 HOH 6   106 263 HOH HOH B . 
H 4 HOH 7   107 497 HOH HOH B . 
H 4 HOH 8   108 45  HOH HOH B . 
H 4 HOH 9   109 278 HOH HOH B . 
H 4 HOH 10  110 364 HOH HOH B . 
H 4 HOH 11  111 357 HOH HOH B . 
H 4 HOH 12  112 236 HOH HOH B . 
H 4 HOH 13  113 235 HOH HOH B . 
H 4 HOH 14  114 217 HOH HOH B . 
H 4 HOH 15  115 358 HOH HOH B . 
H 4 HOH 16  116 339 HOH HOH B . 
H 4 HOH 17  117 347 HOH HOH B . 
H 4 HOH 18  118 140 HOH HOH B . 
H 4 HOH 19  119 189 HOH HOH B . 
H 4 HOH 20  120 491 HOH HOH B . 
H 4 HOH 21  121 478 HOH HOH B . 
H 4 HOH 22  122 411 HOH HOH B . 
H 4 HOH 23  123 324 HOH HOH B . 
H 4 HOH 24  124 360 HOH HOH B . 
H 4 HOH 25  125 483 HOH HOH B . 
H 4 HOH 26  126 127 HOH HOH B . 
H 4 HOH 27  127 212 HOH HOH B . 
H 4 HOH 28  128 446 HOH HOH B . 
H 4 HOH 29  129 280 HOH HOH B . 
H 4 HOH 30  130 406 HOH HOH B . 
H 4 HOH 31  131 476 HOH HOH B . 
H 4 HOH 32  132 410 HOH HOH B . 
H 4 HOH 33  133 313 HOH HOH B . 
H 4 HOH 34  134 434 HOH HOH B . 
H 4 HOH 35  135 463 HOH HOH B . 
H 4 HOH 36  136 407 HOH HOH B . 
H 4 HOH 37  137 421 HOH HOH B . 
H 4 HOH 38  138 431 HOH HOH B . 
H 4 HOH 39  139 307 HOH HOH B . 
H 4 HOH 40  140 473 HOH HOH B . 
H 4 HOH 41  141 64  HOH HOH B . 
H 4 HOH 42  142 466 HOH HOH B . 
I 4 HOH 1   401 99  HOH HOH C . 
I 4 HOH 2   402 205 HOH HOH C . 
I 4 HOH 3   403 369 HOH HOH C . 
I 4 HOH 4   404 370 HOH HOH C . 
I 4 HOH 5   405 34  HOH HOH C . 
I 4 HOH 6   406 158 HOH HOH C . 
I 4 HOH 7   407 253 HOH HOH C . 
I 4 HOH 8   408 286 HOH HOH C . 
I 4 HOH 9   409 170 HOH HOH C . 
I 4 HOH 10  410 321 HOH HOH C . 
I 4 HOH 11  411 275 HOH HOH C . 
I 4 HOH 12  412 390 HOH HOH C . 
I 4 HOH 13  413 18  HOH HOH C . 
I 4 HOH 14  414 395 HOH HOH C . 
I 4 HOH 15  415 187 HOH HOH C . 
I 4 HOH 16  416 186 HOH HOH C . 
I 4 HOH 17  417 49  HOH HOH C . 
I 4 HOH 18  418 206 HOH HOH C . 
I 4 HOH 19  419 301 HOH HOH C . 
I 4 HOH 20  420 12  HOH HOH C . 
I 4 HOH 21  421 274 HOH HOH C . 
I 4 HOH 22  422 216 HOH HOH C . 
I 4 HOH 23  423 113 HOH HOH C . 
I 4 HOH 24  424 180 HOH HOH C . 
I 4 HOH 25  425 123 HOH HOH C . 
I 4 HOH 26  426 240 HOH HOH C . 
I 4 HOH 27  427 334 HOH HOH C . 
I 4 HOH 28  428 43  HOH HOH C . 
I 4 HOH 29  429 15  HOH HOH C . 
I 4 HOH 30  430 495 HOH HOH C . 
I 4 HOH 31  431 1   HOH HOH C . 
I 4 HOH 32  432 299 HOH HOH C . 
I 4 HOH 33  433 120 HOH HOH C . 
I 4 HOH 34  434 272 HOH HOH C . 
I 4 HOH 35  435 356 HOH HOH C . 
I 4 HOH 36  436 51  HOH HOH C . 
I 4 HOH 37  437 41  HOH HOH C . 
I 4 HOH 38  438 317 HOH HOH C . 
I 4 HOH 39  439 23  HOH HOH C . 
I 4 HOH 40  440 81  HOH HOH C . 
I 4 HOH 41  441 243 HOH HOH C . 
I 4 HOH 42  442 13  HOH HOH C . 
I 4 HOH 43  443 346 HOH HOH C . 
I 4 HOH 44  444 214 HOH HOH C . 
I 4 HOH 45  445 178 HOH HOH C . 
I 4 HOH 46  446 175 HOH HOH C . 
I 4 HOH 47  447 105 HOH HOH C . 
I 4 HOH 48  448 50  HOH HOH C . 
I 4 HOH 49  449 341 HOH HOH C . 
I 4 HOH 50  450 143 HOH HOH C . 
I 4 HOH 51  451 269 HOH HOH C . 
I 4 HOH 52  452 32  HOH HOH C . 
I 4 HOH 53  453 397 HOH HOH C . 
I 4 HOH 54  454 351 HOH HOH C . 
I 4 HOH 55  455 153 HOH HOH C . 
I 4 HOH 56  456 74  HOH HOH C . 
I 4 HOH 57  457 146 HOH HOH C . 
I 4 HOH 58  458 84  HOH HOH C . 
I 4 HOH 59  459 378 HOH HOH C . 
I 4 HOH 60  460 75  HOH HOH C . 
I 4 HOH 61  461 87  HOH HOH C . 
I 4 HOH 62  462 485 HOH HOH C . 
I 4 HOH 63  463 383 HOH HOH C . 
I 4 HOH 64  464 44  HOH HOH C . 
I 4 HOH 65  465 114 HOH HOH C . 
I 4 HOH 66  466 29  HOH HOH C . 
I 4 HOH 67  467 300 HOH HOH C . 
I 4 HOH 68  468 38  HOH HOH C . 
I 4 HOH 69  469 53  HOH HOH C . 
I 4 HOH 70  470 90  HOH HOH C . 
I 4 HOH 71  471 352 HOH HOH C . 
I 4 HOH 72  472 119 HOH HOH C . 
I 4 HOH 73  473 489 HOH HOH C . 
I 4 HOH 74  474 91  HOH HOH C . 
I 4 HOH 75  475 159 HOH HOH C . 
I 4 HOH 76  476 121 HOH HOH C . 
I 4 HOH 77  477 3   HOH HOH C . 
I 4 HOH 78  478 363 HOH HOH C . 
I 4 HOH 79  479 152 HOH HOH C . 
I 4 HOH 80  480 195 HOH HOH C . 
I 4 HOH 81  481 106 HOH HOH C . 
I 4 HOH 82  482 239 HOH HOH C . 
I 4 HOH 83  483 8   HOH HOH C . 
I 4 HOH 84  484 54  HOH HOH C . 
I 4 HOH 85  485 219 HOH HOH C . 
I 4 HOH 86  486 94  HOH HOH C . 
I 4 HOH 87  487 211 HOH HOH C . 
I 4 HOH 88  488 134 HOH HOH C . 
I 4 HOH 89  489 167 HOH HOH C . 
I 4 HOH 90  490 238 HOH HOH C . 
I 4 HOH 91  491 261 HOH HOH C . 
I 4 HOH 92  492 40  HOH HOH C . 
I 4 HOH 93  493 273 HOH HOH C . 
I 4 HOH 94  494 270 HOH HOH C . 
I 4 HOH 95  495 122 HOH HOH C . 
I 4 HOH 96  496 27  HOH HOH C . 
I 4 HOH 97  497 345 HOH HOH C . 
I 4 HOH 98  498 344 HOH HOH C . 
I 4 HOH 99  499 48  HOH HOH C . 
I 4 HOH 100 500 335 HOH HOH C . 
I 4 HOH 101 501 176 HOH HOH C . 
I 4 HOH 102 502 162 HOH HOH C . 
I 4 HOH 103 503 435 HOH HOH C . 
I 4 HOH 104 504 353 HOH HOH C . 
I 4 HOH 105 505 311 HOH HOH C . 
I 4 HOH 106 506 295 HOH HOH C . 
I 4 HOH 107 507 118 HOH HOH C . 
I 4 HOH 108 508 7   HOH HOH C . 
I 4 HOH 109 509 248 HOH HOH C . 
I 4 HOH 110 510 10  HOH HOH C . 
I 4 HOH 111 511 479 HOH HOH C . 
I 4 HOH 112 512 20  HOH HOH C . 
I 4 HOH 113 513 100 HOH HOH C . 
I 4 HOH 114 514 385 HOH HOH C . 
I 4 HOH 115 515 163 HOH HOH C . 
I 4 HOH 116 516 73  HOH HOH C . 
I 4 HOH 117 517 17  HOH HOH C . 
I 4 HOH 118 518 126 HOH HOH C . 
I 4 HOH 119 519 306 HOH HOH C . 
I 4 HOH 120 520 85  HOH HOH C . 
I 4 HOH 121 521 110 HOH HOH C . 
I 4 HOH 122 522 223 HOH HOH C . 
I 4 HOH 123 523 185 HOH HOH C . 
I 4 HOH 124 524 101 HOH HOH C . 
I 4 HOH 125 525 255 HOH HOH C . 
I 4 HOH 126 526 298 HOH HOH C . 
I 4 HOH 127 527 304 HOH HOH C . 
I 4 HOH 128 528 271 HOH HOH C . 
I 4 HOH 129 529 197 HOH HOH C . 
I 4 HOH 130 530 233 HOH HOH C . 
I 4 HOH 131 531 396 HOH HOH C . 
I 4 HOH 132 532 190 HOH HOH C . 
I 4 HOH 133 533 482 HOH HOH C . 
I 4 HOH 134 534 160 HOH HOH C . 
I 4 HOH 135 535 111 HOH HOH C . 
I 4 HOH 136 536 381 HOH HOH C . 
I 4 HOH 137 537 188 HOH HOH C . 
I 4 HOH 138 538 245 HOH HOH C . 
I 4 HOH 139 539 254 HOH HOH C . 
I 4 HOH 140 540 319 HOH HOH C . 
I 4 HOH 141 541 359 HOH HOH C . 
I 4 HOH 142 542 386 HOH HOH C . 
I 4 HOH 143 543 462 HOH HOH C . 
I 4 HOH 144 544 109 HOH HOH C . 
I 4 HOH 145 545 400 HOH HOH C . 
I 4 HOH 146 546 150 HOH HOH C . 
I 4 HOH 147 547 103 HOH HOH C . 
I 4 HOH 148 548 194 HOH HOH C . 
I 4 HOH 149 549 315 HOH HOH C . 
I 4 HOH 150 550 444 HOH HOH C . 
I 4 HOH 151 551 472 HOH HOH C . 
I 4 HOH 152 552 375 HOH HOH C . 
I 4 HOH 153 553 19  HOH HOH C . 
I 4 HOH 154 554 165 HOH HOH C . 
I 4 HOH 155 555 424 HOH HOH C . 
I 4 HOH 156 556 429 HOH HOH C . 
I 4 HOH 157 557 394 HOH HOH C . 
I 4 HOH 158 558 282 HOH HOH C . 
I 4 HOH 159 559 338 HOH HOH C . 
I 4 HOH 160 560 215 HOH HOH C . 
I 4 HOH 161 561 309 HOH HOH C . 
I 4 HOH 162 562 393 HOH HOH C . 
I 4 HOH 163 563 108 HOH HOH C . 
I 4 HOH 164 564 330 HOH HOH C . 
I 4 HOH 165 565 493 HOH HOH C . 
I 4 HOH 166 566 380 HOH HOH C . 
I 4 HOH 167 567 433 HOH HOH C . 
I 4 HOH 168 568 398 HOH HOH C . 
I 4 HOH 169 569 388 HOH HOH C . 
I 4 HOH 170 570 457 HOH HOH C . 
I 4 HOH 171 571 131 HOH HOH C . 
I 4 HOH 172 572 449 HOH HOH C . 
I 4 HOH 173 573 308 HOH HOH C . 
I 4 HOH 174 574 256 HOH HOH C . 
I 4 HOH 175 575 139 HOH HOH C . 
I 4 HOH 176 576 384 HOH HOH C . 
I 4 HOH 177 577 471 HOH HOH C . 
I 4 HOH 178 578 404 HOH HOH C . 
I 4 HOH 179 579 474 HOH HOH C . 
I 4 HOH 180 580 441 HOH HOH C . 
I 4 HOH 181 581 387 HOH HOH C . 
I 4 HOH 182 582 475 HOH HOH C . 
I 4 HOH 183 583 480 HOH HOH C . 
I 4 HOH 184 584 164 HOH HOH C . 
I 4 HOH 185 585 428 HOH HOH C . 
I 4 HOH 186 586 494 HOH HOH C . 
I 4 HOH 187 587 228 HOH HOH C . 
I 4 HOH 188 588 325 HOH HOH C . 
I 4 HOH 189 589 138 HOH HOH C . 
I 4 HOH 190 590 331 HOH HOH C . 
I 4 HOH 191 591 456 HOH HOH C . 
I 4 HOH 192 592 450 HOH HOH C . 
I 4 HOH 193 593 477 HOH HOH C . 
I 4 HOH 194 594 442 HOH HOH C . 
I 4 HOH 195 595 203 HOH HOH C . 
I 4 HOH 196 596 468 HOH HOH C . 
I 4 HOH 197 597 469 HOH HOH C . 
J 4 HOH 1   101 174 HOH HOH D . 
J 4 HOH 2   102 130 HOH HOH D . 
J 4 HOH 3   103 207 HOH HOH D . 
J 4 HOH 4   104 402 HOH HOH D . 
J 4 HOH 5   105 5   HOH HOH D . 
J 4 HOH 6   106 218 HOH HOH D . 
J 4 HOH 7   107 366 HOH HOH D . 
J 4 HOH 8   108 224 HOH HOH D . 
J 4 HOH 9   109 237 HOH HOH D . 
J 4 HOH 10  110 182 HOH HOH D . 
J 4 HOH 11  111 59  HOH HOH D . 
J 4 HOH 12  112 290 HOH HOH D . 
J 4 HOH 13  113 293 HOH HOH D . 
J 4 HOH 14  114 287 HOH HOH D . 
J 4 HOH 15  115 77  HOH HOH D . 
J 4 HOH 16  116 137 HOH HOH D . 
J 4 HOH 17  117 112 HOH HOH D . 
J 4 HOH 18  118 66  HOH HOH D . 
J 4 HOH 19  119 412 HOH HOH D . 
J 4 HOH 20  120 376 HOH HOH D . 
J 4 HOH 21  121 181 HOH HOH D . 
J 4 HOH 22  122 79  HOH HOH D . 
J 4 HOH 23  123 60  HOH HOH D . 
J 4 HOH 24  124 392 HOH HOH D . 
J 4 HOH 25  125 490 HOH HOH D . 
J 4 HOH 26  126 427 HOH HOH D . 
J 4 HOH 27  127 209 HOH HOH D . 
J 4 HOH 28  128 285 HOH HOH D . 
J 4 HOH 29  129 267 HOH HOH D . 
J 4 HOH 30  130 329 HOH HOH D . 
J 4 HOH 31  131 281 HOH HOH D . 
J 4 HOH 32  132 389 HOH HOH D . 
J 4 HOH 33  133 225 HOH HOH D . 
J 4 HOH 34  134 437 HOH HOH D . 
J 4 HOH 35  135 419 HOH HOH D . 
J 4 HOH 36  136 231 HOH HOH D . 
J 4 HOH 37  137 425 HOH HOH D . 
J 4 HOH 38  138 192 HOH HOH D . 
J 4 HOH 39  139 326 HOH HOH D . 
J 4 HOH 40  140 465 HOH HOH D . 
J 4 HOH 41  141 229 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.67 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CH5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.480 
_cell.length_a_esd                 ? 
_cell.length_b                     108.380 
_cell.length_b_esd                 ? 
_cell.length_c                     59.150 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CH5 
_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                   9CH5 
_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             2.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.53 
_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              5.5 
_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    '240 mM sodium malonate pH 5.5 with 2% PEG 3350' 
_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         2021-11-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033167 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033167 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CH5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.0 
_reflns.d_resolution_low                               19.90 
_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                                     75115 
_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                           85.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.29 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.19 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.077 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.0 
_reflns_shell.d_res_low                                     2.1 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10193 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.473 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.907 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CH5 
_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                            2.00 
_refine.ls_d_res_low                             19.90 
_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                     40198 
_refine.ls_number_reflns_R_free                  1987 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.31 
_refine.ls_percent_reflns_R_free                 4.94 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2418 
_refine.ls_R_factor_R_free                       0.2794 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2398 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 31.88 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.20 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        19.90 
_refine_hist.number_atoms_solvent             487 
_refine_hist.number_atoms_total               5452 
_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        4965 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_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' ? 0.007  ? ?   ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.041  ? ?   ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.424 ? 702 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.058  ? 782 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 902 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.00 2.05  . . 151 2989 99.00 . . . . 0.1983 . . . . . . . . . . . 0.2506 
'X-RAY DIFFRACTION' 2.05 2.11  . . 60  1272 42.00 . . . . 0.2151 . . . . . . . . . . . 0.2186 
'X-RAY DIFFRACTION' 2.11 2.17  . . 131 2968 98.00 . . . . 0.1968 . . . . . . . . . . . 0.2475 
'X-RAY DIFFRACTION' 2.17 2.24  . . 146 2881 97.00 . . . . 0.1762 . . . . . . . . . . . 0.2243 
'X-RAY DIFFRACTION' 2.24 2.32  . . 106 2096 69.00 . . . . 0.1737 . . . . . . . . . . . 0.2181 
'X-RAY DIFFRACTION' 2.32 2.41  . . 166 2967 98.00 . . . . 0.1797 . . . . . . . . . . . 0.2275 
'X-RAY DIFFRACTION' 2.41 2.52  . . 135 2952 98.00 . . . . 0.2080 . . . . . . . . . . . 0.2308 
'X-RAY DIFFRACTION' 2.52 2.65  . . 152 2890 96.00 . . . . 0.2328 . . . . . . . . . . . 0.2585 
'X-RAY DIFFRACTION' 2.65 2.82  . . 183 2900 96.00 . . . . 0.2366 . . . . . . . . . . . 0.2834 
'X-RAY DIFFRACTION' 2.82 3.03  . . 145 2954 98.00 . . . . 0.2578 . . . . . . . . . . . 0.2624 
'X-RAY DIFFRACTION' 3.03 3.34  . . 156 2991 99.00 . . . . 0.2709 . . . . . . . . . . . 0.3047 
'X-RAY DIFFRACTION' 3.34 3.82  . . 129 2581 86.00 . . . . 0.2704 . . . . . . . . . . . 0.3264 
'X-RAY DIFFRACTION' 3.82 4.80  . . 161 2812 93.00 . . . . 0.2488 . . . . . . . . . . . 0.3302 
'X-RAY DIFFRACTION' 4.80 19.90 . . 166 2958 97.00 . . . . 0.2721 . . . . . . . . . . . 0.2759 
# 
_struct.entry_id                     9CH5 
_struct.title                        
'Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA-L63D) heteromeric complex (bound to SAM)' 
_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        9CH5 
_struct_keywords.text            'Alpha-N-methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q8EGW3_SHEON Q8EGW3 ? 1 
;MGSLVCVGTGLQLAGQISVLSRSYIEHADIVFSLLPDGFSQRWLTKLNPNVINLQQFYAQNGEVKNRRDTYEQMVNAILD
AVRAGKKTVCALYGHPGVFACVSHMAITRAKAEGFSAKMEPGISAEACLWADLGIDPGNSGHQSFEASQFMFFNHVPDPT
THLLLWQIAIAGEHTLTQFHTSSDRLQILVEQLNQWYPLDHEVVIYEAANLPIQAPRIERLPLANLPQAHLMPISTLLIP
PAKKLEYNYAILAKLGIGPEDLG
;
1 
2 UNP Q8EGW2_SHEON Q8EGW2 ? 2 MSGLSDFFTQLGQDAQLMEDYKQNPEAVMRAHGLTDEQINAVMTGDMEKLKTLSGDSSYQSYLVISHGNGD 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9CH5 A 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
2 2 9CH5 B 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
3 1 9CH5 C 1 ? 263 ? Q8EGW3 1 ? 263 ? 1 263 
4 2 9CH5 D 8 ? 78  ? Q8EGW2 1 ? 71  ? 1 71  
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
2 9CH5 MET B 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 1  
2 9CH5 HIS B 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 2  
2 9CH5 HIS B 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 3  
2 9CH5 HIS B 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 4  
2 9CH5 HIS B 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 5  
2 9CH5 HIS B 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 6  
2 9CH5 HIS B 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  7  
2 9CH5 ASP B 70 ? UNP Q8EGW2 LEU 63 'engineered mutation'   63 8  
4 9CH5 MET D 1  ? UNP Q8EGW2 ?   ?  'initiating methionine' -6 9  
4 9CH5 HIS D 2  ? UNP Q8EGW2 ?   ?  'expression tag'        -5 10 
4 9CH5 HIS D 3  ? UNP Q8EGW2 ?   ?  'expression tag'        -4 11 
4 9CH5 HIS D 4  ? UNP Q8EGW2 ?   ?  'expression tag'        -3 12 
4 9CH5 HIS D 5  ? UNP Q8EGW2 ?   ?  'expression tag'        -2 13 
4 9CH5 HIS D 6  ? UNP Q8EGW2 ?   ?  'expression tag'        -1 14 
4 9CH5 HIS D 7  ? UNP Q8EGW2 ?   ?  'expression tag'        0  15 
4 9CH5 ASP D 70 ? UNP Q8EGW2 LEU 63 'engineered mutation'   63 16 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10290 ? 
1 MORE         -65   ? 
1 'SSA (A^2)'  24360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 18  ? ALA A 28  ? SER A 18  ALA A 28  1 ? 11 
HELX_P HELX_P2  AA2 ASP A 37  ? ASN A 48  ? ASP A 37  ASN A 48  1 ? 12 
HELX_P HELX_P3  AA3 GLN A 55  ? TYR A 58  ? GLN A 55  TYR A 58  5 ? 4  
HELX_P HELX_P4  AA4 ASN A 66  ? GLY A 85  ? ASN A 66  GLY A 85  1 ? 20 
HELX_P HELX_P5  AA5 CYS A 101 ? GLU A 113 ? CYS A 101 GLU A 113 1 ? 13 
HELX_P HELX_P6  AA6 SER A 124 ? GLY A 134 ? SER A 124 GLY A 134 1 ? 11 
HELX_P HELX_P7  AA7 ALA A 147 ? PHE A 153 ? ALA A 147 PHE A 153 1 ? 7  
HELX_P HELX_P8  AA8 GLN A 167 ? ALA A 171 ? GLN A 167 ALA A 171 5 ? 5  
HELX_P HELX_P9  AA9 SER A 182 ? ASN A 194 ? SER A 182 ASN A 194 1 ? 13 
HELX_P HELX_P10 AB1 ALA A 224 ? ALA A 229 ? ALA A 224 ALA A 229 5 ? 6  
HELX_P HELX_P11 AB2 ASN A 248 ? LEU A 255 ? ASN A 248 LEU A 255 1 ? 8  
HELX_P HELX_P12 AB3 GLY A 258 ? LEU A 262 ? GLY A 258 LEU A 262 5 ? 5  
HELX_P HELX_P13 AB4 LEU B 11  ? ASP B 21  ? LEU B 4   ASP B 14  1 ? 11 
HELX_P HELX_P14 AB5 ASP B 21  ? ASN B 31  ? ASP B 14  ASN B 24  1 ? 11 
HELX_P HELX_P15 AB6 ASN B 31  ? HIS B 39  ? ASN B 24  HIS B 32  1 ? 9  
HELX_P HELX_P16 AB7 THR B 42  ? GLY B 52  ? THR B 35  GLY B 45  1 ? 11 
HELX_P HELX_P17 AB8 ASP B 53  ? LEU B 60  ? ASP B 46  LEU B 53  1 ? 8  
HELX_P HELX_P18 AB9 SER C 18  ? ALA C 28  ? SER C 18  ALA C 28  1 ? 11 
HELX_P HELX_P19 AC1 ASP C 37  ? ASN C 48  ? ASP C 37  ASN C 48  1 ? 12 
HELX_P HELX_P20 AC2 GLN C 55  ? TYR C 58  ? GLN C 55  TYR C 58  5 ? 4  
HELX_P HELX_P21 AC3 ASN C 66  ? GLY C 85  ? ASN C 66  GLY C 85  1 ? 20 
HELX_P HELX_P22 AC4 CYS C 101 ? GLU C 113 ? CYS C 101 GLU C 113 1 ? 13 
HELX_P HELX_P23 AC5 SER C 124 ? GLY C 134 ? SER C 124 GLY C 134 1 ? 11 
HELX_P HELX_P24 AC6 ALA C 147 ? PHE C 153 ? ALA C 147 PHE C 153 1 ? 7  
HELX_P HELX_P25 AC7 GLN C 167 ? ALA C 171 ? GLN C 167 ALA C 171 5 ? 5  
HELX_P HELX_P26 AC8 SER C 182 ? ASN C 194 ? SER C 182 ASN C 194 1 ? 13 
HELX_P HELX_P27 AC9 ALA C 224 ? ALA C 229 ? ALA C 224 ALA C 229 5 ? 6  
HELX_P HELX_P28 AD1 ASN C 248 ? LEU C 255 ? ASN C 248 LEU C 255 1 ? 8  
HELX_P HELX_P29 AD2 GLY C 258 ? LEU C 262 ? GLY C 258 LEU C 262 5 ? 5  
HELX_P HELX_P30 AD3 SER D 12  ? ASP D 21  ? SER D 5   ASP D 14  1 ? 10 
HELX_P HELX_P31 AD4 ASP D 21  ? ASN D 31  ? ASP D 14  ASN D 24  1 ? 11 
HELX_P HELX_P32 AD5 ASN D 31  ? HIS D 39  ? ASN D 24  HIS D 32  1 ? 9  
HELX_P HELX_P33 AD6 THR D 42  ? GLY D 52  ? THR D 35  GLY D 45  1 ? 11 
HELX_P HELX_P34 AD7 ASP D 53  ? SER D 61  ? ASP D 46  SER D 54  1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5  ? 
AA2 ? 10 ? 
AA3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? parallel      
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? parallel      
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? 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  VAL A 51  ? ASN A 53  ? VAL A 51  ASN A 53  
AA1 2  ILE A 30  ? LEU A 34  ? ILE A 30  LEU A 34  
AA1 3  LYS A 87  ? LEU A 92  ? LYS A 87  LEU A 92  
AA1 4  SER A 3   ? GLY A 8   ? SER A 3   GLY A 8   
AA1 5  SER A 116 ? MET A 119 ? SER A 116 MET A 119 
AA2 1  ARG A 217 ? PRO A 222 ? ARG A 217 PRO A 222 
AA2 2  GLU A 202 ? GLU A 207 ? GLU A 202 GLU A 207 
AA2 3  THR A 236 ? ILE A 239 ? THR A 236 ILE A 239 
AA2 4  HIS A 162 ? TRP A 166 ? HIS A 162 TRP A 166 
AA2 5  HIS A 142 ? GLU A 146 ? HIS A 142 GLU A 146 
AA2 6  HIS C 142 ? GLU C 146 ? HIS C 142 GLU C 146 
AA2 7  HIS C 162 ? TRP C 166 ? HIS C 162 TRP C 166 
AA2 8  THR C 236 ? ILE C 239 ? THR C 236 ILE C 239 
AA2 9  GLU C 202 ? GLU C 207 ? GLU C 202 GLU C 207 
AA2 10 ARG C 217 ? PRO C 222 ? ARG C 217 PRO C 222 
AA3 1  VAL C 51  ? ASN C 53  ? VAL C 51  ASN C 53  
AA3 2  ILE C 30  ? LEU C 34  ? ILE C 30  LEU C 34  
AA3 3  LYS C 87  ? LEU C 92  ? LYS C 87  LEU C 92  
AA3 4  SER C 3   ? GLY C 8   ? SER C 3   GLY C 8   
AA3 5  SER C 116 ? MET C 119 ? SER C 116 MET C 119 
# 
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 ILE A 52  ? O ILE A 52  N VAL A 31  ? N VAL A 31  
AA1 2 3  N PHE A 32  ? N PHE A 32  O ALA A 91  ? O ALA A 91  
AA1 3 4  O CYS A 90  ? O CYS A 90  N VAL A 7   ? N VAL A 7   
AA1 4 5  N LEU A 4   ? N LEU A 4   O SER A 116 ? O SER A 116 
AA2 1 2  O LEU A 221 ? O LEU A 221 N VAL A 203 ? N VAL A 203 
AA2 2 3  N VAL A 204 ? N VAL A 204 O LEU A 238 ? O LEU A 238 
AA2 3 4  O ILE A 239 ? O ILE A 239 N LEU A 163 ? N LEU A 163 
AA2 4 5  O TRP A 166 ? O TRP A 166 N PHE A 145 ? N PHE A 145 
AA2 5 6  N HIS A 142 ? N HIS A 142 O SER C 144 ? O SER C 144 
AA2 6 7  N GLN C 143 ? N GLN C 143 O LEU C 164 ? O LEU C 164 
AA2 7 8  N LEU C 163 ? N LEU C 163 O ILE C 239 ? O ILE C 239 
AA2 8 9  O LEU C 238 ? O LEU C 238 N VAL C 204 ? N VAL C 204 
AA2 9 10 N VAL C 203 ? N VAL C 203 O LEU C 221 ? O LEU C 221 
AA3 1 2  O ILE C 52  ? O ILE C 52  N VAL C 31  ? N VAL C 31  
AA3 2 3  N PHE C 32  ? N PHE C 32  O ALA C 91  ? O ALA C 91  
AA3 3 4  O CYS C 90  ? O CYS C 90  N VAL C 7   ? N VAL C 7   
AA3 4 5  N LEU C 4   ? N LEU C 4   O SER C 116 ? O SER C 116 
# 
_pdbx_entry_details.entry_id                   9CH5 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH1 A ARG 67  ? ? O A HOH 401 ? ? 2.10 
2 1 O   A HOH 465 ? ? O A HOH 564 ? ? 2.11 
3 1 OH  C TYR 71  ? ? O D VAL 64  ? ? 2.12 
4 1 O   C GLY 85  ? ? O C HOH 401 ? ? 2.15 
5 1 OE2 C GLU 72  ? ? O C HOH 402 ? ? 2.19 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CE 
_pdbx_validate_rmsd_bond.auth_asym_id_1            C 
_pdbx_validate_rmsd_bond.auth_comp_id_1            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             243 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            NZ 
_pdbx_validate_rmsd_bond.auth_asym_id_2            C 
_pdbx_validate_rmsd_bond.auth_comp_id_2            LYS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             243 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.851 
_pdbx_validate_rmsd_bond.bond_target_value         1.486 
_pdbx_validate_rmsd_bond.bond_deviation            0.365 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.025 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB C LYS 243 ? ? CG C LYS 243 ? ? CD C LYS 243 ? ? 145.93 111.60 34.33  2.60 N 
2 1 CD C LYS 243 ? ? CE C LYS 243 ? ? NZ C LYS 243 ? ? 83.84  111.70 -27.86 2.30 N 
3 1 CA C LYS 243 ? ? C  C LYS 243 ? ? N  C LYS 244 ? ? 102.40 117.20 -14.80 2.20 Y 
4 1 CA C GLU 260 ? ? CB C GLU 260 ? ? CG C GLU 260 ? ? 131.05 113.40 17.65  2.20 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 ALA A 14 ? ? 75.01 -41.14 
2 1 ALA C 14 ? ? 74.79 -41.08 
3 1 ASP D 63 ? ? 73.97 -52.60 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    GLN 
_pdbx_validate_planes.auth_asym_id    D 
_pdbx_validate_planes.auth_seq_id     16 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.096 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             LYS 
_pdbx_validate_main_chain_plane.auth_asym_id             C 
_pdbx_validate_main_chain_plane.auth_seq_id              243 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   12.46 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 603 ? 6.02  . 
2  1 O ? A HOH 604 ? 6.13  . 
3  1 O ? A HOH 605 ? 6.98  . 
4  1 O ? A HOH 606 ? 8.57  . 
5  1 O ? A HOH 607 ? 10.42 . 
6  1 O ? C HOH 592 ? 5.85  . 
7  1 O ? C HOH 593 ? 6.09  . 
8  1 O ? C HOH 594 ? 6.58  . 
9  1 O ? C HOH 595 ? 7.09  . 
10 1 O ? C HOH 596 ? 7.39  . 
11 1 O ? C HOH 597 ? 9.08  . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1  ? A MET 1  
2  1 Y 1 B MET -6 ? B MET 1  
3  1 Y 1 B HIS -5 ? B HIS 2  
4  1 Y 1 B HIS -4 ? B HIS 3  
5  1 Y 1 B HIS -3 ? B HIS 4  
6  1 Y 1 B HIS -2 ? B HIS 5  
7  1 Y 1 B HIS -1 ? B HIS 6  
8  1 Y 1 B HIS 0  ? B HIS 7  
9  1 Y 1 B MET 1  ? B MET 8  
10 1 Y 1 B SER 2  ? B SER 9  
11 1 Y 1 B SER 54 ? B SER 61 
12 1 Y 1 B GLY 55 ? B GLY 62 
13 1 Y 1 B ASP 56 ? B ASP 63 
14 1 Y 1 B SER 57 ? B SER 64 
15 1 Y 1 B SER 58 ? B SER 65 
16 1 Y 1 B TYR 59 ? B TYR 66 
17 1 Y 1 B GLN 60 ? B GLN 67 
18 1 Y 1 B SER 61 ? B SER 68 
19 1 Y 1 B TYR 62 ? B TYR 69 
20 1 Y 1 B ASP 63 ? B ASP 70 
21 1 Y 1 B VAL 64 ? B VAL 71 
22 1 Y 1 B ILE 65 ? B ILE 72 
23 1 Y 1 B SER 66 ? B SER 73 
24 1 Y 1 B HIS 67 ? B HIS 74 
25 1 Y 1 B GLY 68 ? B GLY 75 
26 1 Y 1 B ASN 69 ? B ASN 76 
27 1 Y 1 B GLY 70 ? B GLY 77 
28 1 Y 1 B ASP 71 ? B ASP 78 
29 1 Y 1 C MET 1  ? C MET 1  
30 1 Y 1 D MET -6 ? D MET 1  
31 1 Y 1 D HIS -5 ? D HIS 2  
32 1 Y 1 D HIS -4 ? D HIS 3  
33 1 Y 1 D HIS -3 ? D HIS 4  
34 1 Y 1 D HIS -2 ? D HIS 5  
35 1 Y 1 D HIS -1 ? D HIS 6  
36 1 Y 1 D HIS 0  ? D HIS 7  
37 1 Y 1 D MET 1  ? D MET 8  
38 1 Y 1 D SER 2  ? D SER 9  
39 1 Y 1 D GLY 3  ? D GLY 10 
40 1 Y 1 D GLY 55 ? D GLY 62 
41 1 Y 1 D ASP 56 ? D ASP 63 
42 1 Y 1 D SER 57 ? D SER 64 
43 1 Y 1 D SER 58 ? D SER 65 
44 1 Y 1 D TYR 59 ? D TYR 66 
45 1 Y 1 D GLN 60 ? D GLN 67 
46 1 Y 1 D SER 61 ? D SER 68 
47 1 Y 1 D SER 66 ? D SER 73 
48 1 Y 1 D HIS 67 ? D HIS 74 
49 1 Y 1 D GLY 68 ? D GLY 75 
50 1 Y 1 D ASN 69 ? D ASN 76 
51 1 Y 1 D GLY 70 ? D GLY 77 
52 1 Y 1 D ASP 71 ? D ASP 78 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N      N N N 1   
ALA CA     C N S 2   
ALA C      C N N 3   
ALA O      O N N 4   
ALA CB     C N N 5   
ALA OXT    O N N 6   
ALA H      H N N 7   
ALA H2     H N N 8   
ALA HA     H N N 9   
ALA HB1    H N N 10  
ALA HB2    H N N 11  
ALA HB3    H N N 12  
ALA HXT    H N N 13  
ARG N      N N N 14  
ARG CA     C N S 15  
ARG C      C N N 16  
ARG O      O N N 17  
ARG CB     C N N 18  
ARG CG     C N N 19  
ARG CD     C N N 20  
ARG NE     N N N 21  
ARG CZ     C N N 22  
ARG NH1    N N N 23  
ARG NH2    N N N 24  
ARG OXT    O N N 25  
ARG H      H N N 26  
ARG H2     H N N 27  
ARG HA     H N N 28  
ARG HB2    H N N 29  
ARG HB3    H N N 30  
ARG HG2    H N N 31  
ARG HG3    H N N 32  
ARG HD2    H N N 33  
ARG HD3    H N N 34  
ARG HE     H N N 35  
ARG HH11   H N N 36  
ARG HH12   H N N 37  
ARG HH21   H N N 38  
ARG HH22   H N N 39  
ARG HXT    H N N 40  
ASN N      N N N 41  
ASN CA     C N S 42  
ASN C      C N N 43  
ASN O      O N N 44  
ASN CB     C N N 45  
ASN CG     C N N 46  
ASN OD1    O N N 47  
ASN ND2    N N N 48  
ASN OXT    O N N 49  
ASN H      H N N 50  
ASN H2     H N N 51  
ASN HA     H N N 52  
ASN HB2    H N N 53  
ASN HB3    H N N 54  
ASN HD21   H N N 55  
ASN HD22   H N N 56  
ASN HXT    H N N 57  
ASP N      N N N 58  
ASP CA     C N S 59  
ASP C      C N N 60  
ASP O      O N N 61  
ASP CB     C N N 62  
ASP CG     C N N 63  
ASP OD1    O N N 64  
ASP OD2    O N N 65  
ASP OXT    O N N 66  
ASP H      H N N 67  
ASP H2     H N N 68  
ASP HA     H N N 69  
ASP HB2    H N N 70  
ASP HB3    H N N 71  
ASP HD2    H N N 72  
ASP HXT    H N N 73  
CYS N      N N N 74  
CYS CA     C N R 75  
CYS C      C N N 76  
CYS O      O N N 77  
CYS CB     C N N 78  
CYS SG     S N N 79  
CYS OXT    O N N 80  
CYS H      H N N 81  
CYS H2     H N N 82  
CYS HA     H N N 83  
CYS HB2    H N N 84  
CYS HB3    H N N 85  
CYS HG     H N N 86  
CYS HXT    H N N 87  
GLN N      N N N 88  
GLN CA     C N S 89  
GLN C      C N N 90  
GLN O      O N N 91  
GLN CB     C N N 92  
GLN CG     C N N 93  
GLN CD     C N N 94  
GLN OE1    O N N 95  
GLN NE2    N N N 96  
GLN OXT    O N N 97  
GLN H      H N N 98  
GLN H2     H N N 99  
GLN HA     H N N 100 
GLN HB2    H N N 101 
GLN HB3    H N N 102 
GLN HG2    H N N 103 
GLN HG3    H N N 104 
GLN HE21   H N N 105 
GLN HE22   H N N 106 
GLN HXT    H N N 107 
GLU N      N N N 108 
GLU CA     C N S 109 
GLU C      C N N 110 
GLU O      O N N 111 
GLU CB     C N N 112 
GLU CG     C N N 113 
GLU CD     C N N 114 
GLU OE1    O N N 115 
GLU OE2    O N N 116 
GLU OXT    O N N 117 
GLU H      H N N 118 
GLU H2     H N N 119 
GLU HA     H N N 120 
GLU HB2    H N N 121 
GLU HB3    H N N 122 
GLU HG2    H N N 123 
GLU HG3    H N N 124 
GLU HE2    H N N 125 
GLU HXT    H N N 126 
GLY N      N N N 127 
GLY CA     C N N 128 
GLY C      C N N 129 
GLY O      O N N 130 
GLY OXT    O N N 131 
GLY H      H N N 132 
GLY H2     H N N 133 
GLY HA2    H N N 134 
GLY HA3    H N N 135 
GLY HXT    H N N 136 
HIS N      N N N 137 
HIS CA     C N S 138 
HIS C      C N N 139 
HIS O      O N N 140 
HIS CB     C N N 141 
HIS CG     C Y N 142 
HIS ND1    N Y N 143 
HIS CD2    C Y N 144 
HIS CE1    C Y N 145 
HIS NE2    N Y N 146 
HIS OXT    O N N 147 
HIS H      H N N 148 
HIS H2     H N N 149 
HIS HA     H N N 150 
HIS HB2    H N N 151 
HIS HB3    H N N 152 
HIS HD1    H N N 153 
HIS HD2    H N N 154 
HIS HE1    H N N 155 
HIS HE2    H N N 156 
HIS HXT    H N N 157 
HOH O      O N N 158 
HOH H1     H N N 159 
HOH H2     H N N 160 
ILE N      N N N 161 
ILE CA     C N S 162 
ILE C      C N N 163 
ILE O      O N N 164 
ILE CB     C N S 165 
ILE CG1    C N N 166 
ILE CG2    C N N 167 
ILE CD1    C N N 168 
ILE OXT    O N N 169 
ILE H      H N N 170 
ILE H2     H N N 171 
ILE HA     H N N 172 
ILE HB     H N N 173 
ILE HG12   H N N 174 
ILE HG13   H N N 175 
ILE HG21   H N N 176 
ILE HG22   H N N 177 
ILE HG23   H N N 178 
ILE HD11   H N N 179 
ILE HD12   H N N 180 
ILE HD13   H N N 181 
ILE HXT    H N N 182 
LEU N      N N N 183 
LEU CA     C N S 184 
LEU C      C N N 185 
LEU O      O N N 186 
LEU CB     C N N 187 
LEU CG     C N N 188 
LEU CD1    C N N 189 
LEU CD2    C N N 190 
LEU OXT    O N N 191 
LEU H      H N N 192 
LEU H2     H N N 193 
LEU HA     H N N 194 
LEU HB2    H N N 195 
LEU HB3    H N N 196 
LEU HG     H N N 197 
LEU HD11   H N N 198 
LEU HD12   H N N 199 
LEU HD13   H N N 200 
LEU HD21   H N N 201 
LEU HD22   H N N 202 
LEU HD23   H N N 203 
LEU HXT    H N N 204 
LYS N      N N N 205 
LYS CA     C N S 206 
LYS C      C N N 207 
LYS O      O N N 208 
LYS CB     C N N 209 
LYS CG     C N N 210 
LYS CD     C N N 211 
LYS CE     C N N 212 
LYS NZ     N N N 213 
LYS OXT    O N N 214 
LYS H      H N N 215 
LYS H2     H N N 216 
LYS HA     H N N 217 
LYS HB2    H N N 218 
LYS HB3    H N N 219 
LYS HG2    H N N 220 
LYS HG3    H N N 221 
LYS HD2    H N N 222 
LYS HD3    H N N 223 
LYS HE2    H N N 224 
LYS HE3    H N N 225 
LYS HZ1    H N N 226 
LYS HZ2    H N N 227 
LYS HZ3    H N N 228 
LYS HXT    H N N 229 
MET N      N N N 230 
MET CA     C N S 231 
MET C      C N N 232 
MET O      O N N 233 
MET CB     C N N 234 
MET CG     C N N 235 
MET SD     S N N 236 
MET CE     C N N 237 
MET OXT    O N N 238 
MET H      H N N 239 
MET H2     H N N 240 
MET HA     H N N 241 
MET HB2    H N N 242 
MET HB3    H N N 243 
MET HG2    H N N 244 
MET HG3    H N N 245 
MET HE1    H N N 246 
MET HE2    H N N 247 
MET HE3    H N N 248 
MET HXT    H N N 249 
PHE N      N N N 250 
PHE CA     C N S 251 
PHE C      C N N 252 
PHE O      O N N 253 
PHE CB     C N N 254 
PHE CG     C Y N 255 
PHE CD1    C Y N 256 
PHE CD2    C Y N 257 
PHE CE1    C Y N 258 
PHE CE2    C Y N 259 
PHE CZ     C Y N 260 
PHE OXT    O N N 261 
PHE H      H N N 262 
PHE H2     H N N 263 
PHE HA     H N N 264 
PHE HB2    H N N 265 
PHE HB3    H N N 266 
PHE HD1    H N N 267 
PHE HD2    H N N 268 
PHE HE1    H N N 269 
PHE HE2    H N N 270 
PHE HZ     H N N 271 
PHE HXT    H N N 272 
PRO N      N N N 273 
PRO CA     C N S 274 
PRO C      C N N 275 
PRO O      O N N 276 
PRO CB     C N N 277 
PRO CG     C N N 278 
PRO CD     C N N 279 
PRO OXT    O N N 280 
PRO H      H N N 281 
PRO HA     H N N 282 
PRO HB2    H N N 283 
PRO HB3    H N N 284 
PRO HG2    H N N 285 
PRO HG3    H N N 286 
PRO HD2    H N N 287 
PRO HD3    H N N 288 
PRO HXT    H N N 289 
SAH N      N N N 290 
SAH CA     C N S 291 
SAH CB     C N N 292 
SAH CG     C N N 293 
SAH SD     S N N 294 
SAH C      C N N 295 
SAH O      O N N 296 
SAH OXT    O N N 297 
SAH "C5'"  C N N 298 
SAH "C4'"  C N S 299 
SAH "O4'"  O N N 300 
SAH "C3'"  C N S 301 
SAH "O3'"  O N N 302 
SAH "C2'"  C N R 303 
SAH "O2'"  O N N 304 
SAH "C1'"  C N R 305 
SAH N9     N Y N 306 
SAH C8     C Y N 307 
SAH N7     N Y N 308 
SAH C5     C Y N 309 
SAH C6     C Y N 310 
SAH N6     N N N 311 
SAH N1     N Y N 312 
SAH C2     C Y N 313 
SAH N3     N Y N 314 
SAH C4     C Y N 315 
SAH HN1    H N N 316 
SAH HN2    H N N 317 
SAH HA     H N N 318 
SAH HB1    H N N 319 
SAH HB2    H N N 320 
SAH HG1    H N N 321 
SAH HG2    H N N 322 
SAH HXT    H N N 323 
SAH "H5'1" H N N 324 
SAH "H5'2" H N N 325 
SAH "H4'"  H N N 326 
SAH "H3'"  H N N 327 
SAH "HO3'" H N N 328 
SAH "H2'"  H N N 329 
SAH "HO2'" H N N 330 
SAH "H1'"  H N N 331 
SAH H8     H N N 332 
SAH HN61   H N N 333 
SAH HN62   H N N 334 
SAH H2     H N N 335 
SER N      N N N 336 
SER CA     C N S 337 
SER C      C N N 338 
SER O      O N N 339 
SER CB     C N N 340 
SER OG     O N N 341 
SER OXT    O N N 342 
SER H      H N N 343 
SER H2     H N N 344 
SER HA     H N N 345 
SER HB2    H N N 346 
SER HB3    H N N 347 
SER HG     H N N 348 
SER HXT    H N N 349 
THR N      N N N 350 
THR CA     C N S 351 
THR C      C N N 352 
THR O      O N N 353 
THR CB     C N R 354 
THR OG1    O N N 355 
THR CG2    C N N 356 
THR OXT    O N N 357 
THR H      H N N 358 
THR H2     H N N 359 
THR HA     H N N 360 
THR HB     H N N 361 
THR HG1    H N N 362 
THR HG21   H N N 363 
THR HG22   H N N 364 
THR HG23   H N N 365 
THR HXT    H N N 366 
TRP N      N N N 367 
TRP CA     C N S 368 
TRP C      C N N 369 
TRP O      O N N 370 
TRP CB     C N N 371 
TRP CG     C Y N 372 
TRP CD1    C Y N 373 
TRP CD2    C Y N 374 
TRP NE1    N Y N 375 
TRP CE2    C Y N 376 
TRP CE3    C Y N 377 
TRP CZ2    C Y N 378 
TRP CZ3    C Y N 379 
TRP CH2    C Y N 380 
TRP OXT    O N N 381 
TRP H      H N N 382 
TRP H2     H N N 383 
TRP HA     H N N 384 
TRP HB2    H N N 385 
TRP HB3    H N N 386 
TRP HD1    H N N 387 
TRP HE1    H N N 388 
TRP HE3    H N N 389 
TRP HZ2    H N N 390 
TRP HZ3    H N N 391 
TRP HH2    H N N 392 
TRP HXT    H N N 393 
TYR N      N N N 394 
TYR CA     C N S 395 
TYR C      C N N 396 
TYR O      O N N 397 
TYR CB     C N N 398 
TYR CG     C Y N 399 
TYR CD1    C Y N 400 
TYR CD2    C Y N 401 
TYR CE1    C Y N 402 
TYR CE2    C Y N 403 
TYR CZ     C Y N 404 
TYR OH     O N N 405 
TYR OXT    O N N 406 
TYR H      H N N 407 
TYR H2     H N N 408 
TYR HA     H N N 409 
TYR HB2    H N N 410 
TYR HB3    H N N 411 
TYR HD1    H N N 412 
TYR HD2    H N N 413 
TYR HE1    H N N 414 
TYR HE2    H N N 415 
TYR HH     H N N 416 
TYR HXT    H N N 417 
VAL N      N N N 418 
VAL CA     C N S 419 
VAL C      C N N 420 
VAL O      O N N 421 
VAL CB     C N N 422 
VAL CG1    C N N 423 
VAL CG2    C N N 424 
VAL OXT    O N N 425 
VAL H      H N N 426 
VAL H2     H N N 427 
VAL HA     H N N 428 
VAL HB     H N N 429 
VAL HG11   H N N 430 
VAL HG12   H N N 431 
VAL HG13   H N N 432 
VAL HG21   H N N 433 
VAL HG22   H N N 434 
VAL HG23   H N N 435 
VAL HXT    H N N 436 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ARG N     CA     sing N N 13  
ARG N     H      sing N N 14  
ARG N     H2     sing N N 15  
ARG CA    C      sing N N 16  
ARG CA    CB     sing N N 17  
ARG CA    HA     sing N N 18  
ARG C     O      doub N N 19  
ARG C     OXT    sing N N 20  
ARG CB    CG     sing N N 21  
ARG CB    HB2    sing N N 22  
ARG CB    HB3    sing N N 23  
ARG CG    CD     sing N N 24  
ARG CG    HG2    sing N N 25  
ARG CG    HG3    sing N N 26  
ARG CD    NE     sing N N 27  
ARG CD    HD2    sing N N 28  
ARG CD    HD3    sing N N 29  
ARG NE    CZ     sing N N 30  
ARG NE    HE     sing N N 31  
ARG CZ    NH1    sing N N 32  
ARG CZ    NH2    doub N N 33  
ARG NH1   HH11   sing N N 34  
ARG NH1   HH12   sing N N 35  
ARG NH2   HH21   sing N N 36  
ARG NH2   HH22   sing N N 37  
ARG OXT   HXT    sing N N 38  
ASN N     CA     sing N N 39  
ASN N     H      sing N N 40  
ASN N     H2     sing N N 41  
ASN CA    C      sing N N 42  
ASN CA    CB     sing N N 43  
ASN CA    HA     sing N N 44  
ASN C     O      doub N N 45  
ASN C     OXT    sing N N 46  
ASN CB    CG     sing N N 47  
ASN CB    HB2    sing N N 48  
ASN CB    HB3    sing N N 49  
ASN CG    OD1    doub N N 50  
ASN CG    ND2    sing N N 51  
ASN ND2   HD21   sing N N 52  
ASN ND2   HD22   sing N N 53  
ASN OXT   HXT    sing N N 54  
ASP N     CA     sing N N 55  
ASP N     H      sing N N 56  
ASP N     H2     sing N N 57  
ASP CA    C      sing N N 58  
ASP CA    CB     sing N N 59  
ASP CA    HA     sing N N 60  
ASP C     O      doub N N 61  
ASP C     OXT    sing N N 62  
ASP CB    CG     sing N N 63  
ASP CB    HB2    sing N N 64  
ASP CB    HB3    sing N N 65  
ASP CG    OD1    doub N N 66  
ASP CG    OD2    sing N N 67  
ASP OD2   HD2    sing N N 68  
ASP OXT   HXT    sing N N 69  
CYS N     CA     sing N N 70  
CYS N     H      sing N N 71  
CYS N     H2     sing N N 72  
CYS CA    C      sing N N 73  
CYS CA    CB     sing N N 74  
CYS CA    HA     sing N N 75  
CYS C     O      doub N N 76  
CYS C     OXT    sing N N 77  
CYS CB    SG     sing N N 78  
CYS CB    HB2    sing N N 79  
CYS CB    HB3    sing N N 80  
CYS SG    HG     sing N N 81  
CYS OXT   HXT    sing N N 82  
GLN N     CA     sing N N 83  
GLN N     H      sing N N 84  
GLN N     H2     sing N N 85  
GLN CA    C      sing N N 86  
GLN CA    CB     sing N N 87  
GLN CA    HA     sing N N 88  
GLN C     O      doub N N 89  
GLN C     OXT    sing N N 90  
GLN CB    CG     sing N N 91  
GLN CB    HB2    sing N N 92  
GLN CB    HB3    sing N N 93  
GLN CG    CD     sing N N 94  
GLN CG    HG2    sing N N 95  
GLN CG    HG3    sing N N 96  
GLN CD    OE1    doub N N 97  
GLN CD    NE2    sing N N 98  
GLN NE2   HE21   sing N N 99  
GLN NE2   HE22   sing N N 100 
GLN OXT   HXT    sing N N 101 
GLU N     CA     sing N N 102 
GLU N     H      sing N N 103 
GLU N     H2     sing N N 104 
GLU CA    C      sing N N 105 
GLU CA    CB     sing N N 106 
GLU CA    HA     sing N N 107 
GLU C     O      doub N N 108 
GLU C     OXT    sing N N 109 
GLU CB    CG     sing N N 110 
GLU CB    HB2    sing N N 111 
GLU CB    HB3    sing N N 112 
GLU CG    CD     sing N N 113 
GLU CG    HG2    sing N N 114 
GLU CG    HG3    sing N N 115 
GLU CD    OE1    doub N N 116 
GLU CD    OE2    sing N N 117 
GLU OE2   HE2    sing N N 118 
GLU OXT   HXT    sing N N 119 
GLY N     CA     sing N N 120 
GLY N     H      sing N N 121 
GLY N     H2     sing N N 122 
GLY CA    C      sing N N 123 
GLY CA    HA2    sing N N 124 
GLY CA    HA3    sing N N 125 
GLY C     O      doub N N 126 
GLY C     OXT    sing N N 127 
GLY OXT   HXT    sing N N 128 
HIS N     CA     sing N N 129 
HIS N     H      sing N N 130 
HIS N     H2     sing N N 131 
HIS CA    C      sing N N 132 
HIS CA    CB     sing N N 133 
HIS CA    HA     sing N N 134 
HIS C     O      doub N N 135 
HIS C     OXT    sing N N 136 
HIS CB    CG     sing N N 137 
HIS CB    HB2    sing N N 138 
HIS CB    HB3    sing N N 139 
HIS CG    ND1    sing Y N 140 
HIS CG    CD2    doub Y N 141 
HIS ND1   CE1    doub Y N 142 
HIS ND1   HD1    sing N N 143 
HIS CD2   NE2    sing Y N 144 
HIS CD2   HD2    sing N N 145 
HIS CE1   NE2    sing Y N 146 
HIS CE1   HE1    sing N N 147 
HIS NE2   HE2    sing N N 148 
HIS OXT   HXT    sing N N 149 
HOH O     H1     sing N N 150 
HOH O     H2     sing N N 151 
ILE N     CA     sing N N 152 
ILE N     H      sing N N 153 
ILE N     H2     sing N N 154 
ILE CA    C      sing N N 155 
ILE CA    CB     sing N N 156 
ILE CA    HA     sing N N 157 
ILE C     O      doub N N 158 
ILE C     OXT    sing N N 159 
ILE CB    CG1    sing N N 160 
ILE CB    CG2    sing N N 161 
ILE CB    HB     sing N N 162 
ILE CG1   CD1    sing N N 163 
ILE CG1   HG12   sing N N 164 
ILE CG1   HG13   sing N N 165 
ILE CG2   HG21   sing N N 166 
ILE CG2   HG22   sing N N 167 
ILE CG2   HG23   sing N N 168 
ILE CD1   HD11   sing N N 169 
ILE CD1   HD12   sing N N 170 
ILE CD1   HD13   sing N N 171 
ILE OXT   HXT    sing N N 172 
LEU N     CA     sing N N 173 
LEU N     H      sing N N 174 
LEU N     H2     sing N N 175 
LEU CA    C      sing N N 176 
LEU CA    CB     sing N N 177 
LEU CA    HA     sing N N 178 
LEU C     O      doub N N 179 
LEU C     OXT    sing N N 180 
LEU CB    CG     sing N N 181 
LEU CB    HB2    sing N N 182 
LEU CB    HB3    sing N N 183 
LEU CG    CD1    sing N N 184 
LEU CG    CD2    sing N N 185 
LEU CG    HG     sing N N 186 
LEU CD1   HD11   sing N N 187 
LEU CD1   HD12   sing N N 188 
LEU CD1   HD13   sing N N 189 
LEU CD2   HD21   sing N N 190 
LEU CD2   HD22   sing N N 191 
LEU CD2   HD23   sing N N 192 
LEU OXT   HXT    sing N N 193 
LYS N     CA     sing N N 194 
LYS N     H      sing N N 195 
LYS N     H2     sing N N 196 
LYS CA    C      sing N N 197 
LYS CA    CB     sing N N 198 
LYS CA    HA     sing N N 199 
LYS C     O      doub N N 200 
LYS C     OXT    sing N N 201 
LYS CB    CG     sing N N 202 
LYS CB    HB2    sing N N 203 
LYS CB    HB3    sing N N 204 
LYS CG    CD     sing N N 205 
LYS CG    HG2    sing N N 206 
LYS CG    HG3    sing N N 207 
LYS CD    CE     sing N N 208 
LYS CD    HD2    sing N N 209 
LYS CD    HD3    sing N N 210 
LYS CE    NZ     sing N N 211 
LYS CE    HE2    sing N N 212 
LYS CE    HE3    sing N N 213 
LYS NZ    HZ1    sing N N 214 
LYS NZ    HZ2    sing N N 215 
LYS NZ    HZ3    sing N N 216 
LYS OXT   HXT    sing N N 217 
MET N     CA     sing N N 218 
MET N     H      sing N N 219 
MET N     H2     sing N N 220 
MET CA    C      sing N N 221 
MET CA    CB     sing N N 222 
MET CA    HA     sing N N 223 
MET C     O      doub N N 224 
MET C     OXT    sing N N 225 
MET CB    CG     sing N N 226 
MET CB    HB2    sing N N 227 
MET CB    HB3    sing N N 228 
MET CG    SD     sing N N 229 
MET CG    HG2    sing N N 230 
MET CG    HG3    sing N N 231 
MET SD    CE     sing N N 232 
MET CE    HE1    sing N N 233 
MET CE    HE2    sing N N 234 
MET CE    HE3    sing N N 235 
MET OXT   HXT    sing N N 236 
PHE N     CA     sing N N 237 
PHE N     H      sing N N 238 
PHE N     H2     sing N N 239 
PHE CA    C      sing N N 240 
PHE CA    CB     sing N N 241 
PHE CA    HA     sing N N 242 
PHE C     O      doub N N 243 
PHE C     OXT    sing N N 244 
PHE CB    CG     sing N N 245 
PHE CB    HB2    sing N N 246 
PHE CB    HB3    sing N N 247 
PHE CG    CD1    doub Y N 248 
PHE CG    CD2    sing Y N 249 
PHE CD1   CE1    sing Y N 250 
PHE CD1   HD1    sing N N 251 
PHE CD2   CE2    doub Y N 252 
PHE CD2   HD2    sing N N 253 
PHE CE1   CZ     doub Y N 254 
PHE CE1   HE1    sing N N 255 
PHE CE2   CZ     sing Y N 256 
PHE CE2   HE2    sing N N 257 
PHE CZ    HZ     sing N N 258 
PHE OXT   HXT    sing N N 259 
PRO N     CA     sing N N 260 
PRO N     CD     sing N N 261 
PRO N     H      sing N N 262 
PRO CA    C      sing N N 263 
PRO CA    CB     sing N N 264 
PRO CA    HA     sing N N 265 
PRO C     O      doub N N 266 
PRO C     OXT    sing N N 267 
PRO CB    CG     sing N N 268 
PRO CB    HB2    sing N N 269 
PRO CB    HB3    sing N N 270 
PRO CG    CD     sing N N 271 
PRO CG    HG2    sing N N 272 
PRO CG    HG3    sing N N 273 
PRO CD    HD2    sing N N 274 
PRO CD    HD3    sing N N 275 
PRO OXT   HXT    sing N N 276 
SAH N     CA     sing N N 277 
SAH N     HN1    sing N N 278 
SAH N     HN2    sing N N 279 
SAH CA    CB     sing N N 280 
SAH CA    C      sing N N 281 
SAH CA    HA     sing N N 282 
SAH CB    CG     sing N N 283 
SAH CB    HB1    sing N N 284 
SAH CB    HB2    sing N N 285 
SAH CG    SD     sing N N 286 
SAH CG    HG1    sing N N 287 
SAH CG    HG2    sing N N 288 
SAH SD    "C5'"  sing N N 289 
SAH C     O      doub N N 290 
SAH C     OXT    sing N N 291 
SAH OXT   HXT    sing N N 292 
SAH "C5'" "C4'"  sing N N 293 
SAH "C5'" "H5'1" sing N N 294 
SAH "C5'" "H5'2" sing N N 295 
SAH "C4'" "O4'"  sing N N 296 
SAH "C4'" "C3'"  sing N N 297 
SAH "C4'" "H4'"  sing N N 298 
SAH "O4'" "C1'"  sing N N 299 
SAH "C3'" "O3'"  sing N N 300 
SAH "C3'" "C2'"  sing N N 301 
SAH "C3'" "H3'"  sing N N 302 
SAH "O3'" "HO3'" sing N N 303 
SAH "C2'" "O2'"  sing N N 304 
SAH "C2'" "C1'"  sing N N 305 
SAH "C2'" "H2'"  sing N N 306 
SAH "O2'" "HO2'" sing N N 307 
SAH "C1'" N9     sing N N 308 
SAH "C1'" "H1'"  sing N N 309 
SAH N9    C8     sing Y N 310 
SAH N9    C4     sing Y N 311 
SAH C8    N7     doub Y N 312 
SAH C8    H8     sing N N 313 
SAH N7    C5     sing Y N 314 
SAH C5    C6     sing Y N 315 
SAH C5    C4     doub Y N 316 
SAH C6    N6     sing N N 317 
SAH C6    N1     doub Y N 318 
SAH N6    HN61   sing N N 319 
SAH N6    HN62   sing N N 320 
SAH N1    C2     sing Y N 321 
SAH C2    N3     doub Y N 322 
SAH C2    H2     sing N N 323 
SAH N3    C4     sing Y N 324 
SER N     CA     sing N N 325 
SER N     H      sing N N 326 
SER N     H2     sing N N 327 
SER CA    C      sing N N 328 
SER CA    CB     sing N N 329 
SER CA    HA     sing N N 330 
SER C     O      doub N N 331 
SER C     OXT    sing N N 332 
SER CB    OG     sing N N 333 
SER CB    HB2    sing N N 334 
SER CB    HB3    sing N N 335 
SER OG    HG     sing N N 336 
SER OXT   HXT    sing N N 337 
THR N     CA     sing N N 338 
THR N     H      sing N N 339 
THR N     H2     sing N N 340 
THR CA    C      sing N N 341 
THR CA    CB     sing N N 342 
THR CA    HA     sing N N 343 
THR C     O      doub N N 344 
THR C     OXT    sing N N 345 
THR CB    OG1    sing N N 346 
THR CB    CG2    sing N N 347 
THR CB    HB     sing N N 348 
THR OG1   HG1    sing N N 349 
THR CG2   HG21   sing N N 350 
THR CG2   HG22   sing N N 351 
THR CG2   HG23   sing N N 352 
THR OXT   HXT    sing N N 353 
TRP N     CA     sing N N 354 
TRP N     H      sing N N 355 
TRP N     H2     sing N N 356 
TRP CA    C      sing N N 357 
TRP CA    CB     sing N N 358 
TRP CA    HA     sing N N 359 
TRP C     O      doub N N 360 
TRP C     OXT    sing N N 361 
TRP CB    CG     sing N N 362 
TRP CB    HB2    sing N N 363 
TRP CB    HB3    sing N N 364 
TRP CG    CD1    doub Y N 365 
TRP CG    CD2    sing Y N 366 
TRP CD1   NE1    sing Y N 367 
TRP CD1   HD1    sing N N 368 
TRP CD2   CE2    doub Y N 369 
TRP CD2   CE3    sing Y N 370 
TRP NE1   CE2    sing Y N 371 
TRP NE1   HE1    sing N N 372 
TRP CE2   CZ2    sing Y N 373 
TRP CE3   CZ3    doub Y N 374 
TRP CE3   HE3    sing N N 375 
TRP CZ2   CH2    doub Y N 376 
TRP CZ2   HZ2    sing N N 377 
TRP CZ3   CH2    sing Y N 378 
TRP CZ3   HZ3    sing N N 379 
TRP CH2   HH2    sing N N 380 
TRP OXT   HXT    sing N N 381 
TYR N     CA     sing N N 382 
TYR N     H      sing N N 383 
TYR N     H2     sing N N 384 
TYR CA    C      sing N N 385 
TYR CA    CB     sing N N 386 
TYR CA    HA     sing N N 387 
TYR C     O      doub N N 388 
TYR C     OXT    sing N N 389 
TYR CB    CG     sing N N 390 
TYR CB    HB2    sing N N 391 
TYR CB    HB3    sing N N 392 
TYR CG    CD1    doub Y N 393 
TYR CG    CD2    sing Y N 394 
TYR CD1   CE1    sing Y N 395 
TYR CD1   HD1    sing N N 396 
TYR CD2   CE2    doub Y N 397 
TYR CD2   HD2    sing N N 398 
TYR CE1   CZ     doub Y N 399 
TYR CE1   HE1    sing N N 400 
TYR CE2   CZ     sing Y N 401 
TYR CE2   HE2    sing N N 402 
TYR CZ    OH     sing N N 403 
TYR OH    HH     sing N N 404 
TYR OXT   HXT    sing N N 405 
VAL N     CA     sing N N 406 
VAL N     H      sing N N 407 
VAL N     H2     sing N N 408 
VAL CA    C      sing N N 409 
VAL CA    CB     sing N N 410 
VAL CA    HA     sing N N 411 
VAL C     O      doub N N 412 
VAL C     OXT    sing N N 413 
VAL CB    CG1    sing N N 414 
VAL CB    CG2    sing N N 415 
VAL CB    HB     sing N N 416 
VAL CG1   HG11   sing N N 417 
VAL CG1   HG12   sing N N 418 
VAL CG1   HG13   sing N N 419 
VAL CG2   HG21   sing N N 420 
VAL CG2   HG22   sing N N 421 
VAL CG2   HG23   sing N N 422 
VAL OXT   HXT    sing N N 423 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           R35GM133475 
_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   7LTE 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CH5 
_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]   0.019055 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001222 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009227 
_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]   0.016941 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLY A 1 2   ? 38.515  14.949  19.099 1.00 21.93 ?  2   GLY A N     1 
ATOM   2    C CA    . GLY A 1 2   ? 37.105  14.734  18.845 1.00 23.58 ?  2   GLY A CA    1 
ATOM   3    C C     . GLY A 1 2   ? 36.493  13.676  19.744 1.00 25.92 ?  2   GLY A C     1 
ATOM   4    O O     . GLY A 1 2   ? 37.205  12.975  20.465 1.00 27.00 ?  2   GLY A O     1 
ATOM   5    N N     . SER A 1 3   ? 35.168  13.555  19.696 1.00 21.55 ?  3   SER A N     1 
ATOM   6    C CA    . SER A 1 3   ? 34.451  12.615  20.545 1.00 23.84 ?  3   SER A CA    1 
ATOM   7    C C     . SER A 1 3   ? 33.217  12.125  19.803 1.00 22.12 ?  3   SER A C     1 
ATOM   8    O O     . SER A 1 3   ? 32.895  12.597  18.711 1.00 22.61 ?  3   SER A O     1 
ATOM   9    C CB    . SER A 1 3   ? 34.074  13.251  21.883 1.00 21.54 ?  3   SER A CB    1 
ATOM   10   O OG    . SER A 1 3   ? 33.325  14.439  21.689 1.00 23.57 ?  3   SER A OG    1 
ATOM   11   N N     . LEU A 1 4   ? 32.523  11.170  20.416 1.00 23.18 ?  4   LEU A N     1 
ATOM   12   C CA    . LEU A 1 4   ? 31.355  10.553  19.803 1.00 20.09 ?  4   LEU A CA    1 
ATOM   13   C C     . LEU A 1 4   ? 30.264  10.356  20.843 1.00 20.81 ?  4   LEU A C     1 
ATOM   14   O O     . LEU A 1 4   ? 30.511  9.788   21.910 1.00 20.45 ?  4   LEU A O     1 
ATOM   15   C CB    . LEU A 1 4   ? 31.716  9.209   19.160 1.00 20.30 ?  4   LEU A CB    1 
ATOM   16   C CG    . LEU A 1 4   ? 30.575  8.440   18.500 1.00 23.00 ?  4   LEU A CG    1 
ATOM   17   C CD1   . LEU A 1 4   ? 29.876  9.301   17.460 1.00 20.25 ?  4   LEU A CD1   1 
ATOM   18   C CD2   . LEU A 1 4   ? 31.092  7.154   17.875 1.00 18.79 ?  4   LEU A CD2   1 
ATOM   19   N N     . VAL A 1 5   ? 29.061  10.830  20.530 1.00 21.43 ?  5   VAL A N     1 
ATOM   20   C CA    . VAL A 1 5   ? 27.859  10.516  21.293 1.00 17.37 ?  5   VAL A CA    1 
ATOM   21   C C     . VAL A 1 5   ? 26.819  9.985   20.321 1.00 17.02 ?  5   VAL A C     1 
ATOM   22   O O     . VAL A 1 5   ? 26.497  10.647  19.329 1.00 18.00 ?  5   VAL A O     1 
ATOM   23   C CB    . VAL A 1 5   ? 27.300  11.746  22.034 1.00 17.50 ?  5   VAL A CB    1 
ATOM   24   C CG1   . VAL A 1 5   ? 26.113  11.347  22.909 1.00 20.35 ?  5   VAL A CG1   1 
ATOM   25   C CG2   . VAL A 1 5   ? 28.385  12.436  22.837 1.00 22.94 ?  5   VAL A CG2   1 
ATOM   26   N N     . CYS A 1 6   ? 26.287  8.804   20.604 1.00 18.24 ?  6   CYS A N     1 
ATOM   27   C CA    . CYS A 1 6   ? 25.194  8.242   19.824 1.00 15.40 ?  6   CYS A CA    1 
ATOM   28   C C     . CYS A 1 6   ? 23.911  8.389   20.630 1.00 13.47 ?  6   CYS A C     1 
ATOM   29   O O     . CYS A 1 6   ? 23.837  7.937   21.778 1.00 14.10 ?  6   CYS A O     1 
ATOM   30   C CB    . CYS A 1 6   ? 25.463  6.777   19.478 1.00 17.87 ?  6   CYS A CB    1 
ATOM   31   S SG    . CYS A 1 6   ? 27.005  6.510   18.564 1.00 21.09 ?  6   CYS A SG    1 
ATOM   32   N N     . VAL A 1 7   ? 22.909  9.028   20.035 1.00 16.73 ?  7   VAL A N     1 
ATOM   33   C CA    . VAL A 1 7   ? 21.621  9.233   20.680 1.00 19.35 ?  7   VAL A CA    1 
ATOM   34   C C     . VAL A 1 7   ? 20.535  8.608   19.813 1.00 19.82 ?  7   VAL A C     1 
ATOM   35   O O     . VAL A 1 7   ? 20.758  8.240   18.661 1.00 15.44 ?  7   VAL A O     1 
ATOM   36   C CB    . VAL A 1 7   ? 21.319  10.723  20.940 1.00 19.60 ?  7   VAL A CB    1 
ATOM   37   C CG1   . VAL A 1 7   ? 22.449  11.364  21.732 1.00 14.49 ?  7   VAL A CG1   1 
ATOM   38   C CG2   . VAL A 1 7   ? 21.092  11.458  19.628 1.00 18.84 ?  7   VAL A CG2   1 
ATOM   39   N N     . GLY A 1 8   ? 19.347  8.491   20.393 1.00 17.84 ?  8   GLY A N     1 
ATOM   40   C CA    . GLY A 1 8   ? 18.168  8.146   19.631 1.00 16.55 ?  8   GLY A CA    1 
ATOM   41   C C     . GLY A 1 8   ? 17.167  9.278   19.571 1.00 17.28 ?  8   GLY A C     1 
ATOM   42   O O     . GLY A 1 8   ? 17.145  10.140  20.451 1.00 14.98 ?  8   GLY A O     1 
ATOM   43   N N     . THR A 1 9   ? 16.322  9.283   18.545 1.00 17.45 ?  9   THR A N     1 
ATOM   44   C CA    . THR A 1 9   ? 15.302  10.308  18.389 1.00 19.78 ?  9   THR A CA    1 
ATOM   45   C C     . THR A 1 9   ? 13.904  9.772   18.652 1.00 19.99 ?  9   THR A C     1 
ATOM   46   O O     . THR A 1 9   ? 12.927  10.516  18.506 1.00 21.48 ?  9   THR A O     1 
ATOM   47   C CB    . THR A 1 9   ? 15.354  10.913  16.979 1.00 21.78 ?  9   THR A CB    1 
ATOM   48   O OG1   . THR A 1 9   ? 15.123  9.882   16.011 1.00 15.61 ?  9   THR A OG1   1 
ATOM   49   C CG2   . THR A 1 9   ? 16.707  11.548  16.720 1.00 19.56 ?  9   THR A CG2   1 
ATOM   50   N N     . GLY A 1 10  ? 13.784  8.511   19.045 1.00 17.77 ?  10  GLY A N     1 
ATOM   51   C CA    . GLY A 1 10  ? 12.486  7.913   19.215 1.00 14.11 ?  10  GLY A CA    1 
ATOM   52   C C     . GLY A 1 10  ? 11.865  7.599   17.869 1.00 18.23 ?  10  GLY A C     1 
ATOM   53   O O     . GLY A 1 10  ? 12.483  7.730   16.808 1.00 20.32 ?  10  GLY A O     1 
ATOM   54   N N     . LEU A 1 11  ? 10.611  7.167   17.923 1.00 14.22 ?  11  LEU A N     1 
ATOM   55   C CA    . LEU A 1 11  ? 9.867   6.820   16.719 1.00 13.61 ?  11  LEU A CA    1 
ATOM   56   C C     . LEU A 1 11  ? 9.006   7.972   16.226 1.00 15.93 ?  11  LEU A C     1 
ATOM   57   O O     . LEU A 1 11  ? 8.871   8.167   15.014 1.00 14.47 ?  11  LEU A O     1 
ATOM   58   C CB    . LEU A 1 11  ? 8.988   5.588   16.966 1.00 13.37 ?  11  LEU A CB    1 
ATOM   59   C CG    . LEU A 1 11  ? 9.650   4.200   16.893 1.00 18.43 ?  11  LEU A CG    1 
ATOM   60   C CD1   . LEU A 1 11  ? 9.996   3.853   15.456 1.00 23.61 ?  11  LEU A CD1   1 
ATOM   61   C CD2   . LEU A 1 11  ? 10.873  4.071   17.791 1.00 22.14 ?  11  LEU A CD2   1 
ATOM   62   N N     . GLN A 1 12  ? 8.439   8.748   17.145 1.00 14.04 ?  12  GLN A N     1 
ATOM   63   C CA    . GLN A 1 12  ? 7.570   9.857   16.793 1.00 20.52 ?  12  GLN A CA    1 
ATOM   64   C C     . GLN A 1 12  ? 8.379   11.108  16.475 1.00 20.12 ?  12  GLN A C     1 
ATOM   65   O O     . GLN A 1 12  ? 9.454   11.347  17.035 1.00 21.94 ?  12  GLN A O     1 
ATOM   66   C CB    . GLN A 1 12  ? 6.588   10.156  17.926 1.00 18.64 ?  12  GLN A CB    1 
ATOM   67   C CG    . GLN A 1 12  ? 5.327   9.305   17.907 1.00 19.37 ?  12  GLN A CG    1 
ATOM   68   C CD    . GLN A 1 12  ? 4.345   9.734   16.832 1.00 21.92 ?  12  GLN A CD    1 
ATOM   69   O OE1   . GLN A 1 12  ? 4.601   10.674  16.081 1.00 19.28 ?  12  GLN A OE1   1 
ATOM   70   N NE2   . GLN A 1 12  ? 3.212   9.047   16.759 1.00 25.13 ?  12  GLN A NE2   1 
ATOM   71   N N     . LEU A 1 13  ? 7.843   11.902  15.555 1.00 19.18 ?  13  LEU A N     1 
ATOM   72   C CA    . LEU A 1 13  ? 8.457   13.157  15.139 1.00 16.70 ?  13  LEU A CA    1 
ATOM   73   C C     . LEU A 1 13  ? 8.668   14.103  16.318 1.00 19.59 ?  13  LEU A C     1 
ATOM   74   O O     . LEU A 1 13  ? 7.717   14.434  17.036 1.00 18.73 ?  13  LEU A O     1 
ATOM   75   C CB    . LEU A 1 13  ? 7.575   13.815  14.077 1.00 18.34 ?  13  LEU A CB    1 
ATOM   76   C CG    . LEU A 1 13  ? 7.988   15.152  13.474 1.00 18.80 ?  13  LEU A CG    1 
ATOM   77   C CD1   . LEU A 1 13  ? 9.359   15.069  12.852 1.00 16.51 ?  13  LEU A CD1   1 
ATOM   78   C CD2   . LEU A 1 13  ? 6.967   15.560  12.438 1.00 18.10 ?  13  LEU A CD2   1 
ATOM   79   N N     . ALA A 1 14  ? 9.931   14.489  16.538 1.00 19.48 ?  14  ALA A N     1 
ATOM   80   C CA    . ALA A 1 14  ? 10.295  15.681  17.301 1.00 18.95 ?  14  ALA A CA    1 
ATOM   81   C C     . ALA A 1 14  ? 10.127  15.527  18.810 1.00 20.03 ?  14  ALA A C     1 
ATOM   82   O O     . ALA A 1 14  ? 10.970  16.002  19.578 1.00 19.12 ?  14  ALA A O     1 
ATOM   83   C CB    . ALA A 1 14  ? 9.486   16.891  16.807 1.00 17.57 ?  14  ALA A CB    1 
ATOM   84   N N     . GLY A 1 15  ? 9.046   14.891  19.252 1.00 18.63 ?  15  GLY A N     1 
ATOM   85   C CA    . GLY A 1 15  ? 8.691   14.924  20.657 1.00 18.43 ?  15  GLY A CA    1 
ATOM   86   C C     . GLY A 1 15  ? 9.160   13.756  21.500 1.00 20.51 ?  15  GLY A C     1 
ATOM   87   O O     . GLY A 1 15  ? 9.070   13.809  22.727 1.00 19.86 ?  15  GLY A O     1 
ATOM   88   N N     . GLN A 1 16  ? 9.666   12.699  20.872 1.00 17.63 ?  16  GLN A N     1 
ATOM   89   C CA    . GLN A 1 16  ? 9.990   11.470  21.585 1.00 19.35 ?  16  GLN A CA    1 
ATOM   90   C C     . GLN A 1 16  ? 11.480  11.336  21.892 1.00 21.08 ?  16  GLN A C     1 
ATOM   91   O O     . GLN A 1 16  ? 11.888  10.354  22.521 1.00 14.04 ?  16  GLN A O     1 
ATOM   92   C CB    . GLN A 1 16  ? 9.497   10.256  20.782 1.00 18.93 ?  16  GLN A CB    1 
ATOM   93   C CG    . GLN A 1 16  ? 9.336   8.984   21.598 1.00 18.82 ?  16  GLN A CG    1 
ATOM   94   C CD    . GLN A 1 16  ? 8.283   8.052   21.029 1.00 25.45 ?  16  GLN A CD    1 
ATOM   95   O OE1   . GLN A 1 16  ? 8.445   7.497   19.942 1.00 19.62 ?  16  GLN A OE1   1 
ATOM   96   N NE2   . GLN A 1 16  ? 7.188   7.888   21.760 1.00 20.96 ?  16  GLN A NE2   1 
ATOM   97   N N     . ILE A 1 17  ? 12.293  12.307  21.484 1.00 17.04 ?  17  ILE A N     1 
ATOM   98   C CA    . ILE A 1 17  ? 13.697  12.352  21.873 1.00 16.94 ?  17  ILE A CA    1 
ATOM   99   C C     . ILE A 1 17  ? 13.807  12.886  23.296 1.00 18.08 ?  17  ILE A C     1 
ATOM   100  O O     . ILE A 1 17  ? 12.995  13.700  23.741 1.00 19.89 ?  17  ILE A O     1 
ATOM   101  C CB    . ILE A 1 17  ? 14.500  13.209  20.869 1.00 21.30 ?  17  ILE A CB    1 
ATOM   102  C CG1   . ILE A 1 17  ? 16.007  13.078  21.112 1.00 19.42 ?  17  ILE A CG1   1 
ATOM   103  C CG2   . ILE A 1 17  ? 14.059  14.666  20.927 1.00 17.18 ?  17  ILE A CG2   1 
ATOM   104  C CD1   . ILE A 1 17  ? 16.855  13.651  20.001 1.00 21.26 ?  17  ILE A CD1   1 
ATOM   105  N N     A SER A 1 18  ? 14.831  12.420  24.010 0.27 19.38 ?  18  SER A N     1 
ATOM   106  N N     B SER A 1 18  ? 14.810  12.419  24.032 0.73 18.26 ?  18  SER A N     1 
ATOM   107  C CA    A SER A 1 18  ? 15.118  12.887  25.357 0.27 20.01 ?  18  SER A CA    1 
ATOM   108  C CA    B SER A 1 18  ? 14.968  12.884  25.400 0.73 20.14 ?  18  SER A CA    1 
ATOM   109  C C     A SER A 1 18  ? 15.429  14.378  25.352 0.27 18.67 ?  18  SER A C     1 
ATOM   110  C C     B SER A 1 18  ? 15.545  14.299  25.416 0.73 18.58 ?  18  SER A C     1 
ATOM   111  O O     A SER A 1 18  ? 15.793  14.964  24.327 0.27 18.56 ?  18  SER A O     1 
ATOM   112  O O     B SER A 1 18  ? 16.185  14.755  24.462 0.73 17.57 ?  18  SER A O     1 
ATOM   113  C CB    A SER A 1 18  ? 16.311  12.132  25.946 0.27 19.03 ?  18  SER A CB    1 
ATOM   114  C CB    B SER A 1 18  ? 15.855  11.929  26.203 0.73 19.82 ?  18  SER A CB    1 
ATOM   115  O OG    A SER A 1 18  ? 15.968  10.804  26.270 0.27 19.10 ?  18  SER A OG    1 
ATOM   116  O OG    B SER A 1 18  ? 17.217  12.062  25.856 0.73 16.99 ?  18  SER A OG    1 
ATOM   117  N N     . VAL A 1 19  ? 15.297  14.995  26.528 1.00 17.73 ?  19  VAL A N     1 
ATOM   118  C CA    . VAL A 1 19  ? 15.687  16.398  26.655 1.00 20.09 ?  19  VAL A CA    1 
ATOM   119  C C     . VAL A 1 19  ? 17.198  16.544  26.520 1.00 20.17 ?  19  VAL A C     1 
ATOM   120  O O     . VAL A 1 19  ? 17.694  17.425  25.806 1.00 20.45 ?  19  VAL A O     1 
ATOM   121  C CB    . VAL A 1 19  ? 15.181  16.979  27.987 1.00 21.24 ?  19  VAL A CB    1 
ATOM   122  C CG1   . VAL A 1 19  ? 15.739  18.372  28.210 1.00 23.52 ?  19  VAL A CG1   1 
ATOM   123  C CG2   . VAL A 1 19  ? 13.658  16.995  28.015 1.00 22.11 ?  19  VAL A CG2   1 
ATOM   124  N N     . LEU A 1 20  ? 17.952  15.682  27.207 1.00 18.83 ?  20  LEU A N     1 
ATOM   125  C CA    . LEU A 1 20  ? 19.407  15.722  27.095 1.00 18.77 ?  20  LEU A CA    1 
ATOM   126  C C     . LEU A 1 20  ? 19.857  15.382  25.679 1.00 18.77 ?  20  LEU A C     1 
ATOM   127  O O     . LEU A 1 20  ? 20.774  16.016  25.141 1.00 21.56 ?  20  LEU A O     1 
ATOM   128  C CB    . LEU A 1 20  ? 20.042  14.769  28.105 1.00 20.69 ?  20  LEU A CB    1 
ATOM   129  C CG    . LEU A 1 20  ? 21.553  14.567  27.990 1.00 19.37 ?  20  LEU A CG    1 
ATOM   130  C CD1   . LEU A 1 20  ? 22.292  15.890  28.166 1.00 22.25 ?  20  LEU A CD1   1 
ATOM   131  C CD2   . LEU A 1 20  ? 22.047  13.538  28.996 1.00 20.22 ?  20  LEU A CD2   1 
ATOM   132  N N     . SER A 1 21  ? 19.226  14.380  25.061 1.00 16.15 ?  21  SER A N     1 
ATOM   133  C CA    . SER A 1 21  ? 19.648  13.938  23.733 1.00 15.37 ?  21  SER A CA    1 
ATOM   134  C C     . SER A 1 21  ? 19.442  15.031  22.694 1.00 17.29 ?  21  SER A C     1 
ATOM   135  O O     . SER A 1 21  ? 20.272  15.205  21.793 1.00 18.03 ?  21  SER A O     1 
ATOM   136  C CB    . SER A 1 21  ? 18.894  12.669  23.335 1.00 17.18 ?  21  SER A CB    1 
ATOM   137  O OG    . SER A 1 21  ? 19.338  11.559  24.094 1.00 20.84 ?  21  SER A OG    1 
ATOM   138  N N     . ARG A 1 22  ? 18.331  15.769  22.793 1.00 14.05 ?  22  ARG A N     1 
ATOM   139  C CA    . ARG A 1 22  ? 18.121  16.911  21.908 1.00 14.83 ?  22  ARG A CA    1 
ATOM   140  C C     . ARG A 1 22  ? 19.236  17.937  22.075 1.00 15.78 ?  22  ARG A C     1 
ATOM   141  O O     . ARG A 1 22  ? 19.711  18.519  21.092 1.00 14.07 ?  22  ARG A O     1 
ATOM   142  C CB    . ARG A 1 22  ? 16.763  17.555  22.189 1.00 18.10 ?  22  ARG A CB    1 
ATOM   143  C CG    . ARG A 1 22  ? 16.240  18.452  21.073 1.00 22.51 ?  22  ARG A CG    1 
ATOM   144  C CD    . ARG A 1 22  ? 15.054  19.285  21.541 1.00 24.14 ?  22  ARG A CD    1 
ATOM   145  N NE    . ARG A 1 22  ? 14.498  20.117  20.479 1.00 27.76 ?  22  ARG A NE    1 
ATOM   146  C CZ    . ARG A 1 22  ? 14.697  21.425  20.370 1.00 28.94 ?  22  ARG A CZ    1 
ATOM   147  N NH1   . ARG A 1 22  ? 15.483  22.080  21.211 1.00 30.93 ?  22  ARG A NH1   1 
ATOM   148  N NH2   . ARG A 1 22  ? 14.100  22.094  19.386 1.00 33.66 ?  22  ARG A NH2   1 
ATOM   149  N N     . SER A 1 23  ? 19.663  18.170  23.320 1.00 17.58 ?  23  SER A N     1 
ATOM   150  C CA    . SER A 1 23  ? 20.721  19.142  23.580 1.00 16.37 ?  23  SER A CA    1 
ATOM   151  C C     . SER A 1 23  ? 22.039  18.695  22.966 1.00 19.40 ?  23  SER A C     1 
ATOM   152  O O     . SER A 1 23  ? 22.824  19.525  22.492 1.00 18.61 ?  23  SER A O     1 
ATOM   153  C CB    . SER A 1 23  ? 20.872  19.360  25.087 1.00 15.79 ?  23  SER A CB    1 
ATOM   154  O OG    . SER A 1 23  ? 21.865  20.327  25.371 1.00 15.91 ?  23  SER A OG    1 
ATOM   155  N N     . TYR A 1 24  ? 22.305  17.384  22.976 1.00 16.14 ?  24  TYR A N     1 
ATOM   156  C CA    . TYR A 1 24  ? 23.523  16.871  22.355 1.00 15.88 ?  24  TYR A CA    1 
ATOM   157  C C     . TYR A 1 24  ? 23.545  17.180  20.865 1.00 17.64 ?  24  TYR A C     1 
ATOM   158  O O     . TYR A 1 24  ? 24.575  17.595  20.320 1.00 19.64 ?  24  TYR A O     1 
ATOM   159  C CB    . TYR A 1 24  ? 23.636  15.366  22.584 1.00 16.39 ?  24  TYR A CB    1 
ATOM   160  C CG    . TYR A 1 24  ? 24.419  15.003  23.818 1.00 20.75 ?  24  TYR A CG    1 
ATOM   161  C CD1   . TYR A 1 24  ? 25.776  15.281  23.908 1.00 20.47 ?  24  TYR A CD1   1 
ATOM   162  C CD2   . TYR A 1 24  ? 23.803  14.383  24.896 1.00 21.50 ?  24  TYR A CD2   1 
ATOM   163  C CE1   . TYR A 1 24  ? 26.495  14.954  25.037 1.00 23.97 ?  24  TYR A CE1   1 
ATOM   164  C CE2   . TYR A 1 24  ? 24.514  14.051  26.028 1.00 18.07 ?  24  TYR A CE2   1 
ATOM   165  C CZ    . TYR A 1 24  ? 25.856  14.343  26.094 1.00 24.84 ?  24  TYR A CZ    1 
ATOM   166  O OH    . TYR A 1 24  ? 26.571  14.008  27.223 1.00 26.33 ?  24  TYR A OH    1 
ATOM   167  N N     . ILE A 1 25  ? 22.415  16.967  20.190 1.00 16.86 ?  25  ILE A N     1 
ATOM   168  C CA    . ILE A 1 25  ? 22.309  17.288  18.770 1.00 19.09 ?  25  ILE A CA    1 
ATOM   169  C C     . ILE A 1 25  ? 22.552  18.774  18.551 1.00 19.68 ?  25  ILE A C     1 
ATOM   170  O O     . ILE A 1 25  ? 23.327  19.177  17.675 1.00 20.61 ?  25  ILE A O     1 
ATOM   171  C CB    . ILE A 1 25  ? 20.935  16.856  18.228 1.00 18.33 ?  25  ILE A CB    1 
ATOM   172  C CG1   . ILE A 1 25  ? 20.896  15.338  18.021 1.00 16.85 ?  25  ILE A CG1   1 
ATOM   173  C CG2   . ILE A 1 25  ? 20.616  17.592  16.942 1.00 20.81 ?  25  ILE A CG2   1 
ATOM   174  C CD1   . ILE A 1 25  ? 19.526  14.813  17.641 1.00 17.69 ?  25  ILE A CD1   1 
ATOM   175  N N     . GLU A 1 26  ? 21.875  19.607  19.346 1.00 19.63 ?  26  GLU A N     1 
ATOM   176  C CA    . GLU A 1 26  ? 21.965  21.059  19.214 1.00 22.02 ?  26  GLU A CA    1 
ATOM   177  C C     . GLU A 1 26  ? 23.412  21.544  19.235 1.00 23.82 ?  26  GLU A C     1 
ATOM   178  O O     . GLU A 1 26  ? 23.820  22.365  18.406 1.00 23.57 ?  26  GLU A O     1 
ATOM   179  C CB    . GLU A 1 26  ? 21.169  21.719  20.339 1.00 20.63 ?  26  GLU A CB    1 
ATOM   180  C CG    . GLU A 1 26  ? 20.914  23.204  20.168 1.00 30.61 ?  26  GLU A CG    1 
ATOM   181  C CD    . GLU A 1 26  ? 20.081  23.773  21.299 1.00 41.46 ?  26  GLU A CD    1 
ATOM   182  O OE1   . GLU A 1 26  ? 19.516  22.976  22.077 1.00 39.55 ?  26  GLU A OE1   1 
ATOM   183  O OE2   . GLU A 1 26  ? 19.993  25.015  21.416 1.00 50.75 -1 26  GLU A OE2   1 
ATOM   184  N N     . HIS A 1 27  ? 24.205  21.038  20.174 1.00 16.93 ?  27  HIS A N     1 
ATOM   185  C CA    . HIS A 1 27  ? 25.543  21.559  20.422 1.00 25.54 ?  27  HIS A CA    1 
ATOM   186  C C     . HIS A 1 27  ? 26.628  20.837  19.636 1.00 24.60 ?  27  HIS A C     1 
ATOM   187  O O     . HIS A 1 27  ? 27.799  21.208  19.747 1.00 20.52 ?  27  HIS A O     1 
ATOM   188  C CB    . HIS A 1 27  ? 25.865  21.486  21.919 1.00 27.79 ?  27  HIS A CB    1 
ATOM   189  C CG    . HIS A 1 27  ? 25.210  22.558  22.731 1.00 30.56 ?  27  HIS A CG    1 
ATOM   190  N ND1   . HIS A 1 27  ? 25.621  23.873  22.697 1.00 31.20 ?  27  HIS A ND1   1 
ATOM   191  C CD2   . HIS A 1 27  ? 24.171  22.511  23.599 1.00 30.04 ?  27  HIS A CD2   1 
ATOM   192  C CE1   . HIS A 1 27  ? 24.864  24.589  23.509 1.00 35.29 ?  27  HIS A CE1   1 
ATOM   193  N NE2   . HIS A 1 27  ? 23.977  23.787  24.069 1.00 36.10 ?  27  HIS A NE2   1 
ATOM   194  N N     . ALA A 1 28  ? 26.275  19.835  18.838 1.00 20.74 ?  28  ALA A N     1 
ATOM   195  C CA    . ALA A 1 28  ? 27.271  19.045  18.128 1.00 21.76 ?  28  ALA A CA    1 
ATOM   196  C C     . ALA A 1 28  ? 27.974  19.860  17.046 1.00 22.25 ?  28  ALA A C     1 
ATOM   197  O O     . ALA A 1 28  ? 27.406  20.788  16.462 1.00 20.88 ?  28  ALA A O     1 
ATOM   198  C CB    . ALA A 1 28  ? 26.621  17.815  17.494 1.00 22.31 ?  28  ALA A CB    1 
ATOM   199  N N     . ASP A 1 29  ? 29.234  19.497  16.785 1.00 22.95 ?  29  ASP A N     1 
ATOM   200  C CA    . ASP A 1 29  ? 29.933  20.021  15.615 1.00 24.01 ?  29  ASP A CA    1 
ATOM   201  C C     . ASP A 1 29  ? 29.282  19.522  14.333 1.00 23.96 ?  29  ASP A C     1 
ATOM   202  O O     . ASP A 1 29  ? 29.139  20.274  13.363 1.00 21.65 ?  29  ASP A O     1 
ATOM   203  C CB    . ASP A 1 29  ? 31.405  19.602  15.638 1.00 18.93 ?  29  ASP A CB    1 
ATOM   204  C CG    . ASP A 1 29  ? 32.218  20.363  16.658 1.00 26.94 ?  29  ASP A CG    1 
ATOM   205  O OD1   . ASP A 1 29  ? 31.735  21.399  17.162 1.00 22.84 ?  29  ASP A OD1   1 
ATOM   206  O OD2   . ASP A 1 29  ? 33.355  19.932  16.948 1.00 25.16 -1 29  ASP A OD2   1 
ATOM   207  N N     . ILE A 1 30  ? 28.883  18.252  14.317 1.00 23.17 ?  30  ILE A N     1 
ATOM   208  C CA    . ILE A 1 30  ? 28.365  17.590  13.127 1.00 21.19 ?  30  ILE A CA    1 
ATOM   209  C C     . ILE A 1 30  ? 27.452  16.465  13.589 1.00 21.74 ?  30  ILE A C     1 
ATOM   210  O O     . ILE A 1 30  ? 27.645  15.888  14.662 1.00 18.19 ?  30  ILE A O     1 
ATOM   211  C CB    . ILE A 1 30  ? 29.519  17.064  12.238 1.00 21.33 ?  30  ILE A CB    1 
ATOM   212  C CG1   . ILE A 1 30  ? 28.999  16.547  10.896 1.00 18.65 ?  30  ILE A CG1   1 
ATOM   213  C CG2   . ILE A 1 30  ? 30.319  15.992  12.965 1.00 18.32 ?  30  ILE A CG2   1 
ATOM   214  C CD1   . ILE A 1 30  ? 30.065  16.480  9.822  1.00 24.94 ?  30  ILE A CD1   1 
ATOM   215  N N     . VAL A 1 31  ? 26.432  16.170  12.788 1.00 19.95 ?  31  VAL A N     1 
ATOM   216  C CA    . VAL A 1 31  ? 25.480  15.108  13.094 1.00 19.76 ?  31  VAL A CA    1 
ATOM   217  C C     . VAL A 1 31  ? 25.406  14.156  11.908 1.00 21.15 ?  31  VAL A C     1 
ATOM   218  O O     . VAL A 1 31  ? 25.283  14.593  10.759 1.00 22.12 ?  31  VAL A O     1 
ATOM   219  C CB    . VAL A 1 31  ? 24.081  15.667  13.427 1.00 19.27 ?  31  VAL A CB    1 
ATOM   220  C CG1   . VAL A 1 31  ? 23.096  14.529  13.666 1.00 17.48 ?  31  VAL A CG1   1 
ATOM   221  C CG2   . VAL A 1 31  ? 24.149  16.579  14.642 1.00 18.07 ?  31  VAL A CG2   1 
ATOM   222  N N     . PHE A 1 32  ? 25.480  12.859  12.188 1.00 22.66 ?  32  PHE A N     1 
ATOM   223  C CA    . PHE A 1 32  ? 25.207  11.812  11.210 1.00 24.02 ?  32  PHE A CA    1 
ATOM   224  C C     . PHE A 1 32  ? 23.854  11.199  11.549 1.00 25.35 ?  32  PHE A C     1 
ATOM   225  O O     . PHE A 1 32  ? 23.662  10.683  12.654 1.00 23.74 ?  32  PHE A O     1 
ATOM   226  C CB    . PHE A 1 32  ? 26.312  10.755  11.212 1.00 22.16 ?  32  PHE A CB    1 
ATOM   227  C CG    . PHE A 1 32  ? 27.642  11.268  10.731 1.00 21.93 ?  32  PHE A CG    1 
ATOM   228  C CD1   . PHE A 1 32  ? 28.487  11.956  11.588 1.00 20.31 ?  32  PHE A CD1   1 
ATOM   229  C CD2   . PHE A 1 32  ? 28.043  11.070  9.421  1.00 20.12 ?  32  PHE A CD2   1 
ATOM   230  C CE1   . PHE A 1 32  ? 29.710  12.431  11.147 1.00 21.47 ?  32  PHE A CE1   1 
ATOM   231  C CE2   . PHE A 1 32  ? 29.265  11.542  8.974  1.00 19.09 ?  32  PHE A CE2   1 
ATOM   232  C CZ    . PHE A 1 32  ? 30.098  12.223  9.839  1.00 22.09 ?  32  PHE A CZ    1 
ATOM   233  N N     . SER A 1 33  ? 22.920  11.263  10.605 1.00 23.09 ?  33  SER A N     1 
ATOM   234  C CA    . SER A 1 33  ? 21.525  10.933  10.856 1.00 23.53 ?  33  SER A CA    1 
ATOM   235  C C     . SER A 1 33  ? 21.098  9.645   10.163 1.00 20.66 ?  33  SER A C     1 
ATOM   236  O O     . SER A 1 33  ? 21.668  9.242   9.146  1.00 19.02 ?  33  SER A O     1 
ATOM   237  C CB    . SER A 1 33  ? 20.611  12.069  10.392 1.00 22.90 ?  33  SER A CB    1 
ATOM   238  O OG    . SER A 1 33  ? 20.766  12.320  9.007  1.00 23.92 ?  33  SER A OG    1 
ATOM   239  N N     . LEU A 1 34  ? 20.068  9.010   10.731 1.00 22.13 ?  34  LEU A N     1 
ATOM   240  C CA    . LEU A 1 34  ? 19.337  7.914   10.086 1.00 21.79 ?  34  LEU A CA    1 
ATOM   241  C C     . LEU A 1 34  ? 17.919  7.956   10.660 1.00 24.18 ?  34  LEU A C     1 
ATOM   242  O O     . LEU A 1 34  ? 17.638  7.367   11.704 1.00 21.47 ?  34  LEU A O     1 
ATOM   243  C CB    . LEU A 1 34  ? 20.007  6.566   10.312 1.00 23.60 ?  34  LEU A CB    1 
ATOM   244  C CG    . LEU A 1 34  ? 19.690  5.409   9.354  1.00 30.69 ?  34  LEU A CG    1 
ATOM   245  C CD1   . LEU A 1 34  ? 18.234  4.957   9.422  1.00 34.87 ?  34  LEU A CD1   1 
ATOM   246  C CD2   . LEU A 1 34  ? 20.054  5.798   7.930  1.00 28.48 ?  34  LEU A CD2   1 
ATOM   247  N N     . LEU A 1 35  ? 17.036  8.657   9.964  1.00 23.53 ?  35  LEU A N     1 
ATOM   248  C CA    . LEU A 1 35  ? 15.722  9.034   10.457 1.00 20.35 ?  35  LEU A CA    1 
ATOM   249  C C     . LEU A 1 35  ? 14.630  8.400   9.598  1.00 24.06 ?  35  LEU A C     1 
ATOM   250  O O     . LEU A 1 35  ? 14.881  8.005   8.453  1.00 23.65 ?  35  LEU A O     1 
ATOM   251  C CB    . LEU A 1 35  ? 15.579  10.565  10.457 1.00 25.09 ?  35  LEU A CB    1 
ATOM   252  C CG    . LEU A 1 35  ? 16.068  11.352  11.680 1.00 29.42 ?  35  LEU A CG    1 
ATOM   253  C CD1   . LEU A 1 35  ? 17.053  10.575  12.550 1.00 26.01 ?  35  LEU A CD1   1 
ATOM   254  C CD2   . LEU A 1 35  ? 16.686  12.658  11.223 1.00 24.41 ?  35  LEU A CD2   1 
ATOM   255  N N     . PRO A 1 36  ? 13.403  8.279   10.120 1.00 22.10 ?  36  PRO A N     1 
ATOM   256  C CA    . PRO A 1 36  ? 12.369  7.527   9.386  1.00 25.91 ?  36  PRO A CA    1 
ATOM   257  C C     . PRO A 1 36  ? 11.838  8.215   8.136  1.00 22.59 ?  36  PRO A C     1 
ATOM   258  O O     . PRO A 1 36  ? 11.346  7.514   7.242  1.00 19.38 ?  36  PRO A O     1 
ATOM   259  C CB    . PRO A 1 36  ? 11.253  7.345   10.430 1.00 21.22 ?  36  PRO A CB    1 
ATOM   260  C CG    . PRO A 1 36  ? 11.898  7.653   11.754 1.00 24.31 ?  36  PRO A CG    1 
ATOM   261  C CD    . PRO A 1 36  ? 12.916  8.697   11.444 1.00 22.16 ?  36  PRO A CD    1 
ATOM   262  N N     . ASP A 1 37  ? 11.909  9.540   8.028  1.00 23.21 ?  37  ASP A N     1 
ATOM   263  C CA    . ASP A 1 37  ? 11.248  10.226  6.922  1.00 29.22 ?  37  ASP A CA    1 
ATOM   264  C C     . ASP A 1 37  ? 11.811  11.633  6.772  1.00 24.75 ?  37  ASP A C     1 
ATOM   265  O O     . ASP A 1 37  ? 12.750  12.031  7.468  1.00 23.42 ?  37  ASP A O     1 
ATOM   266  C CB    . ASP A 1 37  ? 9.730   10.259  7.128  1.00 25.60 ?  37  ASP A CB    1 
ATOM   267  C CG    . ASP A 1 37  ? 9.330   10.852  8.465  1.00 27.05 ?  37  ASP A CG    1 
ATOM   268  O OD1   . ASP A 1 37  ? 9.742   11.995  8.770  1.00 25.35 ?  37  ASP A OD1   1 
ATOM   269  O OD2   . ASP A 1 37  ? 8.590   10.180  9.215  1.00 23.80 -1 37  ASP A OD2   1 
ATOM   270  N N     . GLY A 1 38  ? 11.217  12.387  5.839  1.00 20.91 ?  38  GLY A N     1 
ATOM   271  C CA    . GLY A 1 38  ? 11.673  13.734  5.550  1.00 20.57 ?  38  GLY A CA    1 
ATOM   272  C C     . GLY A 1 38  ? 11.178  14.780  6.521  1.00 26.53 ?  38  GLY A C     1 
ATOM   273  O O     . GLY A 1 38  ? 11.814  15.832  6.655  1.00 25.11 ?  38  GLY A O     1 
ATOM   274  N N     . PHE A 1 39  ? 10.055  14.519  7.195  1.00 21.99 ?  39  PHE A N     1 
ATOM   275  C CA    . PHE A 1 39  ? 9.610   15.422  8.250  1.00 22.05 ?  39  PHE A CA    1 
ATOM   276  C C     . PHE A 1 39  ? 10.599  15.394  9.406  1.00 20.98 ?  39  PHE A C     1 
ATOM   277  O O     . PHE A 1 39  ? 10.978  16.440  9.949  1.00 18.67 ?  39  PHE A O     1 
ATOM   278  C CB    . PHE A 1 39  ? 8.216   15.029  8.743  1.00 23.71 ?  39  PHE A CB    1 
ATOM   279  C CG    . PHE A 1 39  ? 7.123   15.220  7.728  1.00 27.05 ?  39  PHE A CG    1 
ATOM   280  C CD1   . PHE A 1 39  ? 6.665   16.487  7.402  1.00 20.46 ?  39  PHE A CD1   1 
ATOM   281  C CD2   . PHE A 1 39  ? 6.537   14.124  7.115  1.00 20.22 ?  39  PHE A CD2   1 
ATOM   282  C CE1   . PHE A 1 39  ? 5.653   16.656  6.470  1.00 27.04 ?  39  PHE A CE1   1 
ATOM   283  C CE2   . PHE A 1 39  ? 5.527   14.286  6.185  1.00 24.96 ?  39  PHE A CE2   1 
ATOM   284  C CZ    . PHE A 1 39  ? 5.085   15.554  5.862  1.00 26.15 ?  39  PHE A CZ    1 
ATOM   285  N N     . SER A 1 40  ? 11.024  14.188  9.792  1.00 17.91 ?  40  SER A N     1 
ATOM   286  C CA    . SER A 1 40  ? 12.044  14.036  10.823 1.00 23.91 ?  40  SER A CA    1 
ATOM   287  C C     . SER A 1 40  ? 13.363  14.656  10.383 1.00 20.87 ?  40  SER A C     1 
ATOM   288  O O     . SER A 1 40  ? 14.107  15.201  11.207 1.00 25.45 ?  40  SER A O     1 
ATOM   289  C CB    . SER A 1 40  ? 12.226  12.555  11.158 1.00 18.29 ?  40  SER A CB    1 
ATOM   290  O OG    . SER A 1 40  ? 13.034  12.386  12.306 1.00 32.92 ?  40  SER A OG    1 
ATOM   291  N N     . GLN A 1 41  ? 13.673  14.578  9.085  1.00 25.55 ?  41  GLN A N     1 
ATOM   292  C CA    . GLN A 1 41  ? 14.946  15.102  8.602  1.00 18.90 ?  41  GLN A CA    1 
ATOM   293  C C     . GLN A 1 41  ? 14.943  16.625  8.606  1.00 20.04 ?  41  GLN A C     1 
ATOM   294  O O     . GLN A 1 41  ? 15.960  17.252  8.925  1.00 21.60 ?  41  GLN A O     1 
ATOM   295  C CB    . GLN A 1 41  ? 15.238  14.566  7.199  1.00 23.22 ?  41  GLN A CB    1 
ATOM   296  C CG    . GLN A 1 41  ? 16.691  14.705  6.762  1.00 20.02 ?  41  GLN A CG    1 
ATOM   297  C CD    . GLN A 1 41  ? 17.619  13.769  7.517  1.00 21.64 ?  41  GLN A CD    1 
ATOM   298  O OE1   . GLN A 1 41  ? 17.282  12.614  7.770  1.00 25.78 ?  41  GLN A OE1   1 
ATOM   299  N NE2   . GLN A 1 41  ? 18.800  14.265  7.870  1.00 20.15 ?  41  GLN A NE2   1 
ATOM   300  N N     . ARG A 1 42  ? 13.805  17.233  8.256  1.00 18.50 ?  42  ARG A N     1 
ATOM   301  C CA    . ARG A 1 42  ? 13.686  18.686  8.327  1.00 24.13 ?  42  ARG A CA    1 
ATOM   302  C C     . ARG A 1 42  ? 13.830  19.172  9.764  1.00 23.63 ?  42  ARG A C     1 
ATOM   303  O O     . ARG A 1 42  ? 14.548  20.142  10.038 1.00 18.56 ?  42  ARG A O     1 
ATOM   304  C CB    . ARG A 1 42  ? 12.346  19.132  7.739  1.00 20.89 ?  42  ARG A CB    1 
ATOM   305  C CG    . ARG A 1 42  ? 12.294  19.100  6.221  1.00 32.34 ?  42  ARG A CG    1 
ATOM   306  C CD    . ARG A 1 42  ? 10.875  19.297  5.700  1.00 36.46 ?  42  ARG A CD    1 
ATOM   307  N NE    . ARG A 1 42  ? 10.687  18.654  4.405  1.00 42.69 ?  42  ARG A NE    1 
ATOM   308  C CZ    . ARG A 1 42  ? 10.035  17.514  4.218  1.00 40.99 ?  42  ARG A CZ    1 
ATOM   309  N NH1   . ARG A 1 42  ? 9.428   16.893  5.216  1.00 36.49 ?  42  ARG A NH1   1 
ATOM   310  N NH2   . ARG A 1 42  ? 9.984   16.986  2.998  1.00 49.64 ?  42  ARG A NH2   1 
ATOM   311  N N     . TRP A 1 43  ? 13.145  18.502  10.697 1.00 18.01 ?  43  TRP A N     1 
ATOM   312  C CA    . TRP A 1 43  ? 13.234  18.865  12.109 1.00 22.18 ?  43  TRP A CA    1 
ATOM   313  C C     . TRP A 1 43  ? 14.674  18.830  12.600 1.00 23.04 ?  43  TRP A C     1 
ATOM   314  O O     . TRP A 1 43  ? 15.111  19.725  13.336 1.00 22.87 ?  43  TRP A O     1 
ATOM   315  C CB    . TRP A 1 43  ? 12.358  17.927  12.940 1.00 19.66 ?  43  TRP A CB    1 
ATOM   316  C CG    . TRP A 1 43  ? 12.731  17.837  14.392 1.00 18.12 ?  43  TRP A CG    1 
ATOM   317  C CD1   . TRP A 1 43  ? 12.298  18.649  15.401 1.00 20.42 ?  43  TRP A CD1   1 
ATOM   318  C CD2   . TRP A 1 43  ? 13.604  16.876  14.998 1.00 21.92 ?  43  TRP A CD2   1 
ATOM   319  N NE1   . TRP A 1 43  ? 12.852  18.254  16.597 1.00 20.65 ?  43  TRP A NE1   1 
ATOM   320  C CE2   . TRP A 1 43  ? 13.658  17.169  16.375 1.00 23.50 ?  43  TRP A CE2   1 
ATOM   321  C CE3   . TRP A 1 43  ? 14.349  15.797  14.509 1.00 19.08 ?  43  TRP A CE3   1 
ATOM   322  C CZ2   . TRP A 1 43  ? 14.425  16.423  17.268 1.00 19.89 ?  43  TRP A CZ2   1 
ATOM   323  C CZ3   . TRP A 1 43  ? 15.110  15.059  15.396 1.00 20.13 ?  43  TRP A CZ3   1 
ATOM   324  C CH2   . TRP A 1 43  ? 15.142  15.374  16.762 1.00 21.14 ?  43  TRP A CH2   1 
ATOM   325  N N     . LEU A 1 44  ? 15.427  17.803  12.204 1.00 21.47 ?  44  LEU A N     1 
ATOM   326  C CA    . LEU A 1 44  ? 16.812  17.691  12.643 1.00 22.38 ?  44  LEU A CA    1 
ATOM   327  C C     . LEU A 1 44  ? 17.662  18.818  12.072 1.00 20.30 ?  44  LEU A C     1 
ATOM   328  O O     . LEU A 1 44  ? 18.511  19.381  12.774 1.00 21.27 ?  44  LEU A O     1 
ATOM   329  C CB    . LEU A 1 44  ? 17.387  16.338  12.234 1.00 22.96 ?  44  LEU A CB    1 
ATOM   330  C CG    . LEU A 1 44  ? 18.898  16.215  12.429 1.00 21.35 ?  44  LEU A CG    1 
ATOM   331  C CD1   . LEU A 1 44  ? 19.266  16.394  13.893 1.00 24.32 ?  44  LEU A CD1   1 
ATOM   332  C CD2   . LEU A 1 44  ? 19.407  14.895  11.911 1.00 20.57 ?  44  LEU A CD2   1 
ATOM   333  N N     . THR A 1 45  ? 17.445  19.163  10.800 1.00 22.22 ?  45  THR A N     1 
ATOM   334  C CA    . THR A 1 45  ? 18.303  20.149  10.153 1.00 27.43 ?  45  THR A CA    1 
ATOM   335  C C     . THR A 1 45  ? 18.085  21.542  10.728 1.00 23.61 ?  45  THR A C     1 
ATOM   336  O O     . THR A 1 45  ? 19.000  22.374  10.706 1.00 25.35 ?  45  THR A O     1 
ATOM   337  C CB    . THR A 1 45  ? 18.056  20.151  8.645  1.00 27.81 ?  45  THR A CB    1 
ATOM   338  O OG1   . THR A 1 45  ? 16.649  20.240  8.391  1.00 38.08 ?  45  THR A OG1   1 
ATOM   339  C CG2   . THR A 1 45  ? 18.598  18.879  8.014  1.00 27.71 ?  45  THR A CG2   1 
ATOM   340  N N     . LYS A 1 46  ? 16.884  21.814  11.244 1.00 25.72 ?  46  LYS A N     1 
ATOM   341  C CA    . LYS A 1 46  ? 16.648  23.076  11.935 1.00 25.36 ?  46  LYS A CA    1 
ATOM   342  C C     . LYS A 1 46  ? 17.324  23.087  13.300 1.00 28.36 ?  46  LYS A C     1 
ATOM   343  O O     . LYS A 1 46  ? 17.775  24.143  13.761 1.00 28.52 ?  46  LYS A O     1 
ATOM   344  C CB    . LYS A 1 46  ? 15.145  23.328  12.060 1.00 30.92 ?  46  LYS A CB    1 
ATOM   345  C CG    . LYS A 1 46  ? 14.489  23.678  10.729 1.00 37.60 ?  46  LYS A CG    1 
ATOM   346  C CD    . LYS A 1 46  ? 13.229  24.523  10.888 1.00 44.88 ?  46  LYS A CD    1 
ATOM   347  C CE    . LYS A 1 46  ? 12.009  23.685  11.244 1.00 44.12 ?  46  LYS A CE    1 
ATOM   348  N NZ    . LYS A 1 46  ? 12.010  23.190  12.648 1.00 46.38 ?  46  LYS A NZ    1 
ATOM   349  N N     . LEU A 1 47  ? 17.399  21.925  13.957 1.00 23.62 ?  47  LEU A N     1 
ATOM   350  C CA    . LEU A 1 47  ? 18.114  21.824  15.227 1.00 26.73 ?  47  LEU A CA    1 
ATOM   351  C C     . LEU A 1 47  ? 19.601  22.095  15.038 1.00 23.15 ?  47  LEU A C     1 
ATOM   352  O O     . LEU A 1 47  ? 20.220  22.815  15.831 1.00 26.93 ?  47  LEU A O     1 
ATOM   353  C CB    . LEU A 1 47  ? 17.902  20.436  15.832 1.00 23.25 ?  47  LEU A CB    1 
ATOM   354  C CG    . LEU A 1 47  ? 17.238  20.313  17.203 1.00 30.53 ?  47  LEU A CG    1 
ATOM   355  C CD1   . LEU A 1 47  ? 17.292  18.869  17.669 1.00 24.80 ?  47  LEU A CD1   1 
ATOM   356  C CD2   . LEU A 1 47  ? 17.903  21.232  18.214 1.00 29.57 ?  47  LEU A CD2   1 
ATOM   357  N N     . ASN A 1 48  ? 20.185  21.524  13.989 1.00 22.95 ?  48  ASN A N     1 
ATOM   358  C CA    . ASN A 1 48  ? 21.606  21.614  13.688 1.00 21.61 ?  48  ASN A CA    1 
ATOM   359  C C     . ASN A 1 48  ? 21.765  21.437  12.184 1.00 20.89 ?  48  ASN A C     1 
ATOM   360  O O     . ASN A 1 48  ? 21.474  20.358  11.657 1.00 20.86 ?  48  ASN A O     1 
ATOM   361  C CB    . ASN A 1 48  ? 22.393  20.551  14.463 1.00 21.64 ?  48  ASN A CB    1 
ATOM   362  C CG    . ASN A 1 48  ? 23.899  20.741  14.369 1.00 22.23 ?  48  ASN A CG    1 
ATOM   363  O OD1   . ASN A 1 48  ? 24.431  21.127  13.329 1.00 23.41 ?  48  ASN A OD1   1 
ATOM   364  N ND2   . ASN A 1 48  ? 24.595  20.455  15.465 1.00 19.72 ?  48  ASN A ND2   1 
ATOM   365  N N     . PRO A 1 49  ? 22.201  22.467  11.453 1.00 24.81 ?  49  PRO A N     1 
ATOM   366  C CA    . PRO A 1 49  ? 22.243  22.361  9.986  1.00 27.70 ?  49  PRO A CA    1 
ATOM   367  C C     . PRO A 1 49  ? 23.381  21.504  9.452  1.00 27.14 ?  49  PRO A C     1 
ATOM   368  O O     . PRO A 1 49  ? 23.381  21.194  8.254  1.00 24.37 ?  49  PRO A O     1 
ATOM   369  C CB    . PRO A 1 49  ? 22.393  23.820  9.541  1.00 26.11 ?  49  PRO A CB    1 
ATOM   370  C CG    . PRO A 1 49  ? 23.161  24.451  10.663 1.00 25.89 ?  49  PRO A CG    1 
ATOM   371  C CD    . PRO A 1 49  ? 22.649  23.790  11.924 1.00 24.64 ?  49  PRO A CD    1 
ATOM   372  N N     . ASN A 1 50  ? 24.339  21.104  10.289 1.00 25.93 ?  50  ASN A N     1 
ATOM   373  C CA    . ASN A 1 50  ? 25.485  20.318  9.828  1.00 27.77 ?  50  ASN A CA    1 
ATOM   374  C C     . ASN A 1 50  ? 25.169  18.836  9.994  1.00 22.63 ?  50  ASN A C     1 
ATOM   375  O O     . ASN A 1 50  ? 25.638  18.160  10.909 1.00 23.79 ?  50  ASN A O     1 
ATOM   376  C CB    . ASN A 1 50  ? 26.752  20.718  10.575 1.00 26.53 ?  50  ASN A CB    1 
ATOM   377  C CG    . ASN A 1 50  ? 28.013  20.313  9.835  1.00 31.12 ?  50  ASN A CG    1 
ATOM   378  O OD1   . ASN A 1 50  ? 27.967  19.946  8.660  1.00 34.83 ?  50  ASN A OD1   1 
ATOM   379  N ND2   . ASN A 1 50  ? 29.151  20.381  10.519 1.00 30.03 ?  50  ASN A ND2   1 
ATOM   380  N N     . VAL A 1 51  ? 24.355  18.325  9.078  1.00 20.61 ?  51  VAL A N     1 
ATOM   381  C CA    . VAL A 1 51  ? 23.894  16.942  9.103  1.00 22.36 ?  51  VAL A CA    1 
ATOM   382  C C     . VAL A 1 51  ? 24.442  16.216  7.882  1.00 20.07 ?  51  VAL A C     1 
ATOM   383  O O     . VAL A 1 51  ? 24.421  16.747  6.767  1.00 23.58 ?  51  VAL A O     1 
ATOM   384  C CB    . VAL A 1 51  ? 22.352  16.853  9.137  1.00 23.38 ?  51  VAL A CB    1 
ATOM   385  C CG1   . VAL A 1 51  ? 21.893  15.406  9.065  1.00 22.10 ?  51  VAL A CG1   1 
ATOM   386  C CG2   . VAL A 1 51  ? 21.816  17.517  10.391 1.00 24.41 ?  51  VAL A CG2   1 
ATOM   387  N N     . ILE A 1 52  ? 24.933  15.000  8.097  1.00 24.12 ?  52  ILE A N     1 
ATOM   388  C CA    . ILE A 1 52  ? 25.280  14.076  7.023  1.00 24.71 ?  52  ILE A CA    1 
ATOM   389  C C     . ILE A 1 52  ? 24.327  12.893  7.118  1.00 21.67 ?  52  ILE A C     1 
ATOM   390  O O     . ILE A 1 52  ? 24.323  12.168  8.121  1.00 19.19 ?  52  ILE A O     1 
ATOM   391  C CB    . ILE A 1 52  ? 26.743  13.617  7.113  1.00 23.76 ?  52  ILE A CB    1 
ATOM   392  C CG1   . ILE A 1 52  ? 27.688  14.818  7.021  1.00 24.60 ?  52  ILE A CG1   1 
ATOM   393  C CG2   . ILE A 1 52  ? 27.048  12.589  6.032  1.00 25.99 ?  52  ILE A CG2   1 
ATOM   394  C CD1   . ILE A 1 52  ? 27.898  15.323  5.611  1.00 29.99 ?  52  ILE A CD1   1 
ATOM   395  N N     . ASN A 1 53  ? 23.524  12.695  6.077  1.00 19.51 ?  53  ASN A N     1 
ATOM   396  C CA    . ASN A 1 53  ? 22.508  11.646  6.074  1.00 19.38 ?  53  ASN A CA    1 
ATOM   397  C C     . ASN A 1 53  ? 23.170  10.308  5.769  1.00 24.63 ?  53  ASN A C     1 
ATOM   398  O O     . ASN A 1 53  ? 23.683  10.096  4.664  1.00 19.16 ?  53  ASN A O     1 
ATOM   399  C CB    . ASN A 1 53  ? 21.414  11.963  5.059  1.00 21.08 ?  53  ASN A CB    1 
ATOM   400  C CG    . ASN A 1 53  ? 20.167  11.121  5.263  1.00 21.65 ?  53  ASN A CG    1 
ATOM   401  O OD1   . ASN A 1 53  ? 20.197  10.103  5.953  1.00 19.27 ?  53  ASN A OD1   1 
ATOM   402  N ND2   . ASN A 1 53  ? 19.061  11.549  4.663  1.00 23.75 ?  53  ASN A ND2   1 
ATOM   403  N N     . LEU A 1 54  ? 23.156  9.401   6.748  1.00 19.88 ?  54  LEU A N     1 
ATOM   404  C CA    . LEU A 1 54  ? 23.710  8.068   6.556  1.00 16.96 ?  54  LEU A CA    1 
ATOM   405  C C     . LEU A 1 54  ? 22.917  7.246   5.549  1.00 20.97 ?  54  LEU A C     1 
ATOM   406  O O     . LEU A 1 54  ? 23.398  6.188   5.125  1.00 21.64 ?  54  LEU A O     1 
ATOM   407  C CB    . LEU A 1 54  ? 23.774  7.328   7.894  1.00 20.39 ?  54  LEU A CB    1 
ATOM   408  C CG    . LEU A 1 54  ? 24.750  7.900   8.928  1.00 23.51 ?  54  LEU A CG    1 
ATOM   409  C CD1   . LEU A 1 54  ? 24.542  7.238   10.281 1.00 17.51 ?  54  LEU A CD1   1 
ATOM   410  C CD2   . LEU A 1 54  ? 26.189  7.742   8.460  1.00 21.73 ?  54  LEU A CD2   1 
ATOM   411  N N     . GLN A 1 55  ? 21.717  7.701   5.172  1.00 21.88 ?  55  GLN A N     1 
ATOM   412  C CA    . GLN A 1 55  ? 20.918  6.985   4.182  1.00 29.32 ?  55  GLN A CA    1 
ATOM   413  C C     . GLN A 1 55  ? 21.672  6.810   2.870  1.00 28.67 ?  55  GLN A C     1 
ATOM   414  O O     . GLN A 1 55  ? 21.430  5.838   2.142  1.00 32.38 ?  55  GLN A O     1 
ATOM   415  C CB    . GLN A 1 55  ? 19.596  7.715   3.946  1.00 24.66 ?  55  GLN A CB    1 
ATOM   416  C CG    . GLN A 1 55  ? 18.543  6.885   3.226  1.00 33.73 ?  55  GLN A CG    1 
ATOM   417  C CD    . GLN A 1 55  ? 17.764  5.988   4.170  1.00 44.65 ?  55  GLN A CD    1 
ATOM   418  O OE1   . GLN A 1 55  ? 17.622  6.287   5.355  1.00 40.13 ?  55  GLN A OE1   1 
ATOM   419  N NE2   . GLN A 1 55  ? 17.253  4.880   3.645  1.00 49.23 ?  55  GLN A NE2   1 
ATOM   420  N N     . GLN A 1 56  ? 22.573  7.744   2.544  1.00 23.82 ?  56  GLN A N     1 
ATOM   421  C CA    . GLN A 1 56  ? 23.275  7.707   1.265  1.00 28.87 ?  56  GLN A CA    1 
ATOM   422  C C     . GLN A 1 56  ? 24.034  6.404   1.054  1.00 33.61 ?  56  GLN A C     1 
ATOM   423  O O     . GLN A 1 56  ? 24.295  6.033   -0.096 1.00 33.18 ?  56  GLN A O     1 
ATOM   424  C CB    . GLN A 1 56  ? 24.248  8.887   1.157  1.00 29.47 ?  56  GLN A CB    1 
ATOM   425  C CG    . GLN A 1 56  ? 25.444  8.804   2.100  1.00 30.42 ?  56  GLN A CG    1 
ATOM   426  C CD    . GLN A 1 56  ? 26.292  10.064  2.093  1.00 33.94 ?  56  GLN A CD    1 
ATOM   427  O OE1   . GLN A 1 56  ? 26.008  11.023  2.811  1.00 30.02 ?  56  GLN A OE1   1 
ATOM   428  N NE2   . GLN A 1 56  ? 27.341  10.065  1.279  1.00 33.46 ?  56  GLN A NE2   1 
ATOM   429  N N     . PHE A 1 57  ? 24.393  5.704   2.126  1.00 31.26 ?  57  PHE A N     1 
ATOM   430  C CA    . PHE A 1 57  ? 25.242  4.527   2.029  1.00 34.59 ?  57  PHE A CA    1 
ATOM   431  C C     . PHE A 1 57  ? 24.463  3.246   1.761  1.00 32.95 ?  57  PHE A C     1 
ATOM   432  O O     . PHE A 1 57  ? 25.081  2.189   1.596  1.00 27.66 ?  57  PHE A O     1 
ATOM   433  C CB    . PHE A 1 57  ? 26.078  4.381   3.304  1.00 25.42 ?  57  PHE A CB    1 
ATOM   434  C CG    . PHE A 1 57  ? 27.072  5.488   3.498  1.00 29.37 ?  57  PHE A CG    1 
ATOM   435  C CD1   . PHE A 1 57  ? 28.204  5.567   2.704  1.00 24.67 ?  57  PHE A CD1   1 
ATOM   436  C CD2   . PHE A 1 57  ? 26.862  6.464   4.457  1.00 29.37 ?  57  PHE A CD2   1 
ATOM   437  C CE1   . PHE A 1 57  ? 29.116  6.593   2.873  1.00 24.04 ?  57  PHE A CE1   1 
ATOM   438  C CE2   . PHE A 1 57  ? 27.771  7.493   4.630  1.00 25.62 ?  57  PHE A CE2   1 
ATOM   439  C CZ    . PHE A 1 57  ? 28.898  7.556   3.837  1.00 31.31 ?  57  PHE A CZ    1 
ATOM   440  N N     . TYR A 1 58  ? 23.136  3.309   1.714  1.00 32.93 ?  58  TYR A N     1 
ATOM   441  C CA    . TYR A 1 58  ? 22.357  2.141   1.344  1.00 35.00 ?  58  TYR A CA    1 
ATOM   442  C C     . TYR A 1 58  ? 22.432  1.931   -0.165 1.00 39.21 ?  58  TYR A C     1 
ATOM   443  O O     . TYR A 1 58  ? 22.781  2.836   -0.925 1.00 35.22 ?  58  TYR A O     1 
ATOM   444  C CB    . TYR A 1 58  ? 20.901  2.294   1.789  1.00 38.37 ?  58  TYR A CB    1 
ATOM   445  C CG    . TYR A 1 58  ? 20.638  1.888   3.223  1.00 37.70 ?  58  TYR A CG    1 
ATOM   446  C CD1   . TYR A 1 58  ? 20.795  0.570   3.632  1.00 40.82 ?  58  TYR A CD1   1 
ATOM   447  C CD2   . TYR A 1 58  ? 20.226  2.822   4.165  1.00 35.84 ?  58  TYR A CD2   1 
ATOM   448  C CE1   . TYR A 1 58  ? 20.555  0.194   4.940  1.00 36.92 ?  58  TYR A CE1   1 
ATOM   449  C CE2   . TYR A 1 58  ? 19.982  2.455   5.477  1.00 40.82 ?  58  TYR A CE2   1 
ATOM   450  C CZ    . TYR A 1 58  ? 20.149  1.140   5.856  1.00 39.11 ?  58  TYR A CZ    1 
ATOM   451  O OH    . TYR A 1 58  ? 19.909  0.766   7.159  1.00 46.99 ?  58  TYR A OH    1 
ATOM   452  N N     . ALA A 1 59  ? 22.116  0.712   -0.593 1.00 43.65 ?  59  ALA A N     1 
ATOM   453  C CA    . ALA A 1 59  ? 22.156  0.377   -2.013 1.00 46.34 ?  59  ALA A CA    1 
ATOM   454  C C     . ALA A 1 59  ? 21.218  1.281   -2.803 1.00 47.88 ?  59  ALA A C     1 
ATOM   455  O O     . ALA A 1 59  ? 20.035  1.409   -2.473 1.00 49.68 ?  59  ALA A O     1 
ATOM   456  C CB    . ALA A 1 59  ? 21.782  -1.093  -2.219 1.00 49.24 ?  59  ALA A CB    1 
ATOM   457  N N     . GLN A 1 60  ? 21.752  1.918   -3.842 1.00 48.27 ?  60  GLN A N     1 
ATOM   458  C CA    . GLN A 1 60  ? 21.005  2.857   -4.669 1.00 53.88 ?  60  GLN A CA    1 
ATOM   459  C C     . GLN A 1 60  ? 20.753  2.263   -6.048 1.00 54.86 ?  60  GLN A C     1 
ATOM   460  O O     . GLN A 1 60  ? 21.690  1.823   -6.715 1.00 51.90 ?  60  GLN A O     1 
ATOM   461  C CB    . GLN A 1 60  ? 21.782  4.165   -4.824 1.00 50.27 ?  60  GLN A CB    1 
ATOM   462  C CG    . GLN A 1 60  ? 22.354  4.725   -3.535 1.00 50.73 ?  60  GLN A CG    1 
ATOM   463  C CD    . GLN A 1 60  ? 21.320  5.441   -2.702 1.00 41.86 ?  60  GLN A CD    1 
ATOM   464  O OE1   . GLN A 1 60  ? 20.551  6.252   -3.215 1.00 34.95 ?  60  GLN A OE1   1 
ATOM   465  N NE2   . GLN A 1 60  ? 21.302  5.156   -1.405 1.00 39.77 ?  60  GLN A NE2   1 
ATOM   466  N N     . ASN A 1 61  ? 19.502  2.308   -6.499 1.00 60.59 ?  61  ASN A N     1 
ATOM   467  C CA    . ASN A 1 61  ? 19.180  2.050   -7.898 1.00 57.66 ?  61  ASN A CA    1 
ATOM   468  C C     . ASN A 1 61  ? 19.445  0.591   -8.256 1.00 52.55 ?  61  ASN A C     1 
ATOM   469  O O     . ASN A 1 61  ? 20.240  0.305   -9.158 1.00 53.60 ?  61  ASN A O     1 
ATOM   470  C CB    . ASN A 1 61  ? 19.984  2.976   -8.819 1.00 59.81 ?  61  ASN A CB    1 
ATOM   471  C CG    . ASN A 1 61  ? 19.877  4.435   -8.422 1.00 58.07 ?  61  ASN A CG    1 
ATOM   472  O OD1   . ASN A 1 61  ? 19.051  4.806   -7.594 1.00 55.55 ?  61  ASN A OD1   1 
ATOM   473  N ND2   . ASN A 1 61  ? 20.734  5.270   -9.005 1.00 61.02 ?  61  ASN A ND2   1 
ATOM   474  N N     . GLY A 1 62  ? 18.796  -0.338  -7.551 1.00 48.47 ?  62  GLY A N     1 
ATOM   475  C CA    . GLY A 1 62  ? 18.840  -1.746  -7.902 1.00 46.24 ?  62  GLY A CA    1 
ATOM   476  C C     . GLY A 1 62  ? 20.167  -2.455  -7.736 1.00 37.62 ?  62  GLY A C     1 
ATOM   477  O O     . GLY A 1 62  ? 20.253  -3.643  -8.071 1.00 29.16 ?  62  GLY A O     1 
ATOM   478  N N     . GLU A 1 63  ? 21.198  -1.784  -7.231 1.00 39.66 ?  63  GLU A N     1 
ATOM   479  C CA    . GLU A 1 63  ? 22.518  -2.395  -7.128 1.00 35.70 ?  63  GLU A CA    1 
ATOM   480  C C     . GLU A 1 63  ? 22.533  -3.499  -6.080 1.00 38.68 ?  63  GLU A C     1 
ATOM   481  O O     . GLU A 1 63  ? 21.857  -3.412  -5.053 1.00 34.59 ?  63  GLU A O     1 
ATOM   482  C CB    . GLU A 1 63  ? 23.575  -1.364  -6.743 1.00 38.49 ?  63  GLU A CB    1 
ATOM   483  C CG    . GLU A 1 63  ? 23.132  -0.462  -5.617 1.00 46.23 ?  63  GLU A CG    1 
ATOM   484  C CD    . GLU A 1 63  ? 24.058  0.716   -5.406 1.00 51.97 ?  63  GLU A CD    1 
ATOM   485  O OE1   . GLU A 1 63  ? 24.262  1.487   -6.365 1.00 44.64 ?  63  GLU A OE1   1 
ATOM   486  O OE2   . GLU A 1 63  ? 24.561  0.888   -4.279 1.00 52.77 -1 63  GLU A OE2   1 
ATOM   487  N N     . VAL A 1 64  ? 23.308  -4.544  -6.346 1.00 27.36 ?  64  VAL A N     1 
ATOM   488  C CA    . VAL A 1 64  ? 23.498  -5.621  -5.382 1.00 34.48 ?  64  VAL A CA    1 
ATOM   489  C C     . VAL A 1 64  ? 24.515  -5.140  -4.354 1.00 35.99 ?  64  VAL A C     1 
ATOM   490  O O     . VAL A 1 64  ? 25.659  -4.826  -4.701 1.00 29.47 ?  64  VAL A O     1 
ATOM   491  C CB    . VAL A 1 64  ? 23.987  -6.902  -6.074 1.00 31.39 ?  64  VAL A CB    1 
ATOM   492  C CG1   . VAL A 1 64  ? 24.628  -7.846  -5.067 1.00 32.31 ?  64  VAL A CG1   1 
ATOM   493  C CG2   . VAL A 1 64  ? 22.863  -7.565  -6.844 1.00 32.38 ?  64  VAL A CG2   1 
ATOM   494  N N     . LYS A 1 65  ? 24.106  -5.076  -3.088 1.00 34.40 ?  65  LYS A N     1 
ATOM   495  C CA    . LYS A 1 65  ? 25.011  -4.612  -2.040 1.00 31.13 ?  65  LYS A CA    1 
ATOM   496  C C     . LYS A 1 65  ? 24.650  -5.271  -0.719 1.00 33.90 ?  65  LYS A C     1 
ATOM   497  O O     . LYS A 1 65  ? 23.516  -5.141  -0.245 1.00 28.71 ?  65  LYS A O     1 
ATOM   498  C CB    . LYS A 1 65  ? 24.966  -3.088  -1.910 1.00 32.05 ?  65  LYS A CB    1 
ATOM   499  C CG    . LYS A 1 65  ? 25.998  -2.514  -0.954 1.00 29.96 ?  65  LYS A CG    1 
ATOM   500  C CD    . LYS A 1 65  ? 25.947  -0.996  -0.923 1.00 35.42 ?  65  LYS A CD    1 
ATOM   501  C CE    . LYS A 1 65  ? 27.033  -0.418  -0.029 1.00 29.78 ?  65  LYS A CE    1 
ATOM   502  N NZ    . LYS A 1 65  ? 27.150  1.061   -0.176 1.00 24.75 ?  65  LYS A NZ    1 
ATOM   503  N N     . ASN A 1 66  ? 25.619  -5.975  -0.136 1.00 30.88 ?  66  ASN A N     1 
ATOM   504  C CA    . ASN A 1 66  ? 25.468  -6.515  1.207  1.00 28.99 ?  66  ASN A CA    1 
ATOM   505  C C     . ASN A 1 66  ? 25.251  -5.384  2.206  1.00 33.94 ?  66  ASN A C     1 
ATOM   506  O O     . ASN A 1 66  ? 25.978  -4.384  2.195  1.00 27.31 ?  66  ASN A O     1 
ATOM   507  C CB    . ASN A 1 66  ? 26.709  -7.325  1.583  1.00 29.77 ?  66  ASN A CB    1 
ATOM   508  C CG    . ASN A 1 66  ? 26.463  -8.273  2.740  1.00 31.05 ?  66  ASN A CG    1 
ATOM   509  O OD1   . ASN A 1 66  ? 25.992  -7.869  3.802  1.00 28.53 ?  66  ASN A OD1   1 
ATOM   510  N ND2   . ASN A 1 66  ? 26.786  -9.547  2.538  1.00 26.64 ?  66  ASN A ND2   1 
ATOM   511  N N     . ARG A 1 67  ? 24.241  -5.540  3.068  1.00 33.28 ?  67  ARG A N     1 
ATOM   512  C CA    . ARG A 1 67  ? 23.987  -4.527  4.087  1.00 34.36 ?  67  ARG A CA    1 
ATOM   513  C C     . ARG A 1 67  ? 25.158  -4.375  5.050  1.00 29.38 ?  67  ARG A C     1 
ATOM   514  O O     . ARG A 1 67  ? 25.289  -3.321  5.685  1.00 27.61 ?  67  ARG A O     1 
ATOM   515  C CB    . ARG A 1 67  ? 22.709  -4.855  4.861  1.00 31.67 ?  67  ARG A CB    1 
ATOM   516  C CG    . ARG A 1 67  ? 21.824  -3.640  5.118  1.00 42.63 ?  67  ARG A CG    1 
ATOM   517  C CD    . ARG A 1 67  ? 20.344  -3.941  4.932  1.00 40.44 ?  67  ARG A CD    1 
ATOM   518  N NE    . ARG A 1 67  ? 19.995  -5.276  5.401  1.00 41.73 ?  67  ARG A NE    1 
ATOM   519  C CZ    . ARG A 1 67  ? 19.145  -6.086  4.785  1.00 44.34 ?  67  ARG A CZ    1 
ATOM   520  N NH1   . ARG A 1 67  ? 18.506  -5.713  3.688  1.00 42.59 ?  67  ARG A NH1   1 
ATOM   521  N NH2   . ARG A 1 67  ? 18.929  -7.302  5.280  1.00 42.09 ?  67  ARG A NH2   1 
ATOM   522  N N     . ARG A 1 68  ? 26.009  -5.400  5.176  1.00 28.49 ?  68  ARG A N     1 
ATOM   523  C CA    . ARG A 1 68  ? 27.160  -5.288  6.064  1.00 30.64 ?  68  ARG A CA    1 
ATOM   524  C C     . ARG A 1 68  ? 28.180  -4.293  5.525  1.00 31.38 ?  68  ARG A C     1 
ATOM   525  O O     . ARG A 1 68  ? 28.899  -3.658  6.307  1.00 32.12 ?  68  ARG A O     1 
ATOM   526  C CB    . ARG A 1 68  ? 27.810  -6.655  6.267  1.00 27.76 ?  68  ARG A CB    1 
ATOM   527  C CG    . ARG A 1 68  ? 27.048  -7.570  7.212  1.00 37.89 ?  68  ARG A CG    1 
ATOM   528  C CD    . ARG A 1 68  ? 27.704  -8.937  7.314  1.00 42.56 ?  68  ARG A CD    1 
ATOM   529  N NE    . ARG A 1 68  ? 26.738  -9.986  7.617  1.00 44.76 ?  68  ARG A NE    1 
ATOM   530  C CZ    . ARG A 1 68  ? 26.665  -10.620 8.780  1.00 55.86 ?  68  ARG A CZ    1 
ATOM   531  N NH1   . ARG A 1 68  ? 27.490  -10.335 9.774  1.00 61.10 ?  68  ARG A NH1   1 
ATOM   532  N NH2   . ARG A 1 68  ? 25.741  -11.562 8.951  1.00 61.95 ?  68  ARG A NH2   1 
ATOM   533  N N     . ASP A 1 69  ? 28.260  -4.142  4.200  1.00 26.80 ?  69  ASP A N     1 
ATOM   534  C CA    . ASP A 1 69  ? 29.128  -3.120  3.627  1.00 29.04 ?  69  ASP A CA    1 
ATOM   535  C C     . ASP A 1 69  ? 28.526  -1.735  3.806  1.00 27.18 ?  69  ASP A C     1 
ATOM   536  O O     . ASP A 1 69  ? 29.263  -0.754  3.958  1.00 27.58 ?  69  ASP A O     1 
ATOM   537  C CB    . ASP A 1 69  ? 29.386  -3.411  2.149  1.00 31.70 ?  69  ASP A CB    1 
ATOM   538  C CG    . ASP A 1 69  ? 30.090  -4.732  1.934  1.00 33.10 ?  69  ASP A CG    1 
ATOM   539  O OD1   . ASP A 1 69  ? 31.020  -5.041  2.708  1.00 30.72 ?  69  ASP A OD1   1 
ATOM   540  O OD2   . ASP A 1 69  ? 29.719  -5.461  0.990  1.00 37.11 -1 69  ASP A OD2   1 
ATOM   541  N N     . THR A 1 70  ? 27.194  -1.640  3.774  1.00 27.94 ?  70  THR A N     1 
ATOM   542  C CA    . THR A 1 70  ? 26.528  -0.376  4.070  1.00 26.29 ?  70  THR A CA    1 
ATOM   543  C C     . THR A 1 70  ? 26.890  0.109   5.467  1.00 26.23 ?  70  THR A C     1 
ATOM   544  O O     . THR A 1 70  ? 27.303  1.261   5.650  1.00 22.85 ?  70  THR A O     1 
ATOM   545  C CB    . THR A 1 70  ? 25.016  -0.539  3.933  1.00 27.83 ?  70  THR A CB    1 
ATOM   546  O OG1   . THR A 1 70  ? 24.680  -0.750  2.559  1.00 29.92 ?  70  THR A OG1   1 
ATOM   547  C CG2   . THR A 1 70  ? 24.292  0.700   4.441  1.00 31.04 ?  70  THR A CG2   1 
ATOM   548  N N     . TYR A 1 71  ? 26.738  -0.765  6.468  1.00 25.34 ?  71  TYR A N     1 
ATOM   549  C CA    . TYR A 1 71  ? 26.971  -0.370  7.853  1.00 24.98 ?  71  TYR A CA    1 
ATOM   550  C C     . TYR A 1 71  ? 28.432  -0.011  8.084  1.00 26.86 ?  71  TYR A C     1 
ATOM   551  O O     . TYR A 1 71  ? 28.736  0.942   8.813  1.00 24.76 ?  71  TYR A O     1 
ATOM   552  C CB    . TYR A 1 71  ? 26.542  -1.493  8.794  1.00 27.40 ?  71  TYR A CB    1 
ATOM   553  C CG    . TYR A 1 71  ? 25.080  -1.862  8.686  1.00 29.95 ?  71  TYR A CG    1 
ATOM   554  C CD1   . TYR A 1 71  ? 24.124  -0.908  8.364  1.00 29.38 ?  71  TYR A CD1   1 
ATOM   555  C CD2   . TYR A 1 71  ? 24.658  -3.169  8.890  1.00 33.99 ?  71  TYR A CD2   1 
ATOM   556  C CE1   . TYR A 1 71  ? 22.786  -1.243  8.258  1.00 31.83 ?  71  TYR A CE1   1 
ATOM   557  C CE2   . TYR A 1 71  ? 23.325  -3.514  8.789  1.00 37.50 ?  71  TYR A CE2   1 
ATOM   558  C CZ    . TYR A 1 71  ? 22.395  -2.548  8.472  1.00 34.72 ?  71  TYR A CZ    1 
ATOM   559  O OH    . TYR A 1 71  ? 21.066  -2.892  8.369  1.00 42.14 ?  71  TYR A OH    1 
ATOM   560  N N     . GLU A 1 72  ? 29.348  -0.782  7.491  1.00 26.19 ?  72  GLU A N     1 
ATOM   561  C CA    . GLU A 1 72  ? 30.770  -0.469  7.596  1.00 23.43 ?  72  GLU A CA    1 
ATOM   562  C C     . GLU A 1 72  ? 31.057  0.939   7.092  1.00 24.75 ?  72  GLU A C     1 
ATOM   563  O O     . GLU A 1 72  ? 31.811  1.693   7.720  1.00 24.12 ?  72  GLU A O     1 
ATOM   564  C CB    . GLU A 1 72  ? 31.594  -1.495  6.818  1.00 27.01 ?  72  GLU A CB    1 
ATOM   565  C CG    . GLU A 1 72  ? 33.091  -1.224  6.816  1.00 28.19 ?  72  GLU A CG    1 
ATOM   566  C CD    . GLU A 1 72  ? 33.673  -1.139  8.214  1.00 31.13 ?  72  GLU A CD    1 
ATOM   567  O OE1   . GLU A 1 72  ? 33.203  -1.879  9.105  1.00 31.06 ?  72  GLU A OE1   1 
ATOM   568  O OE2   . GLU A 1 72  ? 34.602  -0.328  8.424  1.00 32.02 -1 72  GLU A OE2   1 
ATOM   569  N N     . GLN A 1 73  ? 30.468  1.307   5.952  1.00 21.92 ?  73  GLN A N     1 
ATOM   570  C CA    . GLN A 1 73  ? 30.679  2.642   5.404  1.00 24.72 ?  73  GLN A CA    1 
ATOM   571  C C     . GLN A 1 73  ? 30.091  3.714   6.315  1.00 26.01 ?  73  GLN A C     1 
ATOM   572  O O     . GLN A 1 73  ? 30.666  4.802   6.450  1.00 23.82 ?  73  GLN A O     1 
ATOM   573  C CB    . GLN A 1 73  ? 30.090  2.722   3.997  1.00 26.97 ?  73  GLN A CB    1 
ATOM   574  C CG    . GLN A 1 73  ? 30.906  1.948   2.966  1.00 28.60 ?  73  GLN A CG    1 
ATOM   575  C CD    . GLN A 1 73  ? 30.155  1.707   1.671  1.00 33.99 ?  73  GLN A CD    1 
ATOM   576  O OE1   . GLN A 1 73  ? 29.154  2.362   1.388  1.00 27.74 ?  73  GLN A OE1   1 
ATOM   577  N NE2   . GLN A 1 73  ? 30.639  0.758   0.876  1.00 36.04 ?  73  GLN A NE2   1 
ATOM   578  N N     . MET A 1 74  ? 28.947  3.432   6.946  1.00 22.01 ?  74  MET A N     1 
ATOM   579  C CA    . MET A 1 74  ? 28.403  4.365   7.930  1.00 23.48 ?  74  MET A CA    1 
ATOM   580  C C     . MET A 1 74  ? 29.368  4.537   9.095  1.00 20.13 ?  74  MET A C     1 
ATOM   581  O O     . MET A 1 74  ? 29.670  5.663   9.510  1.00 20.69 ?  74  MET A O     1 
ATOM   582  C CB    . MET A 1 74  ? 27.044  3.886   8.441  1.00 20.18 ?  74  MET A CB    1 
ATOM   583  C CG    . MET A 1 74  ? 25.929  3.872   7.412  1.00 24.47 ?  74  MET A CG    1 
ATOM   584  S SD    . MET A 1 74  ? 24.528  2.897   7.995  1.00 31.58 ?  74  MET A SD    1 
ATOM   585  C CE    . MET A 1 74  ? 23.273  3.323   6.792  1.00 25.93 ?  74  MET A CE    1 
ATOM   586  N N     . VAL A 1 75  ? 29.854  3.419   9.641  1.00 23.11 ?  75  VAL A N     1 
ATOM   587  C CA    . VAL A 1 75  ? 30.752  3.466   10.792 1.00 24.13 ?  75  VAL A CA    1 
ATOM   588  C C     . VAL A 1 75  ? 32.022  4.229   10.439 1.00 23.95 ?  75  VAL A C     1 
ATOM   589  O O     . VAL A 1 75  ? 32.519  5.042   11.228 1.00 25.61 ?  75  VAL A O     1 
ATOM   590  C CB    . VAL A 1 75  ? 31.062  2.038   11.283 1.00 20.76 ?  75  VAL A CB    1 
ATOM   591  C CG1   . VAL A 1 75  ? 32.286  2.024   12.185 1.00 22.59 ?  75  VAL A CG1   1 
ATOM   592  C CG2   . VAL A 1 75  ? 29.853  1.444   11.988 1.00 21.60 ?  75  VAL A CG2   1 
ATOM   593  N N     . ASN A 1 76  ? 32.561  3.983   9.244  1.00 20.94 ?  76  ASN A N     1 
ATOM   594  C CA    . ASN A 1 76  ? 33.793  4.648   8.832  1.00 24.79 ?  76  ASN A CA    1 
ATOM   595  C C     . ASN A 1 76  ? 33.582  6.148   8.666  1.00 23.56 ?  76  ASN A C     1 
ATOM   596  O O     . ASN A 1 76  ? 34.454  6.946   9.030  1.00 23.85 ?  76  ASN A O     1 
ATOM   597  C CB    . ASN A 1 76  ? 34.313  4.030   7.535  1.00 24.82 ?  76  ASN A CB    1 
ATOM   598  C CG    . ASN A 1 76  ? 35.517  4.763   6.982  1.00 30.25 ?  76  ASN A CG    1 
ATOM   599  O OD1   . ASN A 1 76  ? 35.464  5.326   5.887  1.00 38.70 ?  76  ASN A OD1   1 
ATOM   600  N ND2   . ASN A 1 76  ? 36.610  4.762   7.735  1.00 25.37 ?  76  ASN A ND2   1 
ATOM   601  N N     . ALA A 1 77  ? 32.436  6.549   8.110  1.00 23.95 ?  77  ALA A N     1 
ATOM   602  C CA    . ALA A 1 77  ? 32.153  7.970   7.940  1.00 21.36 ?  77  ALA A CA    1 
ATOM   603  C C     . ALA A 1 77  ? 32.033  8.667   9.289  1.00 22.43 ?  77  ALA A C     1 
ATOM   604  O O     . ALA A 1 77  ? 32.510  9.795   9.458  1.00 19.48 ?  77  ALA A O     1 
ATOM   605  C CB    . ALA A 1 77  ? 30.876  8.159   7.122  1.00 23.34 ?  77  ALA A CB    1 
ATOM   606  N N     . ILE A 1 78  ? 31.393  8.010   10.260 1.00 21.88 ?  78  ILE A N     1 
ATOM   607  C CA    . ILE A 1 78  ? 31.277  8.581   11.600 1.00 17.38 ?  78  ILE A CA    1 
ATOM   608  C C     . ILE A 1 78  ? 32.659  8.755   12.213 1.00 21.63 ?  78  ILE A C     1 
ATOM   609  O O     . ILE A 1 78  ? 32.987  9.811   12.766 1.00 20.27 ?  78  ILE A O     1 
ATOM   610  C CB    . ILE A 1 78  ? 30.377  7.700   12.486 1.00 21.27 ?  78  ILE A CB    1 
ATOM   611  C CG1   . ILE A 1 78  ? 28.940  7.696   11.960 1.00 23.18 ?  78  ILE A CG1   1 
ATOM   612  C CG2   . ILE A 1 78  ? 30.426  8.163   13.933 1.00 24.49 ?  78  ILE A CG2   1 
ATOM   613  C CD1   . ILE A 1 78  ? 28.095  6.569   12.511 1.00 22.07 ?  78  ILE A CD1   1 
ATOM   614  N N     . LEU A 1 79  ? 33.489  7.712   12.125 1.00 19.51 ?  79  LEU A N     1 
ATOM   615  C CA    . LEU A 1 79  ? 34.805  7.749   12.751 1.00 22.96 ?  79  LEU A CA    1 
ATOM   616  C C     . LEU A 1 79  ? 35.719  8.769   12.083 1.00 19.82 ?  79  LEU A C     1 
ATOM   617  O O     . LEU A 1 79  ? 36.602  9.331   12.743 1.00 20.01 ?  79  LEU A O     1 
ATOM   618  C CB    . LEU A 1 79  ? 35.439  6.357   12.720 1.00 18.56 ?  79  LEU A CB    1 
ATOM   619  C CG    . LEU A 1 79  ? 35.248  5.487   13.970 1.00 25.46 ?  79  LEU A CG    1 
ATOM   620  C CD1   . LEU A 1 79  ? 36.086  6.015   15.125 1.00 23.64 ?  79  LEU A CD1   1 
ATOM   621  C CD2   . LEU A 1 79  ? 33.782  5.386   14.369 1.00 22.10 ?  79  LEU A CD2   1 
ATOM   622  N N     . ASP A 1 80  ? 35.529  9.019   10.782 1.00 20.67 ?  80  ASP A N     1 
ATOM   623  C CA    . ASP A 1 80  ? 36.347  10.017  10.095 1.00 22.35 ?  80  ASP A CA    1 
ATOM   624  C C     . ASP A 1 80  ? 36.158  11.399  10.707 1.00 23.64 ?  80  ASP A C     1 
ATOM   625  O O     . ASP A 1 80  ? 37.126  12.150  10.879 1.00 20.70 ?  80  ASP A O     1 
ATOM   626  C CB    . ASP A 1 80  ? 36.013  10.047  8.603  1.00 20.15 ?  80  ASP A CB    1 
ATOM   627  C CG    . ASP A 1 80  ? 36.764  8.997   7.815  1.00 26.95 ?  80  ASP A CG    1 
ATOM   628  O OD1   . ASP A 1 80  ? 37.671  8.356   8.387  1.00 26.10 ?  80  ASP A OD1   1 
ATOM   629  O OD2   . ASP A 1 80  ? 36.456  8.816   6.618  1.00 32.34 -1 80  ASP A OD2   1 
ATOM   630  N N     . ALA A 1 81  ? 34.915  11.759  11.030 1.00 20.30 ?  81  ALA A N     1 
ATOM   631  C CA    . ALA A 1 81  ? 34.664  13.052  11.659 1.00 19.11 ?  81  ALA A CA    1 
ATOM   632  C C     . ALA A 1 81  ? 35.281  13.104  13.049 1.00 19.84 ?  81  ALA A C     1 
ATOM   633  O O     . ALA A 1 81  ? 35.801  14.145  13.468 1.00 21.05 ?  81  ALA A O     1 
ATOM   634  C CB    . ALA A 1 81  ? 33.162  13.322  11.724 1.00 18.83 ?  81  ALA A CB    1 
ATOM   635  N N     . VAL A 1 82  ? 35.237  11.984  13.773 1.00 21.22 ?  82  VAL A N     1 
ATOM   636  C CA    . VAL A 1 82  ? 35.820  11.927  15.111 1.00 22.34 ?  82  VAL A CA    1 
ATOM   637  C C     . VAL A 1 82  ? 37.334  12.065  15.032 1.00 17.84 ?  82  VAL A C     1 
ATOM   638  O O     . VAL A 1 82  ? 37.943  12.848  15.771 1.00 22.07 ?  82  VAL A O     1 
ATOM   639  C CB    . VAL A 1 82  ? 35.408  10.624  15.820 1.00 21.03 ?  82  VAL A CB    1 
ATOM   640  C CG1   . VAL A 1 82  ? 36.234  10.408  17.077 1.00 20.30 ?  82  VAL A CG1   1 
ATOM   641  C CG2   . VAL A 1 82  ? 33.919  10.637  16.138 1.00 19.34 ?  82  VAL A CG2   1 
ATOM   642  N N     . ARG A 1 83  ? 37.961  11.302  14.130 1.00 21.50 ?  83  ARG A N     1 
ATOM   643  C CA    . ARG A 1 83  ? 39.411  11.362  13.966 1.00 23.00 ?  83  ARG A CA    1 
ATOM   644  C C     . ARG A 1 83  ? 39.869  12.761  13.570 1.00 24.45 ?  83  ARG A C     1 
ATOM   645  O O     . ARG A 1 83  ? 40.950  13.207  13.972 1.00 24.86 ?  83  ARG A O     1 
ATOM   646  C CB    . ARG A 1 83  ? 39.859  10.350  12.913 1.00 22.80 ?  83  ARG A CB    1 
ATOM   647  C CG    . ARG A 1 83  ? 39.728  8.894   13.325 1.00 23.96 ?  83  ARG A CG    1 
ATOM   648  C CD    . ARG A 1 83  ? 39.653  8.006   12.091 1.00 27.29 ?  83  ARG A CD    1 
ATOM   649  N NE    . ARG A 1 83  ? 39.309  6.627   12.413 1.00 27.16 ?  83  ARG A NE    1 
ATOM   650  C CZ    . ARG A 1 83  ? 38.703  5.795   11.576 1.00 27.50 ?  83  ARG A CZ    1 
ATOM   651  N NH1   . ARG A 1 83  ? 38.391  6.159   10.341 1.00 29.47 ?  83  ARG A NH1   1 
ATOM   652  N NH2   . ARG A 1 83  ? 38.414  4.561   11.980 1.00 24.57 ?  83  ARG A NH2   1 
ATOM   653  N N     . ALA A 1 84  ? 39.059  13.467  12.777 1.00 24.34 ?  84  ALA A N     1 
ATOM   654  C CA    . ALA A 1 84  ? 39.427  14.808  12.334 1.00 26.03 ?  84  ALA A CA    1 
ATOM   655  C C     . ALA A 1 84  ? 39.498  15.787  13.496 1.00 23.54 ?  84  ALA A C     1 
ATOM   656  O O     . ALA A 1 84  ? 40.224  16.783  13.421 1.00 25.07 ?  84  ALA A O     1 
ATOM   657  C CB    . ALA A 1 84  ? 38.435  15.304  11.283 1.00 23.16 ?  84  ALA A CB    1 
ATOM   658  N N     . GLY A 1 85  ? 38.754  15.528  14.568 1.00 21.28 ?  85  GLY A N     1 
ATOM   659  C CA    . GLY A 1 85  ? 38.718  16.404  15.729 1.00 20.10 ?  85  GLY A CA    1 
ATOM   660  C C     . GLY A 1 85  ? 37.338  16.919  16.075 1.00 22.95 ?  85  GLY A C     1 
ATOM   661  O O     . GLY A 1 85  ? 37.209  17.722  17.011 1.00 19.53 ?  85  GLY A O     1 
ATOM   662  N N     . LYS A 1 86  ? 36.300  16.495  15.361 1.00 19.48 ?  86  LYS A N     1 
ATOM   663  C CA    . LYS A 1 86  ? 34.964  17.045  15.535 1.00 20.65 ?  86  LYS A CA    1 
ATOM   664  C C     . LYS A 1 86  ? 34.254  16.412  16.724 1.00 23.80 ?  86  LYS A C     1 
ATOM   665  O O     . LYS A 1 86  ? 34.367  15.209  16.971 1.00 18.73 ?  86  LYS A O     1 
ATOM   666  C CB    . LYS A 1 86  ? 34.133  16.823  14.270 1.00 18.08 ?  86  LYS A CB    1 
ATOM   667  C CG    . LYS A 1 86  ? 34.797  17.301  12.992 1.00 22.61 ?  86  LYS A CG    1 
ATOM   668  C CD    . LYS A 1 86  ? 33.996  16.874  11.773 1.00 24.63 ?  86  LYS A CD    1 
ATOM   669  C CE    . LYS A 1 86  ? 34.633  17.362  10.483 1.00 29.31 ?  86  LYS A CE    1 
ATOM   670  N NZ    . LYS A 1 86  ? 34.466  18.830  10.313 1.00 34.52 ?  86  LYS A NZ    1 
ATOM   671  N N     . LYS A 1 87  ? 33.516  17.236  17.462 1.00 20.69 ?  87  LYS A N     1 
ATOM   672  C CA    . LYS A 1 87  ? 32.582  16.752  18.477 1.00 20.99 ?  87  LYS A CA    1 
ATOM   673  C C     . LYS A 1 87  ? 31.365  16.198  17.747 1.00 21.40 ?  87  LYS A C     1 
ATOM   674  O O     . LYS A 1 87  ? 30.486  16.948  17.317 1.00 19.65 ?  87  LYS A O     1 
ATOM   675  C CB    . LYS A 1 87  ? 32.208  17.869  19.446 1.00 21.37 ?  87  LYS A CB    1 
ATOM   676  C CG    . LYS A 1 87  ? 31.244  17.444  20.541 1.00 21.85 ?  87  LYS A CG    1 
ATOM   677  C CD    . LYS A 1 87  ? 30.993  18.562  21.541 1.00 23.65 ?  87  LYS A CD    1 
ATOM   678  C CE    . LYS A 1 87  ? 30.213  19.708  20.935 1.00 27.38 ?  87  LYS A CE    1 
ATOM   679  N NZ    . LYS A 1 87  ? 30.104  20.856  21.880 1.00 27.29 ?  87  LYS A NZ    1 
ATOM   680  N N     . THR A 1 88  ? 31.311  14.878  17.604 1.00 19.68 ?  88  THR A N     1 
ATOM   681  C CA    . THR A 1 88  ? 30.435  14.219  16.646 1.00 21.94 ?  88  THR A CA    1 
ATOM   682  C C     . THR A 1 88  ? 29.268  13.546  17.356 1.00 21.25 ?  88  THR A C     1 
ATOM   683  O O     . THR A 1 88  ? 29.448  12.895  18.390 1.00 18.75 ?  88  THR A O     1 
ATOM   684  C CB    . THR A 1 88  ? 31.216  13.179  15.834 1.00 23.85 ?  88  THR A CB    1 
ATOM   685  O OG1   . THR A 1 88  ? 32.356  13.807  15.235 1.00 22.50 ?  88  THR A OG1   1 
ATOM   686  C CG2   . THR A 1 88  ? 30.345  12.578  14.743 1.00 23.57 ?  88  THR A CG2   1 
ATOM   687  N N     . VAL A 1 89  ? 28.071  13.702  16.792 1.00 17.50 ?  89  VAL A N     1 
ATOM   688  C CA    . VAL A 1 89  ? 26.871  13.032  17.278 1.00 21.22 ?  89  VAL A CA    1 
ATOM   689  C C     . VAL A 1 89  ? 26.288  12.182  16.157 1.00 20.21 ?  89  VAL A C     1 
ATOM   690  O O     . VAL A 1 89  ? 26.204  12.622  15.006 1.00 23.05 ?  89  VAL A O     1 
ATOM   691  C CB    . VAL A 1 89  ? 25.824  14.043  17.798 1.00 19.95 ?  89  VAL A CB    1 
ATOM   692  C CG1   . VAL A 1 89  ? 24.471  13.370  18.001 1.00 22.30 ?  89  VAL A CG1   1 
ATOM   693  C CG2   . VAL A 1 89  ? 26.297  14.660  19.104 1.00 18.80 ?  89  VAL A CG2   1 
ATOM   694  N N     . CYS A 1 90  ? 25.891  10.959  16.496 1.00 22.62 ?  90  CYS A N     1 
ATOM   695  C CA    . CYS A 1 90  ? 25.113  10.099  15.614 1.00 22.83 ?  90  CYS A CA    1 
ATOM   696  C C     . CYS A 1 90  ? 23.685  10.044  16.144 1.00 25.89 ?  90  CYS A C     1 
ATOM   697  O O     . CYS A 1 90  ? 23.461  9.641   17.291 1.00 28.35 ?  90  CYS A O     1 
ATOM   698  C CB    . CYS A 1 90  ? 25.722  8.697   15.531 1.00 24.71 ?  90  CYS A CB    1 
ATOM   699  S SG    . CYS A 1 90  ? 24.738  7.506   14.595 1.00 31.84 ?  90  CYS A SG    1 
ATOM   700  N N     . ALA A 1 91  ? 22.729  10.461  15.321 1.00 26.52 ?  91  ALA A N     1 
ATOM   701  C CA    . ALA A 1 91  ? 21.317  10.503  15.695 1.00 24.06 ?  91  ALA A CA    1 
ATOM   702  C C     . ALA A 1 91  ? 20.566  9.436   14.904 1.00 20.03 ?  91  ALA A C     1 
ATOM   703  O O     . ALA A 1 91  ? 20.289  9.609   13.714 1.00 25.11 ?  91  ALA A O     1 
ATOM   704  C CB    . ALA A 1 91  ? 20.730  11.889  15.450 1.00 20.05 ?  91  ALA A CB    1 
ATOM   705  N N     . LEU A 1 92  ? 20.243  8.332   15.568 1.00 19.32 ?  92  LEU A N     1 
ATOM   706  C CA    . LEU A 1 92  ? 19.498  7.230   14.979 1.00 21.20 ?  92  LEU A CA    1 
ATOM   707  C C     . LEU A 1 92  ? 18.071  7.253   15.509 1.00 20.43 ?  92  LEU A C     1 
ATOM   708  O O     . LEU A 1 92  ? 17.799  7.776   16.591 1.00 26.42 ?  92  LEU A O     1 
ATOM   709  C CB    . LEU A 1 92  ? 20.150  5.879   15.301 1.00 21.40 ?  92  LEU A CB    1 
ATOM   710  C CG    . LEU A 1 92  ? 21.580  5.650   14.804 1.00 21.48 ?  92  LEU A CG    1 
ATOM   711  C CD1   . LEU A 1 92  ? 21.998  4.209   15.050 1.00 21.77 ?  92  LEU A CD1   1 
ATOM   712  C CD2   . LEU A 1 92  ? 21.710  6.006   13.338 1.00 20.16 ?  92  LEU A CD2   1 
ATOM   713  N N     . TYR A 1 93  ? 17.149  6.693   14.734 1.00 20.32 ?  93  TYR A N     1 
ATOM   714  C CA    . TYR A 1 93  ? 15.761  6.693   15.170 1.00 19.35 ?  93  TYR A CA    1 
ATOM   715  C C     . TYR A 1 93  ? 15.546  5.622   16.233 1.00 20.21 ?  93  TYR A C     1 
ATOM   716  O O     . TYR A 1 93  ? 16.194  4.569   16.230 1.00 19.54 ?  93  TYR A O     1 
ATOM   717  C CB    . TYR A 1 93  ? 14.810  6.493   13.983 1.00 21.43 ?  93  TYR A CB    1 
ATOM   718  C CG    . TYR A 1 93  ? 14.702  5.085   13.434 1.00 19.37 ?  93  TYR A CG    1 
ATOM   719  C CD1   . TYR A 1 93  ? 13.825  4.161   13.992 1.00 20.93 ?  93  TYR A CD1   1 
ATOM   720  C CD2   . TYR A 1 93  ? 15.458  4.689   12.337 1.00 19.11 ?  93  TYR A CD2   1 
ATOM   721  C CE1   . TYR A 1 93  ? 13.717  2.878   13.485 1.00 22.30 ?  93  TYR A CE1   1 
ATOM   722  C CE2   . TYR A 1 93  ? 15.356  3.408   11.824 1.00 20.03 ?  93  TYR A CE2   1 
ATOM   723  C CZ    . TYR A 1 93  ? 14.485  2.510   12.401 1.00 20.58 ?  93  TYR A CZ    1 
ATOM   724  O OH    . TYR A 1 93  ? 14.380  1.234   11.893 1.00 23.57 ?  93  TYR A OH    1 
ATOM   725  N N     . GLY A 1 94  ? 14.632  5.911   17.153 1.00 15.69 ?  94  GLY A N     1 
ATOM   726  C CA    . GLY A 1 94  ? 14.353  4.981   18.238 1.00 18.63 ?  94  GLY A CA    1 
ATOM   727  C C     . GLY A 1 94  ? 15.444  5.014   19.285 1.00 20.81 ?  94  GLY A C     1 
ATOM   728  O O     . GLY A 1 94  ? 15.877  6.085   19.719 1.00 16.57 ?  94  GLY A O     1 
ATOM   729  N N     . HIS A 1 95  ? 15.893  3.827   19.700 1.00 17.24 ?  95  HIS A N     1 
ATOM   730  C CA    . HIS A 1 95  ? 17.013  3.630   20.616 1.00 14.76 ?  95  HIS A CA    1 
ATOM   731  C C     . HIS A 1 95  ? 18.230  3.207   19.811 1.00 15.47 ?  95  HIS A C     1 
ATOM   732  O O     . HIS A 1 95  ? 18.154  2.226   19.058 1.00 16.31 ?  95  HIS A O     1 
ATOM   733  C CB    . HIS A 1 95  ? 16.652  2.563   21.651 1.00 13.69 ?  95  HIS A CB    1 
ATOM   734  C CG    . HIS A 1 95  ? 17.706  2.298   22.687 1.00 14.63 ?  95  HIS A CG    1 
ATOM   735  N ND1   . HIS A 1 95  ? 19.041  2.136   22.388 1.00 15.79 ?  95  HIS A ND1   1 
ATOM   736  C CD2   . HIS A 1 95  ? 17.604  2.137   24.029 1.00 13.82 ?  95  HIS A CD2   1 
ATOM   737  C CE1   . HIS A 1 95  ? 19.717  1.899   23.499 1.00 17.72 ?  95  HIS A CE1   1 
ATOM   738  N NE2   . HIS A 1 95  ? 18.868  1.894   24.509 1.00 16.32 ?  95  HIS A NE2   1 
ATOM   739  N N     . PRO A 1 96  ? 19.363  3.905   19.927 1.00 14.77 ?  96  PRO A N     1 
ATOM   740  C CA    . PRO A 1 96  ? 20.453  3.697   18.960 1.00 18.68 ?  96  PRO A CA    1 
ATOM   741  C C     . PRO A 1 96  ? 21.143  2.350   19.082 1.00 18.59 ?  96  PRO A C     1 
ATOM   742  O O     . PRO A 1 96  ? 21.840  1.948   18.143 1.00 20.62 ?  96  PRO A O     1 
ATOM   743  C CB    . PRO A 1 96  ? 21.417  4.850   19.276 1.00 18.71 ?  96  PRO A CB    1 
ATOM   744  C CG    . PRO A 1 96  ? 21.213  5.078   20.741 1.00 17.55 ?  96  PRO A CG    1 
ATOM   745  C CD    . PRO A 1 96  ? 19.725  4.907   20.945 1.00 15.16 ?  96  PRO A CD    1 
ATOM   746  N N     . GLY A 1 97  ? 20.979  1.644   20.196 1.00 14.89 ?  97  GLY A N     1 
ATOM   747  C CA    . GLY A 1 97  ? 21.621  0.359   20.381 1.00 21.61 ?  97  GLY A CA    1 
ATOM   748  C C     . GLY A 1 97  ? 20.674  -0.818  20.424 1.00 21.46 ?  97  GLY A C     1 
ATOM   749  O O     . GLY A 1 97  ? 21.052  -1.910  20.856 1.00 23.42 ?  97  GLY A O     1 
ATOM   750  N N     . VAL A 1 98  ? 19.438  -0.612  19.985 1.00 18.60 ?  98  VAL A N     1 
ATOM   751  C CA    . VAL A 1 98  ? 18.415  -1.654  19.983 1.00 21.58 ?  98  VAL A CA    1 
ATOM   752  C C     . VAL A 1 98  ? 18.217  -2.106  18.543 1.00 21.69 ?  98  VAL A C     1 
ATOM   753  O O     . VAL A 1 98  ? 17.721  -1.343  17.703 1.00 18.81 ?  98  VAL A O     1 
ATOM   754  C CB    . VAL A 1 98  ? 17.099  -1.170  20.607 1.00 23.65 ?  98  VAL A CB    1 
ATOM   755  C CG1   . VAL A 1 98  ? 15.979  -2.150  20.311 1.00 19.42 ?  98  VAL A CG1   1 
ATOM   756  C CG2   . VAL A 1 98  ? 17.266  -1.005  22.110 1.00 19.64 ?  98  VAL A CG2   1 
ATOM   757  N N     . PHE A 1 99  ? 18.602  -3.353  18.268 1.00 20.61 ?  99  PHE A N     1 
ATOM   758  C CA    . PHE A 1 99  ? 18.589  -3.923  16.921 1.00 19.97 ?  99  PHE A CA    1 
ATOM   759  C C     . PHE A 1 99  ? 19.216  -2.961  15.917 1.00 20.86 ?  99  PHE A C     1 
ATOM   760  O O     . PHE A 1 99  ? 18.671  -2.689  14.850 1.00 20.73 ?  99  PHE A O     1 
ATOM   761  C CB    . PHE A 1 99  ? 17.169  -4.306  16.503 1.00 18.81 ?  99  PHE A CB    1 
ATOM   762  C CG    . PHE A 1 99  ? 16.649  -5.540  17.187 1.00 16.92 ?  99  PHE A CG    1 
ATOM   763  C CD1   . PHE A 1 99  ? 16.176  -5.480  18.486 1.00 15.58 ?  99  PHE A CD1   1 
ATOM   764  C CD2   . PHE A 1 99  ? 16.639  -6.760  16.532 1.00 19.53 ?  99  PHE A CD2   1 
ATOM   765  C CE1   . PHE A 1 99  ? 15.699  -6.610  19.120 1.00 18.71 ?  99  PHE A CE1   1 
ATOM   766  C CE2   . PHE A 1 99  ? 16.162  -7.897  17.159 1.00 16.63 ?  99  PHE A CE2   1 
ATOM   767  C CZ    . PHE A 1 99  ? 15.692  -7.821  18.456 1.00 17.35 ?  99  PHE A CZ    1 
ATOM   768  N N     . ALA A 1 100 ? 20.385  -2.440  16.275 1.00 21.58 ?  100 ALA A N     1 
ATOM   769  C CA    . ALA A 1 100 ? 21.126  -1.534  15.409 1.00 20.35 ?  100 ALA A CA    1 
ATOM   770  C C     . ALA A 1 100 ? 22.604  -1.666  15.735 1.00 26.31 ?  100 ALA A C     1 
ATOM   771  O O     . ALA A 1 100 ? 22.998  -1.526  16.897 1.00 32.09 ?  100 ALA A O     1 
ATOM   772  C CB    . ALA A 1 100 ? 20.661  -0.086  15.586 1.00 23.09 ?  100 ALA A CB    1 
ATOM   773  N N     . CYS A 1 101 ? 23.415  -1.949  14.719 1.00 25.50 ?  101 CYS A N     1 
ATOM   774  C CA    . CYS A 1 101 ? 24.822  -2.225  14.955 1.00 30.11 ?  101 CYS A CA    1 
ATOM   775  C C     . CYS A 1 101 ? 25.708  -1.001  14.785 1.00 23.07 ?  101 CYS A C     1 
ATOM   776  O O     . CYS A 1 101 ? 26.760  -0.935  15.429 1.00 27.63 ?  101 CYS A O     1 
ATOM   777  C CB    . CYS A 1 101 ? 25.311  -3.330  14.009 1.00 30.14 ?  101 CYS A CB    1 
ATOM   778  S SG    . CYS A 1 101 ? 25.141  -2.930  12.256 1.00 35.37 ?  101 CYS A SG    1 
ATOM   779  N N     . VAL A 1 102 ? 25.272  -0.011  13.999 1.00 25.78 ?  102 VAL A N     1 
ATOM   780  C CA    . VAL A 1 102 ? 26.163  1.069   13.577 1.00 23.29 ?  102 VAL A CA    1 
ATOM   781  C C     . VAL A 1 102 ? 26.752  1.784   14.786 1.00 20.66 ?  102 VAL A C     1 
ATOM   782  O O     . VAL A 1 102 ? 27.962  2.029   14.853 1.00 23.54 ?  102 VAL A O     1 
ATOM   783  C CB    . VAL A 1 102 ? 25.418  2.043   12.646 1.00 23.27 ?  102 VAL A CB    1 
ATOM   784  C CG1   . VAL A 1 102 ? 26.188  3.351   12.508 1.00 19.45 ?  102 VAL A CG1   1 
ATOM   785  C CG2   . VAL A 1 102 ? 25.186  1.403   11.286 1.00 23.50 ?  102 VAL A CG2   1 
ATOM   786  N N     . SER A 1 103 ? 25.910  2.119   15.766 1.00 17.64 ?  103 SER A N     1 
ATOM   787  C CA    . SER A 1 103 ? 26.388  2.897   16.905 1.00 20.50 ?  103 SER A CA    1 
ATOM   788  C C     . SER A 1 103 ? 27.277  2.060   17.817 1.00 18.86 ?  103 SER A C     1 
ATOM   789  O O     . SER A 1 103 ? 28.289  2.559   18.326 1.00 19.12 ?  103 SER A O     1 
ATOM   790  C CB    . SER A 1 103 ? 25.205  3.476   17.683 1.00 20.00 ?  103 SER A CB    1 
ATOM   791  O OG    . SER A 1 103 ? 24.565  4.494   16.935 1.00 24.94 ?  103 SER A OG    1 
ATOM   792  N N     . HIS A 1 104 ? 26.914  0.791   18.043 1.00 16.86 ?  104 HIS A N     1 
ATOM   793  C CA    . HIS A 1 104 ? 27.771  -0.084  18.842 1.00 21.56 ?  104 HIS A CA    1 
ATOM   794  C C     . HIS A 1 104 ? 29.140  -0.255  18.192 1.00 18.46 ?  104 HIS A C     1 
ATOM   795  O O     . HIS A 1 104 ? 30.170  -0.199  18.876 1.00 15.89 ?  104 HIS A O     1 
ATOM   796  C CB    . HIS A 1 104 ? 27.108  -1.447  19.048 1.00 20.09 ?  104 HIS A CB    1 
ATOM   797  C CG    . HIS A 1 104 ? 25.999  -1.443  20.058 1.00 20.13 ?  104 HIS A CG    1 
ATOM   798  N ND1   . HIS A 1 104 ? 26.207  -1.183  21.395 1.00 16.38 ?  104 HIS A ND1   1 
ATOM   799  C CD2   . HIS A 1 104 ? 24.675  -1.701  19.930 1.00 19.40 ?  104 HIS A CD2   1 
ATOM   800  C CE1   . HIS A 1 104 ? 25.059  -1.262  22.045 1.00 17.94 ?  104 HIS A CE1   1 
ATOM   801  N NE2   . HIS A 1 104 ? 24.113  -1.575  21.178 1.00 19.04 ?  104 HIS A NE2   1 
ATOM   802  N N     . MET A 1 105 ? 29.170  -0.457  16.869 1.00 19.48 ?  105 MET A N     1 
ATOM   803  C CA    . MET A 1 105 ? 30.446  -0.615  16.176 1.00 18.97 ?  105 MET A CA    1 
ATOM   804  C C     . MET A 1 105 ? 31.243  0.682   16.191 1.00 21.44 ?  105 MET A C     1 
ATOM   805  O O     . MET A 1 105 ? 32.467  0.665   16.372 1.00 20.97 ?  105 MET A O     1 
ATOM   806  C CB    . MET A 1 105 ? 30.225  -1.075  14.735 1.00 24.53 ?  105 MET A CB    1 
ATOM   807  C CG    . MET A 1 105 ? 29.254  -2.228  14.562 1.00 27.77 ?  105 MET A CG    1 
ATOM   808  S SD    . MET A 1 105 ? 28.831  -2.511  12.831 1.00 31.58 ?  105 MET A SD    1 
ATOM   809  C CE    . MET A 1 105 ? 30.325  -3.283  12.221 1.00 30.26 ?  105 MET A CE    1 
ATOM   810  N N     . ALA A 1 106 ? 30.567  1.816   15.996 1.00 16.41 ?  106 ALA A N     1 
ATOM   811  C CA    . ALA A 1 106 ? 31.258  3.101   16.016 1.00 17.36 ?  106 ALA A CA    1 
ATOM   812  C C     . ALA A 1 106 ? 31.865  3.371   17.385 1.00 20.29 ?  106 ALA A C     1 
ATOM   813  O O     . ALA A 1 106 ? 33.002  3.844   17.487 1.00 20.81 ?  106 ALA A O     1 
ATOM   814  C CB    . ALA A 1 106 ? 30.296  4.221   15.623 1.00 16.51 ?  106 ALA A CB    1 
ATOM   815  N N     . ILE A 1 107 ? 31.121  3.069   18.452 1.00 18.27 ?  107 ILE A N     1 
ATOM   816  C CA    . ILE A 1 107 ? 31.621  3.314   19.800 1.00 19.17 ?  107 ILE A CA    1 
ATOM   817  C C     . ILE A 1 107 ? 32.781  2.379   20.115 1.00 19.14 ?  107 ILE A C     1 
ATOM   818  O O     . ILE A 1 107 ? 33.793  2.798   20.689 1.00 19.81 ?  107 ILE A O     1 
ATOM   819  C CB    . ILE A 1 107 ? 30.481  3.175   20.824 1.00 15.67 ?  107 ILE A CB    1 
ATOM   820  C CG1   . ILE A 1 107 ? 29.510  4.352   20.700 1.00 16.03 ?  107 ILE A CG1   1 
ATOM   821  C CG2   . ILE A 1 107 ? 31.027  3.079   22.236 1.00 21.92 ?  107 ILE A CG2   1 
ATOM   822  C CD1   . ILE A 1 107 ? 28.286  4.215   21.565 1.00 16.41 ?  107 ILE A CD1   1 
ATOM   823  N N     . THR A 1 108 ? 32.653  1.101   19.750 1.00 21.83 ?  108 THR A N     1 
ATOM   824  C CA    . THR A 1 108 ? 33.744  0.153   19.962 1.00 22.03 ?  108 THR A CA    1 
ATOM   825  C C     . THR A 1 108 ? 35.007  0.609   19.245 1.00 21.86 ?  108 THR A C     1 
ATOM   826  O O     . THR A 1 108 ? 36.104  0.593   19.818 1.00 24.44 ?  108 THR A O     1 
ATOM   827  C CB    . THR A 1 108 ? 33.333  -1.240  19.483 1.00 21.67 ?  108 THR A CB    1 
ATOM   828  O OG1   . THR A 1 108 ? 32.292  -1.749  20.323 1.00 21.59 ?  108 THR A OG1   1 
ATOM   829  C CG2   . THR A 1 108 ? 34.519  -2.195  19.523 1.00 25.16 ?  108 THR A CG2   1 
ATOM   830  N N     . ARG A 1 109 ? 34.867  1.035   17.987 1.00 21.98 ?  109 ARG A N     1 
ATOM   831  C CA    . ARG A 1 109 ? 36.031  1.444   17.209 1.00 26.95 ?  109 ARG A CA    1 
ATOM   832  C C     . ARG A 1 109 ? 36.621  2.740   17.753 1.00 23.74 ?  109 ARG A C     1 
ATOM   833  O O     . ARG A 1 109 ? 37.847  2.893   17.817 1.00 23.71 ?  109 ARG A O     1 
ATOM   834  C CB    . ARG A 1 109 ? 35.654  1.591   15.735 1.00 26.54 ?  109 ARG A CB    1 
ATOM   835  C CG    . ARG A 1 109 ? 36.840  1.636   14.783 1.00 24.31 ?  109 ARG A CG    1 
ATOM   836  C CD    . ARG A 1 109 ? 36.402  1.533   13.326 1.00 25.74 ?  109 ARG A CD    1 
ATOM   837  N NE    . ARG A 1 109 ? 35.637  0.318   13.066 1.00 26.58 ?  109 ARG A NE    1 
ATOM   838  C CZ    . ARG A 1 109 ? 35.131  -0.006  11.883 1.00 29.08 ?  109 ARG A CZ    1 
ATOM   839  N NH1   . ARG A 1 109 ? 35.292  0.773   10.824 1.00 25.82 ?  109 ARG A NH1   1 
ATOM   840  N NH2   . ARG A 1 109 ? 34.447  -1.140  11.755 1.00 32.55 ?  109 ARG A NH2   1 
ATOM   841  N N     . ALA A 1 110 ? 35.762  3.690   18.133 1.00 20.99 ?  110 ALA A N     1 
ATOM   842  C CA    . ALA A 1 110 ? 36.245  4.958   18.675 1.00 19.36 ?  110 ALA A CA    1 
ATOM   843  C C     . ALA A 1 110 ? 37.026  4.746   19.967 1.00 21.29 ?  110 ALA A C     1 
ATOM   844  O O     . ALA A 1 110 ? 38.091  5.346   20.162 1.00 21.00 ?  110 ALA A O     1 
ATOM   845  C CB    . ALA A 1 110 ? 35.075  5.913   18.907 1.00 19.43 ?  110 ALA A CB    1 
ATOM   846  N N     . LYS A 1 111 ? 36.510  3.894   20.861 1.00 21.93 ?  111 LYS A N     1 
ATOM   847  C CA    . LYS A 1 111 ? 37.194  3.641   22.127 1.00 25.12 ?  111 LYS A CA    1 
ATOM   848  C C     . LYS A 1 111 ? 38.565  3.017   21.897 1.00 25.62 ?  111 LYS A C     1 
ATOM   849  O O     . LYS A 1 111 ? 39.519  3.309   22.626 1.00 26.87 ?  111 LYS A O     1 
ATOM   850  C CB    . LYS A 1 111 ? 36.351  2.728   23.017 1.00 25.72 ?  111 LYS A CB    1 
ATOM   851  C CG    . LYS A 1 111 ? 35.222  3.401   23.777 1.00 27.47 ?  111 LYS A CG    1 
ATOM   852  C CD    . LYS A 1 111 ? 34.410  2.351   24.527 1.00 28.36 ?  111 LYS A CD    1 
ATOM   853  C CE    . LYS A 1 111 ? 33.135  2.910   25.133 1.00 24.67 ?  111 LYS A CE    1 
ATOM   854  N NZ    . LYS A 1 111 ? 33.393  4.019   26.086 1.00 40.32 ?  111 LYS A NZ    1 
ATOM   855  N N     . ALA A 1 112 ? 38.682  2.149   20.889 1.00 25.96 ?  112 ALA A N     1 
ATOM   856  C CA    . ALA A 1 112 ? 39.943  1.462   20.641 1.00 24.96 ?  112 ALA A CA    1 
ATOM   857  C C     . ALA A 1 112 ? 40.995  2.390   20.058 1.00 23.63 ?  112 ALA A C     1 
ATOM   858  O O     . ALA A 1 112 ? 42.192  2.120   20.205 1.00 28.73 ?  112 ALA A O     1 
ATOM   859  C CB    . ALA A 1 112 ? 39.718  0.269   19.708 1.00 26.95 ?  112 ALA A CB    1 
ATOM   860  N N     . GLU A 1 113 ? 40.578  3.472   19.404 1.00 24.05 ?  113 GLU A N     1 
ATOM   861  C CA    . GLU A 1 113 ? 41.500  4.453   18.855 1.00 21.05 ?  113 GLU A CA    1 
ATOM   862  C C     . GLU A 1 113 ? 41.748  5.609   19.814 1.00 24.41 ?  113 GLU A C     1 
ATOM   863  O O     . GLU A 1 113 ? 42.423  6.576   19.445 1.00 24.31 ?  113 GLU A O     1 
ATOM   864  C CB    . GLU A 1 113 ? 40.972  4.982   17.519 1.00 24.62 ?  113 GLU A CB    1 
ATOM   865  C CG    . GLU A 1 113 ? 40.998  3.961   16.391 1.00 27.39 ?  113 GLU A CG    1 
ATOM   866  C CD    . GLU A 1 113 ? 40.270  4.442   15.150 1.00 29.35 ?  113 GLU A CD    1 
ATOM   867  O OE1   . GLU A 1 113 ? 40.124  5.671   14.980 1.00 29.92 ?  113 GLU A OE1   1 
ATOM   868  O OE2   . GLU A 1 113 ? 39.845  3.589   14.341 1.00 31.97 -1 113 GLU A OE2   1 
ATOM   869  N N     . GLY A 1 114 ? 41.222  5.524   21.033 1.00 24.20 ?  114 GLY A N     1 
ATOM   870  C CA    . GLY A 1 114 ? 41.514  6.498   22.063 1.00 22.34 ?  114 GLY A CA    1 
ATOM   871  C C     . GLY A 1 114 ? 40.564  7.665   22.156 1.00 22.23 ?  114 GLY A C     1 
ATOM   872  O O     . GLY A 1 114 ? 40.898  8.663   22.803 1.00 20.58 ?  114 GLY A O     1 
ATOM   873  N N     . PHE A 1 115 ? 39.393  7.579   21.540 1.00 20.17 ?  115 PHE A N     1 
ATOM   874  C CA    . PHE A 1 115 ? 38.422  8.659   21.591 1.00 22.46 ?  115 PHE A CA    1 
ATOM   875  C C     . PHE A 1 115 ? 37.329  8.358   22.609 1.00 23.96 ?  115 PHE A C     1 
ATOM   876  O O     . PHE A 1 115 ? 36.945  7.205   22.819 1.00 23.69 ?  115 PHE A O     1 
ATOM   877  C CB    . PHE A 1 115 ? 37.796  8.899   20.214 1.00 20.95 ?  115 PHE A CB    1 
ATOM   878  C CG    . PHE A 1 115 ? 38.804  9.126   19.121 1.00 17.60 ?  115 PHE A CG    1 
ATOM   879  C CD1   . PHE A 1 115 ? 39.646  10.225  19.155 1.00 19.68 ?  115 PHE A CD1   1 
ATOM   880  C CD2   . PHE A 1 115 ? 38.909  8.240   18.062 1.00 24.34 ?  115 PHE A CD2   1 
ATOM   881  C CE1   . PHE A 1 115 ? 40.574  10.438  18.154 1.00 22.04 ?  115 PHE A CE1   1 
ATOM   882  C CE2   . PHE A 1 115 ? 39.837  8.447   17.054 1.00 20.95 ?  115 PHE A CE2   1 
ATOM   883  C CZ    . PHE A 1 115 ? 40.670  9.548   17.103 1.00 21.77 ?  115 PHE A CZ    1 
ATOM   884  N N     . SER A 1 116 ? 36.838  9.415   23.249 1.00 18.83 ?  116 SER A N     1 
ATOM   885  C CA    . SER A 1 116 ? 35.685  9.311   24.135 1.00 27.68 ?  116 SER A CA    1 
ATOM   886  C C     . SER A 1 116 ? 34.434  9.004   23.318 1.00 23.69 ?  116 SER A C     1 
ATOM   887  O O     . SER A 1 116 ? 34.103  9.736   22.379 1.00 18.83 ?  116 SER A O     1 
ATOM   888  C CB    . SER A 1 116 ? 35.513  10.608  24.928 1.00 20.30 ?  116 SER A CB    1 
ATOM   889  O OG    . SER A 1 116 ? 34.303  10.606  25.660 1.00 35.52 ?  116 SER A OG    1 
ATOM   890  N N     . ALA A 1 117 ? 33.738  7.925   23.671 1.00 26.85 ?  117 ALA A N     1 
ATOM   891  C CA    . ALA A 1 117 ? 32.515  7.537   22.984 1.00 21.74 ?  117 ALA A CA    1 
ATOM   892  C C     . ALA A 1 117 ? 31.493  7.034   23.993 1.00 19.96 ?  117 ALA A C     1 
ATOM   893  O O     . ALA A 1 117 ? 31.843  6.335   24.947 1.00 17.49 ?  117 ALA A O     1 
ATOM   894  C CB    . ALA A 1 117 ? 32.783  6.458   21.927 1.00 18.67 ?  117 ALA A CB    1 
ATOM   895  N N     . LYS A 1 118 ? 30.228  7.385   23.767 1.00 19.56 ?  118 LYS A N     1 
ATOM   896  C CA    . LYS A 1 118 ? 29.157  6.974   24.661 1.00 18.04 ?  118 LYS A CA    1 
ATOM   897  C C     . LYS A 1 118 ? 27.862  6.807   23.881 1.00 16.07 ?  118 LYS A C     1 
ATOM   898  O O     . LYS A 1 118 ? 27.717  7.299   22.760 1.00 16.12 ?  118 LYS A O     1 
ATOM   899  C CB    . LYS A 1 118 ? 28.964  7.991   25.789 1.00 19.21 ?  118 LYS A CB    1 
ATOM   900  C CG    . LYS A 1 118 ? 28.995  9.433   25.323 1.00 21.81 ?  118 LYS A CG    1 
ATOM   901  C CD    . LYS A 1 118 ? 29.395  10.336  26.465 1.00 41.73 ?  118 LYS A CD    1 
ATOM   902  C CE    . LYS A 1 118 ? 29.230  11.797  26.125 1.00 29.21 ?  118 LYS A CE    1 
ATOM   903  N NZ    . LYS A 1 118 ? 27.796  12.162  26.101 1.00 37.04 ?  118 LYS A NZ    1 
ATOM   904  N N     . MET A 1 119 ? 26.918  6.100   24.498 1.00 18.39 ?  119 MET A N     1 
ATOM   905  C CA    . MET A 1 119 ? 25.595  5.873   23.935 1.00 17.84 ?  119 MET A CA    1 
ATOM   906  C C     . MET A 1 119 ? 24.544  6.349   24.924 1.00 17.10 ?  119 MET A C     1 
ATOM   907  O O     . MET A 1 119 ? 24.579  5.975   26.101 1.00 18.14 ?  119 MET A O     1 
ATOM   908  C CB    . MET A 1 119 ? 25.374  4.395   23.613 1.00 19.83 ?  119 MET A CB    1 
ATOM   909  C CG    . MET A 1 119 ? 24.177  4.136   22.716 1.00 24.95 ?  119 MET A CG    1 
ATOM   910  S SD    . MET A 1 119 ? 23.746  2.390   22.632 1.00 23.31 ?  119 MET A SD    1 
ATOM   911  C CE    . MET A 1 119 ? 24.558  1.977   21.088 1.00 18.87 ?  119 MET A CE    1 
ATOM   912  N N     . GLU A 1 120 ? 23.622  7.167   24.447 1.00 20.87 ?  120 GLU A N     1 
ATOM   913  C CA    . GLU A 1 120 ? 22.509  7.608   25.277 1.00 21.05 ?  120 GLU A CA    1 
ATOM   914  C C     . GLU A 1 120 ? 21.263  6.824   24.902 1.00 22.81 ?  120 GLU A C     1 
ATOM   915  O O     . GLU A 1 120 ? 20.901  6.788   23.717 1.00 21.39 ?  120 GLU A O     1 
ATOM   916  C CB    . GLU A 1 120 ? 22.260  9.103   25.096 1.00 19.81 ?  120 GLU A CB    1 
ATOM   917  C CG    . GLU A 1 120 ? 23.297  9.989   25.773 1.00 25.18 ?  120 GLU A CG    1 
ATOM   918  C CD    . GLU A 1 120 ? 23.260  9.886   27.284 1.00 20.72 ?  120 GLU A CD    1 
ATOM   919  O OE1   . GLU A 1 120 ? 22.157  9.711   27.846 1.00 25.94 ?  120 GLU A OE1   1 
ATOM   920  O OE2   . GLU A 1 120 ? 24.335  9.983   27.914 1.00 26.18 -1 120 GLU A OE2   1 
ATOM   921  N N     . PRO A 1 121 ? 20.595  6.175   25.855 1.00 21.13 ?  121 PRO A N     1 
ATOM   922  C CA    . PRO A 1 121 ? 19.421  5.365   25.507 1.00 18.02 ?  121 PRO A CA    1 
ATOM   923  C C     . PRO A 1 121 ? 18.281  6.208   24.952 1.00 17.65 ?  121 PRO A C     1 
ATOM   924  O O     . PRO A 1 121 ? 18.149  7.397   25.250 1.00 16.57 ?  121 PRO A O     1 
ATOM   925  C CB    . PRO A 1 121 ? 19.035  4.708   26.838 1.00 21.69 ?  121 PRO A CB    1 
ATOM   926  C CG    . PRO A 1 121 ? 19.616  5.588   27.886 1.00 23.00 ?  121 PRO A CG    1 
ATOM   927  C CD    . PRO A 1 121 ? 20.874  6.165   27.302 1.00 19.40 ?  121 PRO A CD    1 
ATOM   928  N N     . GLY A 1 122 ? 17.457  5.565   24.124 1.00 17.28 ?  122 GLY A N     1 
ATOM   929  C CA    . GLY A 1 122 ? 16.298  6.200   23.535 1.00 18.50 ?  122 GLY A CA    1 
ATOM   930  C C     . GLY A 1 122 ? 15.076  5.304   23.640 1.00 18.56 ?  122 GLY A C     1 
ATOM   931  O O     . GLY A 1 122 ? 15.144  4.179   24.143 1.00 16.69 ?  122 GLY A O     1 
ATOM   932  N N     . ILE A 1 123 ? 13.957  5.835   23.156 1.00 16.76 ?  123 ILE A N     1 
ATOM   933  C CA    . ILE A 1 123 ? 12.687  5.117   23.167 1.00 14.82 ?  123 ILE A CA    1 
ATOM   934  C C     . ILE A 1 123 ? 12.576  4.311   21.879 1.00 22.91 ?  123 ILE A C     1 
ATOM   935  O O     . ILE A 1 123 ? 12.516  4.881   20.786 1.00 22.10 ?  123 ILE A O     1 
ATOM   936  C CB    . ILE A 1 123 ? 11.504  6.084   23.321 1.00 19.11 ?  123 ILE A CB    1 
ATOM   937  C CG1   . ILE A 1 123 ? 11.598  6.819   24.663 1.00 21.72 ?  123 ILE A CG1   1 
ATOM   938  C CG2   . ILE A 1 123 ? 10.185  5.342   23.196 1.00 17.65 ?  123 ILE A CG2   1 
ATOM   939  C CD1   . ILE A 1 123 ? 10.751  8.068   24.744 1.00 17.43 ?  123 ILE A CD1   1 
ATOM   940  N N     . SER A 1 124 ? 12.541  2.988   22.007 1.00 17.50 ?  124 SER A N     1 
ATOM   941  C CA    . SER A 1 124 ? 12.590  2.085   20.870 1.00 16.61 ?  124 SER A CA    1 
ATOM   942  C C     . SER A 1 124 ? 11.181  1.681   20.440 1.00 17.95 ?  124 SER A C     1 
ATOM   943  O O     . SER A 1 124 ? 10.179  2.044   21.059 1.00 17.55 ?  124 SER A O     1 
ATOM   944  C CB    . SER A 1 124 ? 13.426  0.847   21.210 1.00 15.45 ?  124 SER A CB    1 
ATOM   945  O OG    . SER A 1 124 ? 12.743  -0.000  22.113 1.00 19.16 ?  124 SER A OG    1 
ATOM   946  N N     . ALA A 1 125 ? 11.111  0.919   19.345 1.00 18.95 ?  125 ALA A N     1 
ATOM   947  C CA    . ALA A 1 125 ? 9.822   0.440   18.859 1.00 16.79 ?  125 ALA A CA    1 
ATOM   948  C C     . ALA A 1 125 ? 9.190   -0.528  19.845 1.00 19.65 ?  125 ALA A C     1 
ATOM   949  O O     . ALA A 1 125 ? 7.959   -0.584  19.957 1.00 18.70 ?  125 ALA A O     1 
ATOM   950  C CB    . ALA A 1 125 ? 9.987   -0.222  17.491 1.00 17.36 ?  125 ALA A CB    1 
ATOM   951  N N     . GLU A 1 126 ? 10.017  -1.299  20.557 1.00 18.05 ?  126 GLU A N     1 
ATOM   952  C CA    . GLU A 1 126 ? 9.505   -2.181  21.599 1.00 22.85 ?  126 GLU A CA    1 
ATOM   953  C C     . GLU A 1 126 ? 8.829   -1.381  22.704 1.00 22.13 ?  126 GLU A C     1 
ATOM   954  O O     . GLU A 1 126 ? 7.747   -1.750  23.179 1.00 21.44 ?  126 GLU A O     1 
ATOM   955  C CB    . GLU A 1 126 ? 10.645  -3.019  22.169 1.00 25.33 ?  126 GLU A CB    1 
ATOM   956  C CG    . GLU A 1 126 ? 10.256  -3.925  23.321 1.00 22.40 ?  126 GLU A CG    1 
ATOM   957  C CD    . GLU A 1 126 ? 11.420  -4.192  24.248 1.00 27.04 ?  126 GLU A CD    1 
ATOM   958  O OE1   . GLU A 1 126 ? 12.342  -4.929  23.844 1.00 33.11 ?  126 GLU A OE1   1 
ATOM   959  O OE2   . GLU A 1 126 ? 11.418  -3.661  25.381 1.00 35.90 -1 126 GLU A OE2   1 
ATOM   960  N N     . ALA A 1 127 ? 9.460   -0.284  23.137 1.00 20.22 ?  127 ALA A N     1 
ATOM   961  C CA    . ALA A 1 127 ? 8.857   0.561   24.162 1.00 16.69 ?  127 ALA A CA    1 
ATOM   962  C C     . ALA A 1 127 ? 7.535   1.142   23.681 1.00 16.54 ?  127 ALA A C     1 
ATOM   963  O O     . ALA A 1 127 ? 6.591   1.293   24.466 1.00 17.71 ?  127 ALA A O     1 
ATOM   964  C CB    . ALA A 1 127 ? 9.824   1.676   24.559 1.00 21.15 ?  127 ALA A CB    1 
ATOM   965  N N     . CYS A 1 128 ? 7.449   1.471   22.389 1.00 16.98 ?  128 CYS A N     1 
ATOM   966  C CA    . CYS A 1 128 ? 6.199   1.984   21.842 1.00 16.21 ?  128 CYS A CA    1 
ATOM   967  C C     . CYS A 1 128 ? 5.124   0.907   21.828 1.00 18.78 ?  128 CYS A C     1 
ATOM   968  O O     . CYS A 1 128 ? 3.939   1.212   22.018 1.00 19.99 ?  128 CYS A O     1 
ATOM   969  C CB    . CYS A 1 128 ? 6.423   2.532   20.432 1.00 12.70 ?  128 CYS A CB    1 
ATOM   970  S SG    . CYS A 1 128 ? 7.415   4.044   20.357 1.00 19.01 ?  128 CYS A SG    1 
ATOM   971  N N     . LEU A 1 129 ? 5.519   -0.352  21.610 1.00 14.86 ?  129 LEU A N     1 
ATOM   972  C CA    . LEU A 1 129 ? 4.550   -1.439  21.501 1.00 17.52 ?  129 LEU A CA    1 
ATOM   973  C C     . LEU A 1 129 ? 3.830   -1.671  22.823 1.00 18.45 ?  129 LEU A C     1 
ATOM   974  O O     . LEU A 1 129 ? 2.597   -1.761  22.859 1.00 15.30 ?  129 LEU A O     1 
ATOM   975  C CB    . LEU A 1 129 ? 5.248   -2.715  21.028 1.00 15.90 ?  129 LEU A CB    1 
ATOM   976  C CG    . LEU A 1 129 ? 4.395   -3.962  20.771 1.00 20.38 ?  129 LEU A CG    1 
ATOM   977  C CD1   . LEU A 1 129 ? 5.047   -4.798  19.691 1.00 14.34 ?  129 LEU A CD1   1 
ATOM   978  C CD2   . LEU A 1 129 ? 4.219   -4.803  22.030 1.00 17.70 ?  129 LEU A CD2   1 
ATOM   979  N N     . TRP A 1 130 ? 4.590   -1.802  23.916 1.00 17.10 ?  130 TRP A N     1 
ATOM   980  C CA    . TRP A 1 130 ? 3.986   -1.966  25.237 1.00 20.73 ?  130 TRP A CA    1 
ATOM   981  C C     . TRP A 1 130 ? 2.920   -0.907  25.492 1.00 18.50 ?  130 TRP A C     1 
ATOM   982  O O     . TRP A 1 130 ? 1.823   -1.210  25.975 1.00 17.38 ?  130 TRP A O     1 
ATOM   983  C CB    . TRP A 1 130 ? 5.060   -1.903  26.324 1.00 22.08 ?  130 TRP A CB    1 
ATOM   984  C CG    . TRP A 1 130 ? 6.231   -2.831  26.132 1.00 22.48 ?  130 TRP A CG    1 
ATOM   985  C CD1   . TRP A 1 130 ? 7.551   -2.508  26.265 1.00 18.30 ?  130 TRP A CD1   1 
ATOM   986  C CD2   . TRP A 1 130 ? 6.192   -4.226  25.791 1.00 18.69 ?  130 TRP A CD2   1 
ATOM   987  N NE1   . TRP A 1 130 ? 8.334   -3.609  26.021 1.00 20.82 ?  130 TRP A NE1   1 
ATOM   988  C CE2   . TRP A 1 130 ? 7.526   -4.675  25.728 1.00 21.23 ?  130 TRP A CE2   1 
ATOM   989  C CE3   . TRP A 1 130 ? 5.162   -5.137  25.530 1.00 17.15 ?  130 TRP A CE3   1 
ATOM   990  C CZ2   . TRP A 1 130 ? 7.858   -5.992  25.412 1.00 17.72 ?  130 TRP A CZ2   1 
ATOM   991  C CZ3   . TRP A 1 130 ? 5.494   -6.446  25.217 1.00 19.71 ?  130 TRP A CZ3   1 
ATOM   992  C CH2   . TRP A 1 130 ? 6.832   -6.860  25.163 1.00 18.41 ?  130 TRP A CH2   1 
ATOM   993  N N     . ALA A 1 131 ? 3.232   0.348   25.168 1.00 15.39 ?  131 ALA A N     1 
ATOM   994  C CA    . ALA A 1 131 ? 2.297   1.439   25.420 1.00 16.02 ?  131 ALA A CA    1 
ATOM   995  C C     . ALA A 1 131 ? 1.097   1.370   24.484 1.00 15.30 ?  131 ALA A C     1 
ATOM   996  O O     . ALA A 1 131 ? -0.045  1.557   24.918 1.00 16.66 ?  131 ALA A O     1 
ATOM   997  C CB    . ALA A 1 131 ? 3.010   2.784   25.278 1.00 20.54 ?  131 ALA A CB    1 
ATOM   998  N N     . ASP A 1 132 ? 1.335   1.095   23.197 1.00 15.93 ?  132 ASP A N     1 
ATOM   999  C CA    . ASP A 1 132 ? 0.251   1.133   22.219 1.00 18.82 ?  132 ASP A CA    1 
ATOM   1000 C C     . ASP A 1 132 ? -0.723  -0.018  22.426 1.00 18.88 ?  132 ASP A C     1 
ATOM   1001 O O     . ASP A 1 132 ? -1.930  0.137   22.218 1.00 19.07 ?  132 ASP A O     1 
ATOM   1002 C CB    . ASP A 1 132 ? 0.818   1.103   20.800 1.00 18.05 ?  132 ASP A CB    1 
ATOM   1003 C CG    . ASP A 1 132 ? 1.274   2.463   20.333 1.00 19.08 ?  132 ASP A CG    1 
ATOM   1004 O OD1   . ASP A 1 132 ? 0.888   3.466   20.970 1.00 22.52 ?  132 ASP A OD1   1 
ATOM   1005 O OD2   . ASP A 1 132 ? 2.012   2.536   19.328 1.00 19.51 -1 132 ASP A OD2   1 
ATOM   1006 N N     . LEU A 1 133 ? -0.221  -1.180  22.822 1.00 17.45 ?  133 LEU A N     1 
ATOM   1007 C CA    . LEU A 1 133 ? -1.046  -2.367  22.984 1.00 20.29 ?  133 LEU A CA    1 
ATOM   1008 C C     . LEU A 1 133 ? -1.500  -2.566  24.423 1.00 24.24 ?  133 LEU A C     1 
ATOM   1009 O O     . LEU A 1 133 ? -2.252  -3.506  24.698 1.00 24.13 ?  133 LEU A O     1 
ATOM   1010 C CB    . LEU A 1 133 ? -0.289  -3.609  22.494 1.00 22.83 ?  133 LEU A CB    1 
ATOM   1011 C CG    . LEU A 1 133 ? -0.327  -3.866  20.981 1.00 23.86 ?  133 LEU A CG    1 
ATOM   1012 C CD1   . LEU A 1 133 ? 0.434   -2.801  20.201 1.00 18.34 ?  133 LEU A CD1   1 
ATOM   1013 C CD2   . LEU A 1 133 ? 0.215   -5.238  20.665 1.00 22.85 ?  133 LEU A CD2   1 
ATOM   1014 N N     . GLY A 1 134 ? -1.076  -1.696  25.335 1.00 19.42 ?  134 GLY A N     1 
ATOM   1015 C CA    . GLY A 1 134 ? -1.386  -1.860  26.747 1.00 18.37 ?  134 GLY A CA    1 
ATOM   1016 C C     . GLY A 1 134 ? -0.855  -3.148  27.334 1.00 21.74 ?  134 GLY A C     1 
ATOM   1017 O O     . GLY A 1 134 ? -1.538  -3.790  28.142 1.00 19.99 ?  134 GLY A O     1 
ATOM   1018 N N     . ILE A 1 135 ? 0.358   -3.538  26.952 1.00 25.64 ?  135 ILE A N     1 
ATOM   1019 C CA    . ILE A 1 135 ? 0.991   -4.764  27.419 1.00 14.37 ?  135 ILE A CA    1 
ATOM   1020 C C     . ILE A 1 135 ? 2.209   -4.403  28.255 1.00 22.25 ?  135 ILE A C     1 
ATOM   1021 O O     . ILE A 1 135 ? 3.028   -3.573  27.846 1.00 21.08 ?  135 ILE A O     1 
ATOM   1022 C CB    . ILE A 1 135 ? 1.397   -5.670  26.244 1.00 16.98 ?  135 ILE A CB    1 
ATOM   1023 C CG1   . ILE A 1 135 ? 0.226   -5.847  25.274 1.00 23.75 ?  135 ILE A CG1   1 
ATOM   1024 C CG2   . ILE A 1 135 ? 1.922   -7.001  26.757 1.00 20.29 ?  135 ILE A CG2   1 
ATOM   1025 C CD1   . ILE A 1 135 ? 0.351   -7.058  24.374 1.00 27.72 ?  135 ILE A CD1   1 
ATOM   1026 N N     . ASP A 1 136 ? 2.336   -5.030  29.421 1.00 18.07 ?  136 ASP A N     1 
ATOM   1027 C CA    . ASP A 1 136 ? 3.538   -4.904  30.232 1.00 26.01 ?  136 ASP A CA    1 
ATOM   1028 C C     . ASP A 1 136 ? 4.424   -6.107  29.957 1.00 25.15 ?  136 ASP A C     1 
ATOM   1029 O O     . ASP A 1 136 ? 3.961   -7.247  30.126 1.00 23.13 ?  136 ASP A O     1 
ATOM   1030 C CB    . ASP A 1 136 ? 3.172   -4.827  31.717 1.00 23.54 ?  136 ASP A CB    1 
ATOM   1031 C CG    . ASP A 1 136 ? 4.385   -4.732  32.642 1.00 23.52 ?  136 ASP A CG    1 
ATOM   1032 O OD1   . ASP A 1 136 ? 5.541   -4.900  32.199 1.00 21.11 ?  136 ASP A OD1   1 
ATOM   1033 O OD2   . ASP A 1 136 ? 4.174   -4.477  33.845 1.00 27.87 -1 136 ASP A OD2   1 
ATOM   1034 N N     . PRO A 1 137 ? 5.675   -5.921  29.525 1.00 23.06 ?  137 PRO A N     1 
ATOM   1035 C CA    . PRO A 1 137 ? 6.546   -7.084  29.288 1.00 19.60 ?  137 PRO A CA    1 
ATOM   1036 C C     . PRO A 1 137 ? 6.722   -7.953  30.516 1.00 24.33 ?  137 PRO A C     1 
ATOM   1037 O O     . PRO A 1 137 ? 7.107   -9.122  30.386 1.00 20.45 ?  137 PRO A O     1 
ATOM   1038 C CB    . PRO A 1 137 ? 7.877   -6.451  28.854 1.00 24.17 ?  137 PRO A CB    1 
ATOM   1039 C CG    . PRO A 1 137 ? 7.804   -5.019  29.292 1.00 19.58 ?  137 PRO A CG    1 
ATOM   1040 C CD    . PRO A 1 137 ? 6.355   -4.645  29.247 1.00 20.34 ?  137 PRO A CD    1 
ATOM   1041 N N     . GLY A 1 138 ? 6.448   -7.418  31.709 1.00 23.08 ?  138 GLY A N     1 
ATOM   1042 C CA    . GLY A 1 138 ? 6.619   -8.175  32.935 1.00 22.79 ?  138 GLY A CA    1 
ATOM   1043 C C     . GLY A 1 138 ? 5.478   -9.109  33.260 1.00 24.28 ?  138 GLY A C     1 
ATOM   1044 O O     . GLY A 1 138 ? 5.654   -10.015 34.083 1.00 21.26 ?  138 GLY A O     1 
ATOM   1045 N N     . ASN A 1 139 ? 4.313   -8.894  32.642 1.00 22.79 ?  139 ASN A N     1 
ATOM   1046 C CA    . ASN A 1 139 ? 3.115   -9.655  32.983 1.00 28.96 ?  139 ASN A CA    1 
ATOM   1047 C C     . ASN A 1 139 ? 3.392   -11.154 32.937 1.00 21.97 ?  139 ASN A C     1 
ATOM   1048 O O     . ASN A 1 139 ? 3.187   -11.870 33.923 1.00 17.86 ?  139 ASN A O     1 
ATOM   1049 C CB    . ASN A 1 139 ? 1.966   -9.278  32.043 1.00 29.91 ?  139 ASN A CB    1 
ATOM   1050 C CG    . ASN A 1 139 ? 0.624   -9.801  32.522 1.00 30.63 ?  139 ASN A CG    1 
ATOM   1051 O OD1   . ASN A 1 139 ? 0.167   -9.462  33.614 1.00 34.42 ?  139 ASN A OD1   1 
ATOM   1052 N ND2   . ASN A 1 139 ? -0.022  -10.619 31.699 1.00 27.88 ?  139 ASN A ND2   1 
ATOM   1053 N N     . SER A 1 140 ? 3.871   -11.647 31.791 1.00 22.53 ?  140 SER A N     1 
ATOM   1054 C CA    . SER A 1 140 ? 4.247   -13.050 31.661 1.00 21.75 ?  140 SER A CA    1 
ATOM   1055 C C     . SER A 1 140 ? 5.608   -13.217 30.991 1.00 20.90 ?  140 SER A C     1 
ATOM   1056 O O     . SER A 1 140 ? 5.927   -14.311 30.517 1.00 26.73 ?  140 SER A O     1 
ATOM   1057 C CB    . SER A 1 140 ? 3.182   -13.834 30.890 1.00 18.85 ?  140 SER A CB    1 
ATOM   1058 O OG    . SER A 1 140 ? 2.886   -13.216 29.652 1.00 22.33 ?  140 SER A OG    1 
ATOM   1059 N N     . GLY A 1 141 ? 6.421   -12.165 30.951 1.00 20.64 ?  141 GLY A N     1 
ATOM   1060 C CA    . GLY A 1 141 ? 7.744   -12.239 30.369 1.00 19.76 ?  141 GLY A CA    1 
ATOM   1061 C C     . GLY A 1 141 ? 7.765   -11.827 28.907 1.00 16.35 ?  141 GLY A C     1 
ATOM   1062 O O     . GLY A 1 141 ? 6.737   -11.669 28.246 1.00 15.87 ?  141 GLY A O     1 
ATOM   1063 N N     . HIS A 1 142 ? 8.979   -11.676 28.387 1.00 22.66 ?  142 HIS A N     1 
ATOM   1064 C CA    . HIS A 1 142 ? 9.185   -11.053 27.087 1.00 20.51 ?  142 HIS A CA    1 
ATOM   1065 C C     . HIS A 1 142 ? 10.417  -11.656 26.424 1.00 15.87 ?  142 HIS A C     1 
ATOM   1066 O O     . HIS A 1 142 ? 11.456  -11.830 27.067 1.00 16.43 ?  142 HIS A O     1 
ATOM   1067 C CB    . HIS A 1 142 ? 9.326   -9.530  27.249 1.00 17.77 ?  142 HIS A CB    1 
ATOM   1068 C CG    . HIS A 1 142 ? 10.049  -8.850  26.128 1.00 20.82 ?  142 HIS A CG    1 
ATOM   1069 N ND1   . HIS A 1 142 ? 10.881  -7.773  26.340 1.00 21.13 ?  142 HIS A ND1   1 
ATOM   1070 C CD2   . HIS A 1 142 ? 10.038  -9.059  24.790 1.00 15.02 ?  142 HIS A CD2   1 
ATOM   1071 C CE1   . HIS A 1 142 ? 11.375  -7.366  25.185 1.00 24.38 ?  142 HIS A CE1   1 
ATOM   1072 N NE2   . HIS A 1 142 ? 10.880  -8.130  24.228 1.00 25.84 ?  142 HIS A NE2   1 
ATOM   1073 N N     . GLN A 1 143 ? 10.282  -11.978 25.138 1.00 20.84 ?  143 GLN A N     1 
ATOM   1074 C CA    . GLN A 1 143 ? 11.371  -12.474 24.310 1.00 23.05 ?  143 GLN A CA    1 
ATOM   1075 C C     . GLN A 1 143 ? 11.438  -11.673 23.019 1.00 20.84 ?  143 GLN A C     1 
ATOM   1076 O O     . GLN A 1 143 ? 10.411  -11.420 22.385 1.00 19.01 ?  143 GLN A O     1 
ATOM   1077 C CB    . GLN A 1 143 ? 11.177  -13.943 23.959 1.00 23.34 ?  143 GLN A CB    1 
ATOM   1078 C CG    . GLN A 1 143 ? 11.303  -14.918 25.099 1.00 30.45 ?  143 GLN A CG    1 
ATOM   1079 C CD    . GLN A 1 143 ? 11.213  -16.337 24.599 1.00 28.22 ?  143 GLN A CD    1 
ATOM   1080 O OE1   . GLN A 1 143 ? 12.157  -17.118 24.707 1.00 39.55 ?  143 GLN A OE1   1 
ATOM   1081 N NE2   . GLN A 1 143 ? 10.076  -16.666 24.003 1.00 27.26 ?  143 GLN A NE2   1 
ATOM   1082 N N     . SER A 1 144 ? 12.650  -11.290 22.623 1.00 14.99 ?  144 SER A N     1 
ATOM   1083 C CA    . SER A 1 144 ? 12.882  -10.637 21.340 1.00 20.08 ?  144 SER A CA    1 
ATOM   1084 C C     . SER A 1 144 ? 13.956  -11.389 20.568 1.00 20.46 ?  144 SER A C     1 
ATOM   1085 O O     . SER A 1 144 ? 14.997  -11.744 21.131 1.00 21.95 ?  144 SER A O     1 
ATOM   1086 C CB    . SER A 1 144 ? 13.293  -9.171  21.527 1.00 16.88 ?  144 SER A CB    1 
ATOM   1087 O OG    . SER A 1 144 ? 12.160  -8.346  21.730 1.00 19.59 ?  144 SER A OG    1 
ATOM   1088 N N     . PHE A 1 145 ? 13.700  -11.625 19.283 1.00 16.58 ?  145 PHE A N     1 
ATOM   1089 C CA    . PHE A 1 145 ? 14.701  -12.127 18.352 1.00 21.04 ?  145 PHE A CA    1 
ATOM   1090 C C     . PHE A 1 145 ? 14.558  -11.399 17.027 1.00 19.19 ?  145 PHE A C     1 
ATOM   1091 O O     . PHE A 1 145 ? 13.472  -10.938 16.671 1.00 19.52 ?  145 PHE A O     1 
ATOM   1092 C CB    . PHE A 1 145 ? 14.570  -13.632 18.061 1.00 15.13 ?  145 PHE A CB    1 
ATOM   1093 C CG    . PHE A 1 145 ? 14.492  -14.499 19.279 1.00 16.13 ?  145 PHE A CG    1 
ATOM   1094 C CD1   . PHE A 1 145 ? 15.645  -14.992 19.867 1.00 17.63 ?  145 PHE A CD1   1 
ATOM   1095 C CD2   . PHE A 1 145 ? 13.267  -14.852 19.816 1.00 18.52 ?  145 PHE A CD2   1 
ATOM   1096 C CE1   . PHE A 1 145 ? 15.577  -15.805 20.981 1.00 19.47 ?  145 PHE A CE1   1 
ATOM   1097 C CE2   . PHE A 1 145 ? 13.191  -15.665 20.932 1.00 25.22 ?  145 PHE A CE2   1 
ATOM   1098 C CZ    . PHE A 1 145 ? 14.348  -16.141 21.515 1.00 22.30 ?  145 PHE A CZ    1 
ATOM   1099 N N     . GLU A 1 146 ? 15.663  -11.299 16.299 1.00 17.95 ?  146 GLU A N     1 
ATOM   1100 C CA    . GLU A 1 146 ? 15.579  -10.946 14.890 1.00 19.08 ?  146 GLU A CA    1 
ATOM   1101 C C     . GLU A 1 146 ? 15.035  -12.145 14.123 1.00 19.20 ?  146 GLU A C     1 
ATOM   1102 O O     . GLU A 1 146 ? 15.436  -13.287 14.365 1.00 14.85 ?  146 GLU A O     1 
ATOM   1103 C CB    . GLU A 1 146 ? 16.954  -10.530 14.358 1.00 19.03 ?  146 GLU A CB    1 
ATOM   1104 C CG    . GLU A 1 146 ? 16.908  -9.588  13.160 1.00 19.72 ?  146 GLU A CG    1 
ATOM   1105 C CD    . GLU A 1 146 ? 17.137  -10.289 11.836 1.00 24.82 ?  146 GLU A CD    1 
ATOM   1106 O OE1   . GLU A 1 146 ? 17.543  -11.469 11.845 1.00 19.42 ?  146 GLU A OE1   1 
ATOM   1107 O OE2   . GLU A 1 146 ? 16.925  -9.650  10.783 1.00 20.84 -1 146 GLU A OE2   1 
ATOM   1108 N N     . ALA A 1 147 ? 14.095  -11.883 13.211 1.00 15.78 ?  147 ALA A N     1 
ATOM   1109 C CA    . ALA A 1 147 ? 13.334  -12.966 12.593 1.00 18.31 ?  147 ALA A CA    1 
ATOM   1110 C C     . ALA A 1 147 ? 14.243  -13.940 11.853 1.00 19.67 ?  147 ALA A C     1 
ATOM   1111 O O     . ALA A 1 147 ? 14.098  -15.160 11.983 1.00 19.58 ?  147 ALA A O     1 
ATOM   1112 C CB    . ALA A 1 147 ? 12.277  -12.392 11.650 1.00 17.62 ?  147 ALA A CB    1 
ATOM   1113 N N     . SER A 1 148 ? 15.193  -13.419 11.072 1.00 20.30 ?  148 SER A N     1 
ATOM   1114 C CA    . SER A 1 148 ? 16.055  -14.293 10.281 1.00 18.68 ?  148 SER A CA    1 
ATOM   1115 C C     . SER A 1 148 ? 16.985  -15.111 11.168 1.00 22.16 ?  148 SER A C     1 
ATOM   1116 O O     . SER A 1 148 ? 17.225  -16.294 10.894 1.00 18.06 ?  148 SER A O     1 
ATOM   1117 C CB    . SER A 1 148 ? 16.852  -13.469 9.271  1.00 20.37 ?  148 SER A CB    1 
ATOM   1118 O OG    . SER A 1 148 ? 16.017  -13.021 8.218  1.00 21.72 ?  148 SER A OG    1 
ATOM   1119 N N     . GLN A 1 149 ? 17.529  -14.500 12.227 1.00 20.06 ?  149 GLN A N     1 
ATOM   1120 C CA    . GLN A 1 149 ? 18.358  -15.260 13.159 1.00 20.89 ?  149 GLN A CA    1 
ATOM   1121 C C     . GLN A 1 149 ? 17.557  -16.393 13.784 1.00 20.67 ?  149 GLN A C     1 
ATOM   1122 O O     . GLN A 1 149 ? 18.086  -17.485 14.022 1.00 19.16 ?  149 GLN A O     1 
ATOM   1123 C CB    . GLN A 1 149 ? 18.926  -14.346 14.244 1.00 21.19 ?  149 GLN A CB    1 
ATOM   1124 C CG    . GLN A 1 149 ? 19.943  -15.032 15.147 1.00 27.00 ?  149 GLN A CG    1 
ATOM   1125 C CD    . GLN A 1 149 ? 20.343  -14.186 16.338 1.00 30.26 ?  149 GLN A CD    1 
ATOM   1126 O OE1   . GLN A 1 149 ? 19.872  -14.407 17.454 1.00 23.05 ?  149 GLN A OE1   1 
ATOM   1127 N NE2   . GLN A 1 149 ? 21.215  -13.210 16.107 1.00 21.89 ?  149 GLN A NE2   1 
ATOM   1128 N N     . PHE A 1 150 ? 16.272  -16.147 14.053 1.00 18.61 ?  150 PHE A N     1 
ATOM   1129 C CA    . PHE A 1 150 ? 15.406  -17.184 14.602 1.00 20.94 ?  150 PHE A CA    1 
ATOM   1130 C C     . PHE A 1 150 ? 15.287  -18.360 13.644 1.00 23.51 ?  150 PHE A C     1 
ATOM   1131 O O     . PHE A 1 150 ? 15.095  -19.502 14.079 1.00 24.85 ?  150 PHE A O     1 
ATOM   1132 C CB    . PHE A 1 150 ? 14.028  -16.595 14.912 1.00 12.73 ?  150 PHE A CB    1 
ATOM   1133 C CG    . PHE A 1 150 ? 13.116  -17.527 15.653 1.00 18.31 ?  150 PHE A CG    1 
ATOM   1134 C CD1   . PHE A 1 150 ? 13.156  -17.598 17.036 1.00 19.14 ?  150 PHE A CD1   1 
ATOM   1135 C CD2   . PHE A 1 150 ? 12.218  -18.329 14.970 1.00 18.65 ?  150 PHE A CD2   1 
ATOM   1136 C CE1   . PHE A 1 150 ? 12.317  -18.457 17.724 1.00 23.60 ?  150 PHE A CE1   1 
ATOM   1137 C CE2   . PHE A 1 150 ? 11.380  -19.190 15.652 1.00 23.26 ?  150 PHE A CE2   1 
ATOM   1138 C CZ    . PHE A 1 150 ? 11.429  -19.253 17.029 1.00 21.82 ?  150 PHE A CZ    1 
ATOM   1139 N N     . MET A 1 151 ? 15.392  -18.100 12.340 1.00 20.50 ?  151 MET A N     1 
ATOM   1140 C CA    . MET A 1 151 ? 15.302  -19.150 11.334 1.00 24.96 ?  151 MET A CA    1 
ATOM   1141 C C     . MET A 1 151 ? 16.650  -19.819 11.096 1.00 23.13 ?  151 MET A C     1 
ATOM   1142 O O     . MET A 1 151 ? 16.720  -21.044 10.953 1.00 24.05 ?  151 MET A O     1 
ATOM   1143 C CB    . MET A 1 151 ? 14.769  -18.578 10.016 1.00 22.85 ?  151 MET A CB    1 
ATOM   1144 C CG    . MET A 1 151 ? 13.331  -18.089 10.079 1.00 24.64 ?  151 MET A CG    1 
ATOM   1145 S SD    . MET A 1 151 ? 12.773  -17.356 8.528  1.00 22.84 ?  151 MET A SD    1 
ATOM   1146 C CE    . MET A 1 151 ? 12.623  -18.815 7.498  1.00 25.26 ?  151 MET A CE    1 
ATOM   1147 N N     . PHE A 1 152 ? 17.725  -19.027 11.063 1.00 23.10 ?  152 PHE A N     1 
ATOM   1148 C CA    . PHE A 1 152 ? 19.032  -19.534 10.663 1.00 24.42 ?  152 PHE A CA    1 
ATOM   1149 C C     . PHE A 1 152 ? 19.740  -20.258 11.800 1.00 27.62 ?  152 PHE A C     1 
ATOM   1150 O O     . PHE A 1 152 ? 20.586  -21.122 11.544 1.00 26.42 ?  152 PHE A O     1 
ATOM   1151 C CB    . PHE A 1 152 ? 19.914  -18.388 10.164 1.00 20.57 ?  152 PHE A CB    1 
ATOM   1152 C CG    . PHE A 1 152 ? 19.359  -17.658 8.972  1.00 22.46 ?  152 PHE A CG    1 
ATOM   1153 C CD1   . PHE A 1 152 ? 18.488  -18.283 8.096  1.00 24.96 ?  152 PHE A CD1   1 
ATOM   1154 C CD2   . PHE A 1 152 ? 19.708  -16.338 8.735  1.00 22.98 ?  152 PHE A CD2   1 
ATOM   1155 C CE1   . PHE A 1 152 ? 17.976  -17.604 7.003  1.00 24.62 ?  152 PHE A CE1   1 
ATOM   1156 C CE2   . PHE A 1 152 ? 19.200  -15.656 7.644  1.00 23.47 ?  152 PHE A CE2   1 
ATOM   1157 C CZ    . PHE A 1 152 ? 18.334  -16.289 6.779  1.00 23.42 ?  152 PHE A CZ    1 
ATOM   1158 N N     . PHE A 1 153 ? 19.418  -19.923 13.046 1.00 24.44 ?  153 PHE A N     1 
ATOM   1159 C CA    . PHE A 1 153 ? 20.099  -20.466 14.211 1.00 25.99 ?  153 PHE A CA    1 
ATOM   1160 C C     . PHE A 1 153 ? 19.070  -21.067 15.161 1.00 24.04 ?  153 PHE A C     1 
ATOM   1161 O O     . PHE A 1 153 ? 17.860  -20.944 14.959 1.00 24.24 ?  153 PHE A O     1 
ATOM   1162 C CB    . PHE A 1 153 ? 20.932  -19.383 14.911 1.00 27.07 ?  153 PHE A CB    1 
ATOM   1163 C CG    . PHE A 1 153 ? 21.942  -18.721 14.009 1.00 30.55 ?  153 PHE A CG    1 
ATOM   1164 C CD1   . PHE A 1 153 ? 23.212  -19.253 13.855 1.00 30.80 ?  153 PHE A CD1   1 
ATOM   1165 C CD2   . PHE A 1 153 ? 21.611  -17.577 13.301 1.00 28.66 ?  153 PHE A CD2   1 
ATOM   1166 C CE1   . PHE A 1 153 ? 24.136  -18.647 13.022 1.00 37.84 ?  153 PHE A CE1   1 
ATOM   1167 C CE2   . PHE A 1 153 ? 22.529  -16.968 12.466 1.00 26.72 ?  153 PHE A CE2   1 
ATOM   1168 C CZ    . PHE A 1 153 ? 23.793  -17.505 12.327 1.00 30.81 ?  153 PHE A CZ    1 
ATOM   1169 N N     . ASN A 1 154 ? 19.562  -21.731 16.205 1.00 26.29 ?  154 ASN A N     1 
ATOM   1170 C CA    . ASN A 1 154 ? 18.707  -22.498 17.114 1.00 24.08 ?  154 ASN A CA    1 
ATOM   1171 C C     . ASN A 1 154 ? 18.250  -21.617 18.273 1.00 22.12 ?  154 ASN A C     1 
ATOM   1172 O O     . ASN A 1 154 ? 19.010  -21.353 19.209 1.00 26.64 ?  154 ASN A O     1 
ATOM   1173 C CB    . ASN A 1 154 ? 19.440  -23.739 17.613 1.00 22.06 ?  154 ASN A CB    1 
ATOM   1174 C CG    . ASN A 1 154 ? 19.752  -24.717 16.496 1.00 27.76 ?  154 ASN A CG    1 
ATOM   1175 O OD1   . ASN A 1 154 ? 18.908  -24.984 15.640 1.00 26.12 ?  154 ASN A OD1   1 
ATOM   1176 N ND2   . ASN A 1 154 ? 20.963  -25.262 16.504 1.00 26.77 ?  154 ASN A ND2   1 
ATOM   1177 N N     . HIS A 1 155 ? 16.995  -21.174 18.214 1.00 23.29 ?  155 HIS A N     1 
ATOM   1178 C CA    . HIS A 1 155 ? 16.342  -20.455 19.298 1.00 23.40 ?  155 HIS A CA    1 
ATOM   1179 C C     . HIS A 1 155 ? 15.057  -21.180 19.674 1.00 23.27 ?  155 HIS A C     1 
ATOM   1180 O O     . HIS A 1 155 ? 14.298  -21.609 18.801 1.00 22.27 ?  155 HIS A O     1 
ATOM   1181 C CB    . HIS A 1 155 ? 16.023  -19.008 18.911 1.00 22.82 ?  155 HIS A CB    1 
ATOM   1182 C CG    . HIS A 1 155 ? 17.212  -18.099 18.926 1.00 22.10 ?  155 HIS A CG    1 
ATOM   1183 N ND1   . HIS A 1 155 ? 17.958  -17.865 20.061 1.00 21.14 ?  155 HIS A ND1   1 
ATOM   1184 C CD2   . HIS A 1 155 ? 17.778  -17.356 17.945 1.00 20.89 ?  155 HIS A CD2   1 
ATOM   1185 C CE1   . HIS A 1 155 ? 18.934  -17.020 19.778 1.00 20.88 ?  155 HIS A CE1   1 
ATOM   1186 N NE2   . HIS A 1 155 ? 18.848  -16.697 18.500 1.00 24.45 ?  155 HIS A NE2   1 
ATOM   1187 N N     . VAL A 1 156 ? 14.814  -21.317 20.974 1.00 25.10 ?  156 VAL A N     1 
ATOM   1188 C CA    . VAL A 1 156 ? 13.612  -21.945 21.505 1.00 28.38 ?  156 VAL A CA    1 
ATOM   1189 C C     . VAL A 1 156 ? 12.811  -20.879 22.250 1.00 26.65 ?  156 VAL A C     1 
ATOM   1190 O O     . VAL A 1 156 ? 13.267  -20.380 23.291 1.00 23.74 ?  156 VAL A O     1 
ATOM   1191 C CB    . VAL A 1 156 ? 13.945  -23.128 22.425 1.00 23.54 ?  156 VAL A CB    1 
ATOM   1192 C CG1   . VAL A 1 156 ? 12.671  -23.695 23.028 1.00 33.40 ?  156 VAL A CG1   1 
ATOM   1193 C CG2   . VAL A 1 156 ? 14.699  -24.202 21.658 1.00 29.19 ?  156 VAL A CG2   1 
ATOM   1194 N N     . PRO A 1 157 ? 11.632  -20.494 21.770 1.00 23.56 ?  157 PRO A N     1 
ATOM   1195 C CA    . PRO A 1 157 ? 10.823  -19.517 22.501 1.00 27.63 ?  157 PRO A CA    1 
ATOM   1196 C C     . PRO A 1 157 ? 10.036  -20.144 23.643 1.00 26.84 ?  157 PRO A C     1 
ATOM   1197 O O     . PRO A 1 157 ? 9.652   -21.315 23.605 1.00 26.66 ?  157 PRO A O     1 
ATOM   1198 C CB    . PRO A 1 157 ? 9.883   -18.964 21.424 1.00 23.76 ?  157 PRO A CB    1 
ATOM   1199 C CG    . PRO A 1 157 ? 9.710   -20.104 20.473 1.00 22.43 ?  157 PRO A CG    1 
ATOM   1200 C CD    . PRO A 1 157 ? 10.989  -20.916 20.512 1.00 24.47 ?  157 PRO A CD    1 
ATOM   1201 N N     . ASP A 1 158 ? 9.809   -19.332 24.675 1.00 27.16 ?  158 ASP A N     1 
ATOM   1202 C CA    . ASP A 1 158 ? 8.919   -19.688 25.773 1.00 21.62 ?  158 ASP A CA    1 
ATOM   1203 C C     . ASP A 1 158 ? 7.516   -19.239 25.395 1.00 25.18 ?  158 ASP A C     1 
ATOM   1204 O O     . ASP A 1 158 ? 7.258   -18.029 25.328 1.00 19.68 ?  158 ASP A O     1 
ATOM   1205 C CB    . ASP A 1 158 ? 9.372   -19.006 27.065 1.00 24.15 ?  158 ASP A CB    1 
ATOM   1206 C CG    . ASP A 1 158 ? 8.513   -19.367 28.269 1.00 20.18 ?  158 ASP A CG    1 
ATOM   1207 O OD1   . ASP A 1 158 ? 7.441   -19.989 28.111 1.00 21.03 ?  158 ASP A OD1   1 
ATOM   1208 O OD2   . ASP A 1 158 ? 8.916   -19.016 29.398 1.00 23.69 -1 158 ASP A OD2   1 
ATOM   1209 N N     . PRO A 1 159 ? 6.575   -20.160 25.149 1.00 24.22 ?  159 PRO A N     1 
ATOM   1210 C CA    . PRO A 1 159 ? 5.255   -19.767 24.648 1.00 24.59 ?  159 PRO A CA    1 
ATOM   1211 C C     . PRO A 1 159 ? 4.334   -19.152 25.690 1.00 24.34 ?  159 PRO A C     1 
ATOM   1212 O O     . PRO A 1 159 ? 3.170   -18.888 25.376 1.00 23.57 ?  159 PRO A O     1 
ATOM   1213 C CB    . PRO A 1 159 ? 4.685   -21.095 24.127 1.00 26.82 ?  159 PRO A CB    1 
ATOM   1214 C CG    . PRO A 1 159 ? 5.343   -22.144 24.954 1.00 32.31 ?  159 PRO A CG    1 
ATOM   1215 C CD    . PRO A 1 159 ? 6.700   -21.613 25.346 1.00 26.18 ?  159 PRO A CD    1 
ATOM   1216 N N     . THR A 1 160 ? 4.806   -18.918 26.914 1.00 27.29 ?  160 THR A N     1 
ATOM   1217 C CA    . THR A 1 160 ? 4.035   -18.177 27.904 1.00 26.86 ?  160 THR A CA    1 
ATOM   1218 C C     . THR A 1 160 ? 4.322   -16.683 27.866 1.00 23.68 ?  160 THR A C     1 
ATOM   1219 O O     . THR A 1 160 ? 3.613   -15.911 28.521 1.00 21.34 ?  160 THR A O     1 
ATOM   1220 C CB    . THR A 1 160 ? 4.313   -18.693 29.322 1.00 23.47 ?  160 THR A CB    1 
ATOM   1221 O OG1   . THR A 1 160 ? 5.706   -18.550 29.621 1.00 17.65 ?  160 THR A OG1   1 
ATOM   1222 C CG2   . THR A 1 160 ? 3.897   -20.143 29.470 1.00 22.81 ?  160 THR A CG2   1 
ATOM   1223 N N     . THR A 1 161 ? 5.338   -16.262 27.123 1.00 22.05 ?  161 THR A N     1 
ATOM   1224 C CA    . THR A 1 161 ? 5.767   -14.874 27.090 1.00 22.44 ?  161 THR A CA    1 
ATOM   1225 C C     . THR A 1 161 ? 5.149   -14.159 25.896 1.00 21.38 ?  161 THR A C     1 
ATOM   1226 O O     . THR A 1 161 ? 4.545   -14.770 25.012 1.00 24.94 ?  161 THR A O     1 
ATOM   1227 C CB    . THR A 1 161 ? 7.296   -14.787 27.020 1.00 18.04 ?  161 THR A CB    1 
ATOM   1228 O OG1   . THR A 1 161 ? 7.742   -15.350 25.781 1.00 24.52 ?  161 THR A OG1   1 
ATOM   1229 C CG2   . THR A 1 161 ? 7.924   -15.559 28.164 1.00 19.82 ?  161 THR A CG2   1 
ATOM   1230 N N     . HIS A 1 162 ? 5.304   -12.838 25.883 1.00 17.56 ?  162 HIS A N     1 
ATOM   1231 C CA    . HIS A 1 162 ? 5.078   -12.068 24.668 1.00 19.86 ?  162 HIS A CA    1 
ATOM   1232 C C     . HIS A 1 162 ? 6.333   -12.140 23.808 1.00 20.65 ?  162 HIS A C     1 
ATOM   1233 O O     . HIS A 1 162 ? 7.408   -11.689 24.221 1.00 19.76 ?  162 HIS A O     1 
ATOM   1234 C CB    . HIS A 1 162 ? 4.712   -10.624 24.997 1.00 23.73 ?  162 HIS A CB    1 
ATOM   1235 C CG    . HIS A 1 162 ? 3.265   -10.436 25.325 1.00 23.77 ?  162 HIS A CG    1 
ATOM   1236 N ND1   . HIS A 1 162 ? 2.771   -10.529 26.609 1.00 22.45 ?  162 HIS A ND1   1 
ATOM   1237 C CD2   . HIS A 1 162 ? 2.200   -10.178 24.531 1.00 18.81 ?  162 HIS A CD2   1 
ATOM   1238 C CE1   . HIS A 1 162 ? 1.465   -10.331 26.592 1.00 28.50 ?  162 HIS A CE1   1 
ATOM   1239 N NE2   . HIS A 1 162 ? 1.093   -10.115 25.343 1.00 24.52 ?  162 HIS A NE2   1 
ATOM   1240 N N     . LEU A 1 163 ? 6.199   -12.712 22.619 1.00 18.57 ?  163 LEU A N     1 
ATOM   1241 C CA    . LEU A 1 163 ? 7.324   -12.956 21.729 1.00 21.53 ?  163 LEU A CA    1 
ATOM   1242 C C     . LEU A 1 163 ? 7.306   -11.947 20.590 1.00 14.55 ?  163 LEU A C     1 
ATOM   1243 O O     . LEU A 1 163 ? 6.263   -11.722 19.967 1.00 18.81 ?  163 LEU A O     1 
ATOM   1244 C CB    . LEU A 1 163 ? 7.280   -14.385 21.177 1.00 14.59 ?  163 LEU A CB    1 
ATOM   1245 C CG    . LEU A 1 163 ? 8.219   -14.718 20.019 1.00 21.42 ?  163 LEU A CG    1 
ATOM   1246 C CD1   . LEU A 1 163 ? 9.669   -14.507 20.419 1.00 19.93 ?  163 LEU A CD1   1 
ATOM   1247 C CD2   . LEU A 1 163 ? 7.995   -16.148 19.559 1.00 18.25 ?  163 LEU A CD2   1 
ATOM   1248 N N     . LEU A 1 164 ? 8.460   -11.340 20.331 1.00 18.09 ?  164 LEU A N     1 
ATOM   1249 C CA    . LEU A 1 164 ? 8.640   -10.392 19.242 1.00 20.76 ?  164 LEU A CA    1 
ATOM   1250 C C     . LEU A 1 164 ? 9.630   -10.964 18.240 1.00 18.70 ?  164 LEU A C     1 
ATOM   1251 O O     . LEU A 1 164 ? 10.689  -11.466 18.628 1.00 19.63 ?  164 LEU A O     1 
ATOM   1252 C CB    . LEU A 1 164 ? 9.148   -9.039  19.754 1.00 20.71 ?  164 LEU A CB    1 
ATOM   1253 C CG    . LEU A 1 164 ? 8.233   -8.116  20.569 1.00 19.91 ?  164 LEU A CG    1 
ATOM   1254 C CD1   . LEU A 1 164 ? 7.054   -7.694  19.714 1.00 19.58 ?  164 LEU A CD1   1 
ATOM   1255 C CD2   . LEU A 1 164 ? 7.771   -8.715  21.896 1.00 23.39 ?  164 LEU A CD2   1 
ATOM   1256 N N     . LEU A 1 165 ? 9.289   -10.885 16.958 1.00 18.35 ?  165 LEU A N     1 
ATOM   1257 C CA    . LEU A 1 165 ? 10.231  -11.156 15.878 1.00 17.28 ?  165 LEU A CA    1 
ATOM   1258 C C     . LEU A 1 165 ? 10.449  -9.857  15.110 1.00 16.83 ?  165 LEU A C     1 
ATOM   1259 O O     . LEU A 1 165 ? 9.546   -9.381  14.412 1.00 15.12 ?  165 LEU A O     1 
ATOM   1260 C CB    . LEU A 1 165 ? 9.725   -12.271 14.962 1.00 17.18 ?  165 LEU A CB    1 
ATOM   1261 C CG    . LEU A 1 165 ? 9.531   -13.635 15.633 1.00 18.59 ?  165 LEU A CG    1 
ATOM   1262 C CD1   . LEU A 1 165 ? 9.195   -14.704 14.603 1.00 16.53 ?  165 LEU A CD1   1 
ATOM   1263 C CD2   . LEU A 1 165 ? 10.760  -14.027 16.445 1.00 17.27 ?  165 LEU A CD2   1 
ATOM   1264 N N     . TRP A 1 166 ? 11.644  -9.286  15.244 1.00 14.93 ?  166 TRP A N     1 
ATOM   1265 C CA    . TRP A 1 166 ? 11.972  -8.032  14.587 1.00 15.18 ?  166 TRP A CA    1 
ATOM   1266 C C     . TRP A 1 166 ? 12.393  -8.277  13.143 1.00 21.41 ?  166 TRP A C     1 
ATOM   1267 O O     . TRP A 1 166 ? 12.845  -9.366  12.775 1.00 16.25 ?  166 TRP A O     1 
ATOM   1268 C CB    . TRP A 1 166 ? 13.097  -7.301  15.324 1.00 17.43 ?  166 TRP A CB    1 
ATOM   1269 C CG    . TRP A 1 166 ? 12.782  -6.895  16.736 1.00 19.58 ?  166 TRP A CG    1 
ATOM   1270 C CD1   . TRP A 1 166 ? 12.339  -7.697  17.748 1.00 18.76 ?  166 TRP A CD1   1 
ATOM   1271 C CD2   . TRP A 1 166 ? 12.897  -5.579  17.291 1.00 16.72 ?  166 TRP A CD2   1 
ATOM   1272 N NE1   . TRP A 1 166 ? 12.168  -6.960  18.897 1.00 14.76 ?  166 TRP A NE1   1 
ATOM   1273 C CE2   . TRP A 1 166 ? 12.504  -5.657  18.641 1.00 15.64 ?  166 TRP A CE2   1 
ATOM   1274 C CE3   . TRP A 1 166 ? 13.293  -4.340  16.774 1.00 16.29 ?  166 TRP A CE3   1 
ATOM   1275 C CZ2   . TRP A 1 166 ? 12.496  -4.545  19.483 1.00 20.39 ?  166 TRP A CZ2   1 
ATOM   1276 C CZ3   . TRP A 1 166 ? 13.285  -3.239  17.609 1.00 17.50 ?  166 TRP A CZ3   1 
ATOM   1277 C CH2   . TRP A 1 166 ? 12.888  -3.348  18.949 1.00 19.17 ?  166 TRP A CH2   1 
ATOM   1278 N N     . GLN A 1 167 ? 12.253  -7.231  12.327 1.00 16.71 ?  167 GLN A N     1 
ATOM   1279 C CA    . GLN A 1 167 ? 12.622  -7.277  10.911 1.00 19.29 ?  167 GLN A CA    1 
ATOM   1280 C C     . GLN A 1 167 ? 11.940  -8.447  10.209 1.00 20.54 ?  167 GLN A C     1 
ATOM   1281 O O     . GLN A 1 167 ? 12.550  -9.176  9.424  1.00 16.38 ?  167 GLN A O     1 
ATOM   1282 C CB    . GLN A 1 167 ? 14.144  -7.332  10.749 1.00 18.10 ?  167 GLN A CB    1 
ATOM   1283 C CG    . GLN A 1 167 ? 14.872  -6.308  11.616 1.00 22.19 ?  167 GLN A CG    1 
ATOM   1284 C CD    . GLN A 1 167 ? 16.326  -6.120  11.229 1.00 24.03 ?  167 GLN A CD    1 
ATOM   1285 O OE1   . GLN A 1 167 ? 16.850  -5.007  11.271 1.00 24.30 ?  167 GLN A OE1   1 
ATOM   1286 N NE2   . GLN A 1 167 ? 16.988  -7.209  10.859 1.00 22.23 ?  167 GLN A NE2   1 
ATOM   1287 N N     . ILE A 1 168 ? 10.647  -8.619  10.501 1.00 16.00 ?  168 ILE A N     1 
ATOM   1288 C CA    . ILE A 1 168 ? 9.875   -9.730  9.952  1.00 16.77 ?  168 ILE A CA    1 
ATOM   1289 C C     . ILE A 1 168 ? 9.789   -9.643  8.434  1.00 19.22 ?  168 ILE A C     1 
ATOM   1290 O O     . ILE A 1 168 ? 9.655   -10.665 7.752  1.00 20.08 ?  168 ILE A O     1 
ATOM   1291 C CB    . ILE A 1 168 ? 8.478   -9.762  10.606 1.00 17.33 ?  168 ILE A CB    1 
ATOM   1292 C CG1   . ILE A 1 168 ? 7.673   -10.976 10.137 1.00 13.73 ?  168 ILE A CG1   1 
ATOM   1293 C CG2   . ILE A 1 168 ? 7.723   -8.464  10.340 1.00 16.04 ?  168 ILE A CG2   1 
ATOM   1294 C CD1   . ILE A 1 168 ? 8.217   -12.294 10.637 1.00 13.73 ?  168 ILE A CD1   1 
ATOM   1295 N N     . ALA A 1 169 ? 9.886   -8.434  7.876  1.00 19.69 ?  169 ALA A N     1 
ATOM   1296 C CA    . ALA A 1 169 ? 9.702   -8.251  6.439  1.00 22.51 ?  169 ALA A CA    1 
ATOM   1297 C C     . ALA A 1 169 ? 10.816  -8.887  5.620  1.00 20.25 ?  169 ALA A C     1 
ATOM   1298 O O     . ALA A 1 169 ? 10.623  -9.135  4.426  1.00 21.58 ?  169 ALA A O     1 
ATOM   1299 C CB    . ALA A 1 169 ? 9.600   -6.761  6.104  1.00 22.62 ?  169 ALA A CB    1 
ATOM   1300 N N     . ILE A 1 170 ? 11.971  -9.146  6.225  1.00 19.18 ?  170 ILE A N     1 
ATOM   1301 C CA    . ILE A 1 170 ? 13.087  -9.777  5.535  1.00 24.72 ?  170 ILE A CA    1 
ATOM   1302 C C     . ILE A 1 170 ? 13.388  -11.153 6.124  1.00 20.21 ?  170 ILE A C     1 
ATOM   1303 O O     . ILE A 1 170 ? 14.494  -11.664 5.971  1.00 15.94 ?  170 ILE A O     1 
ATOM   1304 C CB    . ILE A 1 170 ? 14.337  -8.883  5.552  1.00 22.93 ?  170 ILE A CB    1 
ATOM   1305 C CG1   . ILE A 1 170 ? 14.615  -8.373  6.969  1.00 24.20 ?  170 ILE A CG1   1 
ATOM   1306 C CG2   . ILE A 1 170 ? 14.182  -7.721  4.584  1.00 25.27 ?  170 ILE A CG2   1 
ATOM   1307 C CD1   . ILE A 1 170 ? 15.925  -7.626  7.096  1.00 20.58 ?  170 ILE A CD1   1 
ATOM   1308 N N     . ALA A 1 171 ? 12.416  -11.750 6.808  1.00 19.30 ?  171 ALA A N     1 
ATOM   1309 C CA    . ALA A 1 171 ? 12.622  -13.035 7.463  1.00 19.01 ?  171 ALA A CA    1 
ATOM   1310 C C     . ALA A 1 171 ? 13.050  -14.087 6.450  1.00 19.78 ?  171 ALA A C     1 
ATOM   1311 O O     . ALA A 1 171 ? 12.299  -14.415 5.527  1.00 24.00 ?  171 ALA A O     1 
ATOM   1312 C CB    . ALA A 1 171 ? 11.342  -13.469 8.178  1.00 18.81 ?  171 ALA A CB    1 
ATOM   1313 N N     . GLY A 1 172 ? 14.260  -14.614 6.624  1.00 18.86 ?  172 GLY A N     1 
ATOM   1314 C CA    . GLY A 1 172 ? 14.773  -15.647 5.753  1.00 23.64 ?  172 GLY A CA    1 
ATOM   1315 C C     . GLY A 1 172 ? 15.542  -15.148 4.553  1.00 26.13 ?  172 GLY A C     1 
ATOM   1316 O O     . GLY A 1 172 ? 15.995  -15.967 3.743  1.00 26.37 ?  172 GLY A O     1 
ATOM   1317 N N     . GLU A 1 173 ? 15.700  -13.835 4.409  1.00 23.16 ?  173 GLU A N     1 
ATOM   1318 C CA    . GLU A 1 173 ? 16.416  -13.253 3.273  1.00 24.17 ?  173 GLU A CA    1 
ATOM   1319 C C     . GLU A 1 173 ? 17.906  -13.323 3.594  1.00 21.10 ?  173 GLU A C     1 
ATOM   1320 O O     . GLU A 1 173 ? 18.497  -12.391 4.146  1.00 28.43 ?  173 GLU A O     1 
ATOM   1321 C CB    . GLU A 1 173 ? 15.948  -11.825 3.014  1.00 20.86 ?  173 GLU A CB    1 
ATOM   1322 C CG    . GLU A 1 173 ? 16.282  -11.275 1.630  1.00 24.30 ?  173 GLU A CG    1 
ATOM   1323 C CD    . GLU A 1 173 ? 17.770  -11.108 1.396  1.00 25.52 ?  173 GLU A CD    1 
ATOM   1324 O OE1   . GLU A 1 173 ? 18.308  -10.035 1.738  1.00 32.26 ?  173 GLU A OE1   1 
ATOM   1325 O OE2   . GLU A 1 173 ? 18.398  -12.050 0.867  1.00 24.86 -1 173 GLU A OE2   1 
ATOM   1326 N N     . HIS A 1 174 ? 18.518  -14.457 3.245  1.00 23.01 ?  174 HIS A N     1 
ATOM   1327 C CA    . HIS A 1 174 ? 19.833  -14.817 3.765  1.00 25.75 ?  174 HIS A CA    1 
ATOM   1328 C C     . HIS A 1 174 ? 20.963  -13.997 3.160  1.00 27.66 ?  174 HIS A C     1 
ATOM   1329 O O     . HIS A 1 174 ? 22.067  -14.001 3.713  1.00 22.11 ?  174 HIS A O     1 
ATOM   1330 C CB    . HIS A 1 174 ? 20.100  -16.302 3.523  1.00 23.43 ?  174 HIS A CB    1 
ATOM   1331 C CG    . HIS A 1 174 ? 20.293  -16.649 2.082  1.00 23.73 ?  174 HIS A CG    1 
ATOM   1332 N ND1   . HIS A 1 174 ? 19.241  -16.892 1.227  1.00 30.78 ?  174 HIS A ND1   1 
ATOM   1333 C CD2   . HIS A 1 174 ? 21.418  -16.778 1.340  1.00 23.52 ?  174 HIS A CD2   1 
ATOM   1334 C CE1   . HIS A 1 174 ? 19.709  -17.160 0.021  1.00 24.31 ?  174 HIS A CE1   1 
ATOM   1335 N NE2   . HIS A 1 174 ? 21.028  -17.099 0.064  1.00 24.01 ?  174 HIS A NE2   1 
ATOM   1336 N N     . THR A 1 175 ? 20.736  -13.334 2.027  1.00 23.17 ?  175 THR A N     1 
ATOM   1337 C CA    . THR A 1 175 ? 21.811  -12.630 1.340  1.00 27.75 ?  175 THR A CA    1 
ATOM   1338 C C     . THR A 1 175 ? 22.052  -11.224 1.876  1.00 26.44 ?  175 THR A C     1 
ATOM   1339 O O     . THR A 1 175 ? 23.136  -10.669 1.654  1.00 20.95 ?  175 THR A O     1 
ATOM   1340 C CB    . THR A 1 175 ? 21.521  -12.544 -0.166 1.00 30.22 ?  175 THR A CB    1 
ATOM   1341 O OG1   . THR A 1 175 ? 20.486  -11.582 -0.400 1.00 25.76 ?  175 THR A OG1   1 
ATOM   1342 C CG2   . THR A 1 175 ? 21.086  -13.898 -0.714 1.00 26.11 ?  175 THR A CG2   1 
ATOM   1343 N N     . LEU A 1 176 ? 21.070  -10.637 2.569  1.00 28.69 ?  176 LEU A N     1 
ATOM   1344 C CA    . LEU A 1 176 ? 21.158  -9.257  3.054  1.00 30.74 ?  176 LEU A CA    1 
ATOM   1345 C C     . LEU A 1 176 ? 21.403  -8.274  1.910  1.00 31.76 ?  176 LEU A C     1 
ATOM   1346 O O     . LEU A 1 176 ? 22.073  -7.252  2.083  1.00 29.82 ?  176 LEU A O     1 
ATOM   1347 C CB    . LEU A 1 176 ? 22.212  -9.092  4.160  1.00 26.19 ?  176 LEU A CB    1 
ATOM   1348 C CG    . LEU A 1 176 ? 22.246  -10.060 5.357  1.00 34.49 ?  176 LEU A CG    1 
ATOM   1349 C CD1   . LEU A 1 176 ? 22.875  -11.376 5.024  1.00 33.18 ?  176 LEU A CD1   1 
ATOM   1350 C CD2   . LEU A 1 176 ? 23.001  -9.418  6.523  1.00 42.05 ?  176 LEU A CD2   1 
ATOM   1351 N N     . THR A 1 177 ? 20.836  -8.576  0.738  1.00 36.93 ?  177 THR A N     1 
ATOM   1352 C CA    . THR A 1 177 ? 20.905  -7.711  -0.429 1.00 31.70 ?  177 THR A CA    1 
ATOM   1353 C C     . THR A 1 177 ? 19.529  -7.256  -0.891 1.00 34.95 ?  177 THR A C     1 
ATOM   1354 O O     . THR A 1 177 ? 19.441  -6.367  -1.745 1.00 30.27 ?  177 THR A O     1 
ATOM   1355 C CB    . THR A 1 177 ? 21.615  -8.417  -1.594 1.00 31.77 ?  177 THR A CB    1 
ATOM   1356 O OG1   . THR A 1 177 ? 20.750  -9.420  -2.136 1.00 26.69 ?  177 THR A OG1   1 
ATOM   1357 C CG2   . THR A 1 177 ? 22.907  -9.065  -1.128 1.00 26.32 ?  177 THR A CG2   1 
ATOM   1358 N N     . GLN A 1 178 ? 18.461  -7.827  -0.343 1.00 29.80 ?  178 GLN A N     1 
ATOM   1359 C CA    . GLN A 1 178 ? 17.096  -7.498  -0.716 1.00 34.22 ?  178 GLN A CA    1 
ATOM   1360 C C     . GLN A 1 178 ? 16.396  -6.771  0.426  1.00 38.16 ?  178 GLN A C     1 
ATOM   1361 O O     . GLN A 1 178 ? 16.742  -6.928  1.600  1.00 35.56 ?  178 GLN A O     1 
ATOM   1362 C CB    . GLN A 1 178 ? 16.304  -8.756  -1.086 1.00 32.90 ?  178 GLN A CB    1 
ATOM   1363 C CG    . GLN A 1 178 ? 16.927  -9.583  -2.198 1.00 36.79 ?  178 GLN A CG    1 
ATOM   1364 C CD    . GLN A 1 178 ? 16.553  -9.082  -3.576 1.00 42.31 ?  178 GLN A CD    1 
ATOM   1365 O OE1   . GLN A 1 178 ? 15.889  -8.055  -3.717 1.00 37.44 ?  178 GLN A OE1   1 
ATOM   1366 N NE2   . GLN A 1 178 ? 16.967  -9.813  -4.603 1.00 41.38 ?  178 GLN A NE2   1 
ATOM   1367 N N     . PHE A 1 179 ? 15.399  -5.965  0.064  1.00 44.77 ?  179 PHE A N     1 
ATOM   1368 C CA    . PHE A 1 179 ? 14.634  -5.187  1.029  1.00 39.95 ?  179 PHE A CA    1 
ATOM   1369 C C     . PHE A 1 179 ? 13.476  -5.964  1.638  1.00 36.96 ?  179 PHE A C     1 
ATOM   1370 O O     . PHE A 1 179 ? 12.912  -5.519  2.644  1.00 35.35 ?  179 PHE A O     1 
ATOM   1371 C CB    . PHE A 1 179 ? 14.097  -3.914  0.372  1.00 39.36 ?  179 PHE A CB    1 
ATOM   1372 C CG    . PHE A 1 179 ? 15.171  -2.961  -0.053 1.00 58.42 ?  179 PHE A CG    1 
ATOM   1373 C CD1   . PHE A 1 179 ? 16.208  -2.641  0.807  1.00 59.95 ?  179 PHE A CD1   1 
ATOM   1374 C CD2   . PHE A 1 179 ? 15.153  -2.396  -1.315 1.00 59.62 ?  179 PHE A CD2   1 
ATOM   1375 C CE1   . PHE A 1 179 ? 17.204  -1.766  0.418  1.00 62.83 ?  179 PHE A CE1   1 
ATOM   1376 C CE2   . PHE A 1 179 ? 16.145  -1.521  -1.711 1.00 62.47 ?  179 PHE A CE2   1 
ATOM   1377 C CZ    . PHE A 1 179 ? 17.171  -1.206  -0.844 1.00 65.76 ?  179 PHE A CZ    1 
ATOM   1378 N N     . HIS A 1 180 ? 13.099  -7.094  1.045  1.00 28.96 ?  180 HIS A N     1 
ATOM   1379 C CA    . HIS A 1 180 ? 11.977  -7.877  1.534  1.00 30.46 ?  180 HIS A CA    1 
ATOM   1380 C C     . HIS A 1 180 ? 12.227  -9.342  1.218  1.00 27.37 ?  180 HIS A C     1 
ATOM   1381 O O     . HIS A 1 180 ? 13.011  -9.682  0.328  1.00 28.03 ?  180 HIS A O     1 
ATOM   1382 C CB    . HIS A 1 180 ? 10.656  -7.408  0.913  1.00 37.75 ?  180 HIS A CB    1 
ATOM   1383 C CG    . HIS A 1 180 ? 10.570  -7.625  -0.566 1.00 38.03 ?  180 HIS A CG    1 
ATOM   1384 N ND1   . HIS A 1 180 ? 10.088  -8.791  -1.122 1.00 39.45 ?  180 HIS A ND1   1 
ATOM   1385 C CD2   . HIS A 1 180 ? 10.896  -6.820  -1.605 1.00 40.27 ?  180 HIS A CD2   1 
ATOM   1386 C CE1   . HIS A 1 180 ? 10.120  -8.695  -2.439 1.00 35.22 ?  180 HIS A CE1   1 
ATOM   1387 N NE2   . HIS A 1 180 ? 10.608  -7.510  -2.758 1.00 39.46 ?  180 HIS A NE2   1 
ATOM   1388 N N     . THR A 1 181 ? 11.546  -10.209 1.958  1.00 27.89 ?  181 THR A N     1 
ATOM   1389 C CA    . THR A 1 181 ? 11.662  -11.642 1.742  1.00 26.60 ?  181 THR A CA    1 
ATOM   1390 C C     . THR A 1 181 ? 10.550  -12.076 0.788  1.00 27.47 ?  181 THR A C     1 
ATOM   1391 O O     . THR A 1 181 ? 9.977   -11.254 0.069  1.00 30.16 ?  181 THR A O     1 
ATOM   1392 C CB    . THR A 1 181 ? 11.626  -12.379 3.082  1.00 23.53 ?  181 THR A CB    1 
ATOM   1393 O OG1   . THR A 1 181 ? 11.846  -13.774 2.861  1.00 28.55 ?  181 THR A OG1   1 
ATOM   1394 C CG2   . THR A 1 181 ? 10.280  -12.193 3.772  1.00 20.80 ?  181 THR A CG2   1 
ATOM   1395 N N     . SER A 1 182 ? 10.230  -13.361 0.762  1.00 26.61 ?  182 SER A N     1 
ATOM   1396 C CA    . SER A 1 182 ? 9.172   -13.885 -0.084 1.00 29.93 ?  182 SER A CA    1 
ATOM   1397 C C     . SER A 1 182 ? 8.175   -14.653 0.772  1.00 26.88 ?  182 SER A C     1 
ATOM   1398 O O     . SER A 1 182 ? 8.453   -15.013 1.919  1.00 25.40 ?  182 SER A O     1 
ATOM   1399 C CB    . SER A 1 182 ? 9.735   -14.781 -1.190 1.00 35.68 ?  182 SER A CB    1 
ATOM   1400 O OG    . SER A 1 182 ? 10.201  -16.002 -0.663 1.00 40.31 ?  182 SER A OG    1 
ATOM   1401 N N     . SER A 1 183 ? 6.993   -14.892 0.203  1.00 32.95 ?  183 SER A N     1 
ATOM   1402 C CA    . SER A 1 183 ? 5.937   -15.561 0.956  1.00 31.47 ?  183 SER A CA    1 
ATOM   1403 C C     . SER A 1 183 ? 6.287   -17.018 1.231  1.00 33.00 ?  183 SER A C     1 
ATOM   1404 O O     . SER A 1 183 ? 5.803   -17.595 2.214  1.00 30.92 ?  183 SER A O     1 
ATOM   1405 C CB    . SER A 1 183 ? 4.605   -15.450 0.212  1.00 30.84 ?  183 SER A CB    1 
ATOM   1406 O OG    . SER A 1 183 ? 4.642   -16.136 -1.022 1.00 38.07 ?  183 SER A OG    1 
ATOM   1407 N N     . ASP A 1 184 ? 7.116   -17.633 0.380  1.00 32.91 ?  184 ASP A N     1 
ATOM   1408 C CA    . ASP A 1 184 ? 7.530   -19.008 0.644  1.00 33.44 ?  184 ASP A CA    1 
ATOM   1409 C C     . ASP A 1 184 ? 8.447   -19.074 1.860  1.00 31.20 ?  184 ASP A C     1 
ATOM   1410 O O     . ASP A 1 184 ? 8.409   -20.049 2.621  1.00 22.14 ?  184 ASP A O     1 
ATOM   1411 C CB    . ASP A 1 184 ? 8.222   -19.603 -0.584 1.00 32.05 ?  184 ASP A CB    1 
ATOM   1412 C CG    . ASP A 1 184 ? 9.173   -18.628 -1.241 1.00 45.03 ?  184 ASP A CG    1 
ATOM   1413 O OD1   . ASP A 1 184 ? 10.141  -18.198 -0.570 1.00 44.09 -1 184 ASP A OD1   1 
ATOM   1414 O OD2   . ASP A 1 184 ? 8.964   -18.289 -2.424 1.00 56.43 ?  184 ASP A OD2   1 
ATOM   1415 N N     . ARG A 1 185 ? 9.277   -18.044 2.056  1.00 27.95 ?  185 ARG A N     1 
ATOM   1416 C CA    . ARG A 1 185 ? 10.109  -17.975 3.253  1.00 30.90 ?  185 ARG A CA    1 
ATOM   1417 C C     . ARG A 1 185 ? 9.249   -17.789 4.495  1.00 25.01 ?  185 ARG A C     1 
ATOM   1418 O O     . ARG A 1 185 ? 9.500   -18.409 5.536  1.00 27.83 ?  185 ARG A O     1 
ATOM   1419 C CB    . ARG A 1 185 ? 11.113  -16.834 3.129  1.00 27.31 ?  185 ARG A CB    1 
ATOM   1420 C CG    . ARG A 1 185 ? 11.809  -16.797 1.790  1.00 38.41 ?  185 ARG A CG    1 
ATOM   1421 C CD    . ARG A 1 185 ? 12.783  -17.933 1.625  1.00 35.16 ?  185 ARG A CD    1 
ATOM   1422 N NE    . ARG A 1 185 ? 14.154  -17.456 1.731  1.00 44.94 ?  185 ARG A NE    1 
ATOM   1423 C CZ    . ARG A 1 185 ? 15.171  -17.957 1.043  1.00 44.09 ?  185 ARG A CZ    1 
ATOM   1424 N NH1   . ARG A 1 185 ? 15.008  -18.968 0.205  1.00 44.54 ?  185 ARG A NH1   1 
ATOM   1425 N NH2   . ARG A 1 185 ? 16.381  -17.427 1.194  1.00 38.35 ?  185 ARG A NH2   1 
ATOM   1426 N N     . LEU A 1 186 ? 8.239   -16.921 4.402  1.00 28.54 ?  186 LEU A N     1 
ATOM   1427 C CA    . LEU A 1 186 ? 7.359   -16.674 5.534  1.00 27.76 ?  186 LEU A CA    1 
ATOM   1428 C C     . LEU A 1 186 ? 6.542   -17.913 5.871  1.00 25.55 ?  186 LEU A C     1 
ATOM   1429 O O     . LEU A 1 186 ? 6.211   -18.138 7.041  1.00 30.12 ?  186 LEU A O     1 
ATOM   1430 C CB    . LEU A 1 186 ? 6.443   -15.492 5.221  1.00 24.34 ?  186 LEU A CB    1 
ATOM   1431 C CG    . LEU A 1 186 ? 7.121   -14.116 5.205  1.00 28.74 ?  186 LEU A CG    1 
ATOM   1432 C CD1   . LEU A 1 186 ? 6.282   -13.119 4.430  1.00 24.09 ?  186 LEU A CD1   1 
ATOM   1433 C CD2   . LEU A 1 186 ? 7.379   -13.617 6.618  1.00 27.39 ?  186 LEU A CD2   1 
ATOM   1434 N N     . GLN A 1 187 ? 6.221   -18.728 4.861  1.00 26.09 ?  187 GLN A N     1 
ATOM   1435 C CA    . GLN A 1 187 ? 5.523   -19.985 5.107  1.00 28.69 ?  187 GLN A CA    1 
ATOM   1436 C C     . GLN A 1 187 ? 6.418   -20.981 5.833  1.00 24.43 ?  187 GLN A C     1 
ATOM   1437 O O     . GLN A 1 187 ? 5.931   -21.770 6.652  1.00 20.67 ?  187 GLN A O     1 
ATOM   1438 C CB    . GLN A 1 187 ? 5.023   -20.569 3.784  1.00 29.20 ?  187 GLN A CB    1 
ATOM   1439 C CG    . GLN A 1 187 ? 4.374   -21.944 3.891  1.00 29.08 ?  187 GLN A CG    1 
ATOM   1440 C CD    . GLN A 1 187 ? 3.134   -21.939 4.768  1.00 28.76 ?  187 GLN A CD    1 
ATOM   1441 O OE1   . GLN A 1 187 ? 2.343   -20.995 4.744  1.00 31.19 ?  187 GLN A OE1   1 
ATOM   1442 N NE2   . GLN A 1 187 ? 2.956   -23.003 5.542  1.00 28.74 ?  187 GLN A NE2   1 
ATOM   1443 N N     . ILE A 1 188 ? 7.723   -20.957 5.549  1.00 26.42 ?  188 ILE A N     1 
ATOM   1444 C CA    . ILE A 1 188 ? 8.651   -21.820 6.273  1.00 27.83 ?  188 ILE A CA    1 
ATOM   1445 C C     . ILE A 1 188 ? 8.752   -21.373 7.725  1.00 28.81 ?  188 ILE A C     1 
ATOM   1446 O O     . ILE A 1 188 ? 8.848   -22.200 8.642  1.00 26.89 ?  188 ILE A O     1 
ATOM   1447 C CB    . ILE A 1 188 ? 10.027  -21.822 5.580  1.00 27.50 ?  188 ILE A CB    1 
ATOM   1448 C CG1   . ILE A 1 188 ? 9.981   -22.663 4.299  1.00 22.51 ?  188 ILE A CG1   1 
ATOM   1449 C CG2   . ILE A 1 188 ? 11.115  -22.332 6.515  1.00 28.89 ?  188 ILE A CG2   1 
ATOM   1450 C CD1   . ILE A 1 188 ? 11.223  -22.533 3.443  1.00 23.41 ?  188 ILE A CD1   1 
ATOM   1451 N N     . LEU A 1 189 ? 8.722   -20.058 7.955  1.00 23.57 ?  189 LEU A N     1 
ATOM   1452 C CA    . LEU A 1 189 ? 8.693   -19.539 9.318  1.00 25.23 ?  189 LEU A CA    1 
ATOM   1453 C C     . LEU A 1 189 ? 7.444   -20.012 10.051 1.00 20.43 ?  189 LEU A C     1 
ATOM   1454 O O     . LEU A 1 189 ? 7.511   -20.409 11.222 1.00 23.11 ?  189 LEU A O     1 
ATOM   1455 C CB    . LEU A 1 189 ? 8.759   -18.014 9.297  1.00 24.49 ?  189 LEU A CB    1 
ATOM   1456 C CG    . LEU A 1 189 ? 8.688   -17.278 10.633 1.00 29.54 ?  189 LEU A CG    1 
ATOM   1457 C CD1   . LEU A 1 189 ? 9.745   -17.792 11.604 1.00 21.52 ?  189 LEU A CD1   1 
ATOM   1458 C CD2   . LEU A 1 189 ? 8.843   -15.787 10.413 1.00 17.58 ?  189 LEU A CD2   1 
ATOM   1459 N N     . VAL A 1 190 ? 6.294   -19.979 9.372  1.00 26.00 ?  190 VAL A N     1 
ATOM   1460 C CA    . VAL A 1 190 ? 5.038   -20.381 10.002 1.00 24.89 ?  190 VAL A CA    1 
ATOM   1461 C C     . VAL A 1 190 ? 5.105   -21.842 10.418 1.00 24.70 ?  190 VAL A C     1 
ATOM   1462 O O     . VAL A 1 190 ? 4.671   -22.217 11.515 1.00 24.94 ?  190 VAL A O     1 
ATOM   1463 C CB    . VAL A 1 190 ? 3.855   -20.118 9.050  1.00 25.73 ?  190 VAL A CB    1 
ATOM   1464 C CG1   . VAL A 1 190 ? 2.600   -20.824 9.537  1.00 21.57 ?  190 VAL A CG1   1 
ATOM   1465 C CG2   . VAL A 1 190 ? 3.611   -18.625 8.900  1.00 23.65 ?  190 VAL A CG2   1 
ATOM   1466 N N     . GLU A 1 191 ? 5.669   -22.687 9.554  1.00 22.33 ?  191 GLU A N     1 
ATOM   1467 C CA    . GLU A 1 191 ? 5.813   -24.101 9.878  1.00 31.16 ?  191 GLU A CA    1 
ATOM   1468 C C     . GLU A 1 191 ? 6.794   -24.303 11.028 1.00 26.14 ?  191 GLU A C     1 
ATOM   1469 O O     . GLU A 1 191 ? 6.555   -25.129 11.919 1.00 26.63 ?  191 GLU A O     1 
ATOM   1470 C CB    . GLU A 1 191 ? 6.234   -24.871 8.626  1.00 28.44 ?  191 GLU A CB    1 
ATOM   1471 C CG    . GLU A 1 191 ? 5.153   -24.839 7.544  1.00 28.94 ?  191 GLU A CG    1 
ATOM   1472 C CD    . GLU A 1 191 ? 5.625   -25.341 6.194  1.00 35.96 ?  191 GLU A CD    1 
ATOM   1473 O OE1   . GLU A 1 191 ? 6.689   -25.992 6.131  1.00 44.09 ?  191 GLU A OE1   1 
ATOM   1474 O OE2   . GLU A 1 191 ? 4.927   -25.078 5.190  1.00 43.57 -1 191 GLU A OE2   1 
ATOM   1475 N N     . GLN A 1 192 ? 7.901   -23.553 11.029 1.00 25.47 ?  192 GLN A N     1 
ATOM   1476 C CA    . GLN A 1 192 ? 8.824   -23.592 12.161 1.00 25.72 ?  192 GLN A CA    1 
ATOM   1477 C C     . GLN A 1 192 ? 8.121   -23.175 13.447 1.00 27.37 ?  192 GLN A C     1 
ATOM   1478 O O     . GLN A 1 192 ? 8.230   -23.848 14.478 1.00 26.95 ?  192 GLN A O     1 
ATOM   1479 C CB    . GLN A 1 192 ? 10.027  -22.685 11.901 1.00 23.20 ?  192 GLN A CB    1 
ATOM   1480 C CG    . GLN A 1 192 ? 11.053  -22.691 13.028 1.00 24.06 ?  192 GLN A CG    1 
ATOM   1481 C CD    . GLN A 1 192 ? 12.185  -21.706 12.803 1.00 23.28 ?  192 GLN A CD    1 
ATOM   1482 O OE1   . GLN A 1 192 ? 12.092  -20.823 11.953 1.00 24.15 ?  192 GLN A OE1   1 
ATOM   1483 N NE2   . GLN A 1 192 ? 13.261  -21.853 13.571 1.00 25.50 ?  192 GLN A NE2   1 
ATOM   1484 N N     . LEU A 1 193 ? 7.395   -22.056 13.401 1.00 21.61 ?  193 LEU A N     1 
ATOM   1485 C CA    . LEU A 1 193 ? 6.706   -21.555 14.584 1.00 21.79 ?  193 LEU A CA    1 
ATOM   1486 C C     . LEU A 1 193 ? 5.634   -22.519 15.069 1.00 23.08 ?  193 LEU A C     1 
ATOM   1487 O O     . LEU A 1 193 ? 5.270   -22.485 16.250 1.00 22.88 ?  193 LEU A O     1 
ATOM   1488 C CB    . LEU A 1 193 ? 6.089   -20.188 14.284 1.00 20.14 ?  193 LEU A CB    1 
ATOM   1489 C CG    . LEU A 1 193 ? 7.093   -19.037 14.193 1.00 19.61 ?  193 LEU A CG    1 
ATOM   1490 C CD1   . LEU A 1 193 ? 6.398   -17.752 13.775 1.00 15.37 ?  193 LEU A CD1   1 
ATOM   1491 C CD2   . LEU A 1 193 ? 7.812   -18.857 15.521 1.00 20.25 ?  193 LEU A CD2   1 
ATOM   1492 N N     . ASN A 1 194 ? 5.127   -23.378 14.182 1.00 22.51 ?  194 ASN A N     1 
ATOM   1493 C CA    . ASN A 1 194 ? 4.062   -24.308 14.535 1.00 24.84 ?  194 ASN A CA    1 
ATOM   1494 C C     . ASN A 1 194 ? 4.511   -25.348 15.555 1.00 22.28 ?  194 ASN A C     1 
ATOM   1495 O O     . ASN A 1 194 ? 3.662   -26.076 16.086 1.00 27.67 ?  194 ASN A O     1 
ATOM   1496 C CB    . ASN A 1 194 ? 3.527   -24.988 13.270 1.00 32.06 ?  194 ASN A CB    1 
ATOM   1497 C CG    . ASN A 1 194 ? 2.187   -25.666 13.490 1.00 32.10 ?  194 ASN A CG    1 
ATOM   1498 O OD1   . ASN A 1 194 ? 1.973   -26.794 13.049 1.00 35.80 ?  194 ASN A OD1   1 
ATOM   1499 N ND2   . ASN A 1 194 ? 1.277   -24.977 14.173 1.00 29.97 ?  194 ASN A ND2   1 
ATOM   1500 N N     . GLN A 1 195 ? 5.817   -25.440 15.832 1.00 24.81 ?  195 GLN A N     1 
ATOM   1501 C CA    . GLN A 1 195 ? 6.285   -26.292 16.919 1.00 28.85 ?  195 GLN A CA    1 
ATOM   1502 C C     . GLN A 1 195 ? 5.706   -25.848 18.255 1.00 30.32 ?  195 GLN A C     1 
ATOM   1503 O O     . GLN A 1 195 ? 5.539   -26.667 19.165 1.00 29.09 ?  195 GLN A O     1 
ATOM   1504 C CB    . GLN A 1 195 ? 7.810   -26.275 16.993 1.00 29.38 ?  195 GLN A CB    1 
ATOM   1505 C CG    . GLN A 1 195 ? 8.528   -26.796 15.762 1.00 31.17 ?  195 GLN A CG    1 
ATOM   1506 C CD    . GLN A 1 195 ? 10.021  -26.523 15.814 1.00 33.50 ?  195 GLN A CD    1 
ATOM   1507 O OE1   . GLN A 1 195 ? 10.778  -27.263 16.443 1.00 34.67 ?  195 GLN A OE1   1 
ATOM   1508 N NE2   . GLN A 1 195 ? 10.451  -25.451 15.157 1.00 31.52 ?  195 GLN A NE2   1 
ATOM   1509 N N     . TRP A 1 196 ? 5.400   -24.559 18.391 1.00 28.76 ?  196 TRP A N     1 
ATOM   1510 C CA    . TRP A 1 196 ? 4.940   -23.986 19.648 1.00 28.75 ?  196 TRP A CA    1 
ATOM   1511 C C     . TRP A 1 196 ? 3.615   -23.250 19.541 1.00 25.09 ?  196 TRP A C     1 
ATOM   1512 O O     . TRP A 1 196 ? 2.925   -23.119 20.561 1.00 28.99 ?  196 TRP A O     1 
ATOM   1513 C CB    . TRP A 1 196 ? 5.984   -23.012 20.214 1.00 24.17 ?  196 TRP A CB    1 
ATOM   1514 C CG    . TRP A 1 196 ? 7.365   -23.578 20.341 1.00 22.06 ?  196 TRP A CG    1 
ATOM   1515 C CD1   . TRP A 1 196 ? 7.888   -24.227 21.420 1.00 25.70 ?  196 TRP A CD1   1 
ATOM   1516 C CD2   . TRP A 1 196 ? 8.407   -23.529 19.358 1.00 22.73 ?  196 TRP A CD2   1 
ATOM   1517 N NE1   . TRP A 1 196 ? 9.189   -24.593 21.167 1.00 19.62 ?  196 TRP A NE1   1 
ATOM   1518 C CE2   . TRP A 1 196 ? 9.530   -24.176 19.908 1.00 25.57 ?  196 TRP A CE2   1 
ATOM   1519 C CE3   . TRP A 1 196 ? 8.497   -23.002 18.065 1.00 24.65 ?  196 TRP A CE3   1 
ATOM   1520 C CZ2   . TRP A 1 196 ? 10.729  -24.312 19.211 1.00 24.13 ?  196 TRP A CZ2   1 
ATOM   1521 C CZ3   . TRP A 1 196 ? 9.688   -23.140 17.374 1.00 26.37 ?  196 TRP A CZ3   1 
ATOM   1522 C CH2   . TRP A 1 196 ? 10.788  -23.790 17.950 1.00 24.56 ?  196 TRP A CH2   1 
ATOM   1523 N N     . TYR A 1 197 ? 3.229   -22.771 18.359 1.00 23.72 ?  197 TYR A N     1 
ATOM   1524 C CA    . TYR A 1 197 ? 2.025   -21.976 18.205 1.00 25.21 ?  197 TYR A CA    1 
ATOM   1525 C C     . TYR A 1 197 ? 1.114   -22.588 17.148 1.00 24.74 ?  197 TYR A C     1 
ATOM   1526 O O     . TYR A 1 197 ? 1.583   -22.924 16.052 1.00 23.68 ?  197 TYR A O     1 
ATOM   1527 C CB    . TYR A 1 197 ? 2.382   -20.526 17.825 1.00 22.67 ?  197 TYR A CB    1 
ATOM   1528 C CG    . TYR A 1 197 ? 3.316   -19.876 18.821 1.00 24.02 ?  197 TYR A CG    1 
ATOM   1529 C CD1   . TYR A 1 197 ? 4.694   -20.018 18.709 1.00 24.14 ?  197 TYR A CD1   1 
ATOM   1530 C CD2   . TYR A 1 197 ? 2.818   -19.145 19.890 1.00 17.10 ?  197 TYR A CD2   1 
ATOM   1531 C CE1   . TYR A 1 197 ? 5.549   -19.434 19.625 1.00 23.49 ?  197 TYR A CE1   1 
ATOM   1532 C CE2   . TYR A 1 197 ? 3.662   -18.560 20.809 1.00 21.63 ?  197 TYR A CE2   1 
ATOM   1533 C CZ    . TYR A 1 197 ? 5.025   -18.706 20.672 1.00 20.72 ?  197 TYR A CZ    1 
ATOM   1534 O OH    . TYR A 1 197 ? 5.869   -18.121 21.590 1.00 23.80 ?  197 TYR A OH    1 
ATOM   1535 N N     . PRO A 1 198 ? -0.178  -22.748 17.436 1.00 25.55 ?  198 PRO A N     1 
ATOM   1536 C CA    . PRO A 1 198 ? -1.104  -23.288 16.433 1.00 28.39 ?  198 PRO A CA    1 
ATOM   1537 C C     . PRO A 1 198 ? -1.218  -22.376 15.220 1.00 25.25 ?  198 PRO A C     1 
ATOM   1538 O O     . PRO A 1 198 ? -0.858  -21.197 15.252 1.00 26.25 ?  198 PRO A O     1 
ATOM   1539 C CB    . PRO A 1 198 ? -2.440  -23.386 17.183 1.00 22.85 ?  198 PRO A CB    1 
ATOM   1540 C CG    . PRO A 1 198 ? -2.122  -23.207 18.630 1.00 32.37 ?  198 PRO A CG    1 
ATOM   1541 C CD    . PRO A 1 198 ? -0.833  -22.458 18.723 1.00 22.48 ?  198 PRO A CD    1 
ATOM   1542 N N     . LEU A 1 199 ? -1.732  -22.948 14.129 1.00 27.75 ?  199 LEU A N     1 
ATOM   1543 C CA    . LEU A 1 199 ? -1.845  -22.189 12.889 1.00 29.98 ?  199 LEU A CA    1 
ATOM   1544 C C     . LEU A 1 199 ? -2.894  -21.090 12.994 1.00 26.74 ?  199 LEU A C     1 
ATOM   1545 O O     . LEU A 1 199 ? -2.804  -20.082 12.286 1.00 30.66 ?  199 LEU A O     1 
ATOM   1546 C CB    . LEU A 1 199 ? -2.159  -23.128 11.725 1.00 32.94 ?  199 LEU A CB    1 
ATOM   1547 C CG    . LEU A 1 199 ? -1.003  -24.048 11.311 1.00 32.58 ?  199 LEU A CG    1 
ATOM   1548 C CD1   . LEU A 1 199 ? -1.449  -25.035 10.244 1.00 27.31 ?  199 LEU A CD1   1 
ATOM   1549 C CD2   . LEU A 1 199 ? 0.193   -23.236 10.834 1.00 32.20 ?  199 LEU A CD2   1 
ATOM   1550 N N     . ASP A 1 200 ? -3.886  -21.256 13.868 1.00 26.12 ?  200 ASP A N     1 
ATOM   1551 C CA    . ASP A 1 200 ? -4.909  -20.241 14.080 1.00 28.81 ?  200 ASP A CA    1 
ATOM   1552 C C     . ASP A 1 200 ? -4.573  -19.317 15.244 1.00 27.53 ?  200 ASP A C     1 
ATOM   1553 O O     . ASP A 1 200 ? -5.423  -18.519 15.655 1.00 29.88 ?  200 ASP A O     1 
ATOM   1554 C CB    . ASP A 1 200 ? -6.281  -20.890 14.298 1.00 28.87 ?  200 ASP A CB    1 
ATOM   1555 C CG    . ASP A 1 200 ? -6.313  -21.809 15.501 1.00 35.40 ?  200 ASP A CG    1 
ATOM   1556 O OD1   . ASP A 1 200 ? -5.237  -22.113 16.059 1.00 36.41 ?  200 ASP A OD1   1 
ATOM   1557 O OD2   . ASP A 1 200 ? -7.423  -22.229 15.896 1.00 37.03 -1 200 ASP A OD2   1 
ATOM   1558 N N     . HIS A 1 201 ? -3.361  -19.422 15.788 1.00 27.83 ?  201 HIS A N     1 
ATOM   1559 C CA    . HIS A 1 201 ? -2.920  -18.523 16.846 1.00 27.63 ?  201 HIS A CA    1 
ATOM   1560 C C     . HIS A 1 201 ? -2.894  -17.086 16.342 1.00 28.06 ?  201 HIS A C     1 
ATOM   1561 O O     . HIS A 1 201 ? -2.271  -16.787 15.319 1.00 22.80 ?  201 HIS A O     1 
ATOM   1562 C CB    . HIS A 1 201 ? -1.532  -18.941 17.331 1.00 30.33 ?  201 HIS A CB    1 
ATOM   1563 C CG    . HIS A 1 201 ? -1.037  -18.163 18.510 1.00 27.66 ?  201 HIS A CG    1 
ATOM   1564 N ND1   . HIS A 1 201 ? -1.577  -18.295 19.771 1.00 25.76 ?  201 HIS A ND1   1 
ATOM   1565 C CD2   . HIS A 1 201 ? -0.043  -17.249 18.622 1.00 27.75 ?  201 HIS A CD2   1 
ATOM   1566 C CE1   . HIS A 1 201 ? -0.940  -17.494 20.608 1.00 28.50 ?  201 HIS A CE1   1 
ATOM   1567 N NE2   . HIS A 1 201 ? -0.006  -16.848 19.936 1.00 25.69 ?  201 HIS A NE2   1 
ATOM   1568 N N     . GLU A 1 202 ? -3.569  -16.194 17.063 1.00 23.09 ?  202 GLU A N     1 
ATOM   1569 C CA    . GLU A 1 202 ? -3.619  -14.799 16.650 1.00 24.76 ?  202 GLU A CA    1 
ATOM   1570 C C     . GLU A 1 202 ? -2.279  -14.129 16.919 1.00 24.10 ?  202 GLU A C     1 
ATOM   1571 O O     . GLU A 1 202 ? -1.759  -14.178 18.036 1.00 23.32 ?  202 GLU A O     1 
ATOM   1572 C CB    . GLU A 1 202 ? -4.737  -14.054 17.383 1.00 24.15 ?  202 GLU A CB    1 
ATOM   1573 C CG    . GLU A 1 202 ? -4.890  -12.602 16.938 1.00 26.39 ?  202 GLU A CG    1 
ATOM   1574 C CD    . GLU A 1 202 ? -6.060  -11.897 17.596 1.00 28.62 ?  202 GLU A CD    1 
ATOM   1575 O OE1   . GLU A 1 202 ? -6.001  -11.658 18.821 1.00 24.26 ?  202 GLU A OE1   1 
ATOM   1576 O OE2   . GLU A 1 202 ? -7.038  -11.571 16.889 1.00 27.62 -1 202 GLU A OE2   1 
ATOM   1577 N N     . VAL A 1 203 ? -1.720  -13.506 15.887 1.00 23.01 ?  203 VAL A N     1 
ATOM   1578 C CA    . VAL A 1 203 ? -0.513  -12.706 16.007 1.00 20.78 ?  203 VAL A CA    1 
ATOM   1579 C C     . VAL A 1 203 ? -0.857  -11.282 15.591 1.00 21.80 ?  203 VAL A C     1 
ATOM   1580 O O     . VAL A 1 203 ? -1.926  -11.011 15.047 1.00 22.88 ?  203 VAL A O     1 
ATOM   1581 C CB    . VAL A 1 203 ? 0.654   -13.264 15.167 1.00 20.80 ?  203 VAL A CB    1 
ATOM   1582 C CG1   . VAL A 1 203 ? 0.992   -14.682 15.608 1.00 20.24 ?  203 VAL A CG1   1 
ATOM   1583 C CG2   . VAL A 1 203 ? 0.310   -13.229 13.688 1.00 20.96 ?  203 VAL A CG2   1 
ATOM   1584 N N     . VAL A 1 204 ? 0.068   -10.367 15.850 1.00 20.06 ?  204 VAL A N     1 
ATOM   1585 C CA    . VAL A 1 204 ? -0.161  -8.944  15.625 1.00 22.03 ?  204 VAL A CA    1 
ATOM   1586 C C     . VAL A 1 204 ? 0.996   -8.377  14.815 1.00 19.38 ?  204 VAL A C     1 
ATOM   1587 O O     . VAL A 1 204 ? 2.160   -8.504  15.210 1.00 21.75 ?  204 VAL A O     1 
ATOM   1588 C CB    . VAL A 1 204 ? -0.312  -8.169  16.950 1.00 21.59 ?  204 VAL A CB    1 
ATOM   1589 C CG1   . VAL A 1 204 ? -0.505  -6.686  16.678 1.00 23.03 ?  204 VAL A CG1   1 
ATOM   1590 C CG2   . VAL A 1 204 ? -1.467  -8.729  17.767 1.00 22.73 ?  204 VAL A CG2   1 
ATOM   1591 N N     . ILE A 1 205 ? 0.677   -7.754  13.686 1.00 18.40 ?  205 ILE A N     1 
ATOM   1592 C CA    . ILE A 1 205 ? 1.638   -6.946  12.947 1.00 18.82 ?  205 ILE A CA    1 
ATOM   1593 C C     . ILE A 1 205 ? 1.531   -5.524  13.482 1.00 18.96 ?  205 ILE A C     1 
ATOM   1594 O O     . ILE A 1 205 ? 0.513   -4.853  13.301 1.00 20.96 ?  205 ILE A O     1 
ATOM   1595 C CB    . ILE A 1 205 ? 1.390   -7.003  11.436 1.00 18.63 ?  205 ILE A CB    1 
ATOM   1596 C CG1   . ILE A 1 205 ? 1.557   -8.439  10.930 1.00 16.71 ?  205 ILE A CG1   1 
ATOM   1597 C CG2   . ILE A 1 205 ? 2.327   -6.050  10.706 1.00 18.81 ?  205 ILE A CG2   1 
ATOM   1598 C CD1   . ILE A 1 205 ? 1.027   -8.661  9.530  1.00 22.95 ?  205 ILE A CD1   1 
ATOM   1599 N N     . TYR A 1 206 ? 2.584   -5.066  14.146 1.00 20.59 ?  206 TYR A N     1 
ATOM   1600 C CA    . TYR A 1 206 ? 2.609   -3.772  14.809 1.00 20.03 ?  206 TYR A CA    1 
ATOM   1601 C C     . TYR A 1 206 ? 3.541   -2.826  14.068 1.00 21.40 ?  206 TYR A C     1 
ATOM   1602 O O     . TYR A 1 206 ? 4.651   -3.206  13.684 1.00 20.46 ?  206 TYR A O     1 
ATOM   1603 C CB    . TYR A 1 206 ? 3.065   -3.910  16.266 1.00 19.39 ?  206 TYR A CB    1 
ATOM   1604 C CG    . TYR A 1 206 ? 3.314   -2.594  16.967 1.00 19.06 ?  206 TYR A CG    1 
ATOM   1605 C CD1   . TYR A 1 206 ? 2.260   -1.761  17.318 1.00 20.95 ?  206 TYR A CD1   1 
ATOM   1606 C CD2   . TYR A 1 206 ? 4.605   -2.185  17.276 1.00 19.58 ?  206 TYR A CD2   1 
ATOM   1607 C CE1   . TYR A 1 206 ? 2.485   -0.557  17.963 1.00 18.68 ?  206 TYR A CE1   1 
ATOM   1608 C CE2   . TYR A 1 206 ? 4.838   -0.981  17.919 1.00 17.80 ?  206 TYR A CE2   1 
ATOM   1609 C CZ    . TYR A 1 206 ? 3.775   -0.175  18.259 1.00 17.63 ?  206 TYR A CZ    1 
ATOM   1610 O OH    . TYR A 1 206 ? 3.999   1.023   18.900 1.00 24.03 ?  206 TYR A OH    1 
ATOM   1611 N N     . GLU A 1 207 ? 3.082   -1.594  13.864 1.00 19.26 ?  207 GLU A N     1 
ATOM   1612 C CA    . GLU A 1 207 ? 3.938   -0.517  13.374 1.00 20.79 ?  207 GLU A CA    1 
ATOM   1613 C C     . GLU A 1 207 ? 3.640   0.731   14.192 1.00 21.21 ?  207 GLU A C     1 
ATOM   1614 O O     . GLU A 1 207 ? 2.551   1.302   14.087 1.00 20.80 ?  207 GLU A O     1 
ATOM   1615 C CB    . GLU A 1 207 ? 3.726   -0.257  11.881 1.00 20.96 ?  207 GLU A CB    1 
ATOM   1616 C CG    . GLU A 1 207 ? 4.115   -1.426  10.983 1.00 18.15 ?  207 GLU A CG    1 
ATOM   1617 C CD    . GLU A 1 207 ? 3.684   -1.228  9.543  1.00 23.51 ?  207 GLU A CD    1 
ATOM   1618 O OE1   . GLU A 1 207 ? 3.211   -0.121  9.207  1.00 19.90 ?  207 GLU A OE1   1 
ATOM   1619 O OE2   . GLU A 1 207 ? 3.820   -2.179  8.745  1.00 21.59 -1 207 GLU A OE2   1 
ATOM   1620 N N     . ALA A 1 208 ? 4.599   1.140   15.017 1.00 18.68 ?  208 ALA A N     1 
ATOM   1621 C CA    . ALA A 1 208 ? 4.493   2.398   15.737 1.00 22.50 ?  208 ALA A CA    1 
ATOM   1622 C C     . ALA A 1 208 ? 4.424   3.560   14.755 1.00 21.13 ?  208 ALA A C     1 
ATOM   1623 O O     . ALA A 1 208 ? 5.044   3.542   13.689 1.00 19.55 ?  208 ALA A O     1 
ATOM   1624 C CB    . ALA A 1 208 ? 5.687   2.578   16.680 1.00 20.50 ?  208 ALA A CB    1 
ATOM   1625 N N     . ALA A 1 209 ? 3.655   4.577   15.122 1.00 16.94 ?  209 ALA A N     1 
ATOM   1626 C CA    . ALA A 1 209 ? 3.490   5.734   14.256 1.00 20.12 ?  209 ALA A CA    1 
ATOM   1627 C C     . ALA A 1 209 ? 4.736   6.609   14.276 1.00 18.60 ?  209 ALA A C     1 
ATOM   1628 O O     . ALA A 1 209 ? 5.402   6.750   15.305 1.00 20.40 ?  209 ALA A O     1 
ATOM   1629 C CB    . ALA A 1 209 ? 2.269   6.550   14.685 1.00 16.87 ?  209 ALA A CB    1 
ATOM   1630 N N     . ASN A 1 210 ? 5.053   7.194   13.121 1.00 17.74 ?  210 ASN A N     1 
ATOM   1631 C CA    . ASN A 1 210 ? 6.162   8.130   13.001 1.00 16.48 ?  210 ASN A CA    1 
ATOM   1632 C C     . ASN A 1 210 ? 5.712   9.583   13.009 1.00 14.63 ?  210 ASN A C     1 
ATOM   1633 O O     . ASN A 1 210 ? 6.544   10.472  13.224 1.00 16.59 ?  210 ASN A O     1 
ATOM   1634 C CB    . ASN A 1 210 ? 6.960   7.860   11.717 1.00 17.96 ?  210 ASN A CB    1 
ATOM   1635 C CG    . ASN A 1 210 ? 7.655   6.512   11.735 1.00 18.56 ?  210 ASN A CG    1 
ATOM   1636 O OD1   . ASN A 1 210 ? 7.438   5.678   10.856 1.00 19.66 ?  210 ASN A OD1   1 
ATOM   1637 N ND2   . ASN A 1 210 ? 8.496   6.293   12.738 1.00 17.15 ?  210 ASN A ND2   1 
ATOM   1638 N N     . LEU A 1 211 ? 4.425   9.844   12.780 1.00 18.20 ?  211 LEU A N     1 
ATOM   1639 C CA    . LEU A 1 211 ? 3.892   11.194  12.731 1.00 19.60 ?  211 LEU A CA    1 
ATOM   1640 C C     . LEU A 1 211 ? 2.797   11.370  13.779 1.00 20.18 ?  211 LEU A C     1 
ATOM   1641 O O     . LEU A 1 211 ? 2.095   10.411  14.115 1.00 15.77 ?  211 LEU A O     1 
ATOM   1642 C CB    . LEU A 1 211 ? 3.325   11.509  11.339 1.00 18.86 ?  211 LEU A CB    1 
ATOM   1643 C CG    . LEU A 1 211 ? 4.358   11.557  10.210 1.00 21.43 ?  211 LEU A CG    1 
ATOM   1644 C CD1   . LEU A 1 211 ? 3.692   11.884  8.881  1.00 16.98 ?  211 LEU A CD1   1 
ATOM   1645 C CD2   . LEU A 1 211 ? 5.459   12.558  10.530 1.00 20.59 ?  211 LEU A CD2   1 
ATOM   1646 N N     . PRO A 1 212 ? 2.621   12.585  14.310 1.00 18.99 ?  212 PRO A N     1 
ATOM   1647 C CA    . PRO A 1 212 ? 1.653   12.776  15.404 1.00 19.45 ?  212 PRO A CA    1 
ATOM   1648 C C     . PRO A 1 212 ? 0.202   12.714  14.960 1.00 24.14 ?  212 PRO A C     1 
ATOM   1649 O O     . PRO A 1 212 ? -0.683  12.630  15.823 1.00 24.60 ?  212 PRO A O     1 
ATOM   1650 C CB    . PRO A 1 212 ? 2.006   14.166  15.947 1.00 22.04 ?  212 PRO A CB    1 
ATOM   1651 C CG    . PRO A 1 212 ? 2.621   14.877  14.788 1.00 20.53 ?  212 PRO A CG    1 
ATOM   1652 C CD    . PRO A 1 212 ? 3.333   13.830  13.973 1.00 19.33 ?  212 PRO A CD    1 
ATOM   1653 N N     . ILE A 1 213 ? -0.071  12.744  13.656 1.00 21.09 ?  213 ILE A N     1 
ATOM   1654 C CA    . ILE A 1 213 ? -1.431  12.629  13.142 1.00 22.84 ?  213 ILE A CA    1 
ATOM   1655 C C     . ILE A 1 213 ? -1.738  11.206  12.692 1.00 26.80 ?  213 ILE A C     1 
ATOM   1656 O O     . ILE A 1 213 ? -2.767  10.962  12.058 1.00 20.39 ?  213 ILE A O     1 
ATOM   1657 C CB    . ILE A 1 213 ? -1.689  13.642  12.007 1.00 23.64 ?  213 ILE A CB    1 
ATOM   1658 C CG1   . ILE A 1 213 ? -0.577  13.626  10.942 1.00 28.15 ?  213 ILE A CG1   1 
ATOM   1659 C CG2   . ILE A 1 213 ? -1.803  15.048  12.572 1.00 26.38 ?  213 ILE A CG2   1 
ATOM   1660 C CD1   . ILE A 1 213 ? -0.494  12.386  10.066 1.00 25.68 ?  213 ILE A CD1   1 
ATOM   1661 N N     . GLN A 1 214 ? -0.861  10.261  13.009 1.00 23.14 ?  214 GLN A N     1 
ATOM   1662 C CA    . GLN A 1 214 ? -0.904  8.914   12.463 1.00 22.53 ?  214 GLN A CA    1 
ATOM   1663 C C     . GLN A 1 214 ? -1.213  7.918   13.571 1.00 21.68 ?  214 GLN A C     1 
ATOM   1664 O O     . GLN A 1 214 ? -0.604  7.967   14.645 1.00 25.10 ?  214 GLN A O     1 
ATOM   1665 C CB    . GLN A 1 214 ? 0.428   8.556   11.797 1.00 20.34 ?  214 GLN A CB    1 
ATOM   1666 C CG    . GLN A 1 214 ? 0.525   7.108   11.343 1.00 22.87 ?  214 GLN A CG    1 
ATOM   1667 C CD    . GLN A 1 214 ? 1.930   6.718   10.923 1.00 23.43 ?  214 GLN A CD    1 
ATOM   1668 O OE1   . GLN A 1 214 ? 2.890   7.448   11.169 1.00 23.62 ?  214 GLN A OE1   1 
ATOM   1669 N NE2   . GLN A 1 214 ? 2.056   5.558   10.287 1.00 22.19 ?  214 GLN A NE2   1 
ATOM   1670 N N     . ALA A 1 215 ? -2.163  7.035   13.312 1.00 20.95 ?  215 ALA A N     1 
ATOM   1671 C CA    . ALA A 1 215 ? -2.438  5.953   14.237 1.00 22.18 ?  215 ALA A CA    1 
ATOM   1672 C C     . ALA A 1 215 ? -1.447  4.813   14.009 1.00 25.30 ?  215 ALA A C     1 
ATOM   1673 O O     . ALA A 1 215 ? -0.982  4.601   12.886 1.00 26.40 ?  215 ALA A O     1 
ATOM   1674 C CB    . ALA A 1 215 ? -3.864  5.446   14.055 1.00 19.26 ?  215 ALA A CB    1 
ATOM   1675 N N     . PRO A 1 216 ? -1.096  4.074   15.056 1.00 23.76 ?  216 PRO A N     1 
ATOM   1676 C CA    . PRO A 1 216 ? -0.220  2.916   14.870 1.00 23.90 ?  216 PRO A CA    1 
ATOM   1677 C C     . PRO A 1 216 ? -0.943  1.801   14.135 1.00 24.12 ?  216 PRO A C     1 
ATOM   1678 O O     . PRO A 1 216 ? -2.171  1.710   14.132 1.00 22.20 ?  216 PRO A O     1 
ATOM   1679 C CB    . PRO A 1 216 ? 0.125   2.504   16.304 1.00 25.30 ?  216 PRO A CB    1 
ATOM   1680 C CG    . PRO A 1 216 ? -1.089  2.899   17.080 1.00 23.86 ?  216 PRO A CG    1 
ATOM   1681 C CD    . PRO A 1 216 ? -1.525  4.209   16.459 1.00 28.11 ?  216 PRO A CD    1 
ATOM   1682 N N     . ARG A 1 217 ? -0.159  0.944   13.496 1.00 19.13 ?  217 ARG A N     1 
ATOM   1683 C CA    . ARG A 1 217 ? -0.688  -0.264  12.881 1.00 23.22 ?  217 ARG A CA    1 
ATOM   1684 C C     . ARG A 1 217 ? -0.747  -1.361  13.934 1.00 21.42 ?  217 ARG A C     1 
ATOM   1685 O O     . ARG A 1 217 ? 0.275   -1.714  14.531 1.00 21.83 ?  217 ARG A O     1 
ATOM   1686 C CB    . ARG A 1 217 ? 0.167   -0.705  11.694 1.00 19.28 ?  217 ARG A CB    1 
ATOM   1687 C CG    . ARG A 1 217 ? -0.444  -1.850  10.895 1.00 25.10 ?  217 ARG A CG    1 
ATOM   1688 C CD    . ARG A 1 217 ? 0.454   -2.263  9.741  1.00 22.67 ?  217 ARG A CD    1 
ATOM   1689 N NE    . ARG A 1 217 ? -0.091  -3.392  8.995  1.00 27.17 ?  217 ARG A NE    1 
ATOM   1690 C CZ    . ARG A 1 217 ? 0.590   -4.090  8.095  1.00 27.52 ?  217 ARG A CZ    1 
ATOM   1691 N NH1   . ARG A 1 217 ? 1.861   -3.827  7.832  1.00 19.42 ?  217 ARG A NH1   1 
ATOM   1692 N NH2   . ARG A 1 217 ? -0.016  -5.080  7.446  1.00 23.05 ?  217 ARG A NH2   1 
ATOM   1693 N N     . ILE A 1 218 ? -1.947  -1.876  14.181 1.00 20.69 ?  218 ILE A N     1 
ATOM   1694 C CA    . ILE A 1 218 ? -2.148  -3.011  15.074 1.00 22.56 ?  218 ILE A CA    1 
ATOM   1695 C C     . ILE A 1 218 ? -3.050  -4.000  14.350 1.00 27.94 ?  218 ILE A C     1 
ATOM   1696 O O     . ILE A 1 218 ? -4.268  -4.017  14.554 1.00 29.28 ?  218 ILE A O     1 
ATOM   1697 C CB    . ILE A 1 218 ? -2.750  -2.582  16.427 1.00 25.79 ?  218 ILE A CB    1 
ATOM   1698 C CG1   . ILE A 1 218 ? -1.914  -1.462  17.058 1.00 22.12 ?  218 ILE A CG1   1 
ATOM   1699 C CG2   . ILE A 1 218 ? -2.839  -3.769  17.377 1.00 20.66 ?  218 ILE A CG2   1 
ATOM   1700 C CD1   . ILE A 1 218 ? -2.454  -0.966  18.381 1.00 26.51 ?  218 ILE A CD1   1 
ATOM   1701 N N     . GLU A 1 219 ? -2.457  -4.822  13.491 1.00 26.06 ?  219 GLU A N     1 
ATOM   1702 C CA    . GLU A 1 219 ? -3.203  -5.695  12.595 1.00 25.12 ?  219 GLU A CA    1 
ATOM   1703 C C     . GLU A 1 219 ? -3.171  -7.116  13.143 1.00 31.42 ?  219 GLU A C     1 
ATOM   1704 O O     . GLU A 1 219 ? -2.104  -7.733  13.231 1.00 23.44 ?  219 GLU A O     1 
ATOM   1705 C CB    . GLU A 1 219 ? -2.625  -5.648  11.180 1.00 24.81 ?  219 GLU A CB    1 
ATOM   1706 C CG    . GLU A 1 219 ? -3.440  -6.420  10.153 1.00 32.81 ?  219 GLU A CG    1 
ATOM   1707 C CD    . GLU A 1 219 ? -2.809  -6.398  8.776  1.00 33.71 ?  219 GLU A CD    1 
ATOM   1708 O OE1   . GLU A 1 219 ? -2.433  -5.302  8.310  1.00 34.01 ?  219 GLU A OE1   1 
ATOM   1709 O OE2   . GLU A 1 219 ? -2.688  -7.477  8.158  1.00 34.56 -1 219 GLU A OE2   1 
ATOM   1710 N N     . ARG A 1 220 ? -4.341  -7.625  13.510 1.00 27.07 ?  220 ARG A N     1 
ATOM   1711 C CA    . ARG A 1 220 ? -4.483  -8.953  14.083 1.00 24.36 ?  220 ARG A CA    1 
ATOM   1712 C C     . ARG A 1 220 ? -4.887  -9.944  13.003 1.00 25.92 ?  220 ARG A C     1 
ATOM   1713 O O     . ARG A 1 220 ? -5.750  -9.656  12.169 1.00 26.39 ?  220 ARG A O     1 
ATOM   1714 C CB    . ARG A 1 220 ? -5.511  -8.936  15.213 1.00 26.70 ?  220 ARG A CB    1 
ATOM   1715 C CG    . ARG A 1 220 ? -5.091  -8.015  16.337 1.00 30.55 ?  220 ARG A CG    1 
ATOM   1716 C CD    . ARG A 1 220 ? -6.238  -7.617  17.242 1.00 32.51 ?  220 ARG A CD    1 
ATOM   1717 N NE    . ARG A 1 220 ? -5.770  -6.706  18.278 1.00 29.63 ?  220 ARG A NE    1 
ATOM   1718 C CZ    . ARG A 1 220 ? -4.975  -7.057  19.281 1.00 32.78 ?  220 ARG A CZ    1 
ATOM   1719 N NH1   . ARG A 1 220 ? -4.660  -8.323  19.507 1.00 36.09 ?  220 ARG A NH1   1 
ATOM   1720 N NH2   . ARG A 1 220 ? -4.505  -6.117  20.098 1.00 24.06 ?  220 ARG A NH2   1 
ATOM   1721 N N     . LEU A 1 221 ? -4.253  -11.113 13.022 1.00 24.17 ?  221 LEU A N     1 
ATOM   1722 C CA    . LEU A 1 221 ? -4.477  -12.129 12.004 1.00 20.52 ?  221 LEU A CA    1 
ATOM   1723 C C     . LEU A 1 221 ? -3.978  -13.461 12.537 1.00 26.54 ?  221 LEU A C     1 
ATOM   1724 O O     . LEU A 1 221 ? -3.061  -13.484 13.366 1.00 22.07 ?  221 LEU A O     1 
ATOM   1725 C CB    . LEU A 1 221 ? -3.753  -11.770 10.694 1.00 27.00 ?  221 LEU A CB    1 
ATOM   1726 C CG    . LEU A 1 221 ? -2.222  -11.873 10.635 1.00 27.56 ?  221 LEU A CG    1 
ATOM   1727 C CD1   . LEU A 1 221 ? -1.747  -11.809 9.193  1.00 28.36 ?  221 LEU A CD1   1 
ATOM   1728 C CD2   . LEU A 1 221 ? -1.538  -10.787 11.459 1.00 23.86 ?  221 LEU A CD2   1 
ATOM   1729 N N     . PRO A 1 222 ? -4.563  -14.577 12.103 1.00 23.05 ?  222 PRO A N     1 
ATOM   1730 C CA    . PRO A 1 222 ? -4.011  -15.882 12.481 1.00 24.03 ?  222 PRO A CA    1 
ATOM   1731 C C     . PRO A 1 222 ? -2.617  -16.058 11.904 1.00 24.82 ?  222 PRO A C     1 
ATOM   1732 O O     . PRO A 1 222 ? -2.282  -15.505 10.852 1.00 22.69 ?  222 PRO A O     1 
ATOM   1733 C CB    . PRO A 1 222 ? -5.002  -16.885 11.876 1.00 22.99 ?  222 PRO A CB    1 
ATOM   1734 C CG    . PRO A 1 222 ? -5.748  -16.134 10.827 1.00 23.10 ?  222 PRO A CG    1 
ATOM   1735 C CD    . PRO A 1 222 ? -5.743  -14.689 11.228 1.00 22.01 ?  222 PRO A CD    1 
ATOM   1736 N N     . LEU A 1 223 ? -1.794  -16.827 12.624 1.00 23.30 ?  223 LEU A N     1 
ATOM   1737 C CA    . LEU A 1 223 ? -0.421  -17.064 12.187 1.00 23.64 ?  223 LEU A CA    1 
ATOM   1738 C C     . LEU A 1 223 ? -0.374  -17.636 10.774 1.00 21.97 ?  223 LEU A C     1 
ATOM   1739 O O     . LEU A 1 223 ? 0.561   -17.346 10.018 1.00 27.57 ?  223 LEU A O     1 
ATOM   1740 C CB    . LEU A 1 223 ? 0.284   -17.999 13.171 1.00 23.13 ?  223 LEU A CB    1 
ATOM   1741 C CG    . LEU A 1 223 ? 1.665   -18.530 12.791 1.00 23.92 ?  223 LEU A CG    1 
ATOM   1742 C CD1   . LEU A 1 223 ? 2.647   -17.388 12.576 1.00 18.74 ?  223 LEU A CD1   1 
ATOM   1743 C CD2   . LEU A 1 223 ? 2.182   -19.491 13.849 1.00 23.29 ?  223 LEU A CD2   1 
ATOM   1744 N N     . ALA A 1 224 ? -1.374  -18.438 10.399 1.00 26.40 ?  224 ALA A N     1 
ATOM   1745 C CA    . ALA A 1 224 ? -1.373  -19.067 9.082  1.00 28.67 ?  224 ALA A CA    1 
ATOM   1746 C C     . ALA A 1 224 ? -1.409  -18.034 7.963  1.00 23.29 ?  224 ALA A C     1 
ATOM   1747 O O     . ALA A 1 224 ? -0.904  -18.295 6.866  1.00 26.04 ?  224 ALA A O     1 
ATOM   1748 C CB    . ALA A 1 224 ? -2.559  -20.025 8.956  1.00 30.64 ?  224 ALA A CB    1 
ATOM   1749 N N     . ASN A 1 225 ? -2.000  -16.868 8.214  1.00 29.67 ?  225 ASN A N     1 
ATOM   1750 C CA    . ASN A 1 225 ? -2.178  -15.851 7.186  1.00 27.50 ?  225 ASN A CA    1 
ATOM   1751 C C     . ASN A 1 225 ? -0.979  -14.923 7.054  1.00 25.39 ?  225 ASN A C     1 
ATOM   1752 O O     . ASN A 1 225 ? -1.006  -14.017 6.211  1.00 25.13 ?  225 ASN A O     1 
ATOM   1753 C CB    . ASN A 1 225 ? -3.437  -15.023 7.470  1.00 25.34 ?  225 ASN A CB    1 
ATOM   1754 C CG    . ASN A 1 225 ? -4.713  -15.802 7.225  1.00 31.16 ?  225 ASN A CG    1 
ATOM   1755 O OD1   . ASN A 1 225 ? -4.683  -17.016 7.020  1.00 28.82 ?  225 ASN A OD1   1 
ATOM   1756 N ND2   . ASN A 1 225 ? -5.843  -15.105 7.240  1.00 26.03 ?  225 ASN A ND2   1 
ATOM   1757 N N     . LEU A 1 226 ? 0.058   -15.116 7.872  1.00 27.41 ?  226 LEU A N     1 
ATOM   1758 C CA    . LEU A 1 226 ? 1.228   -14.241 7.815  1.00 21.21 ?  226 LEU A CA    1 
ATOM   1759 C C     . LEU A 1 226 ? 1.872   -14.192 6.433  1.00 25.14 ?  226 LEU A C     1 
ATOM   1760 O O     . LEU A 1 226 ? 2.198   -13.083 5.973  1.00 20.20 ?  226 LEU A O     1 
ATOM   1761 C CB    . LEU A 1 226 ? 2.242   -14.666 8.879  1.00 21.99 ?  226 LEU A CB    1 
ATOM   1762 C CG    . LEU A 1 226 ? 3.608   -13.973 8.798  1.00 24.56 ?  226 LEU A CG    1 
ATOM   1763 C CD1   . LEU A 1 226 ? 3.463   -12.476 9.045  1.00 25.22 ?  226 LEU A CD1   1 
ATOM   1764 C CD2   . LEU A 1 226 ? 4.604   -14.593 9.768  1.00 21.52 ?  226 LEU A CD2   1 
ATOM   1765 N N     . PRO A 1 227 ? 2.087   -15.308 5.724  1.00 29.15 ?  227 PRO A N     1 
ATOM   1766 C CA    . PRO A 1 227 ? 2.766   -15.217 4.419  1.00 24.96 ?  227 PRO A CA    1 
ATOM   1767 C C     . PRO A 1 227 ? 2.037   -14.362 3.398  1.00 25.15 ?  227 PRO A C     1 
ATOM   1768 O O     . PRO A 1 227 ? 2.670   -13.897 2.444  1.00 27.34 ?  227 PRO A O     1 
ATOM   1769 C CB    . PRO A 1 227 ? 2.848   -16.681 3.964  1.00 20.92 ?  227 PRO A CB    1 
ATOM   1770 C CG    . PRO A 1 227 ? 2.780   -17.466 5.222  1.00 21.84 ?  227 PRO A CG    1 
ATOM   1771 C CD    . PRO A 1 227 ? 1.819   -16.715 6.082  1.00 20.45 ?  227 PRO A CD    1 
ATOM   1772 N N     . GLN A 1 228 ? 0.735   -14.140 3.558  1.00 19.48 ?  228 GLN A N     1 
ATOM   1773 C CA    . GLN A 1 228 ? -0.026  -13.339 2.609  1.00 29.31 ?  228 GLN A CA    1 
ATOM   1774 C C     . GLN A 1 228 ? -0.135  -11.880 3.027  1.00 26.51 ?  228 GLN A C     1 
ATOM   1775 O O     . GLN A 1 228 ? -0.710  -11.078 2.285  1.00 22.47 ?  228 GLN A O     1 
ATOM   1776 C CB    . GLN A 1 228 ? -1.434  -13.917 2.430  1.00 30.83 ?  228 GLN A CB    1 
ATOM   1777 C CG    . GLN A 1 228 ? -1.506  -15.151 1.546  1.00 36.11 ?  228 GLN A CG    1 
ATOM   1778 C CD    . GLN A 1 228 ? -1.016  -16.396 2.254  1.00 29.53 ?  228 GLN A CD    1 
ATOM   1779 O OE1   . GLN A 1 228 ? -1.615  -16.842 3.231  1.00 38.27 ?  228 GLN A OE1   1 
ATOM   1780 N NE2   . GLN A 1 228 ? 0.076   -16.969 1.760  1.00 40.61 ?  228 GLN A NE2   1 
ATOM   1781 N N     . ALA A 1 229 ? 0.410   -11.518 4.183  1.00 22.88 ?  229 ALA A N     1 
ATOM   1782 C CA    . ALA A 1 229 ? 0.188   -10.204 4.758  1.00 20.32 ?  229 ALA A CA    1 
ATOM   1783 C C     . ALA A 1 229 ? 1.103   -9.164  4.116  1.00 22.60 ?  229 ALA A C     1 
ATOM   1784 O O     . ALA A 1 229 ? 2.143   -9.478  3.532  1.00 23.77 ?  229 ALA A O     1 
ATOM   1785 C CB    . ALA A 1 229 ? 0.412   -10.234 6.269  1.00 21.04 ?  229 ALA A CB    1 
ATOM   1786 N N     . HIS A 1 230 ? 0.696   -7.903  4.239  1.00 24.49 ?  230 HIS A N     1 
ATOM   1787 C CA    . HIS A 1 230 ? 1.449   -6.767  3.715  1.00 31.24 ?  230 HIS A CA    1 
ATOM   1788 C C     . HIS A 1 230 ? 2.436   -6.297  4.778  1.00 31.70 ?  230 HIS A C     1 
ATOM   1789 O O     . HIS A 1 230 ? 2.046   -5.664  5.763  1.00 28.98 ?  230 HIS A O     1 
ATOM   1790 C CB    . HIS A 1 230 ? 0.495   -5.644  3.311  1.00 30.69 ?  230 HIS A CB    1 
ATOM   1791 C CG    . HIS A 1 230 ? 1.168   -4.477  2.660  1.00 38.03 ?  230 HIS A CG    1 
ATOM   1792 N ND1   . HIS A 1 230 ? 1.248   -4.330  1.292  1.00 41.69 ?  230 HIS A ND1   1 
ATOM   1793 C CD2   . HIS A 1 230 ? 1.791   -3.400  3.191  1.00 36.95 ?  230 HIS A CD2   1 
ATOM   1794 C CE1   . HIS A 1 230 ? 1.889   -3.210  1.009  1.00 46.53 ?  230 HIS A CE1   1 
ATOM   1795 N NE2   . HIS A 1 230 ? 2.233   -2.629  2.144  1.00 39.92 ?  230 HIS A NE2   1 
ATOM   1796 N N     . LEU A 1 231 ? 3.713   -6.607  4.584  1.00 22.83 ?  231 LEU A N     1 
ATOM   1797 C CA    . LEU A 1 231 ? 4.757   -6.261  5.536  1.00 26.12 ?  231 LEU A CA    1 
ATOM   1798 C C     . LEU A 1 231 ? 5.649   -5.157  4.982  1.00 27.66 ?  231 LEU A C     1 
ATOM   1799 O O     . LEU A 1 231 ? 5.874   -5.059  3.774  1.00 29.83 ?  231 LEU A O     1 
ATOM   1800 C CB    . LEU A 1 231 ? 5.607   -7.485  5.894  1.00 20.85 ?  231 LEU A CB    1 
ATOM   1801 C CG    . LEU A 1 231 ? 4.825   -8.638  6.525  1.00 25.92 ?  231 LEU A CG    1 
ATOM   1802 C CD1   . LEU A 1 231 ? 5.679   -9.894  6.616  1.00 22.88 ?  231 LEU A CD1   1 
ATOM   1803 C CD2   . LEU A 1 231 ? 4.303   -8.232  7.895  1.00 19.23 ?  231 LEU A CD2   1 
ATOM   1804 N N     . MET A 1 232 ? 6.146   -4.324  5.882  1.00 25.25 ?  232 MET A N     1 
ATOM   1805 C CA    . MET A 1 232 ? 7.027   -3.207  5.582  1.00 20.59 ?  232 MET A CA    1 
ATOM   1806 C C     . MET A 1 232 ? 8.297   -3.337  6.405  1.00 25.30 ?  232 MET A C     1 
ATOM   1807 O O     . MET A 1 232 ? 8.329   -4.071  7.401  1.00 22.03 ?  232 MET A O     1 
ATOM   1808 C CB    . MET A 1 232 ? 6.332   -1.870  5.884  1.00 26.26 ?  232 MET A CB    1 
ATOM   1809 C CG    . MET A 1 232 ? 5.106   -1.609  5.031  1.00 30.96 ?  232 MET A CG    1 
ATOM   1810 S SD    . MET A 1 232 ? 5.510   -1.412  3.286  1.00 38.57 ?  232 MET A SD    1 
ATOM   1811 C CE    . MET A 1 232 ? 6.403   0.141   3.324  1.00 39.18 ?  232 MET A CE    1 
ATOM   1812 N N     . PRO A 1 233 ? 9.376   -2.655  6.006  1.00 23.75 ?  233 PRO A N     1 
ATOM   1813 C CA    . PRO A 1 233 ? 10.599  -2.667  6.830  1.00 27.90 ?  233 PRO A CA    1 
ATOM   1814 C C     . PRO A 1 233 ? 10.388  -2.264  8.282  1.00 26.00 ?  233 PRO A C     1 
ATOM   1815 O O     . PRO A 1 233 ? 11.147  -2.714  9.149  1.00 24.67 ?  233 PRO A O     1 
ATOM   1816 C CB    . PRO A 1 233 ? 11.514  -1.677  6.098  1.00 23.93 ?  233 PRO A CB    1 
ATOM   1817 C CG    . PRO A 1 233 ? 11.094  -1.800  4.671  1.00 28.03 ?  233 PRO A CG    1 
ATOM   1818 C CD    . PRO A 1 233 ? 9.596   -1.964  4.721  1.00 27.74 ?  233 PRO A CD    1 
ATOM   1819 N N     . ILE A 1 234 ? 9.377   -1.443  8.586  1.00 23.17 ?  234 ILE A N     1 
ATOM   1820 C CA    . ILE A 1 234 ? 9.155   -1.007  9.961  1.00 21.60 ?  234 ILE A CA    1 
ATOM   1821 C C     . ILE A 1 234 ? 8.238   -1.951  10.726 1.00 22.00 ?  234 ILE A C     1 
ATOM   1822 O O     . ILE A 1 234 ? 7.887   -1.664  11.877 1.00 21.18 ?  234 ILE A O     1 
ATOM   1823 C CB    . ILE A 1 234 ? 8.585   0.428   10.022 1.00 25.94 ?  234 ILE A CB    1 
ATOM   1824 C CG1   . ILE A 1 234 ? 7.309   0.545   9.182  1.00 23.46 ?  234 ILE A CG1   1 
ATOM   1825 C CG2   . ILE A 1 234 ? 9.631   1.441   9.577  1.00 24.12 ?  234 ILE A CG2   1 
ATOM   1826 C CD1   . ILE A 1 234 ? 6.422   1.702   9.592  1.00 20.00 ?  234 ILE A CD1   1 
ATOM   1827 N N     . SER A 1 235 ? 7.840   -3.069  10.128 1.00 19.09 ?  235 SER A N     1 
ATOM   1828 C CA    . SER A 1 235 ? 6.910   -3.987  10.772 1.00 17.90 ?  235 SER A CA    1 
ATOM   1829 C C     . SER A 1 235 ? 7.626   -4.869  11.788 1.00 17.59 ?  235 SER A C     1 
ATOM   1830 O O     . SER A 1 235 ? 8.722   -5.378  11.533 1.00 17.46 ?  235 SER A O     1 
ATOM   1831 C CB    . SER A 1 235 ? 6.214   -4.865  9.728  1.00 20.41 ?  235 SER A CB    1 
ATOM   1832 O OG    . SER A 1 235 ? 5.451   -4.082  8.828  1.00 20.76 ?  235 SER A OG    1 
ATOM   1833 N N     . THR A 1 236 ? 7.001   -5.037  12.949 1.00 21.26 ?  236 THR A N     1 
ATOM   1834 C CA    . THR A 1 236 ? 7.405   -6.017  13.946 1.00 19.29 ?  236 THR A CA    1 
ATOM   1835 C C     . THR A 1 236 ? 6.256   -6.986  14.184 1.00 19.53 ?  236 THR A C     1 
ATOM   1836 O O     . THR A 1 236 ? 5.099   -6.573  14.300 1.00 20.59 ?  236 THR A O     1 
ATOM   1837 C CB    . THR A 1 236 ? 7.806   -5.339  15.265 1.00 20.50 ?  236 THR A CB    1 
ATOM   1838 O OG1   . THR A 1 236 ? 8.942   -4.499  15.037 1.00 16.07 ?  236 THR A OG1   1 
ATOM   1839 C CG2   . THR A 1 236 ? 8.158   -6.373  16.324 1.00 18.49 ?  236 THR A CG2   1 
ATOM   1840 N N     . LEU A 1 237 ? 6.575   -8.275  14.258 1.00 20.56 ?  237 LEU A N     1 
ATOM   1841 C CA    . LEU A 1 237 ? 5.579   -9.306  14.524 1.00 15.71 ?  237 LEU A CA    1 
ATOM   1842 C C     . LEU A 1 237 ? 5.554   -9.619  16.015 1.00 17.00 ?  237 LEU A C     1 
ATOM   1843 O O     . LEU A 1 237 ? 6.564   -10.049 16.581 1.00 17.60 ?  237 LEU A O     1 
ATOM   1844 C CB    . LEU A 1 237 ? 5.874   -10.574 13.723 1.00 15.18 ?  237 LEU A CB    1 
ATOM   1845 C CG    . LEU A 1 237 ? 4.878   -11.721 13.913 1.00 18.53 ?  237 LEU A CG    1 
ATOM   1846 C CD1   . LEU A 1 237 ? 3.516   -11.362 13.335 1.00 19.57 ?  237 LEU A CD1   1 
ATOM   1847 C CD2   . LEU A 1 237 ? 5.406   -13.010 13.301 1.00 17.48 ?  237 LEU A CD2   1 
ATOM   1848 N N     . LEU A 1 238 ? 4.404   -9.403  16.646 1.00 18.26 ?  238 LEU A N     1 
ATOM   1849 C CA    . LEU A 1 238 ? 4.181   -9.803  18.028 1.00 18.36 ?  238 LEU A CA    1 
ATOM   1850 C C     . LEU A 1 238 ? 3.404   -11.111 18.056 1.00 19.07 ?  238 LEU A C     1 
ATOM   1851 O O     . LEU A 1 238 ? 2.394   -11.256 17.356 1.00 17.50 ?  238 LEU A O     1 
ATOM   1852 C CB    . LEU A 1 238 ? 3.422   -8.728  18.810 1.00 15.67 ?  238 LEU A CB    1 
ATOM   1853 C CG    . LEU A 1 238 ? 3.028   -9.149  20.230 1.00 16.26 ?  238 LEU A CG    1 
ATOM   1854 C CD1   . LEU A 1 238 ? 4.226   -9.192  21.162 1.00 14.31 ?  238 LEU A CD1   1 
ATOM   1855 C CD2   . LEU A 1 238 ? 1.955   -8.243  20.792 1.00 17.20 ?  238 LEU A CD2   1 
ATOM   1856 N N     . ILE A 1 239 ? 3.875   -12.054 18.858 1.00 13.15 ?  239 ILE A N     1 
ATOM   1857 C CA    . ILE A 1 239 ? 3.230   -13.345 19.030 1.00 18.83 ?  239 ILE A CA    1 
ATOM   1858 C C     . ILE A 1 239 ? 2.854   -13.492 20.499 1.00 20.82 ?  239 ILE A C     1 
ATOM   1859 O O     . ILE A 1 239 ? 3.697   -13.812 21.336 1.00 21.03 ?  239 ILE A O     1 
ATOM   1860 C CB    . ILE A 1 239 ? 4.138   -14.497 18.563 1.00 20.77 ?  239 ILE A CB    1 
ATOM   1861 C CG1   . ILE A 1 239 ? 4.665   -14.205 17.152 1.00 19.14 ?  239 ILE A CG1   1 
ATOM   1862 C CG2   . ILE A 1 239 ? 3.388   -15.816 18.594 1.00 19.22 ?  239 ILE A CG2   1 
ATOM   1863 C CD1   . ILE A 1 239 ? 5.432   -15.351 16.533 1.00 16.50 ?  239 ILE A CD1   1 
ATOM   1864 N N     . PRO A 1 240 ? 1.593   -13.254 20.849 1.00 21.01 ?  240 PRO A N     1 
ATOM   1865 C CA    . PRO A 1 240 ? 1.172   -13.319 22.254 1.00 18.76 ?  240 PRO A CA    1 
ATOM   1866 C C     . PRO A 1 240 ? 1.305   -14.728 22.801 1.00 22.22 ?  240 PRO A C     1 
ATOM   1867 O O     . PRO A 1 240 ? 1.454   -15.686 22.026 1.00 20.02 ?  240 PRO A O     1 
ATOM   1868 C CB    . PRO A 1 240 ? -0.300  -12.868 22.199 1.00 19.80 ?  240 PRO A CB    1 
ATOM   1869 C CG    . PRO A 1 240 ? -0.425  -12.133 20.893 1.00 22.30 ?  240 PRO A CG    1 
ATOM   1870 C CD    . PRO A 1 240 ? 0.480   -12.876 19.966 1.00 22.15 ?  240 PRO A CD    1 
ATOM   1871 N N     . PRO A 1 241 ? 1.268   -14.891 24.125 1.00 20.20 ?  241 PRO A N     1 
ATOM   1872 C CA    . PRO A 1 241 ? 1.434   -16.223 24.713 1.00 20.78 ?  241 PRO A CA    1 
ATOM   1873 C C     . PRO A 1 241 ? 0.457   -17.228 24.130 1.00 21.40 ?  241 PRO A C     1 
ATOM   1874 O O     . PRO A 1 241 ? -0.710  -16.927 23.873 1.00 23.86 ?  241 PRO A O     1 
ATOM   1875 C CB    . PRO A 1 241 ? 1.172   -15.986 26.205 1.00 24.08 ?  241 PRO A CB    1 
ATOM   1876 C CG    . PRO A 1 241 ? 1.516   -14.555 26.419 1.00 27.17 ?  241 PRO A CG    1 
ATOM   1877 C CD    . PRO A 1 241 ? 1.113   -13.850 25.157 1.00 24.82 ?  241 PRO A CD    1 
ATOM   1878 N N     . ALA A 1 242 ? 0.962   -18.427 23.911 1.00 22.83 ?  242 ALA A N     1 
ATOM   1879 C CA    . ALA A 1 242 ? 0.129   -19.554 23.555 1.00 24.13 ?  242 ALA A CA    1 
ATOM   1880 C C     . ALA A 1 242 ? -0.349  -20.298 24.782 1.00 25.79 ?  242 ALA A C     1 
ATOM   1881 O O     . ALA A 1 242 ? -1.359  -20.992 24.715 1.00 29.39 ?  242 ALA A O     1 
ATOM   1882 C CB    . ALA A 1 242 ? 0.894   -20.534 22.658 1.00 29.69 ?  242 ALA A CB    1 
ATOM   1883 N N     . LYS A 1 243 ? 0.359   -20.223 25.889 1.00 22.76 ?  243 LYS A N     1 
ATOM   1884 C CA    . LYS A 1 243 ? -0.028  -20.953 27.081 1.00 31.37 ?  243 LYS A CA    1 
ATOM   1885 C C     . LYS A 1 243 ? -0.112  -20.021 28.289 1.00 34.20 ?  243 LYS A C     1 
ATOM   1886 O O     . LYS A 1 243 ? 0.602   -19.011 28.388 1.00 28.68 ?  243 LYS A O     1 
ATOM   1887 C CB    . LYS A 1 243 ? 1.030   -22.114 27.289 1.00 33.14 ?  243 LYS A CB    1 
ATOM   1888 C CG    . LYS A 1 243 ? 0.939   -23.084 28.359 1.00 42.73 ?  243 LYS A CG    1 
ATOM   1889 C CD    . LYS A 1 243 ? -0.603  -23.401 28.574 1.00 46.76 ?  243 LYS A CD    1 
ATOM   1890 C CE    . LYS A 1 243 ? -1.264  -23.900 27.339 1.00 53.26 ?  243 LYS A CE    1 
ATOM   1891 N NZ    . LYS A 1 243 ? -2.736  -23.379 27.389 1.00 51.72 ?  243 LYS A NZ    1 
ATOM   1892 N N     . LYS A 1 244 ? -1.014  -20.368 29.199 1.00 31.35 ?  244 LYS A N     1 
ATOM   1893 C CA    . LYS A 1 244 ? -1.071  -19.687 30.475 1.00 42.61 ?  244 LYS A CA    1 
ATOM   1894 C C     . LYS A 1 244 ? 0.096   -20.114 31.361 1.00 39.46 ?  244 LYS A C     1 
ATOM   1895 O O     . LYS A 1 244 ? 0.702   -21.175 31.187 1.00 32.55 ?  244 LYS A O     1 
ATOM   1896 C CB    . LYS A 1 244 ? -2.394  -19.971 31.194 1.00 47.63 ?  244 LYS A CB    1 
ATOM   1897 C CG    . LYS A 1 244 ? -3.681  -19.600 30.451 1.00 53.71 ?  244 LYS A CG    1 
ATOM   1898 C CD    . LYS A 1 244 ? -4.822  -19.254 31.422 1.00 61.10 ?  244 LYS A CD    1 
ATOM   1899 C CE    . LYS A 1 244 ? -4.964  -20.283 32.536 1.00 55.12 ?  244 LYS A CE    1 
ATOM   1900 N NZ    . LYS A 1 244 ? -5.731  -21.494 32.120 1.00 66.94 ?  244 LYS A NZ    1 
ATOM   1901 N N     . LEU A 1 245 ? 0.396   -19.271 32.338 1.00 42.75 ?  245 LEU A N     1 
ATOM   1902 C CA    . LEU A 1 245 ? 1.460   -19.587 33.280 1.00 38.59 ?  245 LEU A CA    1 
ATOM   1903 C C     . LEU A 1 245 ? 1.044   -20.757 34.163 1.00 41.47 ?  245 LEU A C     1 
ATOM   1904 O O     . LEU A 1 245 ? -0.080  -20.803 34.667 1.00 41.56 ?  245 LEU A O     1 
ATOM   1905 C CB    . LEU A 1 245 ? 1.794   -18.368 34.142 1.00 37.76 ?  245 LEU A CB    1 
ATOM   1906 C CG    . LEU A 1 245 ? 2.383   -17.167 33.399 1.00 34.95 ?  245 LEU A CG    1 
ATOM   1907 C CD1   . LEU A 1 245 ? 2.304   -15.919 34.262 1.00 41.43 ?  245 LEU A CD1   1 
ATOM   1908 C CD2   . LEU A 1 245 ? 3.815   -17.443 32.984 1.00 33.34 ?  245 LEU A CD2   1 
ATOM   1909 N N     . GLU A 1 246 ? 1.952   -21.711 34.349 1.00 40.47 ?  246 GLU A N     1 
ATOM   1910 C CA    . GLU A 1 246 ? 1.674   -22.895 35.150 1.00 43.83 ?  246 GLU A CA    1 
ATOM   1911 C C     . GLU A 1 246 ? 2.615   -22.953 36.345 1.00 42.00 ?  246 GLU A C     1 
ATOM   1912 O O     . GLU A 1 246 ? 3.748   -22.468 36.289 1.00 33.53 ?  246 GLU A O     1 
ATOM   1913 C CB    . GLU A 1 246 ? 1.805   -24.174 34.313 1.00 33.34 ?  246 GLU A CB    1 
ATOM   1914 C CG    . GLU A 1 246 ? 0.842   -24.230 33.140 1.00 41.65 ?  246 GLU A CG    1 
ATOM   1915 C CD    . GLU A 1 246 ? 0.805   -25.590 32.479 1.00 43.73 ?  246 GLU A CD    1 
ATOM   1916 O OE1   . GLU A 1 246 ? 0.098   -26.482 32.993 1.00 49.09 ?  246 GLU A OE1   1 
ATOM   1917 O OE2   . GLU A 1 246 ? 1.484   -25.770 31.446 1.00 46.23 -1 246 GLU A OE2   1 
ATOM   1918 N N     . TYR A 1 247 ? 2.139   -23.573 37.422 1.00 39.98 ?  247 TYR A N     1 
ATOM   1919 C CA    . TYR A 1 247 ? 2.849   -23.532 38.693 1.00 37.79 ?  247 TYR A CA    1 
ATOM   1920 C C     . TYR A 1 247 ? 4.095   -24.412 38.655 1.00 32.41 ?  247 TYR A C     1 
ATOM   1921 O O     . TYR A 1 247 ? 4.087   -25.510 38.095 1.00 33.40 ?  247 TYR A O     1 
ATOM   1922 C CB    . TYR A 1 247 ? 1.912   -23.963 39.825 1.00 36.56 ?  247 TYR A CB    1 
ATOM   1923 C CG    . TYR A 1 247 ? 0.889   -22.904 40.190 1.00 39.72 ?  247 TYR A CG    1 
ATOM   1924 C CD1   . TYR A 1 247 ? 1.285   -21.677 40.701 1.00 35.80 ?  247 TYR A CD1   1 
ATOM   1925 C CD2   . TYR A 1 247 ? -0.471  -23.124 40.001 1.00 44.63 ?  247 TYR A CD2   1 
ATOM   1926 C CE1   . TYR A 1 247 ? 0.358   -20.705 41.031 1.00 36.85 ?  247 TYR A CE1   1 
ATOM   1927 C CE2   . TYR A 1 247 ? -1.406  -22.153 40.326 1.00 33.92 ?  247 TYR A CE2   1 
ATOM   1928 C CZ    . TYR A 1 247 ? -0.983  -20.946 40.839 1.00 38.34 ?  247 TYR A CZ    1 
ATOM   1929 O OH    . TYR A 1 247 ? -1.901  -19.972 41.167 1.00 40.34 ?  247 TYR A OH    1 
ATOM   1930 N N     . ASN A 1 248 ? 5.173   -23.915 39.265 1.00 30.72 ?  248 ASN A N     1 
ATOM   1931 C CA    . ASN A 1 248 ? 6.472   -24.593 39.288 1.00 30.44 ?  248 ASN A CA    1 
ATOM   1932 C C     . ASN A 1 248 ? 6.627   -25.297 40.635 1.00 32.38 ?  248 ASN A C     1 
ATOM   1933 O O     . ASN A 1 248 ? 7.255   -24.796 41.568 1.00 25.00 ?  248 ASN A O     1 
ATOM   1934 C CB    . ASN A 1 248 ? 7.595   -23.592 39.030 1.00 33.05 ?  248 ASN A CB    1 
ATOM   1935 C CG    . ASN A 1 248 ? 8.922   -24.262 38.725 1.00 31.90 ?  248 ASN A CG    1 
ATOM   1936 O OD1   . ASN A 1 248 ? 9.141   -25.424 39.064 1.00 33.13 ?  248 ASN A OD1   1 
ATOM   1937 N ND2   . ASN A 1 248 ? 9.813   -23.527 38.069 1.00 33.73 ?  248 ASN A ND2   1 
ATOM   1938 N N     . TYR A 1 249 ? 6.050   -26.498 40.715 1.00 32.07 ?  249 TYR A N     1 
ATOM   1939 C CA    . TYR A 1 249 ? 5.904   -27.185 41.997 1.00 30.46 ?  249 TYR A CA    1 
ATOM   1940 C C     . TYR A 1 249 ? 7.249   -27.522 42.633 1.00 27.19 ?  249 TYR A C     1 
ATOM   1941 O O     . TYR A 1 249 ? 7.387   -27.477 43.862 1.00 29.77 ?  249 TYR A O     1 
ATOM   1942 C CB    . TYR A 1 249 ? 5.083   -28.457 41.805 1.00 30.62 ?  249 TYR A CB    1 
ATOM   1943 C CG    . TYR A 1 249 ? 3.613   -28.192 41.586 1.00 29.72 ?  249 TYR A CG    1 
ATOM   1944 C CD1   . TYR A 1 249 ? 2.881   -27.448 42.498 1.00 31.13 ?  249 TYR A CD1   1 
ATOM   1945 C CD2   . TYR A 1 249 ? 2.962   -28.669 40.458 1.00 33.77 ?  249 TYR A CD2   1 
ATOM   1946 C CE1   . TYR A 1 249 ? 1.539   -27.196 42.304 1.00 35.80 ?  249 TYR A CE1   1 
ATOM   1947 C CE2   . TYR A 1 249 ? 1.620   -28.422 40.252 1.00 35.87 ?  249 TYR A CE2   1 
ATOM   1948 C CZ    . TYR A 1 249 ? 0.914   -27.685 41.178 1.00 36.12 ?  249 TYR A CZ    1 
ATOM   1949 O OH    . TYR A 1 249 ? -0.425  -27.437 40.977 1.00 38.86 ?  249 TYR A OH    1 
ATOM   1950 N N     . ALA A 1 250 ? 8.251   -27.869 41.820 1.00 30.58 ?  250 ALA A N     1 
ATOM   1951 C CA    . ALA A 1 250 ? 9.551   -28.252 42.369 1.00 34.29 ?  250 ALA A CA    1 
ATOM   1952 C C     . ALA A 1 250 ? 10.146  -27.131 43.209 1.00 29.98 ?  250 ALA A C     1 
ATOM   1953 O O     . ALA A 1 250 ? 10.626  -27.361 44.323 1.00 29.57 ?  250 ALA A O     1 
ATOM   1954 C CB    . ALA A 1 250 ? 10.513  -28.642 41.246 1.00 37.96 ?  250 ALA A CB    1 
ATOM   1955 N N     . ILE A 1 251 ? 10.104  -25.902 42.695 1.00 31.40 ?  251 ILE A N     1 
ATOM   1956 C CA    . ILE A 1 251 ? 10.728  -24.787 43.399 1.00 34.83 ?  251 ILE A CA    1 
ATOM   1957 C C     . ILE A 1 251 ? 9.841   -24.311 44.537 1.00 23.37 ?  251 ILE A C     1 
ATOM   1958 O O     . ILE A 1 251 ? 10.332  -23.974 45.621 1.00 25.78 ?  251 ILE A O     1 
ATOM   1959 C CB    . ILE A 1 251 ? 11.043  -23.649 42.412 1.00 29.80 ?  251 ILE A CB    1 
ATOM   1960 C CG1   . ILE A 1 251 ? 11.980  -24.152 41.309 1.00 30.65 ?  251 ILE A CG1   1 
ATOM   1961 C CG2   . ILE A 1 251 ? 11.653  -22.457 43.134 1.00 23.57 ?  251 ILE A CG2   1 
ATOM   1962 C CD1   . ILE A 1 251 ? 13.344  -24.566 41.817 1.00 35.28 ?  251 ILE A CD1   1 
ATOM   1963 N N     . LEU A 1 252 ? 8.526   -24.274 44.307 1.00 26.69 ?  252 LEU A N     1 
ATOM   1964 C CA    . LEU A 1 252 ? 7.600   -23.892 45.367 1.00 31.54 ?  252 LEU A CA    1 
ATOM   1965 C C     . LEU A 1 252 ? 7.776   -24.789 46.589 1.00 28.27 ?  252 LEU A C     1 
ATOM   1966 O O     . LEU A 1 252 ? 7.677   -24.326 47.732 1.00 30.94 ?  252 LEU A O     1 
ATOM   1967 C CB    . LEU A 1 252 ? 6.161   -23.952 44.855 1.00 33.42 ?  252 LEU A CB    1 
ATOM   1968 C CG    . LEU A 1 252 ? 5.770   -23.047 43.669 1.00 28.13 ?  252 LEU A CG    1 
ATOM   1969 C CD1   . LEU A 1 252 ? 4.299   -23.230 43.308 1.00 29.37 ?  252 LEU A CD1   1 
ATOM   1970 C CD2   . LEU A 1 252 ? 6.119   -21.574 43.853 1.00 29.71 ?  252 LEU A CD2   1 
ATOM   1971 N N     . ALA A 1 253 ? 8.047   -26.079 46.363 1.00 27.10 ?  253 ALA A N     1 
ATOM   1972 C CA    . ALA A 1 253 ? 8.284   -26.999 47.471 1.00 31.96 ?  253 ALA A CA    1 
ATOM   1973 C C     . ALA A 1 253 ? 9.598   -26.686 48.174 1.00 35.64 ?  253 ALA A C     1 
ATOM   1974 O O     . ALA A 1 253 ? 9.670   -26.718 49.409 1.00 37.10 ?  253 ALA A O     1 
ATOM   1975 C CB    . ALA A 1 253 ? 8.271   -28.443 46.970 1.00 34.02 ?  253 ALA A CB    1 
ATOM   1976 N N     . LYS A 1 254 ? 10.654  -26.396 47.403 1.00 35.60 ?  254 LYS A N     1 
ATOM   1977 C CA    . LYS A 1 254 ? 11.917  -25.989 48.013 1.00 32.12 ?  254 LYS A CA    1 
ATOM   1978 C C     . LYS A 1 254 ? 11.727  -24.707 48.812 1.00 33.09 ?  254 LYS A C     1 
ATOM   1979 O O     . LYS A 1 254 ? 12.347  -24.518 49.865 1.00 38.63 ?  254 LYS A O     1 
ATOM   1980 C CB    . LYS A 1 254 ? 12.992  -25.805 46.944 1.00 33.36 ?  254 LYS A CB    1 
ATOM   1981 C CG    . LYS A 1 254 ? 13.167  -27.000 46.023 1.00 32.68 ?  254 LYS A CG    1 
ATOM   1982 C CD    . LYS A 1 254 ? 14.624  -27.397 45.861 1.00 42.84 ?  254 LYS A CD    1 
ATOM   1983 C CE    . LYS A 1 254 ? 14.760  -28.902 45.678 1.00 47.37 ?  254 LYS A CE    1 
ATOM   1984 N NZ    . LYS A 1 254 ? 16.100  -29.286 45.152 1.00 45.10 ?  254 LYS A NZ    1 
ATOM   1985 N N     . LEU A 1 255 ? 10.870  -23.814 48.319 1.00 31.25 ?  255 LEU A N     1 
ATOM   1986 C CA    . LEU A 1 255 ? 10.497  -22.609 49.043 1.00 33.92 ?  255 LEU A CA    1 
ATOM   1987 C C     . LEU A 1 255 ? 9.517   -22.898 50.170 1.00 36.52 ?  255 LEU A C     1 
ATOM   1988 O O     . LEU A 1 255 ? 9.187   -21.985 50.936 1.00 32.98 ?  255 LEU A O     1 
ATOM   1989 C CB    . LEU A 1 255 ? 9.882   -21.591 48.075 1.00 29.26 ?  255 LEU A CB    1 
ATOM   1990 C CG    . LEU A 1 255 ? 10.808  -20.963 47.027 1.00 24.51 ?  255 LEU A CG    1 
ATOM   1991 C CD1   . LEU A 1 255 ? 9.998   -20.141 46.040 1.00 27.42 ?  255 LEU A CD1   1 
ATOM   1992 C CD2   . LEU A 1 255 ? 11.888  -20.115 47.676 1.00 29.31 ?  255 LEU A CD2   1 
ATOM   1993 N N     . GLY A 1 256 ? 9.044   -24.140 50.277 1.00 35.72 ?  256 GLY A N     1 
ATOM   1994 C CA    . GLY A 1 256 ? 8.158   -24.542 51.351 1.00 32.59 ?  256 GLY A CA    1 
ATOM   1995 C C     . GLY A 1 256 ? 6.762   -23.977 51.286 1.00 36.15 ?  256 GLY A C     1 
ATOM   1996 O O     . GLY A 1 256 ? 6.075   -23.933 52.311 1.00 42.48 ?  256 GLY A O     1 
ATOM   1997 N N     . ILE A 1 257 ? 6.321   -23.527 50.113 1.00 32.91 ?  257 ILE A N     1 
ATOM   1998 C CA    . ILE A 1 257 ? 5.006   -22.924 49.943 1.00 38.08 ?  257 ILE A CA    1 
ATOM   1999 C C     . ILE A 1 257 ? 4.268   -23.625 48.802 1.00 25.85 ?  257 ILE A C     1 
ATOM   2000 O O     . ILE A 1 257 ? 4.791   -24.532 48.158 1.00 25.29 ?  257 ILE A O     1 
ATOM   2001 C CB    . ILE A 1 257 ? 5.082   -21.386 49.745 1.00 30.12 ?  257 ILE A CB    1 
ATOM   2002 C CG1   . ILE A 1 257 ? 5.961   -20.938 48.563 1.00 39.46 ?  257 ILE A CG1   1 
ATOM   2003 C CG2   . ILE A 1 257 ? 5.620   -20.728 51.001 1.00 33.17 ?  257 ILE A CG2   1 
ATOM   2004 C CD1   . ILE A 1 257 ? 5.588   -21.405 47.196 1.00 41.37 ?  257 ILE A CD1   1 
ATOM   2005 N N     . GLY A 1 258 ? 3.030   -23.200 48.573 1.00 36.15 ?  258 GLY A N     1 
ATOM   2006 C CA    . GLY A 1 258 ? 2.257   -23.669 47.451 1.00 31.23 ?  258 GLY A CA    1 
ATOM   2007 C C     . GLY A 1 258 ? 1.526   -22.543 46.757 1.00 36.16 ?  258 GLY A C     1 
ATOM   2008 O O     . GLY A 1 258 ? 1.684   -21.371 47.107 1.00 34.47 ?  258 GLY A O     1 
ATOM   2009 N N     . PRO A 1 259 ? 0.717   -22.879 45.745 1.00 34.57 ?  259 PRO A N     1 
ATOM   2010 C CA    . PRO A 1 259 ? -0.076  -21.841 45.059 1.00 28.46 ?  259 PRO A CA    1 
ATOM   2011 C C     . PRO A 1 259 ? -0.892  -20.981 46.009 1.00 40.60 ?  259 PRO A C     1 
ATOM   2012 O O     . PRO A 1 259 ? -0.977  -19.761 45.814 1.00 43.19 ?  259 PRO A O     1 
ATOM   2013 C CB    . PRO A 1 259 ? -0.968  -22.653 44.110 1.00 37.54 ?  259 PRO A CB    1 
ATOM   2014 C CG    . PRO A 1 259 ? -0.210  -23.909 43.868 1.00 32.75 ?  259 PRO A CG    1 
ATOM   2015 C CD    . PRO A 1 259 ? 0.516   -24.208 45.145 1.00 32.78 ?  259 PRO A CD    1 
ATOM   2016 N N     . GLU A 1 260 ? -1.491  -21.587 47.041 1.00 44.07 ?  260 GLU A N     1 
ATOM   2017 C CA    . GLU A 1 260 ? -2.423  -20.849 47.886 1.00 42.08 ?  260 GLU A CA    1 
ATOM   2018 C C     . GLU A 1 260 ? -1.702  -19.817 48.739 1.00 45.49 ?  260 GLU A C     1 
ATOM   2019 O O     . GLU A 1 260 ? -2.323  -18.865 49.226 1.00 46.95 ?  260 GLU A O     1 
ATOM   2020 C CB    . GLU A 1 260 ? -3.143  -21.814 48.823 1.00 42.84 ?  260 GLU A CB    1 
ATOM   2021 C CG    . GLU A 1 260 ? -4.589  -21.500 49.122 1.00 48.76 ?  260 GLU A CG    1 
ATOM   2022 C CD    . GLU A 1 260 ? -5.189  -22.517 50.069 1.00 50.46 ?  260 GLU A CD    1 
ATOM   2023 O OE1   . GLU A 1 260 ? -4.674  -22.629 51.204 1.00 47.89 ?  260 GLU A OE1   1 
ATOM   2024 O OE2   . GLU A 1 260 ? -6.152  -23.219 49.686 1.00 58.48 -1 260 GLU A OE2   1 
ATOM   2025 N N     . ASP A 1 261 ? -0.387  -19.953 48.889 1.00 41.71 ?  261 ASP A N     1 
ATOM   2026 C CA    . ASP A 1 261 ? 0.400   -19.034 49.702 1.00 32.39 ?  261 ASP A CA    1 
ATOM   2027 C C     . ASP A 1 261 ? 0.894   -17.839 48.911 1.00 37.61 ?  261 ASP A C     1 
ATOM   2028 O O     . ASP A 1 261 ? 1.410   -16.889 49.508 1.00 40.27 ?  261 ASP A O     1 
ATOM   2029 C CB    . ASP A 1 261 ? 1.599   -19.759 50.329 1.00 36.44 ?  261 ASP A CB    1 
ATOM   2030 C CG    . ASP A 1 261 ? 1.176   -20.857 51.285 1.00 31.84 ?  261 ASP A CG    1 
ATOM   2031 O OD1   . ASP A 1 261 ? 0.305   -20.600 52.145 1.00 38.79 ?  261 ASP A OD1   1 
ATOM   2032 O OD2   . ASP A 1 261 ? 1.728   -21.975 51.192 1.00 41.16 -1 261 ASP A OD2   1 
ATOM   2033 N N     . LEU A 1 262 ? 0.751   -17.867 47.591 1.00 35.95 ?  262 LEU A N     1 
ATOM   2034 C CA    . LEU A 1 262 ? 1.256   -16.784 46.765 1.00 35.85 ?  262 LEU A CA    1 
ATOM   2035 C C     . LEU A 1 262 ? 0.497   -15.497 47.057 1.00 43.53 ?  262 LEU A C     1 
ATOM   2036 O O     . LEU A 1 262 ? -0.725  -15.500 47.222 1.00 46.10 ?  262 LEU A O     1 
ATOM   2037 C CB    . LEU A 1 262 ? 1.130   -17.159 45.291 1.00 36.18 ?  262 LEU A CB    1 
ATOM   2038 C CG    . LEU A 1 262 ? 1.975   -18.379 44.913 1.00 37.16 ?  262 LEU A CG    1 
ATOM   2039 C CD1   . LEU A 1 262 ? 1.811   -18.733 43.448 1.00 28.81 ?  262 LEU A CD1   1 
ATOM   2040 C CD2   . LEU A 1 262 ? 3.434   -18.131 45.252 1.00 36.79 ?  262 LEU A CD2   1 
ATOM   2041 N N     . GLY A 1 263 ? 1.233   -14.396 47.133 1.00 42.63 ?  263 GLY A N     1 
ATOM   2042 C CA    . GLY A 1 263 ? 0.651   -13.115 47.481 1.00 38.66 ?  263 GLY A CA    1 
ATOM   2043 C C     . GLY A 1 263 ? 0.008   -12.426 46.300 1.00 33.65 ?  263 GLY A C     1 
ATOM   2044 O O     . GLY A 1 263 ? 0.508   -12.530 45.178 1.00 33.74 ?  263 GLY A O     1 
ATOM   2045 O OXT   . GLY A 1 263 ? -1.016  -11.753 46.446 1.00 38.30 -1 263 GLY A OXT   1 
ATOM   2046 N N     . GLY B 2 10  ? 4.848   24.959  6.269  1.00 41.14 ?  3   GLY B N     1 
ATOM   2047 C CA    . GLY B 2 10  ? 3.430   24.677  6.351  1.00 37.85 ?  3   GLY B CA    1 
ATOM   2048 C C     . GLY B 2 10  ? 3.113   23.362  7.036  1.00 33.95 ?  3   GLY B C     1 
ATOM   2049 O O     . GLY B 2 10  ? 2.901   23.319  8.249  1.00 34.62 ?  3   GLY B O     1 
ATOM   2050 N N     . LEU B 2 11  ? 3.079   22.284  6.250  1.00 30.16 ?  4   LEU B N     1 
ATOM   2051 C CA    . LEU B 2 11  ? 2.778   20.962  6.791  1.00 26.11 ?  4   LEU B CA    1 
ATOM   2052 C C     . LEU B 2 11  ? 3.844   20.527  7.789  1.00 28.83 ?  4   LEU B C     1 
ATOM   2053 O O     . LEU B 2 11  ? 3.540   20.204  8.943  1.00 27.55 ?  4   LEU B O     1 
ATOM   2054 C CB    . LEU B 2 11  ? 2.661   19.948  5.654  1.00 27.33 ?  4   LEU B CB    1 
ATOM   2055 C CG    . LEU B 2 11  ? 1.866   18.675  5.924  1.00 33.20 ?  4   LEU B CG    1 
ATOM   2056 C CD1   . LEU B 2 11  ? 0.461   19.015  6.383  1.00 30.04 ?  4   LEU B CD1   1 
ATOM   2057 C CD2   . LEU B 2 11  ? 1.821   17.796  4.683  1.00 39.55 ?  4   LEU B CD2   1 
ATOM   2058 N N     . SER B 2 12  ? 5.108   20.513  7.351  1.00 29.72 ?  5   SER B N     1 
ATOM   2059 C CA    . SER B 2 12  ? 6.192   20.052  8.212  1.00 27.50 ?  5   SER B CA    1 
ATOM   2060 C C     . SER B 2 12  ? 6.283   20.893  9.469  1.00 30.30 ?  5   SER B C     1 
ATOM   2061 O O     . SER B 2 12  ? 6.599   20.378  10.548 1.00 23.68 ?  5   SER B O     1 
ATOM   2062 C CB    . SER B 2 12  ? 7.526   20.087  7.471  1.00 22.10 ?  5   SER B CB    1 
ATOM   2063 O OG    . SER B 2 12  ? 8.589   19.726  8.337  1.00 33.76 ?  5   SER B OG    1 
ATOM   2064 N N     . ASP B 2 13  ? 6.008   22.191  9.360  1.00 23.13 ?  6   ASP B N     1 
ATOM   2065 C CA    . ASP B 2 13  ? 6.037   22.994  10.571 1.00 26.75 ?  6   ASP B CA    1 
ATOM   2066 C C     . ASP B 2 13  ? 5.009   22.461  11.560 1.00 27.95 ?  6   ASP B C     1 
ATOM   2067 O O     . ASP B 2 13  ? 5.377   21.962  12.626 1.00 29.54 ?  6   ASP B O     1 
ATOM   2068 C CB    . ASP B 2 13  ? 5.794   24.473  10.237 1.00 28.73 ?  6   ASP B CB    1 
ATOM   2069 C CG    . ASP B 2 13  ? 6.944   25.087  9.451  1.00 29.15 ?  6   ASP B CG    1 
ATOM   2070 O OD1   . ASP B 2 13  ? 8.108   24.882  9.858  1.00 29.33 ?  6   ASP B OD1   1 
ATOM   2071 O OD2   . ASP B 2 13  ? 6.698   25.774  8.438  1.00 38.97 -1 6   ASP B OD2   1 
ATOM   2072 N N     . PHE B 2 14  ? 3.761   22.312  11.105 1.00 20.90 ?  7   PHE B N     1 
ATOM   2073 C CA    . PHE B 2 14  ? 2.657   21.911  11.979 1.00 27.30 ?  7   PHE B CA    1 
ATOM   2074 C C     . PHE B 2 14  ? 2.930   20.578  12.667 1.00 23.56 ?  7   PHE B C     1 
ATOM   2075 O O     . PHE B 2 14  ? 2.571   20.393  13.834 1.00 25.99 ?  7   PHE B O     1 
ATOM   2076 C CB    . PHE B 2 14  ? 1.345   21.851  11.188 1.00 22.40 ?  7   PHE B CB    1 
ATOM   2077 C CG    . PHE B 2 14  ? 0.193   21.244  11.951 1.00 23.59 ?  7   PHE B CG    1 
ATOM   2078 C CD1   . PHE B 2 14  ? -0.354  21.892  13.048 1.00 21.44 ?  7   PHE B CD1   1 
ATOM   2079 C CD2   . PHE B 2 14  ? -0.342  20.025  11.565 1.00 21.62 ?  7   PHE B CD2   1 
ATOM   2080 C CE1   . PHE B 2 14  ? -1.415  21.331  13.748 1.00 22.44 ?  7   PHE B CE1   1 
ATOM   2081 C CE2   . PHE B 2 14  ? -1.399  19.462  12.261 1.00 22.90 ?  7   PHE B CE2   1 
ATOM   2082 C CZ    . PHE B 2 14  ? -1.934  20.115  13.351 1.00 19.90 ?  7   PHE B CZ    1 
ATOM   2083 N N     . PHE B 2 15  ? 3.490   19.608  11.944 1.00 21.37 ?  8   PHE B N     1 
ATOM   2084 C CA    . PHE B 2 15  ? 3.704   18.291  12.543 1.00 22.17 ?  8   PHE B CA    1 
ATOM   2085 C C     . PHE B 2 15  ? 4.752   18.332  13.659 1.00 20.88 ?  8   PHE B C     1 
ATOM   2086 O O     . PHE B 2 15  ? 4.597   17.661  14.687 1.00 20.53 ?  8   PHE B O     1 
ATOM   2087 C CB    . PHE B 2 15  ? 4.114   17.292  11.467 1.00 18.23 ?  8   PHE B CB    1 
ATOM   2088 C CG    . PHE B 2 15  ? 2.996   16.884  10.544 1.00 23.13 ?  8   PHE B CG    1 
ATOM   2089 C CD1   . PHE B 2 15  ? 1.671   17.161  10.849 1.00 23.87 ?  8   PHE B CD1   1 
ATOM   2090 C CD2   . PHE B 2 15  ? 3.277   16.197  9.375  1.00 26.54 ?  8   PHE B CD2   1 
ATOM   2091 C CE1   . PHE B 2 15  ? 0.652   16.771  9.991  1.00 25.83 ?  8   PHE B CE1   1 
ATOM   2092 C CE2   . PHE B 2 15  ? 2.266   15.804  8.518  1.00 28.06 ?  8   PHE B CE2   1 
ATOM   2093 C CZ    . PHE B 2 15  ? 0.953   16.091  8.826  1.00 26.01 ?  8   PHE B CZ    1 
ATOM   2094 N N     . THR B 2 16  ? 5.830   19.099  13.464 1.00 21.68 ?  9   THR B N     1 
ATOM   2095 C CA    . THR B 2 16  ? 6.880   19.236  14.475 1.00 24.87 ?  9   THR B CA    1 
ATOM   2096 C C     . THR B 2 16  ? 6.325   19.933  15.705 1.00 24.90 ?  9   THR B C     1 
ATOM   2097 O O     . THR B 2 16  ? 6.621   19.572  16.855 1.00 19.35 ?  9   THR B O     1 
ATOM   2098 C CB    . THR B 2 16  ? 8.031   20.045  13.874 1.00 24.09 ?  9   THR B CB    1 
ATOM   2099 O OG1   . THR B 2 16  ? 8.687   19.268  12.872 1.00 23.50 ?  9   THR B OG1   1 
ATOM   2100 C CG2   . THR B 2 16  ? 9.041   20.462  14.929 1.00 23.21 ?  9   THR B CG2   1 
ATOM   2101 N N     . GLN B 2 17  ? 5.493   20.928  15.420 1.00 22.67 ?  10  GLN B N     1 
ATOM   2102 C CA    . GLN B 2 17  ? 4.730   21.749  16.341 1.00 26.76 ?  10  GLN B CA    1 
ATOM   2103 C C     . GLN B 2 17  ? 3.928   20.835  17.265 1.00 24.44 ?  10  GLN B C     1 
ATOM   2104 O O     . GLN B 2 17  ? 4.077   20.842  18.493 1.00 23.88 ?  10  GLN B O     1 
ATOM   2105 C CB    . GLN B 2 17  ? 3.758   22.458  15.388 1.00 38.04 ?  10  GLN B CB    1 
ATOM   2106 C CG    . GLN B 2 17  ? 4.187   23.606  14.473 1.00 44.80 ?  10  GLN B CG    1 
ATOM   2107 C CD    . GLN B 2 17  ? 3.540   24.929  14.677 1.00 52.20 ?  10  GLN B CD    1 
ATOM   2108 O OE1   . GLN B 2 17  ? 2.278   24.973  14.622 1.00 54.24 ?  10  GLN B OE1   1 
ATOM   2109 N NE2   . GLN B 2 17  ? 4.270   25.982  14.477 1.00 56.31 ?  10  GLN B NE2   1 
ATOM   2110 N N     . LEU B 2 18  ? 3.106   19.983  16.630 1.00 22.76 ?  11  LEU B N     1 
ATOM   2111 C CA    . LEU B 2 18  ? 2.153   19.091  17.282 1.00 20.97 ?  11  LEU B CA    1 
ATOM   2112 C C     . LEU B 2 18  ? 2.843   17.979  18.057 1.00 17.88 ?  11  LEU B C     1 
ATOM   2113 O O     . LEU B 2 18  ? 2.373   17.583  19.129 1.00 19.03 ?  11  LEU B O     1 
ATOM   2114 C CB    . LEU B 2 18  ? 1.225   18.518  16.212 1.00 19.33 ?  11  LEU B CB    1 
ATOM   2115 C CG    . LEU B 2 18  ? 0.166   17.490  16.589 1.00 22.51 ?  11  LEU B CG    1 
ATOM   2116 C CD1   . LEU B 2 18  ? -0.838  18.110  17.537 1.00 19.31 ?  11  LEU B CD1   1 
ATOM   2117 C CD2   . LEU B 2 18  ? -0.522  16.968  15.339 1.00 20.62 ?  11  LEU B CD2   1 
ATOM   2118 N N     . GLY B 2 19  ? 3.930   17.429  17.509 1.00 20.98 ?  12  GLY B N     1 
ATOM   2119 C CA    . GLY B 2 19  ? 4.607   16.319  18.161 1.00 18.35 ?  12  GLY B CA    1 
ATOM   2120 C C     . GLY B 2 19  ? 5.285   16.695  19.460 1.00 16.33 ?  12  GLY B C     1 
ATOM   2121 O O     . GLY B 2 19  ? 5.521   15.822  20.304 1.00 21.53 ?  12  GLY B O     1 
ATOM   2122 N N     . GLN B 2 20  ? 5.590   17.980  19.643 1.00 17.11 ?  13  GLN B N     1 
ATOM   2123 C CA    . GLN B 2 20  ? 6.335   18.452  20.802 1.00 17.17 ?  13  GLN B CA    1 
ATOM   2124 C C     . GLN B 2 20  ? 5.460   19.111  21.855 1.00 17.53 ?  13  GLN B C     1 
ATOM   2125 O O     . GLN B 2 20  ? 5.859   19.169  23.023 1.00 19.92 ?  13  GLN B O     1 
ATOM   2126 C CB    . GLN B 2 20  ? 7.396   19.478  20.381 1.00 21.68 ?  13  GLN B CB    1 
ATOM   2127 C CG    . GLN B 2 20  ? 8.495   18.961  19.497 1.00 25.20 ?  13  GLN B CG    1 
ATOM   2128 C CD    . GLN B 2 20  ? 9.483   20.052  19.149 1.00 29.37 ?  13  GLN B CD    1 
ATOM   2129 O OE1   . GLN B 2 20  ? 10.433  20.307  19.889 1.00 39.86 ?  13  GLN B OE1   1 
ATOM   2130 N NE2   . GLN B 2 20  ? 9.242   20.732  18.038 1.00 29.43 ?  13  GLN B NE2   1 
ATOM   2131 N N     . ASP B 2 21  ? 4.289   19.606  21.473 1.00 19.04 ?  14  ASP B N     1 
ATOM   2132 C CA    . ASP B 2 21  ? 3.509   20.526  22.291 1.00 19.53 ?  14  ASP B CA    1 
ATOM   2133 C C     . ASP B 2 21  ? 2.257   19.797  22.765 1.00 16.85 ?  14  ASP B C     1 
ATOM   2134 O O     . ASP B 2 21  ? 1.323   19.579  21.984 1.00 17.24 ?  14  ASP B O     1 
ATOM   2135 C CB    . ASP B 2 21  ? 3.171   21.783  21.483 1.00 18.88 ?  14  ASP B CB    1 
ATOM   2136 C CG    . ASP B 2 21  ? 2.398   22.821  22.280 1.00 22.01 ?  14  ASP B CG    1 
ATOM   2137 O OD1   . ASP B 2 21  ? 2.006   22.552  23.431 1.00 19.66 ?  14  ASP B OD1   1 
ATOM   2138 O OD2   . ASP B 2 21  ? 2.193   23.930  21.741 1.00 31.87 -1 14  ASP B OD2   1 
ATOM   2139 N N     . ALA B 2 22  ? 2.231   19.444  24.054 1.00 17.31 ?  15  ALA B N     1 
ATOM   2140 C CA    . ALA B 2 22  ? 1.144   18.620  24.566 1.00 17.39 ?  15  ALA B CA    1 
ATOM   2141 C C     . ALA B 2 22  ? -0.156  19.405  24.636 1.00 27.39 ?  15  ALA B C     1 
ATOM   2142 O O     . ALA B 2 22  ? -1.242  18.812  24.593 1.00 18.83 ?  15  ALA B O     1 
ATOM   2143 C CB    . ALA B 2 22  ? 1.505   18.065  25.944 1.00 16.38 ?  15  ALA B CB    1 
ATOM   2144 N N     . GLN B 2 23  ? -0.064  20.731  24.750 1.00 18.91 ?  16  GLN B N     1 
ATOM   2145 C CA    . GLN B 2 23  ? -1.253  21.570  24.666 1.00 23.81 ?  16  GLN B CA    1 
ATOM   2146 C C     . GLN B 2 23  ? -1.887  21.452  23.287 1.00 29.06 ?  16  GLN B C     1 
ATOM   2147 O O     . GLN B 2 23  ? -3.072  21.124  23.152 1.00 22.33 ?  16  GLN B O     1 
ATOM   2148 C CB    . GLN B 2 23  ? -0.893  23.022  24.973 1.00 25.37 ?  16  GLN B CB    1 
ATOM   2149 C CG    . GLN B 2 23  ? -2.070  23.871  25.418 1.00 35.39 ?  16  GLN B CG    1 
ATOM   2150 C CD    . GLN B 2 23  ? -3.074  23.075  26.230 1.00 34.85 ?  16  GLN B CD    1 
ATOM   2151 O OE1   . GLN B 2 23  ? -2.788  22.655  27.351 1.00 37.71 ?  16  GLN B OE1   1 
ATOM   2152 N NE2   . GLN B 2 23  ? -4.257  22.861  25.664 1.00 36.25 ?  16  GLN B NE2   1 
ATOM   2153 N N     . LEU B 2 24  ? -1.092  21.707  22.243 1.00 24.69 ?  17  LEU B N     1 
ATOM   2154 C CA    . LEU B 2 24  ? -1.581  21.566  20.876 1.00 24.32 ?  17  LEU B CA    1 
ATOM   2155 C C     . LEU B 2 24  ? -2.019  20.135  20.602 1.00 23.63 ?  17  LEU B C     1 
ATOM   2156 O O     . LEU B 2 24  ? -3.017  19.903  19.908 1.00 20.83 ?  17  LEU B O     1 
ATOM   2157 C CB    . LEU B 2 24  ? -0.494  21.990  19.888 1.00 26.49 ?  17  LEU B CB    1 
ATOM   2158 C CG    . LEU B 2 24  ? -0.841  21.904  18.402 1.00 27.75 ?  17  LEU B CG    1 
ATOM   2159 C CD1   . LEU B 2 24  ? -2.062  22.756  18.084 1.00 28.26 ?  17  LEU B CD1   1 
ATOM   2160 C CD2   . LEU B 2 24  ? 0.348   22.319  17.549 1.00 28.32 ?  17  LEU B CD2   1 
ATOM   2161 N N     . MET B 2 25  ? -1.274  19.162  21.134 1.00 24.82 ?  18  MET B N     1 
ATOM   2162 C CA    . MET B 2 25  ? -1.639  17.759  20.961 1.00 24.39 ?  18  MET B CA    1 
ATOM   2163 C C     . MET B 2 25  ? -3.035  17.486  21.507 1.00 22.84 ?  18  MET B C     1 
ATOM   2164 O O     . MET B 2 25  ? -3.855  16.828  20.855 1.00 21.52 ?  18  MET B O     1 
ATOM   2165 C CB    . MET B 2 25  ? -0.610  16.861  21.646 1.00 20.99 ?  18  MET B CB    1 
ATOM   2166 C CG    . MET B 2 25  ? -0.869  15.376  21.474 1.00 28.73 ?  18  MET B CG    1 
ATOM   2167 S SD    . MET B 2 25  ? -1.257  14.949  19.767 1.00 34.67 ?  18  MET B SD    1 
ATOM   2168 C CE    . MET B 2 25  ? 0.361   14.451  19.186 1.00 28.67 ?  18  MET B CE    1 
ATOM   2169 N N     . GLU B 2 26  ? -3.326  17.997  22.707 1.00 20.94 ?  19  GLU B N     1 
ATOM   2170 C CA    . GLU B 2 26  ? -4.649  17.789  23.284 1.00 28.50 ?  19  GLU B CA    1 
ATOM   2171 C C     . GLU B 2 26  ? -5.693  18.653  22.588 1.00 25.64 ?  19  GLU B C     1 
ATOM   2172 O O     . GLU B 2 26  ? -6.861  18.254  22.484 1.00 25.12 ?  19  GLU B O     1 
ATOM   2173 C CB    . GLU B 2 26  ? -4.623  18.066  24.786 1.00 29.86 ?  19  GLU B CB    1 
ATOM   2174 C CG    . GLU B 2 26  ? -3.757  17.087  25.569 1.00 24.45 ?  19  GLU B CG    1 
ATOM   2175 C CD    . GLU B 2 26  ? -4.319  15.678  25.573 1.00 35.81 ?  19  GLU B CD    1 
ATOM   2176 O OE1   . GLU B 2 26  ? -4.018  14.910  24.634 1.00 35.86 ?  19  GLU B OE1   1 
ATOM   2177 O OE2   . GLU B 2 26  ? -5.061  15.336  26.518 1.00 44.82 -1 19  GLU B OE2   1 
ATOM   2178 N N     . ASP B 2 27  ? -5.294  19.835  22.112 1.00 26.50 ?  20  ASP B N     1 
ATOM   2179 C CA    . ASP B 2 27  ? -6.181  20.623  21.261 1.00 26.86 ?  20  ASP B CA    1 
ATOM   2180 C C     . ASP B 2 27  ? -6.542  19.836  20.010 1.00 25.34 ?  20  ASP B C     1 
ATOM   2181 O O     . ASP B 2 27  ? -7.706  19.793  19.594 1.00 22.29 ?  20  ASP B O     1 
ATOM   2182 C CB    . ASP B 2 27  ? -5.515  21.948  20.886 1.00 27.68 ?  20  ASP B CB    1 
ATOM   2183 C CG    . ASP B 2 27  ? -5.389  22.891  22.063 1.00 28.80 ?  20  ASP B CG    1 
ATOM   2184 O OD1   . ASP B 2 27  ? -6.071  22.668  23.086 1.00 30.23 ?  20  ASP B OD1   1 
ATOM   2185 O OD2   . ASP B 2 27  ? -4.608  23.862  21.965 1.00 36.44 -1 20  ASP B OD2   1 
ATOM   2186 N N     . TYR B 2 28  ? -5.540  19.207  19.391 1.00 20.73 ?  21  TYR B N     1 
ATOM   2187 C CA    . TYR B 2 28  ? -5.765  18.447  18.166 1.00 20.65 ?  21  TYR B CA    1 
ATOM   2188 C C     . TYR B 2 28  ? -6.688  17.261  18.417 1.00 24.08 ?  21  TYR B C     1 
ATOM   2189 O O     . TYR B 2 28  ? -7.532  16.935  17.577 1.00 20.57 ?  21  TYR B O     1 
ATOM   2190 C CB    . TYR B 2 28  ? -4.432  17.978  17.582 1.00 21.43 ?  21  TYR B CB    1 
ATOM   2191 C CG    . TYR B 2 28  ? -4.557  17.052  16.389 1.00 24.01 ?  21  TYR B CG    1 
ATOM   2192 C CD1   . TYR B 2 28  ? -4.705  17.560  15.104 1.00 20.63 ?  21  TYR B CD1   1 
ATOM   2193 C CD2   . TYR B 2 28  ? -4.522  15.673  16.548 1.00 22.77 ?  21  TYR B CD2   1 
ATOM   2194 C CE1   . TYR B 2 28  ? -4.821  16.716  14.011 1.00 21.19 ?  21  TYR B CE1   1 
ATOM   2195 C CE2   . TYR B 2 28  ? -4.638  14.823  15.462 1.00 22.51 ?  21  TYR B CE2   1 
ATOM   2196 C CZ    . TYR B 2 28  ? -4.788  15.351  14.198 1.00 26.58 ?  21  TYR B CZ    1 
ATOM   2197 O OH    . TYR B 2 28  ? -4.902  14.507  13.114 1.00 21.97 ?  21  TYR B OH    1 
ATOM   2198 N N     . LYS B 2 29  ? -6.528  16.591  19.560 1.00 23.90 ?  22  LYS B N     1 
ATOM   2199 C CA    . LYS B 2 29  ? -7.318  15.392  19.829 1.00 30.07 ?  22  LYS B CA    1 
ATOM   2200 C C     . LYS B 2 29  ? -8.802  15.717  19.955 1.00 26.31 ?  22  LYS B C     1 
ATOM   2201 O O     . LYS B 2 29  ? -9.657  14.954  19.488 1.00 28.12 ?  22  LYS B O     1 
ATOM   2202 C CB    . LYS B 2 29  ? -6.820  14.714  21.106 1.00 29.20 ?  22  LYS B CB    1 
ATOM   2203 C CG    . LYS B 2 29  ? -5.577  13.857  20.931 1.00 41.38 ?  22  LYS B CG    1 
ATOM   2204 C CD    . LYS B 2 29  ? -5.897  12.378  21.062 1.00 43.00 ?  22  LYS B CD    1 
ATOM   2205 C CE    . LYS B 2 29  ? -4.753  11.634  21.731 1.00 52.62 ?  22  LYS B CE    1 
ATOM   2206 N NZ    . LYS B 2 29  ? -5.191  10.343  22.328 1.00 48.93 ?  22  LYS B NZ    1 
ATOM   2207 N N     . GLN B 2 30  ? -9.124  16.854  20.575 1.00 26.39 ?  23  GLN B N     1 
ATOM   2208 C CA    . GLN B 2 30  ? -10.520 17.260  20.710 1.00 27.12 ?  23  GLN B CA    1 
ATOM   2209 C C     . GLN B 2 30  ? -11.168 17.510  19.351 1.00 24.88 ?  23  GLN B C     1 
ATOM   2210 O O     . GLN B 2 30  ? -12.309 17.097  19.111 1.00 20.50 ?  23  GLN B O     1 
ATOM   2211 C CB    . GLN B 2 30  ? -10.630 18.501  21.595 1.00 28.29 ?  23  GLN B CB    1 
ATOM   2212 C CG    . GLN B 2 30  ? -10.508 18.230  23.098 1.00 31.98 ?  23  GLN B CG    1 
ATOM   2213 C CD    . GLN B 2 30  ? -11.783 17.686  23.733 1.00 38.02 ?  23  GLN B CD    1 
ATOM   2214 O OE1   . GLN B 2 30  ? -11.854 17.524  24.950 1.00 35.46 ?  23  GLN B OE1   1 
ATOM   2215 N NE2   . GLN B 2 30  ? -12.791 17.408  22.913 1.00 47.15 ?  23  GLN B NE2   1 
ATOM   2216 N N     . ASN B 2 31  ? -10.464 18.194  18.452 1.00 23.75 ?  24  ASN B N     1 
ATOM   2217 C CA    . ASN B 2 31  ? -11.047 18.652  17.188 1.00 20.65 ?  24  ASN B CA    1 
ATOM   2218 C C     . ASN B 2 31  ? -9.982  18.665  16.095 1.00 22.78 ?  24  ASN B C     1 
ATOM   2219 O O     . ASN B 2 31  ? -9.444  19.725  15.736 1.00 21.09 ?  24  ASN B O     1 
ATOM   2220 C CB    . ASN B 2 31  ? -11.664 20.041  17.363 1.00 24.38 ?  24  ASN B CB    1 
ATOM   2221 C CG    . ASN B 2 31  ? -12.705 20.365  16.323 1.00 21.07 ?  24  ASN B CG    1 
ATOM   2222 O OD1   . ASN B 2 31  ? -12.655 19.865  15.205 1.00 24.48 ?  24  ASN B OD1   1 
ATOM   2223 N ND2   . ASN B 2 31  ? -13.678 21.191  16.697 1.00 21.35 ?  24  ASN B ND2   1 
ATOM   2224 N N     . PRO B 2 32  ? -9.652  17.486  15.540 1.00 19.49 ?  25  PRO B N     1 
ATOM   2225 C CA    . PRO B 2 32  ? -8.576  17.431  14.533 1.00 20.78 ?  25  PRO B CA    1 
ATOM   2226 C C     . PRO B 2 32  ? -8.786  18.360  13.349 1.00 18.86 ?  25  PRO B C     1 
ATOM   2227 O O     . PRO B 2 32  ? -7.849  19.067  12.954 1.00 20.84 ?  25  PRO B O     1 
ATOM   2228 C CB    . PRO B 2 32  ? -8.576  15.962  14.104 1.00 18.29 ?  25  PRO B CB    1 
ATOM   2229 C CG    . PRO B 2 32  ? -9.310  15.211  15.136 1.00 22.73 ?  25  PRO B CG    1 
ATOM   2230 C CD    . PRO B 2 32  ? -9.996  16.152  16.082 1.00 24.79 ?  25  PRO B CD    1 
ATOM   2231 N N     . GLU B 2 33  ? -9.984  18.364  12.753 1.00 18.60 ?  26  GLU B N     1 
ATOM   2232 C CA    . GLU B 2 33  ? -10.203 19.181  11.560 1.00 20.98 ?  26  GLU B CA    1 
ATOM   2233 C C     . GLU B 2 33  ? -10.058 20.667  11.865 1.00 20.07 ?  26  GLU B C     1 
ATOM   2234 O O     . GLU B 2 33  ? -9.439  21.405  11.093 1.00 22.75 ?  26  GLU B O     1 
ATOM   2235 C CB    . GLU B 2 33  ? -11.581 18.894  10.958 1.00 27.74 ?  26  GLU B CB    1 
ATOM   2236 C CG    . GLU B 2 33  ? -11.552 17.924  9.777  1.00 32.79 ?  26  GLU B CG    1 
ATOM   2237 C CD    . GLU B 2 33  ? -12.764 18.055  8.869  1.00 41.71 ?  26  GLU B CD    1 
ATOM   2238 O OE1   . GLU B 2 33  ? -13.695 18.808  9.224  1.00 35.59 ?  26  GLU B OE1   1 
ATOM   2239 O OE2   . GLU B 2 33  ? -12.784 17.406  7.799  1.00 48.82 -1 26  GLU B OE2   1 
ATOM   2240 N N     . ALA B 2 34  ? -10.612 21.125  12.992 1.00 20.41 ?  27  ALA B N     1 
ATOM   2241 C CA    . ALA B 2 34  ? -10.553 22.550  13.311 1.00 24.37 ?  27  ALA B CA    1 
ATOM   2242 C C     . ALA B 2 34  ? -9.118  23.004  13.536 1.00 23.06 ?  27  ALA B C     1 
ATOM   2243 O O     . ALA B 2 34  ? -8.716  24.074  13.063 1.00 21.55 ?  27  ALA B O     1 
ATOM   2244 C CB    . ALA B 2 34  ? -11.409 22.857  14.537 1.00 24.81 ?  27  ALA B CB    1 
ATOM   2245 N N     . VAL B 2 35  ? -8.330  22.204  14.257 1.00 22.45 ?  28  VAL B N     1 
ATOM   2246 C CA    . VAL B 2 35  ? -6.935  22.563  14.493 1.00 22.09 ?  28  VAL B CA    1 
ATOM   2247 C C     . VAL B 2 35  ? -6.168  22.574  13.178 1.00 22.64 ?  28  VAL B C     1 
ATOM   2248 O O     . VAL B 2 35  ? -5.358  23.473  12.919 1.00 20.07 ?  28  VAL B O     1 
ATOM   2249 C CB    . VAL B 2 35  ? -6.294  21.604  15.514 1.00 23.68 ?  28  VAL B CB    1 
ATOM   2250 C CG1   . VAL B 2 35  ? -4.835  21.965  15.745 1.00 21.19 ?  28  VAL B CG1   1 
ATOM   2251 C CG2   . VAL B 2 35  ? -7.070  21.627  16.823 1.00 25.63 ?  28  VAL B CG2   1 
ATOM   2252 N N     . MET B 2 36  ? -6.417  21.576  12.326 1.00 16.43 ?  29  MET B N     1 
ATOM   2253 C CA    . MET B 2 36  ? -5.694  21.473  11.063 1.00 22.49 ?  29  MET B CA    1 
ATOM   2254 C C     . MET B 2 36  ? -6.023  22.636  10.129 1.00 24.78 ?  29  MET B C     1 
ATOM   2255 O O     . MET B 2 36  ? -5.119  23.205  9.504  1.00 22.92 ?  29  MET B O     1 
ATOM   2256 C CB    . MET B 2 36  ? -5.995  20.128  10.404 1.00 19.46 ?  29  MET B CB    1 
ATOM   2257 C CG    . MET B 2 36  ? -5.077  19.009  10.889 1.00 20.27 ?  29  MET B CG    1 
ATOM   2258 S SD    . MET B 2 36  ? -5.104  17.522  9.871  1.00 20.51 ?  29  MET B SD    1 
ATOM   2259 C CE    . MET B 2 36  ? -6.672  16.803  10.348 1.00 24.44 ?  29  MET B CE    1 
ATOM   2260 N N     . ARG B 2 37  ? -7.306  23.005  10.017 1.00 21.73 ?  30  ARG B N     1 
ATOM   2261 C CA    . ARG B 2 37  ? -7.661  24.161  9.196  1.00 25.28 ?  30  ARG B CA    1 
ATOM   2262 C C     . ARG B 2 37  ? -7.021  25.432  9.733  1.00 24.77 ?  30  ARG B C     1 
ATOM   2263 O O     . ARG B 2 37  ? -6.514  26.256  8.963  1.00 23.90 ?  30  ARG B O     1 
ATOM   2264 C CB    . ARG B 2 37  ? -9.176  24.345  9.135  1.00 29.75 ?  30  ARG B CB    1 
ATOM   2265 C CG    . ARG B 2 37  ? -9.969  23.156  8.647  1.00 32.59 ?  30  ARG B CG    1 
ATOM   2266 C CD    . ARG B 2 37  ? -11.396 23.577  8.331  1.00 36.02 ?  30  ARG B CD    1 
ATOM   2267 N NE    . ARG B 2 37  ? -11.809 23.150  7.000  1.00 44.52 ?  30  ARG B NE    1 
ATOM   2268 C CZ    . ARG B 2 37  ? -12.068 21.891  6.669  1.00 48.69 ?  30  ARG B CZ    1 
ATOM   2269 N NH1   . ARG B 2 37  ? -12.030 20.918  7.565  1.00 46.81 ?  30  ARG B NH1   1 
ATOM   2270 N NH2   . ARG B 2 37  ? -12.389 21.602  5.411  1.00 49.89 ?  30  ARG B NH2   1 
ATOM   2271 N N     . ALA B 2 38  ? -7.041  25.611  11.055 1.00 24.91 ?  31  ALA B N     1 
ATOM   2272 C CA    . ALA B 2 38  ? -6.490  26.819  11.653 1.00 25.73 ?  31  ALA B CA    1 
ATOM   2273 C C     . ALA B 2 38  ? -4.986  26.920  11.458 1.00 26.39 ?  31  ALA B C     1 
ATOM   2274 O O     . ALA B 2 38  ? -4.433  28.017  11.549 1.00 27.99 ?  31  ALA B O     1 
ATOM   2275 C CB    . ALA B 2 38  ? -6.834  26.873  13.142 1.00 25.08 ?  31  ALA B CB    1 
ATOM   2276 N N     . HIS B 2 39  ? -4.309  25.812  11.179 1.00 25.16 ?  32  HIS B N     1 
ATOM   2277 C CA    . HIS B 2 39  ? -2.879  25.854  10.926 1.00 26.48 ?  32  HIS B CA    1 
ATOM   2278 C C     . HIS B 2 39  ? -2.568  25.788  9.439  1.00 23.38 ?  32  HIS B C     1 
ATOM   2279 O O     . HIS B 2 39  ? -1.412  25.571  9.058  1.00 23.16 ?  32  HIS B O     1 
ATOM   2280 C CB    . HIS B 2 39  ? -2.173  24.736  11.691 1.00 20.95 ?  32  HIS B CB    1 
ATOM   2281 C CG    . HIS B 2 39  ? -1.984  25.042  13.145 1.00 28.67 ?  32  HIS B CG    1 
ATOM   2282 N ND1   . HIS B 2 39  ? -2.992  24.897  14.074 1.00 25.75 ?  32  HIS B ND1   1 
ATOM   2283 C CD2   . HIS B 2 39  ? -0.914  25.520  13.823 1.00 26.29 ?  32  HIS B CD2   1 
ATOM   2284 C CE1   . HIS B 2 39  ? -2.545  25.256  15.264 1.00 27.45 ?  32  HIS B CE1   1 
ATOM   2285 N NE2   . HIS B 2 39  ? -1.287  25.639  15.140 1.00 29.99 ?  32  HIS B NE2   1 
ATOM   2286 N N     . GLY B 2 40  ? -3.581  25.969  8.595  1.00 20.99 ?  33  GLY B N     1 
ATOM   2287 C CA    . GLY B 2 40  ? -3.386  26.217  7.184  1.00 24.52 ?  33  GLY B CA    1 
ATOM   2288 C C     . GLY B 2 40  ? -3.361  24.995  6.301  1.00 25.33 ?  33  GLY B C     1 
ATOM   2289 O O     . GLY B 2 40  ? -3.089  25.126  5.100  1.00 26.92 ?  33  GLY B O     1 
ATOM   2290 N N     . LEU B 2 41  ? -3.629  23.814  6.850  1.00 25.52 ?  34  LEU B N     1 
ATOM   2291 C CA    . LEU B 2 41  ? -3.627  22.604  6.041  1.00 25.71 ?  34  LEU B CA    1 
ATOM   2292 C C     . LEU B 2 41  ? -4.747  22.648  5.009  1.00 25.72 ?  34  LEU B C     1 
ATOM   2293 O O     . LEU B 2 41  ? -5.870  23.068  5.303  1.00 24.22 ?  34  LEU B O     1 
ATOM   2294 C CB    . LEU B 2 41  ? -3.770  21.363  6.928  1.00 25.72 ?  34  LEU B CB    1 
ATOM   2295 C CG    . LEU B 2 41  ? -2.472  20.822  7.546  1.00 24.40 ?  34  LEU B CG    1 
ATOM   2296 C CD1   . LEU B 2 41  ? -1.914  21.757  8.611  1.00 24.95 ?  34  LEU B CD1   1 
ATOM   2297 C CD2   . LEU B 2 41  ? -2.692  19.430  8.106  1.00 28.30 ?  34  LEU B CD2   1 
ATOM   2298 N N     . THR B 2 42  ? -4.435  22.214  3.792  1.00 27.69 ?  35  THR B N     1 
ATOM   2299 C CA    . THR B 2 42  ? -5.422  22.172  2.725  1.00 30.33 ?  35  THR B CA    1 
ATOM   2300 C C     . THR B 2 42  ? -6.400  21.019  2.943  1.00 30.90 ?  35  THR B C     1 
ATOM   2301 O O     . THR B 2 42  ? -6.236  20.181  3.836  1.00 28.04 ?  35  THR B O     1 
ATOM   2302 C CB    . THR B 2 42  ? -4.735  22.028  1.367  1.00 31.28 ?  35  THR B CB    1 
ATOM   2303 O OG1   . THR B 2 42  ? -4.025  20.784  1.327  1.00 30.33 ?  35  THR B OG1   1 
ATOM   2304 C CG2   . THR B 2 42  ? -3.765  23.172  1.133  1.00 29.16 ?  35  THR B CG2   1 
ATOM   2305 N N     . ASP B 2 43  ? -7.436  20.988  2.104  1.00 25.93 ?  36  ASP B N     1 
ATOM   2306 C CA    . ASP B 2 43  ? -8.426  19.920  2.202  1.00 33.96 ?  36  ASP B CA    1 
ATOM   2307 C C     . ASP B 2 43  ? -7.828  18.586  1.775  1.00 30.07 ?  36  ASP B C     1 
ATOM   2308 O O     . ASP B 2 43  ? -8.160  17.538  2.344  1.00 28.39 ?  36  ASP B O     1 
ATOM   2309 C CB    . ASP B 2 43  ? -9.658  20.251  1.359  1.00 37.86 ?  36  ASP B CB    1 
ATOM   2310 C CG    . ASP B 2 43  ? -10.408 21.460  1.878  1.00 40.47 ?  36  ASP B CG    1 
ATOM   2311 O OD1   . ASP B 2 43  ? -10.377 21.700  3.106  1.00 40.76 -1 36  ASP B OD1   1 
ATOM   2312 O OD2   . ASP B 2 43  ? -11.040 22.164  1.064  1.00 43.65 ?  36  ASP B OD2   1 
ATOM   2313 N N     . GLU B 2 44  ? -6.943  18.606  0.775  1.00 31.71 ?  37  GLU B N     1 
ATOM   2314 C CA    . GLU B 2 44  ? -6.269  17.377  0.370  1.00 32.06 ?  37  GLU B CA    1 
ATOM   2315 C C     . GLU B 2 44  ? -5.323  16.892  1.462  1.00 29.57 ?  37  GLU B C     1 
ATOM   2316 O O     . GLU B 2 44  ? -5.191  15.682  1.683  1.00 27.17 ?  37  GLU B O     1 
ATOM   2317 C CB    . GLU B 2 44  ? -5.517  17.595  -0.947 1.00 41.02 ?  37  GLU B CB    1 
ATOM   2318 C CG    . GLU B 2 44  ? -4.301  18.508  -0.840 1.00 41.84 ?  37  GLU B CG    1 
ATOM   2319 C CD    . GLU B 2 44  ? -3.820  19.022  -2.181 1.00 50.36 ?  37  GLU B CD    1 
ATOM   2320 O OE1   . GLU B 2 44  ? -3.194  18.243  -2.930 1.00 34.68 ?  37  GLU B OE1   1 
ATOM   2321 O OE2   . GLU B 2 44  ? -4.064  20.210  -2.482 1.00 48.51 -1 37  GLU B OE2   1 
ATOM   2322 N N     . GLN B 2 45  ? -4.659  17.822  2.156  1.00 30.87 ?  38  GLN B N     1 
ATOM   2323 C CA    . GLN B 2 45  ? -3.797  17.440  3.269  1.00 25.18 ?  38  GLN B CA    1 
ATOM   2324 C C     . GLN B 2 45  ? -4.618  16.877  4.421  1.00 28.05 ?  38  GLN B C     1 
ATOM   2325 O O     . GLN B 2 45  ? -4.243  15.865  5.026  1.00 28.81 ?  38  GLN B O     1 
ATOM   2326 C CB    . GLN B 2 45  ? -2.969  18.639  3.728  1.00 28.87 ?  38  GLN B CB    1 
ATOM   2327 C CG    . GLN B 2 45  ? -1.795  18.959  2.813  1.00 25.72 ?  38  GLN B CG    1 
ATOM   2328 C CD    . GLN B 2 45  ? -1.147  20.289  3.136  1.00 30.59 ?  38  GLN B CD    1 
ATOM   2329 O OE1   . GLN B 2 45  ? -1.677  21.077  3.917  1.00 32.13 ?  38  GLN B OE1   1 
ATOM   2330 N NE2   . GLN B 2 45  ? 0.007   20.549  2.530  1.00 31.76 ?  38  GLN B NE2   1 
ATOM   2331 N N     . ILE B 2 46  ? -5.745  17.521  4.736  1.00 26.59 ?  39  ILE B N     1 
ATOM   2332 C CA    . ILE B 2 46  ? -6.605  17.026  5.807  1.00 26.54 ?  39  ILE B CA    1 
ATOM   2333 C C     . ILE B 2 46  ? -7.181  15.668  5.430  1.00 28.16 ?  39  ILE B C     1 
ATOM   2334 O O     . ILE B 2 46  ? -7.230  14.749  6.256  1.00 29.50 ?  39  ILE B O     1 
ATOM   2335 C CB    . ILE B 2 46  ? -7.709  18.050  6.129  1.00 28.01 ?  39  ILE B CB    1 
ATOM   2336 C CG1   . ILE B 2 46  ? -7.105  19.277  6.818  1.00 26.18 ?  39  ILE B CG1   1 
ATOM   2337 C CG2   . ILE B 2 46  ? -8.786  17.432  7.007  1.00 23.72 ?  39  ILE B CG2   1 
ATOM   2338 C CD1   . ILE B 2 46  ? -8.081  20.417  7.007  1.00 25.41 ?  39  ILE B CD1   1 
ATOM   2339 N N     . ASN B 2 47  ? -7.600  15.510  4.170  1.00 26.79 ?  40  ASN B N     1 
ATOM   2340 C CA    . ASN B 2 47  ? -8.121  14.219  3.724  1.00 27.74 ?  40  ASN B CA    1 
ATOM   2341 C C     . ASN B 2 47  ? -7.067  13.127  3.845  1.00 26.74 ?  40  ASN B C     1 
ATOM   2342 O O     . ASN B 2 47  ? -7.375  11.998  4.247  1.00 28.97 ?  40  ASN B O     1 
ATOM   2343 C CB    . ASN B 2 47  ? -8.621  14.307  2.283  1.00 31.06 ?  40  ASN B CB    1 
ATOM   2344 C CG    . ASN B 2 47  ? -9.344  13.049  1.842  1.00 39.84 ?  40  ASN B CG    1 
ATOM   2345 O OD1   . ASN B 2 47  ? -10.388 12.699  2.387  1.00 37.88 ?  40  ASN B OD1   1 
ATOM   2346 N ND2   . ASN B 2 47  ? -8.777  12.352  0.861  1.00 34.91 ?  40  ASN B ND2   1 
ATOM   2347 N N     . ALA B 2 48  ? -5.818  13.440  3.488  1.00 26.25 ?  41  ALA B N     1 
ATOM   2348 C CA    . ALA B 2 48  ? -4.741  12.470  3.651  1.00 31.83 ?  41  ALA B CA    1 
ATOM   2349 C C     . ALA B 2 48  ? -4.608  12.052  5.108  1.00 27.91 ?  41  ALA B C     1 
ATOM   2350 O O     . ALA B 2 48  ? -4.371  10.875  5.407  1.00 27.29 ?  41  ALA B O     1 
ATOM   2351 C CB    . ALA B 2 48  ? -3.425  13.050  3.132  1.00 23.60 ?  41  ALA B CB    1 
ATOM   2352 N N     . VAL B 2 49  ? -4.758  13.008  6.029  1.00 23.70 ?  42  VAL B N     1 
ATOM   2353 C CA    . VAL B 2 49  ? -4.616  12.707  7.450  1.00 22.31 ?  42  VAL B CA    1 
ATOM   2354 C C     . VAL B 2 49  ? -5.762  11.821  7.925  1.00 26.62 ?  42  VAL B C     1 
ATOM   2355 O O     . VAL B 2 49  ? -5.548  10.849  8.660  1.00 31.31 ?  42  VAL B O     1 
ATOM   2356 C CB    . VAL B 2 49  ? -4.527  14.012  8.264  1.00 26.15 ?  42  VAL B CB    1 
ATOM   2357 C CG1   . VAL B 2 49  ? -4.761  13.741  9.742  1.00 25.38 ?  42  VAL B CG1   1 
ATOM   2358 C CG2   . VAL B 2 49  ? -3.183  14.686  8.040  1.00 24.45 ?  42  VAL B CG2   1 
ATOM   2359 N N     . MET B 2 50  ? -6.995  12.132  7.510  1.00 27.88 ?  43  MET B N     1 
ATOM   2360 C CA    . MET B 2 50  ? -8.154  11.415  8.027  1.00 30.82 ?  43  MET B CA    1 
ATOM   2361 C C     . MET B 2 50  ? -8.278  10.015  7.442  1.00 26.85 ?  43  MET B C     1 
ATOM   2362 O O     . MET B 2 50  ? -8.919  9.157   8.057  1.00 29.99 ?  43  MET B O     1 
ATOM   2363 C CB    . MET B 2 50  ? -9.438  12.205  7.758  1.00 25.38 ?  43  MET B CB    1 
ATOM   2364 C CG    . MET B 2 50  ? -9.370  13.670  8.154  1.00 28.59 ?  43  MET B CG    1 
ATOM   2365 S SD    . MET B 2 50  ? -8.929  13.938  9.884  1.00 31.13 ?  43  MET B SD    1 
ATOM   2366 C CE    . MET B 2 50  ? -10.177 12.963  10.716 1.00 25.43 ?  43  MET B CE    1 
ATOM   2367 N N     . THR B 2 51  ? -7.686  9.767   6.276  1.00 28.92 ?  44  THR B N     1 
ATOM   2368 C CA    . THR B 2 51  ? -7.667  8.439   5.681  1.00 29.93 ?  44  THR B CA    1 
ATOM   2369 C C     . THR B 2 51  ? -6.379  7.693   6.001  1.00 27.97 ?  44  THR B C     1 
ATOM   2370 O O     . THR B 2 51  ? -6.253  6.514   5.650  1.00 32.20 ?  44  THR B O     1 
ATOM   2371 C CB    . THR B 2 51  ? -7.855  8.525   4.161  1.00 30.44 ?  44  THR B CB    1 
ATOM   2372 O OG1   . THR B 2 51  ? -6.849  9.377   3.597  1.00 30.00 ?  44  THR B OG1   1 
ATOM   2373 C CG2   . THR B 2 51  ? -9.232  9.070   3.817  1.00 26.18 ?  44  THR B CG2   1 
ATOM   2374 N N     . GLY B 2 52  ? -5.423  8.353   6.650  1.00 26.88 ?  45  GLY B N     1 
ATOM   2375 C CA    . GLY B 2 52  ? -4.177  7.712   7.026  1.00 33.16 ?  45  GLY B CA    1 
ATOM   2376 C C     . GLY B 2 52  ? -3.263  7.396   5.866  1.00 34.66 ?  45  GLY B C     1 
ATOM   2377 O O     . GLY B 2 52  ? -2.550  6.388   5.902  1.00 36.30 ?  45  GLY B O     1 
ATOM   2378 N N     . ASP B 2 53  ? -3.248  8.241   4.839  1.00 33.10 ?  46  ASP B N     1 
ATOM   2379 C CA    . ASP B 2 53  ? -2.429  8.006   3.649  1.00 32.92 ?  46  ASP B CA    1 
ATOM   2380 C C     . ASP B 2 53  ? -1.103  8.735   3.828  1.00 34.76 ?  46  ASP B C     1 
ATOM   2381 O O     . ASP B 2 53  ? -0.946  9.896   3.444  1.00 27.36 ?  46  ASP B O     1 
ATOM   2382 C CB    . ASP B 2 53  ? -3.159  8.463   2.390  1.00 37.57 ?  46  ASP B CB    1 
ATOM   2383 C CG    . ASP B 2 53  ? -2.452  8.041   1.109  1.00 42.71 ?  46  ASP B CG    1 
ATOM   2384 O OD1   . ASP B 2 53  ? -1.226  7.813   1.135  1.00 39.33 ?  46  ASP B OD1   1 
ATOM   2385 O OD2   . ASP B 2 53  ? -3.132  7.936   0.068  1.00 41.37 -1 46  ASP B OD2   1 
ATOM   2386 N N     . MET B 2 54  ? -0.132  8.035   4.421  1.00 35.29 ?  47  MET B N     1 
ATOM   2387 C CA    . MET B 2 54  ? 1.178   8.633   4.640  1.00 40.44 ?  47  MET B CA    1 
ATOM   2388 C C     . MET B 2 54  ? 1.921   8.831   3.324  1.00 43.89 ?  47  MET B C     1 
ATOM   2389 O O     . MET B 2 54  ? 2.767   9.730   3.226  1.00 46.48 ?  47  MET B O     1 
ATOM   2390 C CB    . MET B 2 54  ? 1.997   7.783   5.611  1.00 42.64 ?  47  MET B CB    1 
ATOM   2391 C CG    . MET B 2 54  ? 1.366   7.630   6.995  1.00 35.59 ?  47  MET B CG    1 
ATOM   2392 S SD    . MET B 2 54  ? 0.967   9.193   7.812  1.00 34.33 ?  47  MET B SD    1 
ATOM   2393 C CE    . MET B 2 54  ? -0.826  9.135   7.827  1.00 29.81 ?  47  MET B CE    1 
ATOM   2394 N N     . GLU B 2 55  ? 1.644   7.989   2.321  1.00 38.93 ?  48  GLU B N     1 
ATOM   2395 C CA    . GLU B 2 55  ? 2.240   8.185   1.002  1.00 45.34 ?  48  GLU B CA    1 
ATOM   2396 C C     . GLU B 2 55  ? 1.948   9.590   0.493  1.00 36.98 ?  48  GLU B C     1 
ATOM   2397 O O     . GLU B 2 55  ? 2.856   10.334  0.104  1.00 39.48 ?  48  GLU B O     1 
ATOM   2398 C CB    . GLU B 2 55  ? 1.682   7.157   0.011  1.00 51.18 ?  48  GLU B CB    1 
ATOM   2399 C CG    . GLU B 2 55  ? 2.410   5.820   -0.119 1.00 55.15 ?  48  GLU B CG    1 
ATOM   2400 C CD    . GLU B 2 55  ? 3.840   5.953   -0.616 1.00 64.45 ?  48  GLU B CD    1 
ATOM   2401 O OE1   . GLU B 2 55  ? 4.696   6.454   0.139  1.00 67.50 ?  48  GLU B OE1   1 
ATOM   2402 O OE2   . GLU B 2 55  ? 4.095   5.578   -1.779 1.00 67.09 -1 48  GLU B OE2   1 
ATOM   2403 N N     . LYS B 2 56  ? 0.670   9.977   0.528  1.00 39.57 ?  49  LYS B N     1 
ATOM   2404 C CA    . LYS B 2 56  ? 0.244   11.262  -0.014 1.00 43.34 ?  49  LYS B CA    1 
ATOM   2405 C C     . LYS B 2 56  ? 0.743   12.429  0.828  1.00 43.97 ?  49  LYS B C     1 
ATOM   2406 O O     . LYS B 2 56  ? 1.036   13.501  0.286  1.00 47.73 ?  49  LYS B O     1 
ATOM   2407 C CB    . LYS B 2 56  ? -1.280  11.284  -0.128 1.00 39.14 ?  49  LYS B CB    1 
ATOM   2408 C CG    . LYS B 2 56  ? -1.856  12.532  -0.768 1.00 36.22 ?  49  LYS B CG    1 
ATOM   2409 C CD    . LYS B 2 56  ? -1.381  12.689  -2.204 1.00 51.70 ?  49  LYS B CD    1 
ATOM   2410 C CE    . LYS B 2 56  ? -1.677  11.458  -3.047 1.00 49.04 ?  49  LYS B CE    1 
ATOM   2411 N NZ    . LYS B 2 56  ? -0.527  11.107  -3.926 1.00 52.12 ?  49  LYS B NZ    1 
ATOM   2412 N N     . LEU B 2 57  ? 0.849   12.244  2.147  1.00 35.96 ?  50  LEU B N     1 
ATOM   2413 C CA    . LEU B 2 57  ? 1.325   13.327  3.002  1.00 38.92 ?  50  LEU B CA    1 
ATOM   2414 C C     . LEU B 2 57  ? 2.761   13.700  2.663  1.00 46.94 ?  50  LEU B C     1 
ATOM   2415 O O     . LEU B 2 57  ? 3.122   14.883  2.657  1.00 45.61 ?  50  LEU B O     1 
ATOM   2416 C CB    . LEU B 2 57  ? 1.205   12.932  4.471  1.00 39.00 ?  50  LEU B CB    1 
ATOM   2417 C CG    . LEU B 2 57  ? -0.192  13.100  5.074  1.00 34.90 ?  50  LEU B CG    1 
ATOM   2418 C CD1   . LEU B 2 57  ? -0.226  12.559  6.489  1.00 29.26 ?  50  LEU B CD1   1 
ATOM   2419 C CD2   . LEU B 2 57  ? -0.617  14.560  5.037  1.00 30.41 ?  50  LEU B CD2   1 
ATOM   2420 N N     . LYS B 2 58  ? 3.594   12.700  2.379  1.00 42.70 ?  51  LYS B N     1 
ATOM   2421 C CA    . LYS B 2 58  ? 4.978   12.972  2.012  1.00 48.59 ?  51  LYS B CA    1 
ATOM   2422 C C     . LYS B 2 58  ? 5.053   13.650  0.648  1.00 47.34 ?  51  LYS B C     1 
ATOM   2423 O O     . LYS B 2 58  ? 5.906   14.518  0.424  1.00 47.79 ?  51  LYS B O     1 
ATOM   2424 C CB    . LYS B 2 58  ? 5.782   11.673  2.045  1.00 53.77 ?  51  LYS B CB    1 
ATOM   2425 C CG    . LYS B 2 58  ? 5.887   11.098  3.452  1.00 48.77 ?  51  LYS B CG    1 
ATOM   2426 C CD    . LYS B 2 58  ? 6.361   9.658   3.487  1.00 57.73 ?  51  LYS B CD    1 
ATOM   2427 C CE    . LYS B 2 58  ? 6.408   9.160   4.926  1.00 48.54 ?  51  LYS B CE    1 
ATOM   2428 N NZ    . LYS B 2 58  ? 6.963   7.786   5.061  1.00 46.54 ?  51  LYS B NZ    1 
ATOM   2429 N N     . THR B 2 59  ? 4.172   13.257  -0.275 1.00 44.03 ?  52  THR B N     1 
ATOM   2430 C CA    . THR B 2 59  ? 4.042   13.963  -1.546 1.00 52.23 ?  52  THR B CA    1 
ATOM   2431 C C     . THR B 2 59  ? 3.758   15.444  -1.328 1.00 57.18 ?  52  THR B C     1 
ATOM   2432 O O     . THR B 2 59  ? 4.472   16.312  -1.844 1.00 58.61 ?  52  THR B O     1 
ATOM   2433 C CB    . THR B 2 59  ? 2.932   13.330  -2.386 1.00 50.25 ?  52  THR B CB    1 
ATOM   2434 O OG1   . THR B 2 59  ? 3.197   11.936  -2.569 1.00 49.27 ?  52  THR B OG1   1 
ATOM   2435 C CG2   . THR B 2 59  ? 2.827   14.010  -3.746 1.00 56.19 ?  52  THR B CG2   1 
ATOM   2436 N N     . LEU B 2 60  ? 2.719   15.749  -0.556 1.00 54.20 ?  53  LEU B N     1 
ATOM   2437 C CA    . LEU B 2 60  ? 2.250   17.115  -0.380 1.00 54.40 ?  53  LEU B CA    1 
ATOM   2438 C C     . LEU B 2 60  ? 3.235   17.965  0.412  1.00 55.56 ?  53  LEU B C     1 
ATOM   2439 O O     . LEU B 2 60  ? 3.314   19.177  0.229  1.00 64.62 ?  53  LEU B O     1 
ATOM   2440 C CB    . LEU B 2 60  ? 0.879   17.114  0.310  1.00 50.00 ?  53  LEU B CB    1 
ATOM   2441 C CG    . LEU B 2 60  ? -0.210  16.352  -0.450 1.00 48.44 ?  53  LEU B CG    1 
ATOM   2442 C CD1   . LEU B 2 60  ? -1.507  16.306  0.343  1.00 34.74 ?  53  LEU B CD1   1 
ATOM   2443 C CD2   . LEU B 2 60  ? -0.434  16.962  -1.824 1.00 45.75 ?  53  LEU B CD2   1 
ATOM   2444 N N     . GLY C 1 2   ? -12.662 14.829  32.576 1.00 26.19 ?  2   GLY C N     1 
ATOM   2445 C CA    . GLY C 1 2   ? -11.250 14.628  32.829 1.00 23.98 ?  2   GLY C CA    1 
ATOM   2446 C C     . GLY C 1 2   ? -10.615 13.605  31.906 1.00 25.28 ?  2   GLY C C     1 
ATOM   2447 O O     . GLY C 1 2   ? -11.309 12.920  31.152 1.00 22.99 ?  2   GLY C O     1 
ATOM   2448 N N     . SER C 1 3   ? -9.290  13.501  31.967 1.00 18.31 ?  3   SER C N     1 
ATOM   2449 C CA    . SER C 1 3   ? -8.550  12.588  31.110 1.00 23.54 ?  3   SER C CA    1 
ATOM   2450 C C     . SER C 1 3   ? -7.328  12.095  31.866 1.00 24.11 ?  3   SER C C     1 
ATOM   2451 O O     . SER C 1 3   ? -7.027  12.554  32.970 1.00 22.30 ?  3   SER C O     1 
ATOM   2452 C CB    . SER C 1 3   ? -8.145  13.256  29.796 1.00 20.56 ?  3   SER C CB    1 
ATOM   2453 O OG    . SER C 1 3   ? -7.392  14.434  30.034 1.00 27.30 ?  3   SER C OG    1 
ATOM   2454 N N     . LEU C 1 4   ? -6.622  11.147  31.256 1.00 24.00 ?  4   LEU C N     1 
ATOM   2455 C CA    . LEU C 1 4   ? -5.456  10.537  31.878 1.00 20.81 ?  4   LEU C CA    1 
ATOM   2456 C C     . LEU C 1 4   ? -4.367  10.329  30.839 1.00 21.11 ?  4   LEU C C     1 
ATOM   2457 O O     . LEU C 1 4   ? -4.618  9.758   29.775 1.00 19.95 ?  4   LEU C O     1 
ATOM   2458 C CB    . LEU C 1 4   ? -5.815  9.198   32.532 1.00 23.34 ?  4   LEU C CB    1 
ATOM   2459 C CG    . LEU C 1 4   ? -4.667  8.422   33.175 1.00 23.03 ?  4   LEU C CG    1 
ATOM   2460 C CD1   . LEU C 1 4   ? -3.957  9.270   34.220 1.00 23.69 ?  4   LEU C CD1   1 
ATOM   2461 C CD2   . LEU C 1 4   ? -5.171  7.122   33.783 1.00 18.41 ?  4   LEU C CD2   1 
ATOM   2462 N N     . VAL C 1 5   ? -3.166  10.811  31.138 1.00 17.14 ?  5   VAL C N     1 
ATOM   2463 C CA    . VAL C 1 5   ? -1.967  10.459  30.388 1.00 10.72 ?  5   VAL C CA    1 
ATOM   2464 C C     . VAL C 1 5   ? -0.920  9.983   31.382 1.00 13.30 ?  5   VAL C C     1 
ATOM   2465 O O     . VAL C 1 5   ? -0.607  10.687  32.348 1.00 14.17 ?  5   VAL C O     1 
ATOM   2466 C CB    . VAL C 1 5   ? -1.424  11.638  29.556 1.00 16.80 ?  5   VAL C CB    1 
ATOM   2467 C CG1   . VAL C 1 5   ? -0.224  11.187  28.730 1.00 14.35 ?  5   VAL C CG1   1 
ATOM   2468 C CG2   . VAL C 1 5   ? -2.510  12.202  28.650 1.00 15.88 ?  5   VAL C CG2   1 
ATOM   2469 N N     . CYS C 1 6   ? -0.384  8.793   31.152 1.00 15.73 ?  6   CYS C N     1 
ATOM   2470 C CA    . CYS C 1 6   ? 0.710   8.266   31.950 1.00 13.62 ?  6   CYS C CA    1 
ATOM   2471 C C     . CYS C 1 6   ? 1.995   8.394   31.148 1.00 9.88  ?  6   CYS C C     1 
ATOM   2472 O O     . CYS C 1 6   ? 2.067   7.943   30.001 1.00 9.58  ?  6   CYS C O     1 
ATOM   2473 C CB    . CYS C 1 6   ? 0.461   6.807   32.342 1.00 16.96 ?  6   CYS C CB    1 
ATOM   2474 S SG    . CYS C 1 6   ? -1.118  6.514   33.188 1.00 19.72 ?  6   CYS C SG    1 
ATOM   2475 N N     . VAL C 1 7   ? 3.001   9.025   31.744 1.00 17.34 ?  7   VAL C N     1 
ATOM   2476 C CA    . VAL C 1 7   ? 4.284   9.219   31.090 1.00 16.05 ?  7   VAL C CA    1 
ATOM   2477 C C     . VAL C 1 7   ? 5.365   8.554   31.930 1.00 16.12 ?  7   VAL C C     1 
ATOM   2478 O O     . VAL C 1 7   ? 5.149   8.168   33.079 1.00 16.48 ?  7   VAL C O     1 
ATOM   2479 C CB    . VAL C 1 7   ? 4.615   10.710  30.866 1.00 14.67 ?  7   VAL C CB    1 
ATOM   2480 C CG1   . VAL C 1 7   ? 3.468   11.409  30.149 1.00 13.35 ?  7   VAL C CG1   1 
ATOM   2481 C CG2   . VAL C 1 7   ? 4.923   11.395  32.191 1.00 17.05 ?  7   VAL C CG2   1 
ATOM   2482 N N     . GLY C 1 8   ? 6.542   8.427   31.332 1.00 15.31 ?  8   GLY C N     1 
ATOM   2483 C CA    . GLY C 1 8   ? 7.721   8.064   32.082 1.00 14.57 ?  8   GLY C CA    1 
ATOM   2484 C C     . GLY C 1 8   ? 8.694   9.221   32.133 1.00 16.66 ?  8   GLY C C     1 
ATOM   2485 O O     . GLY C 1 8   ? 8.681   10.087  31.254 1.00 14.91 ?  8   GLY C O     1 
ATOM   2486 N N     . THR C 1 9   ? 9.544   9.249   33.152 1.00 13.31 ?  9   THR C N     1 
ATOM   2487 C CA    . THR C 1 9   ? 10.535  10.303  33.299 1.00 18.13 ?  9   THR C CA    1 
ATOM   2488 C C     . THR C 1 9   ? 11.948  9.803   33.042 1.00 17.79 ?  9   THR C C     1 
ATOM   2489 O O     . THR C 1 9   ? 12.906  10.568  33.204 1.00 18.31 ?  9   THR C O     1 
ATOM   2490 C CB    . THR C 1 9   ? 10.453  10.924  34.698 1.00 18.77 ?  9   THR C CB    1 
ATOM   2491 O OG1   . THR C 1 9   ? 10.642  9.902   35.682 1.00 14.49 ?  9   THR C OG1   1 
ATOM   2492 C CG2   . THR C 1 9   ? 9.099   11.581  34.906 1.00 19.94 ?  9   THR C CG2   1 
ATOM   2493 N N     . GLY C 1 10  ? 12.100  8.548   32.643 1.00 18.84 ?  10  GLY C N     1 
ATOM   2494 C CA    . GLY C 1 10  ? 13.408  7.971   32.478 1.00 16.72 ?  10  GLY C CA    1 
ATOM   2495 C C     . GLY C 1 10  ? 14.015  7.657   33.831 1.00 14.46 ?  10  GLY C C     1 
ATOM   2496 O O     . GLY C 1 10  ? 13.384  7.794   34.883 1.00 18.69 ?  10  GLY C O     1 
ATOM   2497 N N     . LEU C 1 11  ? 15.270  7.224   33.796 1.00 16.17 ?  11  LEU C N     1 
ATOM   2498 C CA    . LEU C 1 11  ? 15.989  6.873   35.015 1.00 15.03 ?  11  LEU C CA    1 
ATOM   2499 C C     . LEU C 1 11  ? 16.851  8.016   35.525 1.00 13.43 ?  11  LEU C C     1 
ATOM   2500 O O     . LEU C 1 11  ? 16.963  8.210   36.739 1.00 10.37 ?  11  LEU C O     1 
ATOM   2501 C CB    . LEU C 1 11  ? 16.863  5.631   34.789 1.00 16.66 ?  11  LEU C CB    1 
ATOM   2502 C CG    . LEU C 1 11  ? 16.189  4.249   34.843 1.00 14.50 ?  11  LEU C CG    1 
ATOM   2503 C CD1   . LEU C 1 11  ? 15.760  3.920   36.268 1.00 20.52 ?  11  LEU C CD1   1 
ATOM   2504 C CD2   . LEU C 1 11  ? 15.023  4.114   33.873 1.00 18.56 ?  11  LEU C CD2   1 
ATOM   2505 N N     . GLN C 1 12  ? 17.450  8.783   34.619 1.00 12.96 ?  12  GLN C N     1 
ATOM   2506 C CA    . GLN C 1 12  ? 18.320  9.883   34.996 1.00 19.64 ?  12  GLN C CA    1 
ATOM   2507 C C     . GLN C 1 12  ? 17.512  11.141  35.289 1.00 17.03 ?  12  GLN C C     1 
ATOM   2508 O O     . GLN C 1 12  ? 16.451  11.382  34.706 1.00 18.65 ?  12  GLN C O     1 
ATOM   2509 C CB    . GLN C 1 12  ? 19.343  10.168  33.896 1.00 14.15 ?  12  GLN C CB    1 
ATOM   2510 C CG    . GLN C 1 12  ? 20.628  9.369   34.023 1.00 19.50 ?  12  GLN C CG    1 
ATOM   2511 C CD    . GLN C 1 12  ? 21.577  9.953   35.052 1.00 19.10 ?  12  GLN C CD    1 
ATOM   2512 O OE1   . GLN C 1 12  ? 21.250  10.927  35.729 1.00 16.67 ?  12  GLN C OE1   1 
ATOM   2513 N NE2   . GLN C 1 12  ? 22.760  9.363   35.171 1.00 25.36 ?  12  GLN C NE2   1 
ATOM   2514 N N     . LEU C 1 13  ? 18.034  11.937  36.215 1.00 19.53 ?  13  LEU C N     1 
ATOM   2515 C CA    . LEU C 1 13  ? 17.409  13.190  36.624 1.00 16.03 ?  13  LEU C CA    1 
ATOM   2516 C C     . LEU C 1 13  ? 17.187  14.127  35.441 1.00 16.49 ?  13  LEU C C     1 
ATOM   2517 O O     . LEU C 1 13  ? 18.136  14.480  34.731 1.00 18.78 ?  13  LEU C O     1 
ATOM   2518 C CB    . LEU C 1 13  ? 18.289  13.861  37.679 1.00 17.58 ?  13  LEU C CB    1 
ATOM   2519 C CG    . LEU C 1 13  ? 17.873  15.196  38.281 1.00 14.97 ?  13  LEU C CG    1 
ATOM   2520 C CD1   . LEU C 1 13  ? 16.509  15.096  38.917 1.00 16.40 ?  13  LEU C CD1   1 
ATOM   2521 C CD2   . LEU C 1 13  ? 18.905  15.614  39.305 1.00 17.12 ?  13  LEU C CD2   1 
ATOM   2522 N N     . ALA C 1 14  ? 15.918  14.488  35.214 1.00 16.32 ?  14  ALA C N     1 
ATOM   2523 C CA    . ALA C 1 14  ? 15.528  15.668  34.443 1.00 18.49 ?  14  ALA C CA    1 
ATOM   2524 C C     . ALA C 1 14  ? 15.706  15.512  32.936 1.00 19.13 ?  14  ALA C C     1 
ATOM   2525 O O     . ALA C 1 14  ? 14.852  15.959  32.164 1.00 17.25 ?  14  ALA C O     1 
ATOM   2526 C CB    . ALA C 1 14  ? 16.302  16.899  34.936 1.00 13.95 ?  14  ALA C CB    1 
ATOM   2527 N N     . GLY C 1 15  ? 16.805  14.899  32.500 1.00 19.53 ?  15  GLY C N     1 
ATOM   2528 C CA    . GLY C 1 15  ? 17.166  14.941  31.096 1.00 17.87 ?  15  GLY C CA    1 
ATOM   2529 C C     . GLY C 1 15  ? 16.722  13.767  30.249 1.00 20.98 ?  15  GLY C C     1 
ATOM   2530 O O     . GLY C 1 15  ? 16.800  13.830  29.020 1.00 18.37 ?  15  GLY C O     1 
ATOM   2531 N N     . GLN C 1 16  ? 16.238  12.697  30.872 1.00 16.94 ?  16  GLN C N     1 
ATOM   2532 C CA    . GLN C 1 16  ? 15.916  11.474  30.148 1.00 19.29 ?  16  GLN C CA    1 
ATOM   2533 C C     . GLN C 1 16  ? 14.424  11.350  29.859 1.00 15.69 ?  16  GLN C C     1 
ATOM   2534 O O     . GLN C 1 16  ? 13.998  10.366  29.243 1.00 15.63 ?  16  GLN C O     1 
ATOM   2535 C CB    . GLN C 1 16  ? 16.418  10.250  30.925 1.00 15.43 ?  16  GLN C CB    1 
ATOM   2536 C CG    . GLN C 1 16  ? 16.653  9.027   30.056 1.00 17.84 ?  16  GLN C CG    1 
ATOM   2537 C CD    . GLN C 1 16  ? 17.658  8.071   30.660 1.00 20.96 ?  16  GLN C CD    1 
ATOM   2538 O OE1   . GLN C 1 16  ? 17.455  7.542   31.753 1.00 17.71 ?  16  GLN C OE1   1 
ATOM   2539 N NE2   . GLN C 1 16  ? 18.764  7.861   29.959 1.00 15.47 ?  16  GLN C NE2   1 
ATOM   2540 N N     . ILE C 1 17  ? 13.631  12.329  30.281 1.00 17.30 ?  17  ILE C N     1 
ATOM   2541 C CA    . ILE C 1 17  ? 12.227  12.412  29.902 1.00 17.70 ?  17  ILE C CA    1 
ATOM   2542 C C     . ILE C 1 17  ? 12.135  12.951  28.481 1.00 18.53 ?  17  ILE C C     1 
ATOM   2543 O O     . ILE C 1 17  ? 12.961  13.760  28.047 1.00 19.93 ?  17  ILE C O     1 
ATOM   2544 C CB    . ILE C 1 17  ? 11.459  13.299  30.906 1.00 15.97 ?  17  ILE C CB    1 
ATOM   2545 C CG1   . ILE C 1 17  ? 9.952   13.250  30.644 1.00 17.54 ?  17  ILE C CG1   1 
ATOM   2546 C CG2   . ILE C 1 17  ? 11.978  14.734  30.868 1.00 15.36 ?  17  ILE C CG2   1 
ATOM   2547 C CD1   . ILE C 1 17  ? 9.129   13.915  31.730 1.00 19.82 ?  17  ILE C CD1   1 
ATOM   2548 N N     . SER C 1 18  ? 11.136  12.493  27.735 1.00 16.80 ?  18  SER C N     1 
ATOM   2549 C CA    . SER C 1 18  ? 10.990  12.961  26.367 1.00 19.32 ?  18  SER C CA    1 
ATOM   2550 C C     . SER C 1 18  ? 10.390  14.365  26.350 1.00 21.47 ?  18  SER C C     1 
ATOM   2551 O O     . SER C 1 18  ? 9.782   14.827  27.322 1.00 17.81 ?  18  SER C O     1 
ATOM   2552 C CB    . SER C 1 18  ? 10.131  11.997  25.546 1.00 20.84 ?  18  SER C CB    1 
ATOM   2553 O OG    . SER C 1 18  ? 8.760   12.121  25.869 1.00 19.93 ?  18  SER C OG    1 
ATOM   2554 N N     . VAL C 1 19  ? 10.582  15.048  25.218 1.00 18.91 ?  19  VAL C N     1 
ATOM   2555 C CA    . VAL C 1 19  ? 10.153  16.441  25.101 1.00 23.54 ?  19  VAL C CA    1 
ATOM   2556 C C     . VAL C 1 19  ? 8.640   16.545  25.245 1.00 20.30 ?  19  VAL C C     1 
ATOM   2557 O O     . VAL C 1 19  ? 8.125   17.409  25.966 1.00 17.16 ?  19  VAL C O     1 
ATOM   2558 C CB    . VAL C 1 19  ? 10.638  17.042  23.769 1.00 19.52 ?  19  VAL C CB    1 
ATOM   2559 C CG1   . VAL C 1 19  ? 10.037  18.420  23.550 1.00 22.61 ?  19  VAL C CG1   1 
ATOM   2560 C CG2   . VAL C 1 19  ? 12.160  17.107  23.742 1.00 17.68 ?  19  VAL C CG2   1 
ATOM   2561 N N     . LEU C 1 20  ? 7.906   15.665  24.558 1.00 20.90 ?  20  LEU C N     1 
ATOM   2562 C CA    . LEU C 1 20  ? 6.450   15.670  24.669 1.00 21.58 ?  20  LEU C CA    1 
ATOM   2563 C C     . LEU C 1 20  ? 6.003   15.330  26.084 1.00 19.37 ?  20  LEU C C     1 
ATOM   2564 O O     . LEU C 1 20  ? 5.085   15.961  26.622 1.00 21.27 ?  20  LEU C O     1 
ATOM   2565 C CB    . LEU C 1 20  ? 5.838   14.685  23.675 1.00 18.08 ?  20  LEU C CB    1 
ATOM   2566 C CG    . LEU C 1 20  ? 4.310   14.580  23.710 1.00 15.13 ?  20  LEU C CG    1 
ATOM   2567 C CD1   . LEU C 1 20  ? 3.656   15.957  23.621 1.00 16.01 ?  20  LEU C CD1   1 
ATOM   2568 C CD2   . LEU C 1 20  ? 3.791   13.662  22.614 1.00 19.27 ?  20  LEU C CD2   1 
ATOM   2569 N N     . SER C 1 21  ? 6.644   14.337  26.704 1.00 17.46 ?  21  SER C N     1 
ATOM   2570 C CA    . SER C 1 21  ? 6.219   13.890  28.028 1.00 15.41 ?  21  SER C CA    1 
ATOM   2571 C C     . SER C 1 21  ? 6.401   14.991  29.063 1.00 19.12 ?  21  SER C C     1 
ATOM   2572 O O     . SER C 1 21  ? 5.560   15.162  29.954 1.00 18.56 ?  21  SER C O     1 
ATOM   2573 C CB    . SER C 1 21  ? 6.992   12.635  28.432 1.00 18.76 ?  21  SER C CB    1 
ATOM   2574 O OG    . SER C 1 21  ? 6.546   11.510  27.696 1.00 21.45 ?  21  SER C OG    1 
ATOM   2575 N N     . ARG C 1 22  ? 7.505   15.739  28.967 1.00 13.94 ?  22  ARG C N     1 
ATOM   2576 C CA    . ARG C 1 22  ? 7.695   16.889  29.846 1.00 14.76 ?  22  ARG C CA    1 
ATOM   2577 C C     . ARG C 1 22  ? 6.582   17.910  29.650 1.00 15.67 ?  22  ARG C C     1 
ATOM   2578 O O     . ARG C 1 22  ? 6.094   18.506  30.620 1.00 12.30 ?  22  ARG C O     1 
ATOM   2579 C CB    . ARG C 1 22  ? 9.059   17.527  29.590 1.00 17.71 ?  22  ARG C CB    1 
ATOM   2580 C CG    . ARG C 1 22  ? 9.527   18.472  30.684 1.00 17.75 ?  22  ARG C CG    1 
ATOM   2581 C CD    . ARG C 1 22  ? 10.804  19.194  30.286 1.00 24.51 ?  22  ARG C CD    1 
ATOM   2582 N NE    . ARG C 1 22  ? 11.293  20.075  31.340 1.00 20.73 ?  22  ARG C NE    1 
ATOM   2583 C CZ    . ARG C 1 22  ? 11.229  21.400  31.298 1.00 28.06 ?  22  ARG C CZ    1 
ATOM   2584 N NH1   . ARG C 1 22  ? 10.652  22.034  30.289 1.00 31.88 ?  22  ARG C NH1   1 
ATOM   2585 N NH2   . ARG C 1 22  ? 11.744  22.108  32.299 1.00 32.02 ?  22  ARG C NH2   1 
ATOM   2586 N N     . SER C 1 23  ? 6.168   18.126  28.397 1.00 15.77 ?  23  SER C N     1 
ATOM   2587 C CA    . SER C 1 23  ? 5.117   19.098  28.115 1.00 18.07 ?  23  SER C CA    1 
ATOM   2588 C C     . SER C 1 23  ? 3.795   18.669  28.735 1.00 18.61 ?  23  SER C C     1 
ATOM   2589 O O     . SER C 1 23  ? 3.020   19.511  29.204 1.00 21.03 ?  23  SER C O     1 
ATOM   2590 C CB    . SER C 1 23  ? 4.968   19.287  26.604 1.00 15.98 ?  23  SER C CB    1 
ATOM   2591 O OG    . SER C 1 23  ? 4.052   20.324  26.301 1.00 14.63 ?  23  SER C OG    1 
ATOM   2592 N N     . TYR C 1 24  ? 3.519   17.361  28.741 1.00 13.61 ?  24  TYR C N     1 
ATOM   2593 C CA    . TYR C 1 24  ? 2.300   16.862  29.373 1.00 15.18 ?  24  TYR C CA    1 
ATOM   2594 C C     . TYR C 1 24  ? 2.290   17.174  30.864 1.00 16.70 ?  24  TYR C C     1 
ATOM   2595 O O     . TYR C 1 24  ? 1.266   17.595  31.415 1.00 18.32 ?  24  TYR C O     1 
ATOM   2596 C CB    . TYR C 1 24  ? 2.165   15.359  29.144 1.00 15.34 ?  24  TYR C CB    1 
ATOM   2597 C CG    . TYR C 1 24  ? 1.397   14.992  27.896 1.00 17.36 ?  24  TYR C CG    1 
ATOM   2598 C CD1   . TYR C 1 24  ? 0.046   15.291  27.774 1.00 17.51 ?  24  TYR C CD1   1 
ATOM   2599 C CD2   . TYR C 1 24  ? 2.022   14.342  26.841 1.00 20.26 ?  24  TYR C CD2   1 
ATOM   2600 C CE1   . TYR C 1 24  ? -0.658  14.957  26.632 1.00 20.93 ?  24  TYR C CE1   1 
ATOM   2601 C CE2   . TYR C 1 24  ? 1.328   14.003  25.698 1.00 19.84 ?  24  TYR C CE2   1 
ATOM   2602 C CZ    . TYR C 1 24  ? -0.011  14.313  25.599 1.00 24.85 ?  24  TYR C CZ    1 
ATOM   2603 O OH    . TYR C 1 24  ? -0.702  13.977  24.458 1.00 28.38 ?  24  TYR C OH    1 
ATOM   2604 N N     . ILE C 1 25  ? 3.424   16.959  31.533 1.00 16.15 ?  25  ILE C N     1 
ATOM   2605 C CA    . ILE C 1 25  ? 3.536   17.274  32.956 1.00 19.97 ?  25  ILE C CA    1 
ATOM   2606 C C     . ILE C 1 25  ? 3.287   18.757  33.185 1.00 17.36 ?  25  ILE C C     1 
ATOM   2607 O O     . ILE C 1 25  ? 2.503   19.153  34.056 1.00 19.77 ?  25  ILE C O     1 
ATOM   2608 C CB    . ILE C 1 25  ? 4.919   16.855  33.487 1.00 19.75 ?  25  ILE C CB    1 
ATOM   2609 C CG1   . ILE C 1 25  ? 4.975   15.343  33.722 1.00 18.26 ?  25  ILE C CG1   1 
ATOM   2610 C CG2   . ILE C 1 25  ? 5.255   17.613  34.757 1.00 19.19 ?  25  ILE C CG2   1 
ATOM   2611 C CD1   . ILE C 1 25  ? 6.350   14.850  34.130 1.00 18.71 ?  25  ILE C CD1   1 
ATOM   2612 N N     . GLU C 1 26  ? 3.973   19.596  32.407 1.00 19.75 ?  26  GLU C N     1 
ATOM   2613 C CA    . GLU C 1 26  ? 3.884   21.046  32.554 1.00 23.24 ?  26  GLU C CA    1 
ATOM   2614 C C     . GLU C 1 26  ? 2.438   21.535  32.509 1.00 21.27 ?  26  GLU C C     1 
ATOM   2615 O O     . GLU C 1 26  ? 2.019   22.358  33.332 1.00 21.74 ?  26  GLU C O     1 
ATOM   2616 C CB    . GLU C 1 26  ? 4.724   21.709  31.462 1.00 20.83 ?  26  GLU C CB    1 
ATOM   2617 C CG    . GLU C 1 26  ? 4.692   23.223  31.424 1.00 31.00 ?  26  GLU C CG    1 
ATOM   2618 C CD    . GLU C 1 26  ? 5.676   23.781  30.415 1.00 41.60 ?  26  GLU C CD    1 
ATOM   2619 O OE1   . GLU C 1 26  ? 6.326   22.974  29.716 1.00 38.78 ?  26  GLU C OE1   1 
ATOM   2620 O OE2   . GLU C 1 26  ? 5.806   25.021  30.321 1.00 47.01 -1 26  GLU C OE2   1 
ATOM   2621 N N     . HIS C 1 27  ? 1.656   21.029  31.559 1.00 18.81 ?  27  HIS C N     1 
ATOM   2622 C CA    . HIS C 1 27  ? 0.321   21.550  31.293 1.00 25.36 ?  27  HIS C CA    1 
ATOM   2623 C C     . HIS C 1 27  ? -0.779  20.831  32.069 1.00 25.08 ?  27  HIS C C     1 
ATOM   2624 O O     . HIS C 1 27  ? -1.950  21.188  31.924 1.00 20.37 ?  27  HIS C O     1 
ATOM   2625 C CB    . HIS C 1 27  ? 0.025   21.481  29.790 1.00 25.08 ?  27  HIS C CB    1 
ATOM   2626 C CG    . HIS C 1 27  ? 0.724   22.535  28.990 1.00 29.85 ?  27  HIS C CG    1 
ATOM   2627 N ND1   . HIS C 1 27  ? 0.302   23.847  28.958 1.00 27.68 ?  27  HIS C ND1   1 
ATOM   2628 C CD2   . HIS C 1 27  ? 1.820   22.474  28.195 1.00 28.74 ?  27  HIS C CD2   1 
ATOM   2629 C CE1   . HIS C 1 27  ? 1.105   24.547  28.177 1.00 32.99 ?  27  HIS C CE1   1 
ATOM   2630 N NE2   . HIS C 1 27  ? 2.034   23.738  27.702 1.00 32.01 ?  27  HIS C NE2   1 
ATOM   2631 N N     . ALA C 1 28  ? -0.436  19.836  32.882 1.00 22.14 ?  28  ALA C N     1 
ATOM   2632 C CA    . ALA C 1 28  ? -1.432  19.050  33.601 1.00 20.27 ?  28  ALA C CA    1 
ATOM   2633 C C     . ALA C 1 28  ? -2.130  19.859  34.692 1.00 19.74 ?  28  ALA C C     1 
ATOM   2634 O O     . ALA C 1 28  ? -1.564  20.793  35.268 1.00 19.00 ?  28  ALA C O     1 
ATOM   2635 C CB    . ALA C 1 28  ? -0.780  17.818  34.230 1.00 18.99 ?  28  ALA C CB    1 
ATOM   2636 N N     . ASP C 1 29  ? -3.386  19.485  34.969 1.00 20.96 ?  29  ASP C N     1 
ATOM   2637 C CA    . ASP C 1 29  ? -4.077  20.001  36.149 1.00 21.19 ?  29  ASP C CA    1 
ATOM   2638 C C     . ASP C 1 29  ? -3.418  19.504  37.427 1.00 21.44 ?  29  ASP C C     1 
ATOM   2639 O O     . ASP C 1 29  ? -3.272  20.257  38.395 1.00 20.86 ?  29  ASP C O     1 
ATOM   2640 C CB    . ASP C 1 29  ? -5.546  19.568  36.146 1.00 17.14 ?  29  ASP C CB    1 
ATOM   2641 C CG    . ASP C 1 29  ? -6.387  20.337  35.157 1.00 27.99 ?  29  ASP C CG    1 
ATOM   2642 O OD1   . ASP C 1 29  ? -5.926  21.384  34.656 1.00 23.85 ?  29  ASP C OD1   1 
ATOM   2643 O OD2   . ASP C 1 29  ? -7.528  19.900  34.891 1.00 28.13 -1 29  ASP C OD2   1 
ATOM   2644 N N     . ILE C 1 30  ? -3.025  18.232  37.445 1.00 21.24 ?  30  ILE C N     1 
ATOM   2645 C CA    . ILE C 1 30  ? -2.521  17.566  38.638 1.00 24.47 ?  30  ILE C CA    1 
ATOM   2646 C C     . ILE C 1 30  ? -1.606  16.441  38.181 1.00 24.45 ?  30  ILE C C     1 
ATOM   2647 O O     . ILE C 1 30  ? -1.805  15.850  37.117 1.00 21.19 ?  30  ILE C O     1 
ATOM   2648 C CB    . ILE C 1 30  ? -3.690  17.042  39.510 1.00 21.52 ?  30  ILE C CB    1 
ATOM   2649 C CG1   . ILE C 1 30  ? -3.195  16.506  40.854 1.00 18.55 ?  30  ILE C CG1   1 
ATOM   2650 C CG2   . ILE C 1 30  ? -4.499  15.991  38.760 1.00 17.87 ?  30  ILE C CG2   1 
ATOM   2651 C CD1   . ILE C 1 30  ? -4.291  16.410  41.900 1.00 26.63 ?  30  ILE C CD1   1 
ATOM   2652 N N     . VAL C 1 31  ? -0.586  16.152  38.982 1.00 17.91 ?  31  VAL C N     1 
ATOM   2653 C CA    . VAL C 1 31  ? 0.372   15.097  38.671 1.00 17.17 ?  31  VAL C CA    1 
ATOM   2654 C C     . VAL C 1 31  ? 0.456   14.141  39.850 1.00 21.08 ?  31  VAL C C     1 
ATOM   2655 O O     . VAL C 1 31  ? 0.556   14.573  41.004 1.00 19.32 ?  31  VAL C O     1 
ATOM   2656 C CB    . VAL C 1 31  ? 1.768   15.660  38.336 1.00 17.35 ?  31  VAL C CB    1 
ATOM   2657 C CG1   . VAL C 1 31  ? 2.714   14.530  37.945 1.00 14.41 ?  31  VAL C CG1   1 
ATOM   2658 C CG2   . VAL C 1 31  ? 1.676   16.684  37.215 1.00 15.68 ?  31  VAL C CG2   1 
ATOM   2659 N N     . PHE C 1 32  ? 0.400   12.846  39.561 1.00 20.37 ?  32  PHE C N     1 
ATOM   2660 C CA    . PHE C 1 32  ? 0.691   11.799  40.531 1.00 23.91 ?  32  PHE C CA    1 
ATOM   2661 C C     . PHE C 1 32  ? 2.047   11.202  40.181 1.00 21.12 ?  32  PHE C C     1 
ATOM   2662 O O     . PHE C 1 32  ? 2.238   10.693  39.072 1.00 21.61 ?  32  PHE C O     1 
ATOM   2663 C CB    . PHE C 1 32  ? -0.404  10.733  40.535 1.00 21.07 ?  32  PHE C CB    1 
ATOM   2664 C CG    . PHE C 1 32  ? -1.725  11.231  41.054 1.00 19.91 ?  32  PHE C CG    1 
ATOM   2665 C CD1   . PHE C 1 32  ? -2.574  11.961  40.240 1.00 19.27 ?  32  PHE C CD1   1 
ATOM   2666 C CD2   . PHE C 1 32  ? -2.107  10.984  42.362 1.00 21.62 ?  32  PHE C CD2   1 
ATOM   2667 C CE1   . PHE C 1 32  ? -3.786  12.426  40.717 1.00 21.78 ?  32  PHE C CE1   1 
ATOM   2668 C CE2   . PHE C 1 32  ? -3.317  11.445  42.846 1.00 19.09 ?  32  PHE C CE2   1 
ATOM   2669 C CZ    . PHE C 1 32  ? -4.157  12.167  42.022 1.00 24.76 ?  32  PHE C CZ    1 
ATOM   2670 N N     . SER C 1 33  ? 2.985   11.274  41.117 1.00 18.45 ?  33  SER C N     1 
ATOM   2671 C CA    . SER C 1 33  ? 4.379   10.942  40.866 1.00 20.80 ?  33  SER C CA    1 
ATOM   2672 C C     . SER C 1 33  ? 4.797   9.661   41.576 1.00 21.64 ?  33  SER C C     1 
ATOM   2673 O O     . SER C 1 33  ? 4.224   9.265   42.594 1.00 20.34 ?  33  SER C O     1 
ATOM   2674 C CB    . SER C 1 33  ? 5.298   12.081  41.318 1.00 20.32 ?  33  SER C CB    1 
ATOM   2675 O OG    . SER C 1 33  ? 5.091   12.392  42.683 1.00 19.27 ?  33  SER C OG    1 
ATOM   2676 N N     . LEU C 1 34  ? 5.827   9.021   41.018 1.00 21.79 ?  34  LEU C N     1 
ATOM   2677 C CA    . LEU C 1 34  ? 6.545   7.933   41.690 1.00 20.84 ?  34  LEU C CA    1 
ATOM   2678 C C     . LEU C 1 34  ? 7.970   7.962   41.132 1.00 22.32 ?  34  LEU C C     1 
ATOM   2679 O O     . LEU C 1 34  ? 8.255   7.369   40.092 1.00 20.73 ?  34  LEU C O     1 
ATOM   2680 C CB    . LEU C 1 34  ? 5.872   6.582   41.479 1.00 18.55 ?  34  LEU C CB    1 
ATOM   2681 C CG    . LEU C 1 34  ? 6.206   5.415   42.419 1.00 25.93 ?  34  LEU C CG    1 
ATOM   2682 C CD1   . LEU C 1 34  ? 7.675   4.992   42.383 1.00 36.75 ?  34  LEU C CD1   1 
ATOM   2683 C CD2   . LEU C 1 34  ? 5.796   5.763   43.842 1.00 24.63 ?  34  LEU C CD2   1 
ATOM   2684 N N     . LEU C 1 35  ? 8.851   8.660   41.832 1.00 20.52 ?  35  LEU C N     1 
ATOM   2685 C CA    . LEU C 1 35  ? 10.174  9.007   41.343 1.00 22.83 ?  35  LEU C CA    1 
ATOM   2686 C C     . LEU C 1 35  ? 11.249  8.363   42.215 1.00 24.98 ?  35  LEU C C     1 
ATOM   2687 O O     . LEU C 1 35  ? 10.991  8.001   43.369 1.00 24.37 ?  35  LEU C O     1 
ATOM   2688 C CB    . LEU C 1 35  ? 10.344  10.534  41.324 1.00 26.11 ?  35  LEU C CB    1 
ATOM   2689 C CG    . LEU C 1 35  ? 9.333   11.247  40.421 1.00 25.55 ?  35  LEU C CG    1 
ATOM   2690 C CD1   . LEU C 1 35  ? 9.536   12.752  40.460 1.00 23.62 ?  35  LEU C CD1   1 
ATOM   2691 C CD2   . LEU C 1 35  ? 9.415   10.719  38.994 1.00 26.03 ?  35  LEU C CD2   1 
ATOM   2692 N N     . PRO C 1 36  ? 12.470  8.205   41.692 1.00 21.07 ?  36  PRO C N     1 
ATOM   2693 C CA    . PRO C 1 36  ? 13.487  7.434   42.430 1.00 27.85 ?  36  PRO C CA    1 
ATOM   2694 C C     . PRO C 1 36  ? 14.032  8.121   43.672 1.00 25.77 ?  36  PRO C C     1 
ATOM   2695 O O     . PRO C 1 36  ? 14.523  7.420   44.566 1.00 21.62 ?  36  PRO C O     1 
ATOM   2696 C CB    . PRO C 1 36  ? 14.596  7.221   41.385 1.00 19.09 ?  36  PRO C CB    1 
ATOM   2697 C CG    . PRO C 1 36  ? 13.947  7.523   40.061 1.00 26.05 ?  36  PRO C CG    1 
ATOM   2698 C CD    . PRO C 1 36  ? 12.971  8.605   40.370 1.00 20.13 ?  36  PRO C CD    1 
ATOM   2699 N N     . ASP C 1 37  ? 13.967  9.446   43.772 1.00 23.95 ?  37  ASP C N     1 
ATOM   2700 C CA    . ASP C 1 37  ? 14.653  10.136  44.857 1.00 24.14 ?  37  ASP C CA    1 
ATOM   2701 C C     . ASP C 1 37  ? 14.083  11.539  45.022 1.00 25.74 ?  37  ASP C C     1 
ATOM   2702 O O     . ASP C 1 37  ? 13.130  11.933  44.344 1.00 20.17 ?  37  ASP C O     1 
ATOM   2703 C CB    . ASP C 1 37  ? 16.162  10.182  44.597 1.00 25.12 ?  37  ASP C CB    1 
ATOM   2704 C CG    . ASP C 1 37  ? 16.506  10.791  43.249 1.00 24.10 ?  37  ASP C CG    1 
ATOM   2705 O OD1   . ASP C 1 37  ? 16.065  11.928  42.965 1.00 26.06 ?  37  ASP C OD1   1 
ATOM   2706 O OD2   . ASP C 1 37  ? 17.226  10.135  42.465 1.00 20.90 -1 37  ASP C OD2   1 
ATOM   2707 N N     . GLY C 1 38  ? 14.689  12.294  45.946 1.00 18.05 ?  38  GLY C N     1 
ATOM   2708 C CA    . GLY C 1 38  ? 14.232  13.637  46.251 1.00 17.86 ?  38  GLY C CA    1 
ATOM   2709 C C     . GLY C 1 38  ? 14.711  14.693  45.284 1.00 20.63 ?  38  GLY C C     1 
ATOM   2710 O O     . GLY C 1 38  ? 14.073  15.745  45.170 1.00 19.49 ?  38  GLY C O     1 
ATOM   2711 N N     . PHE C 1 39  ? 15.825  14.439  44.593 1.00 18.22 ?  39  PHE C N     1 
ATOM   2712 C CA    . PHE C 1 39  ? 16.267  15.353  43.545 1.00 19.92 ?  39  PHE C CA    1 
ATOM   2713 C C     . PHE C 1 39  ? 15.278  15.342  42.388 1.00 19.98 ?  39  PHE C C     1 
ATOM   2714 O O     . PHE C 1 39  ? 14.900  16.396  41.861 1.00 20.36 ?  39  PHE C O     1 
ATOM   2715 C CB    . PHE C 1 39  ? 17.657  14.962  43.043 1.00 20.69 ?  39  PHE C CB    1 
ATOM   2716 C CG    . PHE C 1 39  ? 18.755  15.153  44.050 1.00 25.83 ?  39  PHE C CG    1 
ATOM   2717 C CD1   . PHE C 1 39  ? 19.247  16.416  44.338 1.00 19.70 ?  39  PHE C CD1   1 
ATOM   2718 C CD2   . PHE C 1 39  ? 19.312  14.061  44.695 1.00 20.94 ?  39  PHE C CD2   1 
ATOM   2719 C CE1   . PHE C 1 39  ? 20.264  16.586  45.263 1.00 25.11 ?  39  PHE C CE1   1 
ATOM   2720 C CE2   . PHE C 1 39  ? 20.327  14.224  45.619 1.00 24.03 ?  39  PHE C CE2   1 
ATOM   2721 C CZ    . PHE C 1 39  ? 20.803  15.487  45.903 1.00 25.34 ?  39  PHE C CZ    1 
ATOM   2722 N N     . SER C 1 40  ? 14.852  14.143  41.983 1.00 16.13 ?  40  SER C N     1 
ATOM   2723 C CA    . SER C 1 40  ? 13.846  14.007  40.935 1.00 24.87 ?  40  SER C CA    1 
ATOM   2724 C C     . SER C 1 40  ? 12.529  14.640  41.356 1.00 22.17 ?  40  SER C C     1 
ATOM   2725 O O     . SER C 1 40  ? 11.806  15.201  40.524 1.00 23.33 ?  40  SER C O     1 
ATOM   2726 C CB    . SER C 1 40  ? 13.649  12.529  40.594 1.00 22.63 ?  40  SER C CB    1 
ATOM   2727 O OG    . SER C 1 40  ? 12.994  12.369  39.349 1.00 37.47 ?  40  SER C OG    1 
ATOM   2728 N N     . GLN C 1 41  ? 12.201  14.562  42.648 1.00 25.44 ?  41  GLN C N     1 
ATOM   2729 C CA    . GLN C 1 41  ? 10.923  15.084  43.118 1.00 24.35 ?  41  GLN C CA    1 
ATOM   2730 C C     . GLN C 1 41  ? 10.925  16.607  43.123 1.00 21.26 ?  41  GLN C C     1 
ATOM   2731 O O     . GLN C 1 41  ? 9.904   17.238  42.814 1.00 21.94 ?  41  GLN C O     1 
ATOM   2732 C CB    . GLN C 1 41  ? 10.621  14.538  44.514 1.00 24.90 ?  41  GLN C CB    1 
ATOM   2733 C CG    . GLN C 1 41  ? 9.164   14.649  44.935 1.00 26.56 ?  41  GLN C CG    1 
ATOM   2734 C CD    . GLN C 1 41  ? 8.276   13.657  44.206 1.00 26.05 ?  41  GLN C CD    1 
ATOM   2735 O OE1   . GLN C 1 41  ? 8.633   12.490  44.043 1.00 24.32 ?  41  GLN C OE1   1 
ATOM   2736 N NE2   . GLN C 1 41  ? 7.107   14.116  43.773 1.00 22.50 ?  41  GLN C NE2   1 
ATOM   2737 N N     A ARG C 1 42  ? 12.060  17.213  43.486 0.52 20.67 ?  42  ARG C N     1 
ATOM   2738 N N     B ARG C 1 42  ? 12.066  17.218  43.451 0.48 20.64 ?  42  ARG C N     1 
ATOM   2739 C CA    A ARG C 1 42  ? 12.191  18.665  43.424 0.52 20.93 ?  42  ARG C CA    1 
ATOM   2740 C CA    B ARG C 1 42  ? 12.155  18.673  43.423 0.48 20.78 ?  42  ARG C CA    1 
ATOM   2741 C C     A ARG C 1 42  ? 12.036  19.160  41.992 0.52 22.47 ?  42  ARG C C     1 
ATOM   2742 C C     B ARG C 1 42  ? 12.080  19.199  41.993 0.48 22.36 ?  42  ARG C C     1 
ATOM   2743 O O     A ARG C 1 42  ? 11.327  20.140  41.731 0.52 20.86 ?  42  ARG C O     1 
ATOM   2744 O O     B ARG C 1 42  ? 11.457  20.237  41.737 0.48 20.96 ?  42  ARG C O     1 
ATOM   2745 C CB    A ARG C 1 42  ? 13.548  19.092  43.989 0.52 18.68 ?  42  ARG C CB    1 
ATOM   2746 C CB    B ARG C 1 42  ? 13.445  19.127  44.111 0.48 18.82 ?  42  ARG C CB    1 
ATOM   2747 C CG    A ARG C 1 42  ? 13.613  19.211  45.504 0.52 20.21 ?  42  ARG C CG    1 
ATOM   2748 C CG    B ARG C 1 42  ? 13.448  18.853  45.608 0.48 19.92 ?  42  ARG C CG    1 
ATOM   2749 C CD    A ARG C 1 42  ? 14.989  19.713  45.931 0.52 23.16 ?  42  ARG C CD    1 
ATOM   2750 C CD    B ARG C 1 42  ? 14.565  19.591  46.336 0.48 24.43 ?  42  ARG C CD    1 
ATOM   2751 N NE    A ARG C 1 42  ? 15.011  20.206  47.303 0.52 20.70 ?  42  ARG C NE    1 
ATOM   2752 N NE    B ARG C 1 42  ? 15.812  18.834  46.410 0.48 24.79 ?  42  ARG C NE    1 
ATOM   2753 C CZ    A ARG C 1 42  ? 15.663  19.615  48.298 0.52 27.11 ?  42  ARG C CZ    1 
ATOM   2754 C CZ    B ARG C 1 42  ? 15.975  17.694  47.072 0.48 22.88 ?  42  ARG C CZ    1 
ATOM   2755 N NH1   A ARG C 1 42  ? 16.347  18.496  48.110 0.52 26.60 ?  42  ARG C NH1   1 
ATOM   2756 N NH1   B ARG C 1 42  ? 14.972  17.108  47.710 0.48 23.65 ?  42  ARG C NH1   1 
ATOM   2757 N NH2   A ARG C 1 42  ? 15.630  20.159  49.511 0.52 25.06 ?  42  ARG C NH2   1 
ATOM   2758 N NH2   B ARG C 1 42  ? 17.178  17.127  47.100 0.48 23.18 ?  42  ARG C NH2   1 
ATOM   2759 N N     . TRP C 1 43  ? 12.706  18.491  41.049 1.00 21.98 ?  43  TRP C N     1 
ATOM   2760 C CA    . TRP C 1 43  ? 12.610  18.871  39.642 1.00 22.15 ?  43  TRP C CA    1 
ATOM   2761 C C     . TRP C 1 43  ? 11.170  18.834  39.155 1.00 22.02 ?  43  TRP C C     1 
ATOM   2762 O O     . TRP C 1 43  ? 10.730  19.727  38.421 1.00 19.12 ?  43  TRP C O     1 
ATOM   2763 C CB    . TRP C 1 43  ? 13.482  17.945  38.794 1.00 16.07 ?  43  TRP C CB    1 
ATOM   2764 C CG    . TRP C 1 43  ? 13.077  17.863  37.350 1.00 14.84 ?  43  TRP C CG    1 
ATOM   2765 C CD1   . TRP C 1 43  ? 13.468  18.693  36.340 1.00 15.09 ?  43  TRP C CD1   1 
ATOM   2766 C CD2   . TRP C 1 43  ? 12.203  16.894  36.757 1.00 17.81 ?  43  TRP C CD2   1 
ATOM   2767 N NE1   . TRP C 1 43  ? 12.892  18.301  35.154 1.00 13.82 ?  43  TRP C NE1   1 
ATOM   2768 C CE2   . TRP C 1 43  ? 12.110  17.199  35.385 1.00 19.75 ?  43  TRP C CE2   1 
ATOM   2769 C CE3   . TRP C 1 43  ? 11.490  15.798  37.254 1.00 15.15 ?  43  TRP C CE3   1 
ATOM   2770 C CZ2   . TRP C 1 43  ? 11.333  16.448  34.504 1.00 15.20 ?  43  TRP C CZ2   1 
ATOM   2771 C CZ3   . TRP C 1 43  ? 10.720  15.055  36.379 1.00 21.59 ?  43  TRP C CZ3   1 
ATOM   2772 C CH2   . TRP C 1 43  ? 10.647  15.383  35.019 1.00 21.62 ?  43  TRP C CH2   1 
ATOM   2773 N N     . LEU C 1 44  ? 10.423  17.802  39.550 1.00 21.38 ?  44  LEU C N     1 
ATOM   2774 C CA    . LEU C 1 44  ? 9.038   17.685  39.115 1.00 19.85 ?  44  LEU C CA    1 
ATOM   2775 C C     . LEU C 1 44  ? 8.191   18.816  39.680 1.00 19.52 ?  44  LEU C C     1 
ATOM   2776 O O     . LEU C 1 44  ? 7.337   19.372  38.977 1.00 18.51 ?  44  LEU C O     1 
ATOM   2777 C CB    . LEU C 1 44  ? 8.467   16.336  39.542 1.00 20.51 ?  44  LEU C CB    1 
ATOM   2778 C CG    . LEU C 1 44  ? 6.974   16.191  39.261 1.00 18.33 ?  44  LEU C CG    1 
ATOM   2779 C CD1   . LEU C 1 44  ? 6.702   16.314  37.770 1.00 24.57 ?  44  LEU C CD1   1 
ATOM   2780 C CD2   . LEU C 1 44  ? 6.460   14.882  39.795 1.00 18.43 ?  44  LEU C CD2   1 
ATOM   2781 N N     . THR C 1 45  ? 8.413   19.167  40.949 1.00 22.00 ?  45  THR C N     1 
ATOM   2782 C CA    . THR C 1 45  ? 7.568   20.161  41.598 1.00 25.68 ?  45  THR C CA    1 
ATOM   2783 C C     . THR C 1 45  ? 7.809   21.554  41.033 1.00 24.11 ?  45  THR C C     1 
ATOM   2784 O O     . THR C 1 45  ? 6.904   22.396  41.058 1.00 24.54 ?  45  THR C O     1 
ATOM   2785 C CB    . THR C 1 45  ? 7.805   20.141  43.105 1.00 27.50 ?  45  THR C CB    1 
ATOM   2786 O OG1   . THR C 1 45  ? 7.984   18.786  43.536 1.00 34.13 ?  45  THR C OG1   1 
ATOM   2787 C CG2   . THR C 1 45  ? 6.620   20.739  43.841 1.00 30.69 ?  45  THR C CG2   1 
ATOM   2788 N N     . LYS C 1 46  ? 9.016   21.816  40.521 1.00 26.58 ?  46  LYS C N     1 
ATOM   2789 C CA    . LYS C 1 46  ? 9.258   23.078  39.832 1.00 23.13 ?  46  LYS C CA    1 
ATOM   2790 C C     . LYS C 1 46  ? 8.564   23.096  38.478 1.00 27.49 ?  46  LYS C C     1 
ATOM   2791 O O     . LYS C 1 46  ? 8.115   24.154  38.020 1.00 30.11 ?  46  LYS C O     1 
ATOM   2792 C CB    . LYS C 1 46  ? 10.760  23.313  39.663 1.00 27.34 ?  46  LYS C CB    1 
ATOM   2793 C CG    . LYS C 1 46  ? 11.491  23.647  40.958 1.00 33.32 ?  46  LYS C CG    1 
ATOM   2794 C CD    . LYS C 1 46  ? 12.763  24.459  40.718 1.00 37.45 ?  46  LYS C CD    1 
ATOM   2795 C CE    . LYS C 1 46  ? 13.939  23.598  40.271 1.00 41.99 ?  46  LYS C CE    1 
ATOM   2796 N NZ    . LYS C 1 46  ? 13.836  23.097  38.869 1.00 40.96 ?  46  LYS C NZ    1 
ATOM   2797 N N     . LEU C 1 47  ? 8.475   21.932  37.828 1.00 23.60 ?  47  LEU C N     1 
ATOM   2798 C CA    . LEU C 1 47  ? 7.757   21.819  36.562 1.00 24.17 ?  47  LEU C CA    1 
ATOM   2799 C C     . LEU C 1 47  ? 6.269   22.090  36.749 1.00 25.77 ?  47  LEU C C     1 
ATOM   2800 O O     . LEU C 1 47  ? 5.653   22.805  35.949 1.00 27.05 ?  47  LEU C O     1 
ATOM   2801 C CB    . LEU C 1 47  ? 7.978   20.426  35.974 1.00 22.38 ?  47  LEU C CB    1 
ATOM   2802 C CG    . LEU C 1 47  ? 8.660   20.317  34.614 1.00 27.11 ?  47  LEU C CG    1 
ATOM   2803 C CD1   . LEU C 1 47  ? 8.587   18.885  34.116 1.00 23.97 ?  47  LEU C CD1   1 
ATOM   2804 C CD2   . LEU C 1 47  ? 8.023   21.270  33.618 1.00 30.37 ?  47  LEU C CD2   1 
ATOM   2805 N N     . ASN C 1 48  ? 5.679   21.520  37.796 1.00 21.77 ?  48  ASN C N     1 
ATOM   2806 C CA    . ASN C 1 48  ? 4.257   21.626  38.091 1.00 20.79 ?  48  ASN C CA    1 
ATOM   2807 C C     . ASN C 1 48  ? 4.088   21.428  39.591 1.00 21.73 ?  48  ASN C C     1 
ATOM   2808 O O     . ASN C 1 48  ? 4.353   20.335  40.101 1.00 22.83 ?  48  ASN C O     1 
ATOM   2809 C CB    . ASN C 1 48  ? 3.457   20.588  37.295 1.00 21.83 ?  48  ASN C CB    1 
ATOM   2810 C CG    . ASN C 1 48  ? 1.951   20.773  37.421 1.00 22.46 ?  48  ASN C CG    1 
ATOM   2811 O OD1   . ASN C 1 48  ? 1.436   21.140  38.477 1.00 20.32 ?  48  ASN C OD1   1 
ATOM   2812 N ND2   . ASN C 1 48  ? 1.236   20.507  36.332 1.00 16.93 ?  48  ASN C ND2   1 
ATOM   2813 N N     . PRO C 1 49  ? 3.665   22.453  40.336 1.00 22.86 ?  49  PRO C N     1 
ATOM   2814 C CA    . PRO C 1 49  ? 3.610   22.324  41.801 1.00 26.73 ?  49  PRO C CA    1 
ATOM   2815 C C     . PRO C 1 49  ? 2.459   21.471  42.310 1.00 25.14 ?  49  PRO C C     1 
ATOM   2816 O O     . PRO C 1 49  ? 2.430   21.162  43.508 1.00 25.76 ?  49  PRO C O     1 
ATOM   2817 C CB    . PRO C 1 49  ? 3.473   23.779  42.267 1.00 27.74 ?  49  PRO C CB    1 
ATOM   2818 C CG    . PRO C 1 49  ? 2.707   24.429  41.158 1.00 24.23 ?  49  PRO C CG    1 
ATOM   2819 C CD    . PRO C 1 49  ? 3.213   23.782  39.884 1.00 24.90 ?  49  PRO C CD    1 
ATOM   2820 N N     . ASN C 1 50  ? 1.517   21.075  41.452 1.00 26.12 ?  50  ASN C N     1 
ATOM   2821 C CA    . ASN C 1 50  ? 0.362   20.288  41.885 1.00 26.41 ?  50  ASN C CA    1 
ATOM   2822 C C     . ASN C 1 50  ? 0.694   18.807  41.737 1.00 23.08 ?  50  ASN C C     1 
ATOM   2823 O O     . ASN C 1 50  ? 0.250   18.121  40.819 1.00 22.52 ?  50  ASN C O     1 
ATOM   2824 C CB    . ASN C 1 50  ? -0.883  20.667  41.095 1.00 26.46 ?  50  ASN C CB    1 
ATOM   2825 C CG    . ASN C 1 50  ? -2.158  20.157  41.743 1.00 24.56 ?  50  ASN C CG    1 
ATOM   2826 O OD1   . ASN C 1 50  ? -2.136  19.628  42.855 1.00 28.28 ?  50  ASN C OD1   1 
ATOM   2827 N ND2   . ASN C 1 50  ? -3.279  20.313  41.047 1.00 23.42 ?  50  ASN C ND2   1 
ATOM   2828 N N     . VAL C 1 51  ? 1.491   18.310  42.676 1.00 21.92 ?  51  VAL C N     1 
ATOM   2829 C CA    . VAL C 1 51  ? 1.953   16.928  42.673 1.00 22.71 ?  51  VAL C CA    1 
ATOM   2830 C C     . VAL C 1 51  ? 1.389   16.214  43.892 1.00 19.67 ?  51  VAL C C     1 
ATOM   2831 O O     . VAL C 1 51  ? 1.387   16.758  45.002 1.00 19.66 ?  51  VAL C O     1 
ATOM   2832 C CB    . VAL C 1 51  ? 3.495   16.834  42.663 1.00 24.02 ?  51  VAL C CB    1 
ATOM   2833 C CG1   . VAL C 1 51  ? 3.940   15.382  42.663 1.00 21.32 ?  51  VAL C CG1   1 
ATOM   2834 C CG2   . VAL C 1 51  ? 4.057   17.552  41.454 1.00 21.10 ?  51  VAL C CG2   1 
ATOM   2835 N N     . ILE C 1 52  ? 0.899   14.998  43.679 1.00 21.81 ?  52  ILE C N     1 
ATOM   2836 C CA    . ILE C 1 52  ? 0.549   14.075  44.752 1.00 25.62 ?  52  ILE C CA    1 
ATOM   2837 C C     . ILE C 1 52  ? 1.484   12.879  44.649 1.00 22.69 ?  52  ILE C C     1 
ATOM   2838 O O     . ILE C 1 52  ? 1.479   12.165  43.638 1.00 20.32 ?  52  ILE C O     1 
ATOM   2839 C CB    . ILE C 1 52  ? -0.922  13.640  44.678 1.00 24.09 ?  52  ILE C CB    1 
ATOM   2840 C CG1   . ILE C 1 52  ? -1.828  14.866  44.807 1.00 21.57 ?  52  ILE C CG1   1 
ATOM   2841 C CG2   . ILE C 1 52  ? -1.234  12.612  45.756 1.00 24.38 ?  52  ILE C CG2   1 
ATOM   2842 C CD1   . ILE C 1 52  ? -1.952  15.361  46.227 1.00 33.20 ?  52  ILE C CD1   1 
ATOM   2843 N N     . ASN C 1 53  ? 2.285   12.664  45.689 1.00 21.25 ?  53  ASN C N     1 
ATOM   2844 C CA    . ASN C 1 53  ? 3.291   11.609  45.685 1.00 21.25 ?  53  ASN C CA    1 
ATOM   2845 C C     . ASN C 1 53  ? 2.653   10.257  45.988 1.00 20.57 ?  53  ASN C C     1 
ATOM   2846 O O     . ASN C 1 53  ? 2.138   10.037  47.091 1.00 19.08 ?  53  ASN C O     1 
ATOM   2847 C CB    . ASN C 1 53  ? 4.391   11.916  46.699 1.00 23.33 ?  53  ASN C CB    1 
ATOM   2848 C CG    . ASN C 1 53  ? 5.651   11.112  46.449 1.00 23.11 ?  53  ASN C CG    1 
ATOM   2849 O OD1   . ASN C 1 53  ? 5.619   10.076  45.788 1.00 23.99 ?  53  ASN C OD1   1 
ATOM   2850 N ND2   . ASN C 1 53  ? 6.772   11.590  46.978 1.00 27.39 ?  53  ASN C ND2   1 
ATOM   2851 N N     . LEU C 1 54  ? 2.696   9.347   45.011 1.00 21.30 ?  54  LEU C N     1 
ATOM   2852 C CA    . LEU C 1 54  ? 2.176   8.000   45.209 1.00 19.43 ?  54  LEU C CA    1 
ATOM   2853 C C     . LEU C 1 54  ? 2.981   7.197   46.225 1.00 20.68 ?  54  LEU C C     1 
ATOM   2854 O O     . LEU C 1 54  ? 2.521   6.125   46.641 1.00 16.75 ?  54  LEU C O     1 
ATOM   2855 C CB    . LEU C 1 54  ? 2.134   7.253   43.873 1.00 18.58 ?  54  LEU C CB    1 
ATOM   2856 C CG    . LEU C 1 54  ? 1.302   7.916   42.770 1.00 20.46 ?  54  LEU C CG    1 
ATOM   2857 C CD1   . LEU C 1 54  ? 1.241   7.034   41.531 1.00 11.22 ?  54  LEU C CD1   1 
ATOM   2858 C CD2   . LEU C 1 54  ? -0.094  8.233   43.280 1.00 18.00 ?  54  LEU C CD2   1 
ATOM   2859 N N     . GLN C 1 55  ? 4.169   7.675   46.619 1.00 24.31 ?  55  GLN C N     1 
ATOM   2860 C CA    . GLN C 1 55  ? 4.962   6.965   47.619 1.00 33.79 ?  55  GLN C CA    1 
ATOM   2861 C C     . GLN C 1 55  ? 4.196   6.787   48.925 1.00 24.42 ?  55  GLN C C     1 
ATOM   2862 O O     . GLN C 1 55  ? 4.408   5.797   49.636 1.00 22.63 ?  55  GLN C O     1 
ATOM   2863 C CB    . GLN C 1 55  ? 6.274   7.708   47.873 1.00 25.77 ?  55  GLN C CB    1 
ATOM   2864 C CG    . GLN C 1 55  ? 7.520   6.835   47.780 1.00 36.99 ?  55  GLN C CG    1 
ATOM   2865 C CD    . GLN C 1 55  ? 7.904   6.212   49.111 1.00 54.43 ?  55  GLN C CD    1 
ATOM   2866 O OE1   . GLN C 1 55  ? 7.607   6.758   50.172 1.00 66.29 ?  55  GLN C OE1   1 
ATOM   2867 N NE2   . GLN C 1 55  ? 8.581   5.069   49.057 1.00 51.14 ?  55  GLN C NE2   1 
ATOM   2868 N N     . GLN C 1 56  ? 3.308   7.732   49.255 1.00 22.06 ?  56  GLN C N     1 
ATOM   2869 C CA    . GLN C 1 56  ? 2.598   7.701   50.531 1.00 29.66 ?  56  GLN C CA    1 
ATOM   2870 C C     . GLN C 1 56  ? 1.803   6.421   50.727 1.00 29.53 ?  56  GLN C C     1 
ATOM   2871 O O     . GLN C 1 56  ? 1.532   6.044   51.872 1.00 30.16 ?  56  GLN C O     1 
ATOM   2872 C CB    . GLN C 1 56  ? 1.653   8.899   50.639 1.00 29.65 ?  56  GLN C CB    1 
ATOM   2873 C CG    . GLN C 1 56  ? 0.500   8.849   49.652 1.00 27.58 ?  56  GLN C CG    1 
ATOM   2874 C CD    . GLN C 1 56  ? -0.398  10.064  49.728 1.00 32.25 ?  56  GLN C CD    1 
ATOM   2875 O OE1   . GLN C 1 56  ? -1.359  10.093  50.498 1.00 38.04 ?  56  GLN C OE1   1 
ATOM   2876 N NE2   . GLN C 1 56  ? -0.095  11.075  48.924 1.00 28.67 ?  56  GLN C NE2   1 
ATOM   2877 N N     . PHE C 1 57  ? 1.418   5.751   49.646 1.00 33.47 ?  57  PHE C N     1 
ATOM   2878 C CA    . PHE C 1 57  ? 0.544   4.592   49.733 1.00 35.58 ?  57  PHE C CA    1 
ATOM   2879 C C     . PHE C 1 57  ? 1.310   3.302   49.983 1.00 36.30 ?  57  PHE C C     1 
ATOM   2880 O O     . PHE C 1 57  ? 0.686   2.249   50.146 1.00 27.48 ?  57  PHE C O     1 
ATOM   2881 C CB    . PHE C 1 57  ? -0.300  4.471   48.459 1.00 26.72 ?  57  PHE C CB    1 
ATOM   2882 C CG    . PHE C 1 57  ? -1.184  5.659   48.207 1.00 30.20 ?  57  PHE C CG    1 
ATOM   2883 C CD1   . PHE C 1 57  ? -2.374  5.813   48.899 1.00 25.98 ?  57  PHE C CD1   1 
ATOM   2884 C CD2   . PHE C 1 57  ? -0.822  6.627   47.282 1.00 32.39 ?  57  PHE C CD2   1 
ATOM   2885 C CE1   . PHE C 1 57  ? -3.187  6.910   48.674 1.00 27.20 ?  57  PHE C CE1   1 
ATOM   2886 C CE2   . PHE C 1 57  ? -1.633  7.725   47.053 1.00 24.90 ?  57  PHE C CE2   1 
ATOM   2887 C CZ    . PHE C 1 57  ? -2.815  7.865   47.750 1.00 31.25 ?  57  PHE C CZ    1 
ATOM   2888 N N     . TYR C 1 58  ? 2.638   3.360   50.023 1.00 34.12 ?  58  TYR C N     1 
ATOM   2889 C CA    . TYR C 1 58  ? 3.419   2.189   50.369 1.00 38.12 ?  58  TYR C CA    1 
ATOM   2890 C C     . TYR C 1 58  ? 3.350   1.955   51.874 1.00 38.17 ?  58  TYR C C     1 
ATOM   2891 O O     . TYR C 1 58  ? 3.001   2.846   52.649 1.00 37.91 ?  58  TYR C O     1 
ATOM   2892 C CB    . TYR C 1 58  ? 4.874   2.352   49.928 1.00 40.72 ?  58  TYR C CB    1 
ATOM   2893 C CG    . TYR C 1 58  ? 5.152   1.887   48.517 1.00 35.50 ?  58  TYR C CG    1 
ATOM   2894 C CD1   . TYR C 1 58  ? 5.071   0.543   48.182 1.00 34.09 ?  58  TYR C CD1   1 
ATOM   2895 C CD2   . TYR C 1 58  ? 5.502   2.791   47.523 1.00 37.82 ?  58  TYR C CD2   1 
ATOM   2896 C CE1   . TYR C 1 58  ? 5.324   0.112   46.894 1.00 41.42 ?  58  TYR C CE1   1 
ATOM   2897 C CE2   . TYR C 1 58  ? 5.760   2.369   46.232 1.00 39.43 ?  58  TYR C CE2   1 
ATOM   2898 C CZ    . TYR C 1 58  ? 5.667   1.028   45.925 1.00 40.56 ?  58  TYR C CZ    1 
ATOM   2899 O OH    . TYR C 1 58  ? 5.920   0.601   44.642 1.00 42.45 ?  58  TYR C OH    1 
ATOM   2900 N N     . ALA C 1 59  ? 3.670   0.731   52.280 1.00 42.82 ?  59  ALA C N     1 
ATOM   2901 C CA    . ALA C 1 59  ? 3.634   0.383   53.696 1.00 42.98 ?  59  ALA C CA    1 
ATOM   2902 C C     . ALA C 1 59  ? 4.573   1.283   54.486 1.00 44.71 ?  59  ALA C C     1 
ATOM   2903 O O     . ALA C 1 59  ? 5.756   1.408   54.160 1.00 43.05 ?  59  ALA C O     1 
ATOM   2904 C CB    . ALA C 1 59  ? 4.016   -1.085  53.894 1.00 45.65 ?  59  ALA C CB    1 
ATOM   2905 N N     . GLN C 1 60  ? 4.038   1.919   55.521 1.00 44.16 ?  60  GLN C N     1 
ATOM   2906 C CA    . GLN C 1 60  ? 4.788   2.846   56.355 1.00 55.19 ?  60  GLN C CA    1 
ATOM   2907 C C     . GLN C 1 60  ? 5.001   2.234   57.733 1.00 55.80 ?  60  GLN C C     1 
ATOM   2908 O O     . GLN C 1 60  ? 4.064   1.681   58.321 1.00 52.35 ?  60  GLN C O     1 
ATOM   2909 C CB    . GLN C 1 60  ? 4.052   4.182   56.484 1.00 52.95 ?  60  GLN C CB    1 
ATOM   2910 C CG    . GLN C 1 60  ? 3.419   4.686   55.195 1.00 51.26 ?  60  GLN C CG    1 
ATOM   2911 C CD    . GLN C 1 60  ? 4.411   5.367   54.271 1.00 47.07 ?  60  GLN C CD    1 
ATOM   2912 O OE1   . GLN C 1 60  ? 5.176   6.233   54.690 1.00 43.53 ?  60  GLN C OE1   1 
ATOM   2913 N NE2   . GLN C 1 60  ? 4.394   4.980   52.999 1.00 39.99 ?  60  GLN C NE2   1 
ATOM   2914 N N     . ASN C 1 61  ? 6.237   2.320   58.233 1.00 54.97 ?  61  ASN C N     1 
ATOM   2915 C CA    . ASN C 1 61  ? 6.545   2.088   59.642 1.00 55.22 ?  61  ASN C CA    1 
ATOM   2916 C C     . ASN C 1 61  ? 6.381   0.626   60.052 1.00 52.68 ?  61  ASN C C     1 
ATOM   2917 O O     . ASN C 1 61  ? 5.580   0.315   60.944 1.00 51.45 ?  61  ASN C O     1 
ATOM   2918 C CB    . ASN C 1 61  ? 5.662   2.992   60.517 1.00 60.68 ?  61  ASN C CB    1 
ATOM   2919 C CG    . ASN C 1 61  ? 5.807   4.462   60.166 1.00 63.81 ?  61  ASN C CG    1 
ATOM   2920 O OD1   . ASN C 1 61  ? 6.916   4.957   59.958 1.00 68.98 ?  61  ASN C OD1   1 
ATOM   2921 N ND2   . ASN C 1 61  ? 4.681   5.163   60.077 1.00 61.87 ?  61  ASN C ND2   1 
ATOM   2922 N N     . GLY C 1 62  ? 7.122   -0.275  59.397 1.00 49.14 ?  62  GLY C N     1 
ATOM   2923 C CA    . GLY C 1 62  ? 7.187   -1.676  59.779 1.00 40.24 ?  62  GLY C CA    1 
ATOM   2924 C C     . GLY C 1 62  ? 5.888   -2.433  59.600 1.00 37.02 ?  62  GLY C C     1 
ATOM   2925 O O     . GLY C 1 62  ? 5.787   -3.624  59.895 1.00 34.65 ?  62  GLY C O     1 
ATOM   2926 N N     . GLU C 1 63  ? 4.887   -1.716  59.116 1.00 41.82 ?  63  GLU C N     1 
ATOM   2927 C CA    . GLU C 1 63  ? 3.539   -2.237  58.943 1.00 38.40 ?  63  GLU C CA    1 
ATOM   2928 C C     . GLU C 1 63  ? 3.468   -3.237  57.790 1.00 37.25 ?  63  GLU C C     1 
ATOM   2929 O O     . GLU C 1 63  ? 4.071   -3.039  56.734 1.00 40.64 ?  63  GLU C O     1 
ATOM   2930 C CB    . GLU C 1 63  ? 2.617   -1.026  58.759 1.00 43.81 ?  63  GLU C CB    1 
ATOM   2931 C CG    . GLU C 1 63  ? 1.351   -1.107  57.964 1.00 47.53 ?  63  GLU C CG    1 
ATOM   2932 C CD    . GLU C 1 63  ? 1.086   0.250   57.307 1.00 56.22 ?  63  GLU C CD    1 
ATOM   2933 O OE1   . GLU C 1 63  ? 1.043   0.331   56.066 1.00 60.17 ?  63  GLU C OE1   1 
ATOM   2934 O OE2   . GLU C 1 63  ? 0.999   1.242   58.061 1.00 71.72 -1 63  GLU C OE2   1 
ATOM   2935 N N     . VAL C 1 64  ? 2.738   -4.329  58.012 1.00 31.56 ?  64  VAL C N     1 
ATOM   2936 C CA    . VAL C 1 64  ? 2.564   -5.383  57.013 1.00 33.14 ?  64  VAL C CA    1 
ATOM   2937 C C     . VAL C 1 64  ? 1.494   -4.966  56.014 1.00 37.96 ?  64  VAL C C     1 
ATOM   2938 O O     . VAL C 1 64  ? 0.345   -4.708  56.390 1.00 33.37 ?  64  VAL C O     1 
ATOM   2939 C CB    . VAL C 1 64  ? 2.200   -6.719  57.675 1.00 34.76 ?  64  VAL C CB    1 
ATOM   2940 C CG1   . VAL C 1 64  ? 1.698   -7.708  56.628 1.00 30.97 ?  64  VAL C CG1   1 
ATOM   2941 C CG2   . VAL C 1 64  ? 3.393   -7.289  58.419 1.00 35.17 ?  64  VAL C CG2   1 
ATOM   2942 N N     . LYS C 1 65  ? 1.861   -4.915  54.736 1.00 32.17 ?  65  LYS C N     1 
ATOM   2943 C CA    . LYS C 1 65  ? 0.919   -4.507  53.700 1.00 32.54 ?  65  LYS C CA    1 
ATOM   2944 C C     . LYS C 1 65  ? 1.264   -5.199  52.392 1.00 33.85 ?  65  LYS C C     1 
ATOM   2945 O O     . LYS C 1 65  ? 2.394   -5.082  51.903 1.00 30.72 ?  65  LYS C O     1 
ATOM   2946 C CB    . LYS C 1 65  ? 0.938   -2.990  53.525 1.00 36.30 ?  65  LYS C CB    1 
ATOM   2947 C CG    . LYS C 1 65  ? -0.150  -2.441  52.627 1.00 25.89 ?  65  LYS C CG    1 
ATOM   2948 C CD    . LYS C 1 65  ? -0.122  -0.926  52.629 1.00 32.91 ?  65  LYS C CD    1 
ATOM   2949 C CE    . LYS C 1 65  ? -1.112  -0.340  51.640 1.00 26.99 ?  65  LYS C CE    1 
ATOM   2950 N NZ    . LYS C 1 65  ? -1.392  1.093   51.937 1.00 23.25 ?  65  LYS C NZ    1 
ATOM   2951 N N     . ASN C 1 66  ? 0.294   -5.925  51.839 1.00 29.92 ?  66  ASN C N     1 
ATOM   2952 C CA    . ASN C 1 66  ? 0.443   -6.481  50.503 1.00 28.21 ?  66  ASN C CA    1 
ATOM   2953 C C     . ASN C 1 66  ? 0.652   -5.356  49.498 1.00 30.18 ?  66  ASN C C     1 
ATOM   2954 O O     . ASN C 1 66  ? -0.066  -4.351  49.518 1.00 23.59 ?  66  ASN C O     1 
ATOM   2955 C CB    . ASN C 1 66  ? -0.795  -7.296  50.131 1.00 31.59 ?  66  ASN C CB    1 
ATOM   2956 C CG    . ASN C 1 66  ? -0.532  -8.258  48.999 1.00 34.24 ?  66  ASN C CG    1 
ATOM   2957 O OD1   . ASN C 1 66  ? -0.013  -7.870  47.958 1.00 29.40 ?  66  ASN C OD1   1 
ATOM   2958 N ND2   . ASN C 1 66  ? -0.903  -9.520  49.190 1.00 24.43 ?  66  ASN C ND2   1 
ATOM   2959 N N     . ARG C 1 67  ? 1.657   -5.511  48.633 1.00 30.42 ?  67  ARG C N     1 
ATOM   2960 C CA    . ARG C 1 67  ? 1.907   -4.480  47.633 1.00 34.48 ?  67  ARG C CA    1 
ATOM   2961 C C     . ARG C 1 67  ? 0.744   -4.331  46.654 1.00 29.62 ?  67  ARG C C     1 
ATOM   2962 O O     . ARG C 1 67  ? 0.606   -3.269  46.035 1.00 30.93 ?  67  ARG C O     1 
ATOM   2963 C CB    . ARG C 1 67  ? 3.228   -4.761  46.914 1.00 34.15 ?  67  ARG C CB    1 
ATOM   2964 C CG    . ARG C 1 67  ? 4.401   -4.053  47.605 1.00 43.79 ?  67  ARG C CG    1 
ATOM   2965 C CD    . ARG C 1 67  ? 5.660   -3.974  46.753 1.00 39.73 ?  67  ARG C CD    1 
ATOM   2966 N NE    . ARG C 1 67  ? 6.272   -5.273  46.495 1.00 39.46 ?  67  ARG C NE    1 
ATOM   2967 C CZ    . ARG C 1 67  ? 6.747   -6.104  47.414 1.00 39.66 ?  67  ARG C CZ    1 
ATOM   2968 N NH1   . ARG C 1 67  ? 6.733   -5.802  48.703 1.00 36.23 ?  67  ARG C NH1   1 
ATOM   2969 N NH2   . ARG C 1 67  ? 7.258   -7.270  47.029 1.00 38.44 ?  67  ARG C NH2   1 
ATOM   2970 N N     . ARG C 1 68  ? -0.096  -5.363  46.495 1.00 30.90 ?  68  ARG C N     1 
ATOM   2971 C CA    . ARG C 1 68  ? -1.256  -5.219  45.620 1.00 32.06 ?  68  ARG C CA    1 
ATOM   2972 C C     . ARG C 1 68  ? -2.289  -4.271  46.216 1.00 28.36 ?  68  ARG C C     1 
ATOM   2973 O O     . ARG C 1 68  ? -3.044  -3.633  45.472 1.00 30.14 ?  68  ARG C O     1 
ATOM   2974 C CB    . ARG C 1 68  ? -1.888  -6.577  45.317 1.00 22.63 ?  68  ARG C CB    1 
ATOM   2975 C CG    . ARG C 1 68  ? -1.039  -7.450  44.413 1.00 38.82 ?  68  ARG C CG    1 
ATOM   2976 C CD    . ARG C 1 68  ? -0.537  -8.673  45.136 1.00 42.45 ?  68  ARG C CD    1 
ATOM   2977 N NE    . ARG C 1 68  ? -0.226  -9.770  44.230 1.00 45.71 ?  68  ARG C NE    1 
ATOM   2978 C CZ    . ARG C 1 68  ? -1.125  -10.584 43.696 1.00 42.31 ?  68  ARG C CZ    1 
ATOM   2979 N NH1   . ARG C 1 68  ? -2.417  -10.454 43.952 1.00 38.96 ?  68  ARG C NH1   1 
ATOM   2980 N NH2   . ARG C 1 68  ? -0.718  -11.564 42.893 1.00 34.81 ?  68  ARG C NH2   1 
ATOM   2981 N N     . ASP C 1 69  ? -2.351  -4.171  47.548 1.00 23.29 ?  69  ASP C N     1 
ATOM   2982 C CA    . ASP C 1 69  ? -3.228  -3.175  48.154 1.00 29.97 ?  69  ASP C CA    1 
ATOM   2983 C C     . ASP C 1 69  ? -2.653  -1.780  47.979 1.00 26.68 ?  69  ASP C C     1 
ATOM   2984 O O     . ASP C 1 69  ? -3.404  -0.811  47.824 1.00 25.96 ?  69  ASP C O     1 
ATOM   2985 C CB    . ASP C 1 69  ? -3.437  -3.476  49.638 1.00 30.19 ?  69  ASP C CB    1 
ATOM   2986 C CG    . ASP C 1 69  ? -4.146  -4.789  49.871 1.00 29.61 ?  69  ASP C CG    1 
ATOM   2987 O OD1   . ASP C 1 69  ? -5.210  -5.009  49.256 1.00 32.87 ?  69  ASP C OD1   1 
ATOM   2988 O OD2   . ASP C 1 69  ? -3.645  -5.600  50.678 1.00 41.85 -1 69  ASP C OD2   1 
ATOM   2989 N N     . THR C 1 70  ? -1.323  -1.668  47.999 1.00 25.02 ?  70  THR C N     1 
ATOM   2990 C CA    . THR C 1 70  ? -0.665  -0.399  47.714 1.00 22.68 ?  70  THR C CA    1 
ATOM   2991 C C     . THR C 1 70  ? -1.051  0.105   46.329 1.00 23.58 ?  70  THR C C     1 
ATOM   2992 O O     . THR C 1 70  ? -1.464  1.259   46.164 1.00 19.24 ?  70  THR C O     1 
ATOM   2993 C CB    . THR C 1 70  ? 0.847   -0.573  47.824 1.00 27.23 ?  70  THR C CB    1 
ATOM   2994 O OG1   . THR C 1 70  ? 1.196   -0.895  49.174 1.00 25.08 ?  70  THR C OG1   1 
ATOM   2995 C CG2   . THR C 1 70  ? 1.567   0.698   47.417 1.00 30.09 ?  70  THR C CG2   1 
ATOM   2996 N N     . TYR C 1 71  ? -0.924  -0.762  45.320 1.00 24.15 ?  71  TYR C N     1 
ATOM   2997 C CA    . TYR C 1 71  ? -1.173  -0.371  43.934 1.00 24.14 ?  71  TYR C CA    1 
ATOM   2998 C C     . TYR C 1 71  ? -2.628  0.002   43.718 1.00 25.97 ?  71  TYR C C     1 
ATOM   2999 O O     . TYR C 1 71  ? -2.933  0.955   42.990 1.00 29.92 ?  71  TYR C O     1 
ATOM   3000 C CB    . TYR C 1 71  ? -0.777  -1.512  43.001 1.00 28.39 ?  71  TYR C CB    1 
ATOM   3001 C CG    . TYR C 1 71  ? 0.694   -1.823  43.065 1.00 35.15 ?  71  TYR C CG    1 
ATOM   3002 C CD1   . TYR C 1 71  ? 1.572   -0.921  43.641 1.00 32.37 ?  71  TYR C CD1   1 
ATOM   3003 C CD2   . TYR C 1 71  ? 1.216   -2.992  42.530 1.00 41.90 ?  71  TYR C CD2   1 
ATOM   3004 C CE1   . TYR C 1 71  ? 2.907   -1.170  43.711 1.00 35.63 ?  71  TYR C CE1   1 
ATOM   3005 C CE2   . TYR C 1 71  ? 2.574   -3.253  42.589 1.00 46.24 ?  71  TYR C CE2   1 
ATOM   3006 C CZ    . TYR C 1 71  ? 3.410   -2.332  43.186 1.00 45.79 ?  71  TYR C CZ    1 
ATOM   3007 O OH    . TYR C 1 71  ? 4.764   -2.530  43.277 1.00 51.33 ?  71  TYR C OH    1 
ATOM   3008 N N     . GLU C 1 72  ? -3.538  -0.757  44.327 1.00 25.12 ?  72  GLU C N     1 
ATOM   3009 C CA    . GLU C 1 72  ? -4.961  -0.451  44.233 1.00 25.56 ?  72  GLU C CA    1 
ATOM   3010 C C     . GLU C 1 72  ? -5.241  0.968   44.709 1.00 26.65 ?  72  GLU C C     1 
ATOM   3011 O O     . GLU C 1 72  ? -5.972  1.727   44.058 1.00 23.70 ?  72  GLU C O     1 
ATOM   3012 C CB    . GLU C 1 72  ? -5.756  -1.466  45.053 1.00 20.10 ?  72  GLU C CB    1 
ATOM   3013 C CG    . GLU C 1 72  ? -7.253  -1.244  45.056 1.00 21.73 ?  72  GLU C CG    1 
ATOM   3014 C CD    . GLU C 1 72  ? -7.836  -1.187  43.659 1.00 31.80 ?  72  GLU C CD    1 
ATOM   3015 O OE1   . GLU C 1 72  ? -7.397  -1.974  42.794 1.00 34.98 ?  72  GLU C OE1   1 
ATOM   3016 O OE2   . GLU C 1 72  ? -8.733  -0.349  43.426 1.00 28.82 -1 72  GLU C OE2   1 
ATOM   3017 N N     . GLN C 1 73  ? -4.653  1.347   45.844 1.00 22.69 ?  73  GLN C N     1 
ATOM   3018 C CA    . GLN C 1 73  ? -4.844  2.692   46.374 1.00 23.31 ?  73  GLN C CA    1 
ATOM   3019 C C     . GLN C 1 73  ? -4.221  3.739   45.457 1.00 26.36 ?  73  GLN C C     1 
ATOM   3020 O O     . GLN C 1 73  ? -4.766  4.841   45.307 1.00 23.13 ?  73  GLN C O     1 
ATOM   3021 C CB    . GLN C 1 73  ? -4.276  2.770   47.789 1.00 25.82 ?  73  GLN C CB    1 
ATOM   3022 C CG    . GLN C 1 73  ? -4.960  1.789   48.736 1.00 28.85 ?  73  GLN C CG    1 
ATOM   3023 C CD    . GLN C 1 73  ? -4.271  1.669   50.080 1.00 33.97 ?  73  GLN C CD    1 
ATOM   3024 O OE1   . GLN C 1 73  ? -3.361  2.433   50.398 1.00 26.53 ?  73  GLN C OE1   1 
ATOM   3025 N NE2   . GLN C 1 73  ? -4.699  0.694   50.875 1.00 37.91 ?  73  GLN C NE2   1 
ATOM   3026 N N     . MET C 1 74  ? -3.079  3.420   44.839 1.00 21.91 ?  74  MET C N     1 
ATOM   3027 C CA    . MET C 1 74  ? -2.511  4.323   43.842 1.00 22.65 ?  74  MET C CA    1 
ATOM   3028 C C     . MET C 1 74  ? -3.462  4.494   42.666 1.00 22.48 ?  74  MET C C     1 
ATOM   3029 O O     . MET C 1 74  ? -3.752  5.619   42.241 1.00 24.14 ?  74  MET C O     1 
ATOM   3030 C CB    . MET C 1 74  ? -1.161  3.806   43.346 1.00 22.73 ?  74  MET C CB    1 
ATOM   3031 C CG    . MET C 1 74  ? -0.025  3.865   44.347 1.00 28.09 ?  74  MET C CG    1 
ATOM   3032 S SD    . MET C 1 74  ? 1.385   2.912   43.751 1.00 26.94 ?  74  MET C SD    1 
ATOM   3033 C CE    . MET C 1 74  ? 2.541   3.126   45.100 1.00 21.96 ?  74  MET C CE    1 
ATOM   3034 N N     . VAL C 1 75  ? -3.955  3.377   42.125 1.00 26.58 ?  75  VAL C N     1 
ATOM   3035 C CA    . VAL C 1 75  ? -4.842  3.426   40.965 1.00 23.16 ?  75  VAL C CA    1 
ATOM   3036 C C     . VAL C 1 75  ? -6.111  4.195   41.303 1.00 23.72 ?  75  VAL C C     1 
ATOM   3037 O O     . VAL C 1 75  ? -6.589  5.020   40.514 1.00 30.24 ?  75  VAL C O     1 
ATOM   3038 C CB    . VAL C 1 75  ? -5.153  1.998   40.476 1.00 20.47 ?  75  VAL C CB    1 
ATOM   3039 C CG1   . VAL C 1 75  ? -6.374  1.981   39.568 1.00 19.51 ?  75  VAL C CG1   1 
ATOM   3040 C CG2   . VAL C 1 75  ? -3.941  1.399   39.776 1.00 22.63 ?  75  VAL C CG2   1 
ATOM   3041 N N     . ASN C 1 76  ? -6.667  3.948   42.491 1.00 20.00 ?  76  ASN C N     1 
ATOM   3042 C CA    . ASN C 1 76  ? -7.899  4.620   42.893 1.00 22.68 ?  76  ASN C CA    1 
ATOM   3043 C C     . ASN C 1 76  ? -7.676  6.115   43.069 1.00 20.63 ?  76  ASN C C     1 
ATOM   3044 O O     . ASN C 1 76  ? -8.540  6.924   42.711 1.00 19.51 ?  76  ASN C O     1 
ATOM   3045 C CB    . ASN C 1 76  ? -8.439  3.999   44.180 1.00 20.81 ?  76  ASN C CB    1 
ATOM   3046 C CG    . ASN C 1 76  ? -9.723  4.650   44.650 1.00 24.33 ?  76  ASN C CG    1 
ATOM   3047 O OD1   . ASN C 1 76  ? -10.704 4.720   43.911 1.00 28.66 ?  76  ASN C OD1   1 
ATOM   3048 N ND2   . ASN C 1 76  ? -9.723  5.131   45.888 1.00 31.00 ?  76  ASN C ND2   1 
ATOM   3049 N N     . ALA C 1 77  ? -6.528  6.500   43.632 1.00 22.93 ?  77  ALA C N     1 
ATOM   3050 C CA    . ALA C 1 77  ? -6.227  7.916   43.808 1.00 22.09 ?  77  ALA C CA    1 
ATOM   3051 C C     . ALA C 1 77  ? -6.107  8.616   42.461 1.00 25.93 ?  77  ALA C C     1 
ATOM   3052 O O     . ALA C 1 77  ? -6.569  9.751   42.295 1.00 22.32 ?  77  ALA C O     1 
ATOM   3053 C CB    . ALA C 1 77  ? -4.939  8.085   44.613 1.00 18.12 ?  77  ALA C CB    1 
ATOM   3054 N N     . ILE C 1 78  ? -5.483  7.950   41.486 1.00 23.72 ?  78  ILE C N     1 
ATOM   3055 C CA    . ILE C 1 78  ? -5.355  8.521   40.148 1.00 23.11 ?  78  ILE C CA    1 
ATOM   3056 C C     . ILE C 1 78  ? -6.731  8.722   39.527 1.00 23.29 ?  78  ILE C C     1 
ATOM   3057 O O     . ILE C 1 78  ? -7.037  9.788   38.979 1.00 21.21 ?  78  ILE C O     1 
ATOM   3058 C CB    . ILE C 1 78  ? -4.466  7.624   39.267 1.00 26.19 ?  78  ILE C CB    1 
ATOM   3059 C CG1   . ILE C 1 78  ? -3.035  7.601   39.808 1.00 24.20 ?  78  ILE C CG1   1 
ATOM   3060 C CG2   . ILE C 1 78  ? -4.494  8.086   37.820 1.00 26.63 ?  78  ILE C CG2   1 
ATOM   3061 C CD1   . ILE C 1 78  ? -2.203  6.463   39.271 1.00 20.15 ?  78  ILE C CD1   1 
ATOM   3062 N N     . LEU C 1 79  ? -7.582  7.695   39.604 1.00 19.97 ?  79  LEU C N     1 
ATOM   3063 C CA    . LEU C 1 79  ? -8.892  7.758   38.964 1.00 23.44 ?  79  LEU C CA    1 
ATOM   3064 C C     . LEU C 1 79  ? -9.801  8.787   39.626 1.00 20.70 ?  79  LEU C C     1 
ATOM   3065 O O     . LEU C 1 79  ? -10.674 9.356   38.958 1.00 16.45 ?  79  LEU C O     1 
ATOM   3066 C CB    . LEU C 1 79  ? -9.550  6.378   38.974 1.00 20.07 ?  79  LEU C CB    1 
ATOM   3067 C CG    . LEU C 1 79  ? -9.416  5.554   37.687 1.00 21.11 ?  79  LEU C CG    1 
ATOM   3068 C CD1   . LEU C 1 79  ? -10.202 6.197   36.553 1.00 22.32 ?  79  LEU C CD1   1 
ATOM   3069 C CD2   . LEU C 1 79  ? -7.957  5.368   37.294 1.00 20.28 ?  79  LEU C CD2   1 
ATOM   3070 N N     . ASP C 1 80  ? -9.623  9.034   40.929 1.00 16.65 ?  80  ASP C N     1 
ATOM   3071 C CA    . ASP C 1 80  ? -10.447 10.031  41.609 1.00 22.77 ?  80  ASP C CA    1 
ATOM   3072 C C     . ASP C 1 80  ? -10.262 11.413  40.993 1.00 21.06 ?  80  ASP C C     1 
ATOM   3073 O O     . ASP C 1 80  ? -11.232 12.160  40.820 1.00 21.45 ?  80  ASP C O     1 
ATOM   3074 C CB    . ASP C 1 80  ? -10.121 10.068  43.103 1.00 24.99 ?  80  ASP C CB    1 
ATOM   3075 C CG    . ASP C 1 80  ? -10.922 9.061   43.901 1.00 24.80 ?  80  ASP C CG    1 
ATOM   3076 O OD1   . ASP C 1 80  ? -11.715 8.309   43.295 1.00 25.16 ?  80  ASP C OD1   1 
ATOM   3077 O OD2   . ASP C 1 80  ? -10.765 9.027   45.140 1.00 30.16 -1 80  ASP C OD2   1 
ATOM   3078 N N     . ALA C 1 81  ? -9.019  11.778  40.669 1.00 20.40 ?  81  ALA C N     1 
ATOM   3079 C CA    . ALA C 1 81  ? -8.777  13.071  40.038 1.00 22.33 ?  81  ALA C CA    1 
ATOM   3080 C C     . ALA C 1 81  ? -9.391  13.117  38.646 1.00 21.80 ?  81  ALA C C     1 
ATOM   3081 O O     . ALA C 1 81  ? -9.924  14.152  38.228 1.00 19.94 ?  81  ALA C O     1 
ATOM   3082 C CB    . ALA C 1 81  ? -7.277  13.355  39.977 1.00 19.07 ?  81  ALA C CB    1 
ATOM   3083 N N     . VAL C 1 82  ? -9.330  11.998  37.919 1.00 23.12 ?  82  VAL C N     1 
ATOM   3084 C CA    . VAL C 1 82  ? -9.916  11.939  36.583 1.00 22.32 ?  82  VAL C CA    1 
ATOM   3085 C C     . VAL C 1 82  ? -11.431 12.056  36.671 1.00 21.67 ?  82  VAL C C     1 
ATOM   3086 O O     . VAL C 1 82  ? -12.056 12.837  35.944 1.00 19.87 ?  82  VAL C O     1 
ATOM   3087 C CB    . VAL C 1 82  ? -9.495  10.642  35.869 1.00 20.83 ?  82  VAL C CB    1 
ATOM   3088 C CG1   . VAL C 1 82  ? -10.310 10.435  34.601 1.00 21.14 ?  82  VAL C CG1   1 
ATOM   3089 C CG2   . VAL C 1 82  ? -8.005  10.658  35.565 1.00 20.85 ?  82  VAL C CG2   1 
ATOM   3090 N N     . ARG C 1 83  ? -12.041 11.272  37.564 1.00 21.25 ?  83  ARG C N     1 
ATOM   3091 C CA    . ARG C 1 83  ? -13.488 11.313  37.745 1.00 22.99 ?  83  ARG C CA    1 
ATOM   3092 C C     . ARG C 1 83  ? -13.956 12.696  38.183 1.00 22.05 ?  83  ARG C C     1 
ATOM   3093 O O     . ARG C 1 83  ? -15.053 13.127  37.810 1.00 21.28 ?  83  ARG C O     1 
ATOM   3094 C CB    . ARG C 1 83  ? -13.908 10.235  38.745 1.00 23.81 ?  83  ARG C CB    1 
ATOM   3095 C CG    . ARG C 1 83  ? -13.781 8.834   38.160 1.00 26.67 ?  83  ARG C CG    1 
ATOM   3096 C CD    . ARG C 1 83  ? -14.265 7.731   39.086 1.00 27.33 ?  83  ARG C CD    1 
ATOM   3097 N NE    . ARG C 1 83  ? -13.348 7.481   40.191 1.00 34.64 ?  83  ARG C NE    1 
ATOM   3098 C CZ    . ARG C 1 83  ? -12.842 6.289   40.484 1.00 27.81 ?  83  ARG C CZ    1 
ATOM   3099 N NH1   . ARG C 1 83  ? -13.104 5.223   39.742 1.00 24.60 ?  83  ARG C NH1   1 
ATOM   3100 N NH2   . ARG C 1 83  ? -12.057 6.160   41.549 1.00 20.99 ?  83  ARG C NH2   1 
ATOM   3101 N N     . ALA C 1 84  ? -13.143 13.402  38.975 1.00 23.59 ?  84  ALA C N     1 
ATOM   3102 C CA    . ALA C 1 84  ? -13.516 14.744  39.406 1.00 22.87 ?  84  ALA C CA    1 
ATOM   3103 C C     . ALA C 1 84  ? -13.577 15.708  38.231 1.00 21.78 ?  84  ALA C C     1 
ATOM   3104 O O     . ALA C 1 84  ? -14.310 16.700  38.281 1.00 25.40 ?  84  ALA C O     1 
ATOM   3105 C CB    . ALA C 1 84  ? -12.530 15.254  40.457 1.00 20.37 ?  84  ALA C CB    1 
ATOM   3106 N N     . GLY C 1 85  ? -12.816 15.438  37.174 1.00 19.84 ?  85  GLY C N     1 
ATOM   3107 C CA    . GLY C 1 85  ? -12.770 16.293  35.998 1.00 22.16 ?  85  GLY C CA    1 
ATOM   3108 C C     . GLY C 1 85  ? -11.392 16.822  35.662 1.00 19.63 ?  85  GLY C C     1 
ATOM   3109 O O     . GLY C 1 85  ? -11.264 17.606  34.712 1.00 23.42 ?  85  GLY C O     1 
ATOM   3110 N N     . LYS C 1 86  ? -10.353 16.430  36.390 1.00 19.30 ?  86  LYS C N     1 
ATOM   3111 C CA    . LYS C 1 86  ? -9.032  17.015  36.216 1.00 19.55 ?  86  LYS C CA    1 
ATOM   3112 C C     . LYS C 1 86  ? -8.311  16.395  35.027 1.00 25.29 ?  86  LYS C C     1 
ATOM   3113 O O     . LYS C 1 86  ? -8.387  15.186  34.792 1.00 17.49 ?  86  LYS C O     1 
ATOM   3114 C CB    . LYS C 1 86  ? -8.201  16.818  37.484 1.00 20.53 ?  86  LYS C CB    1 
ATOM   3115 C CG    . LYS C 1 86  ? -8.913  17.250  38.755 1.00 22.32 ?  86  LYS C CG    1 
ATOM   3116 C CD    . LYS C 1 86  ? -7.929  17.724  39.806 1.00 33.05 ?  86  LYS C CD    1 
ATOM   3117 C CE    . LYS C 1 86  ? -8.489  17.555  41.208 1.00 32.07 ?  86  LYS C CE    1 
ATOM   3118 N NZ    . LYS C 1 86  ? -8.914  18.856  41.792 1.00 36.90 ?  86  LYS C NZ    1 
ATOM   3119 N N     . LYS C 1 87  ? -7.605  17.234  34.277 1.00 24.28 ?  87  LYS C N     1 
ATOM   3120 C CA    . LYS C 1 87  ? -6.684  16.755  33.248 1.00 23.05 ?  87  LYS C CA    1 
ATOM   3121 C C     . LYS C 1 87  ? -5.451  16.213  33.959 1.00 21.35 ?  87  LYS C C     1 
ATOM   3122 O O     . LYS C 1 87  ? -4.570  16.967  34.376 1.00 19.15 ?  87  LYS C O     1 
ATOM   3123 C CB    . LYS C 1 87  ? -6.339  17.874  32.270 1.00 22.81 ?  87  LYS C CB    1 
ATOM   3124 C CG    . LYS C 1 87  ? -5.427  17.449  31.131 1.00 26.26 ?  87  LYS C CG    1 
ATOM   3125 C CD    . LYS C 1 87  ? -5.247  18.561  30.105 1.00 22.77 ?  87  LYS C CD    1 
ATOM   3126 C CE    . LYS C 1 87  ? -4.323  19.656  30.602 1.00 21.63 ?  87  LYS C CE    1 
ATOM   3127 N NZ    . LYS C 1 87  ? -4.152  20.734  29.584 1.00 24.27 ?  87  LYS C NZ    1 
ATOM   3128 N N     . THR C 1 88  ? -5.392  14.894  34.103 1.00 18.24 ?  88  THR C N     1 
ATOM   3129 C CA    . THR C 1 88  ? -4.514  14.231  35.056 1.00 20.91 ?  88  THR C CA    1 
ATOM   3130 C C     . THR C 1 88  ? -3.349  13.558  34.343 1.00 20.04 ?  88  THR C C     1 
ATOM   3131 O O     . THR C 1 88  ? -3.528  12.922  33.300 1.00 18.08 ?  88  THR C O     1 
ATOM   3132 C CB    . THR C 1 88  ? -5.294  13.187  35.867 1.00 21.49 ?  88  THR C CB    1 
ATOM   3133 O OG1   . THR C 1 88  ? -6.460  13.800  36.429 1.00 18.90 ?  88  THR C OG1   1 
ATOM   3134 C CG2   . THR C 1 88  ? -4.436  12.624  36.988 1.00 18.77 ?  88  THR C CG2   1 
ATOM   3135 N N     . VAL C 1 89  ? -2.157  13.704  34.914 1.00 16.35 ?  89  VAL C N     1 
ATOM   3136 C CA    . VAL C 1 89  ? -0.957  13.032  34.433 1.00 16.93 ?  89  VAL C CA    1 
ATOM   3137 C C     . VAL C 1 89  ? -0.392  12.170  35.553 1.00 17.66 ?  89  VAL C C     1 
ATOM   3138 O O     . VAL C 1 89  ? -0.329  12.596  36.711 1.00 24.31 ?  89  VAL C O     1 
ATOM   3139 C CB    . VAL C 1 89  ? 0.102   14.036  33.925 1.00 20.51 ?  89  VAL C CB    1 
ATOM   3140 C CG1   . VAL C 1 89  ? 1.434   13.341  33.675 1.00 18.50 ?  89  VAL C CG1   1 
ATOM   3141 C CG2   . VAL C 1 89  ? -0.378  14.693  32.643 1.00 20.41 ?  89  VAL C CG2   1 
ATOM   3142 N N     . CYS C 1 90  ? 0.011   10.954  35.204 1.00 17.35 ?  90  CYS C N     1 
ATOM   3143 C CA    . CYS C 1 90  ? 0.775   10.083  36.086 1.00 21.44 ?  90  CYS C CA    1 
ATOM   3144 C C     . CYS C 1 90  ? 2.213   10.064  35.583 1.00 21.16 ?  90  CYS C C     1 
ATOM   3145 O O     . CYS C 1 90  ? 2.467   9.681   34.435 1.00 25.72 ?  90  CYS C O     1 
ATOM   3146 C CB    . CYS C 1 90  ? 0.180   8.672   36.112 1.00 23.72 ?  90  CYS C CB    1 
ATOM   3147 S SG    . CYS C 1 90  ? 1.088   7.481   37.114 1.00 30.82 ?  90  CYS C SG    1 
ATOM   3148 N N     . ALA C 1 91  ? 3.145   10.490  36.428 1.00 23.29 ?  91  ALA C N     1 
ATOM   3149 C CA    . ALA C 1 91  ? 4.559   10.562  36.069 1.00 18.21 ?  91  ALA C CA    1 
ATOM   3150 C C     . ALA C 1 91  ? 5.308   9.490   36.852 1.00 20.23 ?  91  ALA C C     1 
ATOM   3151 O O     . ALA C 1 91  ? 5.597   9.660   38.039 1.00 20.96 ?  91  ALA C O     1 
ATOM   3152 C CB    . ALA C 1 91  ? 5.123   11.951  36.348 1.00 19.13 ?  91  ALA C CB    1 
ATOM   3153 N N     . LEU C 1 92  ? 5.624   8.390   36.179 1.00 21.30 ?  92  LEU C N     1 
ATOM   3154 C CA    . LEU C 1 92  ? 6.363   7.282   36.764 1.00 23.53 ?  92  LEU C CA    1 
ATOM   3155 C C     . LEU C 1 92  ? 7.786   7.297   36.223 1.00 23.37 ?  92  LEU C C     1 
ATOM   3156 O O     . LEU C 1 92  ? 8.043   7.793   35.124 1.00 24.04 ?  92  LEU C O     1 
ATOM   3157 C CB    . LEU C 1 92  ? 5.702   5.935   36.444 1.00 22.07 ?  92  LEU C CB    1 
ATOM   3158 C CG    . LEU C 1 92  ? 4.278   5.700   36.954 1.00 24.27 ?  92  LEU C CG    1 
ATOM   3159 C CD1   . LEU C 1 92  ? 3.885   4.243   36.773 1.00 29.78 ?  92  LEU C CD1   1 
ATOM   3160 C CD2   . LEU C 1 92  ? 4.145   6.113   38.405 1.00 19.62 ?  92  LEU C CD2   1 
ATOM   3161 N N     . TYR C 1 93  ? 8.716   6.753   36.997 1.00 23.23 ?  93  TYR C N     1 
ATOM   3162 C CA    . TYR C 1 93  ? 10.102  6.746   36.561 1.00 19.04 ?  93  TYR C CA    1 
ATOM   3163 C C     . TYR C 1 93  ? 10.316  5.653   35.518 1.00 23.01 ?  93  TYR C C     1 
ATOM   3164 O O     . TYR C 1 93  ? 9.646   4.614   35.525 1.00 19.23 ?  93  TYR C O     1 
ATOM   3165 C CB    . TYR C 1 93  ? 11.047  6.565   37.755 1.00 21.62 ?  93  TYR C CB    1 
ATOM   3166 C CG    . TYR C 1 93  ? 11.172  5.149   38.261 1.00 17.30 ?  93  TYR C CG    1 
ATOM   3167 C CD1   . TYR C 1 93  ? 12.045  4.249   37.661 1.00 25.27 ?  93  TYR C CD1   1 
ATOM   3168 C CD2   . TYR C 1 93  ? 10.416  4.710   39.340 1.00 24.15 ?  93  TYR C CD2   1 
ATOM   3169 C CE1   . TYR C 1 93  ? 12.159  2.956   38.115 1.00 27.23 ?  93  TYR C CE1   1 
ATOM   3170 C CE2   . TYR C 1 93  ? 10.526  3.414   39.803 1.00 26.74 ?  93  TYR C CE2   1 
ATOM   3171 C CZ    . TYR C 1 93  ? 11.401  2.545   39.184 1.00 22.17 ?  93  TYR C CZ    1 
ATOM   3172 O OH    . TYR C 1 93  ? 11.521  1.252   39.628 1.00 24.15 ?  93  TYR C OH    1 
ATOM   3173 N N     . GLY C 1 94  ? 11.247  5.908   34.607 1.00 18.39 ?  94  GLY C N     1 
ATOM   3174 C CA    . GLY C 1 94  ? 11.531  4.947   33.551 1.00 20.62 ?  94  GLY C CA    1 
ATOM   3175 C C     . GLY C 1 94  ? 10.455  4.970   32.490 1.00 17.87 ?  94  GLY C C     1 
ATOM   3176 O O     . GLY C 1 94  ? 10.048  6.035   32.022 1.00 20.17 ?  94  GLY C O     1 
ATOM   3177 N N     . HIS C 1 95  ? 9.997   3.780   32.091 1.00 15.97 ?  95  HIS C N     1 
ATOM   3178 C CA    . HIS C 1 95  ? 8.879   3.593   31.171 1.00 17.28 ?  95  HIS C CA    1 
ATOM   3179 C C     . HIS C 1 95  ? 7.655   3.169   31.967 1.00 16.36 ?  95  HIS C C     1 
ATOM   3180 O O     . HIS C 1 95  ? 7.724   2.174   32.703 1.00 15.57 ?  95  HIS C O     1 
ATOM   3181 C CB    . HIS C 1 95  ? 9.240   2.535   30.127 1.00 17.76 ?  95  HIS C CB    1 
ATOM   3182 C CG    . HIS C 1 95  ? 8.195   2.296   29.075 1.00 15.96 ?  95  HIS C CG    1 
ATOM   3183 N ND1   . HIS C 1 95  ? 6.852   2.167   29.354 1.00 16.46 ?  95  HIS C ND1   1 
ATOM   3184 C CD2   . HIS C 1 95  ? 8.312   2.143   27.734 1.00 12.83 ?  95  HIS C CD2   1 
ATOM   3185 C CE1   . HIS C 1 95  ? 6.186   1.955   28.233 1.00 17.62 ?  95  HIS C CE1   1 
ATOM   3186 N NE2   . HIS C 1 95  ? 7.050   1.935   27.234 1.00 14.52 ?  95  HIS C NE2   1 
ATOM   3187 N N     . PRO C 1 96  ? 6.526   3.877   31.862 1.00 17.03 ?  96  PRO C N     1 
ATOM   3188 C CA    . PRO C 1 96  ? 5.433   3.659   32.824 1.00 18.23 ?  96  PRO C CA    1 
ATOM   3189 C C     . PRO C 1 96  ? 4.737   2.320   32.676 1.00 16.46 ?  96  PRO C C     1 
ATOM   3190 O O     . PRO C 1 96  ? 4.046   1.896   33.611 1.00 18.77 ?  96  PRO C O     1 
ATOM   3191 C CB    . PRO C 1 96  ? 4.477   4.824   32.528 1.00 18.02 ?  96  PRO C CB    1 
ATOM   3192 C CG    . PRO C 1 96  ? 4.677   5.069   31.066 1.00 17.35 ?  96  PRO C CG    1 
ATOM   3193 C CD    . PRO C 1 96  ? 6.164   4.886   30.851 1.00 16.83 ?  96  PRO C CD    1 
ATOM   3194 N N     . GLY C 1 97  ? 4.901   1.639   31.544 1.00 18.21 ?  97  GLY C N     1 
ATOM   3195 C CA    . GLY C 1 97  ? 4.283   0.352   31.324 1.00 19.29 ?  97  GLY C CA    1 
ATOM   3196 C C     . GLY C 1 97  ? 5.254   -0.804  31.273 1.00 16.85 ?  97  GLY C C     1 
ATOM   3197 O O     . GLY C 1 97  ? 4.871   -1.892  30.835 1.00 22.00 ?  97  GLY C O     1 
ATOM   3198 N N     . VAL C 1 98  ? 6.489   -0.617  31.725 1.00 20.13 ?  98  VAL C N     1 
ATOM   3199 C CA    . VAL C 1 98  ? 7.504   -1.660  31.714 1.00 23.64 ?  98  VAL C CA    1 
ATOM   3200 C C     . VAL C 1 98  ? 7.673   -2.133  33.148 1.00 21.79 ?  98  VAL C C     1 
ATOM   3201 O O     . VAL C 1 98  ? 8.162   -1.388  34.008 1.00 19.14 ?  98  VAL C O     1 
ATOM   3202 C CB    . VAL C 1 98  ? 8.828   -1.158  31.124 1.00 24.26 ?  98  VAL C CB    1 
ATOM   3203 C CG1   . VAL C 1 98  ? 9.958   -2.117  31.465 1.00 18.19 ?  98  VAL C CG1   1 
ATOM   3204 C CG2   . VAL C 1 98  ? 8.702   -1.009  29.620 1.00 17.72 ?  98  VAL C CG2   1 
ATOM   3205 N N     . PHE C 1 99  ? 7.270   -3.377  33.398 1.00 19.76 ?  99  PHE C N     1 
ATOM   3206 C CA    . PHE C 1 99  ? 7.261   -3.955  34.737 1.00 20.80 ?  99  PHE C CA    1 
ATOM   3207 C C     . PHE C 1 99  ? 6.635   -2.990  35.738 1.00 23.41 ?  99  PHE C C     1 
ATOM   3208 O O     . PHE C 1 99  ? 7.183   -2.716  36.797 1.00 23.76 ?  99  PHE C O     1 
ATOM   3209 C CB    . PHE C 1 99  ? 8.674   -4.350  35.169 1.00 19.14 ?  99  PHE C CB    1 
ATOM   3210 C CG    . PHE C 1 99  ? 9.199   -5.577  34.477 1.00 18.18 ?  99  PHE C CG    1 
ATOM   3211 C CD1   . PHE C 1 99  ? 9.702   -5.498  33.190 1.00 15.79 ?  99  PHE C CD1   1 
ATOM   3212 C CD2   . PHE C 1 99  ? 9.203   -6.806  35.118 1.00 20.97 ?  99  PHE C CD2   1 
ATOM   3213 C CE1   . PHE C 1 99  ? 10.186  -6.619  32.550 1.00 18.59 ?  99  PHE C CE1   1 
ATOM   3214 C CE2   . PHE C 1 99  ? 9.691   -7.934  34.484 1.00 19.05 ?  99  PHE C CE2   1 
ATOM   3215 C CZ    . PHE C 1 99  ? 10.182  -7.839  33.196 1.00 18.66 ?  99  PHE C CZ    1 
ATOM   3216 N N     . ALA C 1 100 ? 5.477   -2.448  35.383 1.00 19.44 ?  100 ALA C N     1 
ATOM   3217 C CA    . ALA C 1 100 ? 4.766   -1.537  36.275 1.00 24.00 ?  100 ALA C CA    1 
ATOM   3218 C C     . ALA C 1 100 ? 3.280   -1.629  35.968 1.00 21.82 ?  100 ALA C C     1 
ATOM   3219 O O     . ALA C 1 100 ? 2.874   -1.453  34.815 1.00 27.18 ?  100 ALA C O     1 
ATOM   3220 C CB    . ALA C 1 100 ? 5.269   -0.101  36.117 1.00 24.25 ?  100 ALA C CB    1 
ATOM   3221 N N     . CYS C 1 101 ? 2.472   -1.923  36.987 1.00 27.48 ?  101 CYS C N     1 
ATOM   3222 C CA    . CYS C 1 101 ? 1.060   -2.177  36.748 1.00 26.97 ?  101 CYS C CA    1 
ATOM   3223 C C     . CYS C 1 101 ? 0.167   -0.966  36.981 1.00 24.77 ?  101 CYS C C     1 
ATOM   3224 O O     . CYS C 1 101 ? -0.924  -0.919  36.404 1.00 26.32 ?  101 CYS C O     1 
ATOM   3225 C CB    . CYS C 1 101 ? 0.562   -3.331  37.623 1.00 31.64 ?  101 CYS C CB    1 
ATOM   3226 S SG    . CYS C 1 101 ? 0.739   -3.030  39.372 1.00 38.65 ?  101 CYS C SG    1 
ATOM   3227 N N     . VAL C 1 102 ? 0.588   0.009   37.796 1.00 32.54 ?  102 VAL C N     1 
ATOM   3228 C CA    . VAL C 1 102 ? -0.330  1.077   38.202 1.00 23.37 ?  102 VAL C CA    1 
ATOM   3229 C C     . VAL C 1 102 ? -0.902  1.787   36.982 1.00 18.55 ?  102 VAL C C     1 
ATOM   3230 O O     . VAL C 1 102 ? -2.111  2.027   36.895 1.00 18.47 ?  102 VAL C O     1 
ATOM   3231 C CB    . VAL C 1 102 ? 0.355   2.064   39.165 1.00 24.38 ?  102 VAL C CB    1 
ATOM   3232 C CG1   . VAL C 1 102 ? -0.408  3.371   39.217 1.00 21.00 ?  102 VAL C CG1   1 
ATOM   3233 C CG2   . VAL C 1 102 ? 0.392   1.476   40.566 1.00 31.10 ?  102 VAL C CG2   1 
ATOM   3234 N N     . SER C 1 103 ? -0.049  2.113   36.010 1.00 12.66 ?  103 SER C N     1 
ATOM   3235 C CA    . SER C 1 103 ? -0.517  2.887   34.865 1.00 18.51 ?  103 SER C CA    1 
ATOM   3236 C C     . SER C 1 103 ? -1.398  2.051   33.944 1.00 17.90 ?  103 SER C C     1 
ATOM   3237 O O     . SER C 1 103 ? -2.410  2.551   33.437 1.00 19.77 ?  103 SER C O     1 
ATOM   3238 C CB    . SER C 1 103 ? 0.669   3.471   34.099 1.00 15.46 ?  103 SER C CB    1 
ATOM   3239 O OG    . SER C 1 103 ? 1.311   4.469   34.865 1.00 17.69 ?  103 SER C OG    1 
ATOM   3240 N N     . HIS C 1 104 ? -1.034  0.783   33.706 1.00 19.54 ?  104 HIS C N     1 
ATOM   3241 C CA    . HIS C 1 104 ? -1.894  -0.079  32.897 1.00 20.72 ?  104 HIS C CA    1 
ATOM   3242 C C     . HIS C 1 104 ? -3.263  -0.247  33.544 1.00 17.36 ?  104 HIS C C     1 
ATOM   3243 O O     . HIS C 1 104 ? -4.292  -0.198  32.859 1.00 14.55 ?  104 HIS C O     1 
ATOM   3244 C CB    . HIS C 1 104 ? -1.248  -1.446  32.671 1.00 19.40 ?  104 HIS C CB    1 
ATOM   3245 C CG    . HIS C 1 104 ? -0.186  -1.453  31.613 1.00 25.89 ?  104 HIS C CG    1 
ATOM   3246 N ND1   . HIS C 1 104 ? 1.123   -1.798  31.871 1.00 23.46 ?  104 HIS C ND1   1 
ATOM   3247 C CD2   . HIS C 1 104 ? -0.245  -1.172  30.289 1.00 16.50 ?  104 HIS C CD2   1 
ATOM   3248 C CE1   . HIS C 1 104 ? 1.825   -1.726  30.754 1.00 19.80 ?  104 HIS C CE1   1 
ATOM   3249 N NE2   . HIS C 1 104 ? 1.019   -1.344  29.780 1.00 19.53 ?  104 HIS C NE2   1 
ATOM   3250 N N     . MET C 1 105 ? -3.293  -0.451  34.866 1.00 19.95 ?  105 MET C N     1 
ATOM   3251 C CA    . MET C 1 105 ? -4.568  -0.607  35.560 1.00 16.84 ?  105 MET C CA    1 
ATOM   3252 C C     . MET C 1 105 ? -5.361  0.692   35.538 1.00 18.85 ?  105 MET C C     1 
ATOM   3253 O O     . MET C 1 105 ? -6.588  0.678   35.372 1.00 18.63 ?  105 MET C O     1 
ATOM   3254 C CB    . MET C 1 105 ? -4.341  -1.056  37.002 1.00 18.62 ?  105 MET C CB    1 
ATOM   3255 C CG    . MET C 1 105 ? -3.522  -2.319  37.166 1.00 19.45 ?  105 MET C CG    1 
ATOM   3256 S SD    . MET C 1 105 ? -2.871  -2.455  38.842 1.00 29.63 ?  105 MET C SD    1 
ATOM   3257 C CE    . MET C 1 105 ? -4.348  -2.915  39.743 1.00 35.06 ?  105 MET C CE    1 
ATOM   3258 N N     . ALA C 1 106 ? -4.679  1.825   35.717 1.00 17.73 ?  106 ALA C N     1 
ATOM   3259 C CA    . ALA C 1 106 ? -5.363  3.113   35.683 1.00 16.30 ?  106 ALA C CA    1 
ATOM   3260 C C     . ALA C 1 106 ? -5.972  3.370   34.312 1.00 17.70 ?  106 ALA C C     1 
ATOM   3261 O O     . ALA C 1 106 ? -7.102  3.861   34.209 1.00 21.30 ?  106 ALA C O     1 
ATOM   3262 C CB    . ALA C 1 106 ? -4.396  4.233   36.063 1.00 16.04 ?  106 ALA C CB    1 
ATOM   3263 N N     . ILE C 1 107 ? -5.235  3.049   33.245 1.00 17.56 ?  107 ILE C N     1 
ATOM   3264 C CA    . ILE C 1 107 ? -5.741  3.292   31.897 1.00 19.43 ?  107 ILE C CA    1 
ATOM   3265 C C     . ILE C 1 107 ? -6.911  2.368   31.591 1.00 15.41 ?  107 ILE C C     1 
ATOM   3266 O O     . ILE C 1 107 ? -7.922  2.798   31.023 1.00 17.73 ?  107 ILE C O     1 
ATOM   3267 C CB    . ILE C 1 107 ? -4.611  3.139   30.864 1.00 17.19 ?  107 ILE C CB    1 
ATOM   3268 C CG1   . ILE C 1 107 ? -3.612  4.289   30.997 1.00 15.03 ?  107 ILE C CG1   1 
ATOM   3269 C CG2   . ILE C 1 107 ? -5.170  3.090   29.455 1.00 20.32 ?  107 ILE C CG2   1 
ATOM   3270 C CD1   . ILE C 1 107 ? -2.444  4.168   30.064 1.00 16.25 ?  107 ILE C CD1   1 
ATOM   3271 N N     . THR C 1 108 ? -6.793  1.086   31.951 1.00 21.27 ?  108 THR C N     1 
ATOM   3272 C CA    . THR C 1 108 ? -7.902  0.158   31.746 1.00 21.41 ?  108 THR C CA    1 
ATOM   3273 C C     . THR C 1 108 ? -9.149  0.631   32.479 1.00 20.56 ?  108 THR C C     1 
ATOM   3274 O O     . THR C 1 108 ? -10.254 0.613   31.921 1.00 25.46 ?  108 THR C O     1 
ATOM   3275 C CB    . THR C 1 108 ? -7.518  -1.250  32.203 1.00 21.63 ?  108 THR C CB    1 
ATOM   3276 O OG1   . THR C 1 108 ? -6.447  -1.742  31.390 1.00 20.79 ?  108 THR C OG1   1 
ATOM   3277 C CG2   . THR C 1 108 ? -8.707  -2.193  32.081 1.00 21.49 ?  108 THR C CG2   1 
ATOM   3278 N N     . ARG C 1 109 ? -8.989  1.069   33.732 1.00 21.44 ?  109 ARG C N     1 
ATOM   3279 C CA    . ARG C 1 109 ? -10.142 1.497   34.517 1.00 25.62 ?  109 ARG C CA    1 
ATOM   3280 C C     . ARG C 1 109 ? -10.736 2.784   33.958 1.00 24.69 ?  109 ARG C C     1 
ATOM   3281 O O     . ARG C 1 109 ? -11.963 2.924   33.874 1.00 25.71 ?  109 ARG C O     1 
ATOM   3282 C CB    . ARG C 1 109 ? -9.744  1.691   35.978 1.00 27.82 ?  109 ARG C CB    1 
ATOM   3283 C CG    . ARG C 1 109 ? -10.881 1.491   36.967 1.00 25.92 ?  109 ARG C CG    1 
ATOM   3284 C CD    . ARG C 1 109 ? -10.375 1.442   38.401 1.00 29.25 ?  109 ARG C CD    1 
ATOM   3285 N NE    . ARG C 1 109 ? -9.801  0.146   38.746 1.00 30.20 ?  109 ARG C NE    1 
ATOM   3286 C CZ    . ARG C 1 109 ? -9.303  -0.151  39.940 1.00 30.97 ?  109 ARG C CZ    1 
ATOM   3287 N NH1   . ARG C 1 109 ? -9.299  0.733   40.927 1.00 24.62 ?  109 ARG C NH1   1 
ATOM   3288 N NH2   . ARG C 1 109 ? -8.794  -1.362  40.151 1.00 27.65 ?  109 ARG C NH2   1 
ATOM   3289 N N     . ALA C 1 110 ? -9.881  3.736   33.574 1.00 21.25 ?  110 ALA C N     1 
ATOM   3290 C CA    . ALA C 1 110 ? -10.368 4.991   33.010 1.00 23.23 ?  110 ALA C CA    1 
ATOM   3291 C C     . ALA C 1 110 ? -11.127 4.749   31.713 1.00 22.47 ?  110 ALA C C     1 
ATOM   3292 O O     . ALA C 1 110 ? -12.189 5.342   31.485 1.00 22.76 ?  110 ALA C O     1 
ATOM   3293 C CB    . ALA C 1 110 ? -9.205  5.957   32.783 1.00 20.15 ?  110 ALA C CB    1 
ATOM   3294 N N     . LYS C 1 111 ? -10.589 3.883   30.847 1.00 25.85 ?  111 LYS C N     1 
ATOM   3295 C CA    . LYS C 1 111 ? -11.249 3.594   29.577 1.00 26.64 ?  111 LYS C CA    1 
ATOM   3296 C C     . LYS C 1 111 ? -12.615 2.957   29.800 1.00 28.96 ?  111 LYS C C     1 
ATOM   3297 O O     . LYS C 1 111 ? -13.567 3.233   29.060 1.00 25.46 ?  111 LYS C O     1 
ATOM   3298 C CB    . LYS C 1 111 ? -10.375 2.674   28.727 1.00 22.22 ?  111 LYS C CB    1 
ATOM   3299 C CG    . LYS C 1 111 ? -9.274  3.367   27.942 1.00 30.51 ?  111 LYS C CG    1 
ATOM   3300 C CD    . LYS C 1 111 ? -8.501  2.351   27.116 1.00 27.18 ?  111 LYS C CD    1 
ATOM   3301 C CE    . LYS C 1 111 ? -7.243  2.941   26.505 1.00 30.61 ?  111 LYS C CE    1 
ATOM   3302 N NZ    . LYS C 1 111 ? -7.544  3.946   25.455 1.00 42.20 ?  111 LYS C NZ    1 
ATOM   3303 N N     . ALA C 1 112 ? -12.733 2.102   30.818 1.00 26.05 ?  112 ALA C N     1 
ATOM   3304 C CA    . ALA C 1 112 ? -13.989 1.405   31.067 1.00 28.50 ?  112 ALA C CA    1 
ATOM   3305 C C     . ALA C 1 112 ? -15.051 2.328   31.641 1.00 27.96 ?  112 ALA C C     1 
ATOM   3306 O O     . ALA C 1 112 ? -16.246 2.047   31.492 1.00 25.77 ?  112 ALA C O     1 
ATOM   3307 C CB    . ALA C 1 112 ? -13.758 0.220   32.009 1.00 27.21 ?  112 ALA C CB    1 
ATOM   3308 N N     . GLU C 1 113 ? -14.645 3.414   32.292 1.00 27.17 ?  113 GLU C N     1 
ATOM   3309 C CA    . GLU C 1 113 ? -15.573 4.392   32.836 1.00 24.78 ?  113 GLU C CA    1 
ATOM   3310 C C     . GLU C 1 113 ? -15.822 5.545   31.873 1.00 25.51 ?  113 GLU C C     1 
ATOM   3311 O O     . GLU C 1 113 ? -16.487 6.519   32.244 1.00 23.31 ?  113 GLU C O     1 
ATOM   3312 C CB    . GLU C 1 113 ? -15.056 4.923   34.175 1.00 25.10 ?  113 GLU C CB    1 
ATOM   3313 C CG    . GLU C 1 113 ? -15.122 3.907   35.309 1.00 26.88 ?  113 GLU C CG    1 
ATOM   3314 C CD    . GLU C 1 113 ? -14.366 4.359   36.543 1.00 28.49 ?  113 GLU C CD    1 
ATOM   3315 O OE1   . GLU C 1 113 ? -14.222 5.584   36.737 1.00 28.63 ?  113 GLU C OE1   1 
ATOM   3316 O OE2   . GLU C 1 113 ? -13.920 3.489   37.321 1.00 33.24 -1 113 GLU C OE2   1 
ATOM   3317 N N     . GLY C 1 114 ? -15.296 5.456   30.654 1.00 22.63 ?  114 GLY C N     1 
ATOM   3318 C CA    . GLY C 1 114 ? -15.596 6.421   29.618 1.00 23.17 ?  114 GLY C CA    1 
ATOM   3319 C C     . GLY C 1 114 ? -14.658 7.599   29.523 1.00 25.08 ?  114 GLY C C     1 
ATOM   3320 O O     . GLY C 1 114 ? -15.004 8.592   28.875 1.00 22.59 ?  114 GLY C O     1 
ATOM   3321 N N     . PHE C 1 115 ? -13.487 7.528   30.142 1.00 22.11 ?  115 PHE C N     1 
ATOM   3322 C CA    . PHE C 1 115 ? -12.533 8.624   30.109 1.00 25.73 ?  115 PHE C CA    1 
ATOM   3323 C C     . PHE C 1 115 ? -11.431 8.366   29.088 1.00 23.62 ?  115 PHE C C     1 
ATOM   3324 O O     . PHE C 1 115 ? -11.033 7.225   28.845 1.00 23.55 ?  115 PHE C O     1 
ATOM   3325 C CB    . PHE C 1 115 ? -11.909 8.851   31.488 1.00 21.93 ?  115 PHE C CB    1 
ATOM   3326 C CG    . PHE C 1 115 ? -12.915 9.096   32.578 1.00 21.43 ?  115 PHE C CG    1 
ATOM   3327 C CD1   . PHE C 1 115 ? -13.720 10.223  32.553 1.00 23.64 ?  115 PHE C CD1   1 
ATOM   3328 C CD2   . PHE C 1 115 ? -13.054 8.203   33.626 1.00 22.66 ?  115 PHE C CD2   1 
ATOM   3329 C CE1   . PHE C 1 115 ? -14.647 10.454  33.552 1.00 24.25 ?  115 PHE C CE1   1 
ATOM   3330 C CE2   . PHE C 1 115 ? -13.981 8.428   34.630 1.00 23.20 ?  115 PHE C CE2   1 
ATOM   3331 C CZ    . PHE C 1 115 ? -14.777 9.556   34.591 1.00 22.18 ?  115 PHE C CZ    1 
ATOM   3332 N N     . SER C 1 116 ? -10.949 9.449   28.485 1.00 19.11 ?  116 SER C N     1 
ATOM   3333 C CA    . SER C 1 116 ? -9.788  9.387   27.607 1.00 29.60 ?  116 SER C CA    1 
ATOM   3334 C C     . SER C 1 116 ? -8.543  9.060   28.424 1.00 22.23 ?  116 SER C C     1 
ATOM   3335 O O     . SER C 1 116 ? -8.215  9.772   29.378 1.00 17.41 ?  116 SER C O     1 
ATOM   3336 C CB    . SER C 1 116 ? -9.618  10.719  26.873 1.00 16.37 ?  116 SER C CB    1 
ATOM   3337 O OG    . SER C 1 116 ? -8.576  10.653  25.920 1.00 30.30 ?  116 SER C OG    1 
ATOM   3338 N N     . ALA C 1 117 ? -7.853  7.982   28.059 1.00 20.01 ?  117 ALA C N     1 
ATOM   3339 C CA    . ALA C 1 117 ? -6.626  7.585   28.735 1.00 19.45 ?  117 ALA C CA    1 
ATOM   3340 C C     . ALA C 1 117 ? -5.626  7.042   27.726 1.00 22.56 ?  117 ALA C C     1 
ATOM   3341 O O     . ALA C 1 117 ? -6.004  6.335   26.787 1.00 20.54 ?  117 ALA C O     1 
ATOM   3342 C CB    . ALA C 1 117 ? -6.900  6.535   29.819 1.00 21.29 ?  117 ALA C CB    1 
ATOM   3343 N N     . LYS C 1 118 ? -4.351  7.379   27.919 1.00 23.06 ?  118 LYS C N     1 
ATOM   3344 C CA    . LYS C 1 118 ? -3.299  6.885   27.043 1.00 16.83 ?  118 LYS C CA    1 
ATOM   3345 C C     . LYS C 1 118 ? -1.994  6.776   27.819 1.00 18.20 ?  118 LYS C C     1 
ATOM   3346 O O     . LYS C 1 118 ? -1.848  7.322   28.915 1.00 11.84 ?  118 LYS C O     1 
ATOM   3347 C CB    . LYS C 1 118 ? -3.126  7.770   25.803 1.00 20.00 ?  118 LYS C CB    1 
ATOM   3348 C CG    . LYS C 1 118 ? -2.642  9.177   26.074 1.00 28.47 ?  118 LYS C CG    1 
ATOM   3349 C CD    . LYS C 1 118 ? -2.073  9.786   24.804 1.00 35.77 ?  118 LYS C CD    1 
ATOM   3350 C CE    . LYS C 1 118 ? -2.237  11.291  24.781 1.00 34.94 ?  118 LYS C CE    1 
ATOM   3351 N NZ    . LYS C 1 118 ? -3.628  11.705  25.111 1.00 33.25 ?  118 LYS C NZ    1 
ATOM   3352 N N     . MET C 1 119 ? -1.046  6.048   27.233 1.00 20.64 ?  119 MET C N     1 
ATOM   3353 C CA    . MET C 1 119 ? 0.273   5.848   27.814 1.00 17.03 ?  119 MET C CA    1 
ATOM   3354 C C     . MET C 1 119 ? 1.330   6.321   26.830 1.00 14.42 ?  119 MET C C     1 
ATOM   3355 O O     . MET C 1 119 ? 1.298   5.952   25.651 1.00 14.42 ?  119 MET C O     1 
ATOM   3356 C CB    . MET C 1 119 ? 0.503   4.377   28.164 1.00 20.24 ?  119 MET C CB    1 
ATOM   3357 C CG    . MET C 1 119 ? 1.728   4.122   29.024 1.00 18.48 ?  119 MET C CG    1 
ATOM   3358 S SD    . MET C 1 119 ? 2.176   2.379   29.049 1.00 22.57 ?  119 MET C SD    1 
ATOM   3359 C CE    . MET C 1 119 ? 1.329   1.901   30.554 1.00 22.08 ?  119 MET C CE    1 
ATOM   3360 N N     . GLU C 1 120 ? 2.251   7.140   27.315 1.00 17.95 ?  120 GLU C N     1 
ATOM   3361 C CA    . GLU C 1 120 ? 3.371   7.606   26.510 1.00 21.36 ?  120 GLU C CA    1 
ATOM   3362 C C     . GLU C 1 120 ? 4.606   6.798   26.867 1.00 21.01 ?  120 GLU C C     1 
ATOM   3363 O O     . GLU C 1 120 ? 4.964   6.729   28.052 1.00 18.09 ?  120 GLU C O     1 
ATOM   3364 C CB    . GLU C 1 120 ? 3.632   9.089   26.767 1.00 18.55 ?  120 GLU C CB    1 
ATOM   3365 C CG    . GLU C 1 120 ? 2.702   10.045  26.029 1.00 20.79 ?  120 GLU C CG    1 
ATOM   3366 C CD    . GLU C 1 120 ? 2.795   9.927   24.521 1.00 21.61 ?  120 GLU C CD    1 
ATOM   3367 O OE1   . GLU C 1 120 ? 3.914   9.731   24.001 1.00 27.67 ?  120 GLU C OE1   1 
ATOM   3368 O OE2   . GLU C 1 120 ? 1.747   10.043  23.851 1.00 20.30 -1 120 GLU C OE2   1 
ATOM   3369 N N     . PRO C 1 121 ? 5.271   6.161   25.903 1.00 24.26 ?  121 PRO C N     1 
ATOM   3370 C CA    . PRO C 1 121 ? 6.443   5.344   26.239 1.00 19.06 ?  121 PRO C CA    1 
ATOM   3371 C C     . PRO C 1 121 ? 7.581   6.187   26.798 1.00 19.55 ?  121 PRO C C     1 
ATOM   3372 O O     . PRO C 1 121 ? 7.714   7.375   26.497 1.00 20.54 ?  121 PRO C O     1 
ATOM   3373 C CB    . PRO C 1 121 ? 6.825   4.700   24.899 1.00 21.04 ?  121 PRO C CB    1 
ATOM   3374 C CG    . PRO C 1 121 ? 6.229   5.584   23.859 1.00 26.36 ?  121 PRO C CG    1 
ATOM   3375 C CD    . PRO C 1 121 ? 4.968   6.137   24.460 1.00 23.72 ?  121 PRO C CD    1 
ATOM   3376 N N     . GLY C 1 122 ? 8.405   5.546   27.628 1.00 14.90 ?  122 GLY C N     1 
ATOM   3377 C CA    . GLY C 1 122 ? 9.558   6.187   28.223 1.00 18.65 ?  122 GLY C CA    1 
ATOM   3378 C C     . GLY C 1 122 ? 10.785  5.298   28.123 1.00 19.27 ?  122 GLY C C     1 
ATOM   3379 O O     . GLY C 1 122 ? 10.723  4.171   27.625 1.00 15.85 ?  122 GLY C O     1 
ATOM   3380 N N     . ILE C 1 123 ? 11.899  5.834   28.609 1.00 17.33 ?  123 ILE C N     1 
ATOM   3381 C CA    . ILE C 1 123 ? 13.169  5.117   28.599 1.00 20.04 ?  123 ILE C CA    1 
ATOM   3382 C C     . ILE C 1 123 ? 13.273  4.303   29.880 1.00 21.78 ?  123 ILE C C     1 
ATOM   3383 O O     . ILE C 1 123 ? 13.325  4.863   30.979 1.00 19.19 ?  123 ILE C O     1 
ATOM   3384 C CB    . ILE C 1 123 ? 14.354  6.081   28.456 1.00 18.76 ?  123 ILE C CB    1 
ATOM   3385 C CG1   . ILE C 1 123 ? 14.404  6.630   27.030 1.00 21.77 ?  123 ILE C CG1   1 
ATOM   3386 C CG2   . ILE C 1 123 ? 15.659  5.390   28.809 1.00 20.12 ?  123 ILE C CG2   1 
ATOM   3387 C CD1   . ILE C 1 123 ? 15.042  7.977   26.932 1.00 20.59 ?  123 ILE C CD1   1 
ATOM   3388 N N     . SER C 1 124 ? 13.313  2.983   29.737 1.00 15.52 ?  124 SER C N     1 
ATOM   3389 C CA    . SER C 1 124 ? 13.255  2.076   30.869 1.00 18.23 ?  124 SER C CA    1 
ATOM   3390 C C     . SER C 1 124 ? 14.659  1.677   31.314 1.00 17.63 ?  124 SER C C     1 
ATOM   3391 O O     . SER C 1 124 ? 15.667  2.051   30.710 1.00 17.61 ?  124 SER C O     1 
ATOM   3392 C CB    . SER C 1 124 ? 12.434  0.836   30.511 1.00 13.29 ?  124 SER C CB    1 
ATOM   3393 O OG    . SER C 1 124 ? 13.153  -0.017  29.642 1.00 17.33 ?  124 SER C OG    1 
ATOM   3394 N N     . ALA C 1 125 ? 14.724  0.908   32.403 1.00 19.43 ?  125 ALA C N     1 
ATOM   3395 C CA    . ALA C 1 125 ? 16.013  0.435   32.893 1.00 19.61 ?  125 ALA C CA    1 
ATOM   3396 C C     . ALA C 1 125 ? 16.657  -0.521  31.901 1.00 21.66 ?  125 ALA C C     1 
ATOM   3397 O O     . ALA C 1 125 ? 17.888  -0.559  31.784 1.00 20.17 ?  125 ALA C O     1 
ATOM   3398 C CB    . ALA C 1 125 ? 15.845  -0.241  34.253 1.00 16.87 ?  125 ALA C CB    1 
ATOM   3399 N N     . GLU C 1 126 ? 15.839  -1.292  31.179 1.00 18.62 ?  126 GLU C N     1 
ATOM   3400 C CA    . GLU C 1 126 ? 16.359  -2.165  30.133 1.00 20.64 ?  126 GLU C CA    1 
ATOM   3401 C C     . GLU C 1 126 ? 17.039  -1.353  29.038 1.00 21.15 ?  126 GLU C C     1 
ATOM   3402 O O     . GLU C 1 126 ? 18.128  -1.705  28.569 1.00 24.65 ?  126 GLU C O     1 
ATOM   3403 C CB    . GLU C 1 126 ? 15.226  -3.001  29.548 1.00 25.33 ?  126 GLU C CB    1 
ATOM   3404 C CG    . GLU C 1 126 ? 15.595  -3.753  28.286 1.00 27.48 ?  126 GLU C CG    1 
ATOM   3405 C CD    . GLU C 1 126 ? 14.391  -4.343  27.590 1.00 28.95 ?  126 GLU C CD    1 
ATOM   3406 O OE1   . GLU C 1 126 ? 13.650  -5.117  28.230 1.00 32.40 ?  126 GLU C OE1   1 
ATOM   3407 O OE2   . GLU C 1 126 ? 14.178  -4.024  26.400 1.00 36.48 -1 126 GLU C OE2   1 
ATOM   3408 N N     . ALA C 1 127 ? 16.400  -0.260  28.612 1.00 23.91 ?  127 ALA C N     1 
ATOM   3409 C CA    . ALA C 1 127 ? 16.996  0.600   27.595 1.00 21.47 ?  127 ALA C CA    1 
ATOM   3410 C C     . ALA C 1 127 ? 18.314  1.185   28.081 1.00 17.28 ?  127 ALA C C     1 
ATOM   3411 O O     . ALA C 1 127 ? 19.253  1.363   27.294 1.00 21.13 ?  127 ALA C O     1 
ATOM   3412 C CB    . ALA C 1 127 ? 16.021  1.712   27.209 1.00 17.68 ?  127 ALA C CB    1 
ATOM   3413 N N     . CYS C 1 128 ? 18.404  1.489   29.379 1.00 18.69 ?  128 CYS C N     1 
ATOM   3414 C CA    . CYS C 1 128 ? 19.647  2.015   29.931 1.00 14.28 ?  128 CYS C CA    1 
ATOM   3415 C C     . CYS C 1 128 ? 20.739  0.954   29.923 1.00 20.40 ?  128 CYS C C     1 
ATOM   3416 O O     . CYS C 1 128 ? 21.920  1.268   29.724 1.00 18.61 ?  128 CYS C O     1 
ATOM   3417 C CB    . CYS C 1 128 ? 19.414  2.530   31.349 1.00 12.03 ?  128 CYS C CB    1 
ATOM   3418 S SG    . CYS C 1 128 ? 18.381  4.009   31.458 1.00 18.24 ?  128 CYS C SG    1 
ATOM   3419 N N     . LEU C 1 129 ? 20.359  -0.311  30.135 1.00 15.82 ?  129 LEU C N     1 
ATOM   3420 C CA    . LEU C 1 129 ? 21.337  -1.391  30.232 1.00 18.87 ?  129 LEU C CA    1 
ATOM   3421 C C     . LEU C 1 129 ? 22.046  -1.615  28.901 1.00 22.20 ?  129 LEU C C     1 
ATOM   3422 O O     . LEU C 1 129 ? 23.280  -1.707  28.854 1.00 17.48 ?  129 LEU C O     1 
ATOM   3423 C CB    . LEU C 1 129 ? 20.651  -2.670  30.714 1.00 15.71 ?  129 LEU C CB    1 
ATOM   3424 C CG    . LEU C 1 129 ? 21.482  -3.931  30.953 1.00 19.15 ?  129 LEU C CG    1 
ATOM   3425 C CD1   . LEU C 1 129 ? 20.788  -4.801  31.983 1.00 17.78 ?  129 LEU C CD1   1 
ATOM   3426 C CD2   . LEU C 1 129 ? 21.667  -4.714  29.664 1.00 18.72 ?  129 LEU C CD2   1 
ATOM   3427 N N     . TRP C 1 130 ? 21.276  -1.743  27.815 1.00 15.59 ?  130 TRP C N     1 
ATOM   3428 C CA    . TRP C 1 130 ? 21.861  -1.903  26.486 1.00 19.88 ?  130 TRP C CA    1 
ATOM   3429 C C     . TRP C 1 130 ? 22.923  -0.843  26.218 1.00 18.78 ?  130 TRP C C     1 
ATOM   3430 O O     . TRP C 1 130 ? 24.012  -1.144  25.718 1.00 18.23 ?  130 TRP C O     1 
ATOM   3431 C CB    . TRP C 1 130 ? 20.772  -1.837  25.416 1.00 22.08 ?  130 TRP C CB    1 
ATOM   3432 C CG    . TRP C 1 130 ? 19.620  -2.789  25.612 1.00 24.16 ?  130 TRP C CG    1 
ATOM   3433 C CD1   . TRP C 1 130 ? 18.294  -2.491  25.490 1.00 22.01 ?  130 TRP C CD1   1 
ATOM   3434 C CD2   . TRP C 1 130 ? 19.688  -4.186  25.940 1.00 20.08 ?  130 TRP C CD2   1 
ATOM   3435 N NE1   . TRP C 1 130 ? 17.533  -3.608  25.730 1.00 20.03 ?  130 TRP C NE1   1 
ATOM   3436 C CE2   . TRP C 1 130 ? 18.363  -4.661  26.010 1.00 21.95 ?  130 TRP C CE2   1 
ATOM   3437 C CE3   . TRP C 1 130 ? 20.737  -5.080  26.185 1.00 17.60 ?  130 TRP C CE3   1 
ATOM   3438 C CZ2   . TRP C 1 130 ? 18.059  -5.986  26.317 1.00 21.71 ?  130 TRP C CZ2   1 
ATOM   3439 C CZ3   . TRP C 1 130 ? 20.431  -6.397  26.491 1.00 20.70 ?  130 TRP C CZ3   1 
ATOM   3440 C CH2   . TRP C 1 130 ? 19.103  -6.836  26.552 1.00 19.54 ?  130 TRP C CH2   1 
ATOM   3441 N N     . ALA C 1 131 ? 22.617  0.413   26.549 1.00 16.39 ?  131 ALA C N     1 
ATOM   3442 C CA    . ALA C 1 131 ? 23.553  1.503   26.292 1.00 18.66 ?  131 ALA C CA    1 
ATOM   3443 C C     . ALA C 1 131 ? 24.761  1.426   27.217 1.00 19.56 ?  131 ALA C C     1 
ATOM   3444 O O     . ALA C 1 131 ? 25.899  1.623   26.775 1.00 17.09 ?  131 ALA C O     1 
ATOM   3445 C CB    . ALA C 1 131 ? 22.845  2.849   26.445 1.00 23.11 ?  131 ALA C CB    1 
ATOM   3446 N N     . ASP C 1 132 ? 24.535  1.141   28.504 1.00 16.99 ?  132 ASP C N     1 
ATOM   3447 C CA    . ASP C 1 132 ? 25.630  1.168   29.471 1.00 18.92 ?  132 ASP C CA    1 
ATOM   3448 C C     . ASP C 1 132 ? 26.598  0.015   29.249 1.00 19.12 ?  132 ASP C C     1 
ATOM   3449 O O     . ASP C 1 132 ? 27.810  0.170   29.432 1.00 17.83 ?  132 ASP C O     1 
ATOM   3450 C CB    . ASP C 1 132 ? 25.079  1.130   30.896 1.00 14.37 ?  132 ASP C CB    1 
ATOM   3451 C CG    . ASP C 1 132 ? 24.601  2.483   31.367 1.00 17.55 ?  132 ASP C CG    1 
ATOM   3452 O OD1   . ASP C 1 132 ? 24.938  3.490   30.710 1.00 21.63 ?  132 ASP C OD1   1 
ATOM   3453 O OD2   . ASP C 1 132 ? 23.898  2.545   32.396 1.00 15.64 -1 132 ASP C OD2   1 
ATOM   3454 N N     . LEU C 1 133 ? 26.089  -1.148  28.865 1.00 18.54 ?  133 LEU C N     1 
ATOM   3455 C CA    . LEU C 1 133 ? 26.915  -2.335  28.709 1.00 23.46 ?  133 LEU C CA    1 
ATOM   3456 C C     . LEU C 1 133 ? 27.362  -2.551  27.271 1.00 23.18 ?  133 LEU C C     1 
ATOM   3457 O O     . LEU C 1 133 ? 28.107  -3.500  27.004 1.00 23.10 ?  133 LEU C O     1 
ATOM   3458 C CB    . LEU C 1 133 ? 26.165  -3.572  29.220 1.00 20.71 ?  133 LEU C CB    1 
ATOM   3459 C CG    . LEU C 1 133 ? 26.240  -3.785  30.740 1.00 29.16 ?  133 LEU C CG    1 
ATOM   3460 C CD1   . LEU C 1 133 ? 25.496  -2.701  31.516 1.00 21.22 ?  133 LEU C CD1   1 
ATOM   3461 C CD2   . LEU C 1 133 ? 25.731  -5.152  31.115 1.00 23.93 ?  133 LEU C CD2   1 
ATOM   3462 N N     . GLY C 1 134 ? 26.938  -1.692  26.351 1.00 18.72 ?  134 GLY C N     1 
ATOM   3463 C CA    . GLY C 1 134 ? 27.247  -1.879  24.942 1.00 21.73 ?  134 GLY C CA    1 
ATOM   3464 C C     . GLY C 1 134 ? 26.716  -3.177  24.382 1.00 22.51 ?  134 GLY C C     1 
ATOM   3465 O O     . GLY C 1 134 ? 27.400  -3.836  23.588 1.00 22.41 ?  134 GLY C O     1 
ATOM   3466 N N     . ILE C 1 135 ? 25.510  -3.568  24.782 1.00 22.03 ?  135 ILE C N     1 
ATOM   3467 C CA    . ILE C 1 135 ? 24.875  -4.798  24.324 1.00 17.63 ?  135 ILE C CA    1 
ATOM   3468 C C     . ILE C 1 135 ? 23.644  -4.433  23.507 1.00 20.62 ?  135 ILE C C     1 
ATOM   3469 O O     . ILE C 1 135 ? 22.827  -3.609  23.932 1.00 19.22 ?  135 ILE C O     1 
ATOM   3470 C CB    . ILE C 1 135 ? 24.494  -5.712  25.502 1.00 19.24 ?  135 ILE C CB    1 
ATOM   3471 C CG1   . ILE C 1 135 ? 25.725  -6.033  26.352 1.00 21.67 ?  135 ILE C CG1   1 
ATOM   3472 C CG2   . ILE C 1 135 ? 23.830  -6.986  25.001 1.00 19.99 ?  135 ILE C CG2   1 
ATOM   3473 C CD1   . ILE C 1 135 ? 25.418  -6.881  27.566 1.00 25.80 ?  135 ILE C CD1   1 
ATOM   3474 N N     . ASP C 1 136 ? 23.515  -5.043  22.334 1.00 19.43 ?  136 ASP C N     1 
ATOM   3475 C CA    . ASP C 1 136 ? 22.316  -4.911  21.521 1.00 22.35 ?  136 ASP C CA    1 
ATOM   3476 C C     . ASP C 1 136 ? 21.446  -6.135  21.755 1.00 21.68 ?  136 ASP C C     1 
ATOM   3477 O O     . ASP C 1 136 ? 21.927  -7.261  21.557 1.00 22.60 ?  136 ASP C O     1 
ATOM   3478 C CB    . ASP C 1 136 ? 22.696  -4.785  20.044 1.00 22.26 ?  136 ASP C CB    1 
ATOM   3479 C CG    . ASP C 1 136 ? 21.495  -4.656  19.112 1.00 18.12 ?  136 ASP C CG    1 
ATOM   3480 O OD1   . ASP C 1 136 ? 20.336  -4.820  19.541 1.00 19.05 ?  136 ASP C OD1   1 
ATOM   3481 O OD2   . ASP C 1 136 ? 21.724  -4.377  17.916 1.00 23.74 -1 136 ASP C OD2   1 
ATOM   3482 N N     . PRO C 1 137 ? 20.190  -5.983  22.187 1.00 21.95 ?  137 PRO C N     1 
ATOM   3483 C CA    . PRO C 1 137 ? 19.340  -7.168  22.389 1.00 22.23 ?  137 PRO C CA    1 
ATOM   3484 C C     . PRO C 1 137 ? 19.180  -8.012  21.140 1.00 22.51 ?  137 PRO C C     1 
ATOM   3485 O O     . PRO C 1 137 ? 18.814  -9.190  21.244 1.00 18.44 ?  137 PRO C O     1 
ATOM   3486 C CB    . PRO C 1 137 ? 17.999  -6.569  22.842 1.00 23.92 ?  137 PRO C CB    1 
ATOM   3487 C CG    . PRO C 1 137 ? 18.035  -5.141  22.389 1.00 20.27 ?  137 PRO C CG    1 
ATOM   3488 C CD    . PRO C 1 137 ? 19.474  -4.731  22.484 1.00 19.57 ?  137 PRO C CD    1 
ATOM   3489 N N     . GLY C 1 138 ? 19.450  -7.451  19.958 1.00 23.40 ?  138 GLY C N     1 
ATOM   3490 C CA    . GLY C 1 138 ? 19.294  -8.196  18.723 1.00 19.25 ?  138 GLY C CA    1 
ATOM   3491 C C     . GLY C 1 138 ? 20.448  -9.115  18.400 1.00 20.47 ?  138 GLY C C     1 
ATOM   3492 O O     . GLY C 1 138 ? 20.288  -10.021 17.574 1.00 20.72 ?  138 GLY C O     1 
ATOM   3493 N N     . ASN C 1 139 ? 21.604  -8.892  19.032 1.00 18.67 ?  139 ASN C N     1 
ATOM   3494 C CA    . ASN C 1 139 ? 22.816  -9.636  18.704 1.00 26.77 ?  139 ASN C CA    1 
ATOM   3495 C C     . ASN C 1 139 ? 22.565  -11.140 18.741 1.00 22.55 ?  139 ASN C C     1 
ATOM   3496 O O     . ASN C 1 139 ? 22.786  -11.850 17.754 1.00 18.15 ?  139 ASN C O     1 
ATOM   3497 C CB    . ASN C 1 139 ? 23.945  -9.249  19.663 1.00 24.86 ?  139 ASN C CB    1 
ATOM   3498 C CG    . ASN C 1 139 ? 25.305  -9.724  19.184 1.00 27.36 ?  139 ASN C CG    1 
ATOM   3499 O OD1   . ASN C 1 139 ? 25.922  -10.591 19.802 1.00 27.28 ?  139 ASN C OD1   1 
ATOM   3500 N ND2   . ASN C 1 139 ? 25.781  -9.150  18.085 1.00 25.17 ?  139 ASN C ND2   1 
ATOM   3501 N N     . SER C 1 140 ? 22.094  -11.645 19.884 1.00 19.95 ?  140 SER C N     1 
ATOM   3502 C CA    . SER C 1 140 ? 21.750  -13.056 20.020 1.00 19.53 ?  140 SER C CA    1 
ATOM   3503 C C     . SER C 1 140 ? 20.391  -13.245 20.686 1.00 18.76 ?  140 SER C C     1 
ATOM   3504 O O     . SER C 1 140 ? 20.091  -14.341 21.167 1.00 22.73 ?  140 SER C O     1 
ATOM   3505 C CB    . SER C 1 140 ? 22.827  -13.809 20.806 1.00 22.00 ?  140 SER C CB    1 
ATOM   3506 O OG    . SER C 1 140 ? 23.018  -13.239 22.088 1.00 21.29 ?  140 SER C OG    1 
ATOM   3507 N N     . GLY C 1 141 ? 19.561  -12.207 20.716 1.00 16.36 ?  141 GLY C N     1 
ATOM   3508 C CA    . GLY C 1 141 ? 18.242  -12.294 21.303 1.00 18.69 ?  141 GLY C CA    1 
ATOM   3509 C C     . GLY C 1 141 ? 18.225  -11.862 22.760 1.00 18.23 ?  141 GLY C C     1 
ATOM   3510 O O     . GLY C 1 141 ? 19.255  -11.660 23.405 1.00 17.82 ?  141 GLY C O     1 
ATOM   3511 N N     . HIS C 1 142 ? 17.012  -11.724 23.288 1.00 18.62 ?  142 HIS C N     1 
ATOM   3512 C CA    . HIS C 1 142 ? 16.806  -11.106 24.592 1.00 22.13 ?  142 HIS C CA    1 
ATOM   3513 C C     . HIS C 1 142 ? 15.572  -11.709 25.249 1.00 17.72 ?  142 HIS C C     1 
ATOM   3514 O O     . HIS C 1 142 ? 14.533  -11.866 24.600 1.00 15.92 ?  142 HIS C O     1 
ATOM   3515 C CB    . HIS C 1 142 ? 16.658  -9.584  24.446 1.00 21.28 ?  142 HIS C CB    1 
ATOM   3516 C CG    . HIS C 1 142 ? 15.920  -8.925  25.569 1.00 23.43 ?  142 HIS C CG    1 
ATOM   3517 N ND1   . HIS C 1 142 ? 15.006  -7.916  25.356 1.00 22.44 ?  142 HIS C ND1   1 
ATOM   3518 C CD2   . HIS C 1 142 ? 15.980  -9.100  26.911 1.00 22.56 ?  142 HIS C CD2   1 
ATOM   3519 C CE1   . HIS C 1 142 ? 14.517  -7.515  26.515 1.00 28.94 ?  142 HIS C CE1   1 
ATOM   3520 N NE2   . HIS C 1 142 ? 15.090  -8.218  27.475 1.00 29.62 ?  142 HIS C NE2   1 
ATOM   3521 N N     . GLN C 1 143 ? 15.697  -12.043 26.532 1.00 17.09 ?  143 GLN C N     1 
ATOM   3522 C CA    . GLN C 1 143 ? 14.592  -12.521 27.349 1.00 20.42 ?  143 GLN C CA    1 
ATOM   3523 C C     . GLN C 1 143 ? 14.539  -11.725 28.642 1.00 20.43 ?  143 GLN C C     1 
ATOM   3524 O O     . GLN C 1 143 ? 15.571  -11.482 29.272 1.00 19.45 ?  143 GLN C O     1 
ATOM   3525 C CB    . GLN C 1 143 ? 14.730  -13.997 27.694 1.00 18.37 ?  143 GLN C CB    1 
ATOM   3526 C CG    . GLN C 1 143 ? 14.616  -14.961 26.546 1.00 25.48 ?  143 GLN C CG    1 
ATOM   3527 C CD    . GLN C 1 143 ? 14.684  -16.382 27.043 1.00 24.39 ?  143 GLN C CD    1 
ATOM   3528 O OE1   . GLN C 1 143 ? 13.753  -17.169 26.872 1.00 36.54 ?  143 GLN C OE1   1 
ATOM   3529 N NE2   . GLN C 1 143 ? 15.782  -16.707 27.707 1.00 24.63 ?  143 GLN C NE2   1 
ATOM   3530 N N     . SER C 1 144 ? 13.333  -11.334 29.041 1.00 15.20 ?  144 SER C N     1 
ATOM   3531 C CA    . SER C 1 144 ? 13.100  -10.679 30.321 1.00 18.94 ?  144 SER C CA    1 
ATOM   3532 C C     . SER C 1 144 ? 12.032  -11.437 31.096 1.00 17.67 ?  144 SER C C     1 
ATOM   3533 O O     . SER C 1 144 ? 10.994  -11.806 30.536 1.00 19.67 ?  144 SER C O     1 
ATOM   3534 C CB    . SER C 1 144 ? 12.673  -9.220  30.125 1.00 16.74 ?  144 SER C CB    1 
ATOM   3535 O OG    . SER C 1 144 ? 13.796  -8.391  29.886 1.00 20.12 ?  144 SER C OG    1 
ATOM   3536 N N     . PHE C 1 145 ? 12.294  -11.671 32.380 1.00 16.18 ?  145 PHE C N     1 
ATOM   3537 C CA    . PHE C 1 145 ? 11.296  -12.176 33.311 1.00 20.68 ?  145 PHE C CA    1 
ATOM   3538 C C     . PHE C 1 145 ? 11.447  -11.452 34.638 1.00 20.29 ?  145 PHE C C     1 
ATOM   3539 O O     . PHE C 1 145 ? 12.541  -11.020 35.003 1.00 22.06 ?  145 PHE C O     1 
ATOM   3540 C CB    . PHE C 1 145 ? 11.427  -13.684 33.576 1.00 20.46 ?  145 PHE C CB    1 
ATOM   3541 C CG    . PHE C 1 145 ? 11.482  -14.529 32.338 1.00 20.25 ?  145 PHE C CG    1 
ATOM   3542 C CD1   . PHE C 1 145 ? 10.319  -15.016 31.766 1.00 21.19 ?  145 PHE C CD1   1 
ATOM   3543 C CD2   . PHE C 1 145 ? 12.695  -14.856 31.761 1.00 18.09 ?  145 PHE C CD2   1 
ATOM   3544 C CE1   . PHE C 1 145 ? 10.365  -15.804 30.634 1.00 23.38 ?  145 PHE C CE1   1 
ATOM   3545 C CE2   . PHE C 1 145 ? 12.749  -15.644 30.626 1.00 21.80 ?  145 PHE C CE2   1 
ATOM   3546 C CZ    . PHE C 1 145 ? 11.582  -16.117 30.062 1.00 25.11 ?  145 PHE C CZ    1 
ATOM   3547 N N     . GLU C 1 146 ? 10.340  -11.331 35.362 1.00 20.00 ?  146 GLU C N     1 
ATOM   3548 C CA    . GLU C 1 146 ? 10.419  -10.967 36.767 1.00 20.11 ?  146 GLU C CA    1 
ATOM   3549 C C     . GLU C 1 146 ? 10.939  -12.168 37.549 1.00 18.72 ?  146 GLU C C     1 
ATOM   3550 O O     . GLU C 1 146 ? 10.518  -13.304 37.317 1.00 16.61 ?  146 GLU C O     1 
ATOM   3551 C CB    . GLU C 1 146 ? 9.046   -10.522 37.280 1.00 19.91 ?  146 GLU C CB    1 
ATOM   3552 C CG    . GLU C 1 146 ? 9.089   -9.588  38.483 1.00 19.87 ?  146 GLU C CG    1 
ATOM   3553 C CD    . GLU C 1 146 ? 8.843   -10.293 39.802 1.00 28.68 ?  146 GLU C CD    1 
ATOM   3554 O OE1   . GLU C 1 146 ? 8.469   -11.482 39.783 1.00 19.35 ?  146 GLU C OE1   1 
ATOM   3555 O OE2   . GLU C 1 146 ? 9.011   -9.649  40.858 1.00 21.20 -1 146 GLU C OE2   1 
ATOM   3556 N N     . ALA C 1 147 ? 11.876  -11.913 38.465 1.00 14.93 ?  147 ALA C N     1 
ATOM   3557 C CA    . ALA C 1 147 ? 12.624  -13.000 39.092 1.00 20.11 ?  147 ALA C CA    1 
ATOM   3558 C C     . ALA C 1 147 ? 11.705  -13.971 39.824 1.00 20.78 ?  147 ALA C C     1 
ATOM   3559 O O     . ALA C 1 147 ? 11.851  -15.192 39.699 1.00 17.14 ?  147 ALA C O     1 
ATOM   3560 C CB    . ALA C 1 147 ? 13.677  -12.433 40.044 1.00 11.82 ?  147 ALA C CB    1 
ATOM   3561 N N     . SER C 1 148 ? 10.746  -13.448 40.591 1.00 19.98 ?  148 SER C N     1 
ATOM   3562 C CA    . SER C 1 148 ? 9.876   -14.320 41.376 1.00 23.52 ?  148 SER C CA    1 
ATOM   3563 C C     . SER C 1 148 ? 8.964   -15.152 40.481 1.00 24.45 ?  148 SER C C     1 
ATOM   3564 O O     . SER C 1 148 ? 8.716   -16.330 40.769 1.00 19.09 ?  148 SER C O     1 
ATOM   3565 C CB    . SER C 1 148 ? 9.059   -13.494 42.369 1.00 23.20 ?  148 SER C CB    1 
ATOM   3566 O OG    . SER C 1 148 ? 9.881   -13.020 43.420 1.00 20.85 ?  148 SER C OG    1 
ATOM   3567 N N     . GLN C 1 149 ? 8.439   -14.555 39.405 1.00 20.82 ?  149 GLN C N     1 
ATOM   3568 C CA    . GLN C 1 149 ? 7.627   -15.326 38.467 1.00 22.38 ?  149 GLN C CA    1 
ATOM   3569 C C     . GLN C 1 149 ? 8.441   -16.459 37.855 1.00 22.03 ?  149 GLN C C     1 
ATOM   3570 O O     . GLN C 1 149 ? 7.917   -17.554 37.616 1.00 25.73 ?  149 GLN C O     1 
ATOM   3571 C CB    . GLN C 1 149 ? 7.063   -14.422 37.372 1.00 22.40 ?  149 GLN C CB    1 
ATOM   3572 C CG    . GLN C 1 149 ? 6.154   -15.153 36.393 1.00 25.05 ?  149 GLN C CG    1 
ATOM   3573 C CD    . GLN C 1 149 ? 5.808   -14.324 35.176 1.00 29.10 ?  149 GLN C CD    1 
ATOM   3574 O OE1   . GLN C 1 149 ? 6.396   -14.498 34.110 1.00 22.61 ?  149 GLN C OE1   1 
ATOM   3575 N NE2   . GLN C 1 149 ? 4.846   -13.421 35.325 1.00 28.83 ?  149 GLN C NE2   1 
ATOM   3576 N N     . PHE C 1 150 ? 9.728   -16.212 37.593 1.00 19.47 ?  150 PHE C N     1 
ATOM   3577 C CA    . PHE C 1 150 ? 10.598  -17.252 37.055 1.00 23.59 ?  150 PHE C CA    1 
ATOM   3578 C C     . PHE C 1 150 ? 10.713  -18.422 38.021 1.00 22.84 ?  150 PHE C C     1 
ATOM   3579 O O     . PHE C 1 150 ? 10.888  -19.569 37.594 1.00 18.43 ?  150 PHE C O     1 
ATOM   3580 C CB    . PHE C 1 150 ? 11.980  -16.667 36.755 1.00 21.41 ?  150 PHE C CB    1 
ATOM   3581 C CG    . PHE C 1 150 ? 12.906  -17.612 36.045 1.00 21.14 ?  150 PHE C CG    1 
ATOM   3582 C CD1   . PHE C 1 150 ? 12.909  -17.690 34.663 1.00 22.01 ?  150 PHE C CD1   1 
ATOM   3583 C CD2   . PHE C 1 150 ? 13.774  -18.421 36.760 1.00 17.74 ?  150 PHE C CD2   1 
ATOM   3584 C CE1   . PHE C 1 150 ? 13.763  -18.558 34.006 1.00 27.05 ?  150 PHE C CE1   1 
ATOM   3585 C CE2   . PHE C 1 150 ? 14.626  -19.292 36.110 1.00 23.34 ?  150 PHE C CE2   1 
ATOM   3586 C CZ    . PHE C 1 150 ? 14.621  -19.360 34.732 1.00 21.46 ?  150 PHE C CZ    1 
ATOM   3587 N N     . MET C 1 151 ? 10.613  -18.149 39.321 1.00 22.46 ?  151 MET C N     1 
ATOM   3588 C CA    . MET C 1 151 ? 10.704  -19.178 40.347 1.00 22.33 ?  151 MET C CA    1 
ATOM   3589 C C     . MET C 1 151 ? 9.355   -19.843 40.585 1.00 21.24 ?  151 MET C C     1 
ATOM   3590 O O     . MET C 1 151 ? 9.283   -21.065 40.755 1.00 26.96 ?  151 MET C O     1 
ATOM   3591 C CB    . MET C 1 151 ? 11.222  -18.573 41.656 1.00 19.13 ?  151 MET C CB    1 
ATOM   3592 C CG    . MET C 1 151 ? 12.715  -18.293 41.671 1.00 19.49 ?  151 MET C CG    1 
ATOM   3593 S SD    . MET C 1 151 ? 13.249  -17.438 43.168 1.00 25.07 ?  151 MET C SD    1 
ATOM   3594 C CE    . MET C 1 151 ? 13.176  -18.767 44.367 1.00 23.10 ?  151 MET C CE    1 
ATOM   3595 N N     . PHE C 1 152 ? 8.282   -19.051 40.580 1.00 25.86 ?  152 PHE C N     1 
ATOM   3596 C CA    . PHE C 1 152 ? 6.971   -19.549 40.974 1.00 27.39 ?  152 PHE C CA    1 
ATOM   3597 C C     . PHE C 1 152 ? 6.289   -20.310 39.847 1.00 30.30 ?  152 PHE C C     1 
ATOM   3598 O O     . PHE C 1 152 ? 5.458   -21.185 40.111 1.00 29.88 ?  152 PHE C O     1 
ATOM   3599 C CB    . PHE C 1 152 ? 6.084   -18.386 41.416 1.00 22.19 ?  152 PHE C CB    1 
ATOM   3600 C CG    . PHE C 1 152 ? 6.531   -17.727 42.689 1.00 26.66 ?  152 PHE C CG    1 
ATOM   3601 C CD1   . PHE C 1 152 ? 7.436   -18.351 43.529 1.00 29.30 ?  152 PHE C CD1   1 
ATOM   3602 C CD2   . PHE C 1 152 ? 6.058   -16.473 43.034 1.00 26.20 ?  152 PHE C CD2   1 
ATOM   3603 C CE1   . PHE C 1 152 ? 7.853   -17.743 44.697 1.00 27.91 ?  152 PHE C CE1   1 
ATOM   3604 C CE2   . PHE C 1 152 ? 6.473   -15.859 44.200 1.00 28.63 ?  152 PHE C CE2   1 
ATOM   3605 C CZ    . PHE C 1 152 ? 7.371   -16.494 45.030 1.00 30.86 ?  152 PHE C CZ    1 
ATOM   3606 N N     . PHE C 1 153 ? 6.623   -19.996 38.599 1.00 23.10 ?  153 PHE C N     1 
ATOM   3607 C CA    . PHE C 1 153 ? 5.981   -20.592 37.441 1.00 25.52 ?  153 PHE C CA    1 
ATOM   3608 C C     . PHE C 1 153 ? 7.046   -21.167 36.519 1.00 27.85 ?  153 PHE C C     1 
ATOM   3609 O O     . PHE C 1 153 ? 8.246   -20.967 36.717 1.00 26.17 ?  153 PHE C O     1 
ATOM   3610 C CB    . PHE C 1 153 ? 5.112   -19.565 36.704 1.00 27.80 ?  153 PHE C CB    1 
ATOM   3611 C CG    . PHE C 1 153 ? 4.082   -18.909 37.582 1.00 29.51 ?  153 PHE C CG    1 
ATOM   3612 C CD1   . PHE C 1 153 ? 2.920   -19.578 37.929 1.00 33.55 ?  153 PHE C CD1   1 
ATOM   3613 C CD2   . PHE C 1 153 ? 4.289   -17.634 38.083 1.00 31.30 ?  153 PHE C CD2   1 
ATOM   3614 C CE1   . PHE C 1 153 ? 1.978   -18.979 38.741 1.00 37.83 ?  153 PHE C CE1   1 
ATOM   3615 C CE2   . PHE C 1 153 ? 3.350   -17.033 38.900 1.00 27.62 ?  153 PHE C CE2   1 
ATOM   3616 C CZ    . PHE C 1 153 ? 2.193   -17.707 39.230 1.00 36.50 ?  153 PHE C CZ    1 
ATOM   3617 N N     . ASN C 1 154 ? 6.594   -21.886 35.496 1.00 24.37 ?  154 ASN C N     1 
ATOM   3618 C CA    . ASN C 1 154 ? 7.491   -22.626 34.609 1.00 28.43 ?  154 ASN C CA    1 
ATOM   3619 C C     . ASN C 1 154 ? 7.893   -21.737 33.439 1.00 24.39 ?  154 ASN C C     1 
ATOM   3620 O O     . ASN C 1 154 ? 7.109   -21.506 32.516 1.00 26.27 ?  154 ASN C O     1 
ATOM   3621 C CB    . ASN C 1 154 ? 6.837   -23.919 34.134 1.00 27.66 ?  154 ASN C CB    1 
ATOM   3622 C CG    . ASN C 1 154 ? 6.584   -24.891 35.269 1.00 31.52 ?  154 ASN C CG    1 
ATOM   3623 O OD1   . ASN C 1 154 ? 7.483   -25.185 36.059 1.00 33.30 ?  154 ASN C OD1   1 
ATOM   3624 N ND2   . ASN C 1 154 ? 5.361   -25.398 35.356 1.00 31.78 ?  154 ASN C ND2   1 
ATOM   3625 N N     . HIS C 1 155 ? 9.126   -21.246 33.477 1.00 24.27 ?  155 HIS C N     1 
ATOM   3626 C CA    . HIS C 1 155 ? 9.723   -20.510 32.377 1.00 25.03 ?  155 HIS C CA    1 
ATOM   3627 C C     . HIS C 1 155 ? 11.003  -21.214 31.956 1.00 25.22 ?  155 HIS C C     1 
ATOM   3628 O O     . HIS C 1 155 ? 11.802  -21.632 32.799 1.00 26.18 ?  155 HIS C O     1 
ATOM   3629 C CB    . HIS C 1 155 ? 10.020  -19.061 32.766 1.00 25.48 ?  155 HIS C CB    1 
ATOM   3630 C CG    . HIS C 1 155 ? 8.811   -18.180 32.769 1.00 25.30 ?  155 HIS C CG    1 
ATOM   3631 N ND1   . HIS C 1 155 ? 7.997   -18.031 31.667 1.00 26.03 ?  155 HIS C ND1   1 
ATOM   3632 C CD2   . HIS C 1 155 ? 8.276   -17.402 33.739 1.00 25.75 ?  155 HIS C CD2   1 
ATOM   3633 C CE1   . HIS C 1 155 ? 7.015   -17.197 31.958 1.00 24.24 ?  155 HIS C CE1   1 
ATOM   3634 N NE2   . HIS C 1 155 ? 7.160   -16.802 33.209 1.00 24.69 ?  155 HIS C NE2   1 
ATOM   3635 N N     . VAL C 1 156 ? 11.195  -21.346 30.648 1.00 27.20 ?  156 VAL C N     1 
ATOM   3636 C CA    . VAL C 1 156 ? 12.376  -21.978 30.079 1.00 29.02 ?  156 VAL C CA    1 
ATOM   3637 C C     . VAL C 1 156 ? 13.172  -20.900 29.349 1.00 28.21 ?  156 VAL C C     1 
ATOM   3638 O O     . VAL C 1 156 ? 12.717  -20.385 28.314 1.00 21.47 ?  156 VAL C O     1 
ATOM   3639 C CB    . VAL C 1 156 ? 12.001  -23.131 29.136 1.00 34.75 ?  156 VAL C CB    1 
ATOM   3640 C CG1   . VAL C 1 156 ? 13.197  -23.540 28.286 1.00 33.87 ?  156 VAL C CG1   1 
ATOM   3641 C CG2   . VAL C 1 156 ? 11.469  -24.314 29.929 1.00 34.17 ?  156 VAL C CG2   1 
ATOM   3642 N N     . PRO C 1 157 ? 14.347  -20.517 29.840 1.00 23.15 ?  157 PRO C N     1 
ATOM   3643 C CA    . PRO C 1 157 ? 15.159  -19.531 29.128 1.00 23.40 ?  157 PRO C CA    1 
ATOM   3644 C C     . PRO C 1 157 ? 15.956  -20.153 27.992 1.00 27.92 ?  157 PRO C C     1 
ATOM   3645 O O     . PRO C 1 157 ? 16.346  -21.321 28.032 1.00 26.85 ?  157 PRO C O     1 
ATOM   3646 C CB    . PRO C 1 157 ? 16.082  -18.980 30.221 1.00 25.20 ?  157 PRO C CB    1 
ATOM   3647 C CG    . PRO C 1 157 ? 16.245  -20.122 31.170 1.00 24.53 ?  157 PRO C CG    1 
ATOM   3648 C CD    . PRO C 1 157 ? 14.968  -20.936 31.109 1.00 28.25 ?  157 PRO C CD    1 
ATOM   3649 N N     . ASP C 1 158 ? 16.189  -19.340 26.964 1.00 24.25 ?  158 ASP C N     1 
ATOM   3650 C CA    . ASP C 1 158 ? 17.066  -19.698 25.860 1.00 24.42 ?  158 ASP C CA    1 
ATOM   3651 C C     . ASP C 1 158 ? 18.483  -19.279 26.240 1.00 29.57 ?  158 ASP C C     1 
ATOM   3652 O O     . ASP C 1 158 ? 18.750  -18.070 26.328 1.00 22.17 ?  158 ASP C O     1 
ATOM   3653 C CB    . ASP C 1 158 ? 16.611  -19.003 24.576 1.00 21.57 ?  158 ASP C CB    1 
ATOM   3654 C CG    . ASP C 1 158 ? 17.481  -19.326 23.372 1.00 20.58 ?  158 ASP C CG    1 
ATOM   3655 O OD1   . ASP C 1 158 ? 18.566  -19.929 23.522 1.00 22.21 ?  158 ASP C OD1   1 
ATOM   3656 O OD2   . ASP C 1 158 ? 17.066  -18.973 22.248 1.00 23.51 -1 158 ASP C OD2   1 
ATOM   3657 N N     . PRO C 1 159 ? 19.404  -20.214 26.461 1.00 20.78 ?  159 PRO C N     1 
ATOM   3658 C CA    . PRO C 1 159 ? 20.725  -19.849 26.989 1.00 22.91 ?  159 PRO C CA    1 
ATOM   3659 C C     . PRO C 1 159 ? 21.649  -19.198 25.975 1.00 23.11 ?  159 PRO C C     1 
ATOM   3660 O O     . PRO C 1 159 ? 22.810  -18.930 26.307 1.00 23.27 ?  159 PRO C O     1 
ATOM   3661 C CB    . PRO C 1 159 ? 21.288  -21.199 27.454 1.00 22.40 ?  159 PRO C CB    1 
ATOM   3662 C CG    . PRO C 1 159 ? 20.655  -22.196 26.538 1.00 26.02 ?  159 PRO C CG    1 
ATOM   3663 C CD    . PRO C 1 159 ? 19.286  -21.661 26.197 1.00 24.86 ?  159 PRO C CD    1 
ATOM   3664 N N     . THR C 1 160 ? 21.178  -18.932 24.758 1.00 22.36 ?  160 THR C N     1 
ATOM   3665 C CA    . THR C 1 160 ? 21.958  -18.181 23.786 1.00 23.50 ?  160 THR C CA    1 
ATOM   3666 C C     . THR C 1 160 ? 21.688  -16.686 23.845 1.00 20.78 ?  160 THR C C     1 
ATOM   3667 O O     . THR C 1 160 ? 22.418  -15.910 23.218 1.00 20.97 ?  160 THR C O     1 
ATOM   3668 C CB    . THR C 1 160 ? 21.687  -18.684 22.364 1.00 25.75 ?  160 THR C CB    1 
ATOM   3669 O OG1   . THR C 1 160 ? 20.302  -18.505 22.052 1.00 19.16 ?  160 THR C OG1   1 
ATOM   3670 C CG2   . THR C 1 160 ? 22.051  -20.155 22.231 1.00 23.25 ?  160 THR C CG2   1 
ATOM   3671 N N     . THR C 1 161 ? 20.669  -16.266 24.582 1.00 22.22 ?  161 THR C N     1 
ATOM   3672 C CA    . THR C 1 161 ? 20.246  -14.877 24.628 1.00 19.93 ?  161 THR C CA    1 
ATOM   3673 C C     . THR C 1 161 ? 20.849  -14.172 25.836 1.00 21.57 ?  161 THR C C     1 
ATOM   3674 O O     . THR C 1 161 ? 21.444  -14.788 26.723 1.00 22.59 ?  161 THR C O     1 
ATOM   3675 C CB    . THR C 1 161 ? 18.717  -14.785 24.681 1.00 20.53 ?  161 THR C CB    1 
ATOM   3676 O OG1   . THR C 1 161 ? 18.251  -15.398 25.889 1.00 23.68 ?  161 THR C OG1   1 
ATOM   3677 C CG2   . THR C 1 161 ? 18.098  -15.498 23.490 1.00 19.00 ?  161 THR C CG2   1 
ATOM   3678 N N     . HIS C 1 162 ? 20.694  -12.853 25.850 1.00 19.23 ?  162 HIS C N     1 
ATOM   3679 C CA    . HIS C 1 162 ? 20.900  -12.077 27.065 1.00 19.88 ?  162 HIS C CA    1 
ATOM   3680 C C     . HIS C 1 162 ? 19.630  -12.133 27.902 1.00 21.65 ?  162 HIS C C     1 
ATOM   3681 O O     . HIS C 1 162 ? 18.565  -11.684 27.464 1.00 21.08 ?  162 HIS C O     1 
ATOM   3682 C CB    . HIS C 1 162 ? 21.281  -10.639 26.726 1.00 21.17 ?  162 HIS C CB    1 
ATOM   3683 C CG    . HIS C 1 162 ? 22.719  -10.479 26.345 1.00 22.78 ?  162 HIS C CG    1 
ATOM   3684 N ND1   . HIS C 1 162 ? 23.159  -10.551 25.040 1.00 22.88 ?  162 HIS C ND1   1 
ATOM   3685 C CD2   . HIS C 1 162 ? 23.821  -10.266 27.102 1.00 17.36 ?  162 HIS C CD2   1 
ATOM   3686 C CE1   . HIS C 1 162 ? 24.470  -10.384 25.010 1.00 24.39 ?  162 HIS C CE1   1 
ATOM   3687 N NE2   . HIS C 1 162 ? 24.895  -10.208 26.248 1.00 18.03 ?  162 HIS C NE2   1 
ATOM   3688 N N     . LEU C 1 163 ? 19.738  -12.696 29.099 1.00 20.05 ?  163 LEU C N     1 
ATOM   3689 C CA    . LEU C 1 163 ? 18.598  -12.925 29.974 1.00 19.85 ?  163 LEU C CA    1 
ATOM   3690 C C     . LEU C 1 163 ? 18.609  -11.917 31.114 1.00 18.28 ?  163 LEU C C     1 
ATOM   3691 O O     . LEU C 1 163 ? 19.643  -11.709 31.758 1.00 18.50 ?  163 LEU C O     1 
ATOM   3692 C CB    . LEU C 1 163 ? 18.619  -14.354 30.523 1.00 16.65 ?  163 LEU C CB    1 
ATOM   3693 C CG    . LEU C 1 163 ? 17.682  -14.692 31.678 1.00 23.68 ?  163 LEU C CG    1 
ATOM   3694 C CD1   . LEU C 1 163 ? 16.231  -14.558 31.250 1.00 18.50 ?  163 LEU C CD1   1 
ATOM   3695 C CD2   . LEU C 1 163 ? 17.964  -16.098 32.185 1.00 21.08 ?  163 LEU C CD2   1 
ATOM   3696 N N     . LEU C 1 164 ? 17.458  -11.301 31.362 1.00 20.42 ?  164 LEU C N     1 
ATOM   3697 C CA    . LEU C 1 164 ? 17.274  -10.358 32.455 1.00 18.89 ?  164 LEU C CA    1 
ATOM   3698 C C     . LEU C 1 164 ? 16.285  -10.940 33.454 1.00 17.97 ?  164 LEU C C     1 
ATOM   3699 O O     . LEU C 1 164 ? 15.230  -11.450 33.064 1.00 15.87 ?  164 LEU C O     1 
ATOM   3700 C CB    . LEU C 1 164 ? 16.755  -9.011  31.945 1.00 20.36 ?  164 LEU C CB    1 
ATOM   3701 C CG    . LEU C 1 164 ? 17.687  -8.145  31.100 1.00 21.39 ?  164 LEU C CG    1 
ATOM   3702 C CD1   . LEU C 1 164 ? 16.986  -6.860  30.691 1.00 22.95 ?  164 LEU C CD1   1 
ATOM   3703 C CD2   . LEU C 1 164 ? 18.950  -7.841  31.876 1.00 20.77 ?  164 LEU C CD2   1 
ATOM   3704 N N     . LEU C 1 165 ? 16.628  -10.864 34.736 1.00 20.16 ?  165 LEU C N     1 
ATOM   3705 C CA    . LEU C 1 165 ? 15.693  -11.144 35.820 1.00 18.90 ?  165 LEU C CA    1 
ATOM   3706 C C     . LEU C 1 165 ? 15.468  -9.843  36.581 1.00 18.95 ?  165 LEU C C     1 
ATOM   3707 O O     . LEU C 1 165 ? 16.367  -9.363  37.281 1.00 16.32 ?  165 LEU C O     1 
ATOM   3708 C CB    . LEU C 1 165 ? 16.217  -12.247 36.740 1.00 16.68 ?  165 LEU C CB    1 
ATOM   3709 C CG    . LEU C 1 165 ? 16.407  -13.632 36.116 1.00 16.08 ?  165 LEU C CG    1 
ATOM   3710 C CD1   . LEU C 1 165 ? 16.682  -14.672 37.192 1.00 20.71 ?  165 LEU C CD1   1 
ATOM   3711 C CD2   . LEU C 1 165 ? 15.195  -14.026 35.284 1.00 15.49 ?  165 LEU C CD2   1 
ATOM   3712 N N     . TRP C 1 166 ? 14.273  -9.278  36.443 1.00 15.53 ?  166 TRP C N     1 
ATOM   3713 C CA    . TRP C 1 166 ? 13.951  -8.024  37.103 1.00 18.65 ?  166 TRP C CA    1 
ATOM   3714 C C     . TRP C 1 166 ? 13.533  -8.284  38.547 1.00 19.91 ?  166 TRP C C     1 
ATOM   3715 O O     . TRP C 1 166 ? 13.082  -9.377  38.904 1.00 15.65 ?  166 TRP C O     1 
ATOM   3716 C CB    . TRP C 1 166 ? 12.829  -7.284  36.365 1.00 18.37 ?  166 TRP C CB    1 
ATOM   3717 C CG    . TRP C 1 166 ? 13.137  -6.901  34.936 1.00 16.92 ?  166 TRP C CG    1 
ATOM   3718 C CD1   . TRP C 1 166 ? 13.563  -7.726  33.934 1.00 17.58 ?  166 TRP C CD1   1 
ATOM   3719 C CD2   . TRP C 1 166 ? 13.019  -5.594  34.355 1.00 13.85 ?  166 TRP C CD2   1 
ATOM   3720 N NE1   . TRP C 1 166 ? 13.726  -7.011  32.769 1.00 14.22 ?  166 TRP C NE1   1 
ATOM   3721 C CE2   . TRP C 1 166 ? 13.398  -5.701  33.002 1.00 17.25 ?  166 TRP C CE2   1 
ATOM   3722 C CE3   . TRP C 1 166 ? 12.633  -4.342  34.850 1.00 18.41 ?  166 TRP C CE3   1 
ATOM   3723 C CZ2   . TRP C 1 166 ? 13.402  -4.607  32.138 1.00 21.43 ?  166 TRP C CZ2   1 
ATOM   3724 C CZ3   . TRP C 1 166 ? 12.638  -3.258  33.990 1.00 20.03 ?  166 TRP C CZ3   1 
ATOM   3725 C CH2   . TRP C 1 166 ? 13.021  -3.398  32.649 1.00 20.76 ?  166 TRP C CH2   1 
ATOM   3726 N N     . GLN C 1 167 ? 13.678  -7.249  39.377 1.00 19.72 ?  167 GLN C N     1 
ATOM   3727 C CA    . GLN C 1 167 ? 13.311  -7.312  40.793 1.00 20.76 ?  167 GLN C CA    1 
ATOM   3728 C C     . GLN C 1 167 ? 13.988  -8.489  41.481 1.00 21.31 ?  167 GLN C C     1 
ATOM   3729 O O     . GLN C 1 167 ? 13.379  -9.220  42.265 1.00 17.07 ?  167 GLN C O     1 
ATOM   3730 C CB    . GLN C 1 167 ? 11.796  -7.377  40.947 1.00 20.99 ?  167 GLN C CB    1 
ATOM   3731 C CG    . GLN C 1 167 ? 11.127  -6.470  39.957 1.00 22.81 ?  167 GLN C CG    1 
ATOM   3732 C CD    . GLN C 1 167 ? 9.680   -6.271  40.240 1.00 33.67 ?  167 GLN C CD    1 
ATOM   3733 O OE1   . GLN C 1 167 ? 8.951   -7.204  40.558 1.00 29.30 ?  167 GLN C OE1   1 
ATOM   3734 N NE2   . GLN C 1 167 ? 9.249   -5.043  40.136 1.00 26.60 ?  167 GLN C NE2   1 
ATOM   3735 N N     . ILE C 1 168 ? 15.275  -8.662  41.175 1.00 17.37 ?  168 ILE C N     1 
ATOM   3736 C CA    . ILE C 1 168 ? 16.049  -9.775  41.710 1.00 18.58 ?  168 ILE C CA    1 
ATOM   3737 C C     . ILE C 1 168 ? 16.150  -9.687  43.226 1.00 19.56 ?  168 ILE C C     1 
ATOM   3738 O O     . ILE C 1 168 ? 16.279  -10.710 43.908 1.00 20.09 ?  168 ILE C O     1 
ATOM   3739 C CB    . ILE C 1 168 ? 17.435  -9.796  41.035 1.00 12.46 ?  168 ILE C CB    1 
ATOM   3740 C CG1   . ILE C 1 168 ? 18.252  -11.005 41.487 1.00 13.86 ?  168 ILE C CG1   1 
ATOM   3741 C CG2   . ILE C 1 168 ? 18.182  -8.493  41.294 1.00 14.67 ?  168 ILE C CG2   1 
ATOM   3742 C CD1   . ILE C 1 168 ? 17.699  -12.316 40.991 1.00 15.57 ?  168 ILE C CD1   1 
ATOM   3743 N N     . ALA C 1 169 ? 16.068  -8.475  43.781 1.00 17.62 ?  169 ALA C N     1 
ATOM   3744 C CA    . ALA C 1 169 ? 16.258  -8.280  45.214 1.00 21.03 ?  169 ALA C CA    1 
ATOM   3745 C C     . ALA C 1 169 ? 15.138  -8.892  46.043 1.00 20.88 ?  169 ALA C C     1 
ATOM   3746 O O     . ALA C 1 169 ? 15.319  -9.093  47.247 1.00 18.21 ?  169 ALA C O     1 
ATOM   3747 C CB    . ALA C 1 169 ? 16.384  -6.789  45.535 1.00 22.60 ?  169 ALA C CB    1 
ATOM   3748 N N     . ILE C 1 170 ? 13.980  -9.153  45.441 1.00 17.88 ?  170 ILE C N     1 
ATOM   3749 C CA    . ILE C 1 170 ? 12.860  -9.772  46.135 1.00 22.25 ?  170 ILE C CA    1 
ATOM   3750 C C     . ILE C 1 170 ? 12.534  -11.144 45.549 1.00 17.30 ?  170 ILE C C     1 
ATOM   3751 O O     . ILE C 1 170 ? 11.428  -11.643 45.715 1.00 15.70 ?  170 ILE C O     1 
ATOM   3752 C CB    . ILE C 1 170 ? 11.620  -8.858  46.122 1.00 20.38 ?  170 ILE C CB    1 
ATOM   3753 C CG1   . ILE C 1 170 ? 11.259  -8.467  44.687 1.00 22.17 ?  170 ILE C CG1   1 
ATOM   3754 C CG2   . ILE C 1 170 ? 11.854  -7.619  46.977 1.00 21.17 ?  170 ILE C CG2   1 
ATOM   3755 C CD1   . ILE C 1 170 ? 9.966   -7.695  44.581 1.00 26.64 ?  170 ILE C CD1   1 
ATOM   3756 N N     . ALA C 1 171 ? 13.493  -11.750 44.855 1.00 21.00 ?  171 ALA C N     1 
ATOM   3757 C CA    . ALA C 1 171 ? 13.267  -13.032 44.200 1.00 20.94 ?  171 ALA C CA    1 
ATOM   3758 C C     . ALA C 1 171 ? 12.834  -14.079 45.216 1.00 22.24 ?  171 ALA C C     1 
ATOM   3759 O O     . ALA C 1 171 ? 13.584  -14.410 46.139 1.00 26.24 ?  171 ALA C O     1 
ATOM   3760 C CB    . ALA C 1 171 ? 14.536  -13.482 43.474 1.00 20.15 ?  171 ALA C CB    1 
ATOM   3761 N N     . GLY C 1 172 ? 11.619  -14.595 45.045 1.00 19.81 ?  172 GLY C N     1 
ATOM   3762 C CA    . GLY C 1 172 ? 11.091  -15.618 45.921 1.00 26.11 ?  172 GLY C CA    1 
ATOM   3763 C C     . GLY C 1 172 ? 10.318  -15.104 47.112 1.00 24.98 ?  172 GLY C C     1 
ATOM   3764 O O     . GLY C 1 172 ? 9.856   -15.915 47.926 1.00 27.37 ?  172 GLY C O     1 
ATOM   3765 N N     . GLU C 1 173 ? 10.160  -13.790 47.242 1.00 21.44 ?  173 GLU C N     1 
ATOM   3766 C CA    . GLU C 1 173 ? 9.448   -13.184 48.368 1.00 31.99 ?  173 GLU C CA    1 
ATOM   3767 C C     . GLU C 1 173 ? 7.954   -13.254 48.066 1.00 28.21 ?  173 GLU C C     1 
ATOM   3768 O O     . GLU C 1 173 ? 7.358   -12.321 47.523 1.00 34.71 ?  173 GLU C O     1 
ATOM   3769 C CB    . GLU C 1 173 ? 9.921   -11.752 48.590 1.00 26.45 ?  173 GLU C CB    1 
ATOM   3770 C CG    . GLU C 1 173 ? 9.716   -11.211 49.998 1.00 24.86 ?  173 GLU C CG    1 
ATOM   3771 C CD    . GLU C 1 173 ? 8.262   -11.183 50.418 1.00 30.25 ?  173 GLU C CD    1 
ATOM   3772 O OE1   . GLU C 1 173 ? 7.584   -10.168 50.148 1.00 33.21 ?  173 GLU C OE1   1 
ATOM   3773 O OE2   . GLU C 1 173 ? 7.798   -12.174 51.018 1.00 29.66 -1 173 GLU C OE2   1 
ATOM   3774 N N     . HIS C 1 174 ? 7.341   -14.385 48.428 1.00 27.19 ?  174 HIS C N     1 
ATOM   3775 C CA    . HIS C 1 174 ? 6.015   -14.729 47.922 1.00 31.40 ?  174 HIS C CA    1 
ATOM   3776 C C     . HIS C 1 174 ? 4.894   -13.916 48.556 1.00 25.53 ?  174 HIS C C     1 
ATOM   3777 O O     . HIS C 1 174 ? 3.805   -13.846 47.977 1.00 27.65 ?  174 HIS C O     1 
ATOM   3778 C CB    . HIS C 1 174 ? 5.747   -16.220 48.138 1.00 28.51 ?  174 HIS C CB    1 
ATOM   3779 C CG    . HIS C 1 174 ? 5.588   -16.599 49.576 1.00 30.30 ?  174 HIS C CG    1 
ATOM   3780 N ND1   . HIS C 1 174 ? 6.655   -16.942 50.378 1.00 25.90 ?  174 HIS C ND1   1 
ATOM   3781 C CD2   . HIS C 1 174 ? 4.488   -16.674 50.361 1.00 27.26 ?  174 HIS C CD2   1 
ATOM   3782 C CE1   . HIS C 1 174 ? 6.218   -17.216 51.594 1.00 25.51 ?  174 HIS C CE1   1 
ATOM   3783 N NE2   . HIS C 1 174 ? 4.906   -17.062 51.610 1.00 21.61 ?  174 HIS C NE2   1 
ATOM   3784 N N     . THR C 1 175 ? 5.121   -13.303 49.720 1.00 31.11 ?  175 THR C N     1 
ATOM   3785 C CA    . THR C 1 175 ? 4.029   -12.613 50.401 1.00 31.84 ?  175 THR C CA    1 
ATOM   3786 C C     . THR C 1 175 ? 3.818   -11.205 49.866 1.00 27.44 ?  175 THR C C     1 
ATOM   3787 O O     . THR C 1 175 ? 2.738   -10.633 50.066 1.00 25.65 ?  175 THR C O     1 
ATOM   3788 C CB    . THR C 1 175 ? 4.278   -12.546 51.913 1.00 29.69 ?  175 THR C CB    1 
ATOM   3789 O OG1   . THR C 1 175 ? 5.322   -11.605 52.191 1.00 29.46 ?  175 THR C OG1   1 
ATOM   3790 C CG2   . THR C 1 175 ? 4.661   -13.910 52.463 1.00 32.44 ?  175 THR C CG2   1 
ATOM   3791 N N     . LEU C 1 176 ? 4.827   -10.642 49.197 1.00 28.65 ?  176 LEU C N     1 
ATOM   3792 C CA    . LEU C 1 176 ? 4.773   -9.277  48.673 1.00 36.84 ?  176 LEU C CA    1 
ATOM   3793 C C     . LEU C 1 176 ? 4.546   -8.265  49.795 1.00 34.93 ?  176 LEU C C     1 
ATOM   3794 O O     . LEU C 1 176 ? 3.877   -7.245  49.618 1.00 34.67 ?  176 LEU C O     1 
ATOM   3795 C CB    . LEU C 1 176 ? 3.708   -9.147  47.581 1.00 33.69 ?  176 LEU C CB    1 
ATOM   3796 C CG    . LEU C 1 176 ? 3.667   -10.330 46.601 1.00 38.75 ?  176 LEU C CG    1 
ATOM   3797 C CD1   . LEU C 1 176 ? 2.638   -10.090 45.531 1.00 41.58 ?  176 LEU C CD1   1 
ATOM   3798 C CD2   . LEU C 1 176 ? 5.031   -10.589 45.976 1.00 37.29 ?  176 LEU C CD2   1 
ATOM   3799 N N     . THR C 1 177 ? 5.118   -8.554  50.965 1.00 34.73 ?  177 THR C N     1 
ATOM   3800 C CA    . THR C 1 177 ? 5.057   -7.673  52.118 1.00 34.66 ?  177 THR C CA    1 
ATOM   3801 C C     . THR C 1 177 ? 6.427   -7.216  52.595 1.00 31.56 ?  177 THR C C     1 
ATOM   3802 O O     . THR C 1 177 ? 6.500   -6.317  53.440 1.00 33.67 ?  177 THR C O     1 
ATOM   3803 C CB    . THR C 1 177 ? 4.341   -8.360  53.290 1.00 32.03 ?  177 THR C CB    1 
ATOM   3804 O OG1   . THR C 1 177 ? 5.199   -9.366  53.842 1.00 26.14 ?  177 THR C OG1   1 
ATOM   3805 C CG2   . THR C 1 177 ? 3.039   -8.999  52.838 1.00 24.22 ?  177 THR C CG2   1 
ATOM   3806 N N     . GLN C 1 178 ? 7.505   -7.791  52.075 1.00 30.96 ?  178 GLN C N     1 
ATOM   3807 C CA    . GLN C 1 178 ? 8.853   -7.467  52.508 1.00 34.61 ?  178 GLN C CA    1 
ATOM   3808 C C     . GLN C 1 178 ? 9.567   -6.683  51.416 1.00 39.16 ?  178 GLN C C     1 
ATOM   3809 O O     . GLN C 1 178 ? 9.246   -6.804  50.230 1.00 32.95 ?  178 GLN C O     1 
ATOM   3810 C CB    . GLN C 1 178 ? 9.656   -8.732  52.834 1.00 33.04 ?  178 GLN C CB    1 
ATOM   3811 C CG    . GLN C 1 178 ? 9.037   -9.657  53.882 1.00 36.27 ?  178 GLN C CG    1 
ATOM   3812 C CD    . GLN C 1 178 ? 9.207   -9.160  55.308 1.00 40.18 ?  178 GLN C CD    1 
ATOM   3813 O OE1   . GLN C 1 178 ? 9.456   -7.979  55.547 1.00 42.97 ?  178 GLN C OE1   1 
ATOM   3814 N NE2   . GLN C 1 178 ? 9.089   -10.073 56.265 1.00 36.64 ?  178 GLN C NE2   1 
ATOM   3815 N N     . PHE C 1 179 ? 10.552  -5.883  51.825 1.00 40.75 ?  179 PHE C N     1 
ATOM   3816 C CA    . PHE C 1 179 ? 11.287  -5.060  50.875 1.00 37.42 ?  179 PHE C CA    1 
ATOM   3817 C C     . PHE C 1 179 ? 12.412  -5.826  50.191 1.00 38.46 ?  179 PHE C C     1 
ATOM   3818 O O     . PHE C 1 179 ? 12.932  -5.359  49.172 1.00 37.36 ?  179 PHE C O     1 
ATOM   3819 C CB    . PHE C 1 179 ? 11.869  -3.832  51.584 1.00 46.12 ?  179 PHE C CB    1 
ATOM   3820 C CG    . PHE C 1 179 ? 10.833  -2.846  52.063 1.00 55.71 ?  179 PHE C CG    1 
ATOM   3821 C CD1   . PHE C 1 179 ? 9.777   -2.468  51.249 1.00 57.10 ?  179 PHE C CD1   1 
ATOM   3822 C CD2   . PHE C 1 179 ? 10.925  -2.291  53.331 1.00 52.38 ?  179 PHE C CD2   1 
ATOM   3823 C CE1   . PHE C 1 179 ? 8.829   -1.560  51.693 1.00 48.95 ?  179 PHE C CE1   1 
ATOM   3824 C CE2   . PHE C 1 179 ? 9.982   -1.385  53.779 1.00 54.89 ?  179 PHE C CE2   1 
ATOM   3825 C CZ    . PHE C 1 179 ? 8.935   -1.019  52.960 1.00 51.05 ?  179 PHE C CZ    1 
ATOM   3826 N N     . HIS C 1 180 ? 12.794  -6.986  50.725 1.00 33.64 ?  180 HIS C N     1 
ATOM   3827 C CA    . HIS C 1 180 ? 13.898  -7.775  50.193 1.00 32.94 ?  180 HIS C CA    1 
ATOM   3828 C C     . HIS C 1 180 ? 13.660  -9.250  50.488 1.00 26.84 ?  180 HIS C C     1 
ATOM   3829 O O     . HIS C 1 180 ? 12.859  -9.607  51.356 1.00 28.62 ?  180 HIS C O     1 
ATOM   3830 C CB    . HIS C 1 180 ? 15.237  -7.330  50.783 1.00 37.41 ?  180 HIS C CB    1 
ATOM   3831 C CG    . HIS C 1 180 ? 15.280  -7.390  52.277 1.00 38.66 ?  180 HIS C CG    1 
ATOM   3832 N ND1   . HIS C 1 180 ? 16.159  -8.197  52.964 1.00 42.57 ?  180 HIS C ND1   1 
ATOM   3833 C CD2   . HIS C 1 180 ? 14.570  -6.721  53.216 1.00 40.60 ?  180 HIS C CD2   1 
ATOM   3834 C CE1   . HIS C 1 180 ? 15.979  -8.036  54.262 1.00 39.70 ?  180 HIS C CE1   1 
ATOM   3835 N NE2   . HIS C 1 180 ? 15.021  -7.145  54.442 1.00 44.13 ?  180 HIS C NE2   1 
ATOM   3836 N N     . THR C 1 181 ? 14.370  -10.109 49.754 1.00 26.77 ?  181 THR C N     1 
ATOM   3837 C CA    . THR C 1 181 ? 14.260  -11.551 49.932 1.00 28.84 ?  181 THR C CA    1 
ATOM   3838 C C     . THR C 1 181 ? 15.327  -12.021 50.927 1.00 30.46 ?  181 THR C C     1 
ATOM   3839 O O     . THR C 1 181 ? 15.858  -11.227 51.705 1.00 32.33 ?  181 THR C O     1 
ATOM   3840 C CB    . THR C 1 181 ? 14.370  -12.254 48.577 1.00 26.85 ?  181 THR C CB    1 
ATOM   3841 O OG1   . THR C 1 181 ? 14.166  -13.657 48.753 1.00 26.80 ?  181 THR C OG1   1 
ATOM   3842 C CG2   . THR C 1 181 ? 15.748  -12.040 47.963 1.00 22.04 ?  181 THR C CG2   1 
ATOM   3843 N N     . SER C 1 182 ? 15.654  -13.312 50.922 1.00 27.06 ?  182 SER C N     1 
ATOM   3844 C CA    . SER C 1 182 ? 16.658  -13.874 51.817 1.00 29.74 ?  182 SER C CA    1 
ATOM   3845 C C     . SER C 1 182 ? 17.720  -14.606 51.007 1.00 27.37 ?  182 SER C C     1 
ATOM   3846 O O     . SER C 1 182 ? 17.537  -14.901 49.823 1.00 26.19 ?  182 SER C O     1 
ATOM   3847 C CB    . SER C 1 182 ? 16.040  -14.828 52.851 1.00 33.35 ?  182 SER C CB    1 
ATOM   3848 O OG    . SER C 1 182 ? 15.999  -16.152 52.365 1.00 40.48 ?  182 SER C OG    1 
ATOM   3849 N N     . SER C 1 183 ? 18.852  -14.883 51.659 1.00 34.97 ?  183 SER C N     1 
ATOM   3850 C CA    . SER C 1 183 ? 19.969  -15.516 50.963 1.00 34.76 ?  183 SER C CA    1 
ATOM   3851 C C     . SER C 1 183 ? 19.668  -16.965 50.595 1.00 31.95 ?  183 SER C C     1 
ATOM   3852 O O     . SER C 1 183 ? 20.186  -17.465 49.589 1.00 33.37 ?  183 SER C O     1 
ATOM   3853 C CB    . SER C 1 183 ? 21.234  -15.445 51.821 1.00 31.87 ?  183 SER C CB    1 
ATOM   3854 O OG    . SER C 1 183 ? 21.076  -16.166 53.029 1.00 39.28 ?  183 SER C OG    1 
ATOM   3855 N N     . ASP C 1 184 ? 18.839  -17.655 51.386 1.00 33.66 ?  184 ASP C N     1 
ATOM   3856 C CA    . ASP C 1 184 ? 18.473  -19.022 51.028 1.00 35.97 ?  184 ASP C CA    1 
ATOM   3857 C C     . ASP C 1 184 ? 17.549  -19.048 49.817 1.00 33.13 ?  184 ASP C C     1 
ATOM   3858 O O     . ASP C 1 184 ? 17.583  -20.009 49.038 1.00 22.13 ?  184 ASP C O     1 
ATOM   3859 C CB    . ASP C 1 184 ? 17.841  -19.747 52.217 1.00 38.69 ?  184 ASP C CB    1 
ATOM   3860 C CG    . ASP C 1 184 ? 16.915  -18.867 53.012 1.00 45.78 ?  184 ASP C CG    1 
ATOM   3861 O OD1   . ASP C 1 184 ? 17.398  -17.876 53.602 1.00 43.11 ?  184 ASP C OD1   1 
ATOM   3862 O OD2   . ASP C 1 184 ? 15.703  -19.167 53.060 1.00 51.57 -1 184 ASP C OD2   1 
ATOM   3863 N N     . ARG C 1 185 ? 16.713  -18.016 49.650 1.00 26.76 ?  185 ARG C N     1 
ATOM   3864 C CA    . ARG C 1 185 ? 15.878  -17.932 48.455 1.00 31.26 ?  185 ARG C CA    1 
ATOM   3865 C C     . ARG C 1 185 ? 16.742  -17.777 47.212 1.00 28.07 ?  185 ARG C C     1 
ATOM   3866 O O     . ARG C 1 185 ? 16.500  -18.418 46.184 1.00 23.18 ?  185 ARG C O     1 
ATOM   3867 C CB    . ARG C 1 185 ? 14.920  -16.746 48.556 1.00 29.53 ?  185 ARG C CB    1 
ATOM   3868 C CG    . ARG C 1 185 ? 14.301  -16.514 49.916 1.00 43.07 ?  185 ARG C CG    1 
ATOM   3869 C CD    . ARG C 1 185 ? 13.407  -17.641 50.363 1.00 40.17 ?  185 ARG C CD    1 
ATOM   3870 N NE    . ARG C 1 185 ? 12.044  -17.424 49.896 1.00 46.57 ?  185 ARG C NE    1 
ATOM   3871 C CZ    . ARG C 1 185 ? 10.992  -18.116 50.312 1.00 45.65 ?  185 ARG C CZ    1 
ATOM   3872 N NH1   . ARG C 1 185 ? 11.111  -19.089 51.202 1.00 38.08 ?  185 ARG C NH1   1 
ATOM   3873 N NH2   . ARG C 1 185 ? 9.789   -17.830 49.820 1.00 42.77 ?  185 ARG C NH2   1 
ATOM   3874 N N     . LEU C 1 186 ? 17.757  -16.914 47.293 1.00 25.49 ?  186 LEU C N     1 
ATOM   3875 C CA    . LEU C 1 186 ? 18.638  -16.680 46.157 1.00 23.98 ?  186 LEU C CA    1 
ATOM   3876 C C     . LEU C 1 186 ? 19.475  -17.912 45.845 1.00 25.34 ?  186 LEU C C     1 
ATOM   3877 O O     . LEU C 1 186 ? 19.832  -18.140 44.682 1.00 28.50 ?  186 LEU C O     1 
ATOM   3878 C CB    . LEU C 1 186 ? 19.529  -15.470 46.433 1.00 23.86 ?  186 LEU C CB    1 
ATOM   3879 C CG    . LEU C 1 186 ? 18.810  -14.113 46.409 1.00 26.48 ?  186 LEU C CG    1 
ATOM   3880 C CD1   . LEU C 1 186 ? 19.625  -13.059 47.136 1.00 25.36 ?  186 LEU C CD1   1 
ATOM   3881 C CD2   . LEU C 1 186 ? 18.501  -13.668 44.985 1.00 20.96 ?  186 LEU C CD2   1 
ATOM   3882 N N     . GLN C 1 187 ? 19.795  -18.713 46.866 1.00 28.60 ?  187 GLN C N     1 
ATOM   3883 C CA    . GLN C 1 187 ? 20.510  -19.963 46.633 1.00 25.22 ?  187 GLN C CA    1 
ATOM   3884 C C     . GLN C 1 187 ? 19.637  -20.966 45.891 1.00 24.10 ?  187 GLN C C     1 
ATOM   3885 O O     . GLN C 1 187 ? 20.145  -21.747 45.076 1.00 22.30 ?  187 GLN C O     1 
ATOM   3886 C CB    . GLN C 1 187 ? 20.989  -20.547 47.963 1.00 25.98 ?  187 GLN C CB    1 
ATOM   3887 C CG    . GLN C 1 187 ? 21.681  -21.901 47.856 1.00 31.89 ?  187 GLN C CG    1 
ATOM   3888 C CD    . GLN C 1 187 ? 22.901  -21.869 46.952 1.00 32.51 ?  187 GLN C CD    1 
ATOM   3889 O OE1   . GLN C 1 187 ? 23.663  -20.901 46.948 1.00 34.56 ?  187 GLN C OE1   1 
ATOM   3890 N NE2   . GLN C 1 187 ? 23.095  -22.935 46.185 1.00 31.13 ?  187 GLN C NE2   1 
ATOM   3891 N N     . ILE C 1 188 ? 18.328  -20.959 46.156 1.00 26.28 ?  188 ILE C N     1 
ATOM   3892 C CA    . ILE C 1 188 ? 17.421  -21.828 45.414 1.00 28.52 ?  188 ILE C CA    1 
ATOM   3893 C C     . ILE C 1 188 ? 17.328  -21.369 43.966 1.00 27.01 ?  188 ILE C C     1 
ATOM   3894 O O     . ILE C 1 188 ? 17.241  -22.189 43.041 1.00 27.67 ?  188 ILE C O     1 
ATOM   3895 C CB    . ILE C 1 188 ? 16.041  -21.865 46.098 1.00 28.85 ?  188 ILE C CB    1 
ATOM   3896 C CG1   . ILE C 1 188 ? 16.074  -22.807 47.307 1.00 21.71 ?  188 ILE C CG1   1 
ATOM   3897 C CG2   . ILE C 1 188 ? 14.950  -22.285 45.125 1.00 25.47 ?  188 ILE C CG2   1 
ATOM   3898 C CD1   . ILE C 1 188 ? 14.868  -22.680 48.211 1.00 23.68 ?  188 ILE C CD1   1 
ATOM   3899 N N     . LEU C 1 189 ? 17.356  -20.052 43.745 1.00 23.80 ?  189 LEU C N     1 
ATOM   3900 C CA    . LEU C 1 189 ? 17.388  -19.526 42.384 1.00 28.22 ?  189 LEU C CA    1 
ATOM   3901 C C     . LEU C 1 189 ? 18.628  -20.012 41.645 1.00 21.94 ?  189 LEU C C     1 
ATOM   3902 O O     . LEU C 1 189 ? 18.549  -20.417 40.478 1.00 22.11 ?  189 LEU C O     1 
ATOM   3903 C CB    . LEU C 1 189 ? 17.353  -18.000 42.412 1.00 23.89 ?  189 LEU C CB    1 
ATOM   3904 C CG    . LEU C 1 189 ? 17.380  -17.280 41.064 1.00 28.77 ?  189 LEU C CG    1 
ATOM   3905 C CD1   . LEU C 1 189 ? 16.335  -17.847 40.108 1.00 23.98 ?  189 LEU C CD1   1 
ATOM   3906 C CD2   . LEU C 1 189 ? 17.182  -15.792 41.261 1.00 20.74 ?  189 LEU C CD2   1 
ATOM   3907 N N     . VAL C 1 190 ? 19.782  -19.986 42.317 1.00 24.81 ?  190 VAL C N     1 
ATOM   3908 C CA    . VAL C 1 190 ? 21.031  -20.395 41.683 1.00 23.44 ?  190 VAL C CA    1 
ATOM   3909 C C     . VAL C 1 190 ? 20.957  -21.859 41.277 1.00 27.81 ?  190 VAL C C     1 
ATOM   3910 O O     . VAL C 1 190 ? 21.398  -22.245 40.186 1.00 29.11 ?  190 VAL C O     1 
ATOM   3911 C CB    . VAL C 1 190 ? 22.220  -20.122 42.624 1.00 26.82 ?  190 VAL C CB    1 
ATOM   3912 C CG1   . VAL C 1 190 ? 23.465  -20.856 42.157 1.00 21.91 ?  190 VAL C CG1   1 
ATOM   3913 C CG2   . VAL C 1 190 ? 22.480  -18.627 42.735 1.00 25.00 ?  190 VAL C CG2   1 
ATOM   3914 N N     . GLU C 1 191 ? 20.388  -22.697 42.146 1.00 26.84 ?  191 GLU C N     1 
ATOM   3915 C CA    . GLU C 1 191 ? 20.236  -24.112 41.824 1.00 33.48 ?  191 GLU C CA    1 
ATOM   3916 C C     . GLU C 1 191 ? 19.253  -24.310 40.674 1.00 27.69 ?  191 GLU C C     1 
ATOM   3917 O O     . GLU C 1 191 ? 19.487  -25.143 39.787 1.00 29.05 ?  191 GLU C O     1 
ATOM   3918 C CB    . GLU C 1 191 ? 19.803  -24.884 43.070 1.00 28.70 ?  191 GLU C CB    1 
ATOM   3919 C CG    . GLU C 1 191 ? 20.933  -25.045 44.084 1.00 30.21 ?  191 GLU C CG    1 
ATOM   3920 C CD    . GLU C 1 191 ? 20.449  -25.453 45.460 1.00 33.26 ?  191 GLU C CD    1 
ATOM   3921 O OE1   . GLU C 1 191 ? 19.363  -26.061 45.559 1.00 42.19 ?  191 GLU C OE1   1 
ATOM   3922 O OE2   . GLU C 1 191 ? 21.157  -25.158 46.448 1.00 41.18 -1 191 GLU C OE2   1 
ATOM   3923 N N     . GLN C 1 192 ? 18.149  -23.557 40.672 1.00 25.52 ?  192 GLN C N     1 
ATOM   3924 C CA    . GLN C 1 192 ? 17.225  -23.597 39.540 1.00 27.38 ?  192 GLN C CA    1 
ATOM   3925 C C     . GLN C 1 192 ? 17.931  -23.186 38.255 1.00 26.82 ?  192 GLN C C     1 
ATOM   3926 O O     . GLN C 1 192 ? 17.824  -23.863 37.226 1.00 26.80 ?  192 GLN C O     1 
ATOM   3927 C CB    . GLN C 1 192 ? 16.023  -22.690 39.799 1.00 26.98 ?  192 GLN C CB    1 
ATOM   3928 C CG    . GLN C 1 192 ? 14.982  -22.710 38.683 1.00 25.99 ?  192 GLN C CG    1 
ATOM   3929 C CD    . GLN C 1 192 ? 13.891  -21.674 38.876 1.00 26.12 ?  192 GLN C CD    1 
ATOM   3930 O OE1   . GLN C 1 192 ? 13.980  -20.821 39.756 1.00 29.31 ?  192 GLN C OE1   1 
ATOM   3931 N NE2   . GLN C 1 192 ? 12.855  -21.742 38.045 1.00 27.91 ?  192 GLN C NE2   1 
ATOM   3932 N N     . LEU C 1 193 ? 18.662  -22.071 38.301 1.00 21.74 ?  193 LEU C N     1 
ATOM   3933 C CA    . LEU C 1 193 ? 19.363  -21.579 37.121 1.00 22.47 ?  193 LEU C CA    1 
ATOM   3934 C C     . LEU C 1 193 ? 20.436  -22.550 36.650 1.00 23.85 ?  193 LEU C C     1 
ATOM   3935 O O     . LEU C 1 193 ? 20.819  -22.514 35.474 1.00 27.98 ?  193 LEU C O     1 
ATOM   3936 C CB    . LEU C 1 193 ? 19.981  -20.211 37.415 1.00 18.51 ?  193 LEU C CB    1 
ATOM   3937 C CG    . LEU C 1 193 ? 18.988  -19.047 37.443 1.00 26.42 ?  193 LEU C CG    1 
ATOM   3938 C CD1   . LEU C 1 193 ? 19.682  -17.760 37.855 1.00 20.72 ?  193 LEU C CD1   1 
ATOM   3939 C CD2   . LEU C 1 193 ? 18.317  -18.890 36.087 1.00 24.13 ?  193 LEU C CD2   1 
ATOM   3940 N N     . ASN C 1 194 ? 20.932  -23.413 37.543 1.00 28.01 ?  194 ASN C N     1 
ATOM   3941 C CA    . ASN C 1 194 ? 21.995  -24.344 37.185 1.00 28.67 ?  194 ASN C CA    1 
ATOM   3942 C C     . ASN C 1 194 ? 21.545  -25.380 36.161 1.00 25.84 ?  194 ASN C C     1 
ATOM   3943 O O     . ASN C 1 194 ? 22.393  -26.099 35.619 1.00 33.14 ?  194 ASN C O     1 
ATOM   3944 C CB    . ASN C 1 194 ? 22.528  -25.038 38.443 1.00 30.76 ?  194 ASN C CB    1 
ATOM   3945 C CG    . ASN C 1 194 ? 23.880  -25.691 38.224 1.00 30.47 ?  194 ASN C CG    1 
ATOM   3946 O OD1   . ASN C 1 194 ? 24.786  -25.092 37.642 1.00 35.51 ?  194 ASN C OD1   1 
ATOM   3947 N ND2   . ASN C 1 194 ? 24.024  -26.924 38.693 1.00 33.25 ?  194 ASN C ND2   1 
ATOM   3948 N N     . GLN C 1 195 ? 20.238  -25.472 35.890 1.00 29.22 ?  195 GLN C N     1 
ATOM   3949 C CA    . GLN C 1 195 ? 19.770  -26.321 34.802 1.00 31.02 ?  195 GLN C CA    1 
ATOM   3950 C C     . GLN C 1 195 ? 20.338  -25.871 33.465 1.00 34.16 ?  195 GLN C C     1 
ATOM   3951 O O     . GLN C 1 195 ? 20.513  -26.687 32.553 1.00 34.41 ?  195 GLN C O     1 
ATOM   3952 C CB    . GLN C 1 195 ? 18.244  -26.309 34.727 1.00 30.08 ?  195 GLN C CB    1 
ATOM   3953 C CG    . GLN C 1 195 ? 17.521  -26.816 35.958 1.00 30.66 ?  195 GLN C CG    1 
ATOM   3954 C CD    . GLN C 1 195 ? 16.037  -26.498 35.912 1.00 37.19 ?  195 GLN C CD    1 
ATOM   3955 O OE1   . GLN C 1 195 ? 15.249  -27.234 35.316 1.00 34.18 ?  195 GLN C OE1   1 
ATOM   3956 N NE2   . GLN C 1 195 ? 15.650  -25.390 36.534 1.00 32.98 ?  195 GLN C NE2   1 
ATOM   3957 N N     . TRP C 1 196 ? 20.632  -24.580 33.333 1.00 31.85 ?  196 TRP C N     1 
ATOM   3958 C CA    . TRP C 1 196 ? 21.059  -23.992 32.074 1.00 28.97 ?  196 TRP C CA    1 
ATOM   3959 C C     . TRP C 1 196 ? 22.383  -23.251 32.159 1.00 28.70 ?  196 TRP C C     1 
ATOM   3960 O O     . TRP C 1 196 ? 23.052  -23.110 31.129 1.00 29.76 ?  196 TRP C O     1 
ATOM   3961 C CB    . TRP C 1 196 ? 19.996  -23.015 31.551 1.00 29.16 ?  196 TRP C CB    1 
ATOM   3962 C CG    . TRP C 1 196 ? 18.609  -23.584 31.464 1.00 25.20 ?  196 TRP C CG    1 
ATOM   3963 C CD1   . TRP C 1 196 ? 18.083  -24.305 30.433 1.00 26.68 ?  196 TRP C CD1   1 
ATOM   3964 C CD2   . TRP C 1 196 ? 17.567  -23.462 32.441 1.00 23.64 ?  196 TRP C CD2   1 
ATOM   3965 N NE1   . TRP C 1 196 ? 16.781  -24.647 30.711 1.00 23.22 ?  196 TRP C NE1   1 
ATOM   3966 C CE2   . TRP C 1 196 ? 16.441  -24.141 31.938 1.00 26.21 ?  196 TRP C CE2   1 
ATOM   3967 C CE3   . TRP C 1 196 ? 17.479  -22.848 33.695 1.00 28.18 ?  196 TRP C CE3   1 
ATOM   3968 C CZ2   . TRP C 1 196 ? 15.242  -24.224 32.643 1.00 28.86 ?  196 TRP C CZ2   1 
ATOM   3969 C CZ3   . TRP C 1 196 ? 16.287  -22.932 34.394 1.00 31.88 ?  196 TRP C CZ3   1 
ATOM   3970 C CH2   . TRP C 1 196 ? 15.184  -23.615 33.865 1.00 27.26 ?  196 TRP C CH2   1 
ATOM   3971 N N     . TYR C 1 197 ? 22.789  -22.780 33.338 1.00 23.82 ?  197 TYR C N     1 
ATOM   3972 C CA    . TYR C 1 197 ? 23.991  -21.973 33.480 1.00 25.30 ?  197 TYR C CA    1 
ATOM   3973 C C     . TYR C 1 197 ? 24.911  -22.596 34.522 1.00 25.85 ?  197 TYR C C     1 
ATOM   3974 O O     . TYR C 1 197 ? 24.451  -22.963 35.617 1.00 26.91 ?  197 TYR C O     1 
ATOM   3975 C CB    . TYR C 1 197 ? 23.627  -20.532 33.864 1.00 19.12 ?  197 TYR C CB    1 
ATOM   3976 C CG    . TYR C 1 197 ? 22.670  -19.891 32.885 1.00 25.56 ?  197 TYR C CG    1 
ATOM   3977 C CD1   . TYR C 1 197 ? 21.295  -20.016 33.043 1.00 22.77 ?  197 TYR C CD1   1 
ATOM   3978 C CD2   . TYR C 1 197 ? 23.142  -19.186 31.787 1.00 21.36 ?  197 TYR C CD2   1 
ATOM   3979 C CE1   . TYR C 1 197 ? 20.418  -19.439 32.143 1.00 23.10 ?  197 TYR C CE1   1 
ATOM   3980 C CE2   . TYR C 1 197 ? 22.274  -18.608 30.882 1.00 21.28 ?  197 TYR C CE2   1 
ATOM   3981 C CZ    . TYR C 1 197 ? 20.915  -18.737 31.066 1.00 17.21 ?  197 TYR C CZ    1 
ATOM   3982 O OH    . TYR C 1 197 ? 20.047  -18.160 30.166 1.00 24.05 ?  197 TYR C OH    1 
ATOM   3983 N N     . PRO C 1 198 ? 26.203  -22.739 34.227 1.00 29.47 ?  198 PRO C N     1 
ATOM   3984 C CA    . PRO C 1 198 ? 27.139  -23.278 35.220 1.00 28.96 ?  198 PRO C CA    1 
ATOM   3985 C C     . PRO C 1 198 ? 27.244  -22.378 36.443 1.00 29.00 ?  198 PRO C C     1 
ATOM   3986 O O     . PRO C 1 198 ? 26.867  -21.204 36.423 1.00 28.67 ?  198 PRO C O     1 
ATOM   3987 C CB    . PRO C 1 198 ? 28.473  -23.344 34.462 1.00 29.39 ?  198 PRO C CB    1 
ATOM   3988 C CG    . PRO C 1 198 ? 28.114  -23.266 33.011 1.00 28.39 ?  198 PRO C CG    1 
ATOM   3989 C CD    . PRO C 1 198 ? 26.853  -22.464 32.934 1.00 23.90 ?  198 PRO C CD    1 
ATOM   3990 N N     . LEU C 1 199 ? 27.762  -22.954 37.531 1.00 24.89 ?  199 LEU C N     1 
ATOM   3991 C CA    . LEU C 1 199 ? 27.864  -22.204 38.779 1.00 33.06 ?  199 LEU C CA    1 
ATOM   3992 C C     . LEU C 1 199 ? 28.907  -21.098 38.690 1.00 27.95 ?  199 LEU C C     1 
ATOM   3993 O O     . LEU C 1 199 ? 28.798  -20.090 39.397 1.00 29.81 ?  199 LEU C O     1 
ATOM   3994 C CB    . LEU C 1 199 ? 28.183  -23.147 39.938 1.00 29.39 ?  199 LEU C CB    1 
ATOM   3995 C CG    . LEU C 1 199 ? 27.049  -24.087 40.365 1.00 31.19 ?  199 LEU C CG    1 
ATOM   3996 C CD1   . LEU C 1 199 ? 27.521  -25.027 41.461 1.00 26.36 ?  199 LEU C CD1   1 
ATOM   3997 C CD2   . LEU C 1 199 ? 25.828  -23.298 40.812 1.00 36.46 ?  199 LEU C CD2   1 
ATOM   3998 N N     . ASP C 1 200 ? 29.913  -21.255 37.832 1.00 27.65 ?  200 ASP C N     1 
ATOM   3999 C CA    . ASP C 1 200 ? 30.929  -20.228 37.647 1.00 30.55 ?  200 ASP C CA    1 
ATOM   4000 C C     . ASP C 1 200 ? 30.603  -19.297 36.486 1.00 30.97 ?  200 ASP C C     1 
ATOM   4001 O O     . ASP C 1 200 ? 31.445  -18.475 36.108 1.00 27.83 ?  200 ASP C O     1 
ATOM   4002 C CB    . ASP C 1 200 ? 32.313  -20.866 37.451 1.00 32.23 ?  200 ASP C CB    1 
ATOM   4003 C CG    . ASP C 1 200 ? 32.401  -21.724 36.201 1.00 34.92 ?  200 ASP C CG    1 
ATOM   4004 O OD1   . ASP C 1 200 ? 31.377  -21.898 35.503 1.00 37.36 ?  200 ASP C OD1   1 
ATOM   4005 O OD2   . ASP C 1 200 ? 33.507  -22.228 35.912 1.00 36.87 -1 200 ASP C OD2   1 
ATOM   4006 N N     . HIS C 1 201 ? 29.404  -19.419 35.916 1.00 26.08 ?  201 HIS C N     1 
ATOM   4007 C CA    . HIS C 1 201 ? 28.966  -18.522 34.857 1.00 28.56 ?  201 HIS C CA    1 
ATOM   4008 C C     . HIS C 1 201 ? 28.889  -17.090 35.368 1.00 25.68 ?  201 HIS C C     1 
ATOM   4009 O O     . HIS C 1 201 ? 28.249  -16.813 36.386 1.00 23.66 ?  201 HIS C O     1 
ATOM   4010 C CB    . HIS C 1 201 ? 27.605  -18.970 34.327 1.00 29.40 ?  201 HIS C CB    1 
ATOM   4011 C CG    . HIS C 1 201 ? 27.103  -18.148 33.182 1.00 27.82 ?  201 HIS C CG    1 
ATOM   4012 N ND1   . HIS C 1 201 ? 27.690  -18.170 31.935 1.00 30.89 ?  201 HIS C ND1   1 
ATOM   4013 C CD2   . HIS C 1 201 ? 26.068  -17.279 33.094 1.00 26.20 ?  201 HIS C CD2   1 
ATOM   4014 C CE1   . HIS C 1 201 ? 27.038  -17.351 31.128 1.00 29.66 ?  201 HIS C CE1   1 
ATOM   4015 N NE2   . HIS C 1 201 ? 26.050  -16.797 31.807 1.00 27.66 ?  201 HIS C NE2   1 
ATOM   4016 N N     . GLU C 1 202 ? 29.545  -16.179 34.656 1.00 21.68 ?  202 GLU C N     1 
ATOM   4017 C CA    . GLU C 1 202 ? 29.568  -14.782 35.063 1.00 26.02 ?  202 GLU C CA    1 
ATOM   4018 C C     . GLU C 1 202 ? 28.223  -14.124 34.787 1.00 23.41 ?  202 GLU C C     1 
ATOM   4019 O O     . GLU C 1 202 ? 27.705  -14.187 33.669 1.00 23.39 ?  202 GLU C O     1 
ATOM   4020 C CB    . GLU C 1 202 ? 30.680  -14.033 34.331 1.00 25.73 ?  202 GLU C CB    1 
ATOM   4021 C CG    . GLU C 1 202 ? 30.723  -12.542 34.634 1.00 29.33 ?  202 GLU C CG    1 
ATOM   4022 C CD    . GLU C 1 202 ? 31.841  -11.831 33.903 1.00 27.30 ?  202 GLU C CD    1 
ATOM   4023 O OE1   . GLU C 1 202 ? 31.702  -11.600 32.683 1.00 30.52 ?  202 GLU C OE1   1 
ATOM   4024 O OE2   . GLU C 1 202 ? 32.863  -11.503 34.544 1.00 27.92 -1 202 GLU C OE2   1 
ATOM   4025 N N     . VAL C 1 203 ? 27.656  -13.496 35.813 1.00 22.23 ?  203 VAL C N     1 
ATOM   4026 C CA    . VAL C 1 203 ? 26.452  -12.691 35.682 1.00 20.03 ?  203 VAL C CA    1 
ATOM   4027 C C     . VAL C 1 203 ? 26.800  -11.268 36.101 1.00 24.52 ?  203 VAL C C     1 
ATOM   4028 O O     . VAL C 1 203 ? 27.870  -11.000 36.644 1.00 22.95 ?  203 VAL C O     1 
ATOM   4029 C CB    . VAL C 1 203 ? 25.276  -13.240 36.515 1.00 20.80 ?  203 VAL C CB    1 
ATOM   4030 C CG1   . VAL C 1 203 ? 24.967  -14.678 36.117 1.00 19.58 ?  203 VAL C CG1   1 
ATOM   4031 C CG2   . VAL C 1 203 ? 25.582  -13.141 38.000 1.00 21.91 ?  203 VAL C CG2   1 
ATOM   4032 N N     . VAL C 1 204 ? 25.877  -10.348 35.841 1.00 20.62 ?  204 VAL C N     1 
ATOM   4033 C CA    . VAL C 1 204 ? 26.103  -8.926  36.080 1.00 20.32 ?  204 VAL C CA    1 
ATOM   4034 C C     . VAL C 1 204 ? 24.936  -8.365  36.880 1.00 23.10 ?  204 VAL C C     1 
ATOM   4035 O O     . VAL C 1 204 ? 23.777  -8.489  36.468 1.00 20.59 ?  204 VAL C O     1 
ATOM   4036 C CB    . VAL C 1 204 ? 26.274  -8.138  34.765 1.00 19.88 ?  204 VAL C CB    1 
ATOM   4037 C CG1   . VAL C 1 204 ? 26.494  -6.661  35.058 1.00 19.77 ?  204 VAL C CG1   1 
ATOM   4038 C CG2   . VAL C 1 204 ? 27.424  -8.706  33.945 1.00 20.33 ?  204 VAL C CG2   1 
ATOM   4039 N N     . ILE C 1 205 ? 25.239  -7.748  38.016 1.00 22.19 ?  205 ILE C N     1 
ATOM   4040 C CA    . ILE C 1 205 ? 24.265  -6.954  38.754 1.00 20.53 ?  205 ILE C CA    1 
ATOM   4041 C C     . ILE C 1 205 ? 24.354  -5.527  38.227 1.00 20.96 ?  205 ILE C C     1 
ATOM   4042 O O     . ILE C 1 205 ? 25.367  -4.848  38.402 1.00 23.23 ?  205 ILE C O     1 
ATOM   4043 C CB    . ILE C 1 205 ? 24.510  -7.013  40.266 1.00 20.83 ?  205 ILE C CB    1 
ATOM   4044 C CG1   . ILE C 1 205 ? 24.407  -8.458  40.762 1.00 19.11 ?  205 ILE C CG1   1 
ATOM   4045 C CG2   . ILE C 1 205 ? 23.526  -6.110  41.000 1.00 20.89 ?  205 ILE C CG2   1 
ATOM   4046 C CD1   . ILE C 1 205 ? 24.987  -8.674  42.144 1.00 21.50 ?  205 ILE C CD1   1 
ATOM   4047 N N     . TYR C 1 206 ? 23.292  -5.075  37.573 1.00 19.15 ?  206 TYR C N     1 
ATOM   4048 C CA    . TYR C 1 206 ? 23.252  -3.778  36.917 1.00 17.91 ?  206 TYR C CA    1 
ATOM   4049 C C     . TYR C 1 206 ? 22.316  -2.837  37.662 1.00 18.59 ?  206 TYR C C     1 
ATOM   4050 O O     . TYR C 1 206 ? 21.210  -3.224  38.052 1.00 16.32 ?  206 TYR C O     1 
ATOM   4051 C CB    . TYR C 1 206 ? 22.791  -3.916  35.462 1.00 18.30 ?  206 TYR C CB    1 
ATOM   4052 C CG    . TYR C 1 206 ? 22.543  -2.599  34.766 1.00 17.39 ?  206 TYR C CG    1 
ATOM   4053 C CD1   . TYR C 1 206 ? 23.594  -1.742  34.466 1.00 17.65 ?  206 TYR C CD1   1 
ATOM   4054 C CD2   . TYR C 1 206 ? 21.257  -2.209  34.415 1.00 17.50 ?  206 TYR C CD2   1 
ATOM   4055 C CE1   . TYR C 1 206 ? 23.370  -0.535  33.827 1.00 15.27 ?  206 TYR C CE1   1 
ATOM   4056 C CE2   . TYR C 1 206 ? 21.025  -1.003  33.780 1.00 15.78 ?  206 TYR C CE2   1 
ATOM   4057 C CZ    . TYR C 1 206 ? 22.086  -0.173  33.488 1.00 13.23 ?  206 TYR C CZ    1 
ATOM   4058 O OH    . TYR C 1 206 ? 21.863  1.028   32.853 1.00 28.13 ?  206 TYR C OH    1 
ATOM   4059 N N     . GLU C 1 207 ? 22.770  -1.600  37.863 1.00 18.04 ?  207 GLU C N     1 
ATOM   4060 C CA    . GLU C 1 207 ? 21.912  -0.522  38.351 1.00 19.57 ?  207 GLU C CA    1 
ATOM   4061 C C     . GLU C 1 207 ? 22.210  0.731   37.540 1.00 22.10 ?  207 GLU C C     1 
ATOM   4062 O O     . GLU C 1 207 ? 23.300  1.300   37.649 1.00 19.93 ?  207 GLU C O     1 
ATOM   4063 C CB    . GLU C 1 207 ? 22.120  -0.267  39.846 1.00 20.03 ?  207 GLU C CB    1 
ATOM   4064 C CG    . GLU C 1 207 ? 21.675  -1.417  40.743 1.00 19.62 ?  207 GLU C CG    1 
ATOM   4065 C CD    . GLU C 1 207 ? 22.181  -1.282  42.165 1.00 25.01 ?  207 GLU C CD    1 
ATOM   4066 O OE1   . GLU C 1 207 ? 22.702  -0.202  42.515 1.00 21.19 ?  207 GLU C OE1   1 
ATOM   4067 O OE2   . GLU C 1 207 ? 22.054  -2.256  42.936 1.00 24.28 -1 207 GLU C OE2   1 
ATOM   4068 N N     . ALA C 1 208 ? 21.251  1.148   36.717 1.00 17.27 ?  208 ALA C N     1 
ATOM   4069 C CA    . ALA C 1 208 ? 21.358  2.412   36.003 1.00 19.42 ?  208 ALA C CA    1 
ATOM   4070 C C     . ALA C 1 208 ? 21.427  3.573   36.986 1.00 19.82 ?  208 ALA C C     1 
ATOM   4071 O O     . ALA C 1 208 ? 20.800  3.559   38.048 1.00 19.23 ?  208 ALA C O     1 
ATOM   4072 C CB    . ALA C 1 208 ? 20.167  2.596   35.059 1.00 16.55 ?  208 ALA C CB    1 
ATOM   4073 N N     . ALA C 1 209 ? 22.195  4.591   36.619 1.00 12.11 ?  209 ALA C N     1 
ATOM   4074 C CA    . ALA C 1 209 ? 22.366  5.749   37.485 1.00 18.11 ?  209 ALA C CA    1 
ATOM   4075 C C     . ALA C 1 209 ? 21.122  6.628   37.471 1.00 15.61 ?  209 ALA C C     1 
ATOM   4076 O O     . ALA C 1 209 ? 20.449  6.768   36.447 1.00 14.72 ?  209 ALA C O     1 
ATOM   4077 C CB    . ALA C 1 209 ? 23.585  6.563   37.046 1.00 18.79 ?  209 ALA C CB    1 
ATOM   4078 N N     . ASN C 1 210 ? 20.813  7.217   38.625 1.00 15.39 ?  210 ASN C N     1 
ATOM   4079 C CA    . ASN C 1 210 ? 19.702  8.152   38.743 1.00 18.27 ?  210 ASN C CA    1 
ATOM   4080 C C     . ASN C 1 210 ? 20.147  9.608   38.732 1.00 17.23 ?  210 ASN C C     1 
ATOM   4081 O O     . ASN C 1 210 ? 19.315  10.492  38.499 1.00 17.52 ?  210 ASN C O     1 
ATOM   4082 C CB    . ASN C 1 210 ? 18.904  7.879   40.025 1.00 15.81 ?  210 ASN C CB    1 
ATOM   4083 C CG    . ASN C 1 210 ? 18.136  6.571   39.967 1.00 15.11 ?  210 ASN C CG    1 
ATOM   4084 O OD1   . ASN C 1 210 ? 18.318  5.692   40.812 1.00 16.29 ?  210 ASN C OD1   1 
ATOM   4085 N ND2   . ASN C 1 210 ? 17.277  6.433   38.966 1.00 10.91 ?  210 ASN C ND2   1 
ATOM   4086 N N     . LEU C 1 211 ? 21.430  9.877   38.970 1.00 14.75 ?  211 LEU C N     1 
ATOM   4087 C CA    . LEU C 1 211 ? 21.965  11.227  39.017 1.00 19.07 ?  211 LEU C CA    1 
ATOM   4088 C C     . LEU C 1 211 ? 23.078  11.394  37.986 1.00 19.56 ?  211 LEU C C     1 
ATOM   4089 O O     . LEU C 1 211 ? 23.775  10.429  37.658 1.00 15.79 ?  211 LEU C O     1 
ATOM   4090 C CB    . LEU C 1 211 ? 22.507  11.557  40.415 1.00 17.26 ?  211 LEU C CB    1 
ATOM   4091 C CG    . LEU C 1 211 ? 21.463  11.588  41.536 1.00 20.51 ?  211 LEU C CG    1 
ATOM   4092 C CD1   . LEU C 1 211 ? 22.113  11.915  42.872 1.00 18.12 ?  211 LEU C CD1   1 
ATOM   4093 C CD2   . LEU C 1 211 ? 20.356  12.581  41.212 1.00 19.79 ?  211 LEU C CD2   1 
ATOM   4094 N N     . PRO C 1 212 ? 23.268  12.605  37.451 1.00 19.25 ?  212 PRO C N     1 
ATOM   4095 C CA    . PRO C 1 212 ? 24.259  12.787  36.377 1.00 19.83 ?  212 PRO C CA    1 
ATOM   4096 C C     . PRO C 1 212 ? 25.701  12.725  36.850 1.00 24.50 ?  212 PRO C C     1 
ATOM   4097 O O     . PRO C 1 212 ? 26.606  12.664  36.004 1.00 24.18 ?  212 PRO C O     1 
ATOM   4098 C CB    . PRO C 1 212 ? 23.914  14.170  35.813 1.00 16.59 ?  212 PRO C CB    1 
ATOM   4099 C CG    . PRO C 1 212 ? 23.318  14.904  36.967 1.00 19.67 ?  212 PRO C CG    1 
ATOM   4100 C CD    . PRO C 1 212 ? 22.621  13.875  37.828 1.00 24.58 ?  212 PRO C CD    1 
ATOM   4101 N N     . ILE C 1 213 ? 25.947  12.739  38.160 1.00 22.82 ?  213 ILE C N     1 
ATOM   4102 C CA    . ILE C 1 213 ? 27.298  12.618  38.697 1.00 24.32 ?  213 ILE C CA    1 
ATOM   4103 C C     . ILE C 1 213 ? 27.599  11.190  39.130 1.00 24.07 ?  213 ILE C C     1 
ATOM   4104 O O     . ILE C 1 213 ? 28.630  10.935  39.757 1.00 17.57 ?  213 ILE C O     1 
ATOM   4105 C CB    . ILE C 1 213 ? 27.528  13.612  39.854 1.00 21.87 ?  213 ILE C CB    1 
ATOM   4106 C CG1   . ILE C 1 213 ? 26.414  13.550  40.920 1.00 24.68 ?  213 ILE C CG1   1 
ATOM   4107 C CG2   . ILE C 1 213 ? 27.628  15.032  39.318 1.00 26.78 ?  213 ILE C CG2   1 
ATOM   4108 C CD1   . ILE C 1 213 ? 26.313  12.270  41.742 1.00 23.67 ?  213 ILE C CD1   1 
ATOM   4109 N N     . GLN C 1 214 ? 26.724  10.251  38.795 1.00 27.04 ?  214 GLN C N     1 
ATOM   4110 C CA    . GLN C 1 214 ? 26.757  8.901   39.333 1.00 23.33 ?  214 GLN C CA    1 
ATOM   4111 C C     . GLN C 1 214 ? 27.071  7.913   38.221 1.00 21.06 ?  214 GLN C C     1 
ATOM   4112 O O     . GLN C 1 214 ? 26.463  7.964   37.147 1.00 29.43 ?  214 GLN C O     1 
ATOM   4113 C CB    . GLN C 1 214 ? 25.418  8.548   39.987 1.00 23.09 ?  214 GLN C CB    1 
ATOM   4114 C CG    . GLN C 1 214 ? 25.255  7.077   40.329 1.00 24.27 ?  214 GLN C CG    1 
ATOM   4115 C CD    . GLN C 1 214 ? 23.846  6.735   40.774 1.00 23.39 ?  214 GLN C CD    1 
ATOM   4116 O OE1   . GLN C 1 214 ? 22.905  7.492   40.533 1.00 20.40 ?  214 GLN C OE1   1 
ATOM   4117 N NE2   . GLN C 1 214 ? 23.695  5.589   41.428 1.00 21.62 ?  214 GLN C NE2   1 
ATOM   4118 N N     . ALA C 1 215 ? 28.020  7.029   38.480 1.00 21.63 ?  215 ALA C N     1 
ATOM   4119 C CA    . ALA C 1 215 ? 28.314  5.954   37.555 1.00 21.91 ?  215 ALA C CA    1 
ATOM   4120 C C     . ALA C 1 215 ? 27.322  4.810   37.759 1.00 23.16 ?  215 ALA C C     1 
ATOM   4121 O O     . ALA C 1 215 ? 26.831  4.594   38.870 1.00 24.34 ?  215 ALA C O     1 
ATOM   4122 C CB    . ALA C 1 215 ? 29.737  5.450   37.762 1.00 26.72 ?  215 ALA C CB    1 
ATOM   4123 N N     . PRO C 1 216 ? 26.998  4.070   36.704 1.00 23.16 ?  216 PRO C N     1 
ATOM   4124 C CA    . PRO C 1 216 ? 26.123  2.909   36.868 1.00 25.26 ?  216 PRO C CA    1 
ATOM   4125 C C     . PRO C 1 216 ? 26.832  1.803   37.629 1.00 22.91 ?  216 PRO C C     1 
ATOM   4126 O O     . PRO C 1 216 ? 28.060  1.728   37.673 1.00 23.42 ?  216 PRO C O     1 
ATOM   4127 C CB    . PRO C 1 216 ? 25.828  2.486   35.424 1.00 23.49 ?  216 PRO C CB    1 
ATOM   4128 C CG    . PRO C 1 216 ? 27.062  2.897   34.686 1.00 20.18 ?  216 PRO C CG    1 
ATOM   4129 C CD    . PRO C 1 216 ? 27.438  4.222   35.306 1.00 29.45 ?  216 PRO C CD    1 
ATOM   4130 N N     . ARG C 1 217 ? 26.037  0.944   38.255 1.00 21.77 ?  217 ARG C N     1 
ATOM   4131 C CA    . ARG C 1 217 ? 26.565  -0.262  38.875 1.00 24.13 ?  217 ARG C CA    1 
ATOM   4132 C C     . ARG C 1 217 ? 26.627  -1.354  37.816 1.00 18.00 ?  217 ARG C C     1 
ATOM   4133 O O     . ARG C 1 217 ? 25.601  -1.726  37.238 1.00 21.49 ?  217 ARG C O     1 
ATOM   4134 C CB    . ARG C 1 217 ? 25.706  -0.706  40.057 1.00 21.48 ?  217 ARG C CB    1 
ATOM   4135 C CG    . ARG C 1 217 ? 26.333  -1.838  40.863 1.00 25.12 ?  217 ARG C CG    1 
ATOM   4136 C CD    . ARG C 1 217 ? 25.379  -2.369  41.919 1.00 20.96 ?  217 ARG C CD    1 
ATOM   4137 N NE    . ARG C 1 217 ? 25.957  -3.475  42.672 1.00 25.09 ?  217 ARG C NE    1 
ATOM   4138 C CZ    . ARG C 1 217 ? 25.309  -4.162  43.604 1.00 28.72 ?  217 ARG C CZ    1 
ATOM   4139 N NH1   . ARG C 1 217 ? 24.042  -3.910  43.894 1.00 20.61 ?  217 ARG C NH1   1 
ATOM   4140 N NH2   . ARG C 1 217 ? 25.944  -5.132  44.256 1.00 22.97 ?  217 ARG C NH2   1 
ATOM   4141 N N     . ILE C 1 218 ? 27.831  -1.851  37.552 1.00 17.30 ?  218 ILE C N     1 
ATOM   4142 C CA    . ILE C 1 218 ? 28.033  -2.970  36.638 1.00 20.39 ?  218 ILE C CA    1 
ATOM   4143 C C     . ILE C 1 218 ? 28.960  -3.962  37.325 1.00 22.00 ?  218 ILE C C     1 
ATOM   4144 O O     . ILE C 1 218 ? 30.173  -3.963  37.095 1.00 26.35 ?  218 ILE C O     1 
ATOM   4145 C CB    . ILE C 1 218 ? 28.604  -2.503  35.284 1.00 20.29 ?  218 ILE C CB    1 
ATOM   4146 C CG1   . ILE C 1 218 ? 27.747  -1.371  34.700 1.00 22.93 ?  218 ILE C CG1   1 
ATOM   4147 C CG2   . ILE C 1 218 ? 28.679  -3.662  34.303 1.00 23.35 ?  218 ILE C CG2   1 
ATOM   4148 C CD1   . ILE C 1 218 ? 28.516  -0.402  33.829 1.00 25.51 ?  218 ILE C CD1   1 
ATOM   4149 N N     . GLU C 1 219 ? 28.395  -4.803  38.182 1.00 21.65 ?  219 GLU C N     1 
ATOM   4150 C CA    . GLU C 1 219 ? 29.166  -5.686  39.047 1.00 21.98 ?  219 GLU C CA    1 
ATOM   4151 C C     . GLU C 1 219 ? 29.117  -7.106  38.497 1.00 26.10 ?  219 GLU C C     1 
ATOM   4152 O O     . GLU C 1 219 ? 28.045  -7.719  38.432 1.00 22.12 ?  219 GLU C O     1 
ATOM   4153 C CB    . GLU C 1 219 ? 28.636  -5.642  40.481 1.00 26.40 ?  219 GLU C CB    1 
ATOM   4154 C CG    . GLU C 1 219 ? 29.323  -6.611  41.427 1.00 29.42 ?  219 GLU C CG    1 
ATOM   4155 C CD    . GLU C 1 219 ? 28.836  -6.468  42.853 1.00 31.53 ?  219 GLU C CD    1 
ATOM   4156 O OE1   . GLU C 1 219 ? 28.577  -5.323  43.281 1.00 34.44 ?  219 GLU C OE1   1 
ATOM   4157 O OE2   . GLU C 1 219 ? 28.709  -7.500  43.546 1.00 30.92 -1 219 GLU C OE2   1 
ATOM   4158 N N     . ARG C 1 220 ? 30.274  -7.620  38.102 1.00 23.20 ?  220 ARG C N     1 
ATOM   4159 C CA    . ARG C 1 220 ? 30.399  -8.952  37.533 1.00 24.80 ?  220 ARG C CA    1 
ATOM   4160 C C     . ARG C 1 220 ? 30.824  -9.933  38.617 1.00 25.22 ?  220 ARG C C     1 
ATOM   4161 O O     . ARG C 1 220 ? 31.701  -9.633  39.433 1.00 25.77 ?  220 ARG C O     1 
ATOM   4162 C CB    . ARG C 1 220 ? 31.407  -8.948  36.381 1.00 24.70 ?  220 ARG C CB    1 
ATOM   4163 C CG    . ARG C 1 220 ? 30.984  -8.027  35.250 1.00 24.79 ?  220 ARG C CG    1 
ATOM   4164 C CD    . ARG C 1 220 ? 32.119  -7.711  34.294 1.00 29.85 ?  220 ARG C CD    1 
ATOM   4165 N NE    . ARG C 1 220 ? 31.698  -6.747  33.283 1.00 31.52 ?  220 ARG C NE    1 
ATOM   4166 C CZ    . ARG C 1 220 ? 30.863  -7.019  32.288 1.00 38.00 ?  220 ARG C CZ    1 
ATOM   4167 N NH1   . ARG C 1 220 ? 30.454  -8.255  32.044 1.00 31.71 ?  220 ARG C NH1   1 
ATOM   4168 N NH2   . ARG C 1 220 ? 30.454  -6.032  31.495 1.00 32.22 ?  220 ARG C NH2   1 
ATOM   4169 N N     . LEU C 1 221 ? 30.191  -11.104 38.625 1.00 23.61 ?  221 LEU C N     1 
ATOM   4170 C CA    . LEU C 1 221 ? 30.432  -12.101 39.659 1.00 19.96 ?  221 LEU C CA    1 
ATOM   4171 C C     . LEU C 1 221 ? 29.938  -13.449 39.159 1.00 25.48 ?  221 LEU C C     1 
ATOM   4172 O O     . LEU C 1 221 ? 29.017  -13.496 38.335 1.00 23.17 ?  221 LEU C O     1 
ATOM   4173 C CB    . LEU C 1 221 ? 29.720  -11.721 40.970 1.00 22.19 ?  221 LEU C CB    1 
ATOM   4174 C CG    . LEU C 1 221 ? 28.193  -11.852 41.053 1.00 24.96 ?  221 LEU C CG    1 
ATOM   4175 C CD1   . LEU C 1 221 ? 27.734  -11.789 42.501 1.00 30.59 ?  221 LEU C CD1   1 
ATOM   4176 C CD2   . LEU C 1 221 ? 27.485  -10.781 40.234 1.00 21.01 ?  221 LEU C CD2   1 
ATOM   4177 N N     . PRO C 1 222 ? 30.530  -14.552 39.618 1.00 27.93 ?  222 PRO C N     1 
ATOM   4178 C CA    . PRO C 1 222 ? 29.995  -15.870 39.261 1.00 25.30 ?  222 PRO C CA    1 
ATOM   4179 C C     . PRO C 1 222 ? 28.594  -16.055 39.820 1.00 23.66 ?  222 PRO C C     1 
ATOM   4180 O O     . PRO C 1 222 ? 28.237  -15.490 40.857 1.00 22.52 ?  222 PRO C O     1 
ATOM   4181 C CB    . PRO C 1 222 ? 30.988  -16.850 39.900 1.00 24.32 ?  222 PRO C CB    1 
ATOM   4182 C CG    . PRO C 1 222 ? 31.703  -16.068 40.951 1.00 24.32 ?  222 PRO C CG    1 
ATOM   4183 C CD    . PRO C 1 222 ? 31.711  -14.639 40.495 1.00 25.06 ?  222 PRO C CD    1 
ATOM   4184 N N     . LEU C 1 223 ? 27.792  -16.846 39.100 1.00 22.59 ?  223 LEU C N     1 
ATOM   4185 C CA    . LEU C 1 223 ? 26.414  -17.088 39.516 1.00 24.26 ?  223 LEU C CA    1 
ATOM   4186 C C     . LEU C 1 223 ? 26.340  -17.642 40.935 1.00 21.47 ?  223 LEU C C     1 
ATOM   4187 O O     . LEU C 1 223 ? 25.394  -17.340 41.671 1.00 28.78 ?  223 LEU C O     1 
ATOM   4188 C CB    . LEU C 1 223 ? 25.734  -18.039 38.530 1.00 25.92 ?  223 LEU C CB    1 
ATOM   4189 C CG    . LEU C 1 223 ? 24.337  -18.559 38.867 1.00 26.71 ?  223 LEU C CG    1 
ATOM   4190 C CD1   . LEU C 1 223 ? 23.375  -17.409 39.123 1.00 24.10 ?  223 LEU C CD1   1 
ATOM   4191 C CD2   . LEU C 1 223 ? 23.816  -19.458 37.759 1.00 23.87 ?  223 LEU C CD2   1 
ATOM   4192 N N     . ALA C 1 224 ? 27.331  -18.443 41.338 1.00 27.72 ?  224 ALA C N     1 
ATOM   4193 C CA    . ALA C 1 224 ? 27.302  -19.066 42.658 1.00 27.72 ?  224 ALA C CA    1 
ATOM   4194 C C     . ALA C 1 224 ? 27.327  -18.033 43.777 1.00 25.85 ?  224 ALA C C     1 
ATOM   4195 O O     . ALA C 1 224 ? 26.804  -18.289 44.866 1.00 23.90 ?  224 ALA C O     1 
ATOM   4196 C CB    . ALA C 1 224 ? 28.473  -20.036 42.806 1.00 29.33 ?  224 ALA C CB    1 
ATOM   4197 N N     . ASN C 1 225 ? 27.928  -16.869 43.536 1.00 27.93 ?  225 ASN C N     1 
ATOM   4198 C CA    . ASN C 1 225 ? 28.114  -15.859 44.571 1.00 27.09 ?  225 ASN C CA    1 
ATOM   4199 C C     . ASN C 1 225 ? 26.917  -14.928 44.717 1.00 26.41 ?  225 ASN C C     1 
ATOM   4200 O O     . ASN C 1 225 ? 26.955  -14.023 45.561 1.00 27.11 ?  225 ASN C O     1 
ATOM   4201 C CB    . ASN C 1 225 ? 29.374  -15.034 44.284 1.00 27.42 ?  225 ASN C CB    1 
ATOM   4202 C CG    . ASN C 1 225 ? 30.648  -15.822 44.512 1.00 29.70 ?  225 ASN C CG    1 
ATOM   4203 O OD1   . ASN C 1 225 ? 30.609  -17.027 44.762 1.00 32.59 ?  225 ASN C OD1   1 
ATOM   4204 N ND2   . ASN C 1 225 ? 31.786  -15.143 44.429 1.00 27.27 ?  225 ASN C ND2   1 
ATOM   4205 N N     . LEU C 1 226 ? 25.871  -15.123 43.913 1.00 27.88 ?  226 LEU C N     1 
ATOM   4206 C CA    . LEU C 1 226 ? 24.703  -14.244 43.966 1.00 22.22 ?  226 LEU C CA    1 
ATOM   4207 C C     . LEU C 1 226 ? 24.065  -14.159 45.350 1.00 26.53 ?  226 LEU C C     1 
ATOM   4208 O O     . LEU C 1 226 ? 23.737  -13.038 45.779 1.00 22.30 ?  226 LEU C O     1 
ATOM   4209 C CB    . LEU C 1 226 ? 23.685  -14.694 42.914 1.00 22.78 ?  226 LEU C CB    1 
ATOM   4210 C CG    . LEU C 1 226 ? 22.323  -13.994 42.925 1.00 21.21 ?  226 LEU C CG    1 
ATOM   4211 C CD1   . LEU C 1 226 ? 22.485  -12.509 42.624 1.00 15.92 ?  226 LEU C CD1   1 
ATOM   4212 C CD2   . LEU C 1 226 ? 21.367  -14.651 41.940 1.00 21.50 ?  226 LEU C CD2   1 
ATOM   4213 N N     . PRO C 1 227 ? 23.844  -15.257 46.088 1.00 24.38 ?  227 PRO C N     1 
ATOM   4214 C CA    . PRO C 1 227 ? 23.161  -15.131 47.391 1.00 27.76 ?  227 PRO C CA    1 
ATOM   4215 C C     . PRO C 1 227 ? 23.897  -14.265 48.399 1.00 26.10 ?  227 PRO C C     1 
ATOM   4216 O O     . PRO C 1 227 ? 23.265  -13.773 49.341 1.00 29.47 ?  227 PRO C O     1 
ATOM   4217 C CB    . PRO C 1 227 ? 23.051  -16.583 47.879 1.00 26.48 ?  227 PRO C CB    1 
ATOM   4218 C CG    . PRO C 1 227 ? 23.239  -17.422 46.672 1.00 22.28 ?  227 PRO C CG    1 
ATOM   4219 C CD    . PRO C 1 227 ? 24.172  -16.666 45.791 1.00 23.06 ?  227 PRO C CD    1 
ATOM   4220 N N     . GLN C 1 228 ? 25.202  -14.061 48.242 1.00 26.91 ?  228 GLN C N     1 
ATOM   4221 C CA    . GLN C 1 228 ? 25.965  -13.248 49.179 1.00 29.01 ?  228 GLN C CA    1 
ATOM   4222 C C     . GLN C 1 228 ? 26.065  -11.796 48.739 1.00 22.65 ?  228 GLN C C     1 
ATOM   4223 O O     . GLN C 1 228 ? 26.652  -10.984 49.460 1.00 26.55 ?  228 GLN C O     1 
ATOM   4224 C CB    . GLN C 1 228 ? 27.378  -13.816 49.360 1.00 31.78 ?  228 GLN C CB    1 
ATOM   4225 C CG    . GLN C 1 228 ? 27.454  -15.114 50.146 1.00 35.78 ?  228 GLN C CG    1 
ATOM   4226 C CD    . GLN C 1 228 ? 26.959  -16.304 49.353 1.00 32.71 ?  228 GLN C CD    1 
ATOM   4227 O OE1   . GLN C 1 228 ? 27.520  -16.644 48.311 1.00 37.18 ?  228 GLN C OE1   1 
ATOM   4228 N NE2   . GLN C 1 228 ? 25.906  -16.946 49.843 1.00 42.88 ?  228 GLN C NE2   1 
ATOM   4229 N N     . ALA C 1 229 ? 25.506  -11.456 47.584 1.00 21.37 ?  229 ALA C N     1 
ATOM   4230 C CA    . ALA C 1 229 ? 25.713  -10.146 46.998 1.00 23.79 ?  229 ALA C CA    1 
ATOM   4231 C C     . ALA C 1 229 ? 24.794  -9.114  47.642 1.00 22.19 ?  229 ALA C C     1 
ATOM   4232 O O     . ALA C 1 229 ? 23.751  -9.433  48.218 1.00 26.29 ?  229 ALA C O     1 
ATOM   4233 C CB    . ALA C 1 229 ? 25.472  -10.188 45.489 1.00 24.53 ?  229 ALA C CB    1 
ATOM   4234 N N     . HIS C 1 230 ? 25.198  -7.854  47.528 1.00 26.90 ?  230 HIS C N     1 
ATOM   4235 C CA    . HIS C 1 230 ? 24.429  -6.725  48.049 1.00 27.17 ?  230 HIS C CA    1 
ATOM   4236 C C     . HIS C 1 230 ? 23.466  -6.283  46.955 1.00 27.69 ?  230 HIS C C     1 
ATOM   4237 O O     . HIS C 1 230 ? 23.863  -5.644  45.979 1.00 28.90 ?  230 HIS C O     1 
ATOM   4238 C CB    . HIS C 1 230 ? 25.362  -5.597  48.480 1.00 32.71 ?  230 HIS C CB    1 
ATOM   4239 C CG    . HIS C 1 230 ? 24.665  -4.440  49.124 1.00 43.16 ?  230 HIS C CG    1 
ATOM   4240 N ND1   . HIS C 1 230 ? 24.956  -4.015  50.402 1.00 49.54 ?  230 HIS C ND1   1 
ATOM   4241 C CD2   . HIS C 1 230 ? 23.707  -3.604  48.659 1.00 43.93 ?  230 HIS C CD2   1 
ATOM   4242 C CE1   . HIS C 1 230 ? 24.197  -2.976  50.702 1.00 51.35 ?  230 HIS C CE1   1 
ATOM   4243 N NE2   . HIS C 1 230 ? 23.430  -2.706  49.661 1.00 40.23 ?  230 HIS C NE2   1 
ATOM   4244 N N     . LEU C 1 231 ? 22.195  -6.624  47.116 1.00 24.50 ?  231 LEU C N     1 
ATOM   4245 C CA    . LEU C 1 231 ? 21.170  -6.303  46.137 1.00 25.77 ?  231 LEU C CA    1 
ATOM   4246 C C     . LEU C 1 231 ? 20.261  -5.209  46.680 1.00 26.89 ?  231 LEU C C     1 
ATOM   4247 O O     . LEU C 1 231 ? 20.002  -5.129  47.884 1.00 28.60 ?  231 LEU C O     1 
ATOM   4248 C CB    . LEU C 1 231 ? 20.337  -7.540  45.774 1.00 21.46 ?  231 LEU C CB    1 
ATOM   4249 C CG    . LEU C 1 231 ? 21.108  -8.751  45.245 1.00 21.11 ?  231 LEU C CG    1 
ATOM   4250 C CD1   . LEU C 1 231 ? 20.188  -9.955  45.100 1.00 20.90 ?  231 LEU C CD1   1 
ATOM   4251 C CD2   . LEU C 1 231 ? 21.778  -8.421  43.920 1.00 19.81 ?  231 LEU C CD2   1 
ATOM   4252 N N     . MET C 1 232 ? 19.779  -4.366  45.779 1.00 22.11 ?  232 MET C N     1 
ATOM   4253 C CA    . MET C 1 232 ? 18.888  -3.268  46.105 1.00 18.86 ?  232 MET C CA    1 
ATOM   4254 C C     . MET C 1 232 ? 17.612  -3.379  45.279 1.00 26.18 ?  232 MET C C     1 
ATOM   4255 O O     . MET C 1 232 ? 17.589  -4.065  44.251 1.00 22.84 ?  232 MET C O     1 
ATOM   4256 C CB    . MET C 1 232 ? 19.574  -1.918  45.841 1.00 25.99 ?  232 MET C CB    1 
ATOM   4257 C CG    . MET C 1 232 ? 20.903  -1.754  46.560 1.00 31.11 ?  232 MET C CG    1 
ATOM   4258 S SD    . MET C 1 232 ? 20.684  -1.413  48.318 1.00 35.85 ?  232 MET C SD    1 
ATOM   4259 C CE    . MET C 1 232 ? 19.700  0.083   48.254 1.00 42.17 ?  232 MET C CE    1 
ATOM   4260 N N     . PRO C 1 233 ? 16.523  -2.735  45.713 1.00 26.34 ?  233 PRO C N     1 
ATOM   4261 C CA    . PRO C 1 233 ? 15.291  -2.743  44.900 1.00 29.93 ?  233 PRO C CA    1 
ATOM   4262 C C     . PRO C 1 233 ? 15.474  -2.284  43.460 1.00 22.82 ?  233 PRO C C     1 
ATOM   4263 O O     . PRO C 1 233 ? 14.689  -2.695  42.596 1.00 25.99 ?  233 PRO C O     1 
ATOM   4264 C CB    . PRO C 1 233 ? 14.344  -1.819  45.681 1.00 20.21 ?  233 PRO C CB    1 
ATOM   4265 C CG    . PRO C 1 233 ? 14.865  -1.820  47.079 1.00 33.56 ?  233 PRO C CG    1 
ATOM   4266 C CD    . PRO C 1 233 ? 16.340  -2.067  47.014 1.00 28.16 ?  233 PRO C CD    1 
ATOM   4267 N N     . ILE C 1 234 ? 16.472  -1.443  43.162 1.00 19.75 ?  234 ILE C N     1 
ATOM   4268 C CA    . ILE C 1 234 ? 16.667  -0.983  41.790 1.00 18.62 ?  234 ILE C CA    1 
ATOM   4269 C C     . ILE C 1 234 ? 17.584  -1.911  41.001 1.00 20.15 ?  234 ILE C C     1 
ATOM   4270 O O     . ILE C 1 234 ? 17.922  -1.604  39.851 1.00 17.82 ?  234 ILE C O     1 
ATOM   4271 C CB    . ILE C 1 234 ? 17.206  0.466   41.740 1.00 22.49 ?  234 ILE C CB    1 
ATOM   4272 C CG1   . ILE C 1 234 ? 18.495  0.614   42.550 1.00 18.90 ?  234 ILE C CG1   1 
ATOM   4273 C CG2   . ILE C 1 234 ? 16.171  1.453   42.241 1.00 22.74 ?  234 ILE C CG2   1 
ATOM   4274 C CD1   . ILE C 1 234 ? 19.436  1.649   41.974 1.00 16.43 ?  234 ILE C CD1   1 
ATOM   4275 N N     . SER C 1 235 ? 17.998  -3.036  41.582 1.00 19.20 ?  235 SER C N     1 
ATOM   4276 C CA    . SER C 1 235 ? 18.933  -3.942  40.926 1.00 19.07 ?  235 SER C CA    1 
ATOM   4277 C C     . SER C 1 235 ? 18.229  -4.841  39.913 1.00 14.68 ?  235 SER C C     1 
ATOM   4278 O O     . SER C 1 235 ? 17.150  -5.381  40.178 1.00 15.11 ?  235 SER C O     1 
ATOM   4279 C CB    . SER C 1 235 ? 19.653  -4.807  41.965 1.00 20.77 ?  235 SER C CB    1 
ATOM   4280 O OG    . SER C 1 235 ? 20.460  -4.018  42.820 1.00 22.19 ?  235 SER C OG    1 
ATOM   4281 N N     . THR C 1 236 ? 18.857  -5.003  38.752 1.00 18.94 ?  236 THR C N     1 
ATOM   4282 C CA    . THR C 1 236 ? 18.467  -5.990  37.753 1.00 18.68 ?  236 THR C CA    1 
ATOM   4283 C C     . THR C 1 236 ? 19.624  -6.953  37.522 1.00 18.90 ?  236 THR C C     1 
ATOM   4284 O O     . THR C 1 236 ? 20.780  -6.531  37.417 1.00 22.08 ?  236 THR C O     1 
ATOM   4285 C CB    . THR C 1 236 ? 18.067  -5.311  36.434 1.00 21.12 ?  236 THR C CB    1 
ATOM   4286 O OG1   . THR C 1 236 ? 16.822  -4.627  36.614 1.00 15.90 ?  236 THR C OG1   1 
ATOM   4287 C CG2   . THR C 1 236 ? 17.924  -6.327  35.309 1.00 18.02 ?  236 THR C CG2   1 
ATOM   4288 N N     . LEU C 1 237 ? 19.317  -8.247  37.448 1.00 19.59 ?  237 LEU C N     1 
ATOM   4289 C CA    . LEU C 1 237 ? 20.319  -9.275  37.194 1.00 19.40 ?  237 LEU C CA    1 
ATOM   4290 C C     . LEU C 1 237 ? 20.358  -9.614  35.709 1.00 20.33 ?  237 LEU C C     1 
ATOM   4291 O O     . LEU C 1 237 ? 19.341  -10.015 35.132 1.00 17.84 ?  237 LEU C O     1 
ATOM   4292 C CB    . LEU C 1 237 ? 20.037  -10.537 38.010 1.00 17.11 ?  237 LEU C CB    1 
ATOM   4293 C CG    . LEU C 1 237 ? 21.072  -11.652 37.819 1.00 18.89 ?  237 LEU C CG    1 
ATOM   4294 C CD1   . LEU C 1 237 ? 22.403  -11.264 38.444 1.00 20.51 ?  237 LEU C CD1   1 
ATOM   4295 C CD2   . LEU C 1 237 ? 20.574  -12.975 38.379 1.00 19.61 ?  237 LEU C CD2   1 
ATOM   4296 N N     . LEU C 1 238 ? 21.529  -9.460  35.098 1.00 22.68 ?  238 LEU C N     1 
ATOM   4297 C CA    A LEU C 1 238 ? 21.756  -9.857  33.717 0.88 20.85 ?  238 LEU C CA    1 
ATOM   4298 C CA    B LEU C 1 238 ? 21.754  -9.857  33.714 0.12 20.78 ?  238 LEU C CA    1 
ATOM   4299 C C     . LEU C 1 238 ? 22.532  -11.165 33.695 1.00 20.06 ?  238 LEU C C     1 
ATOM   4300 O O     . LEU C 1 238 ? 23.520  -11.318 34.422 1.00 20.31 ?  238 LEU C O     1 
ATOM   4301 C CB    A LEU C 1 238 ? 22.526  -8.779  32.951 0.88 20.58 ?  238 LEU C CB    1 
ATOM   4302 C CB    B LEU C 1 238 ? 22.518  -8.778  32.940 0.12 20.99 ?  238 LEU C CB    1 
ATOM   4303 C CG    A LEU C 1 238 ? 23.067  -9.198  31.581 0.88 21.88 ?  238 LEU C CG    1 
ATOM   4304 C CG    B LEU C 1 238 ? 22.645  -8.862  31.409 0.12 20.89 ?  238 LEU C CG    1 
ATOM   4305 C CD1   A LEU C 1 238 ? 21.982  -9.163  30.514 0.88 17.74 ?  238 LEU C CD1   1 
ATOM   4306 C CD1   B LEU C 1 238 ? 23.171  -7.556  30.886 0.12 20.27 ?  238 LEU C CD1   1 
ATOM   4307 C CD2   A LEU C 1 238 ? 24.247  -8.337  31.177 0.88 21.40 ?  238 LEU C CD2   1 
ATOM   4308 C CD2   B LEU C 1 238 ? 23.547  -9.982  30.906 0.12 20.68 ?  238 LEU C CD2   1 
ATOM   4309 N N     . ILE C 1 239 ? 22.086  -12.100 32.868 1.00 18.80 ?  239 ILE C N     1 
ATOM   4310 C CA    . ILE C 1 239 ? 22.750  -13.382 32.687 1.00 20.35 ?  239 ILE C CA    1 
ATOM   4311 C C     . ILE C 1 239 ? 23.119  -13.520 31.215 1.00 20.57 ?  239 ILE C C     1 
ATOM   4312 O O     . ILE C 1 239 ? 22.274  -13.837 30.379 1.00 19.77 ?  239 ILE C O     1 
ATOM   4313 C CB    . ILE C 1 239 ? 21.865  -14.550 33.158 1.00 22.01 ?  239 ILE C CB    1 
ATOM   4314 C CG1   . ILE C 1 239 ? 21.301  -14.246 34.553 1.00 20.33 ?  239 ILE C CG1   1 
ATOM   4315 C CG2   . ILE C 1 239 ? 22.656  -15.847 33.167 1.00 20.72 ?  239 ILE C CG2   1 
ATOM   4316 C CD1   . ILE C 1 239 ? 20.393  -15.323 35.096 1.00 18.74 ?  239 ILE C CD1   1 
ATOM   4317 N N     . PRO C 1 240 ? 24.378  -13.270 30.861 1.00 22.83 ?  240 PRO C N     1 
ATOM   4318 C CA    . PRO C 1 240 ? 24.803  -13.331 29.455 1.00 20.77 ?  240 PRO C CA    1 
ATOM   4319 C C     . PRO C 1 240 ? 24.697  -14.742 28.912 1.00 23.88 ?  240 PRO C C     1 
ATOM   4320 O O     . PRO C 1 240 ? 24.527  -15.702 29.681 1.00 22.08 ?  240 PRO C O     1 
ATOM   4321 C CB    . PRO C 1 240 ? 26.267  -12.861 29.507 1.00 22.98 ?  240 PRO C CB    1 
ATOM   4322 C CG    . PRO C 1 240 ? 26.412  -12.161 30.827 1.00 21.73 ?  240 PRO C CG    1 
ATOM   4323 C CD    . PRO C 1 240 ? 25.483  -12.885 31.751 1.00 22.64 ?  240 PRO C CD    1 
ATOM   4324 N N     . PRO C 1 241 ? 24.755  -14.902 27.593 1.00 21.51 ?  241 PRO C N     1 
ATOM   4325 C CA    . PRO C 1 241 ? 24.643  -16.244 27.011 1.00 26.18 ?  241 PRO C CA    1 
ATOM   4326 C C     . PRO C 1 241 ? 25.667  -17.223 27.575 1.00 23.69 ?  241 PRO C C     1 
ATOM   4327 O O     . PRO C 1 241 ? 26.810  -16.862 27.860 1.00 25.11 ?  241 PRO C O     1 
ATOM   4328 C CB    . PRO C 1 241 ? 24.886  -16.003 25.519 1.00 27.16 ?  241 PRO C CB    1 
ATOM   4329 C CG    . PRO C 1 241 ? 24.545  -14.574 25.286 1.00 28.56 ?  241 PRO C CG    1 
ATOM   4330 C CD    . PRO C 1 241 ? 24.890  -13.856 26.560 1.00 24.51 ?  241 PRO C CD    1 
ATOM   4331 N N     . ALA C 1 242 ? 25.237  -18.468 27.738 1.00 30.66 ?  242 ALA C N     1 
ATOM   4332 C CA    . ALA C 1 242 ? 26.116  -19.576 28.047 1.00 28.93 ?  242 ALA C CA    1 
ATOM   4333 C C     . ALA C 1 242 ? 26.620  -20.278 26.805 1.00 30.10 ?  242 ALA C C     1 
ATOM   4334 O O     . ALA C 1 242 ? 27.553  -21.073 26.885 1.00 31.41 ?  242 ALA C O     1 
ATOM   4335 C CB    . ALA C 1 242 ? 25.382  -20.583 28.934 1.00 28.77 ?  242 ALA C CB    1 
ATOM   4336 N N     . LYS C 1 243 ? 26.092  -19.926 25.679 1.00 34.86 ?  243 LYS C N     1 
ATOM   4337 C CA    . LYS C 1 243 ? 26.170  -20.610 24.404 1.00 36.71 ?  243 LYS C CA    1 
ATOM   4338 C C     . LYS C 1 243 ? 25.653  -19.803 23.255 1.00 31.49 ?  243 LYS C C     1 
ATOM   4339 O O     . LYS C 1 243 ? 24.758  -18.939 23.337 1.00 33.73 ?  243 LYS C O     1 
ATOM   4340 C CB    . LYS C 1 243 ? 25.907  -22.108 24.517 1.00 37.69 ?  243 LYS C CB    1 
ATOM   4341 C CG    . LYS C 1 243 ? 27.280  -22.859 24.521 1.00 45.44 ?  243 LYS C CG    1 
ATOM   4342 C CD    . LYS C 1 243 ? 27.968  -24.172 24.669 1.00 53.80 ?  243 LYS C CD    1 
ATOM   4343 C CE    . LYS C 1 243 ? 28.217  -24.543 23.167 1.00 54.11 ?  243 LYS C CE    1 
ATOM   4344 N NZ    . LYS C 1 243 ? 26.419  -24.983 23.185 1.00 56.04 ?  243 LYS C NZ    1 
ATOM   4345 N N     . LYS C 1 244 ? 26.689  -19.795 22.423 1.00 36.60 ?  244 LYS C N     1 
ATOM   4346 C CA    . LYS C 1 244 ? 26.938  -19.234 21.146 1.00 39.86 ?  244 LYS C CA    1 
ATOM   4347 C C     . LYS C 1 244 ? 25.924  -19.831 20.224 1.00 34.46 ?  244 LYS C C     1 
ATOM   4348 O O     . LYS C 1 244 ? 25.502  -20.986 20.365 1.00 29.55 ?  244 LYS C O     1 
ATOM   4349 C CB    . LYS C 1 244 ? 28.367  -19.586 20.657 1.00 36.54 ?  244 LYS C CB    1 
ATOM   4350 C CG    . LYS C 1 244 ? 29.605  -19.656 21.590 1.00 51.80 ?  244 LYS C CG    1 
ATOM   4351 C CD    . LYS C 1 244 ? 30.621  -20.760 21.152 1.00 57.27 ?  244 LYS C CD    1 
ATOM   4352 C CE    . LYS C 1 244 ? 31.857  -20.878 22.055 1.00 61.12 ?  244 LYS C CE    1 
ATOM   4353 N NZ    . LYS C 1 244 ? 31.542  -21.490 23.352 1.00 62.47 ?  244 LYS C NZ    1 
ATOM   4354 N N     . LEU C 1 245 ? 25.605  -19.052 19.226 1.00 34.07 ?  245 LEU C N     1 
ATOM   4355 C CA    . LEU C 1 245 ? 24.576  -19.439 18.287 1.00 30.53 ?  245 LEU C CA    1 
ATOM   4356 C C     . LEU C 1 245 ? 25.072  -20.584 17.414 1.00 32.81 ?  245 LEU C C     1 
ATOM   4357 O O     . LEU C 1 245 ? 26.220  -20.585 16.965 1.00 32.45 ?  245 LEU C O     1 
ATOM   4358 C CB    . LEU C 1 245 ? 24.178  -18.225 17.447 1.00 32.66 ?  245 LEU C CB    1 
ATOM   4359 C CG    . LEU C 1 245 ? 23.622  -17.109 18.344 1.00 31.15 ?  245 LEU C CG    1 
ATOM   4360 C CD1   . LEU C 1 245 ? 23.610  -15.805 17.571 1.00 35.56 ?  245 LEU C CD1   1 
ATOM   4361 C CD2   . LEU C 1 245 ? 22.237  -17.444 18.858 1.00 30.65 ?  245 LEU C CD2   1 
ATOM   4362 N N     . GLU C 1 246 ? 24.228  -21.591 17.229 1.00 31.11 ?  246 GLU C N     1 
ATOM   4363 C CA    . GLU C 1 246 ? 24.556  -22.751 16.421 1.00 31.07 ?  246 GLU C CA    1 
ATOM   4364 C C     . GLU C 1 246 ? 23.572  -22.802 15.267 1.00 33.14 ?  246 GLU C C     1 
ATOM   4365 O O     . GLU C 1 246 ? 22.445  -22.311 15.371 1.00 28.46 ?  246 GLU C O     1 
ATOM   4366 C CB    . GLU C 1 246 ? 24.502  -24.046 17.240 1.00 30.16 ?  246 GLU C CB    1 
ATOM   4367 C CG    . GLU C 1 246 ? 25.439  -24.047 18.436 1.00 35.68 ?  246 GLU C CG    1 
ATOM   4368 C CD    . GLU C 1 246 ? 25.373  -25.343 19.212 1.00 40.33 ?  246 GLU C CD    1 
ATOM   4369 O OE1   . GLU C 1 246 ? 25.992  -26.333 18.770 1.00 40.22 ?  246 GLU C OE1   1 
ATOM   4370 O OE2   . GLU C 1 246 ? 24.705  -25.374 20.268 1.00 42.58 -1 246 GLU C OE2   1 
ATOM   4371 N N     . TYR C 1 247 ? 24.016  -23.388 14.163 1.00 32.64 ?  247 TYR C N     1 
ATOM   4372 C CA    . TYR C 1 247 ? 23.250  -23.340 12.929 1.00 34.26 ?  247 TYR C CA    1 
ATOM   4373 C C     . TYR C 1 247 ? 22.025  -24.237 13.008 1.00 31.80 ?  247 TYR C C     1 
ATOM   4374 O O     . TYR C 1 247 ? 22.065  -25.329 13.580 1.00 30.70 ?  247 TYR C O     1 
ATOM   4375 C CB    . TYR C 1 247 ? 24.127  -23.744 11.746 1.00 34.80 ?  247 TYR C CB    1 
ATOM   4376 C CG    . TYR C 1 247 ? 25.130  -22.686 11.360 1.00 32.45 ?  247 TYR C CG    1 
ATOM   4377 C CD1   . TYR C 1 247 ? 24.710  -21.451 10.892 1.00 32.57 ?  247 TYR C CD1   1 
ATOM   4378 C CD2   . TYR C 1 247 ? 26.495  -22.920 11.459 1.00 34.27 ?  247 TYR C CD2   1 
ATOM   4379 C CE1   . TYR C 1 247 ? 25.617  -20.476 10.536 1.00 32.62 ?  247 TYR C CE1   1 
ATOM   4380 C CE2   . TYR C 1 247 ? 27.412  -21.950 11.104 1.00 30.87 ?  247 TYR C CE2   1 
ATOM   4381 C CZ    . TYR C 1 247 ? 26.965  -20.730 10.643 1.00 33.80 ?  247 TYR C CZ    1 
ATOM   4382 O OH    . TYR C 1 247 ? 27.872  -19.757 10.286 1.00 36.27 ?  247 TYR C OH    1 
ATOM   4383 N N     . ASN C 1 248 ? 20.927  -23.759 12.423 1.00 25.59 ?  248 ASN C N     1 
ATOM   4384 C CA    . ASN C 1 248 ? 19.655  -24.474 12.412 1.00 24.56 ?  248 ASN C CA    1 
ATOM   4385 C C     . ASN C 1 248 ? 19.528  -25.176 11.062 1.00 28.55 ?  248 ASN C C     1 
ATOM   4386 O O     . ASN C 1 248 ? 18.865  -24.704 10.139 1.00 26.56 ?  248 ASN C O     1 
ATOM   4387 C CB    . ASN C 1 248 ? 18.499  -23.508 12.668 1.00 26.51 ?  248 ASN C CB    1 
ATOM   4388 C CG    . ASN C 1 248 ? 17.226  -24.213 13.094 1.00 28.19 ?  248 ASN C CG    1 
ATOM   4389 O OD1   . ASN C 1 248 ? 17.023  -25.392 12.801 1.00 27.71 ?  248 ASN C OD1   1 
ATOM   4390 N ND2   . ASN C 1 248 ? 16.360  -23.491 13.797 1.00 26.51 ?  248 ASN C ND2   1 
ATOM   4391 N N     . TYR C 1 249 ? 20.186  -26.334 10.959 1.00 28.07 ?  249 TYR C N     1 
ATOM   4392 C CA    . TYR C 1 249 ? 20.300  -27.016 9.673  1.00 28.62 ?  249 TYR C CA    1 
ATOM   4393 C C     . TYR C 1 249 ? 18.937  -27.434 9.139  1.00 28.00 ?  249 TYR C C     1 
ATOM   4394 O O     . TYR C 1 249 ? 18.737  -27.475 7.919  1.00 29.58 ?  249 TYR C O     1 
ATOM   4395 C CB    . TYR C 1 249 ? 21.230  -28.223 9.797  1.00 25.44 ?  249 TYR C CB    1 
ATOM   4396 C CG    . TYR C 1 249 ? 22.689  -27.844 9.939  1.00 29.05 ?  249 TYR C CG    1 
ATOM   4397 C CD1   . TYR C 1 249 ? 23.367  -27.220 8.901  1.00 31.05 ?  249 TYR C CD1   1 
ATOM   4398 C CD2   . TYR C 1 249 ? 23.385  -28.106 11.112 1.00 31.07 ?  249 TYR C CD2   1 
ATOM   4399 C CE1   . TYR C 1 249 ? 24.699  -26.868 9.026  1.00 40.33 ?  249 TYR C CE1   1 
ATOM   4400 C CE2   . TYR C 1 249 ? 24.717  -27.759 11.246 1.00 32.82 ?  249 TYR C CE2   1 
ATOM   4401 C CZ    . TYR C 1 249 ? 25.367  -27.140 10.200 1.00 40.24 ?  249 TYR C CZ    1 
ATOM   4402 O OH    . TYR C 1 249 ? 26.694  -26.792 10.329 1.00 41.08 ?  249 TYR C OH    1 
ATOM   4403 N N     . ALA C 1 250 ? 18.001  -27.769 10.031 1.00 26.83 ?  250 ALA C N     1 
ATOM   4404 C CA    . ALA C 1 250 ? 16.671  -28.184 9.598  1.00 28.83 ?  250 ALA C CA    1 
ATOM   4405 C C     . ALA C 1 250 ? 16.008  -27.103 8.752  1.00 28.48 ?  250 ALA C C     1 
ATOM   4406 O O     . ALA C 1 250 ? 15.430  -27.390 7.697  1.00 32.62 ?  250 ALA C O     1 
ATOM   4407 C CB    . ALA C 1 250 ? 15.808  -28.520 10.814 1.00 31.10 ?  250 ALA C CB    1 
ATOM   4408 N N     . ILE C 1 251 ? 16.080  -25.849 9.201  1.00 27.15 ?  251 ILE C N     1 
ATOM   4409 C CA    . ILE C 1 251 ? 15.425  -24.762 8.478  1.00 26.21 ?  251 ILE C CA    1 
ATOM   4410 C C     . ILE C 1 251 ? 16.268  -24.328 7.289  1.00 25.13 ?  251 ILE C C     1 
ATOM   4411 O O     . ILE C 1 251 ? 15.734  -24.015 6.219  1.00 25.83 ?  251 ILE C O     1 
ATOM   4412 C CB    . ILE C 1 251 ? 15.132  -23.586 9.426  1.00 26.25 ?  251 ILE C CB    1 
ATOM   4413 C CG1   . ILE C 1 251 ? 14.398  -24.081 10.676 1.00 29.79 ?  251 ILE C CG1   1 
ATOM   4414 C CG2   . ILE C 1 251 ? 14.314  -22.517 8.716  1.00 26.31 ?  251 ILE C CG2   1 
ATOM   4415 C CD1   . ILE C 1 251 ? 13.069  -24.741 10.377 1.00 29.40 ?  251 ILE C CD1   1 
ATOM   4416 N N     . LEU C 1 252 ? 17.593  -24.291 7.462  1.00 27.49 ?  252 LEU C N     1 
ATOM   4417 C CA    . LEU C 1 252 ? 18.483  -23.954 6.354  1.00 26.22 ?  252 LEU C CA    1 
ATOM   4418 C C     . LEU C 1 252 ? 18.246  -24.874 5.164  1.00 28.43 ?  252 LEU C C     1 
ATOM   4419 O O     . LEU C 1 252 ? 18.308  -24.440 4.007  1.00 28.40 ?  252 LEU C O     1 
ATOM   4420 C CB    . LEU C 1 252 ? 19.941  -24.032 6.809  1.00 29.52 ?  252 LEU C CB    1 
ATOM   4421 C CG    . LEU C 1 252 ? 20.406  -22.969 7.814  1.00 24.27 ?  252 LEU C CG    1 
ATOM   4422 C CD1   . LEU C 1 252 ? 21.829  -23.249 8.274  1.00 26.11 ?  252 LEU C CD1   1 
ATOM   4423 C CD2   . LEU C 1 252 ? 20.297  -21.576 7.217  1.00 31.34 ?  252 LEU C CD2   1 
ATOM   4424 N N     . ALA C 1 253 ? 17.958  -26.149 5.431  1.00 27.33 ?  253 ALA C N     1 
ATOM   4425 C CA    . ALA C 1 253 ? 17.670  -27.087 4.351  1.00 26.80 ?  253 ALA C CA    1 
ATOM   4426 C C     . ALA C 1 253 ? 16.350  -26.747 3.672  1.00 34.06 ?  253 ALA C C     1 
ATOM   4427 O O     . ALA C 1 253 ? 16.247  -26.802 2.440  1.00 35.04 ?  253 ALA C O     1 
ATOM   4428 C CB    . ALA C 1 253 ? 17.647  -28.518 4.889  1.00 36.05 ?  253 ALA C CB    1 
ATOM   4429 N N     . LYS C 1 254 ? 15.328  -26.396 4.461  1.00 31.41 ?  254 LYS C N     1 
ATOM   4430 C CA    . LYS C 1 254 ? 14.050  -25.989 3.883  1.00 29.66 ?  254 LYS C CA    1 
ATOM   4431 C C     . LYS C 1 254 ? 14.215  -24.741 3.027  1.00 30.46 ?  254 LYS C C     1 
ATOM   4432 O O     . LYS C 1 254 ? 13.581  -24.606 1.973  1.00 35.21 ?  254 LYS C O     1 
ATOM   4433 C CB    . LYS C 1 254 ? 13.032  -25.732 4.990  1.00 30.15 ?  254 LYS C CB    1 
ATOM   4434 C CG    . LYS C 1 254 ? 12.780  -26.924 5.886  1.00 33.79 ?  254 LYS C CG    1 
ATOM   4435 C CD    . LYS C 1 254 ? 11.385  -27.481 5.704  1.00 39.25 ?  254 LYS C CD    1 
ATOM   4436 C CE    . LYS C 1 254 ? 11.353  -28.947 6.087  1.00 49.11 ?  254 LYS C CE    1 
ATOM   4437 N NZ    . LYS C 1 254 ? 10.080  -29.326 6.757  1.00 47.77 ?  254 LYS C NZ    1 
ATOM   4438 N N     . LEU C 1 255 ? 15.073  -23.823 3.461  1.00 34.42 ?  255 LEU C N     1 
ATOM   4439 C CA    . LEU C 1 255 ? 15.396  -22.624 2.701  1.00 32.27 ?  255 LEU C CA    1 
ATOM   4440 C C     . LEU C 1 255 ? 16.327  -22.917 1.535  1.00 37.70 ?  255 LEU C C     1 
ATOM   4441 O O     . LEU C 1 255 ? 16.628  -22.006 0.753  1.00 26.70 ?  255 LEU C O     1 
ATOM   4442 C CB    . LEU C 1 255 ? 16.029  -21.575 3.621  1.00 30.28 ?  255 LEU C CB    1 
ATOM   4443 C CG    . LEU C 1 255 ? 15.155  -20.986 4.735  1.00 28.22 ?  255 LEU C CG    1 
ATOM   4444 C CD1   . LEU C 1 255 ? 16.002  -20.186 5.711  1.00 31.57 ?  255 LEU C CD1   1 
ATOM   4445 C CD2   . LEU C 1 255 ? 14.040  -20.128 4.169  1.00 24.84 ?  255 LEU C CD2   1 
ATOM   4446 N N     . GLY C 1 256 ? 16.794  -24.158 1.411  1.00 35.59 ?  256 GLY C N     1 
ATOM   4447 C CA    . GLY C 1 256 ? 17.640  -24.544 0.301  1.00 33.94 ?  256 GLY C CA    1 
ATOM   4448 C C     . GLY C 1 256 ? 19.033  -23.971 0.340  1.00 28.85 ?  256 GLY C C     1 
ATOM   4449 O O     . GLY C 1 256 ? 19.701  -23.915 -0.695 1.00 36.36 ?  256 GLY C O     1 
ATOM   4450 N N     . ILE C 1 257 ? 19.498  -23.548 1.510  1.00 30.08 ?  257 ILE C N     1 
ATOM   4451 C CA    . ILE C 1 257 ? 20.807  -22.937 1.666  1.00 28.37 ?  257 ILE C CA    1 
ATOM   4452 C C     . ILE C 1 257 ? 21.580  -23.684 2.747  1.00 29.40 ?  257 ILE C C     1 
ATOM   4453 O O     . ILE C 1 257 ? 21.062  -24.580 3.410  1.00 27.54 ?  257 ILE C O     1 
ATOM   4454 C CB    . ILE C 1 257 ? 20.717  -21.436 2.013  1.00 23.93 ?  257 ILE C CB    1 
ATOM   4455 C CG1   . ILE C 1 257 ? 20.004  -21.254 3.357  1.00 27.77 ?  257 ILE C CG1   1 
ATOM   4456 C CG2   . ILE C 1 257 ? 20.004  -20.674 0.908  1.00 28.46 ?  257 ILE C CG2   1 
ATOM   4457 C CD1   . ILE C 1 257 ? 20.023  -19.835 3.868  1.00 27.46 ?  257 ILE C CD1   1 
ATOM   4458 N N     . GLY C 1 258 ? 22.832  -23.278 2.930  1.00 29.92 ?  258 GLY C N     1 
ATOM   4459 C CA    . GLY C 1 258 ? 23.667  -23.783 3.992  1.00 30.52 ?  258 GLY C CA    1 
ATOM   4460 C C     . GLY C 1 258 ? 24.387  -22.647 4.684  1.00 34.52 ?  258 GLY C C     1 
ATOM   4461 O O     . GLY C 1 258 ? 24.174  -21.472 4.371  1.00 33.02 ?  258 GLY C O     1 
ATOM   4462 N N     . PRO C 1 259 ? 25.232  -22.971 5.664  1.00 33.25 ?  259 PRO C N     1 
ATOM   4463 C CA    . PRO C 1 259 ? 25.963  -21.903 6.370  1.00 32.19 ?  259 PRO C CA    1 
ATOM   4464 C C     . PRO C 1 259 ? 26.808  -20.977 5.498  1.00 37.71 ?  259 PRO C C     1 
ATOM   4465 O O     . PRO C 1 259 ? 26.675  -19.755 5.653  1.00 37.14 ?  259 PRO C O     1 
ATOM   4466 C CB    . PRO C 1 259 ? 26.821  -22.691 7.378  1.00 36.86 ?  259 PRO C CB    1 
ATOM   4467 C CG    . PRO C 1 259 ? 26.047  -23.940 7.620  1.00 36.38 ?  259 PRO C CG    1 
ATOM   4468 C CD    . PRO C 1 259 ? 25.420  -24.286 6.299  1.00 34.90 ?  259 PRO C CD    1 
ATOM   4469 N N     . GLU C 1 260 ? 27.691  -21.480 4.614  1.00 40.23 ?  260 GLU C N     1 
ATOM   4470 C CA    . GLU C 1 260 ? 28.562  -20.464 4.023  1.00 44.22 ?  260 GLU C CA    1 
ATOM   4471 C C     . GLU C 1 260 ? 27.858  -19.693 2.902  1.00 39.72 ?  260 GLU C C     1 
ATOM   4472 O O     . GLU C 1 260 ? 28.503  -18.914 2.195  1.00 39.95 ?  260 GLU C O     1 
ATOM   4473 C CB    . GLU C 1 260 ? 29.987  -21.007 3.705  1.00 52.04 ?  260 GLU C CB    1 
ATOM   4474 C CG    . GLU C 1 260 ? 30.711  -21.282 2.323  1.00 57.41 ?  260 GLU C CG    1 
ATOM   4475 C CD    . GLU C 1 260 ? 30.173  -22.331 1.349  1.00 63.87 ?  260 GLU C CD    1 
ATOM   4476 O OE1   . GLU C 1 260 ? 28.962  -22.455 1.152  1.00 62.26 ?  260 GLU C OE1   1 
ATOM   4477 O OE2   . GLU C 1 260 ? 31.038  -23.045 0.797  1.00 61.74 -1 260 GLU C OE2   1 
ATOM   4478 N N     . ASP C 1 261 ? 26.534  -19.882 2.747  1.00 37.20 ?  261 ASP C N     1 
ATOM   4479 C CA    . ASP C 1 261 ? 25.682  -19.051 1.895  1.00 32.99 ?  261 ASP C CA    1 
ATOM   4480 C C     . ASP C 1 261 ? 25.139  -17.836 2.625  1.00 37.84 ?  261 ASP C C     1 
ATOM   4481 O O     . ASP C 1 261 ? 24.624  -16.922 1.973  1.00 36.51 ?  261 ASP C O     1 
ATOM   4482 C CB    . ASP C 1 261 ? 24.459  -19.828 1.389  1.00 35.52 ?  261 ASP C CB    1 
ATOM   4483 C CG    . ASP C 1 261 ? 24.806  -20.900 0.404  1.00 36.73 ?  261 ASP C CG    1 
ATOM   4484 O OD1   . ASP C 1 261 ? 25.539  -20.616 -0.566 1.00 39.60 ?  261 ASP C OD1   1 
ATOM   4485 O OD2   . ASP C 1 261 ? 24.306  -22.032 0.575  1.00 36.90 -1 261 ASP C OD2   1 
ATOM   4486 N N     . LEU C 1 262 ? 25.215  -17.817 3.953  1.00 32.18 ?  262 LEU C N     1 
ATOM   4487 C CA    . LEU C 1 262 ? 24.673  -16.702 4.712  1.00 36.06 ?  262 LEU C CA    1 
ATOM   4488 C C     . LEU C 1 262 ? 25.502  -15.455 4.438  1.00 39.72 ?  262 LEU C C     1 
ATOM   4489 O O     . LEU C 1 262 ? 26.734  -15.512 4.392  1.00 40.65 ?  262 LEU C O     1 
ATOM   4490 C CB    . LEU C 1 262 ? 24.679  -17.034 6.204  1.00 37.64 ?  262 LEU C CB    1 
ATOM   4491 C CG    . LEU C 1 262 ? 23.809  -18.220 6.633  1.00 30.99 ?  262 LEU C CG    1 
ATOM   4492 C CD1   . LEU C 1 262 ? 24.077  -18.594 8.081  1.00 34.56 ?  262 LEU C CD1   1 
ATOM   4493 C CD2   . LEU C 1 262 ? 22.337  -17.910 6.428  1.00 27.90 ?  262 LEU C CD2   1 
ATOM   4494 N N     . GLY C 1 263 ? 24.827  -14.325 4.259  1.00 37.89 ?  263 GLY C N     1 
ATOM   4495 C CA    . GLY C 1 263 ? 25.519  -13.094 3.921  1.00 33.59 ?  263 GLY C CA    1 
ATOM   4496 C C     . GLY C 1 263 ? 26.087  -12.401 5.142  1.00 38.37 ?  263 GLY C C     1 
ATOM   4497 O O     . GLY C 1 263 ? 27.005  -11.586 5.033  1.00 33.82 ?  263 GLY C O     1 
ATOM   4498 O OXT   . GLY C 1 263 ? 25.637  -12.642 6.265  1.00 35.28 -1 263 GLY C OXT   1 
ATOM   4499 N N     . LEU D 2 11  ? 22.797  22.219  45.536 1.00 29.03 ?  4   LEU D N     1 
ATOM   4500 C CA    . LEU D 2 11  ? 23.066  20.902  44.979 1.00 30.11 ?  4   LEU D CA    1 
ATOM   4501 C C     . LEU D 2 11  ? 22.028  20.523  43.928 1.00 25.14 ?  4   LEU D C     1 
ATOM   4502 O O     . LEU D 2 11  ? 22.369  20.226  42.784 1.00 24.47 ?  4   LEU D O     1 
ATOM   4503 C CB    . LEU D 2 11  ? 23.094  19.844  46.084 1.00 25.42 ?  4   LEU D CB    1 
ATOM   4504 C CG    . LEU D 2 11  ? 24.466  19.349  46.546 1.00 29.96 ?  4   LEU D CG    1 
ATOM   4505 C CD1   . LEU D 2 11  ? 24.316  18.231  47.567 1.00 34.57 ?  4   LEU D CD1   1 
ATOM   4506 C CD2   . LEU D 2 11  ? 25.297  18.887  45.362 1.00 31.34 ?  4   LEU D CD2   1 
ATOM   4507 N N     . SER D 2 12  ? 20.756  20.541  44.331 1.00 25.81 ?  5   SER D N     1 
ATOM   4508 C CA    . SER D 2 12  ? 19.680  20.109  43.444 1.00 26.82 ?  5   SER D CA    1 
ATOM   4509 C C     . SER D 2 12  ? 19.632  20.958  42.180 1.00 26.17 ?  5   SER D C     1 
ATOM   4510 O O     . SER D 2 12  ? 19.313  20.451  41.097 1.00 22.76 ?  5   SER D O     1 
ATOM   4511 C CB    . SER D 2 12  ? 18.337  20.158  44.176 1.00 21.18 ?  5   SER D CB    1 
ATOM   4512 O OG    . SER D 2 12  ? 17.271  19.785  43.322 1.00 24.62 ?  5   SER D OG    1 
ATOM   4513 N N     . ASP D 2 13  ? 19.937  22.254  42.299 1.00 22.72 ?  6   ASP D N     1 
ATOM   4514 C CA    . ASP D 2 13  ? 19.962  23.115  41.119 1.00 23.60 ?  6   ASP D CA    1 
ATOM   4515 C C     . ASP D 2 13  ? 21.030  22.648  40.137 1.00 23.05 ?  6   ASP D C     1 
ATOM   4516 O O     . ASP D 2 13  ? 20.782  22.542  38.931 1.00 19.92 ?  6   ASP D O     1 
ATOM   4517 C CB    . ASP D 2 13  ? 20.201  24.570  41.526 1.00 26.41 ?  6   ASP D CB    1 
ATOM   4518 C CG    . ASP D 2 13  ? 19.032  25.158  42.289 1.00 25.47 ?  6   ASP D CG    1 
ATOM   4519 O OD1   . ASP D 2 13  ? 17.875  24.954  41.857 1.00 29.41 ?  6   ASP D OD1   1 
ATOM   4520 O OD2   . ASP D 2 13  ? 19.263  25.842  43.306 1.00 34.88 -1 6   ASP D OD2   1 
ATOM   4521 N N     . PHE D 2 14  ? 22.236  22.380  40.640 1.00 21.45 ?  7   PHE D N     1 
ATOM   4522 C CA    . PHE D 2 14  ? 23.330  21.958  39.771 1.00 21.43 ?  7   PHE D CA    1 
ATOM   4523 C C     . PHE D 2 14  ? 22.999  20.648  39.067 1.00 20.54 ?  7   PHE D C     1 
ATOM   4524 O O     . PHE D 2 14  ? 23.202  20.515  37.854 1.00 21.66 ?  7   PHE D O     1 
ATOM   4525 C CB    . PHE D 2 14  ? 24.624  21.822  40.574 1.00 17.08 ?  7   PHE D CB    1 
ATOM   4526 C CG    . PHE D 2 14  ? 25.757  21.221  39.795 1.00 25.39 ?  7   PHE D CG    1 
ATOM   4527 C CD1   . PHE D 2 14  ? 26.309  21.897  38.720 1.00 20.52 ?  7   PHE D CD1   1 
ATOM   4528 C CD2   . PHE D 2 14  ? 26.261  19.975  40.130 1.00 20.49 ?  7   PHE D CD2   1 
ATOM   4529 C CE1   . PHE D 2 14  ? 27.351  21.343  37.996 1.00 23.57 ?  7   PHE D CE1   1 
ATOM   4530 C CE2   . PHE D 2 14  ? 27.301  19.418  39.409 1.00 22.61 ?  7   PHE D CE2   1 
ATOM   4531 C CZ    . PHE D 2 14  ? 27.846  20.103  38.342 1.00 20.21 ?  7   PHE D CZ    1 
ATOM   4532 N N     . PHE D 2 15  ? 22.476  19.670  39.815 1.00 17.74 ?  8   PHE D N     1 
ATOM   4533 C CA    . PHE D 2 15  ? 22.215  18.356  39.235 1.00 20.44 ?  8   PHE D CA    1 
ATOM   4534 C C     . PHE D 2 15  ? 21.143  18.435  38.156 1.00 17.96 ?  8   PHE D C     1 
ATOM   4535 O O     . PHE D 2 15  ? 21.221  17.731  37.141 1.00 19.68 ?  8   PHE D O     1 
ATOM   4536 C CB    . PHE D 2 15  ? 21.794  17.366  40.324 1.00 16.44 ?  8   PHE D CB    1 
ATOM   4537 C CG    . PHE D 2 15  ? 22.911  16.936  41.236 1.00 20.64 ?  8   PHE D CG    1 
ATOM   4538 C CD1   . PHE D 2 15  ? 24.236  17.180  40.912 1.00 22.98 ?  8   PHE D CD1   1 
ATOM   4539 C CD2   . PHE D 2 15  ? 22.629  16.261  42.413 1.00 24.44 ?  8   PHE D CD2   1 
ATOM   4540 C CE1   . PHE D 2 15  ? 25.256  16.773  41.755 1.00 25.77 ?  8   PHE D CE1   1 
ATOM   4541 C CE2   . PHE D 2 15  ? 23.644  15.851  43.258 1.00 27.98 ?  8   PHE D CE2   1 
ATOM   4542 C CZ    . PHE D 2 15  ? 24.958  16.107  42.928 1.00 25.91 ?  8   PHE D CZ    1 
ATOM   4543 N N     . THR D 2 16  ? 20.121  19.269  38.366 1.00 17.41 ?  9   THR D N     1 
ATOM   4544 C CA    . THR D 2 16  ? 19.060  19.394  37.372 1.00 21.49 ?  9   THR D CA    1 
ATOM   4545 C C     . THR D 2 16  ? 19.585  20.024  36.087 1.00 22.33 ?  9   THR D C     1 
ATOM   4546 O O     . THR D 2 16  ? 19.242  19.575  34.985 1.00 20.14 ?  9   THR D O     1 
ATOM   4547 C CB    . THR D 2 16  ? 17.896  20.202  37.948 1.00 24.75 ?  9   THR D CB    1 
ATOM   4548 O OG1   . THR D 2 16  ? 17.275  19.447  38.997 1.00 20.80 ?  9   THR D OG1   1 
ATOM   4549 C CG2   . THR D 2 16  ? 16.857  20.498  36.880 1.00 21.18 ?  9   THR D CG2   1 
ATOM   4550 N N     . GLN D 2 17  ? 20.406  21.073  36.208 1.00 20.55 ?  10  GLN D N     1 
ATOM   4551 C CA    . GLN D 2 17  ? 21.048  21.654  35.032 1.00 15.74 ?  10  GLN D CA    1 
ATOM   4552 C C     . GLN D 2 17  ? 21.922  20.621  34.333 1.00 18.37 ?  10  GLN D C     1 
ATOM   4553 O O     . GLN D 2 17  ? 21.850  20.446  33.110 1.00 19.13 ?  10  GLN D O     1 
ATOM   4554 C CB    . GLN D 2 17  ? 21.882  22.875  35.422 1.00 16.87 ?  10  GLN D CB    1 
ATOM   4555 C CG    . GLN D 2 17  ? 21.096  24.034  36.002 1.00 26.16 ?  10  GLN D CG    1 
ATOM   4556 C CD    . GLN D 2 17  ? 21.997  25.056  36.673 1.00 43.84 ?  10  GLN D CD    1 
ATOM   4557 O OE1   . GLN D 2 17  ? 23.222  24.991  36.559 1.00 39.79 ?  10  GLN D OE1   1 
ATOM   4558 N NE2   . GLN D 2 17  ? 21.393  26.001  37.382 1.00 41.38 ?  10  GLN D NE2   1 
ATOM   4559 N N     . LEU D 2 18  ? 22.768  19.933  35.107 1.00 16.80 ?  11  LEU D N     1 
ATOM   4560 C CA    . LEU D 2 18  ? 23.743  19.010  34.536 1.00 21.55 ?  11  LEU D CA    1 
ATOM   4561 C C     . LEU D 2 18  ? 23.055  17.882  33.777 1.00 16.50 ?  11  LEU D C     1 
ATOM   4562 O O     . LEU D 2 18  ? 23.528  17.458  32.717 1.00 18.81 ?  11  LEU D O     1 
ATOM   4563 C CB    . LEU D 2 18  ? 24.630  18.457  35.654 1.00 19.92 ?  11  LEU D CB    1 
ATOM   4564 C CG    . LEU D 2 18  ? 25.694  17.410  35.324 1.00 20.65 ?  11  LEU D CG    1 
ATOM   4565 C CD1   . LEU D 2 18  ? 26.505  17.832  34.117 1.00 23.35 ?  11  LEU D CD1   1 
ATOM   4566 C CD2   . LEU D 2 18  ? 26.601  17.190  36.525 1.00 23.32 ?  11  LEU D CD2   1 
ATOM   4567 N N     . GLY D 2 19  ? 21.936  17.381  34.306 1.00 20.19 ?  12  GLY D N     1 
ATOM   4568 C CA    . GLY D 2 19  ? 21.227  16.296  33.652 1.00 18.11 ?  12  GLY D CA    1 
ATOM   4569 C C     . GLY D 2 19  ? 20.558  16.688  32.352 1.00 16.29 ?  12  GLY D C     1 
ATOM   4570 O O     . GLY D 2 19  ? 20.311  15.820  31.508 1.00 22.78 ?  12  GLY D O     1 
ATOM   4571 N N     . GLN D 2 20  ? 20.266  17.976  32.167 1.00 15.23 ?  13  GLN D N     1 
ATOM   4572 C CA    . GLN D 2 20  ? 19.518  18.444  31.008 1.00 16.64 ?  13  GLN D CA    1 
ATOM   4573 C C     . GLN D 2 20  ? 20.392  19.087  29.945 1.00 23.80 ?  13  GLN D C     1 
ATOM   4574 O O     . GLN D 2 20  ? 19.982  19.147  28.780 1.00 17.54 ?  13  GLN D O     1 
ATOM   4575 C CB    . GLN D 2 20  ? 18.468  19.486  31.420 1.00 21.79 ?  13  GLN D CB    1 
ATOM   4576 C CG    . GLN D 2 20  ? 17.396  19.008  32.362 1.00 26.00 ?  13  GLN D CG    1 
ATOM   4577 C CD    . GLN D 2 20  ? 16.458  20.129  32.766 1.00 28.62 ?  13  GLN D CD    1 
ATOM   4578 O OE1   . GLN D 2 20  ? 16.737  20.886  33.697 1.00 28.66 ?  13  GLN D OE1   1 
ATOM   4579 N NE2   . GLN D 2 20  ? 15.342  20.249  32.057 1.00 29.56 ?  13  GLN D NE2   1 
ATOM   4580 N N     . ASP D 2 21  ? 21.568  19.574  30.315 1.00 19.45 ?  14  ASP D N     1 
ATOM   4581 C CA    . ASP D 2 21  ? 22.328  20.495  29.483 1.00 18.22 ?  14  ASP D CA    1 
ATOM   4582 C C     . ASP D 2 21  ? 23.575  19.782  28.975 1.00 16.80 ?  14  ASP D C     1 
ATOM   4583 O O     . ASP D 2 21  ? 24.528  19.555  29.732 1.00 15.55 ?  14  ASP D O     1 
ATOM   4584 C CB    . ASP D 2 21  ? 22.679  21.756  30.279 1.00 19.74 ?  14  ASP D CB    1 
ATOM   4585 C CG    . ASP D 2 21  ? 23.431  22.795  29.460 1.00 22.35 ?  14  ASP D CG    1 
ATOM   4586 O OD1   . ASP D 2 21  ? 23.860  22.503  28.330 1.00 18.39 ?  14  ASP D OD1   1 
ATOM   4587 O OD2   . ASP D 2 21  ? 23.585  23.928  29.966 1.00 26.32 -1 14  ASP D OD2   1 
ATOM   4588 N N     . ALA D 2 22  ? 23.566  19.441  27.686 1.00 21.49 ?  15  ALA D N     1 
ATOM   4589 C CA    . ALA D 2 22  ? 24.691  18.709  27.135 1.00 17.12 ?  15  ALA D CA    1 
ATOM   4590 C C     . ALA D 2 22  ? 25.924  19.596  27.035 1.00 26.99 ?  15  ALA D C     1 
ATOM   4591 O O     . ALA D 2 22  ? 27.046  19.063  27.001 1.00 24.14 ?  15  ALA D O     1 
ATOM   4592 C CB    . ALA D 2 22  ? 24.339  18.103  25.781 1.00 18.88 ?  15  ALA D CB    1 
ATOM   4593 N N     . GLN D 2 23  ? 25.764  20.935  26.991 1.00 23.09 ?  16  GLN D N     1 
ATOM   4594 C CA    . GLN D 2 23  ? 26.971  21.744  27.100 1.00 24.69 ?  16  GLN D CA    1 
ATOM   4595 C C     . GLN D 2 23  ? 27.651  21.430  28.420 1.00 29.96 ?  16  GLN D C     1 
ATOM   4596 O O     . GLN D 2 23  ? 28.815  21.015  28.477 1.00 23.34 ?  16  GLN D O     1 
ATOM   4597 C CB    . GLN D 2 23  ? 26.722  23.257  27.189 1.00 34.15 ?  16  GLN D CB    1 
ATOM   4598 C CG    . GLN D 2 23  ? 28.133  23.799  27.248 1.00 37.25 ?  16  GLN D CG    1 
ATOM   4599 C CD    . GLN D 2 23  ? 28.745  23.905  25.877 1.00 43.11 ?  16  GLN D CD    1 
ATOM   4600 O OE1   . GLN D 2 23  ? 29.483  22.936  25.466 1.00 42.31 ?  16  GLN D OE1   1 
ATOM   4601 N NE2   . GLN D 2 23  ? 29.006  25.148  25.508 1.00 49.99 ?  16  GLN D NE2   1 
ATOM   4602 N N     . LEU D 2 24  ? 26.912  21.660  29.506 1.00 23.93 ?  17  LEU D N     1 
ATOM   4603 C CA    . LEU D 2 24  ? 27.449  21.520  30.847 1.00 24.23 ?  17  LEU D CA    1 
ATOM   4604 C C     . LEU D 2 24  ? 27.930  20.104  31.090 1.00 21.92 ?  17  LEU D C     1 
ATOM   4605 O O     . LEU D 2 24  ? 28.965  19.894  31.734 1.00 19.74 ?  17  LEU D O     1 
ATOM   4606 C CB    . LEU D 2 24  ? 26.372  21.932  31.847 1.00 27.98 ?  17  LEU D CB    1 
ATOM   4607 C CG    . LEU D 2 24  ? 26.662  21.691  33.318 1.00 31.87 ?  17  LEU D CG    1 
ATOM   4608 C CD1   . LEU D 2 24  ? 27.979  22.323  33.752 1.00 29.53 ?  17  LEU D CD1   1 
ATOM   4609 C CD2   . LEU D 2 24  ? 25.518  22.192  34.188 1.00 28.17 ?  17  LEU D CD2   1 
ATOM   4610 N N     . MET D 2 25  ? 27.192  19.119  30.577 1.00 21.40 ?  18  MET D N     1 
ATOM   4611 C CA    . MET D 2 25  ? 27.589  17.731  30.767 1.00 23.61 ?  18  MET D CA    1 
ATOM   4612 C C     . MET D 2 25  ? 28.982  17.474  30.214 1.00 20.00 ?  18  MET D C     1 
ATOM   4613 O O     . MET D 2 25  ? 29.806  16.830  30.873 1.00 14.38 ?  18  MET D O     1 
ATOM   4614 C CB    . MET D 2 25  ? 26.575  16.799  30.120 1.00 21.24 ?  18  MET D CB    1 
ATOM   4615 C CG    . MET D 2 25  ? 26.954  15.338  30.260 1.00 29.13 ?  18  MET D CG    1 
ATOM   4616 S SD    . MET D 2 25  ? 27.024  14.840  31.993 1.00 34.06 ?  18  MET D SD    1 
ATOM   4617 C CE    . MET D 2 25  ? 25.282  14.589  32.328 1.00 26.00 ?  18  MET D CE    1 
ATOM   4618 N N     . GLU D 2 26  ? 29.270  17.979  29.011 1.00 24.80 ?  19  GLU D N     1 
ATOM   4619 C CA    . GLU D 2 26  ? 30.596  17.770  28.443 1.00 25.86 ?  19  GLU D CA    1 
ATOM   4620 C C     . GLU D 2 26  ? 31.633  18.629  29.154 1.00 25.09 ?  19  GLU D C     1 
ATOM   4621 O O     . GLU D 2 26  ? 32.801  18.232  29.258 1.00 24.16 ?  19  GLU D O     1 
ATOM   4622 C CB    . GLU D 2 26  ? 30.575  18.053  26.944 1.00 27.83 ?  19  GLU D CB    1 
ATOM   4623 C CG    . GLU D 2 26  ? 29.925  16.943  26.121 1.00 27.50 ?  19  GLU D CG    1 
ATOM   4624 C CD    . GLU D 2 26  ? 30.510  15.572  26.416 1.00 35.77 ?  19  GLU D CD    1 
ATOM   4625 O OE1   . GLU D 2 26  ? 31.672  15.327  26.030 1.00 39.39 ?  19  GLU D OE1   1 
ATOM   4626 O OE2   . GLU D 2 26  ? 29.809  14.738  27.032 1.00 36.91 -1 19  GLU D OE2   1 
ATOM   4627 N N     . ASP D 2 27  ? 31.228  19.803  29.648 1.00 26.30 ?  20  ASP D N     1 
ATOM   4628 C CA    . ASP D 2 27  ? 32.107  20.585  30.513 1.00 19.77 ?  20  ASP D CA    1 
ATOM   4629 C C     . ASP D 2 27  ? 32.466  19.794  31.763 1.00 21.55 ?  20  ASP D C     1 
ATOM   4630 O O     . ASP D 2 27  ? 33.633  19.737  32.171 1.00 21.15 ?  20  ASP D O     1 
ATOM   4631 C CB    . ASP D 2 27  ? 31.437  21.904  30.903 1.00 22.10 ?  20  ASP D CB    1 
ATOM   4632 C CG    . ASP D 2 27  ? 31.280  22.852  29.735 1.00 27.94 ?  20  ASP D CG    1 
ATOM   4633 O OD1   . ASP D 2 27  ? 31.914  22.622  28.683 1.00 28.49 ?  20  ASP D OD1   1 
ATOM   4634 O OD2   . ASP D 2 27  ? 30.527  23.839  29.873 1.00 31.94 -1 20  ASP D OD2   1 
ATOM   4635 N N     . TYR D 2 28  ? 31.460  19.174  32.387 1.00 17.91 ?  21  TYR D N     1 
ATOM   4636 C CA    . TYR D 2 28  ? 31.683  18.439  33.628 1.00 19.50 ?  21  TYR D CA    1 
ATOM   4637 C C     . TYR D 2 28  ? 32.616  17.257  33.410 1.00 20.48 ?  21  TYR D C     1 
ATOM   4638 O O     . TYR D 2 28  ? 33.507  16.999  34.226 1.00 14.98 ?  21  TYR D O     1 
ATOM   4639 C CB    . TYR D 2 28  ? 30.343  17.967  34.199 1.00 16.79 ?  21  TYR D CB    1 
ATOM   4640 C CG    . TYR D 2 28  ? 30.453  17.039  35.389 1.00 18.84 ?  21  TYR D CG    1 
ATOM   4641 C CD1   . TYR D 2 28  ? 30.584  17.542  36.677 1.00 20.50 ?  21  TYR D CD1   1 
ATOM   4642 C CD2   . TYR D 2 28  ? 30.421  15.659  35.224 1.00 23.90 ?  21  TYR D CD2   1 
ATOM   4643 C CE1   . TYR D 2 28  ? 30.686  16.696  37.768 1.00 21.37 ?  21  TYR D CE1   1 
ATOM   4644 C CE2   . TYR D 2 28  ? 30.525  14.807  36.309 1.00 19.37 ?  21  TYR D CE2   1 
ATOM   4645 C CZ    . TYR D 2 28  ? 30.656  15.333  37.576 1.00 21.53 ?  21  TYR D CZ    1 
ATOM   4646 O OH    . TYR D 2 28  ? 30.758  14.487  38.659 1.00 22.54 ?  21  TYR D OH    1 
ATOM   4647 N N     . LYS D 2 29  ? 32.428  16.526  32.312 1.00 22.16 ?  22  LYS D N     1 
ATOM   4648 C CA    . LYS D 2 29  ? 33.246  15.342  32.082 1.00 28.85 ?  22  LYS D CA    1 
ATOM   4649 C C     . LYS D 2 29  ? 34.704  15.715  31.840 1.00 25.96 ?  22  LYS D C     1 
ATOM   4650 O O     . LYS D 2 29  ? 35.608  14.952  32.207 1.00 29.35 ?  22  LYS D O     1 
ATOM   4651 C CB    . LYS D 2 29  ? 32.656  14.518  30.941 1.00 31.01 ?  22  LYS D CB    1 
ATOM   4652 C CG    . LYS D 2 29  ? 31.290  13.954  31.325 1.00 34.37 ?  22  LYS D CG    1 
ATOM   4653 C CD    . LYS D 2 29  ? 31.104  12.508  30.921 1.00 28.57 ?  22  LYS D CD    1 
ATOM   4654 C CE    . LYS D 2 29  ? 30.664  12.375  29.483 1.00 31.96 ?  22  LYS D CE    1 
ATOM   4655 N NZ    . LYS D 2 29  ? 31.068  11.048  28.961 1.00 31.95 ?  22  LYS D NZ    1 
ATOM   4656 N N     . GLN D 2 30  ? 34.949  16.868  31.211 1.00 23.81 ?  23  GLN D N     1 
ATOM   4657 C CA    . GLN D 2 30  ? 36.318  17.336  31.013 1.00 23.98 ?  23  GLN D CA    1 
ATOM   4658 C C     . GLN D 2 30  ? 37.022  17.558  32.347 1.00 24.18 ?  23  GLN D C     1 
ATOM   4659 O O     . GLN D 2 30  ? 38.161  17.120  32.546 1.00 17.07 ?  23  GLN D O     1 
ATOM   4660 C CB    . GLN D 2 30  ? 36.313  18.631  30.205 1.00 29.19 ?  23  GLN D CB    1 
ATOM   4661 C CG    . GLN D 2 30  ? 35.899  18.477  28.753 1.00 34.36 ?  23  GLN D CG    1 
ATOM   4662 C CD    . GLN D 2 30  ? 37.080  18.301  27.824 1.00 41.98 ?  23  GLN D CD    1 
ATOM   4663 O OE1   . GLN D 2 30  ? 37.999  17.530  28.103 1.00 46.44 ?  23  GLN D OE1   1 
ATOM   4664 N NE2   . GLN D 2 30  ? 37.066  19.025  26.711 1.00 45.27 ?  23  GLN D NE2   1 
ATOM   4665 N N     . ASN D 2 31  ? 36.354  18.230  33.282 1.00 20.31 ?  24  ASN D N     1 
ATOM   4666 C CA    . ASN D 2 31  ? 36.978  18.651  34.539 1.00 21.90 ?  24  ASN D CA    1 
ATOM   4667 C C     . ASN D 2 31  ? 35.917  18.678  35.630 1.00 20.74 ?  24  ASN D C     1 
ATOM   4668 O O     . ASN D 2 31  ? 35.395  19.741  35.996 1.00 18.15 ?  24  ASN D O     1 
ATOM   4669 C CB    . ASN D 2 31  ? 37.654  20.015  34.392 1.00 16.83 ?  24  ASN D CB    1 
ATOM   4670 C CG    . ASN D 2 31  ? 38.675  20.283  35.479 1.00 18.08 ?  24  ASN D CG    1 
ATOM   4671 O OD1   . ASN D 2 31  ? 38.613  19.706  36.563 1.00 28.66 ?  24  ASN D OD1   1 
ATOM   4672 N ND2   . ASN D 2 31  ? 39.625  21.167  35.192 1.00 18.60 ?  24  ASN D ND2   1 
ATOM   4673 N N     . PRO D 2 32  ? 35.549  17.506  36.162 1.00 17.22 ?  25  PRO D N     1 
ATOM   4674 C CA    . PRO D 2 32  ? 34.469  17.453  37.169 1.00 20.11 ?  25  PRO D CA    1 
ATOM   4675 C C     . PRO D 2 32  ? 34.675  18.362  38.370 1.00 18.41 ?  25  PRO D C     1 
ATOM   4676 O O     . PRO D 2 32  ? 33.741  19.069  38.773 1.00 20.38 ?  25  PRO D O     1 
ATOM   4677 C CB    . PRO D 2 32  ? 34.446  15.970  37.573 1.00 17.73 ?  25  PRO D CB    1 
ATOM   4678 C CG    . PRO D 2 32  ? 35.079  15.238  36.437 1.00 17.51 ?  25  PRO D CG    1 
ATOM   4679 C CD    . PRO D 2 32  ? 36.085  16.172  35.835 1.00 19.05 ?  25  PRO D CD    1 
ATOM   4680 N N     . GLU D 2 33  ? 35.870  18.350  38.969 1.00 19.81 ?  26  GLU D N     1 
ATOM   4681 C CA    . GLU D 2 33  ? 36.098  19.153  40.166 1.00 19.89 ?  26  GLU D CA    1 
ATOM   4682 C C     . GLU D 2 33  ? 35.965  20.642  39.871 1.00 19.48 ?  26  GLU D C     1 
ATOM   4683 O O     . GLU D 2 33  ? 35.377  21.388  40.662 1.00 22.10 ?  26  GLU D O     1 
ATOM   4684 C CB    . GLU D 2 33  ? 37.470  18.841  40.759 1.00 26.31 ?  26  GLU D CB    1 
ATOM   4685 C CG    . GLU D 2 33  ? 37.412  18.076  42.075 1.00 28.34 ?  26  GLU D CG    1 
ATOM   4686 C CD    . GLU D 2 33  ? 38.722  18.119  42.834 1.00 37.38 ?  26  GLU D CD    1 
ATOM   4687 O OE1   . GLU D 2 33  ? 39.382  19.179  42.818 1.00 36.97 ?  26  GLU D OE1   1 
ATOM   4688 O OE2   . GLU D 2 33  ? 39.090  17.096  43.452 1.00 39.29 -1 26  GLU D OE2   1 
ATOM   4689 N N     . ALA D 2 34  ? 36.513  21.097  38.741 1.00 20.89 ?  27  ALA D N     1 
ATOM   4690 C CA    . ALA D 2 34  ? 36.455  22.519  38.416 1.00 21.35 ?  27  ALA D CA    1 
ATOM   4691 C C     . ALA D 2 34  ? 35.021  22.973  38.188 1.00 20.63 ?  27  ALA D C     1 
ATOM   4692 O O     . ALA D 2 34  ? 34.627  24.052  38.646 1.00 17.77 ?  27  ALA D O     1 
ATOM   4693 C CB    . ALA D 2 34  ? 37.314  22.819  37.190 1.00 25.89 ?  27  ALA D CB    1 
ATOM   4694 N N     . VAL D 2 35  ? 34.229  22.170  37.471 1.00 23.18 ?  28  VAL D N     1 
ATOM   4695 C CA    . VAL D 2 35  ? 32.836  22.532  37.230 1.00 19.26 ?  28  VAL D CA    1 
ATOM   4696 C C     . VAL D 2 35  ? 32.057  22.546  38.538 1.00 20.84 ?  28  VAL D C     1 
ATOM   4697 O O     . VAL D 2 35  ? 31.258  23.457  38.791 1.00 18.86 ?  28  VAL D O     1 
ATOM   4698 C CB    . VAL D 2 35  ? 32.203  21.576  36.204 1.00 22.72 ?  28  VAL D CB    1 
ATOM   4699 C CG1   . VAL D 2 35  ? 30.719  21.864  36.055 1.00 22.56 ?  28  VAL D CG1   1 
ATOM   4700 C CG2   . VAL D 2 35  ? 32.913  21.692  34.865 1.00 25.52 ?  28  VAL D CG2   1 
ATOM   4701 N N     . MET D 2 36  ? 32.278  21.540  39.390 1.00 17.63 ?  29  MET D N     1 
ATOM   4702 C CA    . MET D 2 36  ? 31.543  21.462  40.648 1.00 20.11 ?  29  MET D CA    1 
ATOM   4703 C C     . MET D 2 36  ? 31.894  22.631  41.561 1.00 21.92 ?  29  MET D C     1 
ATOM   4704 O O     . MET D 2 36  ? 31.008  23.228  42.185 1.00 21.53 ?  29  MET D O     1 
ATOM   4705 C CB    . MET D 2 36  ? 31.817  20.124  41.331 1.00 17.36 ?  29  MET D CB    1 
ATOM   4706 C CG    . MET D 2 36  ? 30.925  18.999  40.818 1.00 20.20 ?  29  MET D CG    1 
ATOM   4707 S SD    . MET D 2 36  ? 30.995  17.491  41.802 1.00 20.49 ?  29  MET D SD    1 
ATOM   4708 C CE    . MET D 2 36  ? 32.594  16.843  41.324 1.00 19.43 ?  29  MET D CE    1 
ATOM   4709 N N     . ARG D 2 37  ? 33.184  22.969  41.654 1.00 22.79 ?  30  ARG D N     1 
ATOM   4710 C CA    . ARG D 2 37  ? 33.579  24.145  42.424 1.00 25.13 ?  30  ARG D CA    1 
ATOM   4711 C C     . ARG D 2 37  ? 32.969  25.408  41.832 1.00 23.40 ?  30  ARG D C     1 
ATOM   4712 O O     . ARG D 2 37  ? 32.507  26.289  42.568 1.00 22.51 ?  30  ARG D O     1 
ATOM   4713 C CB    . ARG D 2 37  ? 35.101  24.266  42.471 1.00 27.64 ?  30  ARG D CB    1 
ATOM   4714 C CG    . ARG D 2 37  ? 35.795  23.232  43.339 1.00 29.59 ?  30  ARG D CG    1 
ATOM   4715 C CD    . ARG D 2 37  ? 37.284  23.519  43.442 1.00 35.88 ?  30  ARG D CD    1 
ATOM   4716 N NE    . ARG D 2 37  ? 37.744  23.533  44.826 1.00 43.98 ?  30  ARG D NE    1 
ATOM   4717 C CZ    . ARG D 2 37  ? 37.996  22.442  45.540 1.00 48.82 ?  30  ARG D CZ    1 
ATOM   4718 N NH1   . ARG D 2 37  ? 37.901  21.229  45.013 1.00 45.17 ?  30  ARG D NH1   1 
ATOM   4719 N NH2   . ARG D 2 37  ? 38.368  22.568  46.811 1.00 53.42 ?  30  ARG D NH2   1 
ATOM   4720 N N     . ALA D 2 38  ? 32.956  25.514  40.500 1.00 22.38 ?  31  ALA D N     1 
ATOM   4721 C CA    . ALA D 2 38  ? 32.425  26.701  39.844 1.00 24.42 ?  31  ALA D CA    1 
ATOM   4722 C C     . ALA D 2 38  ? 30.932  26.865  40.080 1.00 23.21 ?  31  ALA D C     1 
ATOM   4723 O O     . ALA D 2 38  ? 30.411  27.971  39.909 1.00 22.66 ?  31  ALA D O     1 
ATOM   4724 C CB    . ALA D 2 38  ? 32.711  26.648  38.340 1.00 21.88 ?  31  ALA D CB    1 
ATOM   4725 N N     . HIS D 2 39  ? 30.234  25.793  40.446 1.00 22.76 ?  32  HIS D N     1 
ATOM   4726 C CA    . HIS D 2 39  ? 28.816  25.867  40.763 1.00 25.68 ?  32  HIS D CA    1 
ATOM   4727 C C     . HIS D 2 39  ? 28.561  25.818  42.265 1.00 21.98 ?  32  HIS D C     1 
ATOM   4728 O O     . HIS D 2 39  ? 27.413  25.643  42.688 1.00 22.57 ?  32  HIS D O     1 
ATOM   4729 C CB    . HIS D 2 39  ? 28.059  24.755  40.038 1.00 21.71 ?  32  HIS D CB    1 
ATOM   4730 C CG    . HIS D 2 39  ? 27.862  25.027  38.579 1.00 26.45 ?  32  HIS D CG    1 
ATOM   4731 N ND1   . HIS D 2 39  ? 28.869  24.871  37.651 1.00 21.71 ?  32  HIS D ND1   1 
ATOM   4732 C CD2   . HIS D 2 39  ? 26.786  25.479  37.892 1.00 22.94 ?  32  HIS D CD2   1 
ATOM   4733 C CE1   . HIS D 2 39  ? 28.417  25.199  36.453 1.00 19.39 ?  32  HIS D CE1   1 
ATOM   4734 N NE2   . HIS D 2 39  ? 27.156  25.573  36.572 1.00 24.53 ?  32  HIS D NE2   1 
ATOM   4735 N N     . GLY D 2 40  ? 29.610  25.962  43.073 1.00 23.33 ?  33  GLY D N     1 
ATOM   4736 C CA    . GLY D 2 40  ? 29.470  26.231  44.490 1.00 23.12 ?  33  GLY D CA    1 
ATOM   4737 C C     . GLY D 2 40  ? 29.414  25.030  45.404 1.00 24.08 ?  33  GLY D C     1 
ATOM   4738 O O     . GLY D 2 40  ? 29.188  25.205  46.609 1.00 27.18 ?  33  GLY D O     1 
ATOM   4739 N N     . LEU D 2 41  ? 29.622  23.825  44.882 1.00 26.21 ?  34  LEU D N     1 
ATOM   4740 C CA    . LEU D 2 41  ? 29.568  22.632  45.717 1.00 26.47 ?  34  LEU D CA    1 
ATOM   4741 C C     . LEU D 2 41  ? 30.675  22.650  46.767 1.00 23.20 ?  34  LEU D C     1 
ATOM   4742 O O     . LEU D 2 41  ? 31.811  23.040  46.490 1.00 20.57 ?  34  LEU D O     1 
ATOM   4743 C CB    . LEU D 2 41  ? 29.681  21.370  44.854 1.00 27.13 ?  34  LEU D CB    1 
ATOM   4744 C CG    . LEU D 2 41  ? 28.376  20.836  44.245 1.00 24.77 ?  34  LEU D CG    1 
ATOM   4745 C CD1   . LEU D 2 41  ? 27.900  21.711  43.097 1.00 22.84 ?  34  LEU D CD1   1 
ATOM   4746 C CD2   . LEU D 2 41  ? 28.557  19.397  43.792 1.00 27.19 ?  34  LEU D CD2   1 
ATOM   4747 N N     . THR D 2 42  ? 30.336  22.223  47.982 1.00 28.36 ?  35  THR D N     1 
ATOM   4748 C CA    . THR D 2 42  ? 31.312  22.168  49.059 1.00 31.15 ?  35  THR D CA    1 
ATOM   4749 C C     . THR D 2 42  ? 32.287  21.014  48.841 1.00 26.97 ?  35  THR D C     1 
ATOM   4750 O O     . THR D 2 42  ? 32.121  20.174  47.950 1.00 22.77 ?  35  THR D O     1 
ATOM   4751 C CB    . THR D 2 42  ? 30.618  22.013  50.413 1.00 28.49 ?  35  THR D CB    1 
ATOM   4752 O OG1   . THR D 2 42  ? 30.024  20.711  50.496 1.00 33.04 ?  35  THR D OG1   1 
ATOM   4753 C CG2   . THR D 2 42  ? 29.546  23.072  50.593 1.00 28.20 ?  35  THR D CG2   1 
ATOM   4754 N N     . ASP D 2 43  ? 33.319  20.980  49.685 1.00 27.18 ?  36  ASP D N     1 
ATOM   4755 C CA    . ASP D 2 43  ? 34.332  19.935  49.572 1.00 32.63 ?  36  ASP D CA    1 
ATOM   4756 C C     . ASP D 2 43  ? 33.771  18.575  49.967 1.00 25.82 ?  36  ASP D C     1 
ATOM   4757 O O     . ASP D 2 43  ? 34.127  17.552  49.368 1.00 20.68 ?  36  ASP D O     1 
ATOM   4758 C CB    . ASP D 2 43  ? 35.551  20.288  50.426 1.00 36.27 ?  36  ASP D CB    1 
ATOM   4759 C CG    . ASP D 2 43  ? 36.269  21.525  49.925 1.00 41.39 ?  36  ASP D CG    1 
ATOM   4760 O OD1   . ASP D 2 43  ? 36.130  21.849  48.724 1.00 36.00 ?  36  ASP D OD1   1 
ATOM   4761 O OD2   . ASP D 2 43  ? 36.975  22.170  50.725 1.00 42.22 -1 36  ASP D OD2   1 
ATOM   4762 N N     . GLU D 2 44  ? 32.899  18.540  50.980 1.00 29.92 ?  37  GLU D N     1 
ATOM   4763 C CA    . GLU D 2 44  ? 32.252  17.282  51.338 1.00 31.21 ?  37  GLU D CA    1 
ATOM   4764 C C     . GLU D 2 44  ? 31.280  16.843  50.251 1.00 28.63 ?  37  GLU D C     1 
ATOM   4765 O O     . GLU D 2 44  ? 31.140  15.643  49.985 1.00 26.60 ?  37  GLU D O     1 
ATOM   4766 C CB    . GLU D 2 44  ? 31.542  17.407  52.685 1.00 35.09 ?  37  GLU D CB    1 
ATOM   4767 C CG    . GLU D 2 44  ? 30.760  18.692  52.874 1.00 39.55 ?  37  GLU D CG    1 
ATOM   4768 C CD    . GLU D 2 44  ? 29.676  18.561  53.923 1.00 42.93 ?  37  GLU D CD    1 
ATOM   4769 O OE1   . GLU D 2 44  ? 29.978  18.740  55.122 1.00 41.53 ?  37  GLU D OE1   1 
ATOM   4770 O OE2   . GLU D 2 44  ? 28.518  18.289  53.546 1.00 42.61 -1 37  GLU D OE2   1 
ATOM   4771 N N     . GLN D 2 45  ? 30.593  17.801  49.618 1.00 31.60 ?  38  GLN D N     1 
ATOM   4772 C CA    . GLN D 2 45  ? 29.715  17.457  48.504 1.00 23.93 ?  38  GLN D CA    1 
ATOM   4773 C C     . GLN D 2 45  ? 30.524  16.922  47.332 1.00 22.73 ?  38  GLN D C     1 
ATOM   4774 O O     . GLN D 2 45  ? 30.139  15.931  46.700 1.00 26.65 ?  38  GLN D O     1 
ATOM   4775 C CB    . GLN D 2 45  ? 28.895  18.675  48.077 1.00 25.09 ?  38  GLN D CB    1 
ATOM   4776 C CG    . GLN D 2 45  ? 27.773  19.046  49.037 1.00 27.74 ?  38  GLN D CG    1 
ATOM   4777 C CD    . GLN D 2 45  ? 27.135  20.381  48.705 1.00 31.91 ?  38  GLN D CD    1 
ATOM   4778 O OE1   . GLN D 2 45  ? 27.559  21.070  47.778 1.00 31.52 ?  38  GLN D OE1   1 
ATOM   4779 N NE2   . GLN D 2 45  ? 26.114  20.757  49.469 1.00 29.37 ?  38  GLN D NE2   1 
ATOM   4780 N N     . ILE D 2 46  ? 31.653  17.568  47.030 1.00 21.05 ?  39  ILE D N     1 
ATOM   4781 C CA    . ILE D 2 46  ? 32.514  17.093  45.953 1.00 22.59 ?  39  ILE D CA    1 
ATOM   4782 C C     . ILE D 2 46  ? 33.098  15.733  46.308 1.00 24.13 ?  39  ILE D C     1 
ATOM   4783 O O     . ILE D 2 46  ? 33.153  14.828  45.468 1.00 26.07 ?  39  ILE D O     1 
ATOM   4784 C CB    . ILE D 2 46  ? 33.614  18.127  45.656 1.00 20.87 ?  39  ILE D CB    1 
ATOM   4785 C CG1   . ILE D 2 46  ? 33.012  19.350  44.960 1.00 25.28 ?  39  ILE D CG1   1 
ATOM   4786 C CG2   . ILE D 2 46  ? 34.719  17.519  44.804 1.00 19.65 ?  39  ILE D CG2   1 
ATOM   4787 C CD1   . ILE D 2 46  ? 34.003  20.461  44.724 1.00 21.73 ?  39  ILE D CD1   1 
ATOM   4788 N N     . ASN D 2 47  ? 33.529  15.562  47.561 1.00 20.58 ?  40  ASN D N     1 
ATOM   4789 C CA    . ASN D 2 47  ? 34.052  14.269  47.994 1.00 23.71 ?  40  ASN D CA    1 
ATOM   4790 C C     . ASN D 2 47  ? 32.992  13.183  47.875 1.00 24.04 ?  40  ASN D C     1 
ATOM   4791 O O     . ASN D 2 47  ? 33.294  12.053  47.471 1.00 24.35 ?  40  ASN D O     1 
ATOM   4792 C CB    . ASN D 2 47  ? 34.568  14.355  49.431 1.00 25.89 ?  40  ASN D CB    1 
ATOM   4793 C CG    . ASN D 2 47  ? 34.778  12.989  50.056 1.00 35.89 ?  40  ASN D CG    1 
ATOM   4794 O OD1   . ASN D 2 47  ? 33.964  12.530  50.860 1.00 30.25 ?  40  ASN D OD1   1 
ATOM   4795 N ND2   . ASN D 2 47  ? 35.867  12.328  49.682 1.00 27.88 ?  40  ASN D ND2   1 
ATOM   4796 N N     . ALA D 2 48  ? 31.747  13.502  48.237 1.00 22.39 ?  41  ALA D N     1 
ATOM   4797 C CA    . ALA D 2 48  ? 30.664  12.537  48.084 1.00 28.84 ?  41  ALA D CA    1 
ATOM   4798 C C     . ALA D 2 48  ? 30.519  12.109  46.630 1.00 24.55 ?  41  ALA D C     1 
ATOM   4799 O O     . ALA D 2 48  ? 30.285  10.929  46.341 1.00 29.99 ?  41  ALA D O     1 
ATOM   4800 C CB    . ALA D 2 48  ? 29.353  13.127  48.603 1.00 20.44 ?  41  ALA D CB    1 
ATOM   4801 N N     . VAL D 2 49  ? 30.663  13.057  45.699 1.00 18.48 ?  42  VAL D N     1 
ATOM   4802 C CA    . VAL D 2 49  ? 30.502  12.745  44.282 1.00 21.71 ?  42  VAL D CA    1 
ATOM   4803 C C     . VAL D 2 49  ? 31.634  11.848  43.797 1.00 22.48 ?  42  VAL D C     1 
ATOM   4804 O O     . VAL D 2 49  ? 31.402  10.863  43.086 1.00 29.30 ?  42  VAL D O     1 
ATOM   4805 C CB    . VAL D 2 49  ? 30.419  14.043  43.456 1.00 22.45 ?  42  VAL D CB    1 
ATOM   4806 C CG1   . VAL D 2 49  ? 30.690  13.764  41.985 1.00 22.77 ?  42  VAL D CG1   1 
ATOM   4807 C CG2   . VAL D 2 49  ? 29.063  14.707  43.642 1.00 22.23 ?  42  VAL D CG2   1 
ATOM   4808 N N     . MET D 2 50  ? 32.873  12.157  44.188 1.00 25.29 ?  43  MET D N     1 
ATOM   4809 C CA    . MET D 2 50  ? 34.021  11.440  43.646 1.00 28.44 ?  43  MET D CA    1 
ATOM   4810 C C     . MET D 2 50  ? 34.147  10.036  44.223 1.00 31.37 ?  43  MET D C     1 
ATOM   4811 O O     . MET D 2 50  ? 34.789  9.182   43.603 1.00 31.03 ?  43  MET D O     1 
ATOM   4812 C CB    . MET D 2 50  ? 35.308  12.232  43.896 1.00 28.11 ?  43  MET D CB    1 
ATOM   4813 C CG    . MET D 2 50  ? 35.247  13.688  43.449 1.00 28.69 ?  43  MET D CG    1 
ATOM   4814 S SD    . MET D 2 50  ? 34.737  13.911  41.733 1.00 30.22 ?  43  MET D SD    1 
ATOM   4815 C CE    . MET D 2 50  ? 35.981  12.955  40.873 1.00 26.52 ?  43  MET D CE    1 
ATOM   4816 N N     . THR D 2 51  ? 33.558  9.780   45.390 1.00 25.93 ?  44  THR D N     1 
ATOM   4817 C CA    . THR D 2 51  ? 33.556  8.451   45.981 1.00 25.89 ?  44  THR D CA    1 
ATOM   4818 C C     . THR D 2 51  ? 32.286  7.674   45.665 1.00 26.90 ?  44  THR D C     1 
ATOM   4819 O O     . THR D 2 51  ? 32.205  6.485   45.997 1.00 33.39 ?  44  THR D O     1 
ATOM   4820 C CB    . THR D 2 51  ? 33.721  8.541   47.506 1.00 24.55 ?  44  THR D CB    1 
ATOM   4821 O OG1   . THR D 2 51  ? 32.589  9.217   48.070 1.00 25.10 ?  44  THR D OG1   1 
ATOM   4822 C CG2   . THR D 2 51  ? 34.988  9.296   47.868 1.00 31.61 ?  44  THR D CG2   1 
ATOM   4823 N N     . GLY D 2 52  ? 31.307  8.307   45.026 1.00 26.82 ?  45  GLY D N     1 
ATOM   4824 C CA    . GLY D 2 52  ? 30.065  7.640   44.672 1.00 32.78 ?  45  GLY D CA    1 
ATOM   4825 C C     . GLY D 2 52  ? 29.151  7.344   45.842 1.00 35.86 ?  45  GLY D C     1 
ATOM   4826 O O     . GLY D 2 52  ? 28.468  6.313   45.845 1.00 37.36 ?  45  GLY D O     1 
ATOM   4827 N N     . ASP D 2 53  ? 29.127  8.218   46.846 1.00 34.18 ?  46  ASP D N     1 
ATOM   4828 C CA    . ASP D 2 53  ? 28.282  8.038   48.030 1.00 35.10 ?  46  ASP D CA    1 
ATOM   4829 C C     . ASP D 2 53  ? 26.987  8.820   47.818 1.00 36.99 ?  46  ASP D C     1 
ATOM   4830 O O     . ASP D 2 53  ? 26.878  9.990   48.191 1.00 29.73 ?  46  ASP D O     1 
ATOM   4831 C CB    . ASP D 2 53  ? 29.011  8.487   49.293 1.00 33.70 ?  46  ASP D CB    1 
ATOM   4832 C CG    . ASP D 2 53  ? 28.363  7.956   50.559 1.00 40.52 ?  46  ASP D CG    1 
ATOM   4833 O OD1   . ASP D 2 53  ? 27.119  8.025   50.675 1.00 40.01 ?  46  ASP D OD1   1 
ATOM   4834 O OD2   . ASP D 2 53  ? 29.097  7.474   51.447 1.00 41.21 -1 46  ASP D OD2   1 
ATOM   4835 N N     . MET D 2 54  ? 25.994  8.160   47.213 1.00 37.19 ?  47  MET D N     1 
ATOM   4836 C CA    . MET D 2 54  ? 24.723  8.826   46.950 1.00 39.86 ?  47  MET D CA    1 
ATOM   4837 C C     . MET D 2 54  ? 23.950  9.083   48.236 1.00 43.00 ?  47  MET D C     1 
ATOM   4838 O O     . MET D 2 54  ? 23.210  10.072  48.325 1.00 41.33 ?  47  MET D O     1 
ATOM   4839 C CB    . MET D 2 54  ? 23.875  7.987   45.993 1.00 39.38 ?  47  MET D CB    1 
ATOM   4840 C CG    . MET D 2 54  ? 24.528  7.698   44.652 1.00 34.62 ?  47  MET D CG    1 
ATOM   4841 S SD    . MET D 2 54  ? 24.988  9.191   43.752 1.00 30.38 ?  47  MET D SD    1 
ATOM   4842 C CE    . MET D 2 54  ? 26.775  9.086   43.822 1.00 30.32 ?  47  MET D CE    1 
ATOM   4843 N N     . GLU D 2 55  ? 24.102  8.202   49.231 1.00 44.05 ?  48  GLU D N     1 
ATOM   4844 C CA    . GLU D 2 55  ? 23.431  8.389   50.513 1.00 46.73 ?  48  GLU D CA    1 
ATOM   4845 C C     . GLU D 2 55  ? 23.794  9.734   51.127 1.00 41.15 ?  48  GLU D C     1 
ATOM   4846 O O     . GLU D 2 55  ? 22.918  10.485  51.574 1.00 43.67 ?  48  GLU D O     1 
ATOM   4847 C CB    . GLU D 2 55  ? 23.780  7.244   51.460 1.00 47.39 ?  48  GLU D CB    1 
ATOM   4848 C CG    . GLU D 2 55  ? 22.814  7.101   52.628 1.00 57.78 ?  48  GLU D CG    1 
ATOM   4849 C CD    . GLU D 2 55  ? 21.415  6.723   52.180 1.00 55.60 ?  48  GLU D CD    1 
ATOM   4850 O OE1   . GLU D 2 55  ? 21.216  5.559   51.770 1.00 58.09 ?  48  GLU D OE1   1 
ATOM   4851 O OE2   . GLU D 2 55  ? 20.518  7.591   52.233 1.00 44.11 -1 48  GLU D OE2   1 
ATOM   4852 N N     . LYS D 2 56  ? 25.092  10.054  51.166 1.00 44.71 ?  49  LYS D N     1 
ATOM   4853 C CA    . LYS D 2 56  ? 25.512  11.308  51.780 1.00 45.59 ?  49  LYS D CA    1 
ATOM   4854 C C     . LYS D 2 56  ? 25.036  12.501  50.965 1.00 46.49 ?  49  LYS D C     1 
ATOM   4855 O O     . LYS D 2 56  ? 24.708  13.547  51.536 1.00 47.82 ?  49  LYS D O     1 
ATOM   4856 C CB    . LYS D 2 56  ? 27.032  11.345  51.936 1.00 42.05 ?  49  LYS D CB    1 
ATOM   4857 C CG    . LYS D 2 56  ? 27.526  12.318  52.998 1.00 39.78 ?  49  LYS D CG    1 
ATOM   4858 C CD    . LYS D 2 56  ? 28.242  11.600  54.132 1.00 47.70 ?  49  LYS D CD    1 
ATOM   4859 C CE    . LYS D 2 56  ? 29.068  12.566  54.968 1.00 54.72 ?  49  LYS D CE    1 
ATOM   4860 N NZ    . LYS D 2 56  ? 28.219  13.573  55.666 1.00 50.28 ?  49  LYS D NZ    1 
ATOM   4861 N N     . LEU D 2 57  ? 24.967  12.354  49.638 1.00 41.71 ?  50  LEU D N     1 
ATOM   4862 C CA    . LEU D 2 57  ? 24.503  13.452  48.798 1.00 39.90 ?  50  LEU D CA    1 
ATOM   4863 C C     . LEU D 2 57  ? 23.056  13.807  49.116 1.00 45.34 ?  50  LEU D C     1 
ATOM   4864 O O     . LEU D 2 57  ? 22.692  14.988  49.165 1.00 45.71 ?  50  LEU D O     1 
ATOM   4865 C CB    . LEU D 2 57  ? 24.651  13.080  47.325 1.00 40.14 ?  50  LEU D CB    1 
ATOM   4866 C CG    . LEU D 2 57  ? 26.055  13.218  46.727 1.00 36.52 ?  50  LEU D CG    1 
ATOM   4867 C CD1   . LEU D 2 57  ? 26.080  12.653  45.322 1.00 30.89 ?  50  LEU D CD1   1 
ATOM   4868 C CD2   . LEU D 2 57  ? 26.502  14.671  46.734 1.00 28.90 ?  50  LEU D CD2   1 
ATOM   4869 N N     . LYS D 2 58  ? 22.215  12.793  49.332 1.00 44.71 ?  51  LYS D N     1 
ATOM   4870 C CA    . LYS D 2 58  ? 20.825  13.050  49.691 1.00 50.16 ?  51  LYS D CA    1 
ATOM   4871 C C     . LYS D 2 58  ? 20.734  13.636  51.093 1.00 53.36 ?  51  LYS D C     1 
ATOM   4872 O O     . LYS D 2 58  ? 19.913  14.524  51.352 1.00 59.23 ?  51  LYS D O     1 
ATOM   4873 C CB    . LYS D 2 58  ? 20.013  11.763  49.579 1.00 47.82 ?  51  LYS D CB    1 
ATOM   4874 C CG    . LYS D 2 58  ? 19.806  11.298  48.149 1.00 46.95 ?  51  LYS D CG    1 
ATOM   4875 C CD    . LYS D 2 58  ? 19.522  9.811   48.071 1.00 55.69 ?  51  LYS D CD    1 
ATOM   4876 C CE    . LYS D 2 58  ? 19.506  9.337   46.628 1.00 47.13 ?  51  LYS D CE    1 
ATOM   4877 N NZ    . LYS D 2 58  ? 19.135  7.901   46.502 1.00 43.44 ?  51  LYS D NZ    1 
ATOM   4878 N N     . THR D 2 59  ? 21.574  13.144  52.007 1.00 49.13 ?  52  THR D N     1 
ATOM   4879 C CA    . THR D 2 59  ? 21.711  13.766  53.319 1.00 53.50 ?  52  THR D CA    1 
ATOM   4880 C C     . THR D 2 59  ? 22.060  15.240  53.176 1.00 55.88 ?  52  THR D C     1 
ATOM   4881 O O     . THR D 2 59  ? 21.418  16.106  53.781 1.00 51.91 ?  52  THR D O     1 
ATOM   4882 C CB    . THR D 2 59  ? 22.772  13.035  54.142 1.00 53.09 ?  52  THR D CB    1 
ATOM   4883 O OG1   . THR D 2 59  ? 22.293  11.730  54.487 1.00 56.51 ?  52  THR D OG1   1 
ATOM   4884 C CG2   . THR D 2 59  ? 23.095  13.804  55.417 1.00 55.88 ?  52  THR D CG2   1 
ATOM   4885 N N     . LEU D 2 60  ? 23.085  15.542  52.376 1.00 49.57 ?  53  LEU D N     1 
ATOM   4886 C CA    . LEU D 2 60  ? 23.571  16.910  52.250 1.00 47.83 ?  53  LEU D CA    1 
ATOM   4887 C C     . LEU D 2 60  ? 22.559  17.823  51.573 1.00 56.02 ?  53  LEU D C     1 
ATOM   4888 O O     . LEU D 2 60  ? 22.655  19.045  51.715 1.00 62.09 ?  53  LEU D O     1 
ATOM   4889 C CB    . LEU D 2 60  ? 24.891  16.925  51.474 1.00 49.15 ?  53  LEU D CB    1 
ATOM   4890 C CG    . LEU D 2 60  ? 26.062  16.214  52.163 1.00 47.88 ?  53  LEU D CG    1 
ATOM   4891 C CD1   . LEU D 2 60  ? 27.379  16.489  51.457 1.00 38.89 ?  53  LEU D CD1   1 
ATOM   4892 C CD2   . LEU D 2 60  ? 26.132  16.598  53.631 1.00 46.04 ?  53  LEU D CD2   1 
ATOM   4893 N N     . SER D 2 61  ? 21.598  17.263  50.849 1.00 56.68 ?  54  SER D N     1 
ATOM   4894 C CA    . SER D 2 61  ? 20.535  18.049  50.241 1.00 59.95 ?  54  SER D CA    1 
ATOM   4895 C C     . SER D 2 61  ? 19.238  17.920  51.023 1.00 56.43 ?  54  SER D C     1 
ATOM   4896 O O     . SER D 2 61  ? 18.206  18.458  50.639 1.00 53.97 ?  54  SER D O     1 
ATOM   4897 C CB    . SER D 2 61  ? 20.308  17.621  48.782 1.00 55.06 ?  54  SER D CB    1 
ATOM   4898 O OG    . SER D 2 61  ? 19.817  18.695  48.004 1.00 57.15 ?  54  SER D OG    1 
ATOM   4899 N N     . TYR D 2 69  ? 10.127  1.140   42.198 1.00 42.74 ?  62  TYR D N     1 
ATOM   4900 C CA    . TYR D 2 69  ? 8.718   0.784   42.197 1.00 51.63 ?  62  TYR D CA    1 
ATOM   4901 C C     . TYR D 2 69  ? 8.420   -0.371  43.155 1.00 55.64 ?  62  TYR D C     1 
ATOM   4902 O O     . TYR D 2 69  ? 7.254   -0.707  43.395 1.00 54.43 ?  62  TYR D O     1 
ATOM   4903 C CB    . TYR D 2 69  ? 8.349   0.419   40.774 1.00 56.17 ?  62  TYR D CB    1 
ATOM   4904 C CG    . TYR D 2 69  ? 6.911   0.555   40.360 1.00 61.18 ?  62  TYR D CG    1 
ATOM   4905 C CD1   . TYR D 2 69  ? 6.042   -0.503  40.517 1.00 62.22 ?  62  TYR D CD1   1 
ATOM   4906 C CD2   . TYR D 2 69  ? 6.421   1.723   39.802 1.00 54.40 ?  62  TYR D CD2   1 
ATOM   4907 C CE1   . TYR D 2 69  ? 4.740   -0.428  40.139 1.00 57.84 ?  62  TYR D CE1   1 
ATOM   4908 C CE2   . TYR D 2 69  ? 5.104   1.810   39.403 1.00 61.68 ?  62  TYR D CE2   1 
ATOM   4909 C CZ    . TYR D 2 69  ? 4.270   0.726   39.584 1.00 58.41 ?  62  TYR D CZ    1 
ATOM   4910 O OH    . TYR D 2 69  ? 2.959   0.767   39.209 1.00 51.31 ?  62  TYR D OH    1 
ATOM   4911 N N     . ASP D 2 70  ? 9.482   -0.998  43.667 1.00 48.89 ?  63  ASP D N     1 
ATOM   4912 C CA    . ASP D 2 70  ? 9.462   -2.056  44.676 1.00 53.61 ?  63  ASP D CA    1 
ATOM   4913 C C     . ASP D 2 70  ? 8.984   -3.396  44.104 1.00 51.84 ?  63  ASP D C     1 
ATOM   4914 O O     . ASP D 2 70  ? 9.679   -4.404  44.266 1.00 53.73 ?  63  ASP D O     1 
ATOM   4915 C CB    . ASP D 2 70  ? 8.638   -1.616  45.893 1.00 46.02 ?  63  ASP D CB    1 
ATOM   4916 C CG    . ASP D 2 70  ? 9.323   -0.499  46.683 1.00 52.07 ?  63  ASP D CG    1 
ATOM   4917 O OD1   . ASP D 2 70  ? 10.575  -0.511  46.788 1.00 50.09 ?  63  ASP D OD1   1 
ATOM   4918 O OD2   . ASP D 2 70  ? 8.619   0.389   47.204 1.00 50.96 ?  63  ASP D OD2   1 
ATOM   4919 N N     . VAL D 2 71  ? 7.823   -3.445  43.436 1.00 51.21 ?  64  VAL D N     1 
ATOM   4920 C CA    . VAL D 2 71  ? 7.443   -4.602  42.625 1.00 51.71 ?  64  VAL D CA    1 
ATOM   4921 C C     . VAL D 2 71  ? 6.549   -4.107  41.498 1.00 56.97 ?  64  VAL D C     1 
ATOM   4922 O O     . VAL D 2 71  ? 5.935   -3.045  41.591 1.00 70.94 ?  64  VAL D O     1 
ATOM   4923 C CB    . VAL D 2 71  ? 6.707   -5.714  43.414 1.00 57.59 ?  64  VAL D CB    1 
ATOM   4924 C CG1   . VAL D 2 71  ? 5.220   -5.404  43.548 1.00 61.01 ?  64  VAL D CG1   1 
ATOM   4925 C CG2   . VAL D 2 71  ? 6.917   -7.080  42.767 1.00 57.54 ?  64  VAL D CG2   1 
ATOM   4926 N N     . ILE D 2 72  ? 6.449   -4.911  40.443 1.00 55.25 ?  65  ILE D N     1 
ATOM   4927 C CA    . ILE D 2 72  ? 5.758   -4.535  39.207 1.00 52.14 ?  65  ILE D CA    1 
ATOM   4928 C C     . ILE D 2 72  ? 4.362   -3.967  39.427 1.00 53.23 ?  65  ILE D C     1 
ATOM   4929 O O     . ILE D 2 72  ? 3.663   -3.646  38.477 1.00 56.89 ?  65  ILE D O     1 
ATOM   4930 C CB    . ILE D 2 72  ? 5.663   -5.738  38.244 1.00 49.52 ?  65  ILE D CB    1 
ATOM   4931 C CG1   . ILE D 2 72  ? 4.854   -6.857  38.887 1.00 59.79 ?  65  ILE D CG1   1 
ATOM   4932 C CG2   . ILE D 2 72  ? 7.052   -6.224  37.869 1.00 44.70 ?  65  ILE D CG2   1 
ATOM   4933 C CD1   . ILE D 2 72  ? 4.896   -8.162  38.114 1.00 51.66 ?  65  ILE D CD1   1 
HETATM 4934 N N     . SAH E 3 .   ? 16.721  1.151   16.633 1.00 17.35 ?  301 SAH A N     1 
HETATM 4935 C CA    . SAH E 3 .   ? 15.354  0.874   16.226 1.00 20.41 ?  301 SAH A CA    1 
HETATM 4936 C CB    . SAH E 3 .   ? 15.302  -0.482  15.517 1.00 16.76 ?  301 SAH A CB    1 
HETATM 4937 C CG    . SAH E 3 .   ? 15.993  -0.503  14.149 1.00 18.49 ?  301 SAH A CG    1 
HETATM 4938 S SD    . SAH E 3 .   ? 16.048  -2.153  13.423 1.00 18.83 ?  301 SAH A SD    1 
HETATM 4939 C C     . SAH E 3 .   ? 14.394  0.911   17.409 1.00 21.60 ?  301 SAH A C     1 
HETATM 4940 O O     . SAH E 3 .   ? 13.299  0.345   17.371 1.00 16.62 ?  301 SAH A O     1 
HETATM 4941 O OXT   . SAH E 3 .   ? 14.703  1.518   18.433 1.00 21.33 ?  301 SAH A OXT   1 
HETATM 4942 C "C5'" . SAH E 3 .   ? 14.591  -2.118  12.360 1.00 19.05 ?  301 SAH A "C5'" 1 
HETATM 4943 C "C4'" . SAH E 3 .   ? 13.489  -2.964  12.977 1.00 18.76 ?  301 SAH A "C4'" 1 
HETATM 4944 O "O4'" . SAH E 3 .   ? 13.002  -2.321  14.137 1.00 17.13 ?  301 SAH A "O4'" 1 
HETATM 4945 C "C3'" . SAH E 3 .   ? 12.300  -3.132  12.051 1.00 21.49 ?  301 SAH A "C3'" 1 
HETATM 4946 O "O3'" . SAH E 3 .   ? 12.466  -4.212  11.165 1.00 17.25 ?  301 SAH A "O3'" 1 
HETATM 4947 C "C2'" . SAH E 3 .   ? 11.209  -3.398  13.051 1.00 19.21 ?  301 SAH A "C2'" 1 
HETATM 4948 O "O2'" . SAH E 3 .   ? 11.279  -4.730  13.501 1.00 19.22 ?  301 SAH A "O2'" 1 
HETATM 4949 C "C1'" . SAH E 3 .   ? 11.595  -2.468  14.180 1.00 19.11 ?  301 SAH A "C1'" 1 
HETATM 4950 N N9    . SAH E 3 .   ? 10.949  -1.179  13.936 1.00 18.44 ?  301 SAH A N9    1 
HETATM 4951 C C8    . SAH E 3 .   ? 11.507  -0.064  13.348 1.00 22.21 ?  301 SAH A C8    1 
HETATM 4952 N N7    . SAH E 3 .   ? 10.552  0.899   13.275 1.00 23.88 ?  301 SAH A N7    1 
HETATM 4953 C C5    . SAH E 3 .   ? 9.407   0.392   13.773 1.00 21.23 ?  301 SAH A C5    1 
HETATM 4954 C C6    . SAH E 3 .   ? 8.140   0.931   13.929 1.00 22.39 ?  301 SAH A C6    1 
HETATM 4955 N N6    . SAH E 3 .   ? 7.881   2.177   13.553 1.00 21.02 ?  301 SAH A N6    1 
HETATM 4956 N N1    . SAH E 3 .   ? 7.143   0.159   14.481 1.00 17.86 ?  301 SAH A N1    1 
HETATM 4957 C C2    . SAH E 3 .   ? 7.394   -1.128  14.876 1.00 16.94 ?  301 SAH A C2    1 
HETATM 4958 N N3    . SAH E 3 .   ? 8.650   -1.661  14.719 1.00 17.59 ?  301 SAH A N3    1 
HETATM 4959 C C4    . SAH E 3 .   ? 9.639   -0.915  14.179 1.00 17.87 ?  301 SAH A C4    1 
HETATM 4960 N N     . SAH F 3 .   ? 9.195   1.058   34.996 1.00 14.10 ?  301 SAH C N     1 
HETATM 4961 C CA    . SAH F 3 .   ? 10.552  0.815   35.453 1.00 18.02 ?  301 SAH C CA    1 
HETATM 4962 C CB    . SAH F 3 .   ? 10.653  -0.556  36.126 1.00 15.82 ?  301 SAH C CB    1 
HETATM 4963 C CG    . SAH F 3 .   ? 9.898   -0.658  37.449 1.00 14.86 ?  301 SAH C CG    1 
HETATM 4964 S SD    . SAH F 3 .   ? 9.926   -2.329  38.139 1.00 21.57 ?  301 SAH C SD    1 
HETATM 4965 C C     . SAH F 3 .   ? 11.528  0.914   34.287 1.00 19.92 ?  301 SAH C C     1 
HETATM 4966 O O     . SAH F 3 .   ? 12.633  0.364   34.326 1.00 14.35 ?  301 SAH C O     1 
HETATM 4967 O OXT   . SAH F 3 .   ? 11.210  1.555   33.281 1.00 15.64 ?  301 SAH C OXT   1 
HETATM 4968 C "C5'" . SAH F 3 .   ? 11.272  -2.204  39.330 1.00 21.41 ?  301 SAH C "C5'" 1 
HETATM 4969 C "C4'" . SAH F 3 .   ? 12.409  -3.016  38.746 1.00 19.77 ?  301 SAH C "C4'" 1 
HETATM 4970 O "O4'" . SAH F 3 .   ? 12.908  -2.371  37.602 1.00 17.80 ?  301 SAH C "O4'" 1 
HETATM 4971 C "C3'" . SAH F 3 .   ? 13.586  -3.166  39.693 1.00 19.79 ?  301 SAH C "C3'" 1 
HETATM 4972 O "O3'" . SAH F 3 .   ? 13.415  -4.244  40.577 1.00 16.82 ?  301 SAH C "O3'" 1 
HETATM 4973 C "C2'" . SAH F 3 .   ? 14.695  -3.425  38.705 1.00 19.30 ?  301 SAH C "C2'" 1 
HETATM 4974 O "O2'" . SAH F 3 .   ? 14.648  -4.761  38.266 1.00 20.37 ?  301 SAH C "O2'" 1 
HETATM 4975 C "C1'" . SAH F 3 .   ? 14.314  -2.499  37.568 1.00 17.85 ?  301 SAH C "C1'" 1 
HETATM 4976 N N9    . SAH F 3 .   ? 14.925  -1.195  37.802 1.00 18.53 ?  301 SAH C N9    1 
HETATM 4977 C C8    . SAH F 3 .   ? 14.344  -0.090  38.385 1.00 18.26 ?  301 SAH C C8    1 
HETATM 4978 N N7    . SAH F 3 .   ? 15.279  0.896   38.442 1.00 21.10 ?  301 SAH C N7    1 
HETATM 4979 C C5    . SAH F 3 .   ? 16.428  0.406   37.932 1.00 23.28 ?  301 SAH C C5    1 
HETATM 4980 C C6    . SAH F 3 .   ? 17.680  0.967   37.755 1.00 23.26 ?  301 SAH C C6    1 
HETATM 4981 N N6    . SAH F 3 .   ? 17.911  2.221   38.121 1.00 20.35 ?  301 SAH C N6    1 
HETATM 4982 N N1    . SAH F 3 .   ? 18.684  0.208   37.195 1.00 18.69 ?  301 SAH C N1    1 
HETATM 4983 C C2    . SAH F 3 .   ? 18.455  -1.088  36.814 1.00 17.94 ?  301 SAH C C2    1 
HETATM 4984 N N3    . SAH F 3 .   ? 17.212  -1.641  36.992 1.00 17.58 ?  301 SAH C N3    1 
HETATM 4985 C C4    . SAH F 3 .   ? 16.221  -0.908  37.541 1.00 17.50 ?  301 SAH C C4    1 
HETATM 4986 O O     . HOH G 4 .   ? 19.025  -6.595  1.851  1.00 50.62 ?  401 HOH A O     1 
HETATM 4987 O O     . HOH G 4 .   ? -3.431  -3.239  29.183 1.00 25.12 ?  402 HOH A O     1 
HETATM 4988 O O     . HOH G 4 .   ? 16.909  7.963   6.690  1.00 25.91 ?  403 HOH A O     1 
HETATM 4989 O O     . HOH G 4 .   ? 11.607  22.903  14.895 1.00 41.79 ?  404 HOH A O     1 
HETATM 4990 O O     . HOH G 4 .   ? 4.463   -18.436 -1.000 1.00 39.73 ?  405 HOH A O     1 
HETATM 4991 O O     . HOH G 4 .   ? -2.531  -18.536 4.531  1.00 39.48 ?  406 HOH A O     1 
HETATM 4992 O O     . HOH G 4 .   ? 2.535   -22.660 31.041 1.00 36.82 ?  407 HOH A O     1 
HETATM 4993 O O     . HOH G 4 .   ? -6.983  -10.277 20.483 1.00 41.30 ?  408 HOH A O     1 
HETATM 4994 O O     . HOH G 4 .   ? 5.544   -27.324 21.463 1.00 32.45 ?  409 HOH A O     1 
HETATM 4995 O O     . HOH G 4 .   ? 2.534   2.078   9.857  1.00 25.83 ?  410 HOH A O     1 
HETATM 4996 O O     . HOH G 4 .   ? 6.426   -27.458 12.477 1.00 32.09 ?  411 HOH A O     1 
HETATM 4997 O O     . HOH G 4 .   ? 34.693  20.984  18.638 1.00 35.63 ?  412 HOH A O     1 
HETATM 4998 O O     . HOH G 4 .   ? 12.244  18.029  19.419 1.00 20.42 ?  413 HOH A O     1 
HETATM 4999 O O     . HOH G 4 .   ? 28.538  -4.944  -1.042 1.00 35.52 ?  414 HOH A O     1 
HETATM 5000 O O     . HOH G 4 .   ? -6.075  -18.676 8.087  1.00 40.39 ?  415 HOH A O     1 
HETATM 5001 O O     . HOH G 4 .   ? 5.765   -16.445 -3.164 1.00 34.64 ?  416 HOH A O     1 
HETATM 5002 O O     . HOH G 4 .   ? -3.182  -3.011  8.692  1.00 31.20 ?  417 HOH A O     1 
HETATM 5003 O O     . HOH G 4 .   ? -3.083  2.151   21.462 1.00 36.73 ?  418 HOH A O     1 
HETATM 5004 O O     . HOH G 4 .   ? 40.042  13.833  17.533 1.00 24.25 ?  419 HOH A O     1 
HETATM 5005 O O     . HOH G 4 .   ? 14.192  -6.426  23.233 1.00 31.15 ?  420 HOH A O     1 
HETATM 5006 O O     . HOH G 4 .   ? 21.373  -3.970  -0.520 1.00 32.66 ?  421 HOH A O     1 
HETATM 5007 O O     . HOH G 4 .   ? 32.215  -4.106  9.446  1.00 30.50 ?  422 HOH A O     1 
HETATM 5008 O O     . HOH G 4 .   ? 4.634   -16.172 22.501 1.00 17.47 ?  423 HOH A O     1 
HETATM 5009 O O     . HOH G 4 .   ? -3.492  9.805   9.982  1.00 22.01 ?  424 HOH A O     1 
HETATM 5010 O O     . HOH G 4 .   ? 16.511  -25.074 16.317 1.00 25.35 ?  425 HOH A O     1 
HETATM 5011 O O     . HOH G 4 .   ? 40.141  1.114   14.364 1.00 35.34 ?  426 HOH A O     1 
HETATM 5012 O O     . HOH G 4 .   ? 4.199   -9.695  29.695 1.00 26.03 ?  427 HOH A O     1 
HETATM 5013 O O     . HOH G 4 .   ? 23.431  24.521  26.396 1.00 32.01 ?  428 HOH A O     1 
HETATM 5014 O O     . HOH G 4 .   ? 18.508  10.457  8.200  1.00 17.50 ?  429 HOH A O     1 
HETATM 5015 O O     . HOH G 4 .   ? 20.901  22.661  25.113 1.00 27.13 ?  430 HOH A O     1 
HETATM 5016 O O     . HOH G 4 .   ? 21.719  22.048  6.501  1.00 34.79 ?  431 HOH A O     1 
HETATM 5017 O O     . HOH G 4 .   ? 31.657  19.868  10.340 1.00 38.20 ?  432 HOH A O     1 
HETATM 5018 O O     . HOH G 4 .   ? 4.679   -25.368 2.648  1.00 47.00 ?  433 HOH A O     1 
HETATM 5019 O O     . HOH G 4 .   ? 3.583   -11.614 3.534  1.00 31.81 ?  434 HOH A O     1 
HETATM 5020 O O     . HOH G 4 .   ? 21.119  -4.671  -2.732 1.00 30.69 ?  435 HOH A O     1 
HETATM 5021 O O     . HOH G 4 .   ? 11.398  12.598  18.455 1.00 18.85 ?  436 HOH A O     1 
HETATM 5022 O O     . HOH G 4 .   ? 13.871  21.412  14.854 1.00 24.70 ?  437 HOH A O     1 
HETATM 5023 O O     . HOH G 4 .   ? -3.994  -15.836 3.375  1.00 41.17 ?  438 HOH A O     1 
HETATM 5024 O O     . HOH G 4 .   ? 0.480   -12.215 29.605 1.00 29.29 ?  439 HOH A O     1 
HETATM 5025 O O     . HOH G 4 .   ? 18.910  8.916   23.270 1.00 16.48 ?  440 HOH A O     1 
HETATM 5026 O O     . HOH G 4 .   ? -1.580  -18.831 35.504 1.00 26.79 ?  441 HOH A O     1 
HETATM 5027 O O     . HOH G 4 .   ? 19.644  25.356  15.598 1.00 40.87 ?  442 HOH A O     1 
HETATM 5028 O O     . HOH G 4 .   ? 38.209  11.914  22.636 1.00 21.80 ?  443 HOH A O     1 
HETATM 5029 O O     . HOH G 4 .   ? 5.177   13.165  16.686 1.00 19.64 ?  444 HOH A O     1 
HETATM 5030 O O     . HOH G 4 .   ? 14.424  -24.082 17.900 1.00 20.30 ?  445 HOH A O     1 
HETATM 5031 O O     . HOH G 4 .   ? 30.811  -3.242  18.733 1.00 34.03 ?  446 HOH A O     1 
HETATM 5032 O O     . HOH G 4 .   ? 1.509   -26.055 17.612 1.00 34.80 ?  447 HOH A O     1 
HETATM 5033 O O     . HOH G 4 .   ? 3.050   -24.330 22.915 1.00 27.05 ?  448 HOH A O     1 
HETATM 5034 O O     . HOH G 4 .   ? 7.289   -22.029 29.797 1.00 28.65 ?  449 HOH A O     1 
HETATM 5035 O O     . HOH G 4 .   ? -1.901  1.511   26.826 1.00 20.49 ?  450 HOH A O     1 
HETATM 5036 O O     . HOH G 4 .   ? 21.725  9.516   30.466 1.00 34.46 ?  451 HOH A O     1 
HETATM 5037 O O     . HOH G 4 .   ? 22.821  23.738  16.347 1.00 26.73 ?  452 HOH A O     1 
HETATM 5038 O O     . HOH G 4 .   ? 35.293  1.223   6.353  1.00 36.67 ?  453 HOH A O     1 
HETATM 5039 O O     . HOH G 4 .   ? -3.166  -20.294 20.583 1.00 34.65 ?  454 HOH A O     1 
HETATM 5040 O O     . HOH G 4 .   ? 18.868  -22.020 21.801 1.00 19.83 ?  455 HOH A O     1 
HETATM 5041 O O     . HOH G 4 .   ? 7.590   -11.870 34.091 1.00 17.27 ?  456 HOH A O     1 
HETATM 5042 O O     . HOH G 4 .   ? 36.781  -0.890  21.949 1.00 21.47 ?  457 HOH A O     1 
HETATM 5043 O O     . HOH G 4 .   ? 13.744  1.956   24.691 1.00 14.96 ?  458 HOH A O     1 
HETATM 5044 O O     . HOH G 4 .   ? 43.326  8.927   23.922 1.00 30.41 ?  459 HOH A O     1 
HETATM 5045 O O     . HOH G 4 .   ? 14.816  -21.458 16.169 1.00 27.94 ?  460 HOH A O     1 
HETATM 5046 O O     . HOH G 4 .   ? 4.979   6.092   17.886 1.00 30.88 ?  461 HOH A O     1 
HETATM 5047 O O     . HOH G 4 .   ? 4.372   -4.781  1.547  1.00 38.53 ?  462 HOH A O     1 
HETATM 5048 O O     . HOH G 4 .   ? 30.233  -0.691  21.717 1.00 25.05 ?  463 HOH A O     1 
HETATM 5049 O O     . HOH G 4 .   ? -6.878  -16.275 15.246 1.00 42.13 ?  464 HOH A O     1 
HETATM 5050 O O     . HOH G 4 .   ? 8.163   -28.763 39.267 1.00 39.89 ?  465 HOH A O     1 
HETATM 5051 O O     . HOH G 4 .   ? 42.399  7.137   14.868 1.00 28.32 ?  466 HOH A O     1 
HETATM 5052 O O     . HOH G 4 .   ? 9.874   4.007   12.265 1.00 20.30 ?  467 HOH A O     1 
HETATM 5053 O O     . HOH G 4 .   ? 2.781   4.667   17.687 1.00 31.82 ?  468 HOH A O     1 
HETATM 5054 O O     . HOH G 4 .   ? 1.012   -19.665 2.791  1.00 43.43 ?  469 HOH A O     1 
HETATM 5055 O O     . HOH G 4 .   ? 21.693  -21.554 18.863 1.00 29.41 ?  470 HOH A O     1 
HETATM 5056 O O     . HOH G 4 .   ? 18.002  2.677   14.787 1.00 15.95 ?  471 HOH A O     1 
HETATM 5057 O O     . HOH G 4 .   ? 8.804   11.054  11.827 1.00 27.36 ?  472 HOH A O     1 
HETATM 5058 O O     . HOH G 4 .   ? -0.209  8.299   17.317 1.00 31.14 ?  473 HOH A O     1 
HETATM 5059 O O     . HOH G 4 .   ? 21.271  -5.421  -9.863 1.00 35.10 ?  474 HOH A O     1 
HETATM 5060 O O     . HOH G 4 .   ? 27.824  0.801   22.336 1.00 17.70 ?  475 HOH A O     1 
HETATM 5061 O O     . HOH G 4 .   ? 32.554  11.469  7.305  1.00 23.22 ?  476 HOH A O     1 
HETATM 5062 O O     . HOH G 4 .   ? 34.966  16.594  21.320 1.00 37.90 ?  477 HOH A O     1 
HETATM 5063 O O     . HOH G 4 .   ? 1.171   -16.590 29.565 1.00 22.52 ?  478 HOH A O     1 
HETATM 5064 O O     . HOH G 4 .   ? -3.002  -14.347 20.474 1.00 25.66 ?  479 HOH A O     1 
HETATM 5065 O O     . HOH G 4 .   ? 10.055  -5.734  9.162  1.00 18.05 ?  480 HOH A O     1 
HETATM 5066 O O     . HOH G 4 .   ? 0.364   3.144   10.990 1.00 36.20 ?  481 HOH A O     1 
HETATM 5067 O O     . HOH G 4 .   ? -2.049  -25.678 14.291 1.00 27.64 ?  482 HOH A O     1 
HETATM 5068 O O     . HOH G 4 .   ? 14.677  -25.689 50.748 1.00 32.97 ?  483 HOH A O     1 
HETATM 5069 O O     . HOH G 4 .   ? 4.249   -7.476  2.026  1.00 26.03 ?  484 HOH A O     1 
HETATM 5070 O O     . HOH G 4 .   ? -0.225  -20.873 6.155  1.00 34.35 ?  485 HOH A O     1 
HETATM 5071 O O     . HOH G 4 .   ? 14.616  -10.981 9.735  1.00 17.86 ?  486 HOH A O     1 
HETATM 5072 O O     . HOH G 4 .   ? 16.278  9.885   23.061 1.00 15.82 ?  487 HOH A O     1 
HETATM 5073 O O     . HOH G 4 .   ? 2.238   -28.202 32.670 1.00 46.37 ?  488 HOH A O     1 
HETATM 5074 O O     . HOH G 4 .   ? -2.051  -7.052  5.500  1.00 29.86 ?  489 HOH A O     1 
HETATM 5075 O O     . HOH G 4 .   ? 14.115  8.742   22.898 1.00 28.03 ?  490 HOH A O     1 
HETATM 5076 O O     . HOH G 4 .   ? 4.273   8.027   8.829  1.00 25.32 ?  491 HOH A O     1 
HETATM 5077 O O     . HOH G 4 .   ? 4.755   6.983   20.722 1.00 33.20 ?  492 HOH A O     1 
HETATM 5078 O O     . HOH G 4 .   ? 4.854   4.322   11.010 1.00 19.14 ?  493 HOH A O     1 
HETATM 5079 O O     . HOH G 4 .   ? 25.229  -4.429  -8.379 1.00 41.69 ?  494 HOH A O     1 
HETATM 5080 O O     . HOH G 4 .   ? 12.298  21.182  17.439 1.00 37.16 ?  495 HOH A O     1 
HETATM 5081 O O     . HOH G 4 .   ? 3.423   4.199   21.929 1.00 24.35 ?  496 HOH A O     1 
HETATM 5082 O O     . HOH G 4 .   ? 19.097  14.139  3.576  1.00 35.70 ?  497 HOH A O     1 
HETATM 5083 O O     . HOH G 4 .   ? 7.547   -22.564 1.710  1.00 41.84 ?  498 HOH A O     1 
HETATM 5084 O O     . HOH G 4 .   ? -2.346  -14.706 24.441 1.00 29.34 ?  499 HOH A O     1 
HETATM 5085 O O     . HOH G 4 .   ? -4.177  -1.194  12.599 1.00 31.30 ?  500 HOH A O     1 
HETATM 5086 O O     . HOH G 4 .   ? 37.515  6.243   25.412 1.00 36.91 ?  501 HOH A O     1 
HETATM 5087 O O     . HOH G 4 .   ? 28.068  4.290   26.348 1.00 20.86 ?  502 HOH A O     1 
HETATM 5088 O O     . HOH G 4 .   ? 23.359  3.420   -8.362 1.00 52.23 ?  503 HOH A O     1 
HETATM 5089 O O     . HOH G 4 .   ? 34.258  10.188  5.455  1.00 31.05 ?  504 HOH A O     1 
HETATM 5090 O O     . HOH G 4 .   ? 13.137  -24.312 14.998 1.00 26.40 ?  505 HOH A O     1 
HETATM 5091 O O     . HOH G 4 .   ? 37.122  2.747   9.679  1.00 38.38 ?  506 HOH A O     1 
HETATM 5092 O O     . HOH G 4 .   ? 9.828   -24.876 8.528  1.00 34.56 ?  507 HOH A O     1 
HETATM 5093 O O     . HOH G 4 .   ? 31.759  11.010  24.165 1.00 24.76 ?  508 HOH A O     1 
HETATM 5094 O O     . HOH G 4 .   ? 19.400  8.972   27.273 1.00 24.95 ?  509 HOH A O     1 
HETATM 5095 O O     . HOH G 4 .   ? 14.642  -3.274  23.513 1.00 36.73 ?  510 HOH A O     1 
HETATM 5096 O O     . HOH G 4 .   ? 30.405  14.093  20.796 1.00 18.27 ?  511 HOH A O     1 
HETATM 5097 O O     . HOH G 4 .   ? 19.930  16.386  6.311  1.00 34.87 ?  512 HOH A O     1 
HETATM 5098 O O     . HOH G 4 .   ? 12.440  10.740  15.489 1.00 22.77 ?  513 HOH A O     1 
HETATM 5099 O O     . HOH G 4 .   ? 0.226   -6.784  30.250 1.00 26.97 ?  514 HOH A O     1 
HETATM 5100 O O     . HOH G 4 .   ? -1.723  -10.077 24.808 1.00 29.68 ?  515 HOH A O     1 
HETATM 5101 O O     . HOH G 4 .   ? 13.637  -22.768 51.735 1.00 37.34 ?  516 HOH A O     1 
HETATM 5102 O O     . HOH G 4 .   ? -4.615  2.010   15.602 1.00 31.21 ?  517 HOH A O     1 
HETATM 5103 O O     . HOH G 4 .   ? 32.674  5.797   4.658  1.00 26.87 ?  518 HOH A O     1 
HETATM 5104 O O     . HOH G 4 .   ? 29.443  22.880  18.087 1.00 32.51 ?  519 HOH A O     1 
HETATM 5105 O O     . HOH G 4 .   ? -3.707  -22.939 33.575 1.00 44.77 ?  520 HOH A O     1 
HETATM 5106 O O     . HOH G 4 .   ? 12.103  13.301  15.053 1.00 20.76 ?  521 HOH A O     1 
HETATM 5107 O O     . HOH G 4 .   ? -4.154  -12.406 20.911 1.00 31.66 ?  522 HOH A O     1 
HETATM 5108 O O     . HOH G 4 .   ? 8.290   -8.273  2.951  1.00 30.20 ?  523 HOH A O     1 
HETATM 5109 O O     . HOH G 4 .   ? 10.394  10.088  13.472 1.00 22.10 ?  524 HOH A O     1 
HETATM 5110 O O     . HOH G 4 .   ? 23.852  14.083  3.551  1.00 19.06 ?  525 HOH A O     1 
HETATM 5111 O O     . HOH G 4 .   ? 13.204  -26.601 17.890 1.00 26.86 ?  526 HOH A O     1 
HETATM 5112 O O     . HOH G 4 .   ? 0.519   -14.609 51.070 1.00 41.43 ?  527 HOH A O     1 
HETATM 5113 O O     . HOH G 4 .   ? 43.560  0.039   21.713 1.00 44.70 ?  528 HOH A O     1 
HETATM 5114 O O     . HOH G 4 .   ? 35.397  21.033  15.149 1.00 31.32 ?  529 HOH A O     1 
HETATM 5115 O O     . HOH G 4 .   ? 39.357  12.032  8.953  1.00 28.53 ?  530 HOH A O     1 
HETATM 5116 O O     . HOH G 4 .   ? -3.008  -12.003 5.380  1.00 34.48 ?  531 HOH A O     1 
HETATM 5117 O O     . HOH G 4 .   ? -0.464  4.855   23.212 1.00 25.81 ?  532 HOH A O     1 
HETATM 5118 O O     . HOH G 4 .   ? 34.886  6.593   26.154 1.00 28.79 ?  533 HOH A O     1 
HETATM 5119 O O     . HOH G 4 .   ? 8.705   -27.311 22.302 1.00 35.86 ?  534 HOH A O     1 
HETATM 5120 O O     . HOH G 4 .   ? -2.078  -6.655  28.799 1.00 33.95 ?  535 HOH A O     1 
HETATM 5121 O O     . HOH G 4 .   ? 14.348  -0.710  24.556 1.00 21.80 ?  536 HOH A O     1 
HETATM 5122 O O     . HOH G 4 .   ? -4.088  1.773   11.790 1.00 37.42 ?  537 HOH A O     1 
HETATM 5123 O O     . HOH G 4 .   ? 27.327  17.753  21.591 1.00 21.46 ?  538 HOH A O     1 
HETATM 5124 O O     . HOH G 4 .   ? 6.678   -13.962 -2.679 1.00 31.40 ?  539 HOH A O     1 
HETATM 5125 O O     . HOH G 4 .   ? -3.510  7.195   10.555 1.00 23.20 ?  540 HOH A O     1 
HETATM 5126 O O     . HOH G 4 .   ? 17.126  20.411  25.335 1.00 29.76 ?  541 HOH A O     1 
HETATM 5127 O O     . HOH G 4 .   ? 40.387  9.761   8.752  1.00 34.73 ?  542 HOH A O     1 
HETATM 5128 O O     . HOH G 4 .   ? 3.070   -26.411 10.188 1.00 32.19 ?  543 HOH A O     1 
HETATM 5129 O O     . HOH G 4 .   ? 9.516   11.103  3.600  1.00 38.91 ?  544 HOH A O     1 
HETATM 5130 O O     . HOH G 4 .   ? -3.640  -11.658 48.082 1.00 31.12 ?  545 HOH A O     1 
HETATM 5131 O O     . HOH G 4 .   ? 32.143  -1.233  2.709  1.00 39.20 ?  546 HOH A O     1 
HETATM 5132 O O     . HOH G 4 .   ? 28.437  24.146  21.370 1.00 45.90 ?  547 HOH A O     1 
HETATM 5133 O O     . HOH G 4 .   ? 17.590  -14.185 -1.334 1.00 41.05 ?  548 HOH A O     1 
HETATM 5134 O O     . HOH G 4 .   ? -7.053  -5.939  13.334 1.00 31.46 ?  549 HOH A O     1 
HETATM 5135 O O     . HOH G 4 .   ? -2.575  -8.836  21.881 1.00 39.07 ?  550 HOH A O     1 
HETATM 5136 O O     . HOH G 4 .   ? 16.872  24.788  20.195 1.00 48.93 ?  551 HOH A O     1 
HETATM 5137 O O     . HOH G 4 .   ? -0.104  -28.129 10.927 1.00 41.55 ?  552 HOH A O     1 
HETATM 5138 O O     . HOH G 4 .   ? 8.842   0.809   6.282  1.00 31.63 ?  553 HOH A O     1 
HETATM 5139 O O     . HOH G 4 .   ? 35.173  2.510   28.389 1.00 41.94 ?  554 HOH A O     1 
HETATM 5140 O O     . HOH G 4 .   ? 0.263   11.199  18.635 1.00 27.46 ?  555 HOH A O     1 
HETATM 5141 O O     . HOH G 4 .   ? -3.233  -18.560 52.380 1.00 35.84 ?  556 HOH A O     1 
HETATM 5142 O O     . HOH G 4 .   ? 27.804  1.103   -3.440 1.00 37.23 ?  557 HOH A O     1 
HETATM 5143 O O     . HOH G 4 .   ? 27.125  4.639   -1.346 1.00 41.31 ?  558 HOH A O     1 
HETATM 5144 O O     . HOH G 4 .   ? -2.707  -4.653  4.908  1.00 27.13 ?  559 HOH A O     1 
HETATM 5145 O O     . HOH G 4 .   ? 8.977   -25.855 3.487  1.00 38.43 ?  560 HOH A O     1 
HETATM 5146 O O     . HOH G 4 .   ? 33.652  -2.676  14.858 1.00 42.91 ?  561 HOH A O     1 
HETATM 5147 O O     . HOH G 4 .   ? -7.655  -14.149 20.796 1.00 37.37 ?  562 HOH A O     1 
HETATM 5148 O O     . HOH G 4 .   ? 32.309  19.627  24.456 1.00 30.55 ?  563 HOH A O     1 
HETATM 5149 O O     . HOH G 4 .   ? 6.330   -29.175 38.309 1.00 33.30 ?  564 HOH A O     1 
HETATM 5150 O O     . HOH G 4 .   ? 31.958  -0.176  23.590 1.00 27.41 ?  565 HOH A O     1 
HETATM 5151 O O     . HOH G 4 .   ? -4.910  -5.114  28.745 1.00 33.69 ?  566 HOH A O     1 
HETATM 5152 O O     . HOH G 4 .   ? 6.154   11.633  21.326 1.00 21.67 ?  567 HOH A O     1 
HETATM 5153 O O     . HOH G 4 .   ? 13.033  -17.585 -2.814 1.00 51.34 ?  568 HOH A O     1 
HETATM 5154 O O     . HOH G 4 .   ? 34.103  13.277  28.340 1.00 28.79 ?  569 HOH A O     1 
HETATM 5155 O O     . HOH G 4 .   ? 14.737  23.787  16.033 1.00 36.23 ?  570 HOH A O     1 
HETATM 5156 O O     . HOH G 4 .   ? 9.613   -26.874 10.214 1.00 40.67 ?  571 HOH A O     1 
HETATM 5157 O O     . HOH G 4 .   ? 5.077   -29.479 5.608  1.00 50.17 ?  572 HOH A O     1 
HETATM 5158 O O     . HOH G 4 .   ? -2.135  -11.805 28.658 1.00 43.93 ?  573 HOH A O     1 
HETATM 5159 O O     . HOH G 4 .   ? -5.066  -3.033  10.059 1.00 48.39 ?  574 HOH A O     1 
HETATM 5160 O O     . HOH G 4 .   ? 11.410  -27.348 23.116 1.00 38.72 ?  575 HOH A O     1 
HETATM 5161 O O     . HOH G 4 .   ? -8.022  -16.297 17.823 1.00 44.04 ?  576 HOH A O     1 
HETATM 5162 O O     . HOH G 4 .   ? 2.391   11.324  20.015 1.00 24.72 ?  577 HOH A O     1 
HETATM 5163 O O     . HOH G 4 .   ? 1.967   -25.198 53.712 1.00 34.99 ?  578 HOH A O     1 
HETATM 5164 O O     . HOH G 4 .   ? 4.417   -22.934 28.197 1.00 34.13 ?  579 HOH A O     1 
HETATM 5165 O O     . HOH G 4 .   ? 36.769  13.968  24.694 1.00 24.87 ?  580 HOH A O     1 
HETATM 5166 O O     . HOH G 4 .   ? -3.575  -8.214  3.968  1.00 34.85 ?  581 HOH A O     1 
HETATM 5167 O O     . HOH G 4 .   ? -8.655  -22.638 29.150 1.00 39.04 ?  582 HOH A O     1 
HETATM 5168 O O     . HOH G 4 .   ? 5.436   -14.829 -5.140 1.00 36.15 ?  583 HOH A O     1 
HETATM 5169 O O     . HOH G 4 .   ? 29.139  15.650  22.292 1.00 23.01 ?  584 HOH A O     1 
HETATM 5170 O O     . HOH G 4 .   ? 16.198  23.914  25.152 1.00 40.59 ?  585 HOH A O     1 
HETATM 5171 O O     . HOH G 4 .   ? -2.967  5.411   21.858 1.00 40.17 ?  586 HOH A O     1 
HETATM 5172 O O     . HOH G 4 .   ? 29.940  12.902  3.642  1.00 39.84 ?  587 HOH A O     1 
HETATM 5173 O O     . HOH G 4 .   ? 37.660  -3.280  21.384 1.00 43.69 ?  588 HOH A O     1 
HETATM 5174 O O     . HOH G 4 .   ? 32.300  8.634   4.167  1.00 37.99 ?  589 HOH A O     1 
HETATM 5175 O O     . HOH G 4 .   ? 5.294   -25.472 23.582 1.00 36.62 ?  590 HOH A O     1 
HETATM 5176 O O     . HOH G 4 .   ? 6.576   -30.451 16.937 1.00 55.78 ?  591 HOH A O     1 
HETATM 5177 O O     . HOH G 4 .   ? -6.749  -2.826  24.250 1.00 38.88 ?  592 HOH A O     1 
HETATM 5178 O O     . HOH G 4 .   ? 11.081  -23.638 55.089 1.00 46.03 ?  593 HOH A O     1 
HETATM 5179 O O     . HOH G 4 .   ? -1.441  -24.942 21.672 1.00 47.24 ?  594 HOH A O     1 
HETATM 5180 O O     . HOH G 4 .   ? 4.840   -28.852 29.733 1.00 43.13 ?  595 HOH A O     1 
HETATM 5181 O O     . HOH G 4 .   ? 11.705  -25.351 25.620 1.00 37.48 ?  596 HOH A O     1 
HETATM 5182 O O     . HOH G 4 .   ? 14.887  21.592  26.253 1.00 42.37 ?  597 HOH A O     1 
HETATM 5183 O O     . HOH G 4 .   ? 30.888  -7.407  12.528 1.00 43.45 ?  598 HOH A O     1 
HETATM 5184 O O     . HOH G 4 .   ? -3.609  -17.103 54.029 1.00 39.04 ?  599 HOH A O     1 
HETATM 5185 O O     . HOH G 4 .   ? -3.807  -23.452 8.323  1.00 37.65 ?  600 HOH A O     1 
HETATM 5186 O O     . HOH G 4 .   ? -5.694  -7.255  27.777 1.00 27.13 ?  601 HOH A O     1 
HETATM 5187 O O     . HOH G 4 .   ? 2.855   -27.066 25.976 1.00 48.52 ?  602 HOH A O     1 
HETATM 5188 O O     . HOH G 4 .   ? -10.429 -21.380 28.357 1.00 40.94 ?  603 HOH A O     1 
HETATM 5189 O O     . HOH G 4 .   ? -11.210 -19.229 30.559 1.00 37.04 ?  604 HOH A O     1 
HETATM 5190 O O     . HOH G 4 .   ? 7.102   -25.700 -1.418 1.00 53.97 ?  605 HOH A O     1 
HETATM 5191 O O     . HOH G 4 .   ? -14.060 -22.057 30.170 1.00 47.99 ?  606 HOH A O     1 
HETATM 5192 O O     . HOH G 4 .   ? 15.485  14.973  -5.816 1.00 61.34 ?  607 HOH A O     1 
HETATM 5193 O O     . HOH H 4 .   ? -9.962  13.039  18.192 1.00 32.27 ?  101 HOH B O     1 
HETATM 5194 O O     . HOH H 4 .   ? -5.777  14.091  0.070  1.00 38.70 ?  102 HOH B O     1 
HETATM 5195 O O     . HOH H 4 .   ? -1.231  5.751   7.871  1.00 39.55 ?  103 HOH B O     1 
HETATM 5196 O O     . HOH H 4 .   ? -0.103  5.558   4.873  1.00 49.19 ?  104 HOH B O     1 
HETATM 5197 O O     . HOH H 4 .   ? 1.589   25.347  12.190 1.00 39.39 ?  105 HOH B O     1 
HETATM 5198 O O     . HOH H 4 .   ? 8.408   18.230  10.425 1.00 28.11 ?  106 HOH B O     1 
HETATM 5199 O O     . HOH H 4 .   ? 5.076   13.337  19.619 1.00 23.28 ?  107 HOH B O     1 
HETATM 5200 O O     . HOH H 4 .   ? 7.721   20.562  24.367 1.00 29.13 ?  108 HOH B O     1 
HETATM 5201 O O     . HOH H 4 .   ? 0.030   23.119  4.396  1.00 38.12 ?  109 HOH B O     1 
HETATM 5202 O O     . HOH H 4 .   ? -6.735  20.428  -1.977 1.00 40.64 ?  110 HOH B O     1 
HETATM 5203 O O     . HOH H 4 .   ? -8.743  23.215  4.679  1.00 37.71 ?  111 HOH B O     1 
HETATM 5204 O O     . HOH H 4 .   ? -10.649 17.874  3.701  1.00 42.52 ?  112 HOH B O     1 
HETATM 5205 O O     . HOH H 4 .   ? -9.531  21.949  20.082 1.00 36.44 ?  113 HOH B O     1 
HETATM 5206 O O     . HOH H 4 .   ? 7.375   23.720  13.849 1.00 36.51 ?  114 HOH B O     1 
HETATM 5207 O O     . HOH H 4 .   ? -4.645  4.805   3.813  1.00 44.40 ?  115 HOH B O     1 
HETATM 5208 O O     . HOH H 4 .   ? 5.951   21.368  4.568  1.00 37.20 ?  116 HOH B O     1 
HETATM 5209 O O     . HOH H 4 .   ? 10.486  23.513  17.535 1.00 39.61 ?  117 HOH B O     1 
HETATM 5210 O O     . HOH H 4 .   ? -11.783 13.338  21.054 1.00 25.65 ?  118 HOH B O     1 
HETATM 5211 O O     . HOH H 4 .   ? -15.581 16.081  8.174  1.00 49.39 ?  119 HOH B O     1 
HETATM 5212 O O     . HOH H 4 .   ? -14.948 17.765  20.634 1.00 37.87 ?  120 HOH B O     1 
HETATM 5213 O O     . HOH H 4 .   ? 0.194   25.573  23.491 1.00 41.36 ?  121 HOH B O     1 
HETATM 5214 O O     . HOH H 4 .   ? 5.275   10.470  -4.480 1.00 47.27 ?  122 HOH B O     1 
HETATM 5215 O O     . HOH H 4 .   ? 5.272   7.534   -4.083 1.00 41.45 ?  123 HOH B O     1 
HETATM 5216 O O     . HOH H 4 .   ? -11.037 15.595  3.854  1.00 44.14 ?  124 HOH B O     1 
HETATM 5217 O O     . HOH H 4 .   ? -1.642  18.873  27.935 1.00 28.86 ?  125 HOH B O     1 
HETATM 5218 O O     . HOH H 4 .   ? -3.409  15.517  29.453 1.00 21.47 ?  126 HOH B O     1 
HETATM 5219 O O     . HOH H 4 .   ? 5.186   19.262  -3.398 1.00 36.29 ?  127 HOH B O     1 
HETATM 5220 O O     . HOH H 4 .   ? -13.645 14.045  7.709  1.00 36.41 ?  128 HOH B O     1 
HETATM 5221 O O     . HOH H 4 .   ? -12.278 22.933  19.524 1.00 19.68 ?  129 HOH B O     1 
HETATM 5222 O O     . HOH H 4 .   ? -11.404 13.903  24.036 1.00 30.95 ?  130 HOH B O     1 
HETATM 5223 O O     . HOH H 4 .   ? -10.194 6.035   9.923  1.00 46.06 ?  131 HOH B O     1 
HETATM 5224 O O     . HOH H 4 .   ? 0.148   26.177  3.161  1.00 41.90 ?  132 HOH B O     1 
HETATM 5225 O O     . HOH H 4 .   ? -5.669  17.680  -6.043 1.00 40.69 ?  133 HOH B O     1 
HETATM 5226 O O     . HOH H 4 .   ? -2.050  2.396   5.898  1.00 40.31 ?  134 HOH B O     1 
HETATM 5227 O O     . HOH H 4 .   ? -4.195  3.888   -0.823 1.00 38.26 ?  135 HOH B O     1 
HETATM 5228 O O     . HOH H 4 .   ? -8.964  19.923  -3.011 1.00 45.45 ?  136 HOH B O     1 
HETATM 5229 O O     . HOH H 4 .   ? -6.504  20.013  -6.364 1.00 39.58 ?  137 HOH B O     1 
HETATM 5230 O O     . HOH H 4 .   ? -6.593  5.466   -2.074 1.00 48.46 ?  138 HOH B O     1 
HETATM 5231 O O     . HOH H 4 .   ? -1.601  3.308   -0.471 1.00 31.37 ?  139 HOH B O     1 
HETATM 5232 O O     . HOH H 4 .   ? -7.814  2.478   2.893  1.00 38.74 ?  140 HOH B O     1 
HETATM 5233 O O     . HOH H 4 .   ? 8.140   19.899  -2.549 1.00 37.77 ?  141 HOH B O     1 
HETATM 5234 O O     . HOH H 4 .   ? -6.334  3.860   -0.067 1.00 42.15 ?  142 HOH B O     1 
HETATM 5235 O O     . HOH I 4 .   ? -11.512 18.388  32.729 1.00 31.29 ?  401 HOH C O     1 
HETATM 5236 O O     . HOH I 4 .   ? -9.297  1.132   44.940 1.00 32.40 ?  402 HOH C O     1 
HETATM 5237 O O     . HOH I 4 .   ? 19.572  -17.073 54.358 1.00 35.84 ?  403 HOH C O     1 
HETATM 5238 O O     . HOH I 4 .   ? 34.727  -10.223 35.051 1.00 44.76 ?  404 HOH C O     1 
HETATM 5239 O O     . HOH I 4 .   ? 3.368   -1.001  50.734 1.00 32.24 ?  405 HOH C O     1 
HETATM 5240 O O     . HOH I 4 .   ? -2.511  -4.949  52.645 1.00 36.12 ?  406 HOH C O     1 
HETATM 5241 O O     . HOH I 4 .   ? 20.007  -27.255 30.291 1.00 38.22 ?  407 HOH C O     1 
HETATM 5242 O O     . HOH I 4 .   ? -14.331 1.131   37.242 1.00 37.28 ?  408 HOH C O     1 
HETATM 5243 O O     . HOH I 4 .   ? 11.764  -6.567  28.527 1.00 27.02 ?  409 HOH C O     1 
HETATM 5244 O O     . HOH I 4 .   ? 27.958  -26.796 12.369 1.00 49.64 ?  410 HOH C O     1 
HETATM 5245 O O     . HOH I 4 .   ? 19.213  -27.380 38.935 1.00 31.58 ?  411 HOH C O     1 
HETATM 5246 O O     . HOH I 4 .   ? 29.815  -15.868 48.083 1.00 43.28 ?  412 HOH C O     1 
HETATM 5247 O O     . HOH I 4 .   ? 14.521  12.366  33.506 1.00 20.66 ?  413 HOH C O     1 
HETATM 5248 O O     . HOH I 4 .   ? 1.241   6.793   23.357 1.00 33.51 ?  414 HOH C O     1 
HETATM 5249 O O     . HOH I 4 .   ? 29.373  -3.109  22.341 1.00 25.77 ?  415 HOH C O     1 
HETATM 5250 O O     . HOH I 4 .   ? -0.460  18.362  45.222 1.00 23.53 ?  416 HOH C O     1 
HETATM 5251 O O     . HOH I 4 .   ? 12.948  -20.795 25.899 1.00 32.23 ?  417 HOH C O     1 
HETATM 5252 O O     . HOH I 4 .   ? 6.721   8.729   24.678 1.00 23.26 ?  418 HOH C O     1 
HETATM 5253 O O     . HOH I 4 .   ? -4.786  -2.966  32.807 1.00 33.46 ?  419 HOH C O     1 
HETATM 5254 O O     . HOH I 4 .   ? 11.803  -23.975 33.690 1.00 32.97 ?  420 HOH C O     1 
HETATM 5255 O O     . HOH I 4 .   ? 29.040  -5.446  28.293 1.00 33.80 ?  421 HOH C O     1 
HETATM 5256 O O     . HOH I 4 .   ? 29.357  9.561   41.741 1.00 26.67 ?  422 HOH C O     1 
HETATM 5257 O O     . HOH I 4 .   ? 3.348   23.582  35.273 1.00 26.42 ?  423 HOH C O     1 
HETATM 5258 O O     . HOH I 4 .   ? 32.042  -18.632 43.428 1.00 39.95 ?  424 HOH C O     1 
HETATM 5259 O O     . HOH I 4 .   ? 24.020  -4.957  17.014 1.00 27.60 ?  425 HOH C O     1 
HETATM 5260 O O     . HOH I 4 .   ? 6.984   13.752  48.283 1.00 31.55 ?  426 HOH C O     1 
HETATM 5261 O O     . HOH I 4 .   ? 9.014   8.006   44.955 1.00 30.40 ?  427 HOH C O     1 
HETATM 5262 O O     . HOH I 4 .   ? 20.739  13.334  35.079 1.00 17.25 ?  428 HOH C O     1 
HETATM 5263 O O     . HOH I 4 .   ? 6.914   8.886   28.383 1.00 16.57 ?  429 HOH C O     1 
HETATM 5264 O O     . HOH I 4 .   ? 4.336   9.759   21.489 1.00 34.61 ?  430 HOH C O     1 
HETATM 5265 O O     . HOH I 4 .   ? 7.218   10.391  43.749 1.00 10.58 ?  431 HOH C O     1 
HETATM 5266 O O     . HOH I 4 .   ? 4.827   -5.347  61.519 1.00 34.93 ?  432 HOH C O     1 
HETATM 5267 O O     . HOH I 4 .   ? 25.294  -12.083 21.936 1.00 27.36 ?  433 HOH C O     1 
HETATM 5268 O O     . HOH I 4 .   ? 23.168  -24.093 28.770 1.00 30.00 ?  434 HOH C O     1 
HETATM 5269 O O     . HOH I 4 .   ? 22.380  -11.590 48.056 1.00 32.77 ?  435 HOH C O     1 
HETATM 5270 O O     . HOH I 4 .   ? 9.775   -24.969 34.936 1.00 35.63 ?  436 HOH C O     1 
HETATM 5271 O O     . HOH I 4 .   ? 11.949  21.441  36.934 1.00 21.99 ?  437 HOH C O     1 
HETATM 5272 O O     . HOH I 4 .   ? -17.511 0.198   30.209 1.00 43.55 ?  438 HOH C O     1 
HETATM 5273 O O     . HOH I 4 .   ? 27.772  1.542   24.995 1.00 22.11 ?  439 HOH C O     1 
HETATM 5274 O O     . HOH I 4 .   ? 17.033  10.857  39.989 1.00 26.49 ?  440 HOH C O     1 
HETATM 5275 O O     . HOH I 4 .   ? 25.744  3.331   40.849 1.00 31.52 ?  441 HOH C O     1 
HETATM 5276 O O     . HOH I 4 .   ? 8.679   19.896  26.458 1.00 26.90 ?  442 HOH C O     1 
HETATM 5277 O O     . HOH I 4 .   ? 23.571  -22.687 20.720 1.00 29.98 ?  443 HOH C O     1 
HETATM 5278 O O     . HOH I 4 .   ? -8.292  21.505  32.992 1.00 47.34 ?  444 HOH C O     1 
HETATM 5279 O O     . HOH I 4 .   ? -11.537 8.603   47.605 1.00 41.16 ?  445 HOH C O     1 
HETATM 5280 O O     . HOH I 4 .   ? -1.524  -2.970  56.973 1.00 38.53 ?  446 HOH C O     1 
HETATM 5281 O O     . HOH I 4 .   ? 3.695   -17.971 53.746 1.00 25.21 ?  447 HOH C O     1 
HETATM 5282 O O     . HOH I 4 .   ? 12.042  8.433   28.938 1.00 23.56 ?  448 HOH C O     1 
HETATM 5283 O O     . HOH I 4 .   ? 22.353  -25.914 19.236 1.00 35.98 ?  449 HOH C O     1 
HETATM 5284 O O     . HOH I 4 .   ? 28.777  -14.433 31.285 1.00 23.43 ?  450 HOH C O     1 
HETATM 5285 O O     . HOH I 4 .   ? -11.158 2.859   42.105 1.00 32.86 ?  451 HOH C O     1 
HETATM 5286 O O     . HOH I 4 .   ? 21.386  -16.098 29.209 1.00 19.04 ?  452 HOH C O     1 
HETATM 5287 O O     . HOH I 4 .   ? 21.511  -15.549 55.557 1.00 40.41 ?  453 HOH C O     1 
HETATM 5288 O O     . HOH I 4 .   ? 2.554   24.663  25.284 1.00 31.19 ?  454 HOH C O     1 
HETATM 5289 O O     . HOH I 4 .   ? 24.724  -16.567 22.094 1.00 18.78 ?  455 HOH C O     1 
HETATM 5290 O O     . HOH I 4 .   ? -6.086  -4.229  42.333 1.00 29.79 ?  456 HOH C O     1 
HETATM 5291 O O     . HOH I 4 .   ? 22.597  4.319   29.782 1.00 26.66 ?  457 HOH C O     1 
HETATM 5292 O O     . HOH I 4 .   ? -17.491 8.987   28.045 1.00 33.41 ?  458 HOH C O     1 
HETATM 5293 O O     . HOH I 4 .   ? 9.748   -5.563  56.602 1.00 42.20 ?  459 HOH C O     1 
HETATM 5294 O O     . HOH I 4 .   ? 2.138   13.906  48.029 1.00 20.16 ?  460 HOH C O     1 
HETATM 5295 O O     . HOH I 4 .   ? -10.154 20.015  34.513 1.00 27.95 ?  461 HOH C O     1 
HETATM 5296 O O     . HOH I 4 .   ? -2.033  4.299   25.488 1.00 23.72 ?  462 HOH C O     1 
HETATM 5297 O O     . HOH I 4 .   ? 25.126  -14.807 0.433  1.00 35.06 ?  463 HOH C O     1 
HETATM 5298 O O     . HOH I 4 .   ? -10.827 -0.729  29.691 1.00 25.05 ?  464 HOH C O     1 
HETATM 5299 O O     . HOH I 4 .   ? 23.885  -0.642  44.863 1.00 30.65 ?  465 HOH C O     1 
HETATM 5300 O O     . HOH I 4 .   ? 12.201  1.999   27.168 1.00 12.41 ?  466 HOH C O     1 
HETATM 5301 O O     . HOH I 4 .   ? 14.925  -26.535 14.014 1.00 30.64 ?  467 HOH C O     1 
HETATM 5302 O O     . HOH I 4 .   ? -7.039  11.527  44.249 1.00 22.92 ?  468 HOH C O     1 
HETATM 5303 O O     . HOH I 4 .   ? -12.131 11.851  28.660 1.00 20.08 ?  469 HOH C O     1 
HETATM 5304 O O     . HOH I 4 .   ? -3.811  -4.030  42.929 1.00 26.71 ?  470 HOH C O     1 
HETATM 5305 O O     . HOH I 4 .   ? 24.573  -26.102 34.050 1.00 35.95 ?  471 HOH C O     1 
HETATM 5306 O O     . HOH I 4 .   ? 15.422  9.918   38.129 1.00 22.47 ?  472 HOH C O     1 
HETATM 5307 O O     . HOH I 4 .   ? 4.107   21.637  45.557 1.00 38.65 ?  473 HOH C O     1 
HETATM 5308 O O     . HOH I 4 .   ? 16.304  11.333  47.880 1.00 39.34 ?  474 HOH C O     1 
HETATM 5309 O O     . HOH I 4 .   ? -14.253 13.825  34.516 1.00 29.60 ?  475 HOH C O     1 
HETATM 5310 O O     . HOH I 4 .   ? 11.240  -21.520 35.453 1.00 25.91 ?  476 HOH C O     1 
HETATM 5311 O O     . HOH I 4 .   ? 15.807  -5.694  42.517 1.00 17.72 ?  477 HOH C O     1 
HETATM 5312 O O     . HOH I 4 .   ? 23.346  2.391   41.991 1.00 29.63 ?  478 HOH C O     1 
HETATM 5313 O O     . HOH I 4 .   ? -16.656 6.791   36.965 1.00 25.52 ?  479 HOH C O     1 
HETATM 5314 O O     . HOH I 4 .   ? -8.407  16.972  29.963 1.00 37.17 ?  480 HOH C O     1 
HETATM 5315 O O     . HOH I 4 .   ? 25.865  -20.840 45.256 1.00 31.38 ?  481 HOH C O     1 
HETATM 5316 O O     . HOH I 4 .   ? -7.821  13.295  25.786 1.00 31.42 ?  482 HOH C O     1 
HETATM 5317 O O     . HOH I 4 .   ? 11.326  -11.149 42.001 1.00 19.50 ?  483 HOH C O     1 
HETATM 5318 O O     . HOH I 4 .   ? 27.615  -7.368  46.075 1.00 29.14 ?  484 HOH C O     1 
HETATM 5319 O O     . HOH I 4 .   ? 30.069  -1.352  39.086 1.00 27.27 ?  485 HOH C O     1 
HETATM 5320 O O     . HOH I 4 .   ? -3.045  23.261  30.469 1.00 29.85 ?  486 HOH C O     1 
HETATM 5321 O O     . HOH I 4 .   ? 28.059  -25.702 37.510 1.00 34.86 ?  487 HOH C O     1 
HETATM 5322 O O     . HOH I 4 .   ? 29.825  -12.212 30.741 1.00 30.80 ?  488 HOH C O     1 
HETATM 5323 O O     . HOH I 4 .   ? 7.784   20.770  28.885 1.00 32.41 ?  489 HOH C O     1 
HETATM 5324 O O     . HOH I 4 .   ? -0.483  23.120  38.181 1.00 40.28 ?  490 HOH C O     1 
HETATM 5325 O O     . HOH I 4 .   ? 28.338  -14.660 27.129 1.00 39.30 ?  491 HOH C O     1 
HETATM 5326 O O     . HOH I 4 .   ? 4.373   -21.991 32.689 1.00 31.69 ?  492 HOH C O     1 
HETATM 5327 O O     . HOH I 4 .   ? 27.592  -10.002 26.922 1.00 28.45 ?  493 HOH C O     1 
HETATM 5328 O O     . HOH I 4 .   ? 4.387   10.263  49.722 1.00 34.55 ?  494 HOH C O     1 
HETATM 5329 O O     . HOH I 4 .   ? 29.270  7.165   40.982 1.00 23.21 ?  495 HOH C O     1 
HETATM 5330 O O     . HOH I 4 .   ? 8.110   2.672   37.015 1.00 21.09 ?  496 HOH C O     1 
HETATM 5331 O O     . HOH I 4 .   ? 28.859  -12.124 46.364 1.00 33.79 ?  497 HOH C O     1 
HETATM 5332 O O     . HOH I 4 .   ? 24.242  -26.781 14.608 1.00 36.29 ?  498 HOH C O     1 
HETATM 5333 O O     . HOH I 4 .   ? 11.167  -5.217  54.488 1.00 33.53 ?  499 HOH C O     1 
HETATM 5334 O O     . HOH I 4 .   ? 11.488  -0.572  27.434 1.00 20.59 ?  500 HOH C O     1 
HETATM 5335 O O     . HOH I 4 .   ? 24.236  -28.469 19.350 1.00 38.29 ?  501 HOH C O     1 
HETATM 5336 O O     . HOH I 4 .   ? 29.298  -20.322 31.055 1.00 31.58 ?  502 HOH C O     1 
HETATM 5337 O O     . HOH I 4 .   ? 16.243  -24.827 43.300 1.00 29.04 ?  503 HOH C O     1 
HETATM 5338 O O     . HOH I 4 .   ? 26.509  -24.692 14.557 1.00 39.40 ?  504 HOH C O     1 
HETATM 5339 O O     . HOH I 4 .   ? 21.352  -9.993  22.450 1.00 27.49 ?  505 HOH C O     1 
HETATM 5340 O O     . HOH I 4 .   ? -14.506 13.613  30.779 1.00 30.82 ?  506 HOH C O     1 
HETATM 5341 O O     . HOH I 4 .   ? 13.764  13.426  36.816 1.00 26.63 ?  507 HOH C O     1 
HETATM 5342 O O     . HOH I 4 .   ? 18.120  -11.872 17.692 1.00 18.09 ?  508 HOH C O     1 
HETATM 5343 O O     . HOH I 4 .   ? 25.036  -19.582 49.158 1.00 33.15 ?  509 HOH C O     1 
HETATM 5344 O O     . HOH I 4 .   ? -4.597  14.086  30.914 1.00 15.30 ?  510 HOH C O     1 
HETATM 5345 O O     . HOH I 4 .   ? 4.992   22.943  26.972 1.00 38.98 ?  511 HOH C O     1 
HETATM 5346 O O     . HOH I 4 .   ? 9.601   9.911   28.549 1.00 16.31 ?  512 HOH C O     1 
HETATM 5347 O O     . HOH I 4 .   ? 25.563  -6.732  21.259 1.00 25.76 ?  513 HOH C O     1 
HETATM 5348 O O     . HOH I 4 .   ? 14.634  -30.137 8.004  1.00 34.40 ?  514 HOH C O     1 
HETATM 5349 O O     . HOH I 4 .   ? 21.143  6.774   31.174 1.00 21.55 ?  515 HOH C O     1 
HETATM 5350 O O     . HOH I 4 .   ? -4.204  -0.636  29.951 1.00 24.88 ?  516 HOH C O     1 
HETATM 5351 O O     . HOH I 4 .   ? 21.066  4.338   40.817 1.00 14.50 ?  517 HOH C O     1 
HETATM 5352 O O     . HOH I 4 .   ? -11.397 6.247   26.139 1.00 32.91 ?  518 HOH C O     1 
HETATM 5353 O O     . HOH I 4 .   ? 9.126   -14.184 52.647 1.00 38.68 ?  519 HOH C O     1 
HETATM 5354 O O     . HOH I 4 .   ? 21.677  -7.741  49.756 1.00 29.69 ?  520 HOH C O     1 
HETATM 5355 O O     . HOH I 4 .   ? 25.561  11.445  33.566 1.00 38.52 ?  521 HOH C O     1 
HETATM 5356 O O     . HOH I 4 .   ? 5.730   15.440  45.996 1.00 33.06 ?  522 HOH C O     1 
HETATM 5357 O O     . HOH I 4 .   ? -13.451 11.934  42.727 1.00 28.95 ?  523 HOH C O     1 
HETATM 5358 O O     . HOH I 4 .   ? 28.620  -8.947  29.829 1.00 36.29 ?  524 HOH C O     1 
HETATM 5359 O O     . HOH I 4 .   ? 25.818  8.741   34.362 1.00 33.52 ?  525 HOH C O     1 
HETATM 5360 O O     . HOH I 4 .   ? 26.545  4.866   28.614 1.00 22.89 ?  526 HOH C O     1 
HETATM 5361 O O     . HOH I 4 .   ? 32.846  -15.937 36.795 1.00 34.03 ?  527 HOH C O     1 
HETATM 5362 O O     . HOH I 4 .   ? 26.023  -28.291 40.451 1.00 38.79 ?  528 HOH C O     1 
HETATM 5363 O O     . HOH I 4 .   ? 13.717  10.640  36.128 1.00 25.12 ?  529 HOH C O     1 
HETATM 5364 O O     . HOH I 4 .   ? -8.975  6.710   25.540 1.00 26.11 ?  530 HOH C O     1 
HETATM 5365 O O     . HOH I 4 .   ? 24.321  -17.886 -1.130 1.00 37.16 ?  531 HOH C O     1 
HETATM 5366 O O     . HOH I 4 .   ? 17.913  -8.462  48.741 1.00 34.77 ?  532 HOH C O     1 
HETATM 5367 O O     . HOH I 4 .   ? 20.289  6.220   33.432 1.00 29.43 ?  533 HOH C O     1 
HETATM 5368 O O     . HOH I 4 .   ? -1.761  1.243   54.995 1.00 43.27 ?  534 HOH C O     1 
HETATM 5369 O O     . HOH I 4 .   ? -7.077  6.032   47.245 1.00 22.90 ?  535 HOH C O     1 
HETATM 5370 O O     . HOH I 4 .   ? -10.592 -2.816  43.026 1.00 44.09 ?  536 HOH C O     1 
HETATM 5371 O O     . HOH I 4 .   ? 32.890  -5.959  38.445 1.00 28.72 ?  537 HOH C O     1 
HETATM 5372 O O     . HOH I 4 .   ? 30.725  2.261   36.114 1.00 29.78 ?  538 HOH C O     1 
HETATM 5373 O O     . HOH I 4 .   ? 22.888  -26.383 41.565 1.00 38.12 ?  539 HOH C O     1 
HETATM 5374 O O     . HOH I 4 .   ? 32.568  -13.709 37.361 1.00 29.52 ?  540 HOH C O     1 
HETATM 5375 O O     . HOH I 4 .   ? -9.319  21.165  37.216 1.00 37.42 ?  541 HOH C O     1 
HETATM 5376 O O     . HOH I 4 .   ? 6.796   -12.038 55.210 1.00 38.63 ?  542 HOH C O     1 
HETATM 5377 O O     . HOH I 4 .   ? 4.351   -11.120 56.427 1.00 30.35 ?  543 HOH C O     1 
HETATM 5378 O O     . HOH I 4 .   ? 17.012  0.902   45.389 1.00 30.39 ?  544 HOH C O     1 
HETATM 5379 O O     . HOH I 4 .   ? 10.818  -12.632 55.108 1.00 36.07 ?  545 HOH C O     1 
HETATM 5380 O O     . HOH I 4 .   ? 13.279  21.576  28.299 1.00 31.96 ?  546 HOH C O     1 
HETATM 5381 O O     . HOH I 4 .   ? 23.541  -14.637 54.752 1.00 41.05 ?  547 HOH C O     1 
HETATM 5382 O O     . HOH I 4 .   ? 12.331  19.554  49.929 1.00 31.79 ?  548 HOH C O     1 
HETATM 5383 O O     . HOH I 4 .   ? -11.367 17.353  30.706 1.00 28.76 ?  549 HOH C O     1 
HETATM 5384 O O     . HOH I 4 .   ? -13.065 -0.042  28.198 1.00 33.62 ?  550 HOH C O     1 
HETATM 5385 O O     . HOH I 4 .   ? -16.395 6.184   41.242 1.00 41.31 ?  551 HOH C O     1 
HETATM 5386 O O     . HOH I 4 .   ? 22.515  -26.892 5.561  1.00 39.16 ?  552 HOH C O     1 
HETATM 5387 O O     . HOH I 4 .   ? 19.570  11.737  30.589 1.00 15.19 ?  553 HOH C O     1 
HETATM 5388 O O     . HOH I 4 .   ? -8.605  -1.628  28.622 1.00 30.24 ?  554 HOH C O     1 
HETATM 5389 O O     . HOH I 4 .   ? 23.624  -8.746  51.670 1.00 27.38 ?  555 HOH C O     1 
HETATM 5390 O O     . HOH I 4 .   ? 17.813  -29.802 1.323  1.00 50.07 ?  556 HOH C O     1 
HETATM 5391 O O     . HOH I 4 .   ? -6.880  20.707  39.487 1.00 28.94 ?  557 HOH C O     1 
HETATM 5392 O O     . HOH I 4 .   ? 16.384  -26.693 41.059 1.00 39.18 ?  558 HOH C O     1 
HETATM 5393 O O     . HOH I 4 .   ? 19.080  -10.706 50.061 1.00 32.43 ?  559 HOH C O     1 
HETATM 5394 O O     . HOH I 4 .   ? 10.353  -26.343 1.709  1.00 38.46 ?  560 HOH C O     1 
HETATM 5395 O O     . HOH I 4 .   ? 11.046  23.883  35.781 1.00 37.45 ?  561 HOH C O     1 
HETATM 5396 O O     . HOH I 4 .   ? 31.562  -2.486  31.882 1.00 44.03 ?  562 HOH C O     1 
HETATM 5397 O O     . HOH I 4 .   ? -6.268  -0.192  27.978 1.00 29.50 ?  563 HOH C O     1 
HETATM 5398 O O     . HOH I 4 .   ? -6.744  19.983  26.904 1.00 39.20 ?  564 HOH C O     1 
HETATM 5399 O O     . HOH I 4 .   ? 22.981  -19.491 51.204 1.00 42.89 ?  565 HOH C O     1 
HETATM 5400 O O     . HOH I 4 .   ? -11.509 14.116  27.532 1.00 33.68 ?  566 HOH C O     1 
HETATM 5401 O O     . HOH I 4 .   ? -17.867 2.056   34.951 1.00 30.59 ?  567 HOH C O     1 
HETATM 5402 O O     . HOH I 4 .   ? 3.974   25.764  34.155 1.00 40.13 ?  568 HOH C O     1 
HETATM 5403 O O     . HOH I 4 .   ? 16.899  -25.971 48.539 1.00 43.70 ?  569 HOH C O     1 
HETATM 5404 O O     . HOH I 4 .   ? 3.004   9.077   56.304 1.00 42.25 ?  570 HOH C O     1 
HETATM 5405 O O     . HOH I 4 .   ? -2.194  0.893   29.366 1.00 15.84 ?  571 HOH C O     1 
HETATM 5406 O O     . HOH I 4 .   ? -1.328  7.501   22.664 1.00 44.26 ?  572 HOH C O     1 
HETATM 5407 O O     . HOH I 4 .   ? -6.466  8.365   47.368 1.00 28.81 ?  573 HOH C O     1 
HETATM 5408 O O     . HOH I 4 .   ? 27.031  0.366   43.944 1.00 43.75 ?  574 HOH C O     1 
HETATM 5409 O O     . HOH I 4 .   ? 11.750  19.492  27.143 1.00 29.44 ?  575 HOH C O     1 
HETATM 5410 O O     . HOH I 4 .   ? -1.193  10.680  20.920 1.00 32.87 ?  576 HOH C O     1 
HETATM 5411 O O     . HOH I 4 .   ? 30.833  9.062   35.971 1.00 32.86 ?  577 HOH C O     1 
HETATM 5412 O O     . HOH I 4 .   ? 25.355  -0.102  52.522 1.00 59.88 ?  578 HOH C O     1 
HETATM 5413 O O     . HOH I 4 .   ? 30.688  4.991   34.607 1.00 31.32 ?  579 HOH C O     1 
HETATM 5414 O O     . HOH I 4 .   ? 28.595  -12.532 26.336 1.00 40.01 ?  580 HOH C O     1 
HETATM 5415 O O     . HOH I 4 .   ? -4.320  17.429  46.011 1.00 40.94 ?  581 HOH C O     1 
HETATM 5416 O O     . HOH I 4 .   ? -18.835 10.189  33.019 1.00 36.68 ?  582 HOH C O     1 
HETATM 5417 O O     . HOH I 4 .   ? 11.228  21.787  25.796 1.00 41.17 ?  583 HOH C O     1 
HETATM 5418 O O     . HOH I 4 .   ? -10.972 -0.106  47.438 1.00 28.64 ?  584 HOH C O     1 
HETATM 5419 O O     . HOH I 4 .   ? -4.650  12.838  48.597 1.00 39.01 ?  585 HOH C O     1 
HETATM 5420 O O     . HOH I 4 .   ? 20.789  -22.095 52.249 1.00 47.59 ?  586 HOH C O     1 
HETATM 5421 O O     . HOH I 4 .   ? 30.514  2.955   33.296 1.00 42.82 ?  587 HOH C O     1 
HETATM 5422 O O     . HOH I 4 .   ? 27.159  -16.007 14.692 1.00 51.24 ?  588 HOH C O     1 
HETATM 5423 O O     . HOH I 4 .   ? 20.851  -25.726 -5.777 1.00 41.17 ?  589 HOH C O     1 
HETATM 5424 O O     . HOH I 4 .   ? -2.417  -9.426  55.539 1.00 43.70 ?  590 HOH C O     1 
HETATM 5425 O O     . HOH I 4 .   ? 29.476  -23.539 43.859 1.00 42.84 ?  591 HOH C O     1 
HETATM 5426 O O     . HOH I 4 .   ? 14.649  22.507  54.780 1.00 40.55 ?  592 HOH C O     1 
HETATM 5427 O O     . HOH I 4 .   ? -9.382  13.565  48.957 1.00 45.49 ?  593 HOH C O     1 
HETATM 5428 O O     . HOH I 4 .   ? 32.664  -16.934 18.741 1.00 54.31 ?  594 HOH C O     1 
HETATM 5429 O O     . HOH I 4 .   ? -7.702  14.939  47.586 1.00 53.72 ?  595 HOH C O     1 
HETATM 5430 O O     . HOH I 4 .   ? -13.380 -3.557  26.112 1.00 39.55 ?  596 HOH C O     1 
HETATM 5431 O O     . HOH I 4 .   ? 7.405   23.025  52.075 1.00 35.90 ?  597 HOH C O     1 
HETATM 5432 O O     . HOH J 4 .   ? 32.237  11.066  51.055 1.00 34.04 ?  101 HOH D O     1 
HETATM 5433 O O     . HOH J 4 .   ? 35.680  12.963  33.382 1.00 29.30 ?  102 HOH D O     1 
HETATM 5434 O O     . HOH J 4 .   ? 17.409  18.355  41.471 1.00 22.47 ?  103 HOH D O     1 
HETATM 5435 O O     . HOH J 4 .   ? 40.728  19.427  37.780 1.00 32.84 ?  104 HOH D O     1 
HETATM 5436 O O     . HOH J 4 .   ? 20.724  13.415  32.082 1.00 13.77 ?  105 HOH D O     1 
HETATM 5437 O O     . HOH J 4 .   ? 40.068  17.803  45.683 1.00 35.10 ?  106 HOH D O     1 
HETATM 5438 O O     . HOH J 4 .   ? 34.110  4.825   46.386 1.00 33.89 ?  107 HOH D O     1 
HETATM 5439 O O     . HOH J 4 .   ? 26.008  23.116  47.260 1.00 29.45 ?  108 HOH D O     1 
HETATM 5440 O O     . HOH J 4 .   ? 34.800  23.311  46.988 1.00 34.72 ?  109 HOH D O     1 
HETATM 5441 O O     . HOH J 4 .   ? 35.304  21.772  32.050 1.00 30.17 ?  110 HOH D O     1 
HETATM 5442 O O     . HOH J 4 .   ? 15.269  20.691  40.237 1.00 23.08 ?  111 HOH D O     1 
HETATM 5443 O O     . HOH J 4 .   ? 21.339  27.571  42.895 1.00 45.39 ?  112 HOH D O     1 
HETATM 5444 O O     . HOH J 4 .   ? 25.867  25.116  44.881 1.00 34.79 ?  113 HOH D O     1 
HETATM 5445 O O     . HOH J 4 .   ? 26.023  5.446   46.760 1.00 44.08 ?  114 HOH D O     1 
HETATM 5446 O O     . HOH J 4 .   ? 18.543  23.946  38.092 1.00 27.62 ?  115 HOH D O     1 
HETATM 5447 O O     . HOH J 4 .   ? 33.823  16.167  27.703 1.00 28.85 ?  116 HOH D O     1 
HETATM 5448 O O     . HOH J 4 .   ? 19.917  21.345  47.100 1.00 27.85 ?  117 HOH D O     1 
HETATM 5449 O O     . HOH J 4 .   ? 37.574  9.530   43.410 1.00 29.83 ?  118 HOH D O     1 
HETATM 5450 O O     . HOH J 4 .   ? 39.083  20.318  49.882 1.00 55.21 ?  119 HOH D O     1 
HETATM 5451 O O     . HOH J 4 .   ? 27.450  5.756   43.151 1.00 37.90 ?  120 HOH D O     1 
HETATM 5452 O O     . HOH J 4 .   ? 35.247  21.258  27.329 1.00 32.90 ?  121 HOH D O     1 
HETATM 5453 O O     . HOH J 4 .   ? 13.900  21.198  34.454 1.00 27.30 ?  122 HOH D O     1 
HETATM 5454 O O     . HOH J 4 .   ? 17.930  21.075  27.816 1.00 21.76 ?  123 HOH D O     1 
HETATM 5455 O O     . HOH J 4 .   ? 31.253  13.332  52.215 1.00 39.17 ?  124 HOH D O     1 
HETATM 5456 O O     . HOH J 4 .   ? 27.592  18.879  23.885 1.00 29.57 ?  125 HOH D O     1 
HETATM 5457 O O     . HOH J 4 .   ? 32.694  17.470  23.886 1.00 40.56 ?  126 HOH D O     1 
HETATM 5458 O O     . HOH J 4 .   ? 30.491  4.376   47.720 1.00 29.48 ?  127 HOH D O     1 
HETATM 5459 O O     . HOH J 4 .   ? 42.059  15.803  43.625 1.00 38.19 ?  128 HOH D O     1 
HETATM 5460 O O     . HOH J 4 .   ? 33.158  20.738  53.415 1.00 36.08 ?  129 HOH D O     1 
HETATM 5461 O O     . HOH J 4 .   ? 15.519  21.533  28.929 1.00 34.83 ?  130 HOH D O     1 
HETATM 5462 O O     . HOH J 4 .   ? 35.482  25.727  46.145 1.00 35.24 ?  131 HOH D O     1 
HETATM 5463 O O     . HOH J 4 .   ? 26.356  26.719  33.387 1.00 45.26 ?  132 HOH D O     1 
HETATM 5464 O O     . HOH J 4 .   ? 37.887  12.442  46.597 1.00 41.01 ?  133 HOH D O     1 
HETATM 5465 O O     . HOH J 4 .   ? 29.268  26.319  33.628 1.00 36.17 ?  134 HOH D O     1 
HETATM 5466 O O     . HOH J 4 .   ? 24.308  20.604  55.175 1.00 39.23 ?  135 HOH D O     1 
HETATM 5467 O O     . HOH J 4 .   ? 25.820  21.532  53.827 1.00 34.07 ?  136 HOH D O     1 
HETATM 5468 O O     . HOH J 4 .   ? 15.801  20.068  53.913 1.00 38.36 ?  137 HOH D O     1 
HETATM 5469 O O     . HOH J 4 .   ? 36.835  23.735  27.927 1.00 25.73 ?  138 HOH D O     1 
HETATM 5470 O O     . HOH J 4 .   ? 18.359  21.719  54.315 1.00 57.43 ?  139 HOH D O     1 
HETATM 5471 O O     . HOH J 4 .   ? 24.571  23.430  53.455 1.00 27.53 ?  140 HOH D O     1 
HETATM 5472 O O     . HOH J 4 .   ? 40.084  15.330  48.517 1.00 28.09 ?  141 HOH D O     1 
# 
