data_9JN6
# 
_entry.id   9JN6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9JN6         pdb_00009jn6 10.2210/pdb9jn6/pdb 
WWPDB D_1300051708 ?            ?                   
# 
_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                        9JN6 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yunyunyang0219@163.com 
_pdbx_contact_author.name_first         Yunyun 
_pdbx_contact_author.name_last          Yang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6042-3617 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, Y.L.'     1 ? 
'Yang, Y.Y.'   2 ? 
'Huang, J.-W.' 3 ? 
'Chen, C.-C.'  4 ? 
'Guo, R.-T.'   5 ? 
# 
_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            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                1265 
_citation.page_last                 1273 
_citation.title                     
'Structural Insights into the N-N Bond-Formation Mechanism of the Heme-Dependent Piperazate Synthase KtzT' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c06124 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yang, Y.'    1 ? 
primary 'Li, Y.'      2 ? 
primary 'Yao, L.'     3 ? 
primary 'Dai, K.'     4 ? 
primary 'Fu, X.'      5 ? 
primary 'Ge, A.'      6 ? 
primary 'Huang, J.W.' 7 ? 
primary 'Guo, R.T.'   8 ? 
primary 'Chen, C.C.'  9 ? 
# 
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 'FMN-binding protein'                     23249.340 4   ? C197A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'         616.487   4   ? ?     ? ? 
3 non-polymer syn '(3~{S})-1,2-diazinane-3-carboxylic acid' 130.145   3   ? ?     ? ? 
4 water       nat water                                     18.015    851 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Regulator 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AGAGAMFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAA
LGGAANVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYF
RRILPGVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGAEATRAVAGLMDRLPTE
;
_entity_poly.pdbx_strand_id                 B,C,D,A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'         HEM   
3 '(3~{S})-1,2-diazinane-3-carboxylic acid' A1ECN 
4 water                                     HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLY n 
1 3   ALA n 
1 4   GLY n 
1 5   ALA n 
1 6   MET n 
1 7   PHE n 
1 8   VAL n 
1 9   PRO n 
1 10  GLY n 
1 11  PRO n 
1 12  TYR n 
1 13  HIS n 
1 14  ALA n 
1 15  PRO n 
1 16  GLU n 
1 17  ASP n 
1 18  ARG n 
1 19  TRP n 
1 20  LEU n 
1 21  VAL n 
1 22  ASP n 
1 23  LEU n 
1 24  VAL n 
1 25  ARG n 
1 26  GLY n 
1 27  HIS n 
1 28  PRO n 
1 29  LEU n 
1 30  ALA n 
1 31  GLN n 
1 32  LEU n 
1 33  ALA n 
1 34  SER n 
1 35  ASN n 
1 36  GLY n 
1 37  ALA n 
1 38  GLY n 
1 39  GLY n 
1 40  ALA n 
1 41  ALA n 
1 42  PRO n 
1 43  HIS n 
1 44  ILE n 
1 45  THR n 
1 46  HIS n 
1 47  VAL n 
1 48  PRO n 
1 49  ILE n 
1 50  ILE n 
1 51  VAL n 
1 52  ASP n 
1 53  PRO n 
1 54  GLU n 
1 55  LEU n 
1 56  ASP n 
1 57  GLY n 
1 58  PRO n 
1 59  VAL n 
1 60  ASP n 
1 61  ARG n 
1 62  LEU n 
1 63  VAL n 
1 64  GLY n 
1 65  ILE n 
1 66  THR n 
1 67  LEU n 
1 68  TRP n 
1 69  GLY n 
1 70  HIS n 
1 71  MET n 
1 72  ASN n 
1 73  ARG n 
1 74  ALA n 
1 75  ASN n 
1 76  PRO n 
1 77  HIS n 
1 78  TRP n 
1 79  ALA n 
1 80  ALA n 
1 81  LEU n 
1 82  GLY n 
1 83  GLY n 
1 84  ALA n 
1 85  ALA n 
1 86  ASN n 
1 87  VAL n 
1 88  VAL n 
1 89  ALA n 
1 90  THR n 
1 91  PHE n 
1 92  ALA n 
1 93  GLY n 
1 94  PRO n 
1 95  ASN n 
1 96  ALA n 
1 97  TYR n 
1 98  VAL n 
1 99  SER n 
1 100 PRO n 
1 101 ALA n 
1 102 VAL n 
1 103 TYR n 
1 104 ARG n 
1 105 THR n 
1 106 ALA n 
1 107 PRO n 
1 108 ALA n 
1 109 ALA n 
1 110 PRO n 
1 111 THR n 
1 112 TRP n 
1 113 ASN n 
1 114 PHE n 
1 115 THR n 
1 116 SER n 
1 117 VAL n 
1 118 GLN n 
1 119 VAL n 
1 120 ARG n 
1 121 GLY n 
1 122 GLU n 
1 123 LEU n 
1 124 ARG n 
1 125 LYS n 
1 126 VAL n 
1 127 GLU n 
1 128 SER n 
1 129 ALA n 
1 130 ASP n 
1 131 ASP n 
1 132 THR n 
1 133 LEU n 
1 134 ALA n 
1 135 THR n 
1 136 VAL n 
1 137 ARG n 
1 138 ALA n 
1 139 THR n 
1 140 VAL n 
1 141 ALA n 
1 142 ALA n 
1 143 LEU n 
1 144 GLU n 
1 145 SER n 
1 146 ARG n 
1 147 PHE n 
1 148 GLY n 
1 149 ALA n 
1 150 GLY n 
1 151 TRP n 
1 152 ASP n 
1 153 MET n 
1 154 THR n 
1 155 GLY n 
1 156 SER n 
1 157 LEU n 
1 158 ASP n 
1 159 TYR n 
1 160 PHE n 
1 161 ARG n 
1 162 ARG n 
1 163 ILE n 
1 164 LEU n 
1 165 PRO n 
1 166 GLY n 
1 167 VAL n 
1 168 GLY n 
1 169 ALA n 
1 170 PHE n 
1 171 ARG n 
1 172 LEU n 
1 173 ARG n 
1 174 VAL n 
1 175 ALA n 
1 176 GLU n 
1 177 ALA n 
1 178 ASP n 
1 179 GLY n 
1 180 MET n 
1 181 PHE n 
1 182 LYS n 
1 183 LEU n 
1 184 SER n 
1 185 GLN n 
1 186 GLU n 
1 187 GLN n 
1 188 GLN n 
1 189 PRO n 
1 190 ALA n 
1 191 ILE n 
1 192 ARG n 
1 193 ARG n 
1 194 ARG n 
1 195 VAL n 
1 196 ARG n 
1 197 HIS n 
1 198 SER n 
1 199 PHE n 
1 200 GLY n 
1 201 GLY n 
1 202 ALA n 
1 203 GLU n 
1 204 ALA n 
1 205 THR n 
1 206 ARG n 
1 207 ALA n 
1 208 VAL n 
1 209 ALA n 
1 210 GLY n 
1 211 LEU n 
1 212 MET n 
1 213 ASP n 
1 214 ARG n 
1 215 LEU n 
1 216 PRO n 
1 217 THR n 
1 218 GLU n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   218 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 KUTG_08928 
_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      'Kutzneria sp. 744' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     345341 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ECN peptide-like        . '(3~{S})-1,2-diazinane-3-carboxylic acid' 
'(S)-Hexahydropyridazine-3-carboxylic acid; S-Piperazic acid; (3S)-piperazate; (3S)-Pyridazin-3-carboxylate' 'C5 H10 N2 O2'     
130.145 
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  
HEM   non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'         HEME 'C34 H32 Fe N4 O4' 616.487 
HIS   'L-peptide linking' y HISTIDINE                                 ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                     ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                   ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                    ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                             ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                   ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                    ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                 ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                  ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                    ? 'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   -4  ?   ?   ?   B . n 
A 1 2   GLY 2   -3  ?   ?   ?   B . n 
A 1 3   ALA 3   -2  ?   ?   ?   B . n 
A 1 4   GLY 4   -1  -1  GLY GLY B . n 
A 1 5   ALA 5   0   0   ALA ALA B . n 
A 1 6   MET 6   1   1   MET MET B . n 
A 1 7   PHE 7   2   2   PHE PHE B . n 
A 1 8   VAL 8   3   3   VAL VAL B . n 
A 1 9   PRO 9   4   4   PRO PRO B . n 
A 1 10  GLY 10  5   5   GLY GLY B . n 
A 1 11  PRO 11  6   6   PRO PRO B . n 
A 1 12  TYR 12  7   7   TYR TYR B . n 
A 1 13  HIS 13  8   8   HIS HIS B . n 
A 1 14  ALA 14  9   9   ALA ALA B . n 
A 1 15  PRO 15  10  10  PRO PRO B . n 
A 1 16  GLU 16  11  11  GLU GLU B . n 
A 1 17  ASP 17  12  12  ASP ASP B . n 
A 1 18  ARG 18  13  13  ARG ARG B . n 
A 1 19  TRP 19  14  14  TRP TRP B . n 
A 1 20  LEU 20  15  15  LEU LEU B . n 
A 1 21  VAL 21  16  16  VAL VAL B . n 
A 1 22  ASP 22  17  17  ASP ASP B . n 
A 1 23  LEU 23  18  18  LEU LEU B . n 
A 1 24  VAL 24  19  19  VAL VAL B . n 
A 1 25  ARG 25  20  20  ARG ARG B . n 
A 1 26  GLY 26  21  21  GLY GLY B . n 
A 1 27  HIS 27  22  22  HIS HIS B . n 
A 1 28  PRO 28  23  23  PRO PRO B . n 
A 1 29  LEU 29  24  24  LEU LEU B . n 
A 1 30  ALA 30  25  25  ALA ALA B . n 
A 1 31  GLN 31  26  26  GLN GLN B . n 
A 1 32  LEU 32  27  27  LEU LEU B . n 
A 1 33  ALA 33  28  28  ALA ALA B . n 
A 1 34  SER 34  29  29  SER SER B . n 
A 1 35  ASN 35  30  30  ASN ASN B . n 
A 1 36  GLY 36  31  31  GLY GLY B . n 
A 1 37  ALA 37  32  32  ALA ALA B . n 
A 1 38  GLY 38  33  33  GLY GLY B . n 
A 1 39  GLY 39  34  34  GLY GLY B . n 
A 1 40  ALA 40  35  35  ALA ALA B . n 
A 1 41  ALA 41  36  36  ALA ALA B . n 
A 1 42  PRO 42  37  37  PRO PRO B . n 
A 1 43  HIS 43  38  38  HIS HIS B . n 
A 1 44  ILE 44  39  39  ILE ILE B . n 
A 1 45  THR 45  40  40  THR THR B . n 
A 1 46  HIS 46  41  41  HIS HIS B . n 
A 1 47  VAL 47  42  42  VAL VAL B . n 
A 1 48  PRO 48  43  43  PRO PRO B . n 
A 1 49  ILE 49  44  44  ILE ILE B . n 
A 1 50  ILE 50  45  45  ILE ILE B . n 
A 1 51  VAL 51  46  46  VAL VAL B . n 
A 1 52  ASP 52  47  47  ASP ASP B . n 
A 1 53  PRO 53  48  48  PRO PRO B . n 
A 1 54  GLU 54  49  49  GLU GLU B . n 
A 1 55  LEU 55  50  50  LEU LEU B . n 
A 1 56  ASP 56  51  51  ASP ASP B . n 
A 1 57  GLY 57  52  52  GLY GLY B . n 
A 1 58  PRO 58  53  53  PRO PRO B . n 
A 1 59  VAL 59  54  54  VAL VAL B . n 
A 1 60  ASP 60  55  55  ASP ASP B . n 
A 1 61  ARG 61  56  56  ARG ARG B . n 
A 1 62  LEU 62  57  57  LEU LEU B . n 
A 1 63  VAL 63  58  58  VAL VAL B . n 
A 1 64  GLY 64  59  59  GLY GLY B . n 
A 1 65  ILE 65  60  60  ILE ILE B . n 
A 1 66  THR 66  61  61  THR THR B . n 
A 1 67  LEU 67  62  62  LEU LEU B . n 
A 1 68  TRP 68  63  63  TRP TRP B . n 
A 1 69  GLY 69  64  64  GLY GLY B . n 
A 1 70  HIS 70  65  65  HIS HIS B . n 
A 1 71  MET 71  66  66  MET MET B . n 
A 1 72  ASN 72  67  67  ASN ASN B . n 
A 1 73  ARG 73  68  68  ARG ARG B . n 
A 1 74  ALA 74  69  69  ALA ALA B . n 
A 1 75  ASN 75  70  70  ASN ASN B . n 
A 1 76  PRO 76  71  71  PRO PRO B . n 
A 1 77  HIS 77  72  72  HIS HIS B . n 
A 1 78  TRP 78  73  73  TRP TRP B . n 
A 1 79  ALA 79  74  74  ALA ALA B . n 
A 1 80  ALA 80  75  75  ALA ALA B . n 
A 1 81  LEU 81  76  76  LEU LEU B . n 
A 1 82  GLY 82  77  77  GLY GLY B . n 
A 1 83  GLY 83  78  78  GLY GLY B . n 
A 1 84  ALA 84  79  79  ALA ALA B . n 
A 1 85  ALA 85  80  80  ALA ALA B . n 
A 1 86  ASN 86  81  81  ASN ASN B . n 
A 1 87  VAL 87  82  82  VAL VAL B . n 
A 1 88  VAL 88  83  83  VAL VAL B . n 
A 1 89  ALA 89  84  84  ALA ALA B . n 
A 1 90  THR 90  85  85  THR THR B . n 
A 1 91  PHE 91  86  86  PHE PHE B . n 
A 1 92  ALA 92  87  87  ALA ALA B . n 
A 1 93  GLY 93  88  88  GLY GLY B . n 
A 1 94  PRO 94  89  89  PRO PRO B . n 
A 1 95  ASN 95  90  90  ASN ASN B . n 
A 1 96  ALA 96  91  91  ALA ALA B . n 
A 1 97  TYR 97  92  92  TYR TYR B . n 
A 1 98  VAL 98  93  93  VAL VAL B . n 
A 1 99  SER 99  94  94  SER SER B . n 
A 1 100 PRO 100 95  95  PRO PRO B . n 
A 1 101 ALA 101 96  96  ALA ALA B . n 
A 1 102 VAL 102 97  97  VAL VAL B . n 
A 1 103 TYR 103 98  98  TYR TYR B . n 
A 1 104 ARG 104 99  99  ARG ARG B . n 
A 1 105 THR 105 100 100 THR THR B . n 
A 1 106 ALA 106 101 101 ALA ALA B . n 
A 1 107 PRO 107 102 102 PRO PRO B . n 
A 1 108 ALA 108 103 103 ALA ALA B . n 
A 1 109 ALA 109 104 104 ALA ALA B . n 
A 1 110 PRO 110 105 105 PRO PRO B . n 
A 1 111 THR 111 106 106 THR THR B . n 
A 1 112 TRP 112 107 107 TRP TRP B . n 
A 1 113 ASN 113 108 108 ASN ASN B . n 
A 1 114 PHE 114 109 109 PHE PHE B . n 
A 1 115 THR 115 110 110 THR THR B . n 
A 1 116 SER 116 111 111 SER SER B . n 
A 1 117 VAL 117 112 112 VAL VAL B . n 
A 1 118 GLN 118 113 113 GLN GLN B . n 
A 1 119 VAL 119 114 114 VAL VAL B . n 
A 1 120 ARG 120 115 115 ARG ARG B . n 
A 1 121 GLY 121 116 116 GLY GLY B . n 
A 1 122 GLU 122 117 117 GLU GLU B . n 
A 1 123 LEU 123 118 118 LEU LEU B . n 
A 1 124 ARG 124 119 119 ARG ARG B . n 
A 1 125 LYS 125 120 120 LYS LYS B . n 
A 1 126 VAL 126 121 121 VAL VAL B . n 
A 1 127 GLU 127 122 122 GLU GLU B . n 
A 1 128 SER 128 123 123 SER SER B . n 
A 1 129 ALA 129 124 124 ALA ALA B . n 
A 1 130 ASP 130 125 125 ASP ASP B . n 
A 1 131 ASP 131 126 126 ASP ASP B . n 
A 1 132 THR 132 127 127 THR THR B . n 
A 1 133 LEU 133 128 128 LEU LEU B . n 
A 1 134 ALA 134 129 129 ALA ALA B . n 
A 1 135 THR 135 130 130 THR THR B . n 
A 1 136 VAL 136 131 131 VAL VAL B . n 
A 1 137 ARG 137 132 132 ARG ARG B . n 
A 1 138 ALA 138 133 133 ALA ALA B . n 
A 1 139 THR 139 134 134 THR THR B . n 
A 1 140 VAL 140 135 135 VAL VAL B . n 
A 1 141 ALA 141 136 136 ALA ALA B . n 
A 1 142 ALA 142 137 137 ALA ALA B . n 
A 1 143 LEU 143 138 138 LEU LEU B . n 
A 1 144 GLU 144 139 139 GLU GLU B . n 
A 1 145 SER 145 140 140 SER SER B . n 
A 1 146 ARG 146 141 141 ARG ARG B . n 
A 1 147 PHE 147 142 142 PHE PHE B . n 
A 1 148 GLY 148 143 143 GLY GLY B . n 
A 1 149 ALA 149 144 144 ALA ALA B . n 
A 1 150 GLY 150 145 145 GLY GLY B . n 
A 1 151 TRP 151 146 146 TRP TRP B . n 
A 1 152 ASP 152 147 147 ASP ASP B . n 
A 1 153 MET 153 148 148 MET MET B . n 
A 1 154 THR 154 149 149 THR THR B . n 
A 1 155 GLY 155 150 150 GLY GLY B . n 
A 1 156 SER 156 151 151 SER SER B . n 
A 1 157 LEU 157 152 152 LEU LEU B . n 
A 1 158 ASP 158 153 153 ASP ASP B . n 
A 1 159 TYR 159 154 154 TYR TYR B . n 
A 1 160 PHE 160 155 155 PHE PHE B . n 
A 1 161 ARG 161 156 156 ARG ARG B . n 
A 1 162 ARG 162 157 157 ARG ARG B . n 
A 1 163 ILE 163 158 158 ILE ILE B . n 
A 1 164 LEU 164 159 159 LEU LEU B . n 
A 1 165 PRO 165 160 160 PRO PRO B . n 
A 1 166 GLY 166 161 161 GLY GLY B . n 
A 1 167 VAL 167 162 162 VAL VAL B . n 
A 1 168 GLY 168 163 163 GLY GLY B . n 
A 1 169 ALA 169 164 164 ALA ALA B . n 
A 1 170 PHE 170 165 165 PHE PHE B . n 
A 1 171 ARG 171 166 166 ARG ARG B . n 
A 1 172 LEU 172 167 167 LEU LEU B . n 
A 1 173 ARG 173 168 168 ARG ARG B . n 
A 1 174 VAL 174 169 169 VAL VAL B . n 
A 1 175 ALA 175 170 170 ALA ALA B . n 
A 1 176 GLU 176 171 171 GLU GLU B . n 
A 1 177 ALA 177 172 172 ALA ALA B . n 
A 1 178 ASP 178 173 173 ASP ASP B . n 
A 1 179 GLY 179 174 174 GLY GLY B . n 
A 1 180 MET 180 175 175 MET MET B . n 
A 1 181 PHE 181 176 176 PHE PHE B . n 
A 1 182 LYS 182 177 177 LYS LYS B . n 
A 1 183 LEU 183 178 178 LEU LEU B . n 
A 1 184 SER 184 179 179 SER SER B . n 
A 1 185 GLN 185 180 180 GLN GLN B . n 
A 1 186 GLU 186 181 181 GLU GLU B . n 
A 1 187 GLN 187 182 182 GLN GLN B . n 
A 1 188 GLN 188 183 183 GLN GLN B . n 
A 1 189 PRO 189 184 184 PRO PRO B . n 
A 1 190 ALA 190 185 185 ALA ALA B . n 
A 1 191 ILE 191 186 186 ILE ILE B . n 
A 1 192 ARG 192 187 187 ARG ARG B . n 
A 1 193 ARG 193 188 188 ARG ARG B . n 
A 1 194 ARG 194 189 189 ARG ARG B . n 
A 1 195 VAL 195 190 190 VAL VAL B . n 
A 1 196 ARG 196 191 191 ARG ARG B . n 
A 1 197 HIS 197 192 192 HIS HIS B . n 
A 1 198 SER 198 193 193 SER SER B . n 
A 1 199 PHE 199 194 194 PHE PHE B . n 
A 1 200 GLY 200 195 195 GLY GLY B . n 
A 1 201 GLY 201 196 196 GLY GLY B . n 
A 1 202 ALA 202 197 197 ALA ALA B . n 
A 1 203 GLU 203 198 198 GLU GLU B . n 
A 1 204 ALA 204 199 199 ALA ALA B . n 
A 1 205 THR 205 200 200 THR THR B . n 
A 1 206 ARG 206 201 201 ARG ARG B . n 
A 1 207 ALA 207 202 202 ALA ALA B . n 
A 1 208 VAL 208 203 203 VAL VAL B . n 
A 1 209 ALA 209 204 204 ALA ALA B . n 
A 1 210 GLY 210 205 205 GLY GLY B . n 
A 1 211 LEU 211 206 206 LEU LEU B . n 
A 1 212 MET 212 207 207 MET MET B . n 
A 1 213 ASP 213 208 208 ASP ASP B . n 
A 1 214 ARG 214 209 209 ARG ARG B . n 
A 1 215 LEU 215 210 210 LEU LEU B . n 
A 1 216 PRO 216 211 211 PRO PRO B . n 
A 1 217 THR 217 212 ?   ?   ?   B . n 
A 1 218 GLU 218 213 ?   ?   ?   B . n 
B 1 1   ALA 1   -4  ?   ?   ?   C . n 
B 1 2   GLY 2   -3  ?   ?   ?   C . n 
B 1 3   ALA 3   -2  ?   ?   ?   C . n 
B 1 4   GLY 4   -1  ?   ?   ?   C . n 
B 1 5   ALA 5   0   0   ALA ALA C . n 
B 1 6   MET 6   1   1   MET MET C . n 
B 1 7   PHE 7   2   2   PHE PHE C . n 
B 1 8   VAL 8   3   3   VAL VAL C . n 
B 1 9   PRO 9   4   4   PRO PRO C . n 
B 1 10  GLY 10  5   5   GLY GLY C . n 
B 1 11  PRO 11  6   6   PRO PRO C . n 
B 1 12  TYR 12  7   7   TYR TYR C . n 
B 1 13  HIS 13  8   8   HIS HIS C . n 
B 1 14  ALA 14  9   9   ALA ALA C . n 
B 1 15  PRO 15  10  10  PRO PRO C . n 
B 1 16  GLU 16  11  11  GLU GLU C . n 
B 1 17  ASP 17  12  12  ASP ASP C . n 
B 1 18  ARG 18  13  13  ARG ARG C . n 
B 1 19  TRP 19  14  14  TRP TRP C . n 
B 1 20  LEU 20  15  15  LEU LEU C . n 
B 1 21  VAL 21  16  16  VAL VAL C . n 
B 1 22  ASP 22  17  17  ASP ASP C . n 
B 1 23  LEU 23  18  18  LEU LEU C . n 
B 1 24  VAL 24  19  19  VAL VAL C . n 
B 1 25  ARG 25  20  20  ARG ARG C . n 
B 1 26  GLY 26  21  21  GLY GLY C . n 
B 1 27  HIS 27  22  22  HIS HIS C . n 
B 1 28  PRO 28  23  23  PRO PRO C . n 
B 1 29  LEU 29  24  24  LEU LEU C . n 
B 1 30  ALA 30  25  25  ALA ALA C . n 
B 1 31  GLN 31  26  26  GLN GLN C . n 
B 1 32  LEU 32  27  27  LEU LEU C . n 
B 1 33  ALA 33  28  28  ALA ALA C . n 
B 1 34  SER 34  29  29  SER SER C . n 
B 1 35  ASN 35  30  30  ASN ASN C . n 
B 1 36  GLY 36  31  31  GLY GLY C . n 
B 1 37  ALA 37  32  32  ALA ALA C . n 
B 1 38  GLY 38  33  33  GLY GLY C . n 
B 1 39  GLY 39  34  34  GLY GLY C . n 
B 1 40  ALA 40  35  35  ALA ALA C . n 
B 1 41  ALA 41  36  36  ALA ALA C . n 
B 1 42  PRO 42  37  37  PRO PRO C . n 
B 1 43  HIS 43  38  38  HIS HIS C . n 
B 1 44  ILE 44  39  39  ILE ILE C . n 
B 1 45  THR 45  40  40  THR THR C . n 
B 1 46  HIS 46  41  41  HIS HIS C . n 
B 1 47  VAL 47  42  42  VAL VAL C . n 
B 1 48  PRO 48  43  43  PRO PRO C . n 
B 1 49  ILE 49  44  44  ILE ILE C . n 
B 1 50  ILE 50  45  45  ILE ILE C . n 
B 1 51  VAL 51  46  46  VAL VAL C . n 
B 1 52  ASP 52  47  47  ASP ASP C . n 
B 1 53  PRO 53  48  48  PRO PRO C . n 
B 1 54  GLU 54  49  49  GLU GLU C . n 
B 1 55  LEU 55  50  50  LEU LEU C . n 
B 1 56  ASP 56  51  51  ASP ASP C . n 
B 1 57  GLY 57  52  52  GLY GLY C . n 
B 1 58  PRO 58  53  53  PRO PRO C . n 
B 1 59  VAL 59  54  54  VAL VAL C . n 
B 1 60  ASP 60  55  55  ASP ASP C . n 
B 1 61  ARG 61  56  56  ARG ARG C . n 
B 1 62  LEU 62  57  57  LEU LEU C . n 
B 1 63  VAL 63  58  58  VAL VAL C . n 
B 1 64  GLY 64  59  59  GLY GLY C . n 
B 1 65  ILE 65  60  60  ILE ILE C . n 
B 1 66  THR 66  61  61  THR THR C . n 
B 1 67  LEU 67  62  62  LEU LEU C . n 
B 1 68  TRP 68  63  63  TRP TRP C . n 
B 1 69  GLY 69  64  64  GLY GLY C . n 
B 1 70  HIS 70  65  65  HIS HIS C . n 
B 1 71  MET 71  66  66  MET MET C . n 
B 1 72  ASN 72  67  67  ASN ASN C . n 
B 1 73  ARG 73  68  68  ARG ARG C . n 
B 1 74  ALA 74  69  69  ALA ALA C . n 
B 1 75  ASN 75  70  70  ASN ASN C . n 
B 1 76  PRO 76  71  71  PRO PRO C . n 
B 1 77  HIS 77  72  72  HIS HIS C . n 
B 1 78  TRP 78  73  73  TRP TRP C . n 
B 1 79  ALA 79  74  74  ALA ALA C . n 
B 1 80  ALA 80  75  75  ALA ALA C . n 
B 1 81  LEU 81  76  76  LEU LEU C . n 
B 1 82  GLY 82  77  77  GLY GLY C . n 
B 1 83  GLY 83  78  78  GLY GLY C . n 
B 1 84  ALA 84  79  79  ALA ALA C . n 
B 1 85  ALA 85  80  80  ALA ALA C . n 
B 1 86  ASN 86  81  81  ASN ASN C . n 
B 1 87  VAL 87  82  82  VAL VAL C . n 
B 1 88  VAL 88  83  83  VAL VAL C . n 
B 1 89  ALA 89  84  84  ALA ALA C . n 
B 1 90  THR 90  85  85  THR THR C . n 
B 1 91  PHE 91  86  86  PHE PHE C . n 
B 1 92  ALA 92  87  87  ALA ALA C . n 
B 1 93  GLY 93  88  88  GLY GLY C . n 
B 1 94  PRO 94  89  89  PRO PRO C . n 
B 1 95  ASN 95  90  90  ASN ASN C . n 
B 1 96  ALA 96  91  91  ALA ALA C . n 
B 1 97  TYR 97  92  92  TYR TYR C . n 
B 1 98  VAL 98  93  93  VAL VAL C . n 
B 1 99  SER 99  94  94  SER SER C . n 
B 1 100 PRO 100 95  95  PRO PRO C . n 
B 1 101 ALA 101 96  96  ALA ALA C . n 
B 1 102 VAL 102 97  97  VAL VAL C . n 
B 1 103 TYR 103 98  98  TYR TYR C . n 
B 1 104 ARG 104 99  99  ARG ARG C . n 
B 1 105 THR 105 100 100 THR THR C . n 
B 1 106 ALA 106 101 101 ALA ALA C . n 
B 1 107 PRO 107 102 102 PRO PRO C . n 
B 1 108 ALA 108 103 103 ALA ALA C . n 
B 1 109 ALA 109 104 104 ALA ALA C . n 
B 1 110 PRO 110 105 105 PRO PRO C . n 
B 1 111 THR 111 106 106 THR THR C . n 
B 1 112 TRP 112 107 107 TRP TRP C . n 
B 1 113 ASN 113 108 108 ASN ASN C . n 
B 1 114 PHE 114 109 109 PHE PHE C . n 
B 1 115 THR 115 110 110 THR THR C . n 
B 1 116 SER 116 111 111 SER SER C . n 
B 1 117 VAL 117 112 112 VAL VAL C . n 
B 1 118 GLN 118 113 113 GLN GLN C . n 
B 1 119 VAL 119 114 114 VAL VAL C . n 
B 1 120 ARG 120 115 115 ARG ARG C . n 
B 1 121 GLY 121 116 116 GLY GLY C . n 
B 1 122 GLU 122 117 117 GLU GLU C . n 
B 1 123 LEU 123 118 118 LEU LEU C . n 
B 1 124 ARG 124 119 119 ARG ARG C . n 
B 1 125 LYS 125 120 120 LYS LYS C . n 
B 1 126 VAL 126 121 121 VAL VAL C . n 
B 1 127 GLU 127 122 122 GLU GLU C . n 
B 1 128 SER 128 123 123 SER SER C . n 
B 1 129 ALA 129 124 124 ALA ALA C . n 
B 1 130 ASP 130 125 125 ASP ASP C . n 
B 1 131 ASP 131 126 126 ASP ASP C . n 
B 1 132 THR 132 127 127 THR THR C . n 
B 1 133 LEU 133 128 128 LEU LEU C . n 
B 1 134 ALA 134 129 129 ALA ALA C . n 
B 1 135 THR 135 130 130 THR THR C . n 
B 1 136 VAL 136 131 131 VAL VAL C . n 
B 1 137 ARG 137 132 132 ARG ARG C . n 
B 1 138 ALA 138 133 133 ALA ALA C . n 
B 1 139 THR 139 134 134 THR THR C . n 
B 1 140 VAL 140 135 135 VAL VAL C . n 
B 1 141 ALA 141 136 136 ALA ALA C . n 
B 1 142 ALA 142 137 137 ALA ALA C . n 
B 1 143 LEU 143 138 138 LEU LEU C . n 
B 1 144 GLU 144 139 139 GLU GLU C . n 
B 1 145 SER 145 140 140 SER SER C . n 
B 1 146 ARG 146 141 141 ARG ARG C . n 
B 1 147 PHE 147 142 142 PHE PHE C . n 
B 1 148 GLY 148 143 143 GLY GLY C . n 
B 1 149 ALA 149 144 144 ALA ALA C . n 
B 1 150 GLY 150 145 145 GLY GLY C . n 
B 1 151 TRP 151 146 146 TRP TRP C . n 
B 1 152 ASP 152 147 147 ASP ASP C . n 
B 1 153 MET 153 148 148 MET MET C . n 
B 1 154 THR 154 149 149 THR THR C . n 
B 1 155 GLY 155 150 150 GLY GLY C . n 
B 1 156 SER 156 151 151 SER SER C . n 
B 1 157 LEU 157 152 152 LEU LEU C . n 
B 1 158 ASP 158 153 153 ASP ASP C . n 
B 1 159 TYR 159 154 154 TYR TYR C . n 
B 1 160 PHE 160 155 155 PHE PHE C . n 
B 1 161 ARG 161 156 156 ARG ARG C . n 
B 1 162 ARG 162 157 157 ARG ARG C . n 
B 1 163 ILE 163 158 158 ILE ILE C . n 
B 1 164 LEU 164 159 159 LEU LEU C . n 
B 1 165 PRO 165 160 160 PRO PRO C . n 
B 1 166 GLY 166 161 161 GLY GLY C . n 
B 1 167 VAL 167 162 162 VAL VAL C . n 
B 1 168 GLY 168 163 163 GLY GLY C . n 
B 1 169 ALA 169 164 164 ALA ALA C . n 
B 1 170 PHE 170 165 165 PHE PHE C . n 
B 1 171 ARG 171 166 166 ARG ARG C . n 
B 1 172 LEU 172 167 167 LEU LEU C . n 
B 1 173 ARG 173 168 168 ARG ARG C . n 
B 1 174 VAL 174 169 169 VAL VAL C . n 
B 1 175 ALA 175 170 170 ALA ALA C . n 
B 1 176 GLU 176 171 171 GLU GLU C . n 
B 1 177 ALA 177 172 172 ALA ALA C . n 
B 1 178 ASP 178 173 173 ASP ASP C . n 
B 1 179 GLY 179 174 174 GLY GLY C . n 
B 1 180 MET 180 175 175 MET MET C . n 
B 1 181 PHE 181 176 176 PHE PHE C . n 
B 1 182 LYS 182 177 177 LYS LYS C . n 
B 1 183 LEU 183 178 178 LEU LEU C . n 
B 1 184 SER 184 179 179 SER SER C . n 
B 1 185 GLN 185 180 180 GLN GLN C . n 
B 1 186 GLU 186 181 181 GLU GLU C . n 
B 1 187 GLN 187 182 182 GLN GLN C . n 
B 1 188 GLN 188 183 183 GLN GLN C . n 
B 1 189 PRO 189 184 184 PRO PRO C . n 
B 1 190 ALA 190 185 185 ALA ALA C . n 
B 1 191 ILE 191 186 186 ILE ILE C . n 
B 1 192 ARG 192 187 187 ARG ARG C . n 
B 1 193 ARG 193 188 188 ARG ARG C . n 
B 1 194 ARG 194 189 189 ARG ARG C . n 
B 1 195 VAL 195 190 190 VAL VAL C . n 
B 1 196 ARG 196 191 191 ARG ARG C . n 
B 1 197 HIS 197 192 192 HIS HIS C . n 
B 1 198 SER 198 193 193 SER SER C . n 
B 1 199 PHE 199 194 194 PHE PHE C . n 
B 1 200 GLY 200 195 195 GLY GLY C . n 
B 1 201 GLY 201 196 196 GLY GLY C . n 
B 1 202 ALA 202 197 197 ALA ALA C . n 
B 1 203 GLU 203 198 198 GLU GLU C . n 
B 1 204 ALA 204 199 199 ALA ALA C . n 
B 1 205 THR 205 200 200 THR THR C . n 
B 1 206 ARG 206 201 201 ARG ARG C . n 
B 1 207 ALA 207 202 202 ALA ALA C . n 
B 1 208 VAL 208 203 203 VAL VAL C . n 
B 1 209 ALA 209 204 204 ALA ALA C . n 
B 1 210 GLY 210 205 205 GLY GLY C . n 
B 1 211 LEU 211 206 206 LEU LEU C . n 
B 1 212 MET 212 207 207 MET MET C . n 
B 1 213 ASP 213 208 208 ASP ASP C . n 
B 1 214 ARG 214 209 209 ARG ARG C . n 
B 1 215 LEU 215 210 210 LEU LEU C . n 
B 1 216 PRO 216 211 211 PRO PRO C . n 
B 1 217 THR 217 212 ?   ?   ?   C . n 
B 1 218 GLU 218 213 ?   ?   ?   C . n 
C 1 1   ALA 1   -4  ?   ?   ?   D . n 
C 1 2   GLY 2   -3  ?   ?   ?   D . n 
C 1 3   ALA 3   -2  ?   ?   ?   D . n 
C 1 4   GLY 4   -1  -1  GLY GLY D . n 
C 1 5   ALA 5   0   0   ALA ALA D . n 
C 1 6   MET 6   1   1   MET MET D . n 
C 1 7   PHE 7   2   2   PHE PHE D . n 
C 1 8   VAL 8   3   3   VAL VAL D . n 
C 1 9   PRO 9   4   4   PRO PRO D . n 
C 1 10  GLY 10  5   5   GLY GLY D . n 
C 1 11  PRO 11  6   6   PRO PRO D . n 
C 1 12  TYR 12  7   7   TYR TYR D . n 
C 1 13  HIS 13  8   8   HIS HIS D . n 
C 1 14  ALA 14  9   9   ALA ALA D . n 
C 1 15  PRO 15  10  10  PRO PRO D . n 
C 1 16  GLU 16  11  11  GLU GLU D . n 
C 1 17  ASP 17  12  12  ASP ASP D . n 
C 1 18  ARG 18  13  13  ARG ARG D . n 
C 1 19  TRP 19  14  14  TRP TRP D . n 
C 1 20  LEU 20  15  15  LEU LEU D . n 
C 1 21  VAL 21  16  16  VAL VAL D . n 
C 1 22  ASP 22  17  17  ASP ASP D . n 
C 1 23  LEU 23  18  18  LEU LEU D . n 
C 1 24  VAL 24  19  19  VAL VAL D . n 
C 1 25  ARG 25  20  20  ARG ARG D . n 
C 1 26  GLY 26  21  21  GLY GLY D . n 
C 1 27  HIS 27  22  22  HIS HIS D . n 
C 1 28  PRO 28  23  23  PRO PRO D . n 
C 1 29  LEU 29  24  24  LEU LEU D . n 
C 1 30  ALA 30  25  25  ALA ALA D . n 
C 1 31  GLN 31  26  26  GLN GLN D . n 
C 1 32  LEU 32  27  27  LEU LEU D . n 
C 1 33  ALA 33  28  28  ALA ALA D . n 
C 1 34  SER 34  29  29  SER SER D . n 
C 1 35  ASN 35  30  30  ASN ASN D . n 
C 1 36  GLY 36  31  31  GLY GLY D . n 
C 1 37  ALA 37  32  32  ALA ALA D . n 
C 1 38  GLY 38  33  33  GLY GLY D . n 
C 1 39  GLY 39  34  34  GLY GLY D . n 
C 1 40  ALA 40  35  35  ALA ALA D . n 
C 1 41  ALA 41  36  36  ALA ALA D . n 
C 1 42  PRO 42  37  37  PRO PRO D . n 
C 1 43  HIS 43  38  38  HIS HIS D . n 
C 1 44  ILE 44  39  39  ILE ILE D . n 
C 1 45  THR 45  40  40  THR THR D . n 
C 1 46  HIS 46  41  41  HIS HIS D . n 
C 1 47  VAL 47  42  42  VAL VAL D . n 
C 1 48  PRO 48  43  43  PRO PRO D . n 
C 1 49  ILE 49  44  44  ILE ILE D . n 
C 1 50  ILE 50  45  45  ILE ILE D . n 
C 1 51  VAL 51  46  46  VAL VAL D . n 
C 1 52  ASP 52  47  47  ASP ASP D . n 
C 1 53  PRO 53  48  48  PRO PRO D . n 
C 1 54  GLU 54  49  49  GLU GLU D . n 
C 1 55  LEU 55  50  50  LEU LEU D . n 
C 1 56  ASP 56  51  51  ASP ASP D . n 
C 1 57  GLY 57  52  52  GLY GLY D . n 
C 1 58  PRO 58  53  53  PRO PRO D . n 
C 1 59  VAL 59  54  54  VAL VAL D . n 
C 1 60  ASP 60  55  55  ASP ASP D . n 
C 1 61  ARG 61  56  56  ARG ARG D . n 
C 1 62  LEU 62  57  57  LEU LEU D . n 
C 1 63  VAL 63  58  58  VAL VAL D . n 
C 1 64  GLY 64  59  59  GLY GLY D . n 
C 1 65  ILE 65  60  60  ILE ILE D . n 
C 1 66  THR 66  61  61  THR THR D . n 
C 1 67  LEU 67  62  62  LEU LEU D . n 
C 1 68  TRP 68  63  63  TRP TRP D . n 
C 1 69  GLY 69  64  64  GLY GLY D . n 
C 1 70  HIS 70  65  65  HIS HIS D . n 
C 1 71  MET 71  66  66  MET MET D . n 
C 1 72  ASN 72  67  67  ASN ASN D . n 
C 1 73  ARG 73  68  68  ARG ARG D . n 
C 1 74  ALA 74  69  69  ALA ALA D . n 
C 1 75  ASN 75  70  70  ASN ASN D . n 
C 1 76  PRO 76  71  71  PRO PRO D . n 
C 1 77  HIS 77  72  72  HIS HIS D . n 
C 1 78  TRP 78  73  73  TRP TRP D . n 
C 1 79  ALA 79  74  74  ALA ALA D . n 
C 1 80  ALA 80  75  75  ALA ALA D . n 
C 1 81  LEU 81  76  76  LEU LEU D . n 
C 1 82  GLY 82  77  77  GLY GLY D . n 
C 1 83  GLY 83  78  78  GLY GLY D . n 
C 1 84  ALA 84  79  79  ALA ALA D . n 
C 1 85  ALA 85  80  80  ALA ALA D . n 
C 1 86  ASN 86  81  81  ASN ASN D . n 
C 1 87  VAL 87  82  82  VAL VAL D . n 
C 1 88  VAL 88  83  83  VAL VAL D . n 
C 1 89  ALA 89  84  84  ALA ALA D . n 
C 1 90  THR 90  85  85  THR THR D . n 
C 1 91  PHE 91  86  86  PHE PHE D . n 
C 1 92  ALA 92  87  87  ALA ALA D . n 
C 1 93  GLY 93  88  88  GLY GLY D . n 
C 1 94  PRO 94  89  89  PRO PRO D . n 
C 1 95  ASN 95  90  90  ASN ASN D . n 
C 1 96  ALA 96  91  91  ALA ALA D . n 
C 1 97  TYR 97  92  92  TYR TYR D . n 
C 1 98  VAL 98  93  93  VAL VAL D . n 
C 1 99  SER 99  94  94  SER SER D . n 
C 1 100 PRO 100 95  95  PRO PRO D . n 
C 1 101 ALA 101 96  96  ALA ALA D . n 
C 1 102 VAL 102 97  97  VAL VAL D . n 
C 1 103 TYR 103 98  98  TYR TYR D . n 
C 1 104 ARG 104 99  99  ARG ARG D . n 
C 1 105 THR 105 100 100 THR THR D . n 
C 1 106 ALA 106 101 101 ALA ALA D . n 
C 1 107 PRO 107 102 102 PRO PRO D . n 
C 1 108 ALA 108 103 103 ALA ALA D . n 
C 1 109 ALA 109 104 104 ALA ALA D . n 
C 1 110 PRO 110 105 105 PRO PRO D . n 
C 1 111 THR 111 106 106 THR THR D . n 
C 1 112 TRP 112 107 107 TRP TRP D . n 
C 1 113 ASN 113 108 108 ASN ASN D . n 
C 1 114 PHE 114 109 109 PHE PHE D . n 
C 1 115 THR 115 110 110 THR THR D . n 
C 1 116 SER 116 111 111 SER SER D . n 
C 1 117 VAL 117 112 112 VAL VAL D . n 
C 1 118 GLN 118 113 113 GLN GLN D . n 
C 1 119 VAL 119 114 114 VAL VAL D . n 
C 1 120 ARG 120 115 115 ARG ARG D . n 
C 1 121 GLY 121 116 116 GLY GLY D . n 
C 1 122 GLU 122 117 117 GLU GLU D . n 
C 1 123 LEU 123 118 118 LEU LEU D . n 
C 1 124 ARG 124 119 119 ARG ARG D . n 
C 1 125 LYS 125 120 120 LYS LYS D . n 
C 1 126 VAL 126 121 121 VAL VAL D . n 
C 1 127 GLU 127 122 122 GLU GLU D . n 
C 1 128 SER 128 123 123 SER SER D . n 
C 1 129 ALA 129 124 124 ALA ALA D . n 
C 1 130 ASP 130 125 125 ASP ASP D . n 
C 1 131 ASP 131 126 126 ASP ASP D . n 
C 1 132 THR 132 127 127 THR THR D . n 
C 1 133 LEU 133 128 128 LEU LEU D . n 
C 1 134 ALA 134 129 129 ALA ALA D . n 
C 1 135 THR 135 130 130 THR THR D . n 
C 1 136 VAL 136 131 131 VAL VAL D . n 
C 1 137 ARG 137 132 132 ARG ARG D . n 
C 1 138 ALA 138 133 133 ALA ALA D . n 
C 1 139 THR 139 134 134 THR THR D . n 
C 1 140 VAL 140 135 135 VAL VAL D . n 
C 1 141 ALA 141 136 136 ALA ALA D . n 
C 1 142 ALA 142 137 137 ALA ALA D . n 
C 1 143 LEU 143 138 138 LEU LEU D . n 
C 1 144 GLU 144 139 139 GLU GLU D . n 
C 1 145 SER 145 140 140 SER SER D . n 
C 1 146 ARG 146 141 141 ARG ARG D . n 
C 1 147 PHE 147 142 142 PHE PHE D . n 
C 1 148 GLY 148 143 143 GLY GLY D . n 
C 1 149 ALA 149 144 144 ALA ALA D . n 
C 1 150 GLY 150 145 145 GLY GLY D . n 
C 1 151 TRP 151 146 146 TRP TRP D . n 
C 1 152 ASP 152 147 147 ASP ASP D . n 
C 1 153 MET 153 148 148 MET MET D . n 
C 1 154 THR 154 149 149 THR THR D . n 
C 1 155 GLY 155 150 150 GLY GLY D . n 
C 1 156 SER 156 151 151 SER SER D . n 
C 1 157 LEU 157 152 152 LEU LEU D . n 
C 1 158 ASP 158 153 153 ASP ASP D . n 
C 1 159 TYR 159 154 154 TYR TYR D . n 
C 1 160 PHE 160 155 155 PHE PHE D . n 
C 1 161 ARG 161 156 156 ARG ARG D . n 
C 1 162 ARG 162 157 157 ARG ARG D . n 
C 1 163 ILE 163 158 158 ILE ILE D . n 
C 1 164 LEU 164 159 159 LEU LEU D . n 
C 1 165 PRO 165 160 160 PRO PRO D . n 
C 1 166 GLY 166 161 161 GLY GLY D . n 
C 1 167 VAL 167 162 162 VAL VAL D . n 
C 1 168 GLY 168 163 163 GLY GLY D . n 
C 1 169 ALA 169 164 164 ALA ALA D . n 
C 1 170 PHE 170 165 165 PHE PHE D . n 
C 1 171 ARG 171 166 166 ARG ARG D . n 
C 1 172 LEU 172 167 167 LEU LEU D . n 
C 1 173 ARG 173 168 168 ARG ARG D . n 
C 1 174 VAL 174 169 169 VAL VAL D . n 
C 1 175 ALA 175 170 170 ALA ALA D . n 
C 1 176 GLU 176 171 171 GLU GLU D . n 
C 1 177 ALA 177 172 172 ALA ALA D . n 
C 1 178 ASP 178 173 173 ASP ASP D . n 
C 1 179 GLY 179 174 174 GLY GLY D . n 
C 1 180 MET 180 175 175 MET MET D . n 
C 1 181 PHE 181 176 176 PHE PHE D . n 
C 1 182 LYS 182 177 177 LYS LYS D . n 
C 1 183 LEU 183 178 178 LEU LEU D . n 
C 1 184 SER 184 179 179 SER SER D . n 
C 1 185 GLN 185 180 180 GLN GLN D . n 
C 1 186 GLU 186 181 181 GLU GLU D . n 
C 1 187 GLN 187 182 182 GLN GLN D . n 
C 1 188 GLN 188 183 183 GLN GLN D . n 
C 1 189 PRO 189 184 184 PRO PRO D . n 
C 1 190 ALA 190 185 185 ALA ALA D . n 
C 1 191 ILE 191 186 186 ILE ILE D . n 
C 1 192 ARG 192 187 187 ARG ARG D . n 
C 1 193 ARG 193 188 188 ARG ARG D . n 
C 1 194 ARG 194 189 189 ARG ARG D . n 
C 1 195 VAL 195 190 190 VAL VAL D . n 
C 1 196 ARG 196 191 191 ARG ARG D . n 
C 1 197 HIS 197 192 192 HIS HIS D . n 
C 1 198 SER 198 193 193 SER SER D . n 
C 1 199 PHE 199 194 194 PHE PHE D . n 
C 1 200 GLY 200 195 195 GLY GLY D . n 
C 1 201 GLY 201 196 196 GLY GLY D . n 
C 1 202 ALA 202 197 197 ALA ALA D . n 
C 1 203 GLU 203 198 198 GLU GLU D . n 
C 1 204 ALA 204 199 199 ALA ALA D . n 
C 1 205 THR 205 200 200 THR THR D . n 
C 1 206 ARG 206 201 201 ARG ARG D . n 
C 1 207 ALA 207 202 202 ALA ALA D . n 
C 1 208 VAL 208 203 203 VAL VAL D . n 
C 1 209 ALA 209 204 204 ALA ALA D . n 
C 1 210 GLY 210 205 205 GLY GLY D . n 
C 1 211 LEU 211 206 206 LEU LEU D . n 
C 1 212 MET 212 207 207 MET MET D . n 
C 1 213 ASP 213 208 208 ASP ASP D . n 
C 1 214 ARG 214 209 209 ARG ARG D . n 
C 1 215 LEU 215 210 210 LEU LEU D . n 
C 1 216 PRO 216 211 211 PRO PRO D . n 
C 1 217 THR 217 212 ?   ?   ?   D . n 
C 1 218 GLU 218 213 ?   ?   ?   D . n 
D 1 1   ALA 1   -4  ?   ?   ?   A . n 
D 1 2   GLY 2   -3  ?   ?   ?   A . n 
D 1 3   ALA 3   -2  ?   ?   ?   A . n 
D 1 4   GLY 4   -1  -1  GLY GLY A . n 
D 1 5   ALA 5   0   0   ALA ALA A . n 
D 1 6   MET 6   1   1   MET MET A . n 
D 1 7   PHE 7   2   2   PHE PHE A . n 
D 1 8   VAL 8   3   3   VAL VAL A . n 
D 1 9   PRO 9   4   4   PRO PRO A . n 
D 1 10  GLY 10  5   5   GLY GLY A . n 
D 1 11  PRO 11  6   6   PRO PRO A . n 
D 1 12  TYR 12  7   7   TYR TYR A . n 
D 1 13  HIS 13  8   8   HIS HIS A . n 
D 1 14  ALA 14  9   9   ALA ALA A . n 
D 1 15  PRO 15  10  10  PRO PRO A . n 
D 1 16  GLU 16  11  11  GLU GLU A . n 
D 1 17  ASP 17  12  12  ASP ASP A . n 
D 1 18  ARG 18  13  13  ARG ARG A . n 
D 1 19  TRP 19  14  14  TRP TRP A . n 
D 1 20  LEU 20  15  15  LEU LEU A . n 
D 1 21  VAL 21  16  16  VAL VAL A . n 
D 1 22  ASP 22  17  17  ASP ASP A . n 
D 1 23  LEU 23  18  18  LEU LEU A . n 
D 1 24  VAL 24  19  19  VAL VAL A . n 
D 1 25  ARG 25  20  20  ARG ARG A . n 
D 1 26  GLY 26  21  21  GLY GLY A . n 
D 1 27  HIS 27  22  22  HIS HIS A . n 
D 1 28  PRO 28  23  23  PRO PRO A . n 
D 1 29  LEU 29  24  24  LEU LEU A . n 
D 1 30  ALA 30  25  25  ALA ALA A . n 
D 1 31  GLN 31  26  26  GLN GLN A . n 
D 1 32  LEU 32  27  27  LEU LEU A . n 
D 1 33  ALA 33  28  28  ALA ALA A . n 
D 1 34  SER 34  29  29  SER SER A . n 
D 1 35  ASN 35  30  30  ASN ASN A . n 
D 1 36  GLY 36  31  31  GLY GLY A . n 
D 1 37  ALA 37  32  32  ALA ALA A . n 
D 1 38  GLY 38  33  33  GLY GLY A . n 
D 1 39  GLY 39  34  34  GLY GLY A . n 
D 1 40  ALA 40  35  35  ALA ALA A . n 
D 1 41  ALA 41  36  36  ALA ALA A . n 
D 1 42  PRO 42  37  37  PRO PRO A . n 
D 1 43  HIS 43  38  38  HIS HIS A . n 
D 1 44  ILE 44  39  39  ILE ILE A . n 
D 1 45  THR 45  40  40  THR THR A . n 
D 1 46  HIS 46  41  41  HIS HIS A . n 
D 1 47  VAL 47  42  42  VAL VAL A . n 
D 1 48  PRO 48  43  43  PRO PRO A . n 
D 1 49  ILE 49  44  44  ILE ILE A . n 
D 1 50  ILE 50  45  45  ILE ILE A . n 
D 1 51  VAL 51  46  46  VAL VAL A . n 
D 1 52  ASP 52  47  47  ASP ASP A . n 
D 1 53  PRO 53  48  48  PRO PRO A . n 
D 1 54  GLU 54  49  49  GLU GLU A . n 
D 1 55  LEU 55  50  50  LEU LEU A . n 
D 1 56  ASP 56  51  51  ASP ASP A . n 
D 1 57  GLY 57  52  52  GLY GLY A . n 
D 1 58  PRO 58  53  53  PRO PRO A . n 
D 1 59  VAL 59  54  54  VAL VAL A . n 
D 1 60  ASP 60  55  55  ASP ASP A . n 
D 1 61  ARG 61  56  56  ARG ARG A . n 
D 1 62  LEU 62  57  57  LEU LEU A . n 
D 1 63  VAL 63  58  58  VAL VAL A . n 
D 1 64  GLY 64  59  59  GLY GLY A . n 
D 1 65  ILE 65  60  60  ILE ILE A . n 
D 1 66  THR 66  61  61  THR THR A . n 
D 1 67  LEU 67  62  62  LEU LEU A . n 
D 1 68  TRP 68  63  63  TRP TRP A . n 
D 1 69  GLY 69  64  64  GLY GLY A . n 
D 1 70  HIS 70  65  65  HIS HIS A . n 
D 1 71  MET 71  66  66  MET MET A . n 
D 1 72  ASN 72  67  67  ASN ASN A . n 
D 1 73  ARG 73  68  68  ARG ARG A . n 
D 1 74  ALA 74  69  69  ALA ALA A . n 
D 1 75  ASN 75  70  70  ASN ASN A . n 
D 1 76  PRO 76  71  71  PRO PRO A . n 
D 1 77  HIS 77  72  72  HIS HIS A . n 
D 1 78  TRP 78  73  73  TRP TRP A . n 
D 1 79  ALA 79  74  74  ALA ALA A . n 
D 1 80  ALA 80  75  75  ALA ALA A . n 
D 1 81  LEU 81  76  76  LEU LEU A . n 
D 1 82  GLY 82  77  77  GLY GLY A . n 
D 1 83  GLY 83  78  78  GLY GLY A . n 
D 1 84  ALA 84  79  79  ALA ALA A . n 
D 1 85  ALA 85  80  80  ALA ALA A . n 
D 1 86  ASN 86  81  81  ASN ASN A . n 
D 1 87  VAL 87  82  82  VAL VAL A . n 
D 1 88  VAL 88  83  83  VAL VAL A . n 
D 1 89  ALA 89  84  84  ALA ALA A . n 
D 1 90  THR 90  85  85  THR THR A . n 
D 1 91  PHE 91  86  86  PHE PHE A . n 
D 1 92  ALA 92  87  87  ALA ALA A . n 
D 1 93  GLY 93  88  88  GLY GLY A . n 
D 1 94  PRO 94  89  89  PRO PRO A . n 
D 1 95  ASN 95  90  90  ASN ASN A . n 
D 1 96  ALA 96  91  91  ALA ALA A . n 
D 1 97  TYR 97  92  92  TYR TYR A . n 
D 1 98  VAL 98  93  93  VAL VAL A . n 
D 1 99  SER 99  94  94  SER SER A . n 
D 1 100 PRO 100 95  95  PRO PRO A . n 
D 1 101 ALA 101 96  96  ALA ALA A . n 
D 1 102 VAL 102 97  97  VAL VAL A . n 
D 1 103 TYR 103 98  98  TYR TYR A . n 
D 1 104 ARG 104 99  99  ARG ARG A . n 
D 1 105 THR 105 100 100 THR THR A . n 
D 1 106 ALA 106 101 101 ALA ALA A . n 
D 1 107 PRO 107 102 102 PRO PRO A . n 
D 1 108 ALA 108 103 103 ALA ALA A . n 
D 1 109 ALA 109 104 104 ALA ALA A . n 
D 1 110 PRO 110 105 105 PRO PRO A . n 
D 1 111 THR 111 106 106 THR THR A . n 
D 1 112 TRP 112 107 107 TRP TRP A . n 
D 1 113 ASN 113 108 108 ASN ASN A . n 
D 1 114 PHE 114 109 109 PHE PHE A . n 
D 1 115 THR 115 110 110 THR THR A . n 
D 1 116 SER 116 111 111 SER SER A . n 
D 1 117 VAL 117 112 112 VAL VAL A . n 
D 1 118 GLN 118 113 113 GLN GLN A . n 
D 1 119 VAL 119 114 114 VAL VAL A . n 
D 1 120 ARG 120 115 115 ARG ARG A . n 
D 1 121 GLY 121 116 116 GLY GLY A . n 
D 1 122 GLU 122 117 117 GLU GLU A . n 
D 1 123 LEU 123 118 118 LEU LEU A . n 
D 1 124 ARG 124 119 119 ARG ARG A . n 
D 1 125 LYS 125 120 120 LYS LYS A . n 
D 1 126 VAL 126 121 121 VAL VAL A . n 
D 1 127 GLU 127 122 122 GLU GLU A . n 
D 1 128 SER 128 123 123 SER SER A . n 
D 1 129 ALA 129 124 124 ALA ALA A . n 
D 1 130 ASP 130 125 125 ASP ASP A . n 
D 1 131 ASP 131 126 126 ASP ASP A . n 
D 1 132 THR 132 127 127 THR THR A . n 
D 1 133 LEU 133 128 128 LEU LEU A . n 
D 1 134 ALA 134 129 129 ALA ALA A . n 
D 1 135 THR 135 130 130 THR THR A . n 
D 1 136 VAL 136 131 131 VAL VAL A . n 
D 1 137 ARG 137 132 132 ARG ARG A . n 
D 1 138 ALA 138 133 133 ALA ALA A . n 
D 1 139 THR 139 134 134 THR THR A . n 
D 1 140 VAL 140 135 135 VAL VAL A . n 
D 1 141 ALA 141 136 136 ALA ALA A . n 
D 1 142 ALA 142 137 137 ALA ALA A . n 
D 1 143 LEU 143 138 138 LEU LEU A . n 
D 1 144 GLU 144 139 139 GLU GLU A . n 
D 1 145 SER 145 140 140 SER SER A . n 
D 1 146 ARG 146 141 141 ARG ARG A . n 
D 1 147 PHE 147 142 142 PHE PHE A . n 
D 1 148 GLY 148 143 143 GLY GLY A . n 
D 1 149 ALA 149 144 144 ALA ALA A . n 
D 1 150 GLY 150 145 145 GLY GLY A . n 
D 1 151 TRP 151 146 146 TRP TRP A . n 
D 1 152 ASP 152 147 147 ASP ASP A . n 
D 1 153 MET 153 148 148 MET MET A . n 
D 1 154 THR 154 149 149 THR THR A . n 
D 1 155 GLY 155 150 150 GLY GLY A . n 
D 1 156 SER 156 151 151 SER SER A . n 
D 1 157 LEU 157 152 152 LEU LEU A . n 
D 1 158 ASP 158 153 153 ASP ASP A . n 
D 1 159 TYR 159 154 154 TYR TYR A . n 
D 1 160 PHE 160 155 155 PHE PHE A . n 
D 1 161 ARG 161 156 156 ARG ARG A . n 
D 1 162 ARG 162 157 157 ARG ARG A . n 
D 1 163 ILE 163 158 158 ILE ILE A . n 
D 1 164 LEU 164 159 159 LEU LEU A . n 
D 1 165 PRO 165 160 160 PRO PRO A . n 
D 1 166 GLY 166 161 161 GLY GLY A . n 
D 1 167 VAL 167 162 162 VAL VAL A . n 
D 1 168 GLY 168 163 163 GLY GLY A . n 
D 1 169 ALA 169 164 164 ALA ALA A . n 
D 1 170 PHE 170 165 165 PHE PHE A . n 
D 1 171 ARG 171 166 166 ARG ARG A . n 
D 1 172 LEU 172 167 167 LEU LEU A . n 
D 1 173 ARG 173 168 168 ARG ARG A . n 
D 1 174 VAL 174 169 169 VAL VAL A . n 
D 1 175 ALA 175 170 170 ALA ALA A . n 
D 1 176 GLU 176 171 171 GLU GLU A . n 
D 1 177 ALA 177 172 172 ALA ALA A . n 
D 1 178 ASP 178 173 173 ASP ASP A . n 
D 1 179 GLY 179 174 174 GLY GLY A . n 
D 1 180 MET 180 175 175 MET MET A . n 
D 1 181 PHE 181 176 176 PHE PHE A . n 
D 1 182 LYS 182 177 177 LYS LYS A . n 
D 1 183 LEU 183 178 178 LEU LEU A . n 
D 1 184 SER 184 179 179 SER SER A . n 
D 1 185 GLN 185 180 180 GLN GLN A . n 
D 1 186 GLU 186 181 181 GLU GLU A . n 
D 1 187 GLN 187 182 182 GLN GLN A . n 
D 1 188 GLN 188 183 183 GLN GLN A . n 
D 1 189 PRO 189 184 184 PRO PRO A . n 
D 1 190 ALA 190 185 185 ALA ALA A . n 
D 1 191 ILE 191 186 186 ILE ILE A . n 
D 1 192 ARG 192 187 187 ARG ARG A . n 
D 1 193 ARG 193 188 188 ARG ARG A . n 
D 1 194 ARG 194 189 189 ARG ARG A . n 
D 1 195 VAL 195 190 190 VAL VAL A . n 
D 1 196 ARG 196 191 191 ARG ARG A . n 
D 1 197 HIS 197 192 192 HIS HIS A . n 
D 1 198 SER 198 193 193 SER SER A . n 
D 1 199 PHE 199 194 194 PHE PHE A . n 
D 1 200 GLY 200 195 195 GLY GLY A . n 
D 1 201 GLY 201 196 196 GLY GLY A . n 
D 1 202 ALA 202 197 197 ALA ALA A . n 
D 1 203 GLU 203 198 198 GLU GLU A . n 
D 1 204 ALA 204 199 199 ALA ALA A . n 
D 1 205 THR 205 200 200 THR THR A . n 
D 1 206 ARG 206 201 201 ARG ARG A . n 
D 1 207 ALA 207 202 202 ALA ALA A . n 
D 1 208 VAL 208 203 203 VAL VAL A . n 
D 1 209 ALA 209 204 204 ALA ALA A . n 
D 1 210 GLY 210 205 205 GLY GLY A . n 
D 1 211 LEU 211 206 206 LEU LEU A . n 
D 1 212 MET 212 207 207 MET MET A . n 
D 1 213 ASP 213 208 208 ASP ASP A . n 
D 1 214 ARG 214 209 209 ARG ARG A . n 
D 1 215 LEU 215 210 210 LEU LEU A . n 
D 1 216 PRO 216 211 211 PRO PRO A . n 
D 1 217 THR 217 212 212 THR THR A . n 
D 1 218 GLU 218 213 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ECN 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ECN 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 2 HEM   1   301 2   HEM   HEM B . 
F 3 A1ECN 1   302 1   A1ECN DRG B . 
G 2 HEM   1   301 3   HEM   HEM C . 
H 2 HEM   1   301 4   HEM   HEM D . 
I 3 A1ECN 1   302 3   A1ECN DRG D . 
J 2 HEM   1   301 5   HEM   HEM A . 
K 3 A1ECN 1   302 2   A1ECN DRG A . 
L 4 HOH   1   401 790 HOH   HOH B . 
L 4 HOH   2   402 745 HOH   HOH B . 
L 4 HOH   3   403 744 HOH   HOH B . 
L 4 HOH   4   404 193 HOH   HOH B . 
L 4 HOH   5   405 804 HOH   HOH B . 
L 4 HOH   6   406 767 HOH   HOH B . 
L 4 HOH   7   407 134 HOH   HOH B . 
L 4 HOH   8   408 436 HOH   HOH B . 
L 4 HOH   9   409 746 HOH   HOH B . 
L 4 HOH   10  410 503 HOH   HOH B . 
L 4 HOH   11  411 398 HOH   HOH B . 
L 4 HOH   12  412 641 HOH   HOH B . 
L 4 HOH   13  413 520 HOH   HOH B . 
L 4 HOH   14  414 311 HOH   HOH B . 
L 4 HOH   15  415 16  HOH   HOH B . 
L 4 HOH   16  416 165 HOH   HOH B . 
L 4 HOH   17  417 612 HOH   HOH B . 
L 4 HOH   18  418 290 HOH   HOH B . 
L 4 HOH   19  419 127 HOH   HOH B . 
L 4 HOH   20  420 175 HOH   HOH B . 
L 4 HOH   21  421 314 HOH   HOH B . 
L 4 HOH   22  422 762 HOH   HOH B . 
L 4 HOH   23  423 621 HOH   HOH B . 
L 4 HOH   24  424 153 HOH   HOH B . 
L 4 HOH   25  425 524 HOH   HOH B . 
L 4 HOH   26  426 212 HOH   HOH B . 
L 4 HOH   27  427 166 HOH   HOH B . 
L 4 HOH   28  428 713 HOH   HOH B . 
L 4 HOH   29  429 184 HOH   HOH B . 
L 4 HOH   30  430 396 HOH   HOH B . 
L 4 HOH   31  431 529 HOH   HOH B . 
L 4 HOH   32  432 577 HOH   HOH B . 
L 4 HOH   33  433 97  HOH   HOH B . 
L 4 HOH   34  434 179 HOH   HOH B . 
L 4 HOH   35  435 574 HOH   HOH B . 
L 4 HOH   36  436 43  HOH   HOH B . 
L 4 HOH   37  437 739 HOH   HOH B . 
L 4 HOH   38  438 588 HOH   HOH B . 
L 4 HOH   39  439 180 HOH   HOH B . 
L 4 HOH   40  440 192 HOH   HOH B . 
L 4 HOH   41  441 387 HOH   HOH B . 
L 4 HOH   42  442 856 HOH   HOH B . 
L 4 HOH   43  443 593 HOH   HOH B . 
L 4 HOH   44  444 339 HOH   HOH B . 
L 4 HOH   45  445 210 HOH   HOH B . 
L 4 HOH   46  446 300 HOH   HOH B . 
L 4 HOH   47  447 546 HOH   HOH B . 
L 4 HOH   48  448 313 HOH   HOH B . 
L 4 HOH   49  449 478 HOH   HOH B . 
L 4 HOH   50  450 381 HOH   HOH B . 
L 4 HOH   51  451 784 HOH   HOH B . 
L 4 HOH   52  452 102 HOH   HOH B . 
L 4 HOH   53  453 133 HOH   HOH B . 
L 4 HOH   54  454 418 HOH   HOH B . 
L 4 HOH   55  455 156 HOH   HOH B . 
L 4 HOH   56  456 132 HOH   HOH B . 
L 4 HOH   57  457 299 HOH   HOH B . 
L 4 HOH   58  458 2   HOH   HOH B . 
L 4 HOH   59  459 653 HOH   HOH B . 
L 4 HOH   60  460 44  HOH   HOH B . 
L 4 HOH   61  461 149 HOH   HOH B . 
L 4 HOH   62  462 434 HOH   HOH B . 
L 4 HOH   63  463 284 HOH   HOH B . 
L 4 HOH   64  464 146 HOH   HOH B . 
L 4 HOH   65  465 471 HOH   HOH B . 
L 4 HOH   66  466 464 HOH   HOH B . 
L 4 HOH   67  467 211 HOH   HOH B . 
L 4 HOH   68  468 67  HOH   HOH B . 
L 4 HOH   69  469 152 HOH   HOH B . 
L 4 HOH   70  470 107 HOH   HOH B . 
L 4 HOH   71  471 281 HOH   HOH B . 
L 4 HOH   72  472 30  HOH   HOH B . 
L 4 HOH   73  473 512 HOH   HOH B . 
L 4 HOH   74  474 394 HOH   HOH B . 
L 4 HOH   75  475 519 HOH   HOH B . 
L 4 HOH   76  476 202 HOH   HOH B . 
L 4 HOH   77  477 54  HOH   HOH B . 
L 4 HOH   78  478 329 HOH   HOH B . 
L 4 HOH   79  479 191 HOH   HOH B . 
L 4 HOH   80  480 106 HOH   HOH B . 
L 4 HOH   81  481 366 HOH   HOH B . 
L 4 HOH   82  482 155 HOH   HOH B . 
L 4 HOH   83  483 141 HOH   HOH B . 
L 4 HOH   84  484 350 HOH   HOH B . 
L 4 HOH   85  485 456 HOH   HOH B . 
L 4 HOH   86  486 325 HOH   HOH B . 
L 4 HOH   87  487 459 HOH   HOH B . 
L 4 HOH   88  488 341 HOH   HOH B . 
L 4 HOH   89  489 383 HOH   HOH B . 
L 4 HOH   90  490 163 HOH   HOH B . 
L 4 HOH   91  491 31  HOH   HOH B . 
L 4 HOH   92  492 736 HOH   HOH B . 
L 4 HOH   93  493 331 HOH   HOH B . 
L 4 HOH   94  494 124 HOH   HOH B . 
L 4 HOH   95  495 78  HOH   HOH B . 
L 4 HOH   96  496 647 HOH   HOH B . 
L 4 HOH   97  497 252 HOH   HOH B . 
L 4 HOH   98  498 830 HOH   HOH B . 
L 4 HOH   99  499 200 HOH   HOH B . 
L 4 HOH   100 500 19  HOH   HOH B . 
L 4 HOH   101 501 137 HOH   HOH B . 
L 4 HOH   102 502 569 HOH   HOH B . 
L 4 HOH   103 503 205 HOH   HOH B . 
L 4 HOH   104 504 251 HOH   HOH B . 
L 4 HOH   105 505 559 HOH   HOH B . 
L 4 HOH   106 506 174 HOH   HOH B . 
L 4 HOH   107 507 99  HOH   HOH B . 
L 4 HOH   108 508 656 HOH   HOH B . 
L 4 HOH   109 509 57  HOH   HOH B . 
L 4 HOH   110 510 110 HOH   HOH B . 
L 4 HOH   111 511 815 HOH   HOH B . 
L 4 HOH   112 512 650 HOH   HOH B . 
L 4 HOH   113 513 142 HOH   HOH B . 
L 4 HOH   114 514 757 HOH   HOH B . 
L 4 HOH   115 515 533 HOH   HOH B . 
L 4 HOH   116 516 84  HOH   HOH B . 
L 4 HOH   117 517 46  HOH   HOH B . 
L 4 HOH   118 518 651 HOH   HOH B . 
L 4 HOH   119 519 154 HOH   HOH B . 
L 4 HOH   120 520 72  HOH   HOH B . 
L 4 HOH   121 521 51  HOH   HOH B . 
L 4 HOH   122 522 441 HOH   HOH B . 
L 4 HOH   123 523 28  HOH   HOH B . 
L 4 HOH   124 524 812 HOH   HOH B . 
L 4 HOH   125 525 232 HOH   HOH B . 
L 4 HOH   126 526 422 HOH   HOH B . 
L 4 HOH   127 527 140 HOH   HOH B . 
L 4 HOH   128 528 776 HOH   HOH B . 
L 4 HOH   129 529 86  HOH   HOH B . 
L 4 HOH   130 530 135 HOH   HOH B . 
L 4 HOH   131 531 435 HOH   HOH B . 
L 4 HOH   132 532 619 HOH   HOH B . 
L 4 HOH   133 533 206 HOH   HOH B . 
L 4 HOH   134 534 411 HOH   HOH B . 
L 4 HOH   135 535 505 HOH   HOH B . 
L 4 HOH   136 536 695 HOH   HOH B . 
L 4 HOH   137 537 95  HOH   HOH B . 
L 4 HOH   138 538 511 HOH   HOH B . 
L 4 HOH   139 539 298 HOH   HOH B . 
L 4 HOH   140 540 302 HOH   HOH B . 
L 4 HOH   141 541 355 HOH   HOH B . 
L 4 HOH   142 542 760 HOH   HOH B . 
L 4 HOH   143 543 842 HOH   HOH B . 
L 4 HOH   144 544 598 HOH   HOH B . 
L 4 HOH   145 545 761 HOH   HOH B . 
L 4 HOH   146 546 241 HOH   HOH B . 
L 4 HOH   147 547 91  HOH   HOH B . 
L 4 HOH   148 548 635 HOH   HOH B . 
L 4 HOH   149 549 4   HOH   HOH B . 
L 4 HOH   150 550 810 HOH   HOH B . 
L 4 HOH   151 551 808 HOH   HOH B . 
L 4 HOH   152 552 157 HOH   HOH B . 
L 4 HOH   153 553 303 HOH   HOH B . 
L 4 HOH   154 554 763 HOH   HOH B . 
L 4 HOH   155 555 439 HOH   HOH B . 
L 4 HOH   156 556 280 HOH   HOH B . 
L 4 HOH   157 557 47  HOH   HOH B . 
L 4 HOH   158 558 223 HOH   HOH B . 
L 4 HOH   159 559 720 HOH   HOH B . 
L 4 HOH   160 560 220 HOH   HOH B . 
L 4 HOH   161 561 283 HOH   HOH B . 
L 4 HOH   162 562 643 HOH   HOH B . 
L 4 HOH   163 563 743 HOH   HOH B . 
L 4 HOH   164 564 774 HOH   HOH B . 
L 4 HOH   165 565 816 HOH   HOH B . 
L 4 HOH   166 566 467 HOH   HOH B . 
L 4 HOH   167 567 368 HOH   HOH B . 
L 4 HOH   168 568 572 HOH   HOH B . 
L 4 HOH   169 569 672 HOH   HOH B . 
L 4 HOH   170 570 732 HOH   HOH B . 
L 4 HOH   171 571 747 HOH   HOH B . 
L 4 HOH   172 572 779 HOH   HOH B . 
L 4 HOH   173 573 226 HOH   HOH B . 
L 4 HOH   174 574 590 HOH   HOH B . 
L 4 HOH   175 575 540 HOH   HOH B . 
L 4 HOH   176 576 693 HOH   HOH B . 
L 4 HOH   177 577 649 HOH   HOH B . 
L 4 HOH   178 578 676 HOH   HOH B . 
L 4 HOH   179 579 741 HOH   HOH B . 
L 4 HOH   180 580 807 HOH   HOH B . 
L 4 HOH   181 581 447 HOH   HOH B . 
L 4 HOH   182 582 273 HOH   HOH B . 
L 4 HOH   183 583 638 HOH   HOH B . 
L 4 HOH   184 584 700 HOH   HOH B . 
L 4 HOH   185 585 829 HOH   HOH B . 
L 4 HOH   186 586 696 HOH   HOH B . 
L 4 HOH   187 587 499 HOH   HOH B . 
L 4 HOH   188 588 194 HOH   HOH B . 
L 4 HOH   189 589 721 HOH   HOH B . 
L 4 HOH   190 590 719 HOH   HOH B . 
L 4 HOH   191 591 172 HOH   HOH B . 
L 4 HOH   192 592 642 HOH   HOH B . 
L 4 HOH   193 593 610 HOH   HOH B . 
L 4 HOH   194 594 177 HOH   HOH B . 
L 4 HOH   195 595 645 HOH   HOH B . 
L 4 HOH   196 596 536 HOH   HOH B . 
L 4 HOH   197 597 451 HOH   HOH B . 
L 4 HOH   198 598 668 HOH   HOH B . 
L 4 HOH   199 599 476 HOH   HOH B . 
L 4 HOH   200 600 622 HOH   HOH B . 
L 4 HOH   201 601 710 HOH   HOH B . 
L 4 HOH   202 602 404 HOH   HOH B . 
L 4 HOH   203 603 604 HOH   HOH B . 
L 4 HOH   204 604 484 HOH   HOH B . 
L 4 HOH   205 605 805 HOH   HOH B . 
L 4 HOH   206 606 343 HOH   HOH B . 
L 4 HOH   207 607 363 HOH   HOH B . 
L 4 HOH   208 608 344 HOH   HOH B . 
L 4 HOH   209 609 230 HOH   HOH B . 
L 4 HOH   210 610 813 HOH   HOH B . 
L 4 HOH   211 611 420 HOH   HOH B . 
L 4 HOH   212 612 687 HOH   HOH B . 
L 4 HOH   213 613 377 HOH   HOH B . 
L 4 HOH   214 614 711 HOH   HOH B . 
M 4 HOH   1   401 795 HOH   HOH C . 
M 4 HOH   2   402 733 HOH   HOH C . 
M 4 HOH   3   403 791 HOH   HOH C . 
M 4 HOH   4   404 801 HOH   HOH C . 
M 4 HOH   5   405 831 HOH   HOH C . 
M 4 HOH   6   406 855 HOH   HOH C . 
M 4 HOH   7   407 490 HOH   HOH C . 
M 4 HOH   8   408 237 HOH   HOH C . 
M 4 HOH   9   409 717 HOH   HOH C . 
M 4 HOH   10  410 765 HOH   HOH C . 
M 4 HOH   11  411 474 HOH   HOH C . 
M 4 HOH   12  412 375 HOH   HOH C . 
M 4 HOH   13  413 321 HOH   HOH C . 
M 4 HOH   14  414 854 HOH   HOH C . 
M 4 HOH   15  415 580 HOH   HOH C . 
M 4 HOH   16  416 100 HOH   HOH C . 
M 4 HOH   17  417 828 HOH   HOH C . 
M 4 HOH   18  418 740 HOH   HOH C . 
M 4 HOH   19  419 453 HOH   HOH C . 
M 4 HOH   20  420 315 HOH   HOH C . 
M 4 HOH   21  421 21  HOH   HOH C . 
M 4 HOH   22  422 307 HOH   HOH C . 
M 4 HOH   23  423 236 HOH   HOH C . 
M 4 HOH   24  424 372 HOH   HOH C . 
M 4 HOH   25  425 213 HOH   HOH C . 
M 4 HOH   26  426 312 HOH   HOH C . 
M 4 HOH   27  427 69  HOH   HOH C . 
M 4 HOH   28  428 429 HOH   HOH C . 
M 4 HOH   29  429 158 HOH   HOH C . 
M 4 HOH   30  430 699 HOH   HOH C . 
M 4 HOH   31  431 150 HOH   HOH C . 
M 4 HOH   32  432 573 HOH   HOH C . 
M 4 HOH   33  433 405 HOH   HOH C . 
M 4 HOH   34  434 264 HOH   HOH C . 
M 4 HOH   35  435 275 HOH   HOH C . 
M 4 HOH   36  436 224 HOH   HOH C . 
M 4 HOH   37  437 285 HOH   HOH C . 
M 4 HOH   38  438 6   HOH   HOH C . 
M 4 HOH   39  439 347 HOH   HOH C . 
M 4 HOH   40  440 407 HOH   HOH C . 
M 4 HOH   41  441 76  HOH   HOH C . 
M 4 HOH   42  442 255 HOH   HOH C . 
M 4 HOH   43  443 89  HOH   HOH C . 
M 4 HOH   44  444 319 HOH   HOH C . 
M 4 HOH   45  445 534 HOH   HOH C . 
M 4 HOH   46  446 271 HOH   HOH C . 
M 4 HOH   47  447 454 HOH   HOH C . 
M 4 HOH   48  448 83  HOH   HOH C . 
M 4 HOH   49  449 309 HOH   HOH C . 
M 4 HOH   50  450 632 HOH   HOH C . 
M 4 HOH   51  451 122 HOH   HOH C . 
M 4 HOH   52  452 144 HOH   HOH C . 
M 4 HOH   53  453 526 HOH   HOH C . 
M 4 HOH   54  454 438 HOH   HOH C . 
M 4 HOH   55  455 262 HOH   HOH C . 
M 4 HOH   56  456 109 HOH   HOH C . 
M 4 HOH   57  457 523 HOH   HOH C . 
M 4 HOH   58  458 596 HOH   HOH C . 
M 4 HOH   59  459 330 HOH   HOH C . 
M 4 HOH   60  460 118 HOH   HOH C . 
M 4 HOH   61  461 389 HOH   HOH C . 
M 4 HOH   62  462 130 HOH   HOH C . 
M 4 HOH   63  463 58  HOH   HOH C . 
M 4 HOH   64  464 231 HOH   HOH C . 
M 4 HOH   65  465 814 HOH   HOH C . 
M 4 HOH   66  466 238 HOH   HOH C . 
M 4 HOH   67  467 203 HOH   HOH C . 
M 4 HOH   68  468 126 HOH   HOH C . 
M 4 HOH   69  469 756 HOH   HOH C . 
M 4 HOH   70  470 218 HOH   HOH C . 
M 4 HOH   71  471 59  HOH   HOH C . 
M 4 HOH   72  472 288 HOH   HOH C . 
M 4 HOH   73  473 49  HOH   HOH C . 
M 4 HOH   74  474 60  HOH   HOH C . 
M 4 HOH   75  475 282 HOH   HOH C . 
M 4 HOH   76  476 403 HOH   HOH C . 
M 4 HOH   77  477 162 HOH   HOH C . 
M 4 HOH   78  478 837 HOH   HOH C . 
M 4 HOH   79  479 222 HOH   HOH C . 
M 4 HOH   80  480 243 HOH   HOH C . 
M 4 HOH   81  481 272 HOH   HOH C . 
M 4 HOH   82  482 279 HOH   HOH C . 
M 4 HOH   83  483 234 HOH   HOH C . 
M 4 HOH   84  484 639 HOH   HOH C . 
M 4 HOH   85  485 270 HOH   HOH C . 
M 4 HOH   86  486 735 HOH   HOH C . 
M 4 HOH   87  487 609 HOH   HOH C . 
M 4 HOH   88  488 90  HOH   HOH C . 
M 4 HOH   89  489 17  HOH   HOH C . 
M 4 HOH   90  490 143 HOH   HOH C . 
M 4 HOH   91  491 364 HOH   HOH C . 
M 4 HOH   92  492 358 HOH   HOH C . 
M 4 HOH   93  493 840 HOH   HOH C . 
M 4 HOH   94  494 244 HOH   HOH C . 
M 4 HOH   95  495 852 HOH   HOH C . 
M 4 HOH   96  496 575 HOH   HOH C . 
M 4 HOH   97  497 655 HOH   HOH C . 
M 4 HOH   98  498 371 HOH   HOH C . 
M 4 HOH   99  499 382 HOH   HOH C . 
M 4 HOH   100 500 823 HOH   HOH C . 
M 4 HOH   101 501 186 HOH   HOH C . 
M 4 HOH   102 502 139 HOH   HOH C . 
M 4 HOH   103 503 530 HOH   HOH C . 
M 4 HOH   104 504 116 HOH   HOH C . 
M 4 HOH   105 505 93  HOH   HOH C . 
M 4 HOH   106 506 197 HOH   HOH C . 
M 4 HOH   107 507 164 HOH   HOH C . 
M 4 HOH   108 508 81  HOH   HOH C . 
M 4 HOH   109 509 327 HOH   HOH C . 
M 4 HOH   110 510 378 HOH   HOH C . 
M 4 HOH   111 511 268 HOH   HOH C . 
M 4 HOH   112 512 563 HOH   HOH C . 
M 4 HOH   113 513 29  HOH   HOH C . 
M 4 HOH   114 514 221 HOH   HOH C . 
M 4 HOH   115 515 53  HOH   HOH C . 
M 4 HOH   116 516 240 HOH   HOH C . 
M 4 HOH   117 517 634 HOH   HOH C . 
M 4 HOH   118 518 318 HOH   HOH C . 
M 4 HOH   119 519 287 HOH   HOH C . 
M 4 HOH   120 520 20  HOH   HOH C . 
M 4 HOH   121 521 742 HOH   HOH C . 
M 4 HOH   122 522 274 HOH   HOH C . 
M 4 HOH   123 523 636 HOH   HOH C . 
M 4 HOH   124 524 3   HOH   HOH C . 
M 4 HOH   125 525 615 HOH   HOH C . 
M 4 HOH   126 526 841 HOH   HOH C . 
M 4 HOH   127 527 328 HOH   HOH C . 
M 4 HOH   128 528 397 HOH   HOH C . 
M 4 HOH   129 529 521 HOH   HOH C . 
M 4 HOH   130 530 25  HOH   HOH C . 
M 4 HOH   131 531 781 HOH   HOH C . 
M 4 HOH   132 532 825 HOH   HOH C . 
M 4 HOH   133 533 7   HOH   HOH C . 
M 4 HOH   134 534 201 HOH   HOH C . 
M 4 HOH   135 535 539 HOH   HOH C . 
M 4 HOH   136 536 176 HOH   HOH C . 
M 4 HOH   137 537 527 HOH   HOH C . 
M 4 HOH   138 538 430 HOH   HOH C . 
M 4 HOH   139 539 151 HOH   HOH C . 
M 4 HOH   140 540 493 HOH   HOH C . 
M 4 HOH   141 541 266 HOH   HOH C . 
M 4 HOH   142 542 722 HOH   HOH C . 
M 4 HOH   143 543 286 HOH   HOH C . 
M 4 HOH   144 544 85  HOH   HOH C . 
M 4 HOH   145 545 489 HOH   HOH C . 
M 4 HOH   146 546 219 HOH   HOH C . 
M 4 HOH   147 547 506 HOH   HOH C . 
M 4 HOH   148 548 584 HOH   HOH C . 
M 4 HOH   149 549 513 HOH   HOH C . 
M 4 HOH   150 550 103 HOH   HOH C . 
M 4 HOH   151 551 131 HOH   HOH C . 
M 4 HOH   152 552 555 HOH   HOH C . 
M 4 HOH   153 553 627 HOH   HOH C . 
M 4 HOH   154 554 88  HOH   HOH C . 
M 4 HOH   155 555 416 HOH   HOH C . 
M 4 HOH   156 556 514 HOH   HOH C . 
M 4 HOH   157 557 14  HOH   HOH C . 
M 4 HOH   158 558 267 HOH   HOH C . 
M 4 HOH   159 559 440 HOH   HOH C . 
M 4 HOH   160 560 316 HOH   HOH C . 
M 4 HOH   161 561 549 HOH   HOH C . 
M 4 HOH   162 562 445 HOH   HOH C . 
M 4 HOH   163 563 497 HOH   HOH C . 
M 4 HOH   164 564 402 HOH   HOH C . 
M 4 HOH   165 565 786 HOH   HOH C . 
M 4 HOH   166 566 692 HOH   HOH C . 
M 4 HOH   167 567 460 HOH   HOH C . 
M 4 HOH   168 568 737 HOH   HOH C . 
M 4 HOH   169 569 629 HOH   HOH C . 
M 4 HOH   170 570 278 HOH   HOH C . 
M 4 HOH   171 571 332 HOH   HOH C . 
M 4 HOH   172 572 391 HOH   HOH C . 
M 4 HOH   173 573 797 HOH   HOH C . 
M 4 HOH   174 574 834 HOH   HOH C . 
M 4 HOH   175 575 681 HOH   HOH C . 
M 4 HOH   176 576 600 HOH   HOH C . 
M 4 HOH   177 577 509 HOH   HOH C . 
M 4 HOH   178 578 734 HOH   HOH C . 
M 4 HOH   179 579 793 HOH   HOH C . 
M 4 HOH   180 580 602 HOH   HOH C . 
M 4 HOH   181 581 613 HOH   HOH C . 
M 4 HOH   182 582 715 HOH   HOH C . 
M 4 HOH   183 583 716 HOH   HOH C . 
M 4 HOH   184 584 308 HOH   HOH C . 
M 4 HOH   185 585 836 HOH   HOH C . 
M 4 HOH   186 586 714 HOH   HOH C . 
M 4 HOH   187 587 788 HOH   HOH C . 
M 4 HOH   188 588 703 HOH   HOH C . 
M 4 HOH   189 589 646 HOH   HOH C . 
M 4 HOH   190 590 535 HOH   HOH C . 
M 4 HOH   191 591 718 HOH   HOH C . 
M 4 HOH   192 592 277 HOH   HOH C . 
M 4 HOH   193 593 764 HOH   HOH C . 
M 4 HOH   194 594 826 HOH   HOH C . 
M 4 HOH   195 595 723 HOH   HOH C . 
M 4 HOH   196 596 466 HOH   HOH C . 
M 4 HOH   197 597 400 HOH   HOH C . 
M 4 HOH   198 598 415 HOH   HOH C . 
M 4 HOH   199 599 796 HOH   HOH C . 
M 4 HOH   200 600 690 HOH   HOH C . 
M 4 HOH   201 601 433 HOH   HOH C . 
M 4 HOH   202 602 671 HOH   HOH C . 
M 4 HOH   203 603 817 HOH   HOH C . 
M 4 HOH   204 604 819 HOH   HOH C . 
M 4 HOH   205 605 516 HOH   HOH C . 
M 4 HOH   206 606 670 HOH   HOH C . 
M 4 HOH   207 607 685 HOH   HOH C . 
M 4 HOH   208 608 754 HOH   HOH C . 
M 4 HOH   209 609 752 HOH   HOH C . 
M 4 HOH   210 610 310 HOH   HOH C . 
M 4 HOH   211 611 818 HOH   HOH C . 
M 4 HOH   212 612 487 HOH   HOH C . 
M 4 HOH   213 613 469 HOH   HOH C . 
M 4 HOH   214 614 751 HOH   HOH C . 
M 4 HOH   215 615 827 HOH   HOH C . 
M 4 HOH   216 616 738 HOH   HOH C . 
M 4 HOH   217 617 578 HOH   HOH C . 
M 4 HOH   218 618 785 HOH   HOH C . 
M 4 HOH   219 619 428 HOH   HOH C . 
M 4 HOH   220 620 431 HOH   HOH C . 
M 4 HOH   221 621 862 HOH   HOH C . 
M 4 HOH   222 622 669 HOH   HOH C . 
M 4 HOH   223 623 858 HOH   HOH C . 
M 4 HOH   224 624 207 HOH   HOH C . 
M 4 HOH   225 625 706 HOH   HOH C . 
M 4 HOH   226 626 766 HOH   HOH C . 
M 4 HOH   227 627 399 HOH   HOH C . 
M 4 HOH   228 628 708 HOH   HOH C . 
M 4 HOH   229 629 753 HOH   HOH C . 
M 4 HOH   230 630 683 HOH   HOH C . 
M 4 HOH   231 631 853 HOH   HOH C . 
N 4 HOH   1   401 246 HOH   HOH D . 
N 4 HOH   2   402 794 HOH   HOH D . 
N 4 HOH   3   403 296 HOH   HOH D . 
N 4 HOH   4   404 648 HOH   HOH D . 
N 4 HOH   5   405 159 HOH   HOH D . 
N 4 HOH   6   406 361 HOH   HOH D . 
N 4 HOH   7   407 37  HOH   HOH D . 
N 4 HOH   8   408 145 HOH   HOH D . 
N 4 HOH   9   409 23  HOH   HOH D . 
N 4 HOH   10  410 806 HOH   HOH D . 
N 4 HOH   11  411 79  HOH   HOH D . 
N 4 HOH   12  412 617 HOH   HOH D . 
N 4 HOH   13  413 507 HOH   HOH D . 
N 4 HOH   14  414 769 HOH   HOH D . 
N 4 HOH   15  415 783 HOH   HOH D . 
N 4 HOH   16  416 294 HOH   HOH D . 
N 4 HOH   17  417 423 HOH   HOH D . 
N 4 HOH   18  418 531 HOH   HOH D . 
N 4 HOH   19  419 117 HOH   HOH D . 
N 4 HOH   20  420 835 HOH   HOH D . 
N 4 HOH   21  421 297 HOH   HOH D . 
N 4 HOH   22  422 113 HOH   HOH D . 
N 4 HOH   23  423 62  HOH   HOH D . 
N 4 HOH   24  424 337 HOH   HOH D . 
N 4 HOH   25  425 775 HOH   HOH D . 
N 4 HOH   26  426 61  HOH   HOH D . 
N 4 HOH   27  427 36  HOH   HOH D . 
N 4 HOH   28  428 658 HOH   HOH D . 
N 4 HOH   29  429 379 HOH   HOH D . 
N 4 HOH   30  430 605 HOH   HOH D . 
N 4 HOH   31  431 570 HOH   HOH D . 
N 4 HOH   32  432 190 HOH   HOH D . 
N 4 HOH   33  433 181 HOH   HOH D . 
N 4 HOH   34  434 295 HOH   HOH D . 
N 4 HOH   35  435 787 HOH   HOH D . 
N 4 HOH   36  436 66  HOH   HOH D . 
N 4 HOH   37  437 269 HOH   HOH D . 
N 4 HOH   38  438 55  HOH   HOH D . 
N 4 HOH   39  439 458 HOH   HOH D . 
N 4 HOH   40  440 618 HOH   HOH D . 
N 4 HOH   41  441 70  HOH   HOH D . 
N 4 HOH   42  442 187 HOH   HOH D . 
N 4 HOH   43  443 362 HOH   HOH D . 
N 4 HOH   44  444 209 HOH   HOH D . 
N 4 HOH   45  445 138 HOH   HOH D . 
N 4 HOH   46  446 170 HOH   HOH D . 
N 4 HOH   47  447 39  HOH   HOH D . 
N 4 HOH   48  448 265 HOH   HOH D . 
N 4 HOH   49  449 12  HOH   HOH D . 
N 4 HOH   50  450 208 HOH   HOH D . 
N 4 HOH   51  451 365 HOH   HOH D . 
N 4 HOH   52  452 558 HOH   HOH D . 
N 4 HOH   53  453 551 HOH   HOH D . 
N 4 HOH   54  454 160 HOH   HOH D . 
N 4 HOH   55  455 477 HOH   HOH D . 
N 4 HOH   56  456 63  HOH   HOH D . 
N 4 HOH   57  457 625 HOH   HOH D . 
N 4 HOH   58  458 1   HOH   HOH D . 
N 4 HOH   59  459 173 HOH   HOH D . 
N 4 HOH   60  460 586 HOH   HOH D . 
N 4 HOH   61  461 64  HOH   HOH D . 
N 4 HOH   62  462 480 HOH   HOH D . 
N 4 HOH   63  463 77  HOH   HOH D . 
N 4 HOH   64  464 326 HOH   HOH D . 
N 4 HOH   65  465 50  HOH   HOH D . 
N 4 HOH   66  466 409 HOH   HOH D . 
N 4 HOH   67  467 10  HOH   HOH D . 
N 4 HOH   68  468 114 HOH   HOH D . 
N 4 HOH   69  469 260 HOH   HOH D . 
N 4 HOH   70  470 502 HOH   HOH D . 
N 4 HOH   71  471 412 HOH   HOH D . 
N 4 HOH   72  472 759 HOH   HOH D . 
N 4 HOH   73  473 276 HOH   HOH D . 
N 4 HOH   74  474 376 HOH   HOH D . 
N 4 HOH   75  475 161 HOH   HOH D . 
N 4 HOH   76  476 419 HOH   HOH D . 
N 4 HOH   77  477 18  HOH   HOH D . 
N 4 HOH   78  478 261 HOH   HOH D . 
N 4 HOH   79  479 543 HOH   HOH D . 
N 4 HOH   80  480 437 HOH   HOH D . 
N 4 HOH   81  481 631 HOH   HOH D . 
N 4 HOH   82  482 92  HOH   HOH D . 
N 4 HOH   83  483 357 HOH   HOH D . 
N 4 HOH   84  484 370 HOH   HOH D . 
N 4 HOH   85  485 204 HOH   HOH D . 
N 4 HOH   86  486 450 HOH   HOH D . 
N 4 HOH   87  487 525 HOH   HOH D . 
N 4 HOH   88  488 601 HOH   HOH D . 
N 4 HOH   89  489 128 HOH   HOH D . 
N 4 HOH   90  490 182 HOH   HOH D . 
N 4 HOH   91  491 9   HOH   HOH D . 
N 4 HOH   92  492 495 HOH   HOH D . 
N 4 HOH   93  493 500 HOH   HOH D . 
N 4 HOH   94  494 616 HOH   HOH D . 
N 4 HOH   95  495 338 HOH   HOH D . 
N 4 HOH   96  496 479 HOH   HOH D . 
N 4 HOH   97  497 306 HOH   HOH D . 
N 4 HOH   98  498 258 HOH   HOH D . 
N 4 HOH   99  499 427 HOH   HOH D . 
N 4 HOH   100 500 395 HOH   HOH D . 
N 4 HOH   101 501 589 HOH   HOH D . 
N 4 HOH   102 502 26  HOH   HOH D . 
N 4 HOH   103 503 196 HOH   HOH D . 
N 4 HOH   104 504 42  HOH   HOH D . 
N 4 HOH   105 505 80  HOH   HOH D . 
N 4 HOH   106 506 183 HOH   HOH D . 
N 4 HOH   107 507 406 HOH   HOH D . 
N 4 HOH   108 508 171 HOH   HOH D . 
N 4 HOH   109 509 48  HOH   HOH D . 
N 4 HOH   110 510 239 HOH   HOH D . 
N 4 HOH   111 511 508 HOH   HOH D . 
N 4 HOH   112 512 322 HOH   HOH D . 
N 4 HOH   113 513 250 HOH   HOH D . 
N 4 HOH   114 514 492 HOH   HOH D . 
N 4 HOH   115 515 537 HOH   HOH D . 
N 4 HOH   116 516 74  HOH   HOH D . 
N 4 HOH   117 517 248 HOH   HOH D . 
N 4 HOH   118 518 56  HOH   HOH D . 
N 4 HOH   119 519 263 HOH   HOH D . 
N 4 HOH   120 520 112 HOH   HOH D . 
N 4 HOH   121 521 562 HOH   HOH D . 
N 4 HOH   122 522 392 HOH   HOH D . 
N 4 HOH   123 523 324 HOH   HOH D . 
N 4 HOH   124 524 199 HOH   HOH D . 
N 4 HOH   125 525 380 HOH   HOH D . 
N 4 HOH   126 526 94  HOH   HOH D . 
N 4 HOH   127 527 483 HOH   HOH D . 
N 4 HOH   128 528 473 HOH   HOH D . 
N 4 HOH   129 529 257 HOH   HOH D . 
N 4 HOH   130 530 833 HOH   HOH D . 
N 4 HOH   131 531 225 HOH   HOH D . 
N 4 HOH   132 532 468 HOH   HOH D . 
N 4 HOH   133 533 565 HOH   HOH D . 
N 4 HOH   134 534 566 HOH   HOH D . 
N 4 HOH   135 535 452 HOH   HOH D . 
N 4 HOH   136 536 637 HOH   HOH D . 
N 4 HOH   137 537 22  HOH   HOH D . 
N 4 HOH   138 538 27  HOH   HOH D . 
N 4 HOH   139 539 129 HOH   HOH D . 
N 4 HOH   140 540 444 HOH   HOH D . 
N 4 HOH   141 541 824 HOH   HOH D . 
N 4 HOH   142 542 482 HOH   HOH D . 
N 4 HOH   143 543 800 HOH   HOH D . 
N 4 HOH   144 544 547 HOH   HOH D . 
N 4 HOH   145 545 82  HOH   HOH D . 
N 4 HOH   146 546 850 HOH   HOH D . 
N 4 HOH   147 547 857 HOH   HOH D . 
N 4 HOH   148 548 772 HOH   HOH D . 
N 4 HOH   149 549 792 HOH   HOH D . 
N 4 HOH   150 550 679 HOH   HOH D . 
N 4 HOH   151 551 432 HOH   HOH D . 
N 4 HOH   152 552 496 HOH   HOH D . 
N 4 HOH   153 553 561 HOH   HOH D . 
N 4 HOH   154 554 859 HOH   HOH D . 
N 4 HOH   155 555 677 HOH   HOH D . 
N 4 HOH   156 556 414 HOH   HOH D . 
N 4 HOH   157 557 680 HOH   HOH D . 
N 4 HOH   158 558 491 HOH   HOH D . 
N 4 HOH   159 559 674 HOH   HOH D . 
N 4 HOH   160 560 755 HOH   HOH D . 
N 4 HOH   161 561 217 HOH   HOH D . 
N 4 HOH   162 562 809 HOH   HOH D . 
N 4 HOH   163 563 293 HOH   HOH D . 
N 4 HOH   164 564 811 HOH   HOH D . 
N 4 HOH   165 565 457 HOH   HOH D . 
N 4 HOH   166 566 448 HOH   HOH D . 
N 4 HOH   167 567 346 HOH   HOH D . 
N 4 HOH   168 568 666 HOH   HOH D . 
N 4 HOH   169 569 704 HOH   HOH D . 
N 4 HOH   170 570 408 HOH   HOH D . 
N 4 HOH   171 571 582 HOH   HOH D . 
N 4 HOH   172 572 104 HOH   HOH D . 
N 4 HOH   173 573 475 HOH   HOH D . 
N 4 HOH   174 574 374 HOH   HOH D . 
N 4 HOH   175 575 832 HOH   HOH D . 
N 4 HOH   176 576 608 HOH   HOH D . 
N 4 HOH   177 577 678 HOH   HOH D . 
N 4 HOH   178 578 410 HOH   HOH D . 
N 4 HOH   179 579 724 HOH   HOH D . 
N 4 HOH   180 580 689 HOH   HOH D . 
N 4 HOH   181 581 725 HOH   HOH D . 
N 4 HOH   182 582 443 HOH   HOH D . 
N 4 HOH   183 583 214 HOH   HOH D . 
N 4 HOH   184 584 709 HOH   HOH D . 
N 4 HOH   185 585 777 HOH   HOH D . 
N 4 HOH   186 586 557 HOH   HOH D . 
N 4 HOH   187 587 292 HOH   HOH D . 
N 4 HOH   188 588 661 HOH   HOH D . 
N 4 HOH   189 589 726 HOH   HOH D . 
N 4 HOH   190 590 665 HOH   HOH D . 
O 4 HOH   1   401 597 HOH   HOH A . 
O 4 HOH   2   402 847 HOH   HOH A . 
O 4 HOH   3   403 41  HOH   HOH A . 
O 4 HOH   4   404 802 HOH   HOH A . 
O 4 HOH   5   405 517 HOH   HOH A . 
O 4 HOH   6   406 367 HOH   HOH A . 
O 4 HOH   7   407 510 HOH   HOH A . 
O 4 HOH   8   408 417 HOH   HOH A . 
O 4 HOH   9   409 728 HOH   HOH A . 
O 4 HOH   10  410 401 HOH   HOH A . 
O 4 HOH   11  411 333 HOH   HOH A . 
O 4 HOH   12  412 167 HOH   HOH A . 
O 4 HOH   13  413 568 HOH   HOH A . 
O 4 HOH   14  414 228 HOH   HOH A . 
O 4 HOH   15  415 595 HOH   HOH A . 
O 4 HOH   16  416 340 HOH   HOH A . 
O 4 HOH   17  417 576 HOH   HOH A . 
O 4 HOH   18  418 470 HOH   HOH A . 
O 4 HOH   19  419 354 HOH   HOH A . 
O 4 HOH   20  420 425 HOH   HOH A . 
O 4 HOH   21  421 729 HOH   HOH A . 
O 4 HOH   22  422 538 HOH   HOH A . 
O 4 HOH   23  423 189 HOH   HOH A . 
O 4 HOH   24  424 553 HOH   HOH A . 
O 4 HOH   25  425 105 HOH   HOH A . 
O 4 HOH   26  426 564 HOH   HOH A . 
O 4 HOH   27  427 567 HOH   HOH A . 
O 4 HOH   28  428 386 HOH   HOH A . 
O 4 HOH   29  429 111 HOH   HOH A . 
O 4 HOH   30  430 640 HOH   HOH A . 
O 4 HOH   31  431 249 HOH   HOH A . 
O 4 HOH   32  432 125 HOH   HOH A . 
O 4 HOH   33  433 334 HOH   HOH A . 
O 4 HOH   34  434 168 HOH   HOH A . 
O 4 HOH   35  435 119 HOH   HOH A . 
O 4 HOH   36  436 545 HOH   HOH A . 
O 4 HOH   37  437 65  HOH   HOH A . 
O 4 HOH   38  438 15  HOH   HOH A . 
O 4 HOH   39  439 256 HOH   HOH A . 
O 4 HOH   40  440 304 HOH   HOH A . 
O 4 HOH   41  441 254 HOH   HOH A . 
O 4 HOH   42  442 33  HOH   HOH A . 
O 4 HOH   43  443 215 HOH   HOH A . 
O 4 HOH   44  444 233 HOH   HOH A . 
O 4 HOH   45  445 515 HOH   HOH A . 
O 4 HOH   46  446 345 HOH   HOH A . 
O 4 HOH   47  447 259 HOH   HOH A . 
O 4 HOH   48  448 654 HOH   HOH A . 
O 4 HOH   49  449 245 HOH   HOH A . 
O 4 HOH   50  450 560 HOH   HOH A . 
O 4 HOH   51  451 421 HOH   HOH A . 
O 4 HOH   52  452 5   HOH   HOH A . 
O 4 HOH   53  453 606 HOH   HOH A . 
O 4 HOH   54  454 242 HOH   HOH A . 
O 4 HOH   55  455 121 HOH   HOH A . 
O 4 HOH   56  456 169 HOH   HOH A . 
O 4 HOH   57  457 504 HOH   HOH A . 
O 4 HOH   58  458 494 HOH   HOH A . 
O 4 HOH   59  459 413 HOH   HOH A . 
O 4 HOH   60  460 463 HOH   HOH A . 
O 4 HOH   61  461 518 HOH   HOH A . 
O 4 HOH   62  462 758 HOH   HOH A . 
O 4 HOH   63  463 335 HOH   HOH A . 
O 4 HOH   64  464 52  HOH   HOH A . 
O 4 HOH   65  465 544 HOH   HOH A . 
O 4 HOH   66  466 465 HOH   HOH A . 
O 4 HOH   67  467 336 HOH   HOH A . 
O 4 HOH   68  468 848 HOH   HOH A . 
O 4 HOH   69  469 147 HOH   HOH A . 
O 4 HOH   70  470 624 HOH   HOH A . 
O 4 HOH   71  471 73  HOH   HOH A . 
O 4 HOH   72  472 556 HOH   HOH A . 
O 4 HOH   73  473 657 HOH   HOH A . 
O 4 HOH   74  474 782 HOH   HOH A . 
O 4 HOH   75  475 583 HOH   HOH A . 
O 4 HOH   76  476 87  HOH   HOH A . 
O 4 HOH   77  477 38  HOH   HOH A . 
O 4 HOH   78  478 488 HOH   HOH A . 
O 4 HOH   79  479 594 HOH   HOH A . 
O 4 HOH   80  480 235 HOH   HOH A . 
O 4 HOH   81  481 323 HOH   HOH A . 
O 4 HOH   82  482 424 HOH   HOH A . 
O 4 HOH   83  483 554 HOH   HOH A . 
O 4 HOH   84  484 317 HOH   HOH A . 
O 4 HOH   85  485 348 HOH   HOH A . 
O 4 HOH   86  486 24  HOH   HOH A . 
O 4 HOH   87  487 359 HOH   HOH A . 
O 4 HOH   88  488 863 HOH   HOH A . 
O 4 HOH   89  489 320 HOH   HOH A . 
O 4 HOH   90  490 115 HOH   HOH A . 
O 4 HOH   91  491 486 HOH   HOH A . 
O 4 HOH   92  492 748 HOH   HOH A . 
O 4 HOH   93  493 227 HOH   HOH A . 
O 4 HOH   94  494 384 HOH   HOH A . 
O 4 HOH   95  495 101 HOH   HOH A . 
O 4 HOH   96  496 579 HOH   HOH A . 
O 4 HOH   97  497 356 HOH   HOH A . 
O 4 HOH   98  498 216 HOH   HOH A . 
O 4 HOH   99  499 369 HOH   HOH A . 
O 4 HOH   100 500 198 HOH   HOH A . 
O 4 HOH   101 501 8   HOH   HOH A . 
O 4 HOH   102 502 188 HOH   HOH A . 
O 4 HOH   103 503 108 HOH   HOH A . 
O 4 HOH   104 504 550 HOH   HOH A . 
O 4 HOH   105 505 195 HOH   HOH A . 
O 4 HOH   106 506 750 HOH   HOH A . 
O 4 HOH   107 507 611 HOH   HOH A . 
O 4 HOH   108 508 607 HOH   HOH A . 
O 4 HOH   109 509 849 HOH   HOH A . 
O 4 HOH   110 510 501 HOH   HOH A . 
O 4 HOH   111 511 123 HOH   HOH A . 
O 4 HOH   112 512 13  HOH   HOH A . 
O 4 HOH   113 513 455 HOH   HOH A . 
O 4 HOH   114 514 75  HOH   HOH A . 
O 4 HOH   115 515 599 HOH   HOH A . 
O 4 HOH   116 516 461 HOH   HOH A . 
O 4 HOH   117 517 462 HOH   HOH A . 
O 4 HOH   118 518 591 HOH   HOH A . 
O 4 HOH   119 519 136 HOH   HOH A . 
O 4 HOH   120 520 11  HOH   HOH A . 
O 4 HOH   121 521 247 HOH   HOH A . 
O 4 HOH   122 522 71  HOH   HOH A . 
O 4 HOH   123 523 32  HOH   HOH A . 
O 4 HOH   124 524 587 HOH   HOH A . 
O 4 HOH   125 525 178 HOH   HOH A . 
O 4 HOH   126 526 120 HOH   HOH A . 
O 4 HOH   127 527 571 HOH   HOH A . 
O 4 HOH   128 528 229 HOH   HOH A . 
O 4 HOH   129 529 34  HOH   HOH A . 
O 4 HOH   130 530 185 HOH   HOH A . 
O 4 HOH   131 531 541 HOH   HOH A . 
O 4 HOH   132 532 442 HOH   HOH A . 
O 4 HOH   133 533 686 HOH   HOH A . 
O 4 HOH   134 534 712 HOH   HOH A . 
O 4 HOH   135 535 68  HOH   HOH A . 
O 4 HOH   136 536 803 HOH   HOH A . 
O 4 HOH   137 537 385 HOH   HOH A . 
O 4 HOH   138 538 96  HOH   HOH A . 
O 4 HOH   139 539 548 HOH   HOH A . 
O 4 HOH   140 540 839 HOH   HOH A . 
O 4 HOH   141 541 768 HOH   HOH A . 
O 4 HOH   142 542 253 HOH   HOH A . 
O 4 HOH   143 543 352 HOH   HOH A . 
O 4 HOH   144 544 426 HOH   HOH A . 
O 4 HOH   145 545 35  HOH   HOH A . 
O 4 HOH   146 546 581 HOH   HOH A . 
O 4 HOH   147 547 351 HOH   HOH A . 
O 4 HOH   148 548 838 HOH   HOH A . 
O 4 HOH   149 549 614 HOH   HOH A . 
O 4 HOH   150 550 821 HOH   HOH A . 
O 4 HOH   151 551 770 HOH   HOH A . 
O 4 HOH   152 552 40  HOH   HOH A . 
O 4 HOH   153 553 449 HOH   HOH A . 
O 4 HOH   154 554 630 HOH   HOH A . 
O 4 HOH   155 555 701 HOH   HOH A . 
O 4 HOH   156 556 780 HOH   HOH A . 
O 4 HOH   157 557 45  HOH   HOH A . 
O 4 HOH   158 558 730 HOH   HOH A . 
O 4 HOH   159 559 698 HOH   HOH A . 
O 4 HOH   160 560 390 HOH   HOH A . 
O 4 HOH   161 561 663 HOH   HOH A . 
O 4 HOH   162 562 585 HOH   HOH A . 
O 4 HOH   163 563 789 HOH   HOH A . 
O 4 HOH   164 564 373 HOH   HOH A . 
O 4 HOH   165 565 592 HOH   HOH A . 
O 4 HOH   166 566 727 HOH   HOH A . 
O 4 HOH   167 567 675 HOH   HOH A . 
O 4 HOH   168 568 446 HOH   HOH A . 
O 4 HOH   169 569 731 HOH   HOH A . 
O 4 HOH   170 570 851 HOH   HOH A . 
O 4 HOH   171 571 843 HOH   HOH A . 
O 4 HOH   172 572 388 HOH   HOH A . 
O 4 HOH   173 573 749 HOH   HOH A . 
O 4 HOH   174 574 771 HOH   HOH A . 
O 4 HOH   175 575 673 HOH   HOH A . 
O 4 HOH   176 576 691 HOH   HOH A . 
O 4 HOH   177 577 844 HOH   HOH A . 
O 4 HOH   178 578 664 HOH   HOH A . 
O 4 HOH   179 579 697 HOH   HOH A . 
O 4 HOH   180 580 603 HOH   HOH A . 
O 4 HOH   181 581 684 HOH   HOH A . 
O 4 HOH   182 582 620 HOH   HOH A . 
O 4 HOH   183 583 773 HOH   HOH A . 
O 4 HOH   184 584 522 HOH   HOH A . 
O 4 HOH   185 585 360 HOH   HOH A . 
O 4 HOH   186 586 652 HOH   HOH A . 
O 4 HOH   187 587 845 HOH   HOH A . 
O 4 HOH   188 588 532 HOH   HOH A . 
O 4 HOH   189 589 305 HOH   HOH A . 
O 4 HOH   190 590 688 HOH   HOH A . 
O 4 HOH   191 591 291 HOH   HOH A . 
O 4 HOH   192 592 644 HOH   HOH A . 
O 4 HOH   193 593 798 HOH   HOH A . 
O 4 HOH   194 594 633 HOH   HOH A . 
O 4 HOH   195 595 626 HOH   HOH A . 
O 4 HOH   196 596 628 HOH   HOH A . 
O 4 HOH   197 597 498 HOH   HOH A . 
O 4 HOH   198 598 694 HOH   HOH A . 
O 4 HOH   199 599 342 HOH   HOH A . 
O 4 HOH   200 600 485 HOH   HOH A . 
O 4 HOH   201 601 707 HOH   HOH A . 
O 4 HOH   202 602 289 HOH   HOH A . 
O 4 HOH   203 603 822 HOH   HOH A . 
O 4 HOH   204 604 778 HOH   HOH A . 
O 4 HOH   205 605 301 HOH   HOH A . 
O 4 HOH   206 606 659 HOH   HOH A . 
O 4 HOH   207 607 528 HOH   HOH A . 
O 4 HOH   208 608 682 HOH   HOH A . 
O 4 HOH   209 609 846 HOH   HOH A . 
O 4 HOH   210 610 393 HOH   HOH A . 
O 4 HOH   211 611 820 HOH   HOH A . 
O 4 HOH   212 612 472 HOH   HOH A . 
O 4 HOH   213 613 799 HOH   HOH A . 
O 4 HOH   214 614 552 HOH   HOH A . 
O 4 HOH   215 615 667 HOH   HOH A . 
O 4 HOH   216 616 705 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC   ? ? ? 5.8.0238 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JN6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     90.878 
_cell.length_a_esd                 ? 
_cell.length_b                     101.613 
_cell.length_b_esd                 ? 
_cell.length_c                     111.155 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JN6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9JN6 
_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             2.73 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.03 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M ammonium acetate, 0.1 M Tris pH 8.0,  
1.0 M sodium citrate
;
_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 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-12-26 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.99987 
_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                        'NSRRC BEAMLINE TPS 05A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.99987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'TPS 05A' 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9JN6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               29.24 
_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                                     109356 
_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                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                7.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.95 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.82 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.59 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17022 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.950 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.6 
_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]                            0.97 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -1.68 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.70 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               24.659 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.970 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JN6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.72 
_refine.ls_d_res_low                             29.24 
_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                     107504 
_refine.ls_number_reflns_R_free                  1999 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.21 
_refine.ls_percent_reflns_R_free                 1.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18766 
_refine.ls_R_factor_R_free                       0.22196 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18702 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.101 
_refine.pdbx_overall_ESU_R_Free                  0.101 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.254 
_refine.overall_SU_ML                            0.072 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        29.24 
_refine_hist.number_atoms_solvent             851 
_refine_hist.number_atoms_total               7493 
_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        6443 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         199 
_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' ? 0.013  0.013  6846  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.017  6294  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.823  1.695  9398  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.561  1.604  14409 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.466  5.000  848   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 31.382 19.130 368   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.765 15.000 929   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 16.563 15.000 76    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.086  0.200  837   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  7924  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  1644  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 2.339  2.391  3413  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.339  2.392  3414  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.499  3.573  4254  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.500  3.573  4255  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 3.348  2.672  3433  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.348  2.672  3433  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.097  3.862  5145  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.890  29.140 8044  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.890  29.143 8045  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.72 
_refine_ls_shell.d_res_low                        1.761 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             138 
_refine_ls_shell.number_reflns_R_work             7434 
_refine_ls_shell.percent_reflns_obs               93.90 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.261 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   ? 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.308 
# 
_struct.entry_id                     9JN6 
_struct.title                        'Crystal structure of KtzT-C197A in complex with HEME and product' 
_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        9JN6 
_struct_keywords.text            'Heme-dependent piperazate synthase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A8CF72_KUTS7 
_struct_ref.pdbx_db_accession          A8CF72 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFVPGPYHAPEDRWLVDLVRGHPLAQLASNGAGGAAPHITHVPIIVDPELDGPVDRLVGITLWGHMNRANPHWAALGGAA
NVVATFAGPNAYVSPAVYRTAPAAPTWNFTSVQVRGELRKVESADDTLATVRATVAALESRFGAGWDMTGSLDYFRRILP
GVGAFRLRVAEADGMFKLSQEQQPAIRRRVRHSFGGCEATRAVAGLMDRLPTE
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9JN6 B 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
2 1 9JN6 C 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
3 1 9JN6 D 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
4 1 9JN6 A 6 ? 218 ? A8CF72 1 ? 213 ? 1 213 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JN6 ALA B 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  1  
1 9JN6 GLY B 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  2  
1 9JN6 ALA B 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  3  
1 9JN6 GLY B 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  4  
1 9JN6 ALA B 5   ? UNP A8CF72 ?   ?   'expression tag'      0   5  
1 9JN6 ALA B 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 6  
2 9JN6 ALA C 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  7  
2 9JN6 GLY C 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  8  
2 9JN6 ALA C 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  9  
2 9JN6 GLY C 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  10 
2 9JN6 ALA C 5   ? UNP A8CF72 ?   ?   'expression tag'      0   11 
2 9JN6 ALA C 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 12 
3 9JN6 ALA D 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  13 
3 9JN6 GLY D 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  14 
3 9JN6 ALA D 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  15 
3 9JN6 GLY D 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  16 
3 9JN6 ALA D 5   ? UNP A8CF72 ?   ?   'expression tag'      0   17 
3 9JN6 ALA D 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 18 
4 9JN6 ALA A 1   ? UNP A8CF72 ?   ?   'expression tag'      -4  19 
4 9JN6 GLY A 2   ? UNP A8CF72 ?   ?   'expression tag'      -3  20 
4 9JN6 ALA A 3   ? UNP A8CF72 ?   ?   'expression tag'      -2  21 
4 9JN6 GLY A 4   ? UNP A8CF72 ?   ?   'expression tag'      -1  22 
4 9JN6 ALA A 5   ? UNP A8CF72 ?   ?   'expression tag'      0   23 
4 9JN6 ALA A 202 ? UNP A8CF72 CYS 197 'engineered mutation' 197 24 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 7080  ? 
1 MORE         -75   ? 
1 'SSA (A^2)'  17650 ? 
2 'ABSA (A^2)' 7490  ? 
2 MORE         -79   ? 
2 'SSA (A^2)'  17760 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,L,M   
2 1 C,D,H,I,J,K,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 9   ? HIS A 13  ? PRO B 4   HIS B 8   5 ? 5  
HELX_P HELX_P2  AA2 ASP A 17  ? HIS A 27  ? ASP B 12  HIS B 22  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 75  ? GLY A 82  ? ASN B 70  GLY B 77  1 ? 8  
HELX_P HELX_P4  AA4 SER A 128 ? GLY A 148 ? SER B 123 GLY B 143 1 ? 21 
HELX_P HELX_P5  AA5 ASP A 152 ? GLY A 155 ? ASP B 147 GLY B 150 5 ? 4  
HELX_P HELX_P6  AA6 SER A 156 ? ILE A 163 ? SER B 151 ILE B 158 1 ? 8  
HELX_P HELX_P7  AA7 GLN A 188 ? GLY A 200 ? GLN B 183 GLY B 195 1 ? 13 
HELX_P HELX_P8  AA8 ALA A 202 ? ARG A 214 ? ALA B 197 ARG B 209 1 ? 13 
HELX_P HELX_P9  AA9 PRO B 9   ? HIS B 13  ? PRO C 4   HIS C 8   5 ? 5  
HELX_P HELX_P10 AB1 ASP B 17  ? HIS B 27  ? ASP C 12  HIS C 22  1 ? 11 
HELX_P HELX_P11 AB2 GLY B 36  ? ALA B 40  ? GLY C 31  ALA C 35  5 ? 5  
HELX_P HELX_P12 AB3 ASN B 75  ? GLY B 82  ? ASN C 70  GLY C 77  1 ? 8  
HELX_P HELX_P13 AB4 SER B 128 ? GLY B 148 ? SER C 123 GLY C 143 1 ? 21 
HELX_P HELX_P14 AB5 MET B 153 ? GLY B 155 ? MET C 148 GLY C 150 5 ? 3  
HELX_P HELX_P15 AB6 SER B 156 ? LEU B 164 ? SER C 151 LEU C 159 1 ? 9  
HELX_P HELX_P16 AB7 GLN B 188 ? GLY B 201 ? GLN C 183 GLY C 196 1 ? 14 
HELX_P HELX_P17 AB8 THR B 205 ? LEU B 215 ? THR C 200 LEU C 210 1 ? 11 
HELX_P HELX_P18 AB9 PRO C 9   ? HIS C 13  ? PRO D 4   HIS D 8   5 ? 5  
HELX_P HELX_P19 AC1 ASP C 17  ? HIS C 27  ? ASP D 12  HIS D 22  1 ? 11 
HELX_P HELX_P20 AC2 ASN C 75  ? GLY C 82  ? ASN D 70  GLY D 77  1 ? 8  
HELX_P HELX_P21 AC3 SER C 99  ? ARG C 104 ? SER D 94  ARG D 99  1 ? 6  
HELX_P HELX_P22 AC4 SER C 128 ? GLY C 148 ? SER D 123 GLY D 143 1 ? 21 
HELX_P HELX_P23 AC5 MET C 153 ? GLY C 155 ? MET D 148 GLY D 150 5 ? 3  
HELX_P HELX_P24 AC6 SER C 156 ? LEU C 164 ? SER D 151 LEU D 159 1 ? 9  
HELX_P HELX_P25 AC7 GLN C 188 ? GLY C 201 ? GLN D 183 GLY D 196 1 ? 14 
HELX_P HELX_P26 AC8 ALA C 202 ? ARG C 214 ? ALA D 197 ARG D 209 1 ? 13 
HELX_P HELX_P27 AC9 PRO D 9   ? HIS D 13  ? PRO A 4   HIS A 8   5 ? 5  
HELX_P HELX_P28 AD1 ASP D 17  ? HIS D 27  ? ASP A 12  HIS A 22  1 ? 11 
HELX_P HELX_P29 AD2 ASN D 75  ? LEU D 81  ? ASN A 70  LEU A 76  1 ? 7  
HELX_P HELX_P30 AD3 SER D 128 ? GLY D 148 ? SER A 123 GLY A 143 1 ? 21 
HELX_P HELX_P31 AD4 MET D 153 ? GLY D 155 ? MET A 148 GLY A 150 5 ? 3  
HELX_P HELX_P32 AD5 SER D 156 ? LEU D 164 ? SER A 151 LEU A 159 1 ? 9  
HELX_P HELX_P33 AD6 GLN D 188 ? GLY D 200 ? GLN A 183 GLY A 195 1 ? 13 
HELX_P HELX_P34 AD7 ALA D 202 ? ARG D 214 ? ALA A 197 ARG A 209 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS   70 NE2 ? ? ? 1_555 E HEM   . FE  ? ? B HIS   65  B HEM   301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc2 metalc ? ? F A1ECN .  NAG ? ? ? 1_555 G HEM   . FE  ? ? B A1ECN 302 C HEM   301 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc3 metalc ? ? B HIS   70 NE2 ? ? ? 1_555 G HEM   . FE  ? ? C HIS   65  C HEM   301 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc4 metalc ? ? C HIS   70 NE2 ? ? ? 1_555 H HEM   . FE  ? ? D HIS   65  D HEM   301 1_555 ? ? ? ? ? ? ? 2.099 ? ? 
metalc5 metalc ? ? H HEM   .  FE  ? ? ? 1_555 K A1ECN . NAG ? ? D HEM   301 A A1ECN 302 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc6 metalc ? ? I A1ECN .  NAG ? ? ? 1_555 J HEM   . FE  ? ? D A1ECN 302 A HEM   301 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc7 metalc ? ? D HIS   70 NE2 ? ? ? 1_555 J HEM   . FE  ? ? A HIS   65  A HEM   301 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS   70 ? B HIS   65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NA  ? E HEM   .  ? B HEM   301 ? 1_555 96.4  ? 
2  NE2 ? A HIS   70 ? B HIS   65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NB  ? E HEM   .  ? B HEM   301 ? 1_555 89.6  ? 
3  NA  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NB  ? E HEM   .  ? B HEM   301 ? 1_555 90.7  ? 
4  NE2 ? A HIS   70 ? B HIS   65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC  ? E HEM   .  ? B HEM   301 ? 1_555 96.0  ? 
5  NA  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC  ? E HEM   .  ? B HEM   301 ? 1_555 167.4 ? 
6  NB  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 NC  ? E HEM   .  ? B HEM   301 ? 1_555 87.2  ? 
7  NE2 ? A HIS   70 ? B HIS   65  ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND  ? E HEM   .  ? B HEM   301 ? 1_555 101.5 ? 
8  NA  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND  ? E HEM   .  ? B HEM   301 ? 1_555 89.4  ? 
9  NB  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND  ? E HEM   .  ? B HEM   301 ? 1_555 168.8 ? 
10 NC  ? E HEM   .  ? B HEM   301 ? 1_555 FE ? E HEM . ? B HEM 301 ? 1_555 ND  ? E HEM   .  ? B HEM   301 ? 1_555 90.2  ? 
11 NAG ? F A1ECN .  ? B A1ECN 302 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NA  ? G HEM   .  ? C HEM   301 ? 1_555 89.1  ? 
12 NAG ? F A1ECN .  ? B A1ECN 302 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NB  ? G HEM   .  ? C HEM   301 ? 1_555 86.1  ? 
13 NA  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NB  ? G HEM   .  ? C HEM   301 ? 1_555 90.2  ? 
14 NAG ? F A1ECN .  ? B A1ECN 302 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NC  ? G HEM   .  ? C HEM   301 ? 1_555 80.7  ? 
15 NA  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NC  ? G HEM   .  ? C HEM   301 ? 1_555 169.7 ? 
16 NB  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NC  ? G HEM   .  ? C HEM   301 ? 1_555 88.1  ? 
17 NAG ? F A1ECN .  ? B A1ECN 302 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 ND  ? G HEM   .  ? C HEM   301 ? 1_555 83.5  ? 
18 NA  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 ND  ? G HEM   .  ? C HEM   301 ? 1_555 89.5  ? 
19 NB  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 ND  ? G HEM   .  ? C HEM   301 ? 1_555 169.7 ? 
20 NC  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 ND  ? G HEM   .  ? C HEM   301 ? 1_555 90.4  ? 
21 NAG ? F A1ECN .  ? B A1ECN 302 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NE2 ? B HIS   70 ? C HIS   65  ? 1_555 173.0 ? 
22 NA  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NE2 ? B HIS   70 ? C HIS   65  ? 1_555 93.8  ? 
23 NB  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NE2 ? B HIS   70 ? C HIS   65  ? 1_555 87.5  ? 
24 NC  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NE2 ? B HIS   70 ? C HIS   65  ? 1_555 96.2  ? 
25 ND  ? G HEM   .  ? C HEM   301 ? 1_555 FE ? G HEM . ? C HEM 301 ? 1_555 NE2 ? B HIS   70 ? C HIS   65  ? 1_555 102.8 ? 
26 NE2 ? C HIS   70 ? D HIS   65  ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NA  ? H HEM   .  ? D HEM   301 ? 1_555 94.8  ? 
27 NE2 ? C HIS   70 ? D HIS   65  ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NB  ? H HEM   .  ? D HEM   301 ? 1_555 87.8  ? 
28 NA  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NB  ? H HEM   .  ? D HEM   301 ? 1_555 90.8  ? 
29 NE2 ? C HIS   70 ? D HIS   65  ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NC  ? H HEM   .  ? D HEM   301 ? 1_555 96.5  ? 
30 NA  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NC  ? H HEM   .  ? D HEM   301 ? 1_555 168.4 ? 
31 NB  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NC  ? H HEM   .  ? D HEM   301 ? 1_555 86.8  ? 
32 NE2 ? C HIS   70 ? D HIS   65  ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 ND  ? H HEM   .  ? D HEM   301 ? 1_555 103.0 ? 
33 NA  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 ND  ? H HEM   .  ? D HEM   301 ? 1_555 89.3  ? 
34 NB  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 ND  ? H HEM   .  ? D HEM   301 ? 1_555 169.2 ? 
35 NC  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 ND  ? H HEM   .  ? D HEM   301 ? 1_555 90.8  ? 
36 NE2 ? C HIS   70 ? D HIS   65  ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NAG ? K A1ECN .  ? A A1ECN 302 ? 1_555 171.4 ? 
37 NA  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NAG ? K A1ECN .  ? A A1ECN 302 ? 1_555 89.6  ? 
38 NB  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NAG ? K A1ECN .  ? A A1ECN 302 ? 1_555 84.7  ? 
39 NC  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NAG ? K A1ECN .  ? A A1ECN 302 ? 1_555 78.8  ? 
40 ND  ? H HEM   .  ? D HEM   301 ? 1_555 FE ? H HEM . ? D HEM 301 ? 1_555 NAG ? K A1ECN .  ? A A1ECN 302 ? 1_555 84.5  ? 
41 NAG ? I A1ECN .  ? D A1ECN 302 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NA  ? J HEM   .  ? A HEM   301 ? 1_555 87.5  ? 
42 NAG ? I A1ECN .  ? D A1ECN 302 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NB  ? J HEM   .  ? A HEM   301 ? 1_555 84.6  ? 
43 NA  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NB  ? J HEM   .  ? A HEM   301 ? 1_555 87.0  ? 
44 NAG ? I A1ECN .  ? D A1ECN 302 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NC  ? J HEM   .  ? A HEM   301 ? 1_555 83.4  ? 
45 NA  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NC  ? J HEM   .  ? A HEM   301 ? 1_555 170.4 ? 
46 NB  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NC  ? J HEM   .  ? A HEM   301 ? 1_555 89.1  ? 
47 NAG ? I A1ECN .  ? D A1ECN 302 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 ND  ? J HEM   .  ? A HEM   301 ? 1_555 83.5  ? 
48 NA  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 ND  ? J HEM   .  ? A HEM   301 ? 1_555 91.7  ? 
49 NB  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 ND  ? J HEM   .  ? A HEM   301 ? 1_555 168.0 ? 
50 NC  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 ND  ? J HEM   .  ? A HEM   301 ? 1_555 90.3  ? 
51 NAG ? I A1ECN .  ? D A1ECN 302 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NE2 ? D HIS   70 ? A HIS   65  ? 1_555 175.0 ? 
52 NA  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NE2 ? D HIS   70 ? A HIS   65  ? 1_555 93.5  ? 
53 NB  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NE2 ? D HIS   70 ? A HIS   65  ? 1_555 90.6  ? 
54 NC  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NE2 ? D HIS   70 ? A HIS   65  ? 1_555 95.3  ? 
55 ND  ? J HEM   .  ? A HEM   301 ? 1_555 FE ? J HEM . ? A HEM 301 ? 1_555 NE2 ? D HIS   70 ? A HIS   65  ? 1_555 101.3 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ALA 106 A . ? ALA 101 B PRO 107 A ? PRO 102 B 1 -8.05 
2 ALA 106 B . ? ALA 101 C PRO 107 B ? PRO 102 C 1 -8.13 
3 ALA 106 C . ? ALA 101 D PRO 107 C ? PRO 102 D 1 -4.20 
4 ALA 106 D . ? ALA 101 A PRO 107 D ? PRO 102 A 1 -1.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 29  ? SER A 34  ? LEU B 24  SER B 29  
AA1 2 HIS A 43  ? VAL A 51  ? HIS B 38  VAL B 46  
AA1 3 THR A 66  ? ASN A 72  ? THR B 61  ASN B 67  
AA1 4 VAL A 167 ? LYS A 182 ? VAL B 162 LYS B 177 
AA1 5 THR A 111 ? LYS A 125 ? THR B 106 LYS B 120 
AA1 6 ALA A 85  ? VAL A 98  ? ALA B 80  VAL B 93  
AA1 7 LEU A 29  ? SER A 34  ? LEU B 24  SER B 29  
AA2 1 LEU B 29  ? SER B 34  ? LEU C 24  SER C 29  
AA2 2 HIS B 43  ? VAL B 51  ? HIS C 38  VAL C 46  
AA2 3 THR B 66  ? ASN B 72  ? THR C 61  ASN C 67  
AA2 4 VAL B 167 ? LYS B 182 ? VAL C 162 LYS C 177 
AA2 5 THR B 111 ? LYS B 125 ? THR C 106 LYS C 120 
AA2 6 ALA B 85  ? VAL B 98  ? ALA C 80  VAL C 93  
AA2 7 LEU B 29  ? SER B 34  ? LEU C 24  SER C 29  
AA3 1 LEU C 29  ? SER C 34  ? LEU D 24  SER D 29  
AA3 2 HIS C 43  ? VAL C 51  ? HIS D 38  VAL D 46  
AA3 3 THR C 66  ? ASN C 72  ? THR D 61  ASN D 67  
AA3 4 VAL C 167 ? LYS C 182 ? VAL D 162 LYS D 177 
AA3 5 THR C 111 ? LYS C 125 ? THR D 106 LYS D 120 
AA3 6 ALA C 84  ? VAL C 98  ? ALA D 79  VAL D 93  
AA3 7 LEU C 29  ? SER C 34  ? LEU D 24  SER D 29  
AA4 1 LEU D 29  ? SER D 34  ? LEU A 24  SER A 29  
AA4 2 HIS D 43  ? VAL D 51  ? HIS A 38  VAL A 46  
AA4 3 THR D 66  ? ASN D 72  ? THR A 61  ASN A 67  
AA4 4 VAL D 167 ? LYS D 182 ? VAL A 162 LYS A 177 
AA4 5 THR D 111 ? LYS D 125 ? THR A 106 LYS A 120 
AA4 6 ALA D 85  ? VAL D 98  ? ALA A 80  VAL A 93  
AA4 7 LEU D 29  ? SER D 34  ? LEU A 24  SER A 29  
# 
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 N LEU A 32  ? N LEU B 27  O THR A 45  ? O THR B 40  
AA1 2 3 N ILE A 50  ? N ILE B 45  O TRP A 68  ? O TRP B 63  
AA1 3 4 N MET A 71  ? N MET B 66  O GLY A 168 ? O GLY B 163 
AA1 4 5 O GLU A 176 ? O GLU B 171 N ARG A 120 ? N ARG B 115 
AA1 5 6 O THR A 111 ? O THR B 106 N VAL A 98  ? N VAL B 93  
AA1 6 7 O VAL A 88  ? O VAL B 83  N ALA A 33  ? N ALA B 28  
AA2 1 2 N LEU B 32  ? N LEU C 27  O THR B 45  ? O THR C 40  
AA2 2 3 N ILE B 50  ? N ILE C 45  O TRP B 68  ? O TRP C 63  
AA2 3 4 N MET B 71  ? N MET C 66  O GLY B 168 ? O GLY C 163 
AA2 4 5 O ARG B 171 ? O ARG C 166 N ARG B 124 ? N ARG C 119 
AA2 5 6 O GLY B 121 ? O GLY C 116 N VAL B 87  ? N VAL C 82  
AA2 6 7 O VAL B 88  ? O VAL C 83  N ALA B 33  ? N ALA C 28  
AA3 1 2 N LEU C 32  ? N LEU D 27  O THR C 45  ? O THR D 40  
AA3 2 3 N ILE C 50  ? N ILE D 45  O TRP C 68  ? O TRP D 63  
AA3 3 4 N MET C 71  ? N MET D 66  O GLY C 168 ? O GLY D 163 
AA3 4 5 O MET C 180 ? O MET D 175 N SER C 116 ? N SER D 111 
AA3 5 6 O VAL C 117 ? O VAL D 112 N PHE C 91  ? N PHE D 86  
AA3 6 7 O VAL C 88  ? O VAL D 83  N ALA C 33  ? N ALA D 28  
AA4 1 2 N LEU D 32  ? N LEU A 27  O THR D 45  ? O THR A 40  
AA4 2 3 N ILE D 50  ? N ILE A 45  O TRP D 68  ? O TRP A 63  
AA4 3 4 N LEU D 67  ? N LEU A 62  O LEU D 172 ? O LEU A 167 
AA4 4 5 O GLU D 176 ? O GLU A 171 N ARG D 120 ? N ARG A 115 
AA4 5 6 O THR D 111 ? O THR A 106 N VAL D 98  ? N VAL A 93  
AA4 6 7 O VAL D 88  ? O VAL A 83  N ALA D 33  ? N ALA A 28  
# 
_pdbx_entry_details.entry_id                   9JN6 
_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 CD2 C LEU 159 ? ? O C HOH 409 ? ? 1.89 
2  1 O   B HOH 498 ? ? O B HOH 585 ? ? 2.06 
3  1 OG1 B THR 40  ? ? O B HOH 401 ? ? 2.07 
4  1 O   D HOH 518 ? ? O D HOH 541 ? ? 2.09 
5  1 NH1 C ARG 168 ? ? O C HOH 401 ? ? 2.11 
6  1 O   C HOH 555 ? ? O C HOH 574 ? ? 2.11 
7  1 O   A HOH 468 ? ? O A HOH 568 ? ? 2.12 
8  1 O   A HOH 472 ? ? O A HOH 563 ? ? 2.13 
9  1 O   A HOH 450 ? ? O A HOH 571 ? ? 2.15 
10 1 O   C HOH 402 ? ? O C HOH 578 ? ? 2.15 
11 1 O   B HOH 551 ? ? O B HOH 580 ? ? 2.16 
12 1 O   D ASN 90  ? ? O D HOH 401 ? ? 2.18 
13 1 O   B HOH 549 ? ? O A HOH 556 ? ? 2.19 
14 1 O   A HOH 419 ? ? O A HOH 594 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     442 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     583 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_445 
_pdbx_validate_symm_contact.dist              2.14 
# 
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 NE C ARG 115 ? ? CZ C ARG 115 ? ? NH1 C ARG 115 ? ? 124.35 120.30 4.05   0.50 N 
2 1 NE C ARG 115 ? ? CZ C ARG 115 ? ? NH2 C ARG 115 ? ? 117.08 120.30 -3.22  0.50 N 
3 1 CG D MET 66  ? ? SD D MET 66  ? ? CE  D MET 66  ? ? 88.27  100.20 -11.93 1.60 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 ASP B 47  ? ? -33.79  114.31 
2  1 ALA B 79  ? ? -100.96 67.16  
3  1 ALA B 144 ? ? -142.24 35.60  
4  1 PHE B 176 ? ? -116.34 79.62  
5  1 LEU B 178 ? ? -142.72 40.66  
6  1 ASP C 47  ? ? -32.46  107.41 
7  1 ALA C 144 ? ? -148.73 39.89  
8  1 PHE C 176 ? ? -117.19 79.98  
9  1 ASP D 47  ? ? -33.65  110.26 
10 1 ALA D 79  ? ? -142.06 55.97  
11 1 ALA D 144 ? ? -146.01 44.02  
12 1 ASP A 47  ? ? -29.71  111.80 
13 1 ALA A 79  ? ? -101.40 65.84  
14 1 PHE A 176 ? ? -114.02 77.84  
# 
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 ? C HOH 630 ? 5.94 . 
2 1 O ? C HOH 631 ? 6.03 . 
3 1 O ? D HOH 590 ? 6.41 . 
4 1 O ? A HOH 616 ? 6.51 . 
# 
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 B ALA -4  ? A ALA 1   
2  1 Y 1 B GLY -3  ? A GLY 2   
3  1 Y 1 B ALA -2  ? A ALA 3   
4  1 Y 1 B THR 212 ? A THR 217 
5  1 Y 1 B GLU 213 ? A GLU 218 
6  1 Y 1 C ALA -4  ? B ALA 1   
7  1 Y 1 C GLY -3  ? B GLY 2   
8  1 Y 1 C ALA -2  ? B ALA 3   
9  1 Y 1 C GLY -1  ? B GLY 4   
10 1 Y 1 C THR 212 ? B THR 217 
11 1 Y 1 C GLU 213 ? B GLU 218 
12 1 Y 1 D ALA -4  ? C ALA 1   
13 1 Y 1 D GLY -3  ? C GLY 2   
14 1 Y 1 D ALA -2  ? C ALA 3   
15 1 Y 1 D THR 212 ? C THR 217 
16 1 Y 1 D GLU 213 ? C GLU 218 
17 1 Y 1 A ALA -4  ? D ALA 1   
18 1 Y 1 A GLY -3  ? D GLY 2   
19 1 Y 1 A ALA -2  ? D ALA 3   
20 1 Y 1 A GLU 213 ? D GLU 218 
# 
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 
A1ECN OXT  O  N N 1   
A1ECN C    C  N N 2   
A1ECN O    O  N N 3   
A1ECN CA   C  N S 4   
A1ECN CB   C  N N 5   
A1ECN CAC  C  N N 6   
A1ECN CAD  C  N N 7   
A1ECN NAG  N  N N 8   
A1ECN N    N  N N 9   
A1ECN HXT  H  N N 10  
A1ECN HA   H  N N 11  
A1ECN H3   H  N N 12  
A1ECN H4   H  N N 13  
A1ECN H5   H  N N 14  
A1ECN H6   H  N N 15  
A1ECN H7   H  N N 16  
A1ECN H1   H  N N 17  
A1ECN H9   H  N N 18  
A1ECN H    H  N N 19  
ALA   N    N  N N 20  
ALA   CA   C  N S 21  
ALA   C    C  N N 22  
ALA   O    O  N N 23  
ALA   CB   C  N N 24  
ALA   OXT  O  N N 25  
ALA   H    H  N N 26  
ALA   H2   H  N N 27  
ALA   HA   H  N N 28  
ALA   HB1  H  N N 29  
ALA   HB2  H  N N 30  
ALA   HB3  H  N N 31  
ALA   HXT  H  N N 32  
ARG   N    N  N N 33  
ARG   CA   C  N S 34  
ARG   C    C  N N 35  
ARG   O    O  N N 36  
ARG   CB   C  N N 37  
ARG   CG   C  N N 38  
ARG   CD   C  N N 39  
ARG   NE   N  N N 40  
ARG   CZ   C  N N 41  
ARG   NH1  N  N N 42  
ARG   NH2  N  N N 43  
ARG   OXT  O  N N 44  
ARG   H    H  N N 45  
ARG   H2   H  N N 46  
ARG   HA   H  N N 47  
ARG   HB2  H  N N 48  
ARG   HB3  H  N N 49  
ARG   HG2  H  N N 50  
ARG   HG3  H  N N 51  
ARG   HD2  H  N N 52  
ARG   HD3  H  N N 53  
ARG   HE   H  N N 54  
ARG   HH11 H  N N 55  
ARG   HH12 H  N N 56  
ARG   HH21 H  N N 57  
ARG   HH22 H  N N 58  
ARG   HXT  H  N N 59  
ASN   N    N  N N 60  
ASN   CA   C  N S 61  
ASN   C    C  N N 62  
ASN   O    O  N N 63  
ASN   CB   C  N N 64  
ASN   CG   C  N N 65  
ASN   OD1  O  N N 66  
ASN   ND2  N  N N 67  
ASN   OXT  O  N N 68  
ASN   H    H  N N 69  
ASN   H2   H  N N 70  
ASN   HA   H  N N 71  
ASN   HB2  H  N N 72  
ASN   HB3  H  N N 73  
ASN   HD21 H  N N 74  
ASN   HD22 H  N N 75  
ASN   HXT  H  N N 76  
ASP   N    N  N N 77  
ASP   CA   C  N S 78  
ASP   C    C  N N 79  
ASP   O    O  N N 80  
ASP   CB   C  N N 81  
ASP   CG   C  N N 82  
ASP   OD1  O  N N 83  
ASP   OD2  O  N N 84  
ASP   OXT  O  N N 85  
ASP   H    H  N N 86  
ASP   H2   H  N N 87  
ASP   HA   H  N N 88  
ASP   HB2  H  N N 89  
ASP   HB3  H  N N 90  
ASP   HD2  H  N N 91  
ASP   HXT  H  N N 92  
CYS   N    N  N N 93  
CYS   CA   C  N R 94  
CYS   C    C  N N 95  
CYS   O    O  N N 96  
CYS   CB   C  N N 97  
CYS   SG   S  N N 98  
CYS   OXT  O  N N 99  
CYS   H    H  N N 100 
CYS   H2   H  N N 101 
CYS   HA   H  N N 102 
CYS   HB2  H  N N 103 
CYS   HB3  H  N N 104 
CYS   HG   H  N N 105 
CYS   HXT  H  N N 106 
GLN   N    N  N N 107 
GLN   CA   C  N S 108 
GLN   C    C  N N 109 
GLN   O    O  N N 110 
GLN   CB   C  N N 111 
GLN   CG   C  N N 112 
GLN   CD   C  N N 113 
GLN   OE1  O  N N 114 
GLN   NE2  N  N N 115 
GLN   OXT  O  N N 116 
GLN   H    H  N N 117 
GLN   H2   H  N N 118 
GLN   HA   H  N N 119 
GLN   HB2  H  N N 120 
GLN   HB3  H  N N 121 
GLN   HG2  H  N N 122 
GLN   HG3  H  N N 123 
GLN   HE21 H  N N 124 
GLN   HE22 H  N N 125 
GLN   HXT  H  N N 126 
GLU   N    N  N N 127 
GLU   CA   C  N S 128 
GLU   C    C  N N 129 
GLU   O    O  N N 130 
GLU   CB   C  N N 131 
GLU   CG   C  N N 132 
GLU   CD   C  N N 133 
GLU   OE1  O  N N 134 
GLU   OE2  O  N N 135 
GLU   OXT  O  N N 136 
GLU   H    H  N N 137 
GLU   H2   H  N N 138 
GLU   HA   H  N N 139 
GLU   HB2  H  N N 140 
GLU   HB3  H  N N 141 
GLU   HG2  H  N N 142 
GLU   HG3  H  N N 143 
GLU   HE2  H  N N 144 
GLU   HXT  H  N N 145 
GLY   N    N  N N 146 
GLY   CA   C  N N 147 
GLY   C    C  N N 148 
GLY   O    O  N N 149 
GLY   OXT  O  N N 150 
GLY   H    H  N N 151 
GLY   H2   H  N N 152 
GLY   HA2  H  N N 153 
GLY   HA3  H  N N 154 
GLY   HXT  H  N N 155 
HEM   CHA  C  N N 156 
HEM   CHB  C  N N 157 
HEM   CHC  C  N N 158 
HEM   CHD  C  N N 159 
HEM   C1A  C  Y N 160 
HEM   C2A  C  Y N 161 
HEM   C3A  C  Y N 162 
HEM   C4A  C  Y N 163 
HEM   CMA  C  N N 164 
HEM   CAA  C  N N 165 
HEM   CBA  C  N N 166 
HEM   CGA  C  N N 167 
HEM   O1A  O  N N 168 
HEM   O2A  O  N N 169 
HEM   C1B  C  N N 170 
HEM   C2B  C  N N 171 
HEM   C3B  C  N N 172 
HEM   C4B  C  N N 173 
HEM   CMB  C  N N 174 
HEM   CAB  C  N N 175 
HEM   CBB  C  N N 176 
HEM   C1C  C  Y N 177 
HEM   C2C  C  Y N 178 
HEM   C3C  C  Y N 179 
HEM   C4C  C  Y N 180 
HEM   CMC  C  N N 181 
HEM   CAC  C  N N 182 
HEM   CBC  C  N N 183 
HEM   C1D  C  N N 184 
HEM   C2D  C  N N 185 
HEM   C3D  C  N N 186 
HEM   C4D  C  N N 187 
HEM   CMD  C  N N 188 
HEM   CAD  C  N N 189 
HEM   CBD  C  N N 190 
HEM   CGD  C  N N 191 
HEM   O1D  O  N N 192 
HEM   O2D  O  N N 193 
HEM   NA   N  Y N 194 
HEM   NB   N  N N 195 
HEM   NC   N  Y N 196 
HEM   ND   N  N N 197 
HEM   FE   FE N N 198 
HEM   HHB  H  N N 199 
HEM   HHC  H  N N 200 
HEM   HHD  H  N N 201 
HEM   HMA  H  N N 202 
HEM   HMAA H  N N 203 
HEM   HMAB H  N N 204 
HEM   HAA  H  N N 205 
HEM   HAAA H  N N 206 
HEM   HBA  H  N N 207 
HEM   HBAA H  N N 208 
HEM   HMB  H  N N 209 
HEM   HMBA H  N N 210 
HEM   HMBB H  N N 211 
HEM   HAB  H  N N 212 
HEM   HBB  H  N N 213 
HEM   HBBA H  N N 214 
HEM   HMC  H  N N 215 
HEM   HMCA H  N N 216 
HEM   HMCB H  N N 217 
HEM   HAC  H  N N 218 
HEM   HBC  H  N N 219 
HEM   HBCA H  N N 220 
HEM   HMD  H  N N 221 
HEM   HMDA H  N N 222 
HEM   HMDB H  N N 223 
HEM   HAD  H  N N 224 
HEM   HADA H  N N 225 
HEM   HBD  H  N N 226 
HEM   HBDA H  N N 227 
HEM   H2A  H  N N 228 
HEM   H2D  H  N N 229 
HEM   HHA  H  N N 230 
HIS   N    N  N N 231 
HIS   CA   C  N S 232 
HIS   C    C  N N 233 
HIS   O    O  N N 234 
HIS   CB   C  N N 235 
HIS   CG   C  Y N 236 
HIS   ND1  N  Y N 237 
HIS   CD2  C  Y N 238 
HIS   CE1  C  Y N 239 
HIS   NE2  N  Y N 240 
HIS   OXT  O  N N 241 
HIS   H    H  N N 242 
HIS   H2   H  N N 243 
HIS   HA   H  N N 244 
HIS   HB2  H  N N 245 
HIS   HB3  H  N N 246 
HIS   HD1  H  N N 247 
HIS   HD2  H  N N 248 
HIS   HE1  H  N N 249 
HIS   HE2  H  N N 250 
HIS   HXT  H  N N 251 
HOH   O    O  N N 252 
HOH   H1   H  N N 253 
HOH   H2   H  N N 254 
ILE   N    N  N N 255 
ILE   CA   C  N S 256 
ILE   C    C  N N 257 
ILE   O    O  N N 258 
ILE   CB   C  N S 259 
ILE   CG1  C  N N 260 
ILE   CG2  C  N N 261 
ILE   CD1  C  N N 262 
ILE   OXT  O  N N 263 
ILE   H    H  N N 264 
ILE   H2   H  N N 265 
ILE   HA   H  N N 266 
ILE   HB   H  N N 267 
ILE   HG12 H  N N 268 
ILE   HG13 H  N N 269 
ILE   HG21 H  N N 270 
ILE   HG22 H  N N 271 
ILE   HG23 H  N N 272 
ILE   HD11 H  N N 273 
ILE   HD12 H  N N 274 
ILE   HD13 H  N N 275 
ILE   HXT  H  N N 276 
LEU   N    N  N N 277 
LEU   CA   C  N S 278 
LEU   C    C  N N 279 
LEU   O    O  N N 280 
LEU   CB   C  N N 281 
LEU   CG   C  N N 282 
LEU   CD1  C  N N 283 
LEU   CD2  C  N N 284 
LEU   OXT  O  N N 285 
LEU   H    H  N N 286 
LEU   H2   H  N N 287 
LEU   HA   H  N N 288 
LEU   HB2  H  N N 289 
LEU   HB3  H  N N 290 
LEU   HG   H  N N 291 
LEU   HD11 H  N N 292 
LEU   HD12 H  N N 293 
LEU   HD13 H  N N 294 
LEU   HD21 H  N N 295 
LEU   HD22 H  N N 296 
LEU   HD23 H  N N 297 
LEU   HXT  H  N N 298 
LYS   N    N  N N 299 
LYS   CA   C  N S 300 
LYS   C    C  N N 301 
LYS   O    O  N N 302 
LYS   CB   C  N N 303 
LYS   CG   C  N N 304 
LYS   CD   C  N N 305 
LYS   CE   C  N N 306 
LYS   NZ   N  N N 307 
LYS   OXT  O  N N 308 
LYS   H    H  N N 309 
LYS   H2   H  N N 310 
LYS   HA   H  N N 311 
LYS   HB2  H  N N 312 
LYS   HB3  H  N N 313 
LYS   HG2  H  N N 314 
LYS   HG3  H  N N 315 
LYS   HD2  H  N N 316 
LYS   HD3  H  N N 317 
LYS   HE2  H  N N 318 
LYS   HE3  H  N N 319 
LYS   HZ1  H  N N 320 
LYS   HZ2  H  N N 321 
LYS   HZ3  H  N N 322 
LYS   HXT  H  N N 323 
MET   N    N  N N 324 
MET   CA   C  N S 325 
MET   C    C  N N 326 
MET   O    O  N N 327 
MET   CB   C  N N 328 
MET   CG   C  N N 329 
MET   SD   S  N N 330 
MET   CE   C  N N 331 
MET   OXT  O  N N 332 
MET   H    H  N N 333 
MET   H2   H  N N 334 
MET   HA   H  N N 335 
MET   HB2  H  N N 336 
MET   HB3  H  N N 337 
MET   HG2  H  N N 338 
MET   HG3  H  N N 339 
MET   HE1  H  N N 340 
MET   HE2  H  N N 341 
MET   HE3  H  N N 342 
MET   HXT  H  N N 343 
PHE   N    N  N N 344 
PHE   CA   C  N S 345 
PHE   C    C  N N 346 
PHE   O    O  N N 347 
PHE   CB   C  N N 348 
PHE   CG   C  Y N 349 
PHE   CD1  C  Y N 350 
PHE   CD2  C  Y N 351 
PHE   CE1  C  Y N 352 
PHE   CE2  C  Y N 353 
PHE   CZ   C  Y N 354 
PHE   OXT  O  N N 355 
PHE   H    H  N N 356 
PHE   H2   H  N N 357 
PHE   HA   H  N N 358 
PHE   HB2  H  N N 359 
PHE   HB3  H  N N 360 
PHE   HD1  H  N N 361 
PHE   HD2  H  N N 362 
PHE   HE1  H  N N 363 
PHE   HE2  H  N N 364 
PHE   HZ   H  N N 365 
PHE   HXT  H  N N 366 
PRO   N    N  N N 367 
PRO   CA   C  N S 368 
PRO   C    C  N N 369 
PRO   O    O  N N 370 
PRO   CB   C  N N 371 
PRO   CG   C  N N 372 
PRO   CD   C  N N 373 
PRO   OXT  O  N N 374 
PRO   H    H  N N 375 
PRO   HA   H  N N 376 
PRO   HB2  H  N N 377 
PRO   HB3  H  N N 378 
PRO   HG2  H  N N 379 
PRO   HG3  H  N N 380 
PRO   HD2  H  N N 381 
PRO   HD3  H  N N 382 
PRO   HXT  H  N N 383 
SER   N    N  N N 384 
SER   CA   C  N S 385 
SER   C    C  N N 386 
SER   O    O  N N 387 
SER   CB   C  N N 388 
SER   OG   O  N N 389 
SER   OXT  O  N N 390 
SER   H    H  N N 391 
SER   H2   H  N N 392 
SER   HA   H  N N 393 
SER   HB2  H  N N 394 
SER   HB3  H  N N 395 
SER   HG   H  N N 396 
SER   HXT  H  N N 397 
THR   N    N  N N 398 
THR   CA   C  N S 399 
THR   C    C  N N 400 
THR   O    O  N N 401 
THR   CB   C  N R 402 
THR   OG1  O  N N 403 
THR   CG2  C  N N 404 
THR   OXT  O  N N 405 
THR   H    H  N N 406 
THR   H2   H  N N 407 
THR   HA   H  N N 408 
THR   HB   H  N N 409 
THR   HG1  H  N N 410 
THR   HG21 H  N N 411 
THR   HG22 H  N N 412 
THR   HG23 H  N N 413 
THR   HXT  H  N N 414 
TRP   N    N  N N 415 
TRP   CA   C  N S 416 
TRP   C    C  N N 417 
TRP   O    O  N N 418 
TRP   CB   C  N N 419 
TRP   CG   C  Y N 420 
TRP   CD1  C  Y N 421 
TRP   CD2  C  Y N 422 
TRP   NE1  N  Y N 423 
TRP   CE2  C  Y N 424 
TRP   CE3  C  Y N 425 
TRP   CZ2  C  Y N 426 
TRP   CZ3  C  Y N 427 
TRP   CH2  C  Y N 428 
TRP   OXT  O  N N 429 
TRP   H    H  N N 430 
TRP   H2   H  N N 431 
TRP   HA   H  N N 432 
TRP   HB2  H  N N 433 
TRP   HB3  H  N N 434 
TRP   HD1  H  N N 435 
TRP   HE1  H  N N 436 
TRP   HE3  H  N N 437 
TRP   HZ2  H  N N 438 
TRP   HZ3  H  N N 439 
TRP   HH2  H  N N 440 
TRP   HXT  H  N N 441 
TYR   N    N  N N 442 
TYR   CA   C  N S 443 
TYR   C    C  N N 444 
TYR   O    O  N N 445 
TYR   CB   C  N N 446 
TYR   CG   C  Y N 447 
TYR   CD1  C  Y N 448 
TYR   CD2  C  Y N 449 
TYR   CE1  C  Y N 450 
TYR   CE2  C  Y N 451 
TYR   CZ   C  Y N 452 
TYR   OH   O  N N 453 
TYR   OXT  O  N N 454 
TYR   H    H  N N 455 
TYR   H2   H  N N 456 
TYR   HA   H  N N 457 
TYR   HB2  H  N N 458 
TYR   HB3  H  N N 459 
TYR   HD1  H  N N 460 
TYR   HD2  H  N N 461 
TYR   HE1  H  N N 462 
TYR   HE2  H  N N 463 
TYR   HH   H  N N 464 
TYR   HXT  H  N N 465 
VAL   N    N  N N 466 
VAL   CA   C  N S 467 
VAL   C    C  N N 468 
VAL   O    O  N N 469 
VAL   CB   C  N N 470 
VAL   CG1  C  N N 471 
VAL   CG2  C  N N 472 
VAL   OXT  O  N N 473 
VAL   H    H  N N 474 
VAL   H2   H  N N 475 
VAL   HA   H  N N 476 
VAL   HB   H  N N 477 
VAL   HG11 H  N N 478 
VAL   HG12 H  N N 479 
VAL   HG13 H  N N 480 
VAL   HG21 H  N N 481 
VAL   HG22 H  N N 482 
VAL   HG23 H  N N 483 
VAL   HXT  H  N N 484 
# 
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 
A1ECN CA  N    sing N N 1   
A1ECN CA  C    sing N N 2   
A1ECN CA  CB   sing N N 3   
A1ECN N   NAG  sing N N 4   
A1ECN C   O    doub N N 5   
A1ECN C   OXT  sing N N 6   
A1ECN CB  CAC  sing N N 7   
A1ECN NAG CAD  sing N N 8   
A1ECN CAC CAD  sing N N 9   
A1ECN OXT HXT  sing N N 10  
A1ECN CA  HA   sing N N 11  
A1ECN CB  H3   sing N N 12  
A1ECN CB  H4   sing N N 13  
A1ECN CAC H5   sing N N 14  
A1ECN CAC H6   sing N N 15  
A1ECN CAD H7   sing N N 16  
A1ECN CAD H1   sing N N 17  
A1ECN NAG H9   sing N N 18  
A1ECN N   H    sing N N 19  
ALA   N   CA   sing N N 20  
ALA   N   H    sing N N 21  
ALA   N   H2   sing N N 22  
ALA   CA  C    sing N N 23  
ALA   CA  CB   sing N N 24  
ALA   CA  HA   sing N N 25  
ALA   C   O    doub N N 26  
ALA   C   OXT  sing N N 27  
ALA   CB  HB1  sing N N 28  
ALA   CB  HB2  sing N N 29  
ALA   CB  HB3  sing N N 30  
ALA   OXT HXT  sing N N 31  
ARG   N   CA   sing N N 32  
ARG   N   H    sing N N 33  
ARG   N   H2   sing N N 34  
ARG   CA  C    sing N N 35  
ARG   CA  CB   sing N N 36  
ARG   CA  HA   sing N N 37  
ARG   C   O    doub N N 38  
ARG   C   OXT  sing N N 39  
ARG   CB  CG   sing N N 40  
ARG   CB  HB2  sing N N 41  
ARG   CB  HB3  sing N N 42  
ARG   CG  CD   sing N N 43  
ARG   CG  HG2  sing N N 44  
ARG   CG  HG3  sing N N 45  
ARG   CD  NE   sing N N 46  
ARG   CD  HD2  sing N N 47  
ARG   CD  HD3  sing N N 48  
ARG   NE  CZ   sing N N 49  
ARG   NE  HE   sing N N 50  
ARG   CZ  NH1  sing N N 51  
ARG   CZ  NH2  doub N N 52  
ARG   NH1 HH11 sing N N 53  
ARG   NH1 HH12 sing N N 54  
ARG   NH2 HH21 sing N N 55  
ARG   NH2 HH22 sing N N 56  
ARG   OXT HXT  sing N N 57  
ASN   N   CA   sing N N 58  
ASN   N   H    sing N N 59  
ASN   N   H2   sing N N 60  
ASN   CA  C    sing N N 61  
ASN   CA  CB   sing N N 62  
ASN   CA  HA   sing N N 63  
ASN   C   O    doub N N 64  
ASN   C   OXT  sing N N 65  
ASN   CB  CG   sing N N 66  
ASN   CB  HB2  sing N N 67  
ASN   CB  HB3  sing N N 68  
ASN   CG  OD1  doub N N 69  
ASN   CG  ND2  sing N N 70  
ASN   ND2 HD21 sing N N 71  
ASN   ND2 HD22 sing N N 72  
ASN   OXT HXT  sing N N 73  
ASP   N   CA   sing N N 74  
ASP   N   H    sing N N 75  
ASP   N   H2   sing N N 76  
ASP   CA  C    sing N N 77  
ASP   CA  CB   sing N N 78  
ASP   CA  HA   sing N N 79  
ASP   C   O    doub N N 80  
ASP   C   OXT  sing N N 81  
ASP   CB  CG   sing N N 82  
ASP   CB  HB2  sing N N 83  
ASP   CB  HB3  sing N N 84  
ASP   CG  OD1  doub N N 85  
ASP   CG  OD2  sing N N 86  
ASP   OD2 HD2  sing N N 87  
ASP   OXT HXT  sing N N 88  
CYS   N   CA   sing N N 89  
CYS   N   H    sing N N 90  
CYS   N   H2   sing N N 91  
CYS   CA  C    sing N N 92  
CYS   CA  CB   sing N N 93  
CYS   CA  HA   sing N N 94  
CYS   C   O    doub N N 95  
CYS   C   OXT  sing N N 96  
CYS   CB  SG   sing N N 97  
CYS   CB  HB2  sing N N 98  
CYS   CB  HB3  sing N N 99  
CYS   SG  HG   sing N N 100 
CYS   OXT HXT  sing N N 101 
GLN   N   CA   sing N N 102 
GLN   N   H    sing N N 103 
GLN   N   H2   sing N N 104 
GLN   CA  C    sing N N 105 
GLN   CA  CB   sing N N 106 
GLN   CA  HA   sing N N 107 
GLN   C   O    doub N N 108 
GLN   C   OXT  sing N N 109 
GLN   CB  CG   sing N N 110 
GLN   CB  HB2  sing N N 111 
GLN   CB  HB3  sing N N 112 
GLN   CG  CD   sing N N 113 
GLN   CG  HG2  sing N N 114 
GLN   CG  HG3  sing N N 115 
GLN   CD  OE1  doub N N 116 
GLN   CD  NE2  sing N N 117 
GLN   NE2 HE21 sing N N 118 
GLN   NE2 HE22 sing N N 119 
GLN   OXT HXT  sing N N 120 
GLU   N   CA   sing N N 121 
GLU   N   H    sing N N 122 
GLU   N   H2   sing N N 123 
GLU   CA  C    sing N N 124 
GLU   CA  CB   sing N N 125 
GLU   CA  HA   sing N N 126 
GLU   C   O    doub N N 127 
GLU   C   OXT  sing N N 128 
GLU   CB  CG   sing N N 129 
GLU   CB  HB2  sing N N 130 
GLU   CB  HB3  sing N N 131 
GLU   CG  CD   sing N N 132 
GLU   CG  HG2  sing N N 133 
GLU   CG  HG3  sing N N 134 
GLU   CD  OE1  doub N N 135 
GLU   CD  OE2  sing N N 136 
GLU   OE2 HE2  sing N N 137 
GLU   OXT HXT  sing N N 138 
GLY   N   CA   sing N N 139 
GLY   N   H    sing N N 140 
GLY   N   H2   sing N N 141 
GLY   CA  C    sing N N 142 
GLY   CA  HA2  sing N N 143 
GLY   CA  HA3  sing N N 144 
GLY   C   O    doub N N 145 
GLY   C   OXT  sing N N 146 
GLY   OXT HXT  sing N N 147 
HEM   CHA C1A  sing N N 148 
HEM   CHA C4D  doub N N 149 
HEM   CHA HHA  sing N N 150 
HEM   CHB C4A  sing N N 151 
HEM   CHB C1B  doub N N 152 
HEM   CHB HHB  sing N N 153 
HEM   CHC C4B  sing N N 154 
HEM   CHC C1C  doub N N 155 
HEM   CHC HHC  sing N N 156 
HEM   CHD C4C  doub N N 157 
HEM   CHD C1D  sing N N 158 
HEM   CHD HHD  sing N N 159 
HEM   C1A C2A  doub Y N 160 
HEM   C1A NA   sing Y N 161 
HEM   C2A C3A  sing Y N 162 
HEM   C2A CAA  sing N N 163 
HEM   C3A C4A  doub Y N 164 
HEM   C3A CMA  sing N N 165 
HEM   C4A NA   sing Y N 166 
HEM   CMA HMA  sing N N 167 
HEM   CMA HMAA sing N N 168 
HEM   CMA HMAB sing N N 169 
HEM   CAA CBA  sing N N 170 
HEM   CAA HAA  sing N N 171 
HEM   CAA HAAA sing N N 172 
HEM   CBA CGA  sing N N 173 
HEM   CBA HBA  sing N N 174 
HEM   CBA HBAA sing N N 175 
HEM   CGA O1A  doub N N 176 
HEM   CGA O2A  sing N N 177 
HEM   C1B C2B  sing N N 178 
HEM   C1B NB   sing N N 179 
HEM   C2B C3B  doub N N 180 
HEM   C2B CMB  sing N N 181 
HEM   C3B C4B  sing N N 182 
HEM   C3B CAB  sing N N 183 
HEM   C4B NB   doub N N 184 
HEM   CMB HMB  sing N N 185 
HEM   CMB HMBA sing N N 186 
HEM   CMB HMBB sing N N 187 
HEM   CAB CBB  doub N N 188 
HEM   CAB HAB  sing N N 189 
HEM   CBB HBB  sing N N 190 
HEM   CBB HBBA sing N N 191 
HEM   C1C C2C  sing Y N 192 
HEM   C1C NC   sing Y N 193 
HEM   C2C C3C  doub Y N 194 
HEM   C2C CMC  sing N N 195 
HEM   C3C C4C  sing Y N 196 
HEM   C3C CAC  sing N N 197 
HEM   C4C NC   sing Y N 198 
HEM   CMC HMC  sing N N 199 
HEM   CMC HMCA sing N N 200 
HEM   CMC HMCB sing N N 201 
HEM   CAC CBC  doub N N 202 
HEM   CAC HAC  sing N N 203 
HEM   CBC HBC  sing N N 204 
HEM   CBC HBCA sing N N 205 
HEM   C1D C2D  sing N N 206 
HEM   C1D ND   doub N N 207 
HEM   C2D C3D  doub N N 208 
HEM   C2D CMD  sing N N 209 
HEM   C3D C4D  sing N N 210 
HEM   C3D CAD  sing N N 211 
HEM   C4D ND   sing N N 212 
HEM   CMD HMD  sing N N 213 
HEM   CMD HMDA sing N N 214 
HEM   CMD HMDB sing N N 215 
HEM   CAD CBD  sing N N 216 
HEM   CAD HAD  sing N N 217 
HEM   CAD HADA sing N N 218 
HEM   CBD CGD  sing N N 219 
HEM   CBD HBD  sing N N 220 
HEM   CBD HBDA sing N N 221 
HEM   CGD O1D  doub N N 222 
HEM   CGD O2D  sing N N 223 
HEM   O2A H2A  sing N N 224 
HEM   O2D H2D  sing N N 225 
HEM   FE  NA   sing N N 226 
HEM   FE  NB   sing N N 227 
HEM   FE  NC   sing N N 228 
HEM   FE  ND   sing N N 229 
HIS   N   CA   sing N N 230 
HIS   N   H    sing N N 231 
HIS   N   H2   sing N N 232 
HIS   CA  C    sing N N 233 
HIS   CA  CB   sing N N 234 
HIS   CA  HA   sing N N 235 
HIS   C   O    doub N N 236 
HIS   C   OXT  sing N N 237 
HIS   CB  CG   sing N N 238 
HIS   CB  HB2  sing N N 239 
HIS   CB  HB3  sing N N 240 
HIS   CG  ND1  sing Y N 241 
HIS   CG  CD2  doub Y N 242 
HIS   ND1 CE1  doub Y N 243 
HIS   ND1 HD1  sing N N 244 
HIS   CD2 NE2  sing Y N 245 
HIS   CD2 HD2  sing N N 246 
HIS   CE1 NE2  sing Y N 247 
HIS   CE1 HE1  sing N N 248 
HIS   NE2 HE2  sing N N 249 
HIS   OXT HXT  sing N N 250 
HOH   O   H1   sing N N 251 
HOH   O   H2   sing N N 252 
ILE   N   CA   sing N N 253 
ILE   N   H    sing N N 254 
ILE   N   H2   sing N N 255 
ILE   CA  C    sing N N 256 
ILE   CA  CB   sing N N 257 
ILE   CA  HA   sing N N 258 
ILE   C   O    doub N N 259 
ILE   C   OXT  sing N N 260 
ILE   CB  CG1  sing N N 261 
ILE   CB  CG2  sing N N 262 
ILE   CB  HB   sing N N 263 
ILE   CG1 CD1  sing N N 264 
ILE   CG1 HG12 sing N N 265 
ILE   CG1 HG13 sing N N 266 
ILE   CG2 HG21 sing N N 267 
ILE   CG2 HG22 sing N N 268 
ILE   CG2 HG23 sing N N 269 
ILE   CD1 HD11 sing N N 270 
ILE   CD1 HD12 sing N N 271 
ILE   CD1 HD13 sing N N 272 
ILE   OXT HXT  sing N N 273 
LEU   N   CA   sing N N 274 
LEU   N   H    sing N N 275 
LEU   N   H2   sing N N 276 
LEU   CA  C    sing N N 277 
LEU   CA  CB   sing N N 278 
LEU   CA  HA   sing N N 279 
LEU   C   O    doub N N 280 
LEU   C   OXT  sing N N 281 
LEU   CB  CG   sing N N 282 
LEU   CB  HB2  sing N N 283 
LEU   CB  HB3  sing N N 284 
LEU   CG  CD1  sing N N 285 
LEU   CG  CD2  sing N N 286 
LEU   CG  HG   sing N N 287 
LEU   CD1 HD11 sing N N 288 
LEU   CD1 HD12 sing N N 289 
LEU   CD1 HD13 sing N N 290 
LEU   CD2 HD21 sing N N 291 
LEU   CD2 HD22 sing N N 292 
LEU   CD2 HD23 sing N N 293 
LEU   OXT HXT  sing N N 294 
LYS   N   CA   sing N N 295 
LYS   N   H    sing N N 296 
LYS   N   H2   sing N N 297 
LYS   CA  C    sing N N 298 
LYS   CA  CB   sing N N 299 
LYS   CA  HA   sing N N 300 
LYS   C   O    doub N N 301 
LYS   C   OXT  sing N N 302 
LYS   CB  CG   sing N N 303 
LYS   CB  HB2  sing N N 304 
LYS   CB  HB3  sing N N 305 
LYS   CG  CD   sing N N 306 
LYS   CG  HG2  sing N N 307 
LYS   CG  HG3  sing N N 308 
LYS   CD  CE   sing N N 309 
LYS   CD  HD2  sing N N 310 
LYS   CD  HD3  sing N N 311 
LYS   CE  NZ   sing N N 312 
LYS   CE  HE2  sing N N 313 
LYS   CE  HE3  sing N N 314 
LYS   NZ  HZ1  sing N N 315 
LYS   NZ  HZ2  sing N N 316 
LYS   NZ  HZ3  sing N N 317 
LYS   OXT HXT  sing N N 318 
MET   N   CA   sing N N 319 
MET   N   H    sing N N 320 
MET   N   H2   sing N N 321 
MET   CA  C    sing N N 322 
MET   CA  CB   sing N N 323 
MET   CA  HA   sing N N 324 
MET   C   O    doub N N 325 
MET   C   OXT  sing N N 326 
MET   CB  CG   sing N N 327 
MET   CB  HB2  sing N N 328 
MET   CB  HB3  sing N N 329 
MET   CG  SD   sing N N 330 
MET   CG  HG2  sing N N 331 
MET   CG  HG3  sing N N 332 
MET   SD  CE   sing N N 333 
MET   CE  HE1  sing N N 334 
MET   CE  HE2  sing N N 335 
MET   CE  HE3  sing N N 336 
MET   OXT HXT  sing N N 337 
PHE   N   CA   sing N N 338 
PHE   N   H    sing N N 339 
PHE   N   H2   sing N N 340 
PHE   CA  C    sing N N 341 
PHE   CA  CB   sing N N 342 
PHE   CA  HA   sing N N 343 
PHE   C   O    doub N N 344 
PHE   C   OXT  sing N N 345 
PHE   CB  CG   sing N N 346 
PHE   CB  HB2  sing N N 347 
PHE   CB  HB3  sing N N 348 
PHE   CG  CD1  doub Y N 349 
PHE   CG  CD2  sing Y N 350 
PHE   CD1 CE1  sing Y N 351 
PHE   CD1 HD1  sing N N 352 
PHE   CD2 CE2  doub Y N 353 
PHE   CD2 HD2  sing N N 354 
PHE   CE1 CZ   doub Y N 355 
PHE   CE1 HE1  sing N N 356 
PHE   CE2 CZ   sing Y N 357 
PHE   CE2 HE2  sing N N 358 
PHE   CZ  HZ   sing N N 359 
PHE   OXT HXT  sing N N 360 
PRO   N   CA   sing N N 361 
PRO   N   CD   sing N N 362 
PRO   N   H    sing N N 363 
PRO   CA  C    sing N N 364 
PRO   CA  CB   sing N N 365 
PRO   CA  HA   sing N N 366 
PRO   C   O    doub N N 367 
PRO   C   OXT  sing N N 368 
PRO   CB  CG   sing N N 369 
PRO   CB  HB2  sing N N 370 
PRO   CB  HB3  sing N N 371 
PRO   CG  CD   sing N N 372 
PRO   CG  HG2  sing N N 373 
PRO   CG  HG3  sing N N 374 
PRO   CD  HD2  sing N N 375 
PRO   CD  HD3  sing N N 376 
PRO   OXT HXT  sing N N 377 
SER   N   CA   sing N N 378 
SER   N   H    sing N N 379 
SER   N   H2   sing N N 380 
SER   CA  C    sing N N 381 
SER   CA  CB   sing N N 382 
SER   CA  HA   sing N N 383 
SER   C   O    doub N N 384 
SER   C   OXT  sing N N 385 
SER   CB  OG   sing N N 386 
SER   CB  HB2  sing N N 387 
SER   CB  HB3  sing N N 388 
SER   OG  HG   sing N N 389 
SER   OXT HXT  sing N N 390 
THR   N   CA   sing N N 391 
THR   N   H    sing N N 392 
THR   N   H2   sing N N 393 
THR   CA  C    sing N N 394 
THR   CA  CB   sing N N 395 
THR   CA  HA   sing N N 396 
THR   C   O    doub N N 397 
THR   C   OXT  sing N N 398 
THR   CB  OG1  sing N N 399 
THR   CB  CG2  sing N N 400 
THR   CB  HB   sing N N 401 
THR   OG1 HG1  sing N N 402 
THR   CG2 HG21 sing N N 403 
THR   CG2 HG22 sing N N 404 
THR   CG2 HG23 sing N N 405 
THR   OXT HXT  sing N N 406 
TRP   N   CA   sing N N 407 
TRP   N   H    sing N N 408 
TRP   N   H2   sing N N 409 
TRP   CA  C    sing N N 410 
TRP   CA  CB   sing N N 411 
TRP   CA  HA   sing N N 412 
TRP   C   O    doub N N 413 
TRP   C   OXT  sing N N 414 
TRP   CB  CG   sing N N 415 
TRP   CB  HB2  sing N N 416 
TRP   CB  HB3  sing N N 417 
TRP   CG  CD1  doub Y N 418 
TRP   CG  CD2  sing Y N 419 
TRP   CD1 NE1  sing Y N 420 
TRP   CD1 HD1  sing N N 421 
TRP   CD2 CE2  doub Y N 422 
TRP   CD2 CE3  sing Y N 423 
TRP   NE1 CE2  sing Y N 424 
TRP   NE1 HE1  sing N N 425 
TRP   CE2 CZ2  sing Y N 426 
TRP   CE3 CZ3  doub Y N 427 
TRP   CE3 HE3  sing N N 428 
TRP   CZ2 CH2  doub Y N 429 
TRP   CZ2 HZ2  sing N N 430 
TRP   CZ3 CH2  sing Y N 431 
TRP   CZ3 HZ3  sing N N 432 
TRP   CH2 HH2  sing N N 433 
TRP   OXT HXT  sing N N 434 
TYR   N   CA   sing N N 435 
TYR   N   H    sing N N 436 
TYR   N   H2   sing N N 437 
TYR   CA  C    sing N N 438 
TYR   CA  CB   sing N N 439 
TYR   CA  HA   sing N N 440 
TYR   C   O    doub N N 441 
TYR   C   OXT  sing N N 442 
TYR   CB  CG   sing N N 443 
TYR   CB  HB2  sing N N 444 
TYR   CB  HB3  sing N N 445 
TYR   CG  CD1  doub Y N 446 
TYR   CG  CD2  sing Y N 447 
TYR   CD1 CE1  sing Y N 448 
TYR   CD1 HD1  sing N N 449 
TYR   CD2 CE2  doub Y N 450 
TYR   CD2 HD2  sing N N 451 
TYR   CE1 CZ   doub Y N 452 
TYR   CE1 HE1  sing N N 453 
TYR   CE2 CZ   sing Y N 454 
TYR   CE2 HE2  sing N N 455 
TYR   CZ  OH   sing N N 456 
TYR   OH  HH   sing N N 457 
TYR   OXT HXT  sing N N 458 
VAL   N   CA   sing N N 459 
VAL   N   H    sing N N 460 
VAL   N   H2   sing N N 461 
VAL   CA  C    sing N N 462 
VAL   CA  CB   sing N N 463 
VAL   CA  HA   sing N N 464 
VAL   C   O    doub N N 465 
VAL   C   OXT  sing N N 466 
VAL   CB  CG1  sing N N 467 
VAL   CB  CG2  sing N N 468 
VAL   CB  HB   sing N N 469 
VAL   CG1 HG11 sing N N 470 
VAL   CG1 HG12 sing N N 471 
VAL   CG1 HG13 sing N N 472 
VAL   CG2 HG21 sing N N 473 
VAL   CG2 HG22 sing N N 474 
VAL   CG2 HG23 sing N N 475 
VAL   OXT HXT  sing N N 476 
# 
_pdbx_audit_support.funding_organization   'Ministry of Science and Technology (MoST, China)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           2021YFA0911400 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9JN6 
_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]   0.011004 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009841 
_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]   0.008996 
_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  
FE 
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 4   ? -33.892 7.811   21.176  1.00 45.59 ?  -1  GLY   B N   1 
ATOM   2    C  CA  . GLY   A 1 4   ? -34.911 6.737   21.030  1.00 42.61 ?  -1  GLY   B CA  1 
ATOM   3    C  C   . GLY   A 1 4   ? -36.289 7.134   21.545  1.00 40.72 ?  -1  GLY   B C   1 
ATOM   4    O  O   . GLY   A 1 4   ? -36.507 8.315   21.908  1.00 43.55 ?  -1  GLY   B O   1 
ATOM   5    N  N   . ALA   A 1 5   ? -37.215 6.178   21.555  1.00 32.63 ?  0   ALA   B N   1 
ATOM   6    C  CA  . ALA   A 1 5   ? -38.624 6.389   21.940  1.00 32.33 ?  0   ALA   B CA  1 
ATOM   7    C  C   . ALA   A 1 5   ? -38.747 6.395   23.470  1.00 30.24 ?  0   ALA   B C   1 
ATOM   8    O  O   . ALA   A 1 5   ? -39.804 6.893   23.973  1.00 27.63 ?  0   ALA   B O   1 
ATOM   9    C  CB  . ALA   A 1 5   ? -39.477 5.321   21.351  1.00 33.12 ?  0   ALA   B CB  1 
ATOM   10   N  N   . MET   A 1 6   ? -37.773 5.803   24.172  1.00 27.27 ?  1   MET   B N   1 
ATOM   11   C  CA  . MET   A 1 6   ? -37.742 5.811   25.657  1.00 25.17 ?  1   MET   B CA  1 
ATOM   12   C  C   . MET   A 1 6   ? -36.446 6.466   26.133  1.00 24.37 ?  1   MET   B C   1 
ATOM   13   O  O   . MET   A 1 6   ? -35.352 6.088   25.658  1.00 26.95 ?  1   MET   B O   1 
ATOM   14   C  CB  . MET   A 1 6   ? -37.855 4.411   26.258  1.00 27.83 ?  1   MET   B CB  1 
ATOM   15   C  CG  . MET   A 1 6   ? -37.882 4.414   27.773  1.00 24.96 ?  1   MET   B CG  1 
ATOM   16   S  SD  . MET   A 1 6   ? -37.910 2.684   28.313  1.00 30.92 ?  1   MET   B SD  1 
ATOM   17   C  CE  . MET   A 1 6   ? -38.066 2.903   30.081  1.00 29.10 ?  1   MET   B CE  1 
ATOM   18   N  N   . PHE   A 1 7   ? -36.542 7.398   27.072  1.00 24.12 ?  2   PHE   B N   1 
ATOM   19   C  CA  . PHE   A 1 7   ? -35.355 8.080   27.635  1.00 23.65 ?  2   PHE   B CA  1 
ATOM   20   C  C   . PHE   A 1 7   ? -34.689 7.173   28.678  1.00 26.55 ?  2   PHE   B C   1 
ATOM   21   O  O   . PHE   A 1 7   ? -35.304 6.982   29.772  1.00 25.90 ?  2   PHE   B O   1 
ATOM   22   C  CB  . PHE   A 1 7   ? -35.773 9.418   28.242  1.00 23.49 ?  2   PHE   B CB  1 
ATOM   23   C  CG  . PHE   A 1 7   ? -34.613 10.198  28.793  1.00 25.22 ?  2   PHE   B CG  1 
ATOM   24   C  CD1 . PHE   A 1 7   ? -33.629 10.654  27.929  1.00 27.37 ?  2   PHE   B CD1 1 
ATOM   25   C  CD2 . PHE   A 1 7   ? -34.513 10.485  30.138  1.00 27.48 ?  2   PHE   B CD2 1 
ATOM   26   C  CE1 . PHE   A 1 7   ? -32.553 11.393  28.402  1.00 30.09 ?  2   PHE   B CE1 1 
ATOM   27   C  CE2 . PHE   A 1 7   ? -33.414 11.173  30.624  1.00 29.74 ?  2   PHE   B CE2 1 
ATOM   28   C  CZ  . PHE   A 1 7   ? -32.460 11.650  29.753  1.00 29.75 ?  2   PHE   B CZ  1 
ATOM   29   N  N   . VAL   A 1 8   ? -33.468 6.683   28.415  1.00 22.64 ?  3   VAL   B N   1 
ATOM   30   C  CA  . VAL   A 1 8   ? -32.752 5.813   29.392  1.00 22.86 ?  3   VAL   B CA  1 
ATOM   31   C  C   . VAL   A 1 8   ? -31.330 6.310   29.520  1.00 26.26 ?  3   VAL   B C   1 
ATOM   32   O  O   . VAL   A 1 8   ? -30.533 6.036   28.613  1.00 28.16 ?  3   VAL   B O   1 
ATOM   33   C  CB  . VAL   A 1 8   ? -32.784 4.321   29.030  1.00 25.57 ?  3   VAL   B CB  1 
ATOM   34   C  CG1 . VAL   A 1 8   ? -32.085 3.435   30.066  1.00 27.22 ?  3   VAL   B CG1 1 
ATOM   35   C  CG2 . VAL   A 1 8   ? -34.209 3.863   28.867  1.00 24.07 ?  3   VAL   B CG2 1 
ATOM   36   N  N   . PRO   A 1 9   ? -30.991 6.978   30.648  1.00 25.96 ?  4   PRO   B N   1 
ATOM   37   C  CA  . PRO   A 1 9   ? -29.620 7.409   30.912  1.00 28.27 ?  4   PRO   B CA  1 
ATOM   38   C  C   . PRO   A 1 9   ? -28.670 6.211   30.810  1.00 28.34 ?  4   PRO   B C   1 
ATOM   39   O  O   . PRO   A 1 9   ? -29.014 5.127   31.259  1.00 24.01 ?  4   PRO   B O   1 
ATOM   40   C  CB  . PRO   A 1 9   ? -29.631 7.964   32.347  1.00 28.78 ?  4   PRO   B CB  1 
ATOM   41   C  CG  . PRO   A 1 9   ? -31.097 8.311   32.601  1.00 31.28 ?  4   PRO   B CG  1 
ATOM   42   C  CD  . PRO   A 1 9   ? -31.888 7.329   31.758  1.00 28.81 ?  4   PRO   B CD  1 
ATOM   43   N  N   . GLY   A 1 10  ? -27.466 6.451   30.285  1.00 29.04 ?  5   GLY   B N   1 
ATOM   44   C  CA  . GLY   A 1 10  ? -26.453 5.416   30.014  1.00 28.70 ?  5   GLY   B CA  1 
ATOM   45   C  C   . GLY   A 1 10  ? -26.246 4.451   31.179  1.00 27.56 ?  5   GLY   B C   1 
ATOM   46   O  O   . GLY   A 1 10  ? -26.142 3.235   30.970  1.00 30.15 ?  5   GLY   B O   1 
ATOM   47   N  N   . PRO   A 1 11  ? -26.149 4.923   32.442  1.00 26.00 ?  6   PRO   B N   1 
ATOM   48   C  CA  . PRO   A 1 11  ? -25.865 4.006   33.545  1.00 27.38 ?  6   PRO   B CA  1 
ATOM   49   C  C   . PRO   A 1 11  ? -26.964 2.955   33.777  1.00 25.33 ?  6   PRO   B C   1 
ATOM   50   O  O   . PRO   A 1 11  ? -26.733 1.989   34.468  1.00 22.71 ?  6   PRO   B O   1 
ATOM   51   C  CB  . PRO   A 1 11  ? -25.758 4.900   34.787  1.00 29.21 ?  6   PRO   B CB  1 
ATOM   52   C  CG  . PRO   A 1 11  ? -25.587 6.311   34.260  1.00 32.04 ?  6   PRO   B CG  1 
ATOM   53   C  CD  . PRO   A 1 11  ? -26.167 6.322   32.860  1.00 30.06 ?  6   PRO   B CD  1 
ATOM   54   N  N   . TYR   A 1 12  ? -28.161 3.200   33.258  1.00 23.56 ?  7   TYR   B N   1 
ATOM   55   C  CA  . TYR   A 1 12  ? -29.346 2.381   33.575  1.00 21.52 ?  7   TYR   B CA  1 
ATOM   56   C  C   . TYR   A 1 12  ? -29.691 1.461   32.408  1.00 24.84 ?  7   TYR   B C   1 
ATOM   57   O  O   . TYR   A 1 12  ? -30.759 0.833   32.393  1.00 22.66 ?  7   TYR   B O   1 
ATOM   58   C  CB  . TYR   A 1 12  ? -30.494 3.303   33.936  1.00 22.40 ?  7   TYR   B CB  1 
ATOM   59   C  CG  . TYR   A 1 12  ? -30.226 4.192   35.106  1.00 21.78 ?  7   TYR   B CG  1 
ATOM   60   C  CD1 . TYR   A 1 12  ? -29.436 3.781   36.175  1.00 22.04 ?  7   TYR   B CD1 1 
ATOM   61   C  CD2 . TYR   A 1 12  ? -30.751 5.474   35.129  1.00 23.96 ?  7   TYR   B CD2 1 
ATOM   62   C  CE1 . TYR   A 1 12  ? -29.199 4.632   37.233  1.00 22.05 ?  7   TYR   B CE1 1 
ATOM   63   C  CE2 . TYR   A 1 12  ? -30.516 6.342   36.184  1.00 24.26 ?  7   TYR   B CE2 1 
ATOM   64   C  CZ  . TYR   A 1 12  ? -29.742 5.911   37.237  1.00 22.14 ?  7   TYR   B CZ  1 
ATOM   65   O  OH  . TYR   A 1 12  ? -29.522 6.743   38.290  1.00 26.84 ?  7   TYR   B OH  1 
ATOM   66   N  N   . HIS   A 1 13  ? -28.797 1.346   31.436  1.00 24.84 ?  8   HIS   B N   1 
ATOM   67   C  CA  . HIS   A 1 13  ? -28.936 0.318   30.373  1.00 25.04 ?  8   HIS   B CA  1 
ATOM   68   C  C   . HIS   A 1 13  ? -28.721 -1.061  30.998  1.00 23.65 ?  8   HIS   B C   1 
ATOM   69   O  O   . HIS   A 1 13  ? -27.824 -1.225  31.821  1.00 26.86 ?  8   HIS   B O   1 
ATOM   70   C  CB  . HIS   A 1 13  ? -27.959 0.615   29.224  1.00 28.47 ?  8   HIS   B CB  1 
ATOM   71   C  CG  . HIS   A 1 13  ? -28.371 1.782   28.390  1.00 34.45 ?  8   HIS   B CG  1 
ATOM   72   N  ND1 . HIS   A 1 13  ? -28.659 1.667   27.047  1.00 45.97 ?  8   HIS   B ND1 1 
ATOM   73   C  CD2 . HIS   A 1 13  ? -28.592 3.077   28.708  1.00 38.32 ?  8   HIS   B CD2 1 
ATOM   74   C  CE1 . HIS   A 1 13  ? -29.018 2.852   26.573  1.00 44.07 ?  8   HIS   B CE1 1 
ATOM   75   N  NE2 . HIS   A 1 13  ? -28.987 3.736   27.574  1.00 40.06 ?  8   HIS   B NE2 1 
ATOM   76   N  N   . ALA   A 1 14  ? -29.506 -2.059  30.596  1.00 24.95 ?  9   ALA   B N   1 
ATOM   77   C  CA  . ALA   A 1 14  ? -29.257 -3.449  31.002  1.00 26.73 ?  9   ALA   B CA  1 
ATOM   78   C  C   . ALA   A 1 14  ? -27.863 -3.854  30.528  1.00 28.52 ?  9   ALA   B C   1 
ATOM   79   O  O   . ALA   A 1 14  ? -27.400 -3.411  29.464  1.00 26.13 ?  9   ALA   B O   1 
ATOM   80   C  CB  . ALA   A 1 14  ? -30.295 -4.364  30.466  1.00 27.00 ?  9   ALA   B CB  1 
ATOM   81   N  N   . PRO   A 1 15  ? -27.184 -4.713  31.306  1.00 28.36 ?  10  PRO   B N   1 
ATOM   82   C  CA  . PRO   A 1 15  ? -25.929 -5.331  30.874  1.00 31.22 ?  10  PRO   B CA  1 
ATOM   83   C  C   . PRO   A 1 15  ? -26.027 -6.181  29.598  1.00 33.84 ?  10  PRO   B C   1 
ATOM   84   O  O   . PRO   A 1 15  ? -25.058 -6.267  28.888  1.00 32.63 ?  10  PRO   B O   1 
ATOM   85   C  CB  . PRO   A 1 15  ? -25.611 -6.280  32.040  1.00 33.39 ?  10  PRO   B CB  1 
ATOM   86   C  CG  . PRO   A 1 15  ? -26.298 -5.674  33.207  1.00 33.49 ?  10  PRO   B CG  1 
ATOM   87   C  CD  . PRO   A 1 15  ? -27.600 -5.180  32.643  1.00 31.66 ?  10  PRO   B CD  1 
ATOM   88   N  N   . GLU   A 1 16  ? -27.180 -6.818  29.361  1.00 30.74 ?  11  GLU   B N   1 
ATOM   89   C  CA  . GLU   A 1 16  ? -27.385 -7.813  28.268  1.00 33.99 ?  11  GLU   B CA  1 
ATOM   90   C  C   . GLU   A 1 16  ? -28.803 -7.633  27.747  1.00 30.81 ?  11  GLU   B C   1 
ATOM   91   O  O   . GLU   A 1 16  ? -29.677 -7.361  28.582  1.00 27.29 ?  11  GLU   B O   1 
ATOM   92   C  CB  . GLU   A 1 16  ? -27.295 -9.262  28.764  1.00 39.86 ?  11  GLU   B CB  1 
ATOM   93   C  CG  . GLU   A 1 16  ? -26.069 -9.603  29.589  1.00 48.67 ?  11  GLU   B CG  1 
ATOM   94   C  CD  . GLU   A 1 16  ? -24.822 -9.924  28.782  1.00 57.99 ?  11  GLU   B CD  1 
ATOM   95   O  OE1 . GLU   A 1 16  ? -24.667 -9.354  27.672  1.00 61.34 ?  11  GLU   B OE1 1 
ATOM   96   O  OE2 . GLU   A 1 16  ? -23.998 -10.737 29.270  1.00 70.83 -1 11  GLU   B OE2 1 
ATOM   97   N  N   . ASP   A 1 17  ? -29.031 -7.843  26.452  1.00 27.47 ?  12  ASP   B N   1 
ATOM   98   C  CA  . ASP   A 1 17  ? -30.391 -7.827  25.859  1.00 29.44 ?  12  ASP   B CA  1 
ATOM   99   C  C   . ASP   A 1 17  ? -31.308 -8.788  26.619  1.00 24.34 ?  12  ASP   B C   1 
ATOM   100  O  O   . ASP   A 1 17  ? -32.521 -8.508  26.680  1.00 25.42 ?  12  ASP   B O   1 
ATOM   101  C  CB  . ASP   A 1 17  ? -30.352 -8.193  24.373  1.00 31.09 ?  12  ASP   B CB  1 
ATOM   102  C  CG  . ASP   A 1 17  ? -29.643 -7.148  23.530  1.00 38.04 ?  12  ASP   B CG  1 
ATOM   103  O  OD1 . ASP   A 1 17  ? -29.897 -5.924  23.752  1.00 36.83 ?  12  ASP   B OD1 1 
ATOM   104  O  OD2 . ASP   A 1 17  ? -28.858 -7.563  22.651  1.00 40.20 -1 12  ASP   B OD2 1 
ATOM   105  N  N   . ARG   A 1 18  ? -30.785 -9.910  27.089  1.00 24.68 ?  13  ARG   B N   1 
ATOM   106  C  CA  . ARG   A 1 18  ? -31.575 -10.971 27.771  1.00 25.42 ?  13  ARG   B CA  1 
ATOM   107  C  C   . ARG   A 1 18  ? -32.349 -10.394 28.970  1.00 22.90 ?  13  ARG   B C   1 
ATOM   108  O  O   . ARG   A 1 18  ? -33.467 -10.910 29.225  1.00 24.17 ?  13  ARG   B O   1 
ATOM   109  C  CB  . ARG   A 1 18  ? -30.697 -12.138 28.228  1.00 28.45 ?  13  ARG   B CB  1 
ATOM   110  C  CG  . ARG   A 1 18  ? -31.448 -13.243 28.958  1.00 34.47 ?  13  ARG   B CG  1 
ATOM   111  C  CD  . ARG   A 1 18  ? -32.504 -13.943 28.137  1.00 37.91 ?  13  ARG   B CD  1 
ATOM   112  N  NE  . ARG   A 1 18  ? -31.849 -14.885 27.232  1.00 49.83 ?  13  ARG   B NE  1 
ATOM   113  C  CZ  . ARG   A 1 18  ? -31.667 -16.186 27.473  1.00 50.28 ?  13  ARG   B CZ  1 
ATOM   114  N  NH1 . ARG   A 1 18  ? -32.113 -16.734 28.592  1.00 48.08 1  13  ARG   B NH1 1 
ATOM   115  N  NH2 . ARG   A 1 18  ? -31.037 -16.935 26.580  1.00 53.38 ?  13  ARG   B NH2 1 
ATOM   116  N  N   . TRP   A 1 19  ? -31.831 -9.362  29.656  1.00 22.99 ?  14  TRP   B N   1 
ATOM   117  C  CA  . TRP   A 1 19  ? -32.500 -8.782  30.841  1.00 20.19 ?  14  TRP   B CA  1 
ATOM   118  C  C   . TRP   A 1 19  ? -33.887 -8.275  30.453  1.00 19.13 ?  14  TRP   B C   1 
ATOM   119  O  O   . TRP   A 1 19  ? -34.744 -8.281  31.329  1.00 20.24 ?  14  TRP   B O   1 
ATOM   120  C  CB  . TRP   A 1 19  ? -31.718 -7.662  31.489  1.00 23.29 ?  14  TRP   B CB  1 
ATOM   121  C  CG  . TRP   A 1 19  ? -30.559 -8.140  32.300  1.00 25.56 ?  14  TRP   B CG  1 
ATOM   122  C  CD1 . TRP   A 1 19  ? -29.653 -9.110  31.969  1.00 30.11 ?  14  TRP   B CD1 1 
ATOM   123  C  CD2 . TRP   A 1 19  ? -30.194 -7.668  33.597  1.00 25.10 ?  14  TRP   B CD2 1 
ATOM   124  N  NE1 . TRP   A 1 19  ? -28.745 -9.277  32.975  1.00 30.39 ?  14  TRP   B NE1 1 
ATOM   125  C  CE2 . TRP   A 1 19  ? -29.056 -8.410  33.992  1.00 28.48 ?  14  TRP   B CE2 1 
ATOM   126  C  CE3 . TRP   A 1 19  ? -30.722 -6.712  34.467  1.00 26.58 ?  14  TRP   B CE3 1 
ATOM   127  C  CZ2 . TRP   A 1 19  ? -28.421 -8.187  35.215  1.00 30.38 ?  14  TRP   B CZ2 1 
ATOM   128  C  CZ3 . TRP   A 1 19  ? -30.088 -6.490  35.665  1.00 28.89 ?  14  TRP   B CZ3 1 
ATOM   129  C  CH2 . TRP   A 1 19  ? -28.955 -7.219  36.033  1.00 26.95 ?  14  TRP   B CH2 1 
ATOM   130  N  N   . LEU   A 1 20  ? -34.040 -7.708  29.258  1.00 20.84 ?  15  LEU   B N   1 
ATOM   131  C  CA  . LEU   A 1 20  ? -35.338 -7.137  28.843  1.00 20.30 ?  15  LEU   B CA  1 
ATOM   132  C  C   . LEU   A 1 20  ? -36.321 -8.296  28.638  1.00 19.29 ?  15  LEU   B C   1 
ATOM   133  O  O   . LEU   A 1 20  ? -37.516 -8.138  28.940  1.00 19.22 ?  15  LEU   B O   1 
ATOM   134  C  CB  . LEU   A 1 20  ? -35.160 -6.303  27.571  1.00 20.54 ?  15  LEU   B CB  1 
ATOM   135  C  CG  . LEU   A 1 20  ? -34.530 -4.936  27.764  1.00 20.58 ?  15  LEU   B CG  1 
ATOM   136  C  CD1 . LEU   A 1 20  ? -33.014 -5.034  27.870  1.00 21.27 ?  15  LEU   B CD1 1 
ATOM   137  C  CD2 . LEU   A 1 20  ? -34.911 -3.983  26.647  1.00 22.99 ?  15  LEU   B CD2 1 
ATOM   138  N  N   . VAL   A 1 21  ? -35.877 -9.368  27.985  1.00 19.71 ?  16  VAL   B N   1 
ATOM   139  C  CA  . VAL   A 1 21  ? -36.729 -10.556 27.734  1.00 19.90 ?  16  VAL   B CA  1 
ATOM   140  C  C   . VAL   A 1 21  ? -37.116 -11.114 29.098  1.00 18.87 ?  16  VAL   B C   1 
ATOM   141  O  O   . VAL   A 1 21  ? -38.290 -11.437 29.303  1.00 18.09 ?  16  VAL   B O   1 
ATOM   142  C  CB  . VAL   A 1 21  ? -36.036 -11.639 26.887  1.00 22.28 ?  16  VAL   B CB  1 
ATOM   143  C  CG1 . VAL   A 1 21  ? -36.949 -12.824 26.734  1.00 22.21 ?  16  VAL   B CG1 1 
ATOM   144  C  CG2 . VAL   A 1 21  ? -35.570 -11.121 25.530  1.00 25.58 ?  16  VAL   B CG2 1 
ATOM   145  N  N   . ASP   A 1 22  ? -36.174 -11.204 30.018  1.00 19.21 ?  17  ASP   B N   1 
ATOM   146  C  CA  . ASP   A 1 22  ? -36.465 -11.776 31.356  1.00 20.54 ?  17  ASP   B CA  1 
ATOM   147  C  C   . ASP   A 1 22  ? -37.553 -10.943 32.044  1.00 18.34 ?  17  ASP   B C   1 
ATOM   148  O  O   . ASP   A 1 22  ? -38.371 -11.521 32.784  1.00 18.75 ?  17  ASP   B O   1 
ATOM   149  C  CB  . ASP   A 1 22  ? -35.268 -11.781 32.298  1.00 24.44 ?  17  ASP   B CB  1 
ATOM   150  C  CG  . ASP   A 1 22  ? -34.138 -12.735 31.930  1.00 29.67 ?  17  ASP   B CG  1 
ATOM   151  O  OD1 . ASP   A 1 22  ? -34.396 -13.670 31.158  1.00 27.34 ?  17  ASP   B OD1 1 
ATOM   152  O  OD2 . ASP   A 1 22  ? -32.986 -12.499 32.417  1.00 34.30 -1 17  ASP   B OD2 1 
ATOM   153  N  N   . LEU   A 1 23  ? -37.510 -9.620  31.897  1.00 17.51 ?  18  LEU   B N   1 
ATOM   154  C  CA  . LEU   A 1 23  ? -38.471 -8.753  32.633  1.00 19.44 ?  18  LEU   B CA  1 
ATOM   155  C  C   . LEU   A 1 23  ? -39.849 -8.988  32.012  1.00 18.03 ?  18  LEU   B C   1 
ATOM   156  O  O   . LEU   A 1 23  ? -40.866 -9.087  32.743  1.00 18.62 ?  18  LEU   B O   1 
ATOM   157  C  CB  . LEU   A 1 23  ? -38.040 -7.278  32.583  1.00 20.97 ?  18  LEU   B CB  1 
ATOM   158  C  CG  . LEU   A 1 23  ? -38.800 -6.356  33.533  1.00 24.48 ?  18  LEU   B CG  1 
ATOM   159  C  CD1 . LEU   A 1 23  ? -38.092 -5.026  33.718  1.00 28.96 ?  18  LEU   B CD1 1 
ATOM   160  C  CD2 . LEU   A 1 23  ? -40.194 -6.050  32.991  1.00 31.25 ?  18  LEU   B CD2 1 
ATOM   161  N  N   . VAL   A 1 24  ? -39.912 -9.066  30.687  1.00 18.13 ?  19  VAL   B N   1 
ATOM   162  C  CA  . VAL   A 1 24  ? -41.205 -9.336  30.006  1.00 17.12 ?  19  VAL   B CA  1 
ATOM   163  C  C   . VAL   A 1 24  ? -41.795 -10.660 30.510  1.00 18.70 ?  19  VAL   B C   1 
ATOM   164  O  O   . VAL   A 1 24  ? -43.022 -10.741 30.799  1.00 19.06 ?  19  VAL   B O   1 
ATOM   165  C  CB  . VAL   A 1 24  ? -41.022 -9.310  28.475  1.00 18.92 ?  19  VAL   B CB  1 
ATOM   166  C  CG1 . VAL   A 1 24  ? -42.186 -9.959  27.782  1.00 18.21 ?  19  VAL   B CG1 1 
ATOM   167  C  CG2 . VAL   A 1 24  ? -40.864 -7.879  28.000  1.00 19.52 ?  19  VAL   B CG2 1 
ATOM   168  N  N   . ARG   A 1 25  ? -40.991 -11.695 30.593  1.00 17.95 ?  20  ARG   B N   1 
ATOM   169  C  CA  . ARG   A 1 25  ? -41.453 -13.018 31.091  1.00 19.35 ?  20  ARG   B CA  1 
ATOM   170  C  C   . ARG   A 1 25  ? -41.882 -12.941 32.555  1.00 18.87 ?  20  ARG   B C   1 
ATOM   171  O  O   . ARG   A 1 25  ? -42.877 -13.592 32.935  1.00 18.14 ?  20  ARG   B O   1 
ATOM   172  C  CB  . ARG   A 1 25  ? -40.390 -14.091 30.885  1.00 22.08 ?  20  ARG   B CB  1 
ATOM   173  C  CG  . ARG   A 1 25  ? -40.124 -14.418 29.422  1.00 24.36 ?  20  ARG   B CG  1 
ATOM   174  C  CD  . ARG   A 1 25  ? -39.224 -15.640 29.414  1.00 27.77 ?  20  ARG   B CD  1 
ATOM   175  N  NE  . ARG   A 1 25  ? -38.532 -15.905 28.165  1.00 30.38 ?  20  ARG   B NE  1 
ATOM   176  C  CZ  . ARG   A 1 25  ? -39.037 -16.579 27.134  1.00 33.23 ?  20  ARG   B CZ  1 
ATOM   177  N  NH1 . ARG   A 1 25  ? -40.291 -17.008 27.140  1.00 29.10 1  20  ARG   B NH1 1 
ATOM   178  N  NH2 . ARG   A 1 25  ? -38.288 -16.763 26.060  1.00 32.66 ?  20  ARG   B NH2 1 
ATOM   179  N  N   . GLY   A 1 26  ? -41.173 -12.154 33.352  1.00 19.06 ?  21  GLY   B N   1 
ATOM   180  C  CA  . GLY   A 1 26  ? -41.415 -12.052 34.794  1.00 18.58 ?  21  GLY   B CA  1 
ATOM   181  C  C   . GLY   A 1 26  ? -42.669 -11.267 35.153  1.00 16.94 ?  21  GLY   B C   1 
ATOM   182  O  O   . GLY   A 1 26  ? -43.128 -11.435 36.290  1.00 17.55 ?  21  GLY   B O   1 
ATOM   183  N  N   . HIS   A 1 27  ? -43.104 -10.365 34.266  1.00 15.89 ?  22  HIS   B N   1 
ATOM   184  C  CA  . HIS   A 1 27  ? -44.096 -9.277  34.534  1.00 19.09 ?  22  HIS   B CA  1 
ATOM   185  C  C   . HIS   A 1 27  ? -45.022 -9.134  33.345  1.00 18.50 ?  22  HIS   B C   1 
ATOM   186  O  O   . HIS   A 1 27  ? -45.077 -8.079  32.705  1.00 18.66 ?  22  HIS   B O   1 
ATOM   187  C  CB  . HIS   A 1 27  ? -43.331 -8.000  34.921  1.00 19.92 ?  22  HIS   B CB  1 
ATOM   188  C  CG  . HIS   A 1 27  ? -42.355 -8.299  36.001  1.00 19.77 ?  22  HIS   B CG  1 
ATOM   189  N  ND1 . HIS   A 1 27  ? -42.750 -8.317  37.323  1.00 19.81 ?  22  HIS   B ND1 1 
ATOM   190  C  CD2 . HIS   A 1 27  ? -41.046 -8.657  35.988  1.00 18.77 ?  22  HIS   B CD2 1 
ATOM   191  C  CE1 . HIS   A 1 27  ? -41.711 -8.649  38.072  1.00 18.27 ?  22  HIS   B CE1 1 
ATOM   192  N  NE2 . HIS   A 1 27  ? -40.666 -8.849  37.282  1.00 18.00 ?  22  HIS   B NE2 1 
ATOM   193  N  N   . PRO   A 1 28  ? -45.786 -10.192 33.035  1.00 17.44 ?  23  PRO   B N   1 
ATOM   194  C  CA  . PRO   A 1 28  ? -46.582 -10.235 31.802  1.00 17.72 ?  23  PRO   B CA  1 
ATOM   195  C  C   . PRO   A 1 28  ? -47.793 -9.295  31.762  1.00 19.71 ?  23  PRO   B C   1 
ATOM   196  O  O   . PRO   A 1 28  ? -48.307 -9.117  30.656  1.00 17.67 ?  23  PRO   B O   1 
ATOM   197  C  CB  . PRO   A 1 28  ? -47.083 -11.673 31.699  1.00 18.39 ?  23  PRO   B CB  1 
ATOM   198  C  CG  . PRO   A 1 28  ? -47.064 -12.157 33.133  1.00 19.09 ?  23  PRO   B CG  1 
ATOM   199  C  CD  . PRO   A 1 28  ? -45.924 -11.427 33.824  1.00 16.86 ?  23  PRO   B CD  1 
ATOM   200  N  N   . LEU   A 1 29  ? -48.250 -8.769  32.909  1.00 17.08 ?  24  LEU   B N   1 
ATOM   201  C  CA  . LEU   A 1 29  ? -49.398 -7.839  32.895  1.00 16.30 ?  24  LEU   B CA  1 
ATOM   202  C  C   . LEU   A 1 29  ? -48.852 -6.446  32.541  1.00 16.69 ?  24  LEU   B C   1 
ATOM   203  O  O   . LEU   A 1 29  ? -48.482 -5.683  33.417  1.00 18.13 ?  24  LEU   B O   1 
ATOM   204  C  CB  . LEU   A 1 29  ? -50.196 -7.887  34.195  1.00 18.21 ?  24  LEU   B CB  1 
ATOM   205  C  CG  . LEU   A 1 29  ? -51.556 -7.184  34.114  1.00 20.06 ?  24  LEU   B CG  1 
ATOM   206  C  CD1 . LEU   A 1 29  ? -52.521 -8.000  33.282  1.00 19.79 ?  24  LEU   B CD1 1 
ATOM   207  C  CD2 . LEU   A 1 29  ? -52.142 -6.855  35.502  1.00 18.86 ?  24  LEU   B CD2 1 
ATOM   208  N  N   . ALA   A 1 30  ? -48.863 -6.133  31.250  1.00 16.70 ?  25  ALA   B N   1 
ATOM   209  C  CA  . ALA   A 1 30  ? -48.312 -4.896  30.674  1.00 17.21 ?  25  ALA   B CA  1 
ATOM   210  C  C   . ALA   A 1 30  ? -49.365 -3.808  30.615  1.00 16.27 ?  25  ALA   B C   1 
ATOM   211  O  O   . ALA   A 1 30  ? -50.605 -4.104  30.595  1.00 18.52 ?  25  ALA   B O   1 
ATOM   212  C  CB  . ALA   A 1 30  ? -47.786 -5.171  29.298  1.00 17.48 ?  25  ALA   B CB  1 
ATOM   213  N  N   . GLN   A 1 31  ? -48.879 -2.572  30.590  1.00 15.45 ?  26  GLN   B N   1 
ATOM   214  C  CA  . GLN   A 1 31  ? -49.741 -1.400  30.277  1.00 16.96 ?  26  GLN   B CA  1 
ATOM   215  C  C   . GLN   A 1 31  ? -49.605 -1.135  28.787  1.00 16.01 ?  26  GLN   B C   1 
ATOM   216  O  O   . GLN   A 1 31  ? -48.500 -0.795  28.279  1.00 15.57 ?  26  GLN   B O   1 
ATOM   217  C  CB  . GLN   A 1 31  ? -49.409 -0.168  31.097  1.00 17.07 ?  26  GLN   B CB  1 
ATOM   218  C  CG  . GLN   A 1 31  ? -49.651 -0.397  32.583  1.00 18.37 ?  26  GLN   B CG  1 
ATOM   219  C  CD  . GLN   A 1 31  ? -49.425 0.858   33.407  1.00 19.16 ?  26  GLN   B CD  1 
ATOM   220  O  OE1 . GLN   A 1 31  ? -49.659 1.968   32.944  1.00 22.75 ?  26  GLN   B OE1 1 
ATOM   221  N  NE2 . GLN   A 1 31  ? -49.004 0.682   34.662  1.00 20.63 ?  26  GLN   B NE2 1 
ATOM   222  N  N   . LEU   A 1 32  ? -50.686 -1.382  28.078  1.00 15.72 ?  27  LEU   B N   1 
ATOM   223  C  CA  . LEU   A 1 32  ? -50.720 -1.142  26.623  1.00 17.42 ?  27  LEU   B CA  1 
ATOM   224  C  C   . LEU   A 1 32  ? -51.256 0.278   26.402  1.00 17.29 ?  27  LEU   B C   1 
ATOM   225  O  O   . LEU   A 1 32  ? -52.346 0.522   26.832  1.00 18.03 ?  27  LEU   B O   1 
ATOM   226  C  CB  . LEU   A 1 32  ? -51.654 -2.176  25.996  1.00 18.70 ?  27  LEU   B CB  1 
ATOM   227  C  CG  . LEU   A 1 32  ? -51.849 -2.013  24.490  1.00 18.57 ?  27  LEU   B CG  1 
ATOM   228  C  CD1 . LEU   A 1 32  ? -50.572 -2.312  23.760  1.00 20.07 ?  27  LEU   B CD1 1 
ATOM   229  C  CD2 . LEU   A 1 32  ? -52.998 -2.867  23.985  1.00 19.52 ?  27  LEU   B CD2 1 
ATOM   230  N  N   . ALA   A 1 33  ? -50.519 1.114   25.693  1.00 18.33 ?  28  ALA   B N   1 
ATOM   231  C  CA  . ALA   A 1 33  ? -50.849 2.516   25.429  1.00 17.26 ?  28  ALA   B CA  1 
ATOM   232  C  C   . ALA   A 1 33  ? -50.921 2.774   23.913  1.00 17.67 ?  28  ALA   B C   1 
ATOM   233  O  O   . ALA   A 1 33  ? -50.015 2.379   23.176  1.00 17.71 ?  28  ALA   B O   1 
ATOM   234  C  CB  . ALA   A 1 33  ? -49.872 3.438   26.119  1.00 16.51 ?  28  ALA   B CB  1 
ATOM   235  N  N   . SER   A 1 34  ? -51.978 3.452   23.517  1.00 19.38 ?  29  SER   B N   1 
ATOM   236  C  CA  . SER   A 1 34  ? -52.127 4.049   22.179  1.00 21.53 ?  29  SER   B CA  1 
ATOM   237  C  C   . SER   A 1 34  ? -52.705 5.458   22.277  1.00 19.21 ?  29  SER   B C   1 
ATOM   238  O  O   . SER   A 1 34  ? -53.286 5.819   23.288  1.00 20.18 ?  29  SER   B O   1 
ATOM   239  C  CB  . SER   A 1 34  ? -52.969 3.167   21.323  1.00 22.65 ?  29  SER   B CB  1 
ATOM   240  O  OG  . SER   A 1 34  ? -54.290 3.020   21.821  1.00 20.81 ?  29  SER   B OG  1 
ATOM   241  N  N   . ASN   A 1 35  ? -52.590 6.214   21.202  1.00 20.15 ?  30  ASN   B N   1 
ATOM   242  C  CA  . ASN   A 1 35  ? -52.950 7.647   21.190  1.00 21.08 ?  30  ASN   B CA  1 
ATOM   243  C  C   . ASN   A 1 35  ? -54.453 7.803   21.405  1.00 21.74 ?  30  ASN   B C   1 
ATOM   244  O  O   . ASN   A 1 35  ? -55.219 6.998   20.843  1.00 21.97 ?  30  ASN   B O   1 
ATOM   245  C  CB  . ASN   A 1 35  ? -52.517 8.336   19.906  1.00 20.45 ?  30  ASN   B CB  1 
ATOM   246  C  CG  . ASN   A 1 35  ? -51.030 8.515   19.797  1.00 24.02 ?  30  ASN   B CG  1 
ATOM   247  O  OD1 . ASN   A 1 35  ? -50.325 8.442   20.794  1.00 24.31 ?  30  ASN   B OD1 1 
ATOM   248  N  ND2 . ASN   A 1 35  ? -50.578 8.899   18.610  1.00 29.09 ?  30  ASN   B ND2 1 
ATOM   249  N  N   . GLY   A 1 36  ? -54.856 8.831   22.152  1.00 21.46 ?  31  GLY   B N   1 
ATOM   250  C  CA  . GLY   A 1 36  ? -56.260 9.261   22.241  1.00 24.40 ?  31  GLY   B CA  1 
ATOM   251  C  C   . GLY   A 1 36  ? -56.604 10.001  20.965  1.00 26.53 ?  31  GLY   B C   1 
ATOM   252  O  O   . GLY   A 1 36  ? -55.671 10.512  20.297  1.00 28.73 ?  31  GLY   B O   1 
ATOM   253  N  N   . ALA   A 1 37  ? -57.879 9.975   20.589  1.00 31.09 ?  32  ALA   B N   1 
ATOM   254  C  CA  . ALA   A 1 37  ? -58.388 10.641  19.368  1.00 34.83 ?  32  ALA   B CA  1 
ATOM   255  C  C   . ALA   A 1 37  ? -58.517 12.124  19.686  1.00 36.85 ?  32  ALA   B C   1 
ATOM   256  O  O   . ALA   A 1 37  ? -58.887 12.419  20.861  1.00 34.84 ?  32  ALA   B O   1 
ATOM   257  C  CB  . ALA   A 1 37  ? -59.712 10.053  18.960  1.00 31.17 ?  32  ALA   B CB  1 
ATOM   258  N  N   . GLY   A 1 38  ? -58.204 12.970  18.691  1.00 42.03 ?  33  GLY   B N   1 
ATOM   259  C  CA  . GLY   A 1 38  ? -58.448 14.423  18.699  1.00 42.75 ?  33  GLY   B CA  1 
ATOM   260  C  C   . GLY   A 1 38  ? -57.916 15.042  19.976  1.00 49.13 ?  33  GLY   B C   1 
ATOM   261  O  O   . GLY   A 1 38  ? -58.724 15.585  20.753  1.00 50.89 ?  33  GLY   B O   1 
ATOM   262  N  N   . GLY   A 1 39  ? -56.618 14.854  20.231  1.00 44.07 ?  34  GLY   B N   1 
ATOM   263  C  CA  . GLY   A 1 39  ? -55.892 15.518  21.330  1.00 48.38 ?  34  GLY   B CA  1 
ATOM   264  C  C   . GLY   A 1 39  ? -56.110 14.897  22.710  1.00 41.10 ?  34  GLY   B C   1 
ATOM   265  O  O   . GLY   A 1 39  ? -55.408 15.358  23.635  1.00 44.39 ?  34  GLY   B O   1 
ATOM   266  N  N   . ALA   A 1 40  ? -56.993 13.897  22.869  1.00 36.60 ?  35  ALA   B N   1 
ATOM   267  C  CA  . ALA   A 1 40  ? -57.284 13.255  24.177  1.00 31.37 ?  35  ALA   B CA  1 
ATOM   268  C  C   . ALA   A 1 40  ? -56.040 12.516  24.654  1.00 26.44 ?  35  ALA   B C   1 
ATOM   269  O  O   . ALA   A 1 40  ? -55.117 12.294  23.859  1.00 27.94 ?  35  ALA   B O   1 
ATOM   270  C  CB  . ALA   A 1 40  ? -58.465 12.319  24.154  1.00 30.15 ?  35  ALA   B CB  1 
ATOM   271  N  N   . ALA   A 1 41  ? -55.977 12.258  25.955  1.00 25.53 ?  36  ALA   B N   1 
ATOM   272  C  CA  . ALA   A 1 41  ? -54.849 11.509  26.537  1.00 23.65 ?  36  ALA   B CA  1 
ATOM   273  C  C   . ALA   A 1 41  ? -54.905 10.090  25.975  1.00 22.08 ?  36  ALA   B C   1 
ATOM   274  O  O   . ALA   A 1 41  ? -55.956 9.592   25.539  1.00 19.76 ?  36  ALA   B O   1 
ATOM   275  C  CB  . ALA   A 1 41  ? -54.890 11.533  28.049  1.00 23.95 ?  36  ALA   B CB  1 
ATOM   276  N  N   . PRO   A 1 42  ? -53.762 9.397   25.942  1.00 19.55 ?  37  PRO   B N   1 
ATOM   277  C  CA  . PRO   A 1 42  ? -53.717 7.994   25.553  1.00 19.27 ?  37  PRO   B CA  1 
ATOM   278  C  C   . PRO   A 1 42  ? -54.722 7.094   26.289  1.00 18.33 ?  37  PRO   B C   1 
ATOM   279  O  O   . PRO   A 1 42  ? -55.038 7.317   27.470  1.00 17.91 ?  37  PRO   B O   1 
ATOM   280  C  CB  . PRO   A 1 42  ? -52.269 7.603   25.890  1.00 19.94 ?  37  PRO   B CB  1 
ATOM   281  C  CG  . PRO   A 1 42  ? -51.505 8.885   25.736  1.00 18.79 ?  37  PRO   B CG  1 
ATOM   282  C  CD  . PRO   A 1 42  ? -52.421 9.932   26.265  1.00 18.04 ?  37  PRO   B CD  1 
ATOM   283  N  N   . HIS   A 1 43  ? -55.184 6.052   25.595  1.00 19.75 ?  38  HIS   B N   1 
ATOM   284  C  CA  . HIS   A 1 43  ? -55.885 4.886   26.173  1.00 21.62 ?  38  HIS   B CA  1 
ATOM   285  C  C   . HIS   A 1 43  ? -54.827 3.984   26.790  1.00 20.42 ?  38  HIS   B C   1 
ATOM   286  O  O   . HIS   A 1 43  ? -53.764 3.830   26.150  1.00 19.50 ?  38  HIS   B O   1 
ATOM   287  C  CB  . HIS   A 1 43  ? -56.570 3.975   25.149  1.00 24.38 ?  38  HIS   B CB  1 
ATOM   288  C  CG  . HIS   A 1 43  ? -57.641 4.641   24.404  1.00 29.44 ?  38  HIS   B CG  1 
ATOM   289  N  ND1 . HIS   A 1 43  ? -58.954 4.464   24.746  1.00 37.22 ?  38  HIS   B ND1 1 
ATOM   290  C  CD2 . HIS   A 1 43  ? -57.586 5.393   23.292  1.00 30.22 ?  38  HIS   B CD2 1 
ATOM   291  C  CE1 . HIS   A 1 43  ? -59.692 5.123   23.870  1.00 37.80 ?  38  HIS   B CE1 1 
ATOM   292  N  NE2 . HIS   A 1 43  ? -58.873 5.735   22.994  1.00 33.81 ?  38  HIS   B NE2 1 
ATOM   293  N  N   . ILE   A 1 44  ? -55.075 3.525   28.016  1.00 18.41 ?  39  ILE   B N   1 
ATOM   294  C  CA  . ILE   A 1 44  ? -54.149 2.618   28.731  1.00 19.23 ?  39  ILE   B CA  1 
ATOM   295  C  C   . ILE   A 1 44  ? -54.954 1.429   29.244  1.00 18.47 ?  39  ILE   B C   1 
ATOM   296  O  O   . ILE   A 1 44  ? -55.986 1.633   29.913  1.00 19.03 ?  39  ILE   B O   1 
ATOM   297  C  CB  . ILE   A 1 44  ? -53.471 3.325   29.916  1.00 22.07 ?  39  ILE   B CB  1 
ATOM   298  C  CG1 . ILE   A 1 44  ? -52.835 4.673   29.560  1.00 21.06 ?  39  ILE   B CG1 1 
ATOM   299  C  CG2 . ILE   A 1 44  ? -52.504 2.363   30.574  1.00 24.20 ?  39  ILE   B CG2 1 
ATOM   300  C  CD1 . ILE   A 1 44  ? -51.420 4.495   29.088  1.00 20.99 ?  39  ILE   B CD1 1 
ATOM   301  N  N   . THR   A 1 45  ? -54.553 0.211   28.864  1.00 16.95 ?  40  THR   B N   1 
ATOM   302  C  CA  . THR   A 1 45  ? -55.174 -1.016  29.353  1.00 17.47 ?  40  THR   B CA  1 
ATOM   303  C  C   . THR   A 1 45  ? -54.123 -1.978  29.884  1.00 17.19 ?  40  THR   B C   1 
ATOM   304  O  O   . THR   A 1 45  ? -53.097 -2.168  29.169  1.00 16.95 ?  40  THR   B O   1 
ATOM   305  C  CB  . THR   A 1 45  ? -56.014 -1.687  28.252  1.00 18.07 ?  40  THR   B CB  1 
ATOM   306  O  OG1 . THR   A 1 45  ? -56.963 -0.710  27.799  1.00 17.83 ?  40  THR   B OG1 1 
ATOM   307  C  CG2 . THR   A 1 45  ? -56.736 -2.879  28.843  1.00 18.68 ?  40  THR   B CG2 1 
ATOM   308  N  N   . HIS   A 1 46  ? -54.380 -2.546  31.071  1.00 17.49 ?  41  HIS   B N   1 
ATOM   309  C  CA  . HIS   A 1 46  ? -53.574 -3.680  31.591  1.00 16.61 ?  41  HIS   B CA  1 
ATOM   310  C  C   . HIS   A 1 46  ? -53.959 -4.955  30.884  1.00 16.04 ?  41  HIS   B C   1 
ATOM   311  O  O   . HIS   A 1 46  ? -55.116 -5.364  30.963  1.00 18.18 ?  41  HIS   B O   1 
ATOM   312  C  CB  . HIS   A 1 46  ? -53.688 -3.853  33.066  1.00 16.91 ?  41  HIS   B CB  1 
ATOM   313  C  CG  . HIS   A 1 46  ? -53.089 -2.736  33.834  1.00 21.70 ?  41  HIS   B CG  1 
ATOM   314  N  ND1 . HIS   A 1 46  ? -51.894 -2.819  34.462  1.00 28.78 ?  41  HIS   B ND1 1 
ATOM   315  C  CD2 . HIS   A 1 46  ? -53.564 -1.508  34.057  1.00 26.78 ?  41  HIS   B CD2 1 
ATOM   316  C  CE1 . HIS   A 1 46  ? -51.629 -1.668  35.052  1.00 28.68 ?  41  HIS   B CE1 1 
ATOM   317  N  NE2 . HIS   A 1 46  ? -52.635 -0.841  34.799  1.00 28.63 ?  41  HIS   B NE2 1 
ATOM   318  N  N   . VAL   A 1 47  ? -53.025 -5.538  30.181  1.00 14.76 ?  42  VAL   B N   1 
ATOM   319  C  CA  . VAL   A 1 47  ? -53.249 -6.746  29.351  1.00 15.32 ?  42  VAL   B CA  1 
ATOM   320  C  C   . VAL   A 1 47  ? -52.120 -7.735  29.527  1.00 14.22 ?  42  VAL   B C   1 
ATOM   321  O  O   . VAL   A 1 47  ? -50.932 -7.348  29.664  1.00 15.09 ?  42  VAL   B O   1 
ATOM   322  C  CB  . VAL   A 1 47  ? -53.375 -6.362  27.864  1.00 17.48 ?  42  VAL   B CB  1 
ATOM   323  C  CG1 . VAL   A 1 47  ? -54.601 -5.502  27.616  1.00 22.02 ?  42  VAL   B CG1 1 
ATOM   324  C  CG2 . VAL   A 1 47  ? -52.149 -5.620  27.326  1.00 19.34 ?  42  VAL   B CG2 1 
ATOM   325  N  N   . PRO   A 1 48  ? -52.486 -9.025  29.530  1.00 15.84 ?  43  PRO   B N   1 
ATOM   326  C  CA  . PRO   A 1 48  ? -51.489 -10.088 29.638  1.00 16.97 ?  43  PRO   B CA  1 
ATOM   327  C  C   . PRO   A 1 48  ? -50.812 -10.267 28.297  1.00 16.49 ?  43  PRO   B C   1 
ATOM   328  O  O   . PRO   A 1 48  ? -51.491 -10.541 27.274  1.00 16.94 ?  43  PRO   B O   1 
ATOM   329  C  CB  . PRO   A 1 48  ? -52.309 -11.330 30.030  1.00 16.37 ?  43  PRO   B CB  1 
ATOM   330  C  CG  . PRO   A 1 48  ? -53.686 -11.044 29.460  1.00 18.69 ?  43  PRO   B CG  1 
ATOM   331  C  CD  . PRO   A 1 48  ? -53.866 -9.542  29.477  1.00 16.04 ?  43  PRO   B CD  1 
ATOM   332  N  N   . ILE   A 1 49  ? -49.483 -10.243 28.322  1.00 17.27 ?  44  ILE   B N   1 
ATOM   333  C  CA  . ILE   A 1 49  ? -48.696 -10.322 27.065  1.00 17.54 ?  44  ILE   B CA  1 
ATOM   334  C  C   . ILE   A 1 49  ? -47.558 -11.320 27.245  1.00 19.76 ?  44  ILE   B C   1 
ATOM   335  O  O   . ILE   A 1 49  ? -46.872 -11.239 28.269  1.00 19.10 ?  44  ILE   B O   1 
ATOM   336  C  CB  . ILE   A 1 49  ? -48.175 -8.938  26.608  1.00 16.48 ?  44  ILE   B CB  1 
ATOM   337  C  CG1 . ILE   A 1 49  ? -49.323 -7.974  26.296  1.00 16.43 ?  44  ILE   B CG1 1 
ATOM   338  C  CG2 . ILE   A 1 49  ? -47.244 -9.140  25.433  1.00 16.41 ?  44  ILE   B CG2 1 
ATOM   339  C  CD1 . ILE   A 1 49  ? -48.852 -6.616  25.815  1.00 19.28 ?  44  ILE   B CD1 1 
ATOM   340  N  N   . ILE   A 1 50  ? -47.363 -12.211 26.264  1.00 18.22 ?  45  ILE   B N   1 
ATOM   341  C  CA  . ILE   A 1 50  ? -46.338 -13.298 26.308  1.00 19.18 ?  45  ILE   B CA  1 
ATOM   342  C  C   . ILE   A 1 50  ? -45.498 -13.259 25.048  1.00 19.61 ?  45  ILE   B C   1 
ATOM   343  O  O   . ILE   A 1 50  ? -45.939 -12.762 24.009  1.00 18.41 ?  45  ILE   B O   1 
ATOM   344  C  CB  . ILE   A 1 50  ? -46.922 -14.715 26.506  1.00 19.65 ?  45  ILE   B CB  1 
ATOM   345  C  CG1 . ILE   A 1 50  ? -47.847 -15.156 25.354  1.00 21.08 ?  45  ILE   B CG1 1 
ATOM   346  C  CG2 . ILE   A 1 50  ? -47.590 -14.850 27.860  1.00 19.42 ?  45  ILE   B CG2 1 
ATOM   347  C  CD1 . ILE   A 1 50  ? -48.068 -16.659 25.306  1.00 21.86 ?  45  ILE   B CD1 1 
ATOM   348  N  N   . VAL   A 1 51  ? -44.276 -13.751 25.163  1.00 21.03 ?  46  VAL   B N   1 
ATOM   349  C  CA  . VAL   A 1 51  ? -43.439 -14.028 23.975  1.00 20.56 ?  46  VAL   B CA  1 
ATOM   350  C  C   . VAL   A 1 51  ? -44.075 -15.126 23.125  1.00 19.67 ?  46  VAL   B C   1 
ATOM   351  O  O   . VAL   A 1 51  ? -44.584 -16.125 23.646  1.00 21.33 ?  46  VAL   B O   1 
ATOM   352  C  CB  . VAL   A 1 51  ? -42.036 -14.425 24.473  1.00 23.76 ?  46  VAL   B CB  1 
ATOM   353  C  CG1 . VAL   A 1 51  ? -41.189 -15.029 23.354  1.00 25.45 ?  46  VAL   B CG1 1 
ATOM   354  C  CG2 . VAL   A 1 51  ? -41.371 -13.236 25.128  1.00 24.66 ?  46  VAL   B CG2 1 
ATOM   355  N  N   . ASP   A 1 52  ? -44.023 -14.965 21.818  1.00 22.96 ?  47  ASP   B N   1 
ATOM   356  C  CA  . ASP   A 1 52  ? -44.384 -15.974 20.803  1.00 22.26 ?  47  ASP   B CA  1 
ATOM   357  C  C   . ASP   A 1 52  ? -44.023 -17.351 21.327  1.00 20.03 ?  47  ASP   B C   1 
ATOM   358  O  O   . ASP   A 1 52  ? -42.861 -17.640 21.533  1.00 21.30 ?  47  ASP   B O   1 
ATOM   359  C  CB  . ASP   A 1 52  ? -43.622 -15.673 19.526  1.00 22.70 ?  47  ASP   B CB  1 
ATOM   360  C  CG  . ASP   A 1 52  ? -43.829 -16.651 18.393  1.00 24.98 ?  47  ASP   B CG  1 
ATOM   361  O  OD1 . ASP   A 1 52  ? -44.703 -17.570 18.503  1.00 25.97 ?  47  ASP   B OD1 1 
ATOM   362  O  OD2 . ASP   A 1 52  ? -43.173 -16.405 17.351  1.00 26.99 -1 47  ASP   B OD2 1 
ATOM   363  N  N   . PRO   A 1 53  ? -45.009 -18.213 21.572  1.00 21.66 ?  48  PRO   B N   1 
ATOM   364  C  CA  . PRO   A 1 53  ? -44.734 -19.552 22.109  1.00 23.26 ?  48  PRO   B CA  1 
ATOM   365  C  C   . PRO   A 1 53  ? -44.061 -20.506 21.113  1.00 24.80 ?  48  PRO   B C   1 
ATOM   366  O  O   . PRO   A 1 53  ? -43.618 -21.551 21.536  1.00 25.76 ?  48  PRO   B O   1 
ATOM   367  C  CB  . PRO   A 1 53  ? -46.141 -20.078 22.434  1.00 25.97 ?  48  PRO   B CB  1 
ATOM   368  C  CG  . PRO   A 1 53  ? -47.060 -19.322 21.552  1.00 24.81 ?  48  PRO   B CG  1 
ATOM   369  C  CD  . PRO   A 1 53  ? -46.449 -17.951 21.395  1.00 24.86 ?  48  PRO   B CD  1 
ATOM   370  N  N   . GLU   A 1 54  ? -44.026 -20.131 19.834  1.00 24.41 ?  49  GLU   B N   1 
ATOM   371  C  CA  . GLU   A 1 54  ? -43.447 -20.975 18.757  1.00 25.03 ?  49  GLU   B CA  1 
ATOM   372  C  C   . GLU   A 1 54  ? -41.923 -20.759 18.680  1.00 29.30 ?  49  GLU   B C   1 
ATOM   373  O  O   . GLU   A 1 54  ? -41.274 -21.504 17.929  1.00 30.78 ?  49  GLU   B O   1 
ATOM   374  C  CB  . GLU   A 1 54  ? -44.184 -20.693 17.453  1.00 26.78 ?  49  GLU   B CB  1 
ATOM   375  C  CG  . GLU   A 1 54  ? -45.679 -20.965 17.555  1.00 25.93 ?  49  GLU   B CG  1 
ATOM   376  C  CD  . GLU   A 1 54  ? -46.081 -22.336 18.098  1.00 31.17 ?  49  GLU   B CD  1 
ATOM   377  O  OE1 . GLU   A 1 54  ? -45.450 -23.380 17.699  1.00 36.83 ?  49  GLU   B OE1 1 
ATOM   378  O  OE2 . GLU   A 1 54  ? -47.022 -22.382 18.918  1.00 33.19 -1 49  GLU   B OE2 1 
ATOM   379  N  N   . LEU   A 1 55  ? -41.340 -19.795 19.399  1.00 26.02 ?  50  LEU   B N   1 
ATOM   380  C  CA  . LEU   A 1 55  ? -39.881 -19.608 19.335  1.00 31.87 ?  50  LEU   B CA  1 
ATOM   381  C  C   . LEU   A 1 55  ? -39.182 -20.790 20.003  1.00 37.81 ?  50  LEU   B C   1 
ATOM   382  O  O   . LEU   A 1 55  ? -39.544 -21.142 21.145  1.00 37.20 ?  50  LEU   B O   1 
ATOM   383  C  CB  . LEU   A 1 55  ? -39.503 -18.276 19.978  1.00 33.01 ?  50  LEU   B CB  1 
ATOM   384  C  CG  . LEU   A 1 55  ? -40.020 -17.065 19.222  1.00 31.88 ?  50  LEU   B CG  1 
ATOM   385  C  CD1 . LEU   A 1 55  ? -39.687 -15.797 19.981  1.00 31.78 ?  50  LEU   B CD1 1 
ATOM   386  C  CD2 . LEU   A 1 55  ? -39.443 -17.002 17.819  1.00 36.21 ?  50  LEU   B CD2 1 
ATOM   387  N  N   . ASP   A 1 56  ? -38.264 -21.392 19.258  1.00 44.38 ?  51  ASP   B N   1 
ATOM   388  C  CA  . ASP   A 1 56  ? -37.202 -22.294 19.769  1.00 55.17 ?  51  ASP   B CA  1 
ATOM   389  C  C   . ASP   A 1 56  ? -35.891 -21.507 19.770  1.00 62.26 ?  51  ASP   B C   1 
ATOM   390  O  O   . ASP   A 1 56  ? -35.833 -20.399 19.165  1.00 63.12 ?  51  ASP   B O   1 
ATOM   391  C  CB  . ASP   A 1 56  ? -37.020 -23.533 18.887  1.00 60.00 ?  51  ASP   B CB  1 
ATOM   392  C  CG  . ASP   A 1 56  ? -38.324 -24.169 18.440  1.00 66.80 ?  51  ASP   B CG  1 
ATOM   393  O  OD1 . ASP   A 1 56  ? -38.850 -25.012 19.204  1.00 62.49 ?  51  ASP   B OD1 1 
ATOM   394  O  OD2 . ASP   A 1 56  ? -38.817 -23.800 17.340  1.00 69.81 -1 51  ASP   B OD2 1 
ATOM   395  N  N   . GLY   A 1 57  ? -34.869 -22.096 20.378  1.00 63.76 ?  52  GLY   B N   1 
ATOM   396  C  CA  . GLY   A 1 57  ? -33.571 -21.454 20.625  1.00 65.34 ?  52  GLY   B CA  1 
ATOM   397  C  C   . GLY   A 1 57  ? -33.678 -20.505 21.812  1.00 65.38 ?  52  GLY   B C   1 
ATOM   398  O  O   . GLY   A 1 57  ? -34.787 -20.185 22.256  1.00 64.04 ?  52  GLY   B O   1 
ATOM   399  N  N   . PRO   A 1 58  ? -32.529 -20.055 22.365  1.00 61.34 ?  53  PRO   B N   1 
ATOM   400  C  CA  . PRO   A 1 58  ? -32.528 -19.001 23.376  1.00 55.08 ?  53  PRO   B CA  1 
ATOM   401  C  C   . PRO   A 1 58  ? -33.153 -17.747 22.756  1.00 45.06 ?  53  PRO   B C   1 
ATOM   402  O  O   . PRO   A 1 58  ? -32.873 -17.476 21.593  1.00 43.47 ?  53  PRO   B O   1 
ATOM   403  C  CB  . PRO   A 1 58  ? -31.039 -18.796 23.700  1.00 58.86 ?  53  PRO   B CB  1 
ATOM   404  C  CG  . PRO   A 1 58  ? -30.375 -20.088 23.254  1.00 59.84 ?  53  PRO   B CG  1 
ATOM   405  C  CD  . PRO   A 1 58  ? -31.174 -20.539 22.053  1.00 61.05 ?  53  PRO   B CD  1 
ATOM   406  N  N   . VAL   A 1 59  ? -34.001 -17.046 23.513  1.00 41.34 ?  54  VAL   B N   1 
ATOM   407  C  CA  . VAL   A 1 59  ? -34.547 -15.722 23.113  1.00 33.48 ?  54  VAL   B CA  1 
ATOM   408  C  C   . VAL   A 1 59  ? -33.766 -14.649 23.868  1.00 31.72 ?  54  VAL   B C   1 
ATOM   409  O  O   . VAL   A 1 59  ? -34.015 -14.454 25.069  1.00 28.54 ?  54  VAL   B O   1 
ATOM   410  C  CB  . VAL   A 1 59  ? -36.064 -15.657 23.358  1.00 34.00 ?  54  VAL   B CB  1 
ATOM   411  C  CG1 . VAL   A 1 59  ? -36.646 -14.336 22.901  1.00 33.73 ?  54  VAL   B CG1 1 
ATOM   412  C  CG2 . VAL   A 1 59  ? -36.746 -16.828 22.655  1.00 35.90 ?  54  VAL   B CG2 1 
ATOM   413  N  N   . ASP   A 1 60  ? -32.828 -13.991 23.188  1.00 33.02 ?  55  ASP   B N   1 
ATOM   414  C  CA  . ASP   A 1 60  ? -31.911 -12.998 23.808  1.00 35.21 ?  55  ASP   B CA  1 
ATOM   415  C  C   . ASP   A 1 60  ? -32.370 -11.563 23.551  1.00 34.30 ?  55  ASP   B C   1 
ATOM   416  O  O   . ASP   A 1 60  ? -31.983 -10.695 24.354  1.00 37.05 ?  55  ASP   B O   1 
ATOM   417  C  CB  . ASP   A 1 60  ? -30.482 -13.196 23.302  1.00 41.99 ?  55  ASP   B CB  1 
ATOM   418  C  CG  . ASP   A 1 60  ? -29.905 -14.541 23.720  1.00 48.55 ?  55  ASP   B CG  1 
ATOM   419  O  OD1 . ASP   A 1 60  ? -30.028 -14.869 24.919  1.00 49.01 ?  55  ASP   B OD1 1 
ATOM   420  O  OD2 . ASP   A 1 60  ? -29.373 -15.264 22.839  1.00 56.37 -1 55  ASP   B OD2 1 
ATOM   421  N  N   . ARG   A 1 61  ? -33.135 -11.318 22.483  1.00 28.70 ?  56  ARG   B N   1 
ATOM   422  C  CA  . ARG   A 1 61  ? -33.506 -9.968  22.009  1.00 29.33 ?  56  ARG   B CA  1 
ATOM   423  C  C   . ARG   A 1 61  ? -35.015 -9.916  21.795  1.00 26.45 ?  56  ARG   B C   1 
ATOM   424  O  O   . ARG   A 1 61  ? -35.558 -10.833 21.168  1.00 27.85 ?  56  ARG   B O   1 
ATOM   425  C  CB  . ARG   A 1 61  ? -32.815 -9.630  20.689  1.00 34.24 ?  56  ARG   B CB  1 
ATOM   426  C  CG  . ARG   A 1 61  ? -31.505 -8.883  20.874  1.00 46.08 ?  56  ARG   B CG  1 
ATOM   427  C  CD  . ARG   A 1 61  ? -30.635 -8.864  19.628  1.00 50.59 ?  56  ARG   B CD  1 
ATOM   428  N  NE  . ARG   A 1 61  ? -29.740 -10.007 19.716  1.00 61.33 ?  56  ARG   B NE  1 
ATOM   429  C  CZ  . ARG   A 1 61  ? -29.912 -11.180 19.114  1.00 58.79 ?  56  ARG   B CZ  1 
ATOM   430  N  NH1 . ARG   A 1 61  ? -29.038 -12.150 19.325  1.00 59.47 1  56  ARG   B NH1 1 
ATOM   431  N  NH2 . ARG   A 1 61  ? -30.942 -11.387 18.312  1.00 63.55 ?  56  ARG   B NH2 1 
ATOM   432  N  N   . LEU   A 1 62  ? -35.639 -8.822  22.200  1.00 24.78 ?  57  LEU   B N   1 
ATOM   433  C  CA  . LEU   A 1 62  ? -37.093 -8.610  21.925  1.00 21.95 ?  57  LEU   B CA  1 
ATOM   434  C  C   . LEU   A 1 62  ? -37.289 -8.080  20.514  1.00 23.25 ?  57  LEU   B C   1 
ATOM   435  O  O   . LEU   A 1 62  ? -38.344 -8.385  19.927  1.00 25.31 ?  57  LEU   B O   1 
ATOM   436  C  CB  . LEU   A 1 62  ? -37.657 -7.601  22.925  1.00 22.64 ?  57  LEU   B CB  1 
ATOM   437  C  CG  . LEU   A 1 62  ? -37.865 -8.126  24.329  1.00 22.16 ?  57  LEU   B CG  1 
ATOM   438  C  CD1 . LEU   A 1 62  ? -38.233 -6.987  25.271  1.00 24.04 ?  57  LEU   B CD1 1 
ATOM   439  C  CD2 . LEU   A 1 62  ? -38.924 -9.210  24.343  1.00 22.76 ?  57  LEU   B CD2 1 
ATOM   440  N  N   . VAL   A 1 63  ? -36.360 -7.270  19.999  1.00 23.99 ?  58  VAL   B N   1 
ATOM   441  C  CA  . VAL   A 1 63  ? -36.568 -6.639  18.666  1.00 23.48 ?  58  VAL   B CA  1 
ATOM   442  C  C   . VAL   A 1 63  ? -36.635 -7.757  17.617  1.00 25.22 ?  58  VAL   B C   1 
ATOM   443  O  O   . VAL   A 1 63  ? -35.694 -8.549  17.541  1.00 26.25 ?  58  VAL   B O   1 
ATOM   444  C  CB  . VAL   A 1 63  ? -35.527 -5.565  18.295  1.00 25.65 ?  58  VAL   B CB  1 
ATOM   445  C  CG1 . VAL   A 1 63  ? -35.639 -5.191  16.817  1.00 25.34 ?  58  VAL   B CG1 1 
ATOM   446  C  CG2 . VAL   A 1 63  ? -35.670 -4.319  19.161  1.00 29.26 ?  58  VAL   B CG2 1 
ATOM   447  N  N   . GLY   A 1 64  ? -37.745 -7.821  16.877  1.00 24.21 ?  59  GLY   B N   1 
ATOM   448  C  CA  . GLY   A 1 64  ? -37.988 -8.748  15.757  1.00 29.37 ?  59  GLY   B CA  1 
ATOM   449  C  C   . GLY   A 1 64  ? -38.816 -9.948  16.169  1.00 31.47 ?  59  GLY   B C   1 
ATOM   450  O  O   . GLY   A 1 64  ? -39.190 -10.740 15.298  1.00 37.10 ?  59  GLY   B O   1 
ATOM   451  N  N   . ILE   A 1 65  ? -39.121 -10.112 17.456  1.00 26.38 ?  60  ILE   B N   1 
ATOM   452  C  CA  . ILE   A 1 65  ? -40.061 -11.184 17.863  1.00 25.81 ?  60  ILE   B CA  1 
ATOM   453  C  C   . ILE   A 1 65  ? -41.476 -10.602 17.932  1.00 23.28 ?  60  ILE   B C   1 
ATOM   454  O  O   . ILE   A 1 65  ? -41.645 -9.372  18.005  1.00 24.41 ?  60  ILE   B O   1 
ATOM   455  C  CB  . ILE   A 1 65  ? -39.650 -11.883 19.164  1.00 27.40 ?  60  ILE   B CB  1 
ATOM   456  C  CG1 . ILE   A 1 65  ? -39.953 -11.041 20.402  1.00 28.06 ?  60  ILE   B CG1 1 
ATOM   457  C  CG2 . ILE   A 1 65  ? -38.203 -12.358 19.128  1.00 27.94 ?  60  ILE   B CG2 1 
ATOM   458  C  CD1 . ILE   A 1 65  ? -39.713 -11.778 21.685  1.00 31.79 ?  60  ILE   B CD1 1 
ATOM   459  N  N   . THR   A 1 66  ? -42.447 -11.489 17.844  1.00 21.21 ?  61  THR   B N   1 
ATOM   460  C  CA  . THR   A 1 66  ? -43.892 -11.181 17.947  1.00 21.75 ?  61  THR   B CA  1 
ATOM   461  C  C   . THR   A 1 66  ? -44.325 -11.511 19.375  1.00 22.61 ?  61  THR   B C   1 
ATOM   462  O  O   . THR   A 1 66  ? -44.012 -12.596 19.849  1.00 26.02 ?  61  THR   B O   1 
ATOM   463  C  CB  . THR   A 1 66  ? -44.703 -11.913 16.877  1.00 23.69 ?  61  THR   B CB  1 
ATOM   464  O  OG1 . THR   A 1 66  ? -44.198 -11.482 15.605  1.00 26.24 ?  61  THR   B OG1 1 
ATOM   465  C  CG2 . THR   A 1 66  ? -46.178 -11.594 16.980  1.00 26.56 ?  61  THR   B CG2 1 
ATOM   466  N  N   . LEU   A 1 67  ? -45.025 -10.596 20.014  1.00 19.61 ?  62  LEU   B N   1 
ATOM   467  C  CA  . LEU   A 1 67  ? -45.671 -10.835 21.311  1.00 19.25 ?  62  LEU   B CA  1 
ATOM   468  C  C   . LEU   A 1 67  ? -47.146 -11.130 21.058  1.00 17.90 ?  62  LEU   B C   1 
ATOM   469  O  O   . LEU   A 1 67  ? -47.706 -10.582 20.104  1.00 18.73 ?  62  LEU   B O   1 
ATOM   470  C  CB  . LEU   A 1 67  ? -45.508 -9.622  22.225  1.00 18.43 ?  62  LEU   B CB  1 
ATOM   471  C  CG  . LEU   A 1 67  ? -44.083 -9.146  22.425  1.00 19.59 ?  62  LEU   B CG  1 
ATOM   472  C  CD1 . LEU   A 1 67  ? -44.085 -7.867  23.273  1.00 20.75 ?  62  LEU   B CD1 1 
ATOM   473  C  CD2 . LEU   A 1 67  ? -43.234 -10.243 23.048  1.00 20.52 ?  62  LEU   B CD2 1 
ATOM   474  N  N   . TRP   A 1 68  ? -47.710 -12.002 21.883  1.00 16.44 ?  63  TRP   B N   1 
ATOM   475  C  CA  . TRP   A 1 68  ? -49.161 -12.314 21.845  1.00 16.98 ?  63  TRP   B CA  1 
ATOM   476  C  C   . TRP   A 1 68  ? -49.809 -11.664 23.040  1.00 17.14 ?  63  TRP   B C   1 
ATOM   477  O  O   . TRP   A 1 68  ? -49.272 -11.773 24.149  1.00 17.36 ?  63  TRP   B O   1 
ATOM   478  C  CB  . TRP   A 1 68  ? -49.381 -13.828 21.910  1.00 18.16 ?  63  TRP   B CB  1 
ATOM   479  C  CG  . TRP   A 1 68  ? -48.900 -14.601 20.701  1.00 18.91 ?  63  TRP   B CG  1 
ATOM   480  C  CD1 . TRP   A 1 68  ? -47.959 -14.232 19.774  1.00 20.05 ?  63  TRP   B CD1 1 
ATOM   481  C  CD2 . TRP   A 1 68  ? -49.271 -15.961 20.403  1.00 18.70 ?  63  TRP   B CD2 1 
ATOM   482  N  NE1 . TRP   A 1 68  ? -47.783 -15.252 18.851  1.00 20.35 ?  63  TRP   B NE1 1 
ATOM   483  C  CE2 . TRP   A 1 68  ? -48.593 -16.309 19.212  1.00 19.64 ?  63  TRP   B CE2 1 
ATOM   484  C  CE3 . TRP   A 1 68  ? -50.173 -16.881 20.989  1.00 19.19 ?  63  TRP   B CE3 1 
ATOM   485  C  CZ2 . TRP   A 1 68  ? -48.744 -17.582 18.654  1.00 21.03 ?  63  TRP   B CZ2 1 
ATOM   486  C  CZ3 . TRP   A 1 68  ? -50.326 -18.136 20.418  1.00 20.90 ?  63  TRP   B CZ3 1 
ATOM   487  C  CH2 . TRP   A 1 68  ? -49.656 -18.444 19.229  1.00 21.97 ?  63  TRP   B CH2 1 
ATOM   488  N  N   . GLY   A 1 69  ? -51.076 -11.278 22.923  1.00 17.26 ?  64  GLY   B N   1 
ATOM   489  C  CA  . GLY   A 1 69  ? -51.778 -10.744 24.077  1.00 17.08 ?  64  GLY   B CA  1 
ATOM   490  C  C   . GLY   A 1 69  ? -53.258 -10.769 23.811  1.00 17.55 ?  64  GLY   B C   1 
ATOM   491  O  O   . GLY   A 1 69  ? -53.666 -11.138 22.677  1.00 16.63 ?  64  GLY   B O   1 
ATOM   492  N  N   . HIS   A 1 70  ? -54.051 -10.454 24.798  1.00 15.69 ?  65  HIS   B N   1 
ATOM   493  C  CA  . HIS   A 1 70  ? -55.517 -10.329 24.600  1.00 16.82 ?  65  HIS   B CA  1 
ATOM   494  C  C   . HIS   A 1 70  ? -56.071 -9.237  25.518  1.00 20.72 ?  65  HIS   B C   1 
ATOM   495  O  O   . HIS   A 1 70  ? -55.436 -8.873  26.508  1.00 18.34 ?  65  HIS   B O   1 
ATOM   496  C  CB  . HIS   A 1 70  ? -56.301 -11.636 24.777  1.00 16.68 ?  65  HIS   B CB  1 
ATOM   497  C  CG  . HIS   A 1 70  ? -56.445 -12.191 26.159  1.00 16.73 ?  65  HIS   B CG  1 
ATOM   498  N  ND1 . HIS   A 1 70  ? -55.417 -12.895 26.769  1.00 17.76 ?  65  HIS   B ND1 1 
ATOM   499  C  CD2 . HIS   A 1 70  ? -57.504 -12.226 26.985  1.00 18.55 ?  65  HIS   B CD2 1 
ATOM   500  C  CE1 . HIS   A 1 70  ? -55.828 -13.326 27.959  1.00 18.59 ?  65  HIS   B CE1 1 
ATOM   501  N  NE2 . HIS   A 1 70  ? -57.177 -12.945 28.129  1.00 17.62 ?  65  HIS   B NE2 1 
ATOM   502  N  N   . MET   A 1 71  ? -57.303 -8.816  25.239  1.00 18.46 ?  66  MET   B N   1 
ATOM   503  C  CA  . MET   A 1 71  ? -57.979 -7.792  26.041  1.00 18.61 ?  66  MET   B CA  1 
ATOM   504  C  C   . MET   A 1 71  ? -59.456 -8.047  25.804  1.00 17.51 ?  66  MET   B C   1 
ATOM   505  O  O   . MET   A 1 71  ? -59.775 -9.003  25.086  1.00 19.27 ?  66  MET   B O   1 
ATOM   506  C  CB  . MET   A 1 71  ? -57.564 -6.381  25.611  1.00 20.40 ?  66  MET   B CB  1 
ATOM   507  C  CG  . MET   A 1 71  ? -58.037 -5.979  24.260  1.00 23.43 ?  66  MET   B CG  1 
ATOM   508  S  SD  . MET   A 1 71  ? -57.785 -4.173  24.033  1.00 34.32 ?  66  MET   B SD  1 
ATOM   509  C  CE  . MET   A 1 71  ? -56.116 -4.333  23.506  1.00 26.76 ?  66  MET   B CE  1 
ATOM   510  N  N   . ASN   A 1 72  ? -60.280 -7.279  26.462  1.00 16.57 ?  67  ASN   B N   1 
ATOM   511  C  CA  . ASN   A 1 72  ? -61.764 -7.374  26.355  1.00 18.36 ?  67  ASN   B CA  1 
ATOM   512  C  C   . ASN   A 1 72  ? -62.223 -6.611  25.102  1.00 19.45 ?  67  ASN   B C   1 
ATOM   513  O  O   . ASN   A 1 72  ? -61.960 -5.392  25.032  1.00 20.05 ?  67  ASN   B O   1 
ATOM   514  C  CB  . ASN   A 1 72  ? -62.325 -6.793  27.636  1.00 19.07 ?  67  ASN   B CB  1 
ATOM   515  C  CG  . ASN   A 1 72  ? -63.815 -6.928  27.741  1.00 20.22 ?  67  ASN   B CG  1 
ATOM   516  O  OD1 . ASN   A 1 72  ? -64.426 -7.394  26.815  1.00 21.23 ?  67  ASN   B OD1 1 
ATOM   517  N  ND2 . ASN   A 1 72  ? -64.326 -6.670  28.926  1.00 25.39 ?  67  ASN   B ND2 1 
ATOM   518  N  N   . ARG   A 1 73  ? -62.975 -7.261  24.199  1.00 20.57 ?  68  ARG   B N   1 
ATOM   519  C  CA  . ARG   A 1 73  ? -63.605 -6.545  23.048  1.00 27.44 ?  68  ARG   B CA  1 
ATOM   520  C  C   . ARG   A 1 73  ? -64.554 -5.443  23.507  1.00 23.73 ?  68  ARG   B C   1 
ATOM   521  O  O   . ARG   A 1 73  ? -64.748 -4.518  22.704  1.00 33.82 ?  68  ARG   B O   1 
ATOM   522  C  CB  . ARG   A 1 73  ? -64.357 -7.527  22.141  1.00 26.70 ?  68  ARG   B CB  1 
ATOM   523  C  CG  . ARG   A 1 73  ? -63.441 -8.303  21.207  1.00 26.60 ?  68  ARG   B CG  1 
ATOM   524  C  CD  . ARG   A 1 73  ? -64.151 -9.421  20.433  1.00 26.54 ?  68  ARG   B CD  1 
ATOM   525  N  NE  . ARG   A 1 73  ? -63.142 -10.078 19.646  1.00 25.14 ?  68  ARG   B NE  1 
ATOM   526  C  CZ  . ARG   A 1 73  ? -62.833 -9.798  18.395  1.00 27.19 ?  68  ARG   B CZ  1 
ATOM   527  N  NH1 . ARG   A 1 73  ? -63.551 -8.911  17.711  1.00 28.05 1  68  ARG   B NH1 1 
ATOM   528  N  NH2 . ARG   A 1 73  ? -61.818 -10.431 17.814  1.00 25.79 ?  68  ARG   B NH2 1 
ATOM   529  N  N   . ALA   A 1 74  ? -65.154 -5.569  24.691  1.00 26.94 ?  69  ALA   B N   1 
ATOM   530  C  CA  . ALA   A 1 74  ? -66.125 -4.621  25.274  1.00 26.64 ?  69  ALA   B CA  1 
ATOM   531  C  C   . ALA   A 1 74  ? -65.411 -3.336  25.700  1.00 26.34 ?  69  ALA   B C   1 
ATOM   532  O  O   . ALA   A 1 74  ? -66.082 -2.343  25.941  1.00 25.10 ?  69  ALA   B O   1 
ATOM   533  C  CB  . ALA   A 1 74  ? -66.832 -5.214  26.451  1.00 27.82 ?  69  ALA   B CB  1 
ATOM   534  N  N   . ASN   A 1 75  ? -64.101 -3.413  25.952  1.00 22.59 ?  70  ASN   B N   1 
ATOM   535  C  CA  . ASN   A 1 75  ? -63.258 -2.255  26.324  1.00 22.43 ?  70  ASN   B CA  1 
ATOM   536  C  C   . ASN   A 1 75  ? -63.202 -1.321  25.120  1.00 21.48 ?  70  ASN   B C   1 
ATOM   537  O  O   . ASN   A 1 75  ? -62.696 -1.715  24.079  1.00 25.12 ?  70  ASN   B O   1 
ATOM   538  C  CB  . ASN   A 1 75  ? -61.842 -2.750  26.674  1.00 23.58 ?  70  ASN   B CB  1 
ATOM   539  C  CG  . ASN   A 1 75  ? -60.924 -1.654  27.152  1.00 24.21 ?  70  ASN   B CG  1 
ATOM   540  O  OD1 . ASN   A 1 75  ? -61.114 -0.467  26.858  1.00 24.68 ?  70  ASN   B OD1 1 
ATOM   541  N  ND2 . ASN   A 1 75  ? -59.874 -2.063  27.829  1.00 22.15 ?  70  ASN   B ND2 1 
ATOM   542  N  N   . PRO   A 1 76  ? -63.595 -0.024  25.221  1.00 19.96 ?  71  PRO   B N   1 
ATOM   543  C  CA  . PRO   A 1 76  ? -63.487 0.899   24.080  1.00 19.26 ?  71  PRO   B CA  1 
ATOM   544  C  C   . PRO   A 1 76  ? -62.112 0.990   23.422  1.00 20.83 ?  71  PRO   B C   1 
ATOM   545  O  O   . PRO   A 1 76  ? -61.929 1.417   22.278  1.00 23.02 ?  71  PRO   B O   1 
ATOM   546  C  CB  . PRO   A 1 76  ? -63.787 2.255   24.704  1.00 20.57 ?  71  PRO   B CB  1 
ATOM   547  C  CG  . PRO   A 1 76  ? -64.631 1.950   25.922  1.00 25.33 ?  71  PRO   B CG  1 
ATOM   548  C  CD  . PRO   A 1 76  ? -64.149 0.598   26.430  1.00 24.62 ?  71  PRO   B CD  1 
ATOM   549  N  N   . HIS   A 1 77  ? -61.095 0.602   24.165  1.00 19.16 ?  72  HIS   B N   1 
ATOM   550  C  CA  . HIS   A 1 77  ? -59.716 0.643   23.660  1.00 19.33 ?  72  HIS   B CA  1 
ATOM   551  C  C   . HIS   A 1 77  ? -59.593 -0.308  22.454  1.00 20.37 ?  72  HIS   B C   1 
ATOM   552  O  O   . HIS   A 1 77  ? -58.881 0.020   21.472  1.00 21.60 ?  72  HIS   B O   1 
ATOM   553  C  CB  . HIS   A 1 77  ? -58.785 0.299   24.824  1.00 18.44 ?  72  HIS   B CB  1 
ATOM   554  C  CG  . HIS   A 1 77  ? -57.361 0.550   24.516  1.00 18.50 ?  72  HIS   B CG  1 
ATOM   555  N  ND1 . HIS   A 1 77  ? -56.345 0.326   25.451  1.00 19.36 ?  72  HIS   B ND1 1 
ATOM   556  C  CD2 . HIS   A 1 77  ? -56.767 1.056   23.424  1.00 20.13 ?  72  HIS   B CD2 1 
ATOM   557  C  CE1 . HIS   A 1 77  ? -55.201 0.677   24.916  1.00 18.04 ?  72  HIS   B CE1 1 
ATOM   558  N  NE2 . HIS   A 1 77  ? -55.439 1.158   23.705  1.00 19.90 ?  72  HIS   B NE2 1 
ATOM   559  N  N   . TRP   A 1 78  ? -60.245 -1.457  22.527  1.00 20.27 ?  73  TRP   B N   1 
ATOM   560  C  CA  . TRP   A 1 78  ? -60.246 -2.423  21.389  1.00 20.78 ?  73  TRP   B CA  1 
ATOM   561  C  C   . TRP   A 1 78  ? -60.709 -1.729  20.089  1.00 23.94 ?  73  TRP   B C   1 
ATOM   562  O  O   . TRP   A 1 78  ? -60.010 -1.781  19.088  1.00 21.17 ?  73  TRP   B O   1 
ATOM   563  C  CB  . TRP   A 1 78  ? -61.097 -3.630  21.767  1.00 23.00 ?  73  TRP   B CB  1 
ATOM   564  C  CG  . TRP   A 1 78  ? -61.236 -4.634  20.677  1.00 23.01 ?  73  TRP   B CG  1 
ATOM   565  C  CD1 . TRP   A 1 78  ? -62.327 -4.820  19.876  1.00 24.58 ?  73  TRP   B CD1 1 
ATOM   566  C  CD2 . TRP   A 1 78  ? -60.234 -5.575  20.239  1.00 23.64 ?  73  TRP   B CD2 1 
ATOM   567  N  NE1 . TRP   A 1 78  ? -62.071 -5.812  18.967  1.00 25.08 ?  73  TRP   B NE1 1 
ATOM   568  C  CE2 . TRP   A 1 78  ? -60.800 -6.287  19.157  1.00 24.10 ?  73  TRP   B CE2 1 
ATOM   569  C  CE3 . TRP   A 1 78  ? -58.914 -5.878  20.629  1.00 24.05 ?  73  TRP   B CE3 1 
ATOM   570  C  CZ2 . TRP   A 1 78  ? -60.121 -7.325  18.533  1.00 24.90 ?  73  TRP   B CZ2 1 
ATOM   571  C  CZ3 . TRP   A 1 78  ? -58.232 -6.886  19.991  1.00 20.79 ?  73  TRP   B CZ3 1 
ATOM   572  C  CH2 . TRP   A 1 78  ? -58.834 -7.606  18.956  1.00 23.97 ?  73  TRP   B CH2 1 
ATOM   573  N  N   . ALA   A 1 79  ? -61.904 -1.137  20.054  1.00 23.63 ?  74  ALA   B N   1 
ATOM   574  C  CA  . ALA   A 1 79  ? -62.379 -0.403  18.853  1.00 28.53 ?  74  ALA   B CA  1 
ATOM   575  C  C   . ALA   A 1 79  ? -61.399 0.718   18.481  1.00 28.28 ?  74  ALA   B C   1 
ATOM   576  O  O   . ALA   A 1 79  ? -61.166 0.942   17.296  1.00 28.44 ?  74  ALA   B O   1 
ATOM   577  C  CB  . ALA   A 1 79  ? -63.777 0.140   19.099  1.00 29.59 ?  74  ALA   B CB  1 
ATOM   578  N  N   . ALA   A 1 80  ? -60.815 1.401   19.470  1.00 28.53 ?  75  ALA   B N   1 
ATOM   579  C  CA  . ALA   A 1 80  ? -59.980 2.603   19.259  1.00 28.15 ?  75  ALA   B CA  1 
ATOM   580  C  C   . ALA   A 1 80  ? -58.708 2.189   18.526  1.00 30.63 ?  75  ALA   B C   1 
ATOM   581  O  O   . ALA   A 1 80  ? -58.141 3.015   17.813  1.00 32.67 ?  75  ALA   B O   1 
ATOM   582  C  CB  . ALA   A 1 80  ? -59.647 3.290   20.551  1.00 25.90 ?  75  ALA   B CB  1 
ATOM   583  N  N   . LEU   A 1 81  ? -58.282 0.929   18.656  1.00 29.46 ?  76  LEU   B N   1 
ATOM   584  C  CA  . LEU   A 1 81  ? -57.008 0.497   18.030  1.00 29.73 ?  76  LEU   B CA  1 
ATOM   585  C  C   . LEU   A 1 81  ? -57.185 0.423   16.501  1.00 38.32 ?  76  LEU   B C   1 
ATOM   586  O  O   . LEU   A 1 81  ? -56.165 0.519   15.757  1.00 41.21 ?  76  LEU   B O   1 
ATOM   587  C  CB  . LEU   A 1 81  ? -56.595 -0.847  18.642  1.00 27.44 ?  76  LEU   B CB  1 
ATOM   588  C  CG  . LEU   A 1 81  ? -55.990 -0.703  20.033  1.00 22.99 ?  76  LEU   B CG  1 
ATOM   589  C  CD1 . LEU   A 1 81  ? -56.027 -2.002  20.770  1.00 24.09 ?  76  LEU   B CD1 1 
ATOM   590  C  CD2 . LEU   A 1 81  ? -54.577 -0.155  19.964  1.00 23.90 ?  76  LEU   B CD2 1 
ATOM   591  N  N   . GLY   A 1 82  ? -58.421 0.259   16.043  1.00 40.22 ?  77  GLY   B N   1 
ATOM   592  C  CA  . GLY   A 1 82  ? -58.718 0.127   14.607  1.00 53.13 ?  77  GLY   B CA  1 
ATOM   593  C  C   . GLY   A 1 82  ? -57.739 -0.830  13.944  1.00 59.98 ?  77  GLY   B C   1 
ATOM   594  O  O   . GLY   A 1 82  ? -57.547 -1.944  14.490  1.00 60.79 ?  77  GLY   B O   1 
ATOM   595  N  N   . GLY   A 1 83  ? -57.091 -0.394  12.860  1.00 59.79 ?  78  GLY   B N   1 
ATOM   596  C  CA  . GLY   A 1 83  ? -56.264 -1.258  11.994  1.00 65.87 ?  78  GLY   B CA  1 
ATOM   597  C  C   . GLY   A 1 83  ? -54.883 -1.512  12.572  1.00 64.45 ?  78  GLY   B C   1 
ATOM   598  O  O   . GLY   A 1 83  ? -54.760 -2.333  13.497  1.00 77.76 ?  78  GLY   B O   1 
ATOM   599  N  N   . ALA   A 1 84  ? -53.875 -0.825  12.038  1.00 62.06 ?  79  ALA   B N   1 
ATOM   600  C  CA  . ALA   A 1 84  ? -52.444 -1.037  12.346  1.00 57.68 ?  79  ALA   B CA  1 
ATOM   601  C  C   . ALA   A 1 84  ? -51.970 0.042   13.335  1.00 51.61 ?  79  ALA   B C   1 
ATOM   602  O  O   . ALA   A 1 84  ? -51.121 0.879   12.941  1.00 55.45 ?  79  ALA   B O   1 
ATOM   603  C  CB  . ALA   A 1 84  ? -51.652 -1.001  11.060  1.00 58.04 ?  79  ALA   B CB  1 
ATOM   604  N  N   . ALA   A 1 85  ? -52.475 0.017   14.574  1.00 40.00 ?  80  ALA   B N   1 
ATOM   605  C  CA  . ALA   A 1 85  ? -52.184 1.062   15.589  1.00 34.04 ?  80  ALA   B CA  1 
ATOM   606  C  C   . ALA   A 1 85  ? -50.729 0.928   16.049  1.00 29.34 ?  80  ALA   B C   1 
ATOM   607  O  O   . ALA   A 1 85  ? -50.303 -0.185  16.342  1.00 26.94 ?  80  ALA   B O   1 
ATOM   608  C  CB  . ALA   A 1 85  ? -53.140 0.967   16.740  1.00 34.09 ?  80  ALA   B CB  1 
ATOM   609  N  N   . ASN   A 1 86  ? -50.014 2.046   16.110  1.00 25.30 ?  81  ASN   B N   1 
ATOM   610  C  CA  . ASN   A 1 86  ? -48.665 2.098   16.695  1.00 25.68 ?  81  ASN   B CA  1 
ATOM   611  C  C   . ASN   A 1 86  ? -48.864 2.180   18.199  1.00 25.15 ?  81  ASN   B C   1 
ATOM   612  O  O   . ASN   A 1 86  ? -49.616 3.044   18.646  1.00 28.13 ?  81  ASN   B O   1 
ATOM   613  C  CB  . ASN   A 1 86  ? -47.883 3.297   16.192  1.00 27.32 ?  81  ASN   B CB  1 
ATOM   614  C  CG  . ASN   A 1 86  ? -47.614 3.128   14.726  1.00 31.61 ?  81  ASN   B CG  1 
ATOM   615  O  OD1 . ASN   A 1 86  ? -47.312 2.013   14.310  1.00 33.35 ?  81  ASN   B OD1 1 
ATOM   616  N  ND2 . ASN   A 1 86  ? -47.775 4.189   13.958  1.00 31.42 ?  81  ASN   B ND2 1 
ATOM   617  N  N   . VAL   A 1 87  ? -48.303 1.233   18.927  1.00 23.08 ?  82  VAL   B N   1 
ATOM   618  C  CA  . VAL   A 1 87  ? -48.567 1.121   20.389  1.00 21.01 ?  82  VAL   B CA  1 
ATOM   619  C  C   . VAL   A 1 87  ? -47.250 1.018   21.126  1.00 19.19 ?  82  VAL   B C   1 
ATOM   620  O  O   . VAL   A 1 87  ? -46.257 0.683   20.539  1.00 18.59 ?  82  VAL   B O   1 
ATOM   621  C  CB  . VAL   A 1 87  ? -49.460 -0.073  20.744  1.00 20.86 ?  82  VAL   B CB  1 
ATOM   622  C  CG1 . VAL   A 1 87  ? -50.820 0.014   20.051  1.00 23.77 ?  82  VAL   B CG1 1 
ATOM   623  C  CG2 . VAL   A 1 87  ? -48.774 -1.405  20.524  1.00 21.86 ?  82  VAL   B CG2 1 
ATOM   624  N  N   . VAL   A 1 88  ? -47.322 1.251   22.433  1.00 18.85 ?  83  VAL   B N   1 
ATOM   625  C  CA  . VAL   A 1 88  ? -46.228 0.925   23.383  1.00 18.99 ?  83  VAL   B CA  1 
ATOM   626  C  C   . VAL   A 1 88  ? -46.823 -0.011  24.441  1.00 18.25 ?  83  VAL   B C   1 
ATOM   627  O  O   . VAL   A 1 88  ? -48.048 0.145   24.783  1.00 19.06 ?  83  VAL   B O   1 
ATOM   628  C  CB  . VAL   A 1 88  ? -45.559 2.169   24.007  1.00 18.76 ?  83  VAL   B CB  1 
ATOM   629  C  CG1 . VAL   A 1 88  ? -46.570 3.070   24.669  1.00 19.44 ?  83  VAL   B CG1 1 
ATOM   630  C  CG2 . VAL   A 1 88  ? -44.503 1.741   25.025  1.00 20.41 ?  83  VAL   B CG2 1 
ATOM   631  N  N   . ALA   A 1 89  ? -46.094 -1.061  24.782  1.00 17.23 ?  84  ALA   B N   1 
ATOM   632  C  CA  . ALA   A 1 89  ? -46.460 -1.948  25.931  1.00 15.83 ?  84  ALA   B CA  1 
ATOM   633  C  C   . ALA   A 1 89  ? -45.345 -1.864  26.936  1.00 15.89 ?  84  ALA   B C   1 
ATOM   634  O  O   . ALA   A 1 89  ? -44.158 -2.033  26.554  1.00 18.50 ?  84  ALA   B O   1 
ATOM   635  C  CB  . ALA   A 1 89  ? -46.791 -3.352  25.491  1.00 17.75 ?  84  ALA   B CB  1 
ATOM   636  N  N   . THR   A 1 90  ? -45.702 -1.447  28.151  1.00 16.42 ?  85  THR   B N   1 
ATOM   637  C  CA  . THR   A 1 90  ? -44.707 -1.198  29.219  1.00 15.62 ?  85  THR   B CA  1 
ATOM   638  C  C   . THR   A 1 90  ? -44.848 -2.304  30.256  1.00 17.73 ?  85  THR   B C   1 
ATOM   639  O  O   . THR   A 1 90  ? -45.976 -2.572  30.714  1.00 16.46 ?  85  THR   B O   1 
ATOM   640  C  CB  . THR   A 1 90  ? -44.887 0.163   29.885  1.00 16.50 ?  85  THR   B CB  1 
ATOM   641  O  OG1 . THR   A 1 90  ? -44.842 1.192   28.871  1.00 18.20 ?  85  THR   B OG1 1 
ATOM   642  C  CG2 . THR   A 1 90  ? -43.793 0.345   30.923  1.00 18.36 ?  85  THR   B CG2 1 
ATOM   643  N  N   . PHE   A 1 91  ? -43.729 -2.904  30.605  1.00 15.27 ?  86  PHE   B N   1 
ATOM   644  C  CA  . PHE   A 1 91  ? -43.649 -4.023  31.565  1.00 17.26 ?  86  PHE   B CA  1 
ATOM   645  C  C   . PHE   A 1 91  ? -42.855 -3.461  32.738  1.00 19.12 ?  86  PHE   B C   1 
ATOM   646  O  O   . PHE   A 1 91  ? -41.757 -2.938  32.537  1.00 21.24 ?  86  PHE   B O   1 
ATOM   647  C  CB  . PHE   A 1 91  ? -42.962 -5.225  30.946  1.00 16.86 ?  86  PHE   B CB  1 
ATOM   648  C  CG  . PHE   A 1 91  ? -43.613 -5.818  29.725  1.00 15.96 ?  86  PHE   B CG  1 
ATOM   649  C  CD1 . PHE   A 1 91  ? -43.456 -5.225  28.478  1.00 16.16 ?  86  PHE   B CD1 1 
ATOM   650  C  CD2 . PHE   A 1 91  ? -44.408 -6.958  29.808  1.00 16.22 ?  86  PHE   B CD2 1 
ATOM   651  C  CE1 . PHE   A 1 91  ? -44.044 -5.760  27.348  1.00 16.33 ?  86  PHE   B CE1 1 
ATOM   652  C  CE2 . PHE   A 1 91  ? -45.016 -7.483  28.682  1.00 16.68 ?  86  PHE   B CE2 1 
ATOM   653  C  CZ  . PHE   A 1 91  ? -44.847 -6.875  27.455  1.00 16.42 ?  86  PHE   B CZ  1 
ATOM   654  N  N   . ALA   A 1 92  ? -43.383 -3.562  33.932  1.00 15.61 ?  87  ALA   B N   1 
ATOM   655  C  CA  . ALA   A 1 92  ? -42.793 -2.930  35.130  1.00 19.04 ?  87  ALA   B CA  1 
ATOM   656  C  C   . ALA   A 1 92  ? -42.354 -4.058  36.065  1.00 19.24 ?  87  ALA   B C   1 
ATOM   657  O  O   . ALA   A 1 92  ? -43.202 -4.893  36.437  1.00 20.69 ?  87  ALA   B O   1 
ATOM   658  C  CB  . ALA   A 1 92  ? -43.832 -2.015  35.774  1.00 19.99 ?  87  ALA   B CB  1 
ATOM   659  N  N   . GLY   A 1 93  ? -41.068 -4.109  36.404  1.00 16.70 ?  88  GLY   B N   1 
ATOM   660  C  CA  . GLY   A 1 93  ? -40.531 -5.145  37.277  1.00 17.92 ?  88  GLY   B CA  1 
ATOM   661  C  C   . GLY   A 1 93  ? -40.289 -4.631  38.702  1.00 18.67 ?  88  GLY   B C   1 
ATOM   662  O  O   . GLY   A 1 93  ? -40.919 -3.698  39.184  1.00 18.32 ?  88  GLY   B O   1 
ATOM   663  N  N   . PRO   A 1 94  ? -39.346 -5.283  39.403  1.00 18.80 ?  89  PRO   B N   1 
ATOM   664  C  CA  . PRO   A 1 94  ? -39.002 -4.923  40.773  1.00 17.67 ?  89  PRO   B CA  1 
ATOM   665  C  C   . PRO   A 1 94  ? -38.648 -3.442  40.881  1.00 16.59 ?  89  PRO   B C   1 
ATOM   666  O  O   . PRO   A 1 94  ? -38.070 -2.856  39.938  1.00 16.33 ?  89  PRO   B O   1 
ATOM   667  C  CB  . PRO   A 1 94  ? -37.784 -5.791  41.056  1.00 19.30 ?  89  PRO   B CB  1 
ATOM   668  C  CG  . PRO   A 1 94  ? -38.012 -7.006  40.167  1.00 18.68 ?  89  PRO   B CG  1 
ATOM   669  C  CD  . PRO   A 1 94  ? -38.535 -6.396  38.893  1.00 19.45 ?  89  PRO   B CD  1 
ATOM   670  N  N   . ASN   A 1 95  ? -39.004 -2.875  42.019  1.00 16.24 ?  90  ASN   B N   1 
ATOM   671  C  CA  . ASN   A 1 95  ? -38.783 -1.442  42.271  1.00 17.10 ?  90  ASN   B CA  1 
ATOM   672  C  C   . ASN   A 1 95  ? -38.858 -1.178  43.770  1.00 16.97 ?  90  ASN   B C   1 
ATOM   673  O  O   . ASN   A 1 95  ? -39.560 -1.945  44.493  1.00 17.06 ?  90  ASN   B O   1 
ATOM   674  C  CB  . ASN   A 1 95  ? -39.777 -0.600  41.497  1.00 17.25 ?  90  ASN   B CB  1 
ATOM   675  C  CG  . ASN   A 1 95  ? -41.173 -0.731  42.063  1.00 18.68 ?  90  ASN   B CG  1 
ATOM   676  O  OD1 . ASN   A 1 95  ? -41.541 0.061   42.936  1.00 19.25 ?  90  ASN   B OD1 1 
ATOM   677  N  ND2 . ASN   A 1 95  ? -41.924 -1.713  41.580  1.00 19.68 ?  90  ASN   B ND2 1 
ATOM   678  N  N   . ALA   A 1 96  ? -38.131 -0.160  44.227  1.00 15.36 ?  91  ALA   B N   1 
ATOM   679  C  CA  . ALA   A 1 96  ? -38.144 0.215   45.658  1.00 15.87 ?  91  ALA   B CA  1 
ATOM   680  C  C   . ALA   A 1 96  ? -37.615 1.631   45.843  1.00 15.25 ?  91  ALA   B C   1 
ATOM   681  O  O   . ALA   A 1 96  ? -36.586 2.020   45.204  1.00 17.64 ?  91  ALA   B O   1 
ATOM   682  C  CB  . ALA   A 1 96  ? -37.381 -0.785  46.441  1.00 16.74 ?  91  ALA   B CB  1 
ATOM   683  N  N   . TYR   A 1 97  ? -38.265 2.383   46.715  1.00 15.10 ?  92  TYR   B N   1 
ATOM   684  C  CA  . TYR   A 1 97  ? -37.775 3.716   47.165  1.00 15.48 ?  92  TYR   B CA  1 
ATOM   685  C  C   . TYR   A 1 97  ? -36.398 3.607   47.852  1.00 15.16 ?  92  TYR   B C   1 
ATOM   686  O  O   . TYR   A 1 97  ? -36.118 2.635   48.599  1.00 16.72 ?  92  TYR   B O   1 
ATOM   687  C  CB  . TYR   A 1 97  ? -38.726 4.316   48.171  1.00 15.13 ?  92  TYR   B CB  1 
ATOM   688  C  CG  . TYR   A 1 97  ? -38.292 5.628   48.734  1.00 14.53 ?  92  TYR   B CG  1 
ATOM   689  C  CD1 . TYR   A 1 97  ? -38.409 6.781   47.963  1.00 14.29 ?  92  TYR   B CD1 1 
ATOM   690  C  CD2 . TYR   A 1 97  ? -37.795 5.737   50.008  1.00 14.31 ?  92  TYR   B CD2 1 
ATOM   691  C  CE1 . TYR   A 1 97  ? -38.054 8.014   48.457  1.00 14.25 ?  92  TYR   B CE1 1 
ATOM   692  C  CE2 . TYR   A 1 97  ? -37.438 6.971   50.522  1.00 16.01 ?  92  TYR   B CE2 1 
ATOM   693  C  CZ  . TYR   A 1 97  ? -37.586 8.122   49.751  1.00 14.09 ?  92  TYR   B CZ  1 
ATOM   694  O  OH  . TYR   A 1 97  ? -37.311 9.382   50.162  1.00 15.54 ?  92  TYR   B OH  1 
ATOM   695  N  N   . VAL   A 1 98  ? -35.560 4.557   47.568  1.00 15.27 ?  93  VAL   B N   1 
ATOM   696  C  CA  . VAL   A 1 98  ? -34.147 4.583   48.091  1.00 16.19 ?  93  VAL   B CA  1 
ATOM   697  C  C   . VAL   A 1 98  ? -34.063 5.797   49.028  1.00 15.90 ?  93  VAL   B C   1 
ATOM   698  O  O   . VAL   A 1 98  ? -34.024 6.980   48.535  1.00 16.35 ?  93  VAL   B O   1 
ATOM   699  C  CB  . VAL   A 1 98  ? -33.080 4.639   46.978  1.00 15.98 ?  93  VAL   B CB  1 
ATOM   700  C  CG1 . VAL   A 1 98  ? -31.669 4.663   47.596  1.00 16.83 ?  93  VAL   B CG1 1 
ATOM   701  C  CG2 . VAL   A 1 98  ? -33.219 3.522   45.969  1.00 15.44 ?  93  VAL   B CG2 1 
ATOM   702  N  N   . SER   A 1 99  ? -34.008 5.539   50.329  1.00 14.48 ?  94  SER   B N   1 
ATOM   703  C  CA  . SER   A 1 99  ? -33.834 6.599   51.344  1.00 15.84 ?  94  SER   B CA  1 
ATOM   704  C  C   . SER   A 1 99  ? -32.362 6.954   51.373  1.00 17.42 ?  94  SER   B C   1 
ATOM   705  O  O   . SER   A 1 99  ? -31.602 6.025   51.529  1.00 16.64 ?  94  SER   B O   1 
ATOM   706  C  CB  . SER   A 1 99  ? -34.236 6.145   52.695  1.00 16.89 ?  94  SER   B CB  1 
ATOM   707  O  OG  . SER   A 1 99  ? -33.917 7.121   53.658  1.00 18.02 ?  94  SER   B OG  1 
ATOM   708  N  N   . PRO   A 1 100 ? -31.944 8.240   51.329  1.00 17.29 ?  95  PRO   B N   1 
ATOM   709  C  CA  . PRO   A 1 100 ? -30.563 8.607   51.600  1.00 19.46 ?  95  PRO   B CA  1 
ATOM   710  C  C   . PRO   A 1 100 ? -30.032 8.181   52.971  1.00 19.57 ?  95  PRO   B C   1 
ATOM   711  O  O   . PRO   A 1 100 ? -28.810 8.134   53.071  1.00 19.15 ?  95  PRO   B O   1 
ATOM   712  C  CB  . PRO   A 1 100 ? -30.584 10.129  51.565  1.00 17.94 ?  95  PRO   B CB  1 
ATOM   713  C  CG  . PRO   A 1 100 ? -31.727 10.415  50.617  1.00 18.25 ?  95  PRO   B CG  1 
ATOM   714  C  CD  . PRO   A 1 100 ? -32.768 9.441   51.097  1.00 19.44 ?  95  PRO   B CD  1 
ATOM   715  N  N   . ALA   A 1 101 ? -30.907 7.850   53.928  1.00 19.80 ?  96  ALA   B N   1 
ATOM   716  C  CA  . ALA   A 1 101 ? -30.526 7.194   55.211  1.00 20.64 ?  96  ALA   B CA  1 
ATOM   717  C  C   . ALA   A 1 101 ? -29.677 5.958   54.936  1.00 22.56 ?  96  ALA   B C   1 
ATOM   718  O  O   . ALA   A 1 101 ? -28.701 5.733   55.677  1.00 23.34 ?  96  ALA   B O   1 
ATOM   719  C  CB  . ALA   A 1 101 ? -31.704 6.825   56.062  1.00 24.61 ?  96  ALA   B CB  1 
ATOM   720  N  N   . VAL   A 1 102 ? -29.954 5.218   53.870  1.00 19.33 ?  97  VAL   B N   1 
ATOM   721  C  CA  . VAL   A 1 102 ? -29.221 3.961   53.553  1.00 18.91 ?  97  VAL   B CA  1 
ATOM   722  C  C   . VAL   A 1 102 ? -27.816 4.324   53.069  1.00 20.78 ?  97  VAL   B C   1 
ATOM   723  O  O   . VAL   A 1 102 ? -26.915 3.534   53.261  1.00 22.76 ?  97  VAL   B O   1 
ATOM   724  C  CB  . VAL   A 1 102 ? -30.008 3.170   52.503  1.00 21.72 ?  97  VAL   B CB  1 
ATOM   725  C  CG1 . VAL   A 1 102 ? -29.291 1.915   52.070  1.00 23.93 ?  97  VAL   B CG1 1 
ATOM   726  C  CG2 . VAL   A 1 102 ? -31.430 2.867   53.031  1.00 21.64 ?  97  VAL   B CG2 1 
ATOM   727  N  N   . TYR   A 1 103 ? -27.657 5.451   52.357  1.00 20.60 ?  98  TYR   B N   1 
ATOM   728  C  CA  . TYR   A 1 103 ? -26.338 5.846   51.817  1.00 20.35 ?  98  TYR   B CA  1 
ATOM   729  C  C   . TYR   A 1 103 ? -25.358 6.128   52.938  1.00 20.58 ?  98  TYR   B C   1 
ATOM   730  O  O   . TYR   A 1 103 ? -24.129 5.872   52.740  1.00 22.28 ?  98  TYR   B O   1 
ATOM   731  C  CB  . TYR   A 1 103 ? -26.503 7.130   51.000  1.00 20.25 ?  98  TYR   B CB  1 
ATOM   732  C  CG  . TYR   A 1 103 ? -27.362 7.037   49.780  1.00 20.51 ?  98  TYR   B CG  1 
ATOM   733  C  CD1 . TYR   A 1 103 ? -27.612 5.837   49.135  1.00 21.12 ?  98  TYR   B CD1 1 
ATOM   734  C  CD2 . TYR   A 1 103 ? -27.777 8.206   49.163  1.00 19.42 ?  98  TYR   B CD2 1 
ATOM   735  C  CE1 . TYR   A 1 103 ? -28.288 5.783   47.927  1.00 19.88 ?  98  TYR   B CE1 1 
ATOM   736  C  CE2 . TYR   A 1 103 ? -28.483 8.164   47.981  1.00 19.28 ?  98  TYR   B CE2 1 
ATOM   737  C  CZ  . TYR   A 1 103 ? -28.746 6.967   47.360  1.00 21.98 ?  98  TYR   B CZ  1 
ATOM   738  O  OH  . TYR   A 1 103 ? -29.463 6.942   46.195  1.00 20.80 ?  98  TYR   B OH  1 
ATOM   739  N  N   . ARG   A 1 104 ? -25.863 6.730   54.029  1.00 21.43 ?  99  ARG   B N   1 
ATOM   740  C  CA  . ARG   A 1 104 ? -25.081 7.252   55.203  1.00 27.09 ?  99  ARG   B CA  1 
ATOM   741  C  C   . ARG   A 1 104 ? -24.053 8.302   54.740  1.00 29.67 ?  99  ARG   B C   1 
ATOM   742  O  O   . ARG   A 1 104 ? -22.933 8.372   55.303  1.00 32.55 ?  99  ARG   B O   1 
ATOM   743  C  CB  . ARG   A 1 104 ? -24.415 6.094   55.956  1.00 28.55 ?  99  ARG   B CB  1 
ATOM   744  C  CG  . ARG   A 1 104 ? -25.355 4.922   56.193  1.00 26.46 ?  99  ARG   B CG  1 
ATOM   745  C  CD  . ARG   A 1 104 ? -24.900 3.983   57.293  1.00 28.61 ?  99  ARG   B CD  1 
ATOM   746  N  NE  . ARG   A 1 104 ? -23.535 3.462   57.168  1.00 28.91 ?  99  ARG   B NE  1 
ATOM   747  C  CZ  . ARG   A 1 104 ? -23.183 2.308   56.607  1.00 27.89 ?  99  ARG   B CZ  1 
ATOM   748  N  NH1 . ARG   A 1 104 ? -24.086 1.485   56.102  1.00 30.23 1  99  ARG   B NH1 1 
ATOM   749  N  NH2 . ARG   A 1 104 ? -21.913 1.939   56.618  1.00 32.20 ?  99  ARG   B NH2 1 
ATOM   750  N  N   . THR   A 1 105 ? -24.390 9.050   53.702  1.00 27.64 ?  100 THR   B N   1 
ATOM   751  C  CA  . THR   A 1 105 ? -23.531 10.090  53.077  1.00 27.20 ?  100 THR   B CA  1 
ATOM   752  C  C   . THR   A 1 105 ? -24.332 11.382  53.019  1.00 28.05 ?  100 THR   B C   1 
ATOM   753  O  O   . THR   A 1 105 ? -25.563 11.342  53.153  1.00 27.05 ?  100 THR   B O   1 
ATOM   754  C  CB  . THR   A 1 105 ? -23.105 9.718   51.655  1.00 30.68 ?  100 THR   B CB  1 
ATOM   755  O  OG1 . THR   A 1 105 ? -24.273 9.548   50.830  1.00 31.86 ?  100 THR   B OG1 1 
ATOM   756  C  CG2 . THR   A 1 105 ? -22.197 8.509   51.643  1.00 34.55 ?  100 THR   B CG2 1 
ATOM   757  N  N   . ALA   A 1 106 ? -23.660 12.506  52.867  1.00 26.77 ?  101 ALA   B N   1 
ATOM   758  C  CA  . ALA   A 1 106 ? -24.312 13.825  52.768  1.00 25.74 ?  101 ALA   B CA  1 
ATOM   759  C  C   . ALA   A 1 106 ? -23.441 14.679  51.870  1.00 27.77 ?  101 ALA   B C   1 
ATOM   760  O  O   . ALA   A 1 106 ? -22.246 14.449  51.853  1.00 27.19 ?  101 ALA   B O   1 
ATOM   761  C  CB  . ALA   A 1 106 ? -24.487 14.468  54.122  1.00 27.24 ?  101 ALA   B CB  1 
ATOM   762  N  N   . PRO   A 1 107 ? -24.006 15.594  51.041  1.00 26.47 ?  102 PRO   B N   1 
ATOM   763  C  CA  . PRO   A 1 107 ? -25.456 15.689  50.838  1.00 22.68 ?  102 PRO   B CA  1 
ATOM   764  C  C   . PRO   A 1 107 ? -25.956 14.581  49.893  1.00 21.33 ?  102 PRO   B C   1 
ATOM   765  O  O   . PRO   A 1 107 ? -25.168 13.875  49.275  1.00 20.82 ?  102 PRO   B O   1 
ATOM   766  C  CB  . PRO   A 1 107 ? -25.553 17.055  50.150  1.00 22.29 ?  102 PRO   B CB  1 
ATOM   767  C  CG  . PRO   A 1 107 ? -24.359 17.040  49.232  1.00 24.48 ?  102 PRO   B CG  1 
ATOM   768  C  CD  . PRO   A 1 107 ? -23.263 16.501  50.141  1.00 24.46 ?  102 PRO   B CD  1 
ATOM   769  N  N   . ALA   A 1 108 ? -27.281 14.500  49.698  1.00 20.05 ?  103 ALA   B N   1 
ATOM   770  C  CA  . ALA   A 1 108 ? -27.860 13.452  48.829  1.00 19.61 ?  103 ALA   B CA  1 
ATOM   771  C  C   . ALA   A 1 108 ? -29.290 13.833  48.524  1.00 18.82 ?  103 ALA   B C   1 
ATOM   772  O  O   . ALA   A 1 108 ? -29.780 14.814  49.086  1.00 18.36 ?  103 ALA   B O   1 
ATOM   773  C  CB  . ALA   A 1 108 ? -27.840 12.103  49.544  1.00 20.94 ?  103 ALA   B CB  1 
ATOM   774  N  N   . ALA   A 1 109 ? -29.914 13.048  47.662  1.00 18.17 ?  104 ALA   B N   1 
ATOM   775  C  CA  . ALA   A 1 109 ? -31.357 13.203  47.391  1.00 18.96 ?  104 ALA   B CA  1 
ATOM   776  C  C   . ALA   A 1 109 ? -31.913 11.804  47.263  1.00 18.34 ?  104 ALA   B C   1 
ATOM   777  O  O   . ALA   A 1 109 ? -31.197 10.882  46.894  1.00 19.49 ?  104 ALA   B O   1 
ATOM   778  C  CB  . ALA   A 1 109 ? -31.558 14.034  46.137  1.00 19.46 ?  104 ALA   B CB  1 
ATOM   779  N  N   . PRO   A 1 110 ? -33.202 11.561  47.586  1.00 17.53 ?  105 PRO   B N   1 
ATOM   780  C  CA  . PRO   A 1 110 ? -33.693 10.211  47.449  1.00 16.87 ?  105 PRO   B CA  1 
ATOM   781  C  C   . PRO   A 1 110 ? -33.904 9.875   45.984  1.00 18.38 ?  105 PRO   B C   1 
ATOM   782  O  O   . PRO   A 1 110 ? -33.838 10.755  45.113  1.00 19.90 ?  105 PRO   B O   1 
ATOM   783  C  CB  . PRO   A 1 110 ? -35.077 10.248  48.149  1.00 17.51 ?  105 PRO   B CB  1 
ATOM   784  C  CG  . PRO   A 1 110 ? -35.029 11.559  48.928  1.00 17.80 ?  105 PRO   B CG  1 
ATOM   785  C  CD  . PRO   A 1 110 ? -34.206 12.484  48.072  1.00 17.95 ?  105 PRO   B CD  1 
ATOM   786  N  N   . THR   A 1 111 ? -34.175 8.598   45.731  1.00 17.30 ?  106 THR   B N   1 
ATOM   787  C  CA  . THR   A 1 111 ? -34.630 8.175   44.402  1.00 18.03 ?  106 THR   B CA  1 
ATOM   788  C  C   . THR   A 1 111 ? -35.540 6.969   44.544  1.00 18.33 ?  106 THR   B C   1 
ATOM   789  O  O   . THR   A 1 111 ? -35.900 6.565   45.669  1.00 16.66 ?  106 THR   B O   1 
ATOM   790  C  CB  . THR   A 1 111 ? -33.442 7.940   43.463  1.00 19.16 ?  106 THR   B CB  1 
ATOM   791  O  OG1 . THR   A 1 111 ? -33.911 7.924   42.097  1.00 21.47 ?  106 THR   B OG1 1 
ATOM   792  C  CG2 . THR   A 1 111 ? -32.676 6.653   43.748  1.00 19.76 ?  106 THR   B CG2 1 
ATOM   793  N  N   . TRP   A 1 112 ? -35.931 6.451   43.402  1.00 18.36 ?  107 TRP   B N   1 
ATOM   794  C  CA  . TRP   A 1 112 ? -36.735 5.216   43.315  1.00 17.88 ?  107 TRP   B CA  1 
ATOM   795  C  C   . TRP   A 1 112 ? -36.038 4.286   42.339  1.00 19.38 ?  107 TRP   B C   1 
ATOM   796  O  O   . TRP   A 1 112 ? -35.931 4.646   41.178  1.00 17.79 ?  107 TRP   B O   1 
ATOM   797  C  CB  . TRP   A 1 112 ? -38.176 5.518   42.885  1.00 17.57 ?  107 TRP   B CB  1 
ATOM   798  C  CG  . TRP   A 1 112 ? -39.147 4.477   43.360  1.00 16.66 ?  107 TRP   B CG  1 
ATOM   799  C  CD1 . TRP   A 1 112 ? -39.238 3.177   42.952  1.00 17.09 ?  107 TRP   B CD1 1 
ATOM   800  C  CD2 . TRP   A 1 112 ? -40.173 4.645   44.355  1.00 16.16 ?  107 TRP   B CD2 1 
ATOM   801  N  NE1 . TRP   A 1 112 ? -40.210 2.516   43.655  1.00 16.56 ?  107 TRP   B NE1 1 
ATOM   802  C  CE2 . TRP   A 1 112 ? -40.782 3.387   44.541  1.00 15.88 ?  107 TRP   B CE2 1 
ATOM   803  C  CE3 . TRP   A 1 112 ? -40.589 5.728   45.148  1.00 16.83 ?  107 TRP   B CE3 1 
ATOM   804  C  CZ2 . TRP   A 1 112 ? -41.846 3.207   45.421  1.00 17.58 ?  107 TRP   B CZ2 1 
ATOM   805  C  CZ3 . TRP   A 1 112 ? -41.622 5.539   46.046  1.00 17.20 ?  107 TRP   B CZ3 1 
ATOM   806  C  CH2 . TRP   A 1 112 ? -42.212 4.292   46.203  1.00 17.23 ?  107 TRP   B CH2 1 
ATOM   807  N  N   . ASN   A 1 113 ? -35.519 3.151   42.813  1.00 16.70 ?  108 ASN   B N   1 
ATOM   808  C  CA  . ASN   A 1 113 ? -34.900 2.163   41.910  1.00 16.34 ?  108 ASN   B CA  1 
ATOM   809  C  C   . ASN   A 1 113 ? -36.060 1.438   41.226  1.00 15.46 ?  108 ASN   B C   1 
ATOM   810  O  O   . ASN   A 1 113 ? -37.021 1.035   41.940  1.00 17.02 ?  108 ASN   B O   1 
ATOM   811  C  CB  . ASN   A 1 113 ? -33.971 1.236   42.690  1.00 16.56 ?  108 ASN   B CB  1 
ATOM   812  C  CG  . ASN   A 1 113 ? -32.596 1.850   42.859  1.00 20.43 ?  108 ASN   B CG  1 
ATOM   813  O  OD1 . ASN   A 1 113 ? -32.351 2.984   42.444  1.00 19.56 ?  108 ASN   B OD1 1 
ATOM   814  N  ND2 . ASN   A 1 113 ? -31.707 1.113   43.489  1.00 17.81 ?  108 ASN   B ND2 1 
ATOM   815  N  N   . PHE   A 1 114 ? -36.017 1.216   39.914  1.00 15.46 ?  109 PHE   B N   1 
ATOM   816  C  CA  . PHE   A 1 114 ? -37.116 0.523   39.246  1.00 15.97 ?  109 PHE   B CA  1 
ATOM   817  C  C   . PHE   A 1 114 ? -36.599 -0.069  37.952  1.00 17.17 ?  109 PHE   B C   1 
ATOM   818  O  O   . PHE   A 1 114 ? -35.481 0.289   37.442  1.00 16.87 ?  109 PHE   B O   1 
ATOM   819  C  CB  . PHE   A 1 114 ? -38.312 1.459   39.029  1.00 14.62 ?  109 PHE   B CB  1 
ATOM   820  C  CG  . PHE   A 1 114 ? -38.131 2.487   37.933  1.00 14.52 ?  109 PHE   B CG  1 
ATOM   821  C  CD1 . PHE   A 1 114 ? -37.523 3.715   38.191  1.00 18.24 ?  109 PHE   B CD1 1 
ATOM   822  C  CD2 . PHE   A 1 114 ? -38.535 2.225   36.640  1.00 17.46 ?  109 PHE   B CD2 1 
ATOM   823  C  CE1 . PHE   A 1 114 ? -37.327 4.652   37.189  1.00 18.37 ?  109 PHE   B CE1 1 
ATOM   824  C  CE2 . PHE   A 1 114 ? -38.350 3.178   35.642  1.00 16.95 ?  109 PHE   B CE2 1 
ATOM   825  C  CZ  . PHE   A 1 114 ? -37.729 4.371   35.911  1.00 17.39 ?  109 PHE   B CZ  1 
ATOM   826  N  N   . THR   A 1 115 ? -37.425 -0.935  37.409  1.00 16.97 ?  110 THR   B N   1 
ATOM   827  C  CA  . THR   A 1 115 ? -37.105 -1.658  36.162  1.00 16.56 ?  110 THR   B CA  1 
ATOM   828  C  C   . THR   A 1 115 ? -38.290 -1.520  35.239  1.00 17.82 ?  110 THR   B C   1 
ATOM   829  O  O   . THR   A 1 115 ? -39.417 -1.679  35.692  1.00 17.06 ?  110 THR   B O   1 
ATOM   830  C  CB  . THR   A 1 115 ? -36.756 -3.123  36.442  1.00 17.50 ?  110 THR   B CB  1 
ATOM   831  O  OG1 . THR   A 1 115 ? -37.815 -3.692  37.207  1.00 19.28 ?  110 THR   B OG1 1 
ATOM   832  C  CG2 . THR   A 1 115 ? -35.427 -3.251  37.133  1.00 18.33 ?  110 THR   B CG2 1 
ATOM   833  N  N   . SER   A 1 116 ? -38.027 -1.273  33.969  1.00 17.24 ?  111 SER   B N   1 
ATOM   834  C  CA  . SER   A 1 116 ? -39.138 -1.049  33.015  1.00 19.01 ?  111 SER   B CA  1 
ATOM   835  C  C   . SER   A 1 116 ? -38.669 -1.504  31.639  1.00 18.02 ?  111 SER   B C   1 
ATOM   836  O  O   . SER   A 1 116 ? -37.469 -1.281  31.334  1.00 19.51 ?  111 SER   B O   1 
ATOM   837  C  CB  . SER   A 1 116 ? -39.506 0.415   32.980  1.00 20.93 ?  111 SER   B CB  1 
ATOM   838  O  OG  . SER   A 1 116 ? -40.529 0.610   32.049  1.00 28.09 ?  111 SER   B OG  1 
ATOM   839  N  N   . VAL   A 1 117 ? -39.528 -2.174  30.890  1.00 17.16 ?  112 VAL   B N   1 
ATOM   840  C  CA  . VAL   A 1 117 ? -39.265 -2.428  29.455  1.00 16.03 ?  112 VAL   B CA  1 
ATOM   841  C  C   . VAL   A 1 117 ? -40.404 -1.803  28.680  1.00 16.34 ?  112 VAL   B C   1 
ATOM   842  O  O   . VAL   A 1 117 ? -41.579 -2.082  29.021  1.00 16.57 ?  112 VAL   B O   1 
ATOM   843  C  CB  . VAL   A 1 117 ? -39.080 -3.929  29.170  1.00 16.55 ?  112 VAL   B CB  1 
ATOM   844  C  CG1 . VAL   A 1 117 ? -39.107 -4.239  27.686  1.00 17.45 ?  112 VAL   B CG1 1 
ATOM   845  C  CG2 . VAL   A 1 117 ? -37.781 -4.417  29.800  1.00 19.45 ?  112 VAL   B CG2 1 
ATOM   846  N  N   . GLN   A 1 118 ? -40.093 -0.997  27.675  1.00 16.64 ?  113 GLN   B N   1 
ATOM   847  C  CA  . GLN   A 1 118 ? -41.134 -0.455  26.766  1.00 17.27 ?  113 GLN   B CA  1 
ATOM   848  C  C   . GLN   A 1 118 ? -40.896 -1.060  25.388  1.00 17.43 ?  113 GLN   B C   1 
ATOM   849  O  O   . GLN   A 1 118 ? -39.792 -0.949  24.866  1.00 19.79 ?  113 GLN   B O   1 
ATOM   850  C  CB  . GLN   A 1 118 ? -41.119 1.068   26.713  1.00 18.07 ?  113 GLN   B CB  1 
ATOM   851  C  CG  . GLN   A 1 118 ? -41.506 1.721   28.046  1.00 17.70 ?  113 GLN   B CG  1 
ATOM   852  C  CD  . GLN   A 1 118 ? -41.394 3.213   28.001  1.00 18.38 ?  113 GLN   B CD  1 
ATOM   853  O  OE1 . GLN   A 1 118 ? -41.300 3.842   26.937  1.00 18.04 ?  113 GLN   B OE1 1 
ATOM   854  N  NE2 . GLN   A 1 118 ? -41.370 3.796   29.186  1.00 20.58 ?  113 GLN   B NE2 1 
ATOM   855  N  N   . VAL   A 1 119 ? -41.865 -1.757  24.862  1.00 17.51 ?  114 VAL   B N   1 
ATOM   856  C  CA  . VAL   A 1 119 ? -41.762 -2.281  23.491  1.00 18.48 ?  114 VAL   B CA  1 
ATOM   857  C  C   . VAL   A 1 119 ? -42.708 -1.459  22.630  1.00 17.98 ?  114 VAL   B C   1 
ATOM   858  O  O   . VAL   A 1 119 ? -43.863 -1.188  23.046  1.00 19.06 ?  114 VAL   B O   1 
ATOM   859  C  CB  . VAL   A 1 119 ? -42.018 -3.795  23.374  1.00 20.69 ?  114 VAL   B CB  1 
ATOM   860  C  CG1 . VAL   A 1 119 ? -40.990 -4.596  24.152  1.00 22.97 ?  114 VAL   B CG1 1 
ATOM   861  C  CG2 . VAL   A 1 119 ? -43.439 -4.198  23.751  1.00 21.58 ?  114 VAL   B CG2 1 
ATOM   862  N  N   . ARG   A 1 120 ? -42.274 -1.160  21.428  1.00 20.35 ?  115 ARG   B N   1 
ATOM   863  C  CA  . ARG   A 1 120 ? -43.073 -0.377  20.461  1.00 21.15 ?  115 ARG   B CA  1 
ATOM   864  C  C   . ARG   A 1 120 ? -43.212 -1.152  19.166  1.00 20.19 ?  115 ARG   B C   1 
ATOM   865  O  O   . ARG   A 1 120 ? -42.271 -1.794  18.760  1.00 21.46 ?  115 ARG   B O   1 
ATOM   866  C  CB  . ARG   A 1 120 ? -42.443 0.995   20.271  1.00 23.21 ?  115 ARG   B CB  1 
ATOM   867  C  CG  . ARG   A 1 120 ? -42.698 1.916   21.453  1.00 22.66 ?  115 ARG   B CG  1 
ATOM   868  C  CD  . ARG   A 1 120 ? -42.012 3.256   21.291  1.00 24.45 ?  115 ARG   B CD  1 
ATOM   869  N  NE  . ARG   A 1 120 ? -42.544 4.184   22.284  1.00 24.64 ?  115 ARG   B NE  1 
ATOM   870  C  CZ  . ARG   A 1 120 ? -42.207 4.216   23.569  1.00 25.65 ?  115 ARG   B CZ  1 
ATOM   871  N  NH1 . ARG   A 1 120 ? -41.300 3.398   24.068  1.00 22.75 1  115 ARG   B NH1 1 
ATOM   872  N  NH2 . ARG   A 1 120 ? -42.792 5.082   24.360  1.00 27.45 ?  115 ARG   B NH2 1 
ATOM   873  N  N   . GLY   A 1 121 ? -44.405 -1.179  18.617  1.00 21.32 ?  116 GLY   B N   1 
ATOM   874  C  CA  . GLY   A 1 121 ? -44.585 -1.635  17.227  1.00 22.92 ?  116 GLY   B CA  1 
ATOM   875  C  C   . GLY   A 1 121 ? -46.039 -1.579  16.873  1.00 25.36 ?  116 GLY   B C   1 
ATOM   876  O  O   . GLY   A 1 121 ? -46.784 -0.878  17.578  1.00 23.89 ?  116 GLY   B O   1 
ATOM   877  N  N   . GLU   A 1 122 ? -46.420 -2.249  15.802  1.00 24.19 ?  117 GLU   B N   1 
ATOM   878  C  CA  . GLU   A 1 122 ? -47.790 -2.178  15.245  1.00 25.36 ?  117 GLU   B CA  1 
ATOM   879  C  C   . GLU   A 1 122 ? -48.603 -3.328  15.830  1.00 25.95 ?  117 GLU   B C   1 
ATOM   880  O  O   . GLU   A 1 122 ? -48.165 -4.479  15.752  1.00 31.06 ?  117 GLU   B O   1 
ATOM   881  C  CB  . GLU   A 1 122 ? -47.641 -2.153  13.723  1.00 33.92 ?  117 GLU   B CB  1 
ATOM   882  C  CG  . GLU   A 1 122 ? -48.921 -2.084  12.943  1.00 43.52 ?  117 GLU   B CG  1 
ATOM   883  C  CD  . GLU   A 1 122 ? -48.638 -2.301  11.455  1.00 52.19 ?  117 GLU   B CD  1 
ATOM   884  O  OE1 . GLU   A 1 122 ? -49.077 -3.349  10.927  1.00 56.48 ?  117 GLU   B OE1 1 
ATOM   885  O  OE2 . GLU   A 1 122 ? -47.944 -1.437  10.839  1.00 53.86 -1 117 GLU   B OE2 1 
ATOM   886  N  N   . LEU   A 1 123 ? -49.706 -3.015  16.500  1.00 25.84 ?  118 LEU   B N   1 
ATOM   887  C  CA  . LEU   A 1 123 ? -50.601 -4.045  17.033  1.00 25.70 ?  118 LEU   B CA  1 
ATOM   888  C  C   . LEU   A 1 123 ? -51.498 -4.470  15.887  1.00 27.53 ?  118 LEU   B C   1 
ATOM   889  O  O   . LEU   A 1 123 ? -52.034 -3.587  15.204  1.00 27.12 ?  118 LEU   B O   1 
ATOM   890  C  CB  . LEU   A 1 123 ? -51.400 -3.473  18.189  1.00 24.91 ?  118 LEU   B CB  1 
ATOM   891  C  CG  . LEU   A 1 123 ? -52.351 -4.430  18.917  1.00 25.06 ?  118 LEU   B CG  1 
ATOM   892  C  CD1 . LEU   A 1 123 ? -52.476 -4.021  20.372  1.00 25.76 ?  118 LEU   B CD1 1 
ATOM   893  C  CD2 . LEU   A 1 123 ? -53.749 -4.470  18.297  1.00 29.81 ?  118 LEU   B CD2 1 
ATOM   894  N  N   . ARG   A 1 124 ? -51.553 -5.769  15.616  1.00 25.82 ?  119 ARG   B N   1 
ATOM   895  C  CA  . ARG   A 1 124 ? -52.516 -6.307  14.638  1.00 28.47 ?  119 ARG   B CA  1 
ATOM   896  C  C   . ARG   A 1 124 ? -53.484 -7.196  15.373  1.00 26.40 ?  119 ARG   B C   1 
ATOM   897  O  O   . ARG   A 1 124 ? -53.045 -8.059  16.148  1.00 25.01 ?  119 ARG   B O   1 
ATOM   898  C  CB  . ARG   A 1 124 ? -51.811 -6.978  13.460  1.00 35.72 ?  119 ARG   B CB  1 
ATOM   899  C  CG  . ARG   A 1 124 ? -50.704 -7.942  13.816  1.00 47.56 ?  119 ARG   B CG  1 
ATOM   900  C  CD  . ARG   A 1 124 ? -50.165 -8.548  12.529  1.00 56.96 ?  119 ARG   B CD  1 
ATOM   901  N  NE  . ARG   A 1 124 ? -49.559 -9.845  12.762  1.00 54.07 ?  119 ARG   B NE  1 
ATOM   902  C  CZ  . ARG   A 1 124 ? -50.233 -10.978 12.897  1.00 58.01 ?  119 ARG   B CZ  1 
ATOM   903  N  NH1 . ARG   A 1 124 ? -51.562 -10.986 12.848  1.00 57.39 1  119 ARG   B NH1 1 
ATOM   904  N  NH2 . ARG   A 1 124 ? -49.557 -12.100 13.096  1.00 58.45 ?  119 ARG   B NH2 1 
ATOM   905  N  N   . LYS   A 1 125 ? -54.767 -6.967  15.133  1.00 24.64 ?  120 LYS   B N   1 
ATOM   906  C  CA  . LYS   A 1 125 ? -55.837 -7.750  15.740  1.00 25.29 ?  120 LYS   B CA  1 
ATOM   907  C  C   . LYS   A 1 125 ? -55.869 -9.113  15.069  1.00 30.60 ?  120 LYS   B C   1 
ATOM   908  O  O   . LYS   A 1 125 ? -55.642 -9.187  13.856  1.00 27.32 ?  120 LYS   B O   1 
ATOM   909  C  CB  . LYS   A 1 125 ? -57.138 -6.987  15.600  1.00 24.17 ?  120 LYS   B CB  1 
ATOM   910  C  CG  . LYS   A 1 125 ? -57.194 -5.696  16.392  1.00 25.77 ?  120 LYS   B CG  1 
ATOM   911  C  CD  . LYS   A 1 125 ? -58.402 -4.924  16.076  1.00 28.01 ?  120 LYS   B CD  1 
ATOM   912  C  CE  . LYS   A 1 125 ? -58.723 -3.858  17.090  1.00 30.00 ?  120 LYS   B CE  1 
ATOM   913  N  NZ  . LYS   A 1 125 ? -60.121 -3.412  16.862  1.00 33.39 1  120 LYS   B NZ  1 
ATOM   914  N  N   . VAL   A 1 126 ? -56.091 -10.144 15.877  1.00 28.24 ?  121 VAL   B N   1 
ATOM   915  C  CA  . VAL   A 1 126 ? -56.504 -11.506 15.475  1.00 30.56 ?  121 VAL   B CA  1 
ATOM   916  C  C   . VAL   A 1 126 ? -58.039 -11.492 15.406  1.00 29.94 ?  121 VAL   B C   1 
ATOM   917  O  O   . VAL   A 1 126 ? -58.693 -11.102 16.405  1.00 32.61 ?  121 VAL   B O   1 
ATOM   918  C  CB  . VAL   A 1 126 ? -56.014 -12.506 16.532  1.00 35.60 ?  121 VAL   B CB  1 
ATOM   919  C  CG1 . VAL   A 1 126 ? -56.472 -13.907 16.200  1.00 38.24 ?  121 VAL   B CG1 1 
ATOM   920  C  CG2 . VAL   A 1 126 ? -54.501 -12.461 16.729  1.00 32.25 ?  121 VAL   B CG2 1 
ATOM   921  N  N   . GLU   A 1 127 ? -58.644 -11.882 14.295  1.00 30.51 ?  122 GLU   B N   1 
ATOM   922  C  CA  . GLU   A 1 127 ? -60.136 -11.966 14.301  1.00 34.19 ?  122 GLU   B CA  1 
ATOM   923  C  C   . GLU   A 1 127 ? -60.594 -13.434 14.321  1.00 39.29 ?  122 GLU   B C   1 
ATOM   924  O  O   . GLU   A 1 127 ? -61.707 -13.672 14.817  1.00 40.57 ?  122 GLU   B O   1 
ATOM   925  C  CB  . GLU   A 1 127 ? -60.725 -11.134 13.169  1.00 34.54 ?  122 GLU   B CB  1 
ATOM   926  C  CG  . GLU   A 1 127 ? -60.446 -9.646  13.301  1.00 34.33 ?  122 GLU   B CG  1 
ATOM   927  C  CD  . GLU   A 1 127 ? -61.108 -8.917  14.454  1.00 33.13 ?  122 GLU   B CD  1 
ATOM   928  O  OE1 . GLU   A 1 127 ? -61.928 -9.545  15.199  1.00 35.70 ?  122 GLU   B OE1 1 
ATOM   929  O  OE2 . GLU   A 1 127 ? -60.845 -7.686  14.576  1.00 34.37 -1 122 GLU   B OE2 1 
ATOM   930  N  N   . SER   A 1 128 ? -59.766 -14.397 13.903  1.00 33.78 ?  123 SER   B N   1 
ATOM   931  C  CA  . SER   A 1 128 ? -60.200 -15.813 13.816  1.00 34.05 ?  123 SER   B CA  1 
ATOM   932  C  C   . SER   A 1 128 ? -60.341 -16.415 15.219  1.00 30.33 ?  123 SER   B C   1 
ATOM   933  O  O   . SER   A 1 128 ? -59.492 -16.107 16.139  1.00 26.29 ?  123 SER   B O   1 
ATOM   934  C  CB  . SER   A 1 128 ? -59.291 -16.630 12.938  1.00 39.15 ?  123 SER   B CB  1 
ATOM   935  O  OG  . SER   A 1 128 ? -58.507 -17.526 13.703  1.00 36.41 ?  123 SER   B OG  1 
ATOM   936  N  N   . ALA   A 1 129 ? -61.392 -17.206 15.395  1.00 26.18 ?  124 ALA   B N   1 
ATOM   937  C  CA  . ALA   A 1 129 ? -61.670 -17.923 16.654  1.00 29.23 ?  124 ALA   B CA  1 
ATOM   938  C  C   . ALA   A 1 129 ? -60.477 -18.848 16.919  1.00 29.96 ?  124 ALA   B C   1 
ATOM   939  O  O   . ALA   A 1 129 ? -60.136 -19.024 18.088  1.00 25.63 ?  124 ALA   B O   1 
ATOM   940  C  CB  . ALA   A 1 129 ? -62.977 -18.665 16.612  1.00 30.57 ?  124 ALA   B CB  1 
ATOM   941  N  N   . ASP   A 1 130 ? -59.873 -19.426 15.883  1.00 27.77 ?  125 ASP   B N   1 
ATOM   942  C  CA  . ASP   A 1 130 ? -58.846 -20.478 16.123  1.00 30.44 ?  125 ASP   B CA  1 
ATOM   943  C  C   . ASP   A 1 130 ? -57.651 -19.779 16.749  1.00 26.77 ?  125 ASP   B C   1 
ATOM   944  O  O   . ASP   A 1 130 ? -57.095 -20.345 17.705  1.00 24.49 ?  125 ASP   B O   1 
ATOM   945  C  CB  . ASP   A 1 130 ? -58.467 -21.243 14.860  1.00 37.27 ?  125 ASP   B CB  1 
ATOM   946  C  CG  . ASP   A 1 130 ? -59.479 -22.331 14.539  1.00 53.68 ?  125 ASP   B CG  1 
ATOM   947  O  OD1 . ASP   A 1 130 ? -60.017 -22.316 13.395  1.00 62.27 ?  125 ASP   B OD1 1 
ATOM   948  O  OD2 . ASP   A 1 130 ? -59.734 -23.190 15.442  1.00 66.87 -1 125 ASP   B OD2 1 
ATOM   949  N  N   . ASP   A 1 131 ? -57.275 -18.602 16.240  1.00 24.40 ?  126 ASP   B N   1 
ATOM   950  C  CA  . ASP   A 1 131 ? -56.056 -17.879 16.695  1.00 24.31 ?  126 ASP   B CA  1 
ATOM   951  C  C   . ASP   A 1 131 ? -56.319 -17.168 18.032  1.00 22.22 ?  126 ASP   B C   1 
ATOM   952  O  O   . ASP   A 1 131 ? -55.345 -16.936 18.749  1.00 21.99 ?  126 ASP   B O   1 
ATOM   953  C  CB  . ASP   A 1 131 ? -55.570 -16.844 15.686  1.00 28.31 ?  126 ASP   B CB  1 
ATOM   954  C  CG  . ASP   A 1 131 ? -55.038 -17.377 14.374  1.00 33.28 ?  126 ASP   B CG  1 
ATOM   955  O  OD1 . ASP   A 1 131 ? -54.554 -18.538 14.351  1.00 35.12 ?  126 ASP   B OD1 1 
ATOM   956  O  OD2 . ASP   A 1 131 ? -55.145 -16.614 13.371  1.00 34.36 -1 126 ASP   B OD2 1 
ATOM   957  N  N   . THR   A 1 132 ? -57.568 -16.834 18.335  1.00 20.20 ?  127 THR   B N   1 
ATOM   958  C  CA  . THR   A 1 132 ? -58.033 -16.290 19.630  1.00 18.69 ?  127 THR   B CA  1 
ATOM   959  C  C   . THR   A 1 132 ? -57.922 -17.382 20.693  1.00 19.84 ?  127 THR   B C   1 
ATOM   960  O  O   . THR   A 1 132 ? -57.272 -17.158 21.726  1.00 19.82 ?  127 THR   B O   1 
ATOM   961  C  CB  . THR   A 1 132 ? -59.488 -15.779 19.522  1.00 19.92 ?  127 THR   B CB  1 
ATOM   962  O  OG1 . THR   A 1 132 ? -59.584 -14.746 18.549  1.00 18.59 ?  127 THR   B OG1 1 
ATOM   963  C  CG2 . THR   A 1 132 ? -59.966 -15.259 20.850  1.00 20.77 ?  127 THR   B CG2 1 
ATOM   964  N  N   . LEU   A 1 133 ? -58.373 -18.600 20.367  1.00 16.72 ?  128 LEU   B N   1 
ATOM   965  C  CA  . LEU   A 1 133 ? -58.294 -19.719 21.319  1.00 17.39 ?  128 LEU   B CA  1 
ATOM   966  C  C   . LEU   A 1 133 ? -56.803 -20.031 21.527  1.00 17.61 ?  128 LEU   B C   1 
ATOM   967  O  O   . LEU   A 1 133 ? -56.421 -20.204 22.652  1.00 17.47 ?  128 LEU   B O   1 
ATOM   968  C  CB  . LEU   A 1 133 ? -59.050 -20.938 20.771  1.00 20.01 ?  128 LEU   B CB  1 
ATOM   969  C  CG  . LEU   A 1 133 ? -59.043 -22.175 21.656  1.00 19.10 ?  128 LEU   B CG  1 
ATOM   970  C  CD1 . LEU   A 1 133 ? -59.776 -21.944 22.959  1.00 19.83 ?  128 LEU   B CD1 1 
ATOM   971  C  CD2 . LEU   A 1 133 ? -59.617 -23.398 20.920  1.00 18.87 ?  128 LEU   B CD2 1 
ATOM   972  N  N   . ALA   A 1 134 ? -56.025 -20.100 20.476  1.00 16.25 ?  129 ALA   B N   1 
ATOM   973  C  CA  . ALA   A 1 134 ? -54.557 -20.315 20.614  1.00 19.38 ?  129 ALA   B CA  1 
ATOM   974  C  C   . ALA   A 1 134 ? -53.977 -19.305 21.607  1.00 20.14 ?  129 ALA   B C   1 
ATOM   975  O  O   . ALA   A 1 134 ? -53.003 -19.690 22.361  1.00 19.55 ?  129 ALA   B O   1 
ATOM   976  C  CB  . ALA   A 1 134 ? -53.817 -20.175 19.329  1.00 19.54 ?  129 ALA   B CB  1 
ATOM   977  N  N   . THR   A 1 135 ? -54.348 -18.024 21.438  1.00 18.45 ?  130 THR   B N   1 
ATOM   978  C  CA  . THR   A 1 135 ? -53.778 -16.938 22.249  1.00 19.10 ?  130 THR   B CA  1 
ATOM   979  C  C   . THR   A 1 135 ? -54.009 -17.270 23.716  1.00 18.01 ?  130 THR   B C   1 
ATOM   980  O  O   . THR   A 1 135 ? -53.032 -17.195 24.527  1.00 16.68 ?  130 THR   B O   1 
ATOM   981  C  CB  . THR   A 1 135 ? -54.298 -15.549 21.886  1.00 17.40 ?  130 THR   B CB  1 
ATOM   982  O  OG1 . THR   A 1 135 ? -54.091 -15.376 20.489  1.00 17.83 ?  130 THR   B OG1 1 
ATOM   983  C  CG2 . THR   A 1 135 ? -53.610 -14.457 22.690  1.00 18.76 ?  130 THR   B CG2 1 
ATOM   984  N  N   . VAL   A 1 136 ? -55.260 -17.501 24.117  1.00 17.02 ?  131 VAL   B N   1 
ATOM   985  C  CA  . VAL   A 1 136 ? -55.556 -17.692 25.554  1.00 16.76 ?  131 VAL   B CA  1 
ATOM   986  C  C   . VAL   A 1 136 ? -54.988 -19.025 26.056  1.00 16.99 ?  131 VAL   B C   1 
ATOM   987  O  O   . VAL   A 1 136 ? -54.490 -19.013 27.196  1.00 17.26 ?  131 VAL   B O   1 
ATOM   988  C  CB  . VAL   A 1 136 ? -57.066 -17.553 25.897  1.00 18.66 ?  131 VAL   B CB  1 
ATOM   989  C  CG1 . VAL   A 1 136 ? -57.584 -16.161 25.592  1.00 19.72 ?  131 VAL   B CG1 1 
ATOM   990  C  CG2 . VAL   A 1 136 ? -57.893 -18.623 25.250  1.00 18.06 ?  131 VAL   B CG2 1 
ATOM   991  N  N   . ARG   A 1 137 ? -54.955 -20.113 25.255  1.00 16.53 ?  132 ARG   B N   1 
ATOM   992  C  CA  . ARG   A 1 137 ? -54.382 -21.388 25.721  1.00 16.36 ?  132 ARG   B CA  1 
ATOM   993  C  C   . ARG   A 1 137 ? -52.856 -21.216 25.890  1.00 15.95 ?  132 ARG   B C   1 
ATOM   994  O  O   . ARG   A 1 137 ? -52.327 -21.730 26.830  1.00 17.34 ?  132 ARG   B O   1 
ATOM   995  C  CB  . ARG   A 1 137 ? -54.726 -22.544 24.770  1.00 16.36 ?  132 ARG   B CB  1 
ATOM   996  C  CG  . ARG   A 1 137 ? -56.238 -22.779 24.664  1.00 15.33 ?  132 ARG   B CG  1 
ATOM   997  C  CD  . ARG   A 1 137 ? -56.497 -24.130 24.038  1.00 16.70 ?  132 ARG   B CD  1 
ATOM   998  N  NE  . ARG   A 1 137 ? -55.978 -24.258 22.711  1.00 17.07 ?  132 ARG   B NE  1 
ATOM   999  C  CZ  . ARG   A 1 137 ? -56.245 -25.301 21.914  1.00 18.00 ?  132 ARG   B CZ  1 
ATOM   1000 N  NH1 . ARG   A 1 137 ? -57.223 -26.131 22.207  1.00 21.84 1  132 ARG   B NH1 1 
ATOM   1001 N  NH2 . ARG   A 1 137 ? -55.643 -25.404 20.754  1.00 19.91 ?  132 ARG   B NH2 1 
ATOM   1002 N  N   . ALA   A 1 138 ? -52.191 -20.479 25.028  1.00 15.96 ?  133 ALA   B N   1 
ATOM   1003 C  CA  . ALA   A 1 138 ? -50.735 -20.277 25.098  1.00 15.30 ?  133 ALA   B CA  1 
ATOM   1004 C  C   . ALA   A 1 138 ? -50.427 -19.453 26.354  1.00 16.09 ?  133 ALA   B C   1 
ATOM   1005 O  O   . ALA   A 1 138 ? -49.371 -19.691 27.052  1.00 17.32 ?  133 ALA   B O   1 
ATOM   1006 C  CB  . ALA   A 1 138 ? -50.214 -19.608 23.890  1.00 15.56 ?  133 ALA   B CB  1 
ATOM   1007 N  N   . THR   A 1 139 ? -51.297 -18.508 26.627  1.00 16.54 ?  134 THR   B N   1 
ATOM   1008 C  CA  . THR   A 1 139 ? -51.148 -17.617 27.811  1.00 16.76 ?  134 THR   B CA  1 
ATOM   1009 C  C   . THR   A 1 139 ? -51.317 -18.478 29.063  1.00 16.33 ?  134 THR   B C   1 
ATOM   1010 O  O   . THR   A 1 139 ? -50.558 -18.278 30.012  1.00 17.18 ?  134 THR   B O   1 
ATOM   1011 C  CB  . THR   A 1 139 ? -52.091 -16.421 27.743  1.00 17.61 ?  134 THR   B CB  1 
ATOM   1012 O  OG1 . THR   A 1 139 ? -51.864 -15.691 26.532  1.00 16.93 ?  134 THR   B OG1 1 
ATOM   1013 C  CG2 . THR   A 1 139 ? -51.946 -15.509 28.952  1.00 17.91 ?  134 THR   B CG2 1 
ATOM   1014 N  N   . VAL   A 1 140 ? -52.297 -19.370 29.112  1.00 16.22 ?  135 VAL   B N   1 
ATOM   1015 C  CA  . VAL   A 1 140 ? -52.427 -20.236 30.328  1.00 17.43 ?  135 VAL   B CA  1 
ATOM   1016 C  C   . VAL   A 1 140 ? -51.110 -20.990 30.443  1.00 17.14 ?  135 VAL   B C   1 
ATOM   1017 O  O   . VAL   A 1 140 ? -50.582 -21.103 31.579  1.00 17.39 ?  135 VAL   B O   1 
ATOM   1018 C  CB  . VAL   A 1 140 ? -53.624 -21.191 30.264  1.00 17.91 ?  135 VAL   B CB  1 
ATOM   1019 C  CG1 . VAL   A 1 140 ? -53.632 -22.153 31.456  1.00 18.74 ?  135 VAL   B CG1 1 
ATOM   1020 C  CG2 . VAL   A 1 140 ? -54.919 -20.423 30.187  1.00 18.15 ?  135 VAL   B CG2 1 
ATOM   1021 N  N   . ALA   A 1 141 ? -50.663 -21.637 29.373  1.00 17.21 ?  136 ALA   B N   1 
ATOM   1022 C  CA  . ALA   A 1 141 ? -49.469 -22.515 29.485  1.00 18.50 ?  136 ALA   B CA  1 
ATOM   1023 C  C   . ALA   A 1 141 ? -48.278 -21.737 30.057  1.00 22.67 ?  136 ALA   B C   1 
ATOM   1024 O  O   . ALA   A 1 141 ? -47.554 -22.291 31.001  1.00 23.11 ?  136 ALA   B O   1 
ATOM   1025 C  CB  . ALA   A 1 141 ? -49.128 -23.150 28.161  1.00 18.85 ?  136 ALA   B CB  1 
ATOM   1026 N  N   . ALA   A 1 142 ? -48.048 -20.527 29.539  1.00 20.34 ?  137 ALA   B N   1 
ATOM   1027 C  CA  . ALA   A 1 142 ? -46.889 -19.698 29.939  1.00 18.32 ?  137 ALA   B CA  1 
ATOM   1028 C  C   . ALA   A 1 142 ? -47.098 -19.198 31.376  1.00 18.30 ?  137 ALA   B C   1 
ATOM   1029 O  O   . ALA   A 1 142 ? -46.143 -19.245 32.157  1.00 21.09 ?  137 ALA   B O   1 
ATOM   1030 C  CB  . ALA   A 1 142 ? -46.681 -18.593 28.958  1.00 19.03 ?  137 ALA   B CB  1 
ATOM   1031 N  N   . LEU   A 1 143 ? -48.312 -18.807 31.764  1.00 14.63 ?  138 LEU   B N   1 
ATOM   1032 C  CA  . LEU   A 1 143 ? -48.438 -18.111 33.079  1.00 16.31 ?  138 LEU   B CA  1 
ATOM   1033 C  C   . LEU   A 1 143 ? -48.650 -19.144 34.202  1.00 16.74 ?  138 LEU   B C   1 
ATOM   1034 O  O   . LEU   A 1 143 ? -48.152 -18.901 35.292  1.00 16.90 ?  138 LEU   B O   1 
ATOM   1035 C  CB  . LEU   A 1 143 ? -49.550 -17.062 33.111  1.00 16.22 ?  138 LEU   B CB  1 
ATOM   1036 C  CG  . LEU   A 1 143 ? -49.510 -15.895 32.145  1.00 21.65 ?  138 LEU   B CG  1 
ATOM   1037 C  CD1 . LEU   A 1 143 ? -50.274 -14.701 32.666  1.00 17.99 ?  138 LEU   B CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 143 ? -48.168 -15.561 31.547  1.00 23.28 ?  138 LEU   B CD2 1 
ATOM   1039 N  N   . GLU   A 1 144 ? -49.465 -20.181 33.986  1.00 18.69 ?  139 GLU   B N   1 
ATOM   1040 C  CA  . GLU   A 1 144 ? -49.761 -21.165 35.052  1.00 17.85 ?  139 GLU   B CA  1 
ATOM   1041 C  C   . GLU   A 1 144 ? -48.429 -21.815 35.453  1.00 19.00 ?  139 GLU   B C   1 
ATOM   1042 O  O   . GLU   A 1 144 ? -48.232 -22.018 36.671  1.00 18.75 ?  139 GLU   B O   1 
ATOM   1043 C  CB  . GLU   A 1 144 ? -50.825 -22.156 34.629  1.00 19.09 ?  139 GLU   B CB  1 
ATOM   1044 C  CG  . GLU   A 1 144 ? -51.263 -23.095 35.745  1.00 20.98 ?  139 GLU   B CG  1 
ATOM   1045 C  CD  . GLU   A 1 144 ? -51.977 -22.459 36.933  1.00 19.51 ?  139 GLU   B CD  1 
ATOM   1046 O  OE1 . GLU   A 1 144 ? -52.542 -21.300 36.793  1.00 19.68 ?  139 GLU   B OE1 1 
ATOM   1047 O  OE2 . GLU   A 1 144 ? -51.926 -23.101 38.027  1.00 20.43 -1 139 GLU   B OE2 1 
ATOM   1048 N  N   . SER   A 1 145 ? -47.588 -22.161 34.481  1.00 22.40 ?  140 SER   B N   1 
ATOM   1049 C  CA  . SER   A 1 145 ? -46.253 -22.779 34.757  1.00 25.16 ?  140 SER   B CA  1 
ATOM   1050 C  C   . SER   A 1 145 ? -45.423 -21.814 35.618  1.00 23.88 ?  140 SER   B C   1 
ATOM   1051 O  O   . SER   A 1 145 ? -44.915 -22.207 36.678  1.00 26.05 ?  140 SER   B O   1 
ATOM   1052 C  CB  . SER   A 1 145 ? -45.537 -23.153 33.495  1.00 26.29 ?  140 SER   B CB  1 
ATOM   1053 O  OG  . SER   A 1 145 ? -45.312 -22.010 32.682  1.00 36.35 ?  140 SER   B OG  1 
ATOM   1054 N  N   . ARG   A 1 146 ? -45.384 -20.535 35.285  1.00 22.84 ?  141 ARG   B N   1 
ATOM   1055 C  CA  . ARG   A 1 146 ? -44.450 -19.599 35.957  1.00 22.44 ?  141 ARG   B CA  1 
ATOM   1056 C  C   . ARG   A 1 146 ? -44.992 -19.043 37.273  1.00 20.63 ?  141 ARG   B C   1 
ATOM   1057 O  O   . ARG   A 1 146 ? -44.200 -18.812 38.165  1.00 22.20 ?  141 ARG   B O   1 
ATOM   1058 C  CB  . ARG   A 1 146 ? -44.084 -18.462 34.998  1.00 23.23 ?  141 ARG   B CB  1 
ATOM   1059 C  CG  . ARG   A 1 146 ? -43.025 -17.516 35.543  1.00 27.05 ?  141 ARG   B CG  1 
ATOM   1060 C  CD  . ARG   A 1 146 ? -42.631 -16.528 34.462  1.00 29.41 ?  141 ARG   B CD  1 
ATOM   1061 N  NE  . ARG   A 1 146 ? -42.051 -17.230 33.325  1.00 34.94 ?  141 ARG   B NE  1 
ATOM   1062 C  CZ  . ARG   A 1 146 ? -40.740 -17.344 33.081  1.00 39.08 ?  141 ARG   B CZ  1 
ATOM   1063 N  NH1 . ARG   A 1 146 ? -39.837 -16.792 33.879  1.00 42.08 1  141 ARG   B NH1 1 
ATOM   1064 N  NH2 . ARG   A 1 146 ? -40.349 -18.023 32.023  1.00 40.58 ?  141 ARG   B NH2 1 
ATOM   1065 N  N   . PHE   A 1 147 ? -46.297 -18.783 37.411  1.00 17.26 ?  142 PHE   B N   1 
ATOM   1066 C  CA  . PHE   A 1 147 ? -46.892 -18.030 38.538  1.00 18.26 ?  142 PHE   B CA  1 
ATOM   1067 C  C   . PHE   A 1 147 ? -47.962 -18.838 39.280  1.00 18.52 ?  142 PHE   B C   1 
ATOM   1068 O  O   . PHE   A 1 147 ? -48.484 -18.340 40.300  1.00 20.93 ?  142 PHE   B O   1 
ATOM   1069 C  CB  . PHE   A 1 147 ? -47.568 -16.778 37.992  1.00 18.33 ?  142 PHE   B CB  1 
ATOM   1070 C  CG  . PHE   A 1 147 ? -46.630 -15.889 37.219  1.00 17.96 ?  142 PHE   B CG  1 
ATOM   1071 C  CD1 . PHE   A 1 147 ? -45.711 -15.083 37.890  1.00 19.36 ?  142 PHE   B CD1 1 
ATOM   1072 C  CD2 . PHE   A 1 147 ? -46.700 -15.801 35.833  1.00 17.38 ?  142 PHE   B CD2 1 
ATOM   1073 C  CE1 . PHE   A 1 147 ? -44.835 -14.282 37.173  1.00 20.18 ?  142 PHE   B CE1 1 
ATOM   1074 C  CE2 . PHE   A 1 147 ? -45.788 -15.042 35.120  1.00 18.06 ?  142 PHE   B CE2 1 
ATOM   1075 C  CZ  . PHE   A 1 147 ? -44.881 -14.255 35.793  1.00 19.13 ?  142 PHE   B CZ  1 
ATOM   1076 N  N   . GLY   A 1 148 ? -48.306 -20.008 38.761  1.00 19.75 ?  143 GLY   B N   1 
ATOM   1077 C  CA  . GLY   A 1 148 ? -49.504 -20.718 39.221  1.00 20.69 ?  143 GLY   B CA  1 
ATOM   1078 C  C   . GLY   A 1 148 ? -49.227 -21.765 40.279  1.00 23.51 ?  143 GLY   B C   1 
ATOM   1079 O  O   . GLY   A 1 148 ? -48.177 -21.703 40.953  1.00 24.25 ?  143 GLY   B O   1 
ATOM   1080 N  N   . ALA   A 1 149 ? -50.143 -22.729 40.358  1.00 24.30 ?  144 ALA   B N   1 
ATOM   1081 C  CA  . ALA   A 1 149 ? -50.245 -23.721 41.452  1.00 26.20 ?  144 ALA   B CA  1 
ATOM   1082 C  C   . ALA   A 1 149 ? -50.649 -25.076 40.869  1.00 27.52 ?  144 ALA   B C   1 
ATOM   1083 O  O   . ALA   A 1 149 ? -51.349 -25.827 41.559  1.00 28.52 ?  144 ALA   B O   1 
ATOM   1084 C  CB  . ALA   A 1 149 ? -51.214 -23.217 42.494  1.00 25.54 ?  144 ALA   B CB  1 
ATOM   1085 N  N   . GLY   A 1 150 ? -50.166 -25.393 39.673  1.00 23.44 ?  145 GLY   B N   1 
ATOM   1086 C  CA  . GLY   A 1 150 ? -50.281 -26.714 39.039  1.00 23.75 ?  145 GLY   B CA  1 
ATOM   1087 C  C   . GLY   A 1 150 ? -51.677 -26.974 38.505  1.00 26.01 ?  145 GLY   B C   1 
ATOM   1088 O  O   . GLY   A 1 150 ? -52.111 -28.165 38.345  1.00 24.24 ?  145 GLY   B O   1 
ATOM   1089 N  N   . TRP   A 1 151 ? -52.391 -25.928 38.155  1.00 20.40 ?  146 TRP   B N   1 
ATOM   1090 C  CA  . TRP   A 1 151 ? -53.739 -26.128 37.588  1.00 20.40 ?  146 TRP   B CA  1 
ATOM   1091 C  C   . TRP   A 1 151 ? -53.625 -26.732 36.194  1.00 21.89 ?  146 TRP   B C   1 
ATOM   1092 O  O   . TRP   A 1 151 ? -52.822 -26.242 35.358  1.00 23.33 ?  146 TRP   B O   1 
ATOM   1093 C  CB  . TRP   A 1 151 ? -54.490 -24.822 37.503  1.00 19.85 ?  146 TRP   B CB  1 
ATOM   1094 C  CG  . TRP   A 1 151 ? -55.874 -24.955 36.954  1.00 18.03 ?  146 TRP   B CG  1 
ATOM   1095 C  CD1 . TRP   A 1 151 ? -56.932 -25.587 37.533  1.00 19.95 ?  146 TRP   B CD1 1 
ATOM   1096 C  CD2 . TRP   A 1 151 ? -56.350 -24.402 35.715  1.00 17.73 ?  146 TRP   B CD2 1 
ATOM   1097 N  NE1 . TRP   A 1 151 ? -58.046 -25.469 36.732  1.00 19.94 ?  146 TRP   B NE1 1 
ATOM   1098 C  CE2 . TRP   A 1 151 ? -57.730 -24.739 35.630  1.00 16.93 ?  146 TRP   B CE2 1 
ATOM   1099 C  CE3 . TRP   A 1 151 ? -55.788 -23.646 34.685  1.00 16.31 ?  146 TRP   B CE3 1 
ATOM   1100 C  CZ2 . TRP   A 1 151 ? -58.514 -24.331 34.563  1.00 18.42 ?  146 TRP   B CZ2 1 
ATOM   1101 C  CZ3 . TRP   A 1 151 ? -56.566 -23.245 33.631  1.00 17.39 ?  146 TRP   B CZ3 1 
ATOM   1102 C  CH2 . TRP   A 1 151 ? -57.925 -23.581 33.580  1.00 18.50 ?  146 TRP   B CH2 1 
ATOM   1103 N  N   . ASP   A 1 152 ? -54.486 -27.699 35.916  1.00 22.45 ?  147 ASP   B N   1 
ATOM   1104 C  CA  . ASP   A 1 152 ? -54.531 -28.366 34.589  1.00 20.82 ?  147 ASP   B CA  1 
ATOM   1105 C  C   . ASP   A 1 152 ? -55.722 -27.817 33.832  1.00 19.71 ?  147 ASP   B C   1 
ATOM   1106 O  O   . ASP   A 1 152 ? -56.868 -28.024 34.260  1.00 22.00 ?  147 ASP   B O   1 
ATOM   1107 C  CB  . ASP   A 1 152 ? -54.555 -29.895 34.800  1.00 23.80 ?  147 ASP   B CB  1 
ATOM   1108 C  CG  . ASP   A 1 152 ? -54.776 -30.705 33.534  1.00 24.01 ?  147 ASP   B CG  1 
ATOM   1109 O  OD1 . ASP   A 1 152 ? -54.703 -30.115 32.437  1.00 22.00 ?  147 ASP   B OD1 1 
ATOM   1110 O  OD2 . ASP   A 1 152 ? -55.004 -31.946 33.659  1.00 26.78 -1 147 ASP   B OD2 1 
ATOM   1111 N  N   . MET   A 1 153 ? -55.479 -27.142 32.706  1.00 19.77 ?  148 MET   B N   1 
ATOM   1112 C  CA  . MET   A 1 153 ? -56.539 -26.513 31.888  1.00 21.00 ?  148 MET   B CA  1 
ATOM   1113 C  C   . MET   A 1 153 ? -57.338 -27.587 31.145  1.00 21.03 ?  148 MET   B C   1 
ATOM   1114 O  O   . MET   A 1 153 ? -58.405 -27.243 30.632  1.00 19.64 ?  148 MET   B O   1 
ATOM   1115 C  CB  . MET   A 1 153 ? -55.995 -25.519 30.874  1.00 20.03 ?  148 MET   B CB  1 
ATOM   1116 C  CG  . MET   A 1 153 ? -55.235 -26.181 29.699  1.00 21.85 ?  148 MET   B CG  1 
ATOM   1117 S  SD  . MET   A 1 153 ? -54.556 -24.918 28.555  1.00 24.71 ?  148 MET   B SD  1 
ATOM   1118 C  CE  . MET   A 1 153 ? -52.837 -24.780 29.071  1.00 21.20 ?  148 MET   B CE  1 
ATOM   1119 N  N   . THR   A 1 154 ? -56.903 -28.856 31.158  1.00 21.82 ?  149 THR   B N   1 
ATOM   1120 C  CA  . THR   A 1 154 ? -57.528 -29.889 30.295  1.00 21.30 ?  149 THR   B CA  1 
ATOM   1121 C  C   . THR   A 1 154 ? -59.046 -29.888 30.498  1.00 22.67 ?  149 THR   B C   1 
ATOM   1122 O  O   . THR   A 1 154 ? -59.790 -29.804 29.505  1.00 22.43 ?  149 THR   B O   1 
ATOM   1123 C  CB  . THR   A 1 154 ? -56.908 -31.263 30.539  1.00 23.00 ?  149 THR   B CB  1 
ATOM   1124 O  OG1 . THR   A 1 154 ? -55.498 -31.108 30.277  1.00 24.72 ?  149 THR   B OG1 1 
ATOM   1125 C  CG2 . THR   A 1 154 ? -57.576 -32.280 29.639  1.00 24.97 ?  149 THR   B CG2 1 
ATOM   1126 N  N   . GLY   A 1 155 ? -59.491 -29.957 31.745  1.00 23.89 ?  150 GLY   B N   1 
ATOM   1127 C  CA  . GLY   A 1 155 ? -60.938 -30.008 32.047  1.00 23.33 ?  150 GLY   B CA  1 
ATOM   1128 C  C   . GLY   A 1 155 ? -61.707 -28.784 31.598  1.00 24.44 ?  150 GLY   B C   1 
ATOM   1129 O  O   . GLY   A 1 155 ? -62.992 -28.826 31.648  1.00 26.52 ?  150 GLY   B O   1 
ATOM   1130 N  N   . SER   A 1 156 ? -61.037 -27.683 31.260  1.00 20.72 ?  151 SER   B N   1 
ATOM   1131 C  CA  . SER   A 1 156 ? -61.672 -26.377 30.942  1.00 19.98 ?  151 SER   B CA  1 
ATOM   1132 C  C   . SER   A 1 156 ? -61.485 -26.053 29.466  1.00 19.07 ?  151 SER   B C   1 
ATOM   1133 O  O   . SER   A 1 156 ? -61.837 -24.955 29.010  1.00 20.42 ?  151 SER   B O   1 
ATOM   1134 C  CB  . SER   A 1 156 ? -61.155 -25.283 31.867  1.00 18.13 ?  151 SER   B CB  1 
ATOM   1135 O  OG  . SER   A 1 156 ? -61.401 -25.628 33.226  1.00 20.38 ?  151 SER   B OG  1 
ATOM   1136 N  N   . LEU   A 1 157 ? -60.927 -26.991 28.677  1.00 21.49 ?  152 LEU   B N   1 
ATOM   1137 C  CA  . LEU   A 1 157 ? -60.623 -26.615 27.275  1.00 20.64 ?  152 LEU   B CA  1 
ATOM   1138 C  C   . LEU   A 1 157 ? -61.889 -26.281 26.514  1.00 20.43 ?  152 LEU   B C   1 
ATOM   1139 O  O   . LEU   A 1 157 ? -61.877 -25.297 25.720  1.00 20.95 ?  152 LEU   B O   1 
ATOM   1140 C  CB  . LEU   A 1 157 ? -59.856 -27.742 26.597  1.00 23.99 ?  152 LEU   B CB  1 
ATOM   1141 C  CG  . LEU   A 1 157 ? -58.387 -27.830 26.992  1.00 25.50 ?  152 LEU   B CG  1 
ATOM   1142 C  CD1 . LEU   A 1 157 ? -57.813 -29.130 26.435  1.00 31.23 ?  152 LEU   B CD1 1 
ATOM   1143 C  CD2 . LEU   A 1 157 ? -57.632 -26.617 26.501  1.00 30.71 ?  152 LEU   B CD2 1 
ATOM   1144 N  N   . ASP   A 1 158 ? -62.972 -27.017 26.749  1.00 23.08 ?  153 ASP   B N   1 
ATOM   1145 C  CA  . ASP   A 1 158 ? -64.237 -26.705 26.037  1.00 25.37 ?  153 ASP   B CA  1 
ATOM   1146 C  C   . ASP   A 1 158 ? -64.861 -25.448 26.638  1.00 22.74 ?  153 ASP   B C   1 
ATOM   1147 O  O   . ASP   A 1 158 ? -65.424 -24.653 25.898  1.00 19.02 ?  153 ASP   B O   1 
ATOM   1148 C  CB  . ASP   A 1 158 ? -65.176 -27.909 26.008  1.00 29.87 ?  153 ASP   B CB  1 
ATOM   1149 C  CG  . ASP   A 1 158 ? -64.762 -28.899 24.917  1.00 41.72 ?  153 ASP   B CG  1 
ATOM   1150 O  OD1 . ASP   A 1 158 ? -64.610 -28.455 23.740  1.00 40.21 ?  153 ASP   B OD1 1 
ATOM   1151 O  OD2 . ASP   A 1 158 ? -64.590 -30.094 25.254  1.00 48.48 -1 153 ASP   B OD2 1 
ATOM   1152 N  N   . TYR   A 1 159 ? -64.749 -25.260 27.949  1.00 23.36 ?  154 TYR   B N   1 
ATOM   1153 C  CA  . TYR   A 1 159 ? -65.226 -24.014 28.609  1.00 22.14 ?  154 TYR   B CA  1 
ATOM   1154 C  C   . TYR   A 1 159 ? -64.597 -22.782 27.955  1.00 19.95 ?  154 TYR   B C   1 
ATOM   1155 O  O   . TYR   A 1 159 ? -65.248 -21.810 27.663  1.00 20.90 ?  154 TYR   B O   1 
ATOM   1156 C  CB  . TYR   A 1 159 ? -64.914 -24.068 30.099  1.00 21.27 ?  154 TYR   B CB  1 
ATOM   1157 C  CG  . TYR   A 1 159 ? -65.267 -22.806 30.837  1.00 21.79 ?  154 TYR   B CG  1 
ATOM   1158 C  CD1 . TYR   A 1 159 ? -66.594 -22.479 31.048  1.00 20.59 ?  154 TYR   B CD1 1 
ATOM   1159 C  CD2 . TYR   A 1 159 ? -64.291 -21.985 31.371  1.00 21.66 ?  154 TYR   B CD2 1 
ATOM   1160 C  CE1 . TYR   A 1 159 ? -66.934 -21.317 31.718  1.00 21.50 ?  154 TYR   B CE1 1 
ATOM   1161 C  CE2 . TYR   A 1 159 ? -64.607 -20.817 32.051  1.00 21.28 ?  154 TYR   B CE2 1 
ATOM   1162 C  CZ  . TYR   A 1 159 ? -65.947 -20.504 32.252  1.00 20.12 ?  154 TYR   B CZ  1 
ATOM   1163 O  OH  . TYR   A 1 159 ? -66.316 -19.348 32.884  1.00 25.69 ?  154 TYR   B OH  1 
ATOM   1164 N  N   . PHE   A 1 160 ? -63.292 -22.789 27.674  1.00 19.26 ?  155 PHE   B N   1 
ATOM   1165 C  CA  . PHE   A 1 160 ? -62.652 -21.669 26.975  1.00 19.97 ?  155 PHE   B CA  1 
ATOM   1166 C  C   . PHE   A 1 160 ? -63.399 -21.339 25.694  1.00 20.66 ?  155 PHE   B C   1 
ATOM   1167 O  O   . PHE   A 1 160 ? -63.548 -20.154 25.375  1.00 18.68 ?  155 PHE   B O   1 
ATOM   1168 C  CB  . PHE   A 1 160 ? -61.197 -21.965 26.613  1.00 19.27 ?  155 PHE   B CB  1 
ATOM   1169 C  CG  . PHE   A 1 160 ? -60.254 -22.178 27.764  1.00 18.56 ?  155 PHE   B CG  1 
ATOM   1170 C  CD1 . PHE   A 1 160 ? -60.607 -21.946 29.085  1.00 17.89 ?  155 PHE   B CD1 1 
ATOM   1171 C  CD2 . PHE   A 1 160 ? -58.935 -22.512 27.493  1.00 20.08 ?  155 PHE   B CD2 1 
ATOM   1172 C  CE1 . PHE   A 1 160 ? -59.695 -22.140 30.104  1.00 19.91 ?  155 PHE   B CE1 1 
ATOM   1173 C  CE2 . PHE   A 1 160 ? -58.011 -22.678 28.512  1.00 18.98 ?  155 PHE   B CE2 1 
ATOM   1174 C  CZ  . PHE   A 1 160 ? -58.390 -22.468 29.821  1.00 19.68 ?  155 PHE   B CZ  1 
ATOM   1175 N  N   . ARG   A 1 161 ? -63.760 -22.353 24.915  1.00 17.76 ?  156 ARG   B N   1 
ATOM   1176 C  CA  . ARG   A 1 161 ? -64.407 -22.121 23.631  1.00 20.74 ?  156 ARG   B CA  1 
ATOM   1177 C  C   . ARG   A 1 161 ? -65.803 -21.577 23.935  1.00 18.65 ?  156 ARG   B C   1 
ATOM   1178 O  O   . ARG   A 1 161 ? -66.246 -20.732 23.196  1.00 20.66 ?  156 ARG   B O   1 
ATOM   1179 C  CB  . ARG   A 1 161 ? -64.506 -23.420 22.819  1.00 21.83 ?  156 ARG   B CB  1 
ATOM   1180 C  CG  . ARG   A 1 161 ? -63.146 -23.984 22.436  1.00 21.75 ?  156 ARG   B CG  1 
ATOM   1181 C  CD  . ARG   A 1 161 ? -63.320 -25.327 21.725  1.00 22.52 ?  156 ARG   B CD  1 
ATOM   1182 N  NE  . ARG   A 1 161 ? -63.833 -25.027 20.411  1.00 25.57 ?  156 ARG   B NE  1 
ATOM   1183 C  CZ  . ARG   A 1 161 ? -64.320 -25.921 19.543  1.00 28.00 ?  156 ARG   B CZ  1 
ATOM   1184 N  NH1 . ARG   A 1 161 ? -64.305 -27.205 19.815  1.00 30.90 1  156 ARG   B NH1 1 
ATOM   1185 N  NH2 . ARG   A 1 161 ? -64.753 -25.504 18.373  1.00 30.94 ?  156 ARG   B NH2 1 
ATOM   1186 N  N   . ARG   A 1 162 ? -66.393 -21.987 25.054  1.00 20.22 ?  157 ARG   B N   1 
ATOM   1187 C  CA  . ARG   A 1 162 ? -67.788 -21.558 25.426  1.00 20.16 ?  157 ARG   B CA  1 
ATOM   1188 C  C   . ARG   A 1 162 ? -67.822 -20.103 25.966  1.00 20.39 ?  157 ARG   B C   1 
ATOM   1189 O  O   . ARG   A 1 162 ? -68.914 -19.552 26.054  1.00 20.14 ?  157 ARG   B O   1 
ATOM   1190 C  CB  . ARG   A 1 162 ? -68.422 -22.504 26.454  1.00 23.05 ?  157 ARG   B CB  1 
ATOM   1191 C  CG  . ARG   A 1 162 ? -68.800 -23.880 25.945  1.00 25.63 ?  157 ARG   B CG  1 
ATOM   1192 C  CD  . ARG   A 1 162 ? -69.751 -24.611 26.874  1.00 25.73 ?  157 ARG   B CD  1 
ATOM   1193 N  NE  . ARG   A 1 162 ? -69.328 -24.787 28.255  1.00 27.30 ?  157 ARG   B NE  1 
ATOM   1194 C  CZ  . ARG   A 1 162 ? -68.577 -25.793 28.683  1.00 27.21 ?  157 ARG   B CZ  1 
ATOM   1195 N  NH1 . ARG   A 1 162 ? -68.249 -25.875 29.954  1.00 28.50 1  157 ARG   B NH1 1 
ATOM   1196 N  NH2 . ARG   A 1 162 ? -68.168 -26.726 27.837  1.00 29.38 ?  157 ARG   B NH2 1 
ATOM   1197 N  N   . ILE   A 1 163 ? -66.693 -19.500 26.326  1.00 19.45 ?  158 ILE   B N   1 
ATOM   1198 C  CA  . ILE   A 1 163 ? -66.631 -18.094 26.808  1.00 19.40 ?  158 ILE   B CA  1 
ATOM   1199 C  C   . ILE   A 1 163 ? -65.756 -17.249 25.864  1.00 19.94 ?  158 ILE   B C   1 
ATOM   1200 O  O   . ILE   A 1 163 ? -65.474 -16.086 26.204  1.00 23.63 ?  158 ILE   B O   1 
ATOM   1201 C  CB  . ILE   A 1 163 ? -66.140 -18.015 28.255  1.00 20.66 ?  158 ILE   B CB  1 
ATOM   1202 C  CG1 . ILE   A 1 163 ? -64.724 -18.550 28.475  1.00 21.26 ?  158 ILE   B CG1 1 
ATOM   1203 C  CG2 . ILE   A 1 163 ? -67.092 -18.674 29.195  1.00 21.28 ?  158 ILE   B CG2 1 
ATOM   1204 C  CD1 . ILE   A 1 163 ? -64.041 -17.891 29.650  1.00 21.03 ?  158 ILE   B CD1 1 
ATOM   1205 N  N   . LEU   A 1 164 ? -65.476 -17.687 24.655  1.00 21.46 ?  159 LEU   B N   1 
ATOM   1206 C  CA  . LEU   A 1 164 ? -64.426 -17.045 23.795  1.00 20.37 ?  159 LEU   B CA  1 
ATOM   1207 C  C   . LEU   A 1 164 ? -64.813 -15.719 23.152  1.00 22.76 ?  159 LEU   B C   1 
ATOM   1208 O  O   . LEU   A 1 164 ? -63.918 -14.983 22.760  1.00 23.28 ?  159 LEU   B O   1 
ATOM   1209 C  CB  . LEU   A 1 164 ? -64.036 -18.007 22.671  1.00 20.58 ?  159 LEU   B CB  1 
ATOM   1210 C  CG  . LEU   A 1 164 ? -62.682 -17.755 22.010  1.00 22.47 ?  159 LEU   B CG  1 
ATOM   1211 C  CD1 . LEU   A 1 164 ? -61.555 -18.030 23.002  1.00 21.90 ?  159 LEU   B CD1 1 
ATOM   1212 C  CD2 . LEU   A 1 164 ? -62.519 -18.611 20.775  1.00 22.83 ?  159 LEU   B CD2 1 
ATOM   1213 N  N   . PRO   A 1 165 ? -66.077 -15.420 22.758  1.00 20.39 ?  160 PRO   B N   1 
ATOM   1214 C  CA  . PRO   A 1 165 ? -66.330 -14.246 21.919  1.00 20.92 ?  160 PRO   B CA  1 
ATOM   1215 C  C   . PRO   A 1 165 ? -65.829 -12.874 22.431  1.00 22.72 ?  160 PRO   B C   1 
ATOM   1216 O  O   . PRO   A 1 165 ? -65.513 -12.017 21.606  1.00 24.00 ?  160 PRO   B O   1 
ATOM   1217 C  CB  . PRO   A 1 165 ? -67.890 -14.203 21.827  1.00 22.28 ?  160 PRO   B CB  1 
ATOM   1218 C  CG  . PRO   A 1 165 ? -68.307 -15.633 22.052  1.00 22.49 ?  160 PRO   B CG  1 
ATOM   1219 C  CD  . PRO   A 1 165 ? -67.293 -16.195 23.035  1.00 22.51 ?  160 PRO   B CD  1 
ATOM   1220 N  N   . GLY   A 1 166 ? -65.749 -12.687 23.749  1.00 22.56 ?  161 GLY   B N   1 
ATOM   1221 C  CA  . GLY   A 1 166 ? -65.390 -11.433 24.394  1.00 21.36 ?  161 GLY   B CA  1 
ATOM   1222 C  C   . GLY   A 1 166 ? -63.892 -11.206 24.296  1.00 20.49 ?  161 GLY   B C   1 
ATOM   1223 O  O   . GLY   A 1 166 ? -63.459 -10.074 24.440  1.00 17.52 ?  161 GLY   B O   1 
ATOM   1224 N  N   . VAL   A 1 167 ? -63.135 -12.250 23.950  1.00 19.66 ?  162 VAL   B N   1 
ATOM   1225 C  CA  . VAL   A 1 167 ? -61.654 -12.085 23.792  1.00 19.89 ?  162 VAL   B CA  1 
ATOM   1226 C  C   . VAL   A 1 167 ? -61.295 -11.287 22.534  1.00 19.21 ?  162 VAL   B C   1 
ATOM   1227 O  O   . VAL   A 1 167 ? -61.640 -11.721 21.414  1.00 20.93 ?  162 VAL   B O   1 
ATOM   1228 C  CB  . VAL   A 1 167 ? -60.969 -13.451 23.761  1.00 18.69 ?  162 VAL   B CB  1 
ATOM   1229 C  CG1 . VAL   A 1 167 ? -59.452 -13.272 23.633  1.00 18.76 ?  162 VAL   B CG1 1 
ATOM   1230 C  CG2 . VAL   A 1 167 ? -61.354 -14.238 24.983  1.00 19.95 ?  162 VAL   B CG2 1 
ATOM   1231 N  N   . GLY   A 1 168 ? -60.468 -10.249 22.700  1.00 19.27 ?  163 GLY   B N   1 
ATOM   1232 C  CA  . GLY   A 1 168 ? -59.799 -9.509  21.624  1.00 17.10 ?  163 GLY   B CA  1 
ATOM   1233 C  C   . GLY   A 1 168 ? -58.332 -9.836  21.609  1.00 18.58 ?  163 GLY   B C   1 
ATOM   1234 O  O   . GLY   A 1 168 ? -57.550 -9.241  22.378  1.00 20.87 ?  163 GLY   B O   1 
ATOM   1235 N  N   . ALA   A 1 169 ? -57.956 -10.804 20.794  1.00 18.61 ?  164 ALA   B N   1 
ATOM   1236 C  CA  . ALA   A 1 169 ? -56.549 -11.250 20.731  1.00 17.39 ?  164 ALA   B CA  1 
ATOM   1237 C  C   . ALA   A 1 169 ? -55.789 -10.389 19.755  1.00 20.27 ?  164 ALA   B C   1 
ATOM   1238 O  O   . ALA   A 1 169 ? -56.379 -9.891  18.794  1.00 22.56 ?  164 ALA   B O   1 
ATOM   1239 C  CB  . ALA   A 1 169 ? -56.479 -12.728 20.410  1.00 18.94 ?  164 ALA   B CB  1 
ATOM   1240 N  N   . PHE   A 1 170 ? -54.470 -10.272 19.959  1.00 18.86 ?  165 PHE   B N   1 
ATOM   1241 C  CA  . PHE   A 1 170 ? -53.607 -9.417  19.132  1.00 19.53 ?  165 PHE   B CA  1 
ATOM   1242 C  C   . PHE   A 1 170 ? -52.181 -9.959  19.132  1.00 19.07 ?  165 PHE   B C   1 
ATOM   1243 O  O   . PHE   A 1 170 ? -51.793 -10.834 19.925  1.00 18.97 ?  165 PHE   B O   1 
ATOM   1244 C  CB  . PHE   A 1 170 ? -53.669 -7.943  19.578  1.00 18.98 ?  165 PHE   B CB  1 
ATOM   1245 C  CG  . PHE   A 1 170 ? -53.252 -7.647  21.001  1.00 17.04 ?  165 PHE   B CG  1 
ATOM   1246 C  CD1 . PHE   A 1 170 ? -51.936 -7.493  21.316  1.00 19.55 ?  165 PHE   B CD1 1 
ATOM   1247 C  CD2 . PHE   A 1 170 ? -54.175 -7.521  22.016  1.00 18.53 ?  165 PHE   B CD2 1 
ATOM   1248 C  CE1 . PHE   A 1 170 ? -51.564 -7.200  22.620  1.00 20.10 ?  165 PHE   B CE1 1 
ATOM   1249 C  CE2 . PHE   A 1 170 ? -53.802 -7.301  23.334  1.00 17.96 ?  165 PHE   B CE2 1 
ATOM   1250 C  CZ  . PHE   A 1 170 ? -52.484 -7.123  23.619  1.00 19.72 ?  165 PHE   B CZ  1 
ATOM   1251 N  N   . ARG   A 1 171 ? -51.453 -9.443  18.174  1.00 18.18 ?  166 ARG   B N   1 
ATOM   1252 C  CA  . ARG   A 1 171 ? -50.019 -9.705  17.923  1.00 18.39 ?  166 ARG   B CA  1 
ATOM   1253 C  C   . ARG   A 1 171 ? -49.328 -8.350  17.913  1.00 21.27 ?  166 ARG   B C   1 
ATOM   1254 O  O   . ARG   A 1 171 ? -49.826 -7.363  17.298  1.00 22.02 ?  166 ARG   B O   1 
ATOM   1255 C  CB  . ARG   A 1 171 ? -49.823 -10.471 16.618  1.00 19.38 ?  166 ARG   B CB  1 
ATOM   1256 C  CG  . ARG   A 1 171 ? -50.585 -11.778 16.536  1.00 20.91 ?  166 ARG   B CG  1 
ATOM   1257 C  CD  . ARG   A 1 171 ? -49.996 -12.768 17.513  1.00 23.74 ?  166 ARG   B CD  1 
ATOM   1258 N  NE  . ARG   A 1 171 ? -50.587 -14.111 17.472  1.00 24.10 ?  166 ARG   B NE  1 
ATOM   1259 C  CZ  . ARG   A 1 171 ? -51.593 -14.524 18.236  1.00 23.14 ?  166 ARG   B CZ  1 
ATOM   1260 N  NH1 . ARG   A 1 171 ? -52.122 -13.732 19.159  1.00 20.13 1  166 ARG   B NH1 1 
ATOM   1261 N  NH2 . ARG   A 1 171 ? -52.013 -15.773 18.130  1.00 24.40 ?  166 ARG   B NH2 1 
ATOM   1262 N  N   . LEU   A 1 172 ? -48.119 -8.321  18.446  1.00 20.53 ?  167 LEU   B N   1 
ATOM   1263 C  CA  . LEU   A 1 172 ? -47.360 -7.075  18.445  1.00 21.43 ?  167 LEU   B CA  1 
ATOM   1264 C  C   . LEU   A 1 172 ? -45.949 -7.429  18.016  1.00 21.74 ?  167 LEU   B C   1 
ATOM   1265 O  O   . LEU   A 1 172 ? -45.260 -8.038  18.799  1.00 22.23 ?  167 LEU   B O   1 
ATOM   1266 C  CB  . LEU   A 1 172 ? -47.407 -6.459  19.845  1.00 23.10 ?  167 LEU   B CB  1 
ATOM   1267 C  CG  . LEU   A 1 172 ? -46.611 -5.176  20.051  1.00 23.27 ?  167 LEU   B CG  1 
ATOM   1268 C  CD1 . LEU   A 1 172 ? -46.987 -4.069  19.033  1.00 26.37 ?  167 LEU   B CD1 1 
ATOM   1269 C  CD2 . LEU   A 1 172 ? -46.849 -4.685  21.470  1.00 25.24 ?  167 LEU   B CD2 1 
ATOM   1270 N  N   . ARG   A 1 173 ? -45.560 -7.092  16.783  1.00 24.14 ?  168 ARG   B N   1 
ATOM   1271 C  CA  . ARG   A 1 173 ? -44.152 -7.321  16.359  1.00 25.93 ?  168 ARG   B CA  1 
ATOM   1272 C  C   . ARG   A 1 173 ? -43.331 -6.165  16.910  1.00 26.20 ?  168 ARG   B C   1 
ATOM   1273 O  O   . ARG   A 1 173 ? -43.593 -4.985  16.587  1.00 26.80 ?  168 ARG   B O   1 
ATOM   1274 C  CB  . ARG   A 1 173 ? -43.952 -7.457  14.842  1.00 31.57 ?  168 ARG   B CB  1 
ATOM   1275 C  CG  . ARG   A 1 173 ? -42.518 -7.817  14.454  1.00 36.11 ?  168 ARG   B CG  1 
ATOM   1276 C  CD  . ARG   A 1 173 ? -42.383 -8.455  13.080  1.00 49.04 ?  168 ARG   B CD  1 
ATOM   1277 N  NE  . ARG   A 1 173 ? -41.362 -9.509  13.031  1.00 60.62 ?  168 ARG   B NE  1 
ATOM   1278 C  CZ  . ARG   A 1 173 ? -40.094 -9.355  12.626  1.00 63.60 ?  168 ARG   B CZ  1 
ATOM   1279 N  NH1 . ARG   A 1 173 ? -39.269 -10.393 12.619  1.00 64.88 1  168 ARG   B NH1 1 
ATOM   1280 N  NH2 . ARG   A 1 173 ? -39.641 -8.172  12.242  1.00 67.60 ?  168 ARG   B NH2 1 
ATOM   1281 N  N   . VAL   A 1 174 ? -42.298 -6.517  17.649  1.00 24.94 ?  169 VAL   B N   1 
ATOM   1282 C  CA  . VAL   A 1 174 ? -41.462 -5.531  18.356  1.00 25.35 ?  169 VAL   B CA  1 
ATOM   1283 C  C   . VAL   A 1 174 ? -40.518 -4.858  17.352  1.00 24.59 ?  169 VAL   B C   1 
ATOM   1284 O  O   . VAL   A 1 174 ? -39.619 -5.533  16.891  1.00 25.35 ?  169 VAL   B O   1 
ATOM   1285 C  CB  . VAL   A 1 174 ? -40.692 -6.194  19.494  1.00 23.67 ?  169 VAL   B CB  1 
ATOM   1286 C  CG1 . VAL   A 1 174 ? -39.778 -5.185  20.179  1.00 22.31 ?  169 VAL   B CG1 1 
ATOM   1287 C  CG2 . VAL   A 1 174 ? -41.642 -6.868  20.479  1.00 21.83 ?  169 VAL   B CG2 1 
ATOM   1288 N  N   . ALA   A 1 175 ? -40.748 -3.568  17.055  1.00 23.37 ?  170 ALA   B N   1 
ATOM   1289 C  CA  . ALA   A 1 175 ? -39.864 -2.726  16.212  1.00 27.83 ?  170 ALA   B CA  1 
ATOM   1290 C  C   . ALA   A 1 175 ? -38.741 -2.124  17.051  1.00 27.42 ?  170 ALA   B C   1 
ATOM   1291 O  O   . ALA   A 1 175 ? -37.629 -1.938  16.542  1.00 27.73 ?  170 ALA   B O   1 
ATOM   1292 C  CB  . ALA   A 1 175 ? -40.660 -1.623  15.569  1.00 30.37 ?  170 ALA   B CB  1 
ATOM   1293 N  N   . GLU   A 1 176 ? -39.044 -1.809  18.313  1.00 25.71 ?  171 GLU   B N   1 
ATOM   1294 C  CA  . GLU   A 1 176 ? -38.188 -1.045  19.231  1.00 24.77 ?  171 GLU   B CA  1 
ATOM   1295 C  C   . GLU   A 1 176 ? -38.388 -1.631  20.626  1.00 21.88 ?  171 GLU   B C   1 
ATOM   1296 O  O   . GLU   A 1 176 ? -39.566 -1.875  21.005  1.00 19.63 ?  171 GLU   B O   1 
ATOM   1297 C  CB  . GLU   A 1 176 ? -38.577 0.432   19.286  1.00 31.76 ?  171 GLU   B CB  1 
ATOM   1298 C  CG  . GLU   A 1 176 ? -38.442 1.203   17.985  1.00 39.95 ?  171 GLU   B CG  1 
ATOM   1299 C  CD  . GLU   A 1 176 ? -38.792 2.667   18.197  1.00 51.28 ?  171 GLU   B CD  1 
ATOM   1300 O  OE1 . GLU   A 1 176 ? -38.029 3.337   18.944  1.00 55.26 ?  171 GLU   B OE1 1 
ATOM   1301 O  OE2 . GLU   A 1 176 ? -39.883 3.115   17.707  1.00 62.68 -1 171 GLU   B OE2 1 
ATOM   1302 N  N   . ALA   A 1 177 ? -37.292 -1.831  21.354  1.00 23.32 ?  172 ALA   B N   1 
ATOM   1303 C  CA  . ALA   A 1 177 ? -37.358 -2.247  22.768  1.00 21.87 ?  172 ALA   B CA  1 
ATOM   1304 C  C   . ALA   A 1 177 ? -36.355 -1.437  23.578  1.00 25.20 ?  172 ALA   B C   1 
ATOM   1305 O  O   . ALA   A 1 177 ? -35.138 -1.415  23.241  1.00 25.95 ?  172 ALA   B O   1 
ATOM   1306 C  CB  . ALA   A 1 177 ? -37.110 -3.724  22.878  1.00 23.91 ?  172 ALA   B CB  1 
ATOM   1307 N  N   . ASP   A 1 178 ? -36.819 -0.819  24.655  1.00 21.91 ?  173 ASP   B N   1 
ATOM   1308 C  CA  . ASP   A 1 178 ? -35.945 -0.007  25.534  1.00 24.24 ?  173 ASP   B CA  1 
ATOM   1309 C  C   . ASP   A 1 178 ? -36.169 -0.512  26.949  1.00 21.44 ?  173 ASP   B C   1 
ATOM   1310 O  O   . ASP   A 1 178 ? -37.264 -0.952  27.242  1.00 19.71 ?  173 ASP   B O   1 
ATOM   1311 C  CB  . ASP   A 1 178 ? -36.246 1.484   25.388  1.00 26.36 ?  173 ASP   B CB  1 
ATOM   1312 C  CG  . ASP   A 1 178 ? -35.929 2.016   23.986  1.00 32.93 ?  173 ASP   B CG  1 
ATOM   1313 O  OD1 . ASP   A 1 178 ? -36.915 2.278   23.177  1.00 33.41 ?  173 ASP   B OD1 1 
ATOM   1314 O  OD2 . ASP   A 1 178 ? -34.700 2.139   23.695  1.00 33.86 -1 173 ASP   B OD2 1 
ATOM   1315 N  N   . GLY   A 1 179 ? -35.109 -0.526  27.721  1.00 20.05 ?  174 GLY   B N   1 
ATOM   1316 C  CA  . GLY   A 1 179 ? -35.074 -1.084  29.075  1.00 22.11 ?  174 GLY   B CA  1 
ATOM   1317 C  C   . GLY   A 1 179 ? -34.450 -0.095  30.023  1.00 21.05 ?  174 GLY   B C   1 
ATOM   1318 O  O   . GLY   A 1 179 ? -33.230 0.289   29.799  1.00 22.26 ?  174 GLY   B O   1 
ATOM   1319 N  N   . MET   A 1 180 ? -35.193 0.272   31.065  1.00 21.05 ?  175 MET   B N   1 
ATOM   1320 C  CA  . MET   A 1 180 ? -34.689 1.080   32.198  1.00 19.47 ?  175 MET   B CA  1 
ATOM   1321 C  C   . MET   A 1 180 ? -34.395 0.159   33.381  1.00 19.63 ?  175 MET   B C   1 
ATOM   1322 O  O   . MET   A 1 180 ? -35.296 -0.506  33.862  1.00 18.51 ?  175 MET   B O   1 
ATOM   1323 C  CB  . MET   A 1 180 ? -35.692 2.149   32.640  1.00 23.04 ?  175 MET   B CB  1 
ATOM   1324 C  CG  . MET   A 1 180 ? -35.202 2.896   33.873  1.00 24.78 ?  175 MET   B CG  1 
ATOM   1325 S  SD  . MET   A 1 180 ? -34.238 4.372   33.487  1.00 26.79 ?  175 MET   B SD  1 
ATOM   1326 C  CE  . MET   A 1 180 ? -35.463 5.500   32.840  1.00 25.94 ?  175 MET   B CE  1 
ATOM   1327 N  N   . PHE   A 1 181 ? -33.115 0.016   33.747  1.00 18.73 ?  176 PHE   B N   1 
ATOM   1328 C  CA  . PHE   A 1 181 ? -32.692 -0.764  34.919  1.00 18.47 ?  176 PHE   B CA  1 
ATOM   1329 C  C   . PHE   A 1 181 ? -32.036 0.203   35.903  1.00 19.55 ?  176 PHE   B C   1 
ATOM   1330 O  O   . PHE   A 1 181 ? -30.780 0.324   35.972  1.00 19.98 ?  176 PHE   B O   1 
ATOM   1331 C  CB  . PHE   A 1 181 ? -31.841 -1.950  34.483  1.00 20.68 ?  176 PHE   B CB  1 
ATOM   1332 C  CG  . PHE   A 1 181 ? -32.620 -2.969  33.698  1.00 20.00 ?  176 PHE   B CG  1 
ATOM   1333 C  CD1 . PHE   A 1 181 ? -32.857 -2.784  32.349  1.00 21.16 ?  176 PHE   B CD1 1 
ATOM   1334 C  CD2 . PHE   A 1 181 ? -33.229 -4.047  34.340  1.00 21.42 ?  176 PHE   B CD2 1 
ATOM   1335 C  CE1 . PHE   A 1 181 ? -33.584 -3.724  31.629  1.00 22.55 ?  176 PHE   B CE1 1 
ATOM   1336 C  CE2 . PHE   A 1 181 ? -33.983 -4.970  33.620  1.00 19.50 ?  176 PHE   B CE2 1 
ATOM   1337 C  CZ  . PHE   A 1 181 ? -34.190 -4.789  32.278  1.00 22.61 ?  176 PHE   B CZ  1 
ATOM   1338 N  N   . LYS   A 1 182 ? -32.887 0.917   36.636  1.00 18.76 ?  177 LYS   B N   1 
ATOM   1339 C  CA  . LYS   A 1 182 ? -32.423 1.966   37.563  1.00 18.66 ?  177 LYS   B CA  1 
ATOM   1340 C  C   . LYS   A 1 182 ? -32.128 1.298   38.916  1.00 19.07 ?  177 LYS   B C   1 
ATOM   1341 O  O   . LYS   A 1 182 ? -33.065 1.046   39.675  1.00 17.74 ?  177 LYS   B O   1 
ATOM   1342 C  CB  . LYS   A 1 182 ? -33.409 3.123   37.590  1.00 19.41 ?  177 LYS   B CB  1 
ATOM   1343 C  CG  . LYS   A 1 182 ? -32.996 4.245   38.514  1.00 19.75 ?  177 LYS   B CG  1 
ATOM   1344 C  CD  . LYS   A 1 182 ? -33.914 5.406   38.372  1.00 20.96 ?  177 LYS   B CD  1 
ATOM   1345 C  CE  . LYS   A 1 182 ? -33.770 6.406   39.485  1.00 27.04 ?  177 LYS   B CE  1 
ATOM   1346 N  NZ  . LYS   A 1 182 ? -32.351 6.759   39.671  1.00 28.57 1  177 LYS   B NZ  1 
ATOM   1347 N  N   . LEU   A 1 183 ? -30.834 1.042   39.190  1.00 16.95 ?  178 LEU   B N   1 
ATOM   1348 C  CA  . LEU   A 1 183 ? -30.383 0.106   40.235  1.00 19.15 ?  178 LEU   B CA  1 
ATOM   1349 C  C   . LEU   A 1 183 ? -29.130 0.686   40.893  1.00 19.71 ?  178 LEU   B C   1 
ATOM   1350 O  O   . LEU   A 1 183 ? -28.293 -0.097  41.265  1.00 20.64 ?  178 LEU   B O   1 
ATOM   1351 C  CB  . LEU   A 1 183 ? -30.086 -1.238  39.572  1.00 18.40 ?  178 LEU   B CB  1 
ATOM   1352 C  CG  . LEU   A 1 183 ? -31.275 -1.972  38.957  1.00 19.29 ?  178 LEU   B CG  1 
ATOM   1353 C  CD1 . LEU   A 1 183 ? -30.768 -3.232  38.275  1.00 21.29 ?  178 LEU   B CD1 1 
ATOM   1354 C  CD2 . LEU   A 1 183 ? -32.340 -2.352  39.995  1.00 19.99 ?  178 LEU   B CD2 1 
ATOM   1355 N  N   . SER   A 1 184 ? -29.125 1.997   41.126  1.00 17.63 ?  179 SER   B N   1 
ATOM   1356 C  CA  . SER   A 1 184 ? -28.089 2.733   41.891  1.00 20.61 ?  179 SER   B CA  1 
ATOM   1357 C  C   . SER   A 1 184 ? -26.725 2.704   41.165  1.00 18.06 ?  179 SER   B C   1 
ATOM   1358 O  O   . SER   A 1 184 ? -25.741 3.030   41.844  1.00 21.72 ?  179 SER   B O   1 
ATOM   1359 C  CB  . SER   A 1 184 ? -27.976 2.191   43.290  1.00 20.87 ?  179 SER   B CB  1 
ATOM   1360 O  OG  . SER   A 1 184 ? -29.173 2.415   44.000  1.00 20.55 ?  179 SER   B OG  1 
ATOM   1361 N  N   . GLN   A 1 185 ? -26.676 2.442   39.868  1.00 18.38 ?  180 GLN   B N   1 
ATOM   1362 C  CA  . GLN   A 1 185 ? -25.399 2.409   39.097  1.00 20.28 ?  180 GLN   B CA  1 
ATOM   1363 C  C   . GLN   A 1 185 ? -24.700 3.773   39.138  1.00 24.16 ?  180 GLN   B C   1 
ATOM   1364 O  O   . GLN   A 1 185 ? -23.424 3.795   39.044  1.00 27.64 ?  180 GLN   B O   1 
ATOM   1365 C  CB  . GLN   A 1 185 ? -25.584 1.962   37.645  1.00 21.54 ?  180 GLN   B CB  1 
ATOM   1366 C  CG  . GLN   A 1 185 ? -26.085 0.541   37.488  1.00 20.70 ?  180 GLN   B CG  1 
ATOM   1367 C  CD  . GLN   A 1 185 ? -27.590 0.506   37.302  1.00 20.34 ?  180 GLN   B CD  1 
ATOM   1368 O  OE1 . GLN   A 1 185 ? -28.309 1.223   37.993  1.00 20.54 ?  180 GLN   B OE1 1 
ATOM   1369 N  NE2 . GLN   A 1 185 ? -28.042 -0.295  36.346  1.00 20.02 ?  180 GLN   B NE2 1 
ATOM   1370 N  N   . GLU   A 1 186 ? -25.430 4.859   39.361  1.00 23.08 ?  181 GLU   B N   1 
ATOM   1371 C  CA  . GLU   A 1 186 ? -24.882 6.245   39.470  1.00 26.01 ?  181 GLU   B CA  1 
ATOM   1372 C  C   . GLU   A 1 186 ? -24.086 6.436   40.774  1.00 28.65 ?  181 GLU   B C   1 
ATOM   1373 O  O   . GLU   A 1 186 ? -23.292 7.370   40.830  1.00 30.12 ?  181 GLU   B O   1 
ATOM   1374 C  CB  . GLU   A 1 186 ? -26.006 7.274   39.344  1.00 26.67 ?  181 GLU   B CB  1 
ATOM   1375 C  CG  . GLU   A 1 186 ? -26.793 7.575   40.631  1.00 25.77 ?  181 GLU   B CG  1 
ATOM   1376 C  CD  . GLU   A 1 186 ? -27.805 6.534   41.114  1.00 24.17 ?  181 GLU   B CD  1 
ATOM   1377 O  OE1 . GLU   A 1 186 ? -28.075 5.517   40.369  1.00 23.40 ?  181 GLU   B OE1 1 
ATOM   1378 O  OE2 . GLU   A 1 186 ? -28.337 6.750   42.248  1.00 23.23 -1 181 GLU   B OE2 1 
ATOM   1379 N  N   . GLN   A 1 187 ? -24.306 5.622   41.814  1.00 27.04 ?  182 GLN   B N   1 
ATOM   1380 C  CA  . GLN   A 1 187 ? -23.634 5.822   43.122  1.00 23.55 ?  182 GLN   B CA  1 
ATOM   1381 C  C   . GLN   A 1 187 ? -22.221 5.213   43.052  1.00 22.08 ?  182 GLN   B C   1 
ATOM   1382 O  O   . GLN   A 1 187 ? -21.978 4.329   42.199  1.00 23.30 ?  182 GLN   B O   1 
ATOM   1383 C  CB  . GLN   A 1 187 ? -24.440 5.184   44.247  1.00 22.32 ?  182 GLN   B CB  1 
ATOM   1384 C  CG  . GLN   A 1 187 ? -25.840 5.771   44.396  1.00 25.35 ?  182 GLN   B CG  1 
ATOM   1385 C  CD  . GLN   A 1 187 ? -25.803 7.216   44.821  1.00 25.66 ?  182 GLN   B CD  1 
ATOM   1386 O  OE1 . GLN   A 1 187 ? -24.988 7.622   45.658  1.00 29.84 ?  182 GLN   B OE1 1 
ATOM   1387 N  NE2 . GLN   A 1 187 ? -26.638 8.034   44.209  1.00 23.47 ?  182 GLN   B NE2 1 
ATOM   1388 N  N   . GLN   A 1 188 ? -21.372 5.626   43.976  1.00 26.09 ?  183 GLN   B N   1 
ATOM   1389 C  CA  . GLN   A 1 188 ? -20.026 5.026   44.172  1.00 28.61 ?  183 GLN   B CA  1 
ATOM   1390 C  C   . GLN   A 1 188 ? -20.222 3.580   44.626  1.00 30.39 ?  183 GLN   B C   1 
ATOM   1391 O  O   . GLN   A 1 188 ? -21.219 3.244   45.273  1.00 26.19 ?  183 GLN   B O   1 
ATOM   1392 C  CB  . GLN   A 1 188 ? -19.245 5.852   45.193  1.00 31.98 ?  183 GLN   B CB  1 
ATOM   1393 C  CG  . GLN   A 1 188 ? -18.938 7.267   44.722  1.00 36.24 ?  183 GLN   B CG  1 
ATOM   1394 C  CD  . GLN   A 1 188 ? -18.077 7.208   43.482  1.00 44.51 ?  183 GLN   B CD  1 
ATOM   1395 O  OE1 . GLN   A 1 188 ? -18.451 7.693   42.418  1.00 53.93 ?  183 GLN   B OE1 1 
ATOM   1396 N  NE2 . GLN   A 1 188 ? -16.933 6.549   43.586  1.00 45.52 ?  183 GLN   B NE2 1 
ATOM   1397 N  N   . PRO   A 1 189 ? -19.260 2.673   44.365  1.00 30.73 ?  184 PRO   B N   1 
ATOM   1398 C  CA  . PRO   A 1 189 ? -19.439 1.257   44.701  1.00 31.21 ?  184 PRO   B CA  1 
ATOM   1399 C  C   . PRO   A 1 189 ? -19.820 0.928   46.147  1.00 29.05 ?  184 PRO   B C   1 
ATOM   1400 O  O   . PRO   A 1 189 ? -20.666 0.034   46.330  1.00 27.68 ?  184 PRO   B O   1 
ATOM   1401 C  CB  . PRO   A 1 189 ? -18.045 0.675   44.410  1.00 31.44 ?  184 PRO   B CB  1 
ATOM   1402 C  CG  . PRO   A 1 189 ? -17.565 1.522   43.277  1.00 33.57 ?  184 PRO   B CG  1 
ATOM   1403 C  CD  . PRO   A 1 189 ? -17.973 2.923   43.686  1.00 32.22 ?  184 PRO   B CD  1 
ATOM   1404 N  N   . ALA   A 1 190 ? -19.189 1.588   47.126  1.00 29.63 ?  185 ALA   B N   1 
ATOM   1405 C  CA  . ALA   A 1 190 ? -19.472 1.379   48.567  1.00 29.28 ?  185 ALA   B CA  1 
ATOM   1406 C  C   . ALA   A 1 190 ? -20.943 1.743   48.861  1.00 26.68 ?  185 ALA   B C   1 
ATOM   1407 O  O   . ALA   A 1 190 ? -21.546 1.106   49.717  1.00 26.59 ?  185 ALA   B O   1 
ATOM   1408 C  CB  . ALA   A 1 190 ? -18.522 2.174   49.424  1.00 34.00 ?  185 ALA   B CB  1 
ATOM   1409 N  N   . ILE   A 1 191 ? -21.475 2.774   48.215  1.00 26.25 ?  186 ILE   B N   1 
ATOM   1410 C  CA  . ILE   A 1 191 ? -22.879 3.232   48.436  1.00 24.93 ?  186 ILE   B CA  1 
ATOM   1411 C  C   . ILE   A 1 191 ? -23.818 2.229   47.746  1.00 24.63 ?  186 ILE   B C   1 
ATOM   1412 O  O   . ILE   A 1 191 ? -24.869 1.884   48.335  1.00 24.14 ?  186 ILE   B O   1 
ATOM   1413 C  CB  . ILE   A 1 191 ? -23.086 4.673   47.940  1.00 27.09 ?  186 ILE   B CB  1 
ATOM   1414 C  CG1 . ILE   A 1 191 ? -22.130 5.665   48.593  1.00 31.60 ?  186 ILE   B CG1 1 
ATOM   1415 C  CG2 . ILE   A 1 191 ? -24.529 5.103   48.127  1.00 29.21 ?  186 ILE   B CG2 1 
ATOM   1416 C  CD1 . ILE   A 1 191 ? -22.021 5.535   50.082  1.00 32.46 ?  186 ILE   B CD1 1 
ATOM   1417 N  N   . ARG   A 1 192 ? -23.488 1.776   46.547  1.00 22.89 ?  187 ARG   B N   1 
ATOM   1418 C  CA  . ARG   A 1 192 ? -24.275 0.745   45.824  1.00 26.02 ?  187 ARG   B CA  1 
ATOM   1419 C  C   . ARG   A 1 192 ? -24.394 -0.508  46.704  1.00 24.57 ?  187 ARG   B C   1 
ATOM   1420 O  O   . ARG   A 1 192 ? -25.498 -1.076  46.808  1.00 21.16 ?  187 ARG   B O   1 
ATOM   1421 C  CB  . ARG   A 1 192 ? -23.627 0.267   44.523  1.00 29.34 ?  187 ARG   B CB  1 
ATOM   1422 C  CG  . ARG   A 1 192 ? -23.583 1.283   43.405  1.00 36.07 ?  187 ARG   B CG  1 
ATOM   1423 C  CD  . ARG   A 1 192 ? -23.226 0.566   42.097  1.00 40.36 ?  187 ARG   B CD  1 
ATOM   1424 N  NE  . ARG   A 1 192 ? -22.262 1.413   41.456  1.00 48.86 ?  187 ARG   B NE  1 
ATOM   1425 C  CZ  . ARG   A 1 192 ? -20.998 1.092   41.198  1.00 55.32 ?  187 ARG   B CZ  1 
ATOM   1426 N  NH1 . ARG   A 1 192 ? -20.537 -0.126  41.433  1.00 54.75 1  187 ARG   B NH1 1 
ATOM   1427 N  NH2 . ARG   A 1 192 ? -20.215 2.003   40.650  1.00 55.42 ?  187 ARG   B NH2 1 
ATOM   1428 N  N   . ARG   A 1 193 ? -23.287 -0.936  47.313  1.00 22.55 ?  188 ARG   B N   1 
ATOM   1429 C  CA  . ARG   A 1 193 ? -23.283 -2.126  48.200  1.00 24.29 ?  188 ARG   B CA  1 
ATOM   1430 C  C   . ARG   A 1 193 ? -24.219 -1.888  49.393  1.00 21.62 ?  188 ARG   B C   1 
ATOM   1431 O  O   . ARG   A 1 193 ? -24.917 -2.827  49.775  1.00 22.18 ?  188 ARG   B O   1 
ATOM   1432 C  CB  . ARG   A 1 193 ? -21.844 -2.407  48.635  1.00 26.01 ?  188 ARG   B CB  1 
ATOM   1433 C  CG  . ARG   A 1 193 ? -21.663 -3.589  49.574  1.00 34.73 ?  188 ARG   B CG  1 
ATOM   1434 C  CD  . ARG   A 1 193 ? -20.165 -3.838  49.805  1.00 39.32 ?  188 ARG   B CD  1 
ATOM   1435 N  NE  . ARG   A 1 193 ? -19.939 -5.078  50.543  1.00 47.26 ?  188 ARG   B NE  1 
ATOM   1436 C  CZ  . ARG   A 1 193 ? -19.847 -5.181  51.870  1.00 52.35 ?  188 ARG   B CZ  1 
ATOM   1437 N  NH1 . ARG   A 1 193 ? -19.945 -4.113  52.652  1.00 54.11 1  188 ARG   B NH1 1 
ATOM   1438 N  NH2 . ARG   A 1 193 ? -19.658 -6.369  52.415  1.00 53.27 ?  188 ARG   B NH2 1 
ATOM   1439 N  N   . ARG   A 1 194 ? -24.237 -0.676  49.958  1.00 19.87 ?  189 ARG   B N   1 
ATOM   1440 C  CA  . ARG   A 1 194 ? -25.093 -0.372  51.133  1.00 20.02 ?  189 ARG   B CA  1 
ATOM   1441 C  C   . ARG   A 1 194 ? -26.564 -0.491  50.710  1.00 18.70 ?  189 ARG   B C   1 
ATOM   1442 O  O   . ARG   A 1 194 ? -27.379 -0.966  51.488  1.00 18.81 ?  189 ARG   B O   1 
ATOM   1443 C  CB  . ARG   A 1 194 ? -24.866 1.031   51.680  1.00 20.25 ?  189 ARG   B CB  1 
ATOM   1444 C  CG  . ARG   A 1 194 ? -23.512 1.178   52.350  1.00 23.52 ?  189 ARG   B CG  1 
ATOM   1445 C  CD  . ARG   A 1 194 ? -23.204 2.575   52.783  1.00 24.23 ?  189 ARG   B CD  1 
ATOM   1446 N  NE  . ARG   A 1 194 ? -21.814 2.588   53.238  1.00 26.06 ?  189 ARG   B NE  1 
ATOM   1447 C  CZ  . ARG   A 1 194 ? -21.176 3.678   53.606  1.00 29.55 ?  189 ARG   B CZ  1 
ATOM   1448 N  NH1 . ARG   A 1 194 ? -21.770 4.854   53.512  1.00 29.96 1  189 ARG   B NH1 1 
ATOM   1449 N  NH2 . ARG   A 1 194 ? -19.913 3.583   54.001  1.00 32.15 ?  189 ARG   B NH2 1 
ATOM   1450 N  N   . VAL   A 1 195 ? -26.901 -0.004  49.526  1.00 18.26 ?  190 VAL   B N   1 
ATOM   1451 C  CA  . VAL   A 1 195 ? -28.319 -0.085  49.038  1.00 18.44 ?  190 VAL   B CA  1 
ATOM   1452 C  C   . VAL   A 1 195 ? -28.674 -1.562  48.829  1.00 18.02 ?  190 VAL   B C   1 
ATOM   1453 O  O   . VAL   A 1 195 ? -29.765 -2.040  49.239  1.00 17.48 ?  190 VAL   B O   1 
ATOM   1454 C  CB  . VAL   A 1 195 ? -28.507 0.729   47.743  1.00 17.82 ?  190 VAL   B CB  1 
ATOM   1455 C  CG1 . VAL   A 1 195 ? -29.911 0.512   47.199  1.00 18.55 ?  190 VAL   B CG1 1 
ATOM   1456 C  CG2 . VAL   A 1 195 ? -28.207 2.210   47.958  1.00 18.67 ?  190 VAL   B CG2 1 
ATOM   1457 N  N   . ARG   A 1 196 ? -27.796 -2.308  48.184  1.00 19.67 ?  191 ARG   B N   1 
ATOM   1458 C  CA  . ARG   A 1 196 ? -28.035 -3.743  47.896  1.00 19.17 ?  191 ARG   B CA  1 
ATOM   1459 C  C   . ARG   A 1 196 ? -28.255 -4.493  49.218  1.00 20.43 ?  191 ARG   B C   1 
ATOM   1460 O  O   . ARG   A 1 196 ? -29.184 -5.313  49.287  1.00 20.66 ?  191 ARG   B O   1 
ATOM   1461 C  CB  . ARG   A 1 196 ? -26.864 -4.369  47.153  1.00 22.12 ?  191 ARG   B CB  1 
ATOM   1462 C  CG  . ARG   A 1 196 ? -27.046 -5.842  46.850  1.00 25.24 ?  191 ARG   B CG  1 
ATOM   1463 C  CD  . ARG   A 1 196 ? -26.061 -6.296  45.798  1.00 28.13 ?  191 ARG   B CD  1 
ATOM   1464 N  NE  . ARG   A 1 196 ? -24.694 -6.059  46.256  1.00 34.62 ?  191 ARG   B NE  1 
ATOM   1465 C  CZ  . ARG   A 1 196 ? -23.988 -6.889  47.023  1.00 35.61 ?  191 ARG   B CZ  1 
ATOM   1466 N  NH1 . ARG   A 1 196 ? -24.532 -8.004  47.479  1.00 38.78 1  191 ARG   B NH1 1 
ATOM   1467 N  NH2 . ARG   A 1 196 ? -22.744 -6.578  47.346  1.00 37.28 ?  191 ARG   B NH2 1 
ATOM   1468 N  N   . HIS   A 1 197 ? -27.393 -4.288  50.213  1.00 20.32 ?  192 HIS   B N   1 
ATOM   1469 C  CA  . HIS   A 1 197 ? -27.525 -5.004  51.513  1.00 20.39 ?  192 HIS   B CA  1 
ATOM   1470 C  C   . HIS   A 1 197 ? -28.816 -4.568  52.203  1.00 23.25 ?  192 HIS   B C   1 
ATOM   1471 O  O   . HIS   A 1 197 ? -29.483 -5.437  52.760  1.00 21.23 ?  192 HIS   B O   1 
ATOM   1472 C  CB  . HIS   A 1 197 ? -26.300 -4.816  52.385  1.00 25.29 ?  192 HIS   B CB  1 
ATOM   1473 C  CG  . HIS   A 1 197 ? -25.120 -5.558  51.879  1.00 23.65 ?  192 HIS   B CG  1 
ATOM   1474 N  ND1 . HIS   A 1 197 ? -25.224 -6.808  51.328  1.00 27.84 ?  192 HIS   B ND1 1 
ATOM   1475 C  CD2 . HIS   A 1 197 ? -23.802 -5.284  51.943  1.00 27.92 ?  192 HIS   B CD2 1 
ATOM   1476 C  CE1 . HIS   A 1 197 ? -24.030 -7.231  50.970  1.00 26.91 ?  192 HIS   B CE1 1 
ATOM   1477 N  NE2 . HIS   A 1 197 ? -23.157 -6.344  51.353  1.00 26.02 ?  192 HIS   B NE2 1 
ATOM   1478 N  N   . SER   A 1 198 ? -29.167 -3.282  52.156  1.00 20.02 ?  193 SER   B N   1 
ATOM   1479 C  CA  . SER   A 1 198 ? -30.421 -2.802  52.780  1.00 20.83 ?  193 SER   B CA  1 
ATOM   1480 C  C   . SER   A 1 198 ? -31.606 -3.511  52.099  1.00 19.50 ?  193 SER   B C   1 
ATOM   1481 O  O   . SER   A 1 198 ? -32.454 -4.077  52.808  1.00 21.91 ?  193 SER   B O   1 
ATOM   1482 C  CB  . SER   A 1 198 ? -30.519 -1.293  52.750  1.00 20.42 ?  193 SER   B CB  1 
ATOM   1483 O  OG  . SER   A 1 198 ? -31.809 -0.915  53.217  1.00 21.69 ?  193 SER   B OG  1 
ATOM   1484 N  N   . PHE   A 1 199 ? -31.643 -3.605  50.770  1.00 19.27 ?  194 PHE   B N   1 
ATOM   1485 C  CA  . PHE   A 1 199 ? -32.787 -4.224  50.035  1.00 18.35 ?  194 PHE   B CA  1 
ATOM   1486 C  C   . PHE   A 1 199 ? -32.841 -5.740  50.277  1.00 18.82 ?  194 PHE   B C   1 
ATOM   1487 O  O   . PHE   A 1 199 ? -33.937 -6.297  50.267  1.00 17.62 ?  194 PHE   B O   1 
ATOM   1488 C  CB  . PHE   A 1 199 ? -32.758 -3.814  48.567  1.00 19.01 ?  194 PHE   B CB  1 
ATOM   1489 C  CG  . PHE   A 1 199 ? -33.160 -2.382  48.305  1.00 20.46 ?  194 PHE   B CG  1 
ATOM   1490 C  CD1 . PHE   A 1 199 ? -33.816 -1.611  49.248  1.00 21.23 ?  194 PHE   B CD1 1 
ATOM   1491 C  CD2 . PHE   A 1 199 ? -32.912 -1.809  47.064  1.00 20.49 ?  194 PHE   B CD2 1 
ATOM   1492 C  CE1 . PHE   A 1 199 ? -34.223 -0.311  48.957  1.00 20.84 ?  194 PHE   B CE1 1 
ATOM   1493 C  CE2 . PHE   A 1 199 ? -33.363 -0.530  46.765  1.00 19.87 ?  194 PHE   B CE2 1 
ATOM   1494 C  CZ  . PHE   A 1 199 ? -33.981 0.234   47.726  1.00 19.38 ?  194 PHE   B CZ  1 
ATOM   1495 N  N   . GLY   A 1 200 ? -31.721 -6.383  50.584  1.00 18.00 ?  195 GLY   B N   1 
ATOM   1496 C  CA  . GLY   A 1 200 ? -31.676 -7.818  50.888  1.00 17.48 ?  195 GLY   B CA  1 
ATOM   1497 C  C   . GLY   A 1 200 ? -32.263 -8.140  52.243  1.00 19.06 ?  195 GLY   B C   1 
ATOM   1498 O  O   . GLY   A 1 200 ? -32.497 -9.345  52.492  1.00 20.06 ?  195 GLY   B O   1 
ATOM   1499 N  N   . GLY   A 1 201 ? -32.537 -7.140  53.086  1.00 20.07 ?  196 GLY   B N   1 
ATOM   1500 C  CA  . GLY   A 1 201 ? -33.000 -7.331  54.468  1.00 19.97 ?  196 GLY   B CA  1 
ATOM   1501 C  C   . GLY   A 1 201 ? -34.524 -7.338  54.596  1.00 21.13 ?  196 GLY   B C   1 
ATOM   1502 O  O   . GLY   A 1 201 ? -35.000 -7.482  55.724  1.00 22.12 ?  196 GLY   B O   1 
ATOM   1503 N  N   . ALA   A 1 202 ? -35.263 -7.296  53.502  1.00 18.06 ?  197 ALA   B N   1 
ATOM   1504 C  CA  . ALA   A 1 202 ? -36.755 -7.387  53.538  1.00 20.37 ?  197 ALA   B CA  1 
ATOM   1505 C  C   . ALA   A 1 202 ? -37.254 -8.041  52.269  1.00 22.13 ?  197 ALA   B C   1 
ATOM   1506 O  O   . ALA   A 1 202 ? -36.780 -7.699  51.171  1.00 21.73 ?  197 ALA   B O   1 
ATOM   1507 C  CB  . ALA   A 1 202 ? -37.387 -6.034  53.782  1.00 19.93 ?  197 ALA   B CB  1 
ATOM   1508 N  N   . GLU   A 1 203 ? -38.233 -8.925  52.410  1.00 19.82 ?  198 GLU   B N   1 
ATOM   1509 C  CA  . GLU   A 1 203 ? -38.760 -9.653  51.251  1.00 21.83 ?  198 GLU   B CA  1 
ATOM   1510 C  C   . GLU   A 1 203 ? -39.266 -8.656  50.190  1.00 21.43 ?  198 GLU   B C   1 
ATOM   1511 O  O   . GLU   A 1 203 ? -39.096 -8.949  49.000  1.00 22.30 ?  198 GLU   B O   1 
ATOM   1512 C  CB  . GLU   A 1 203 ? -39.870 -10.613 51.658  1.00 24.66 ?  198 GLU   B CB  1 
ATOM   1513 C  CG  . GLU   A 1 203 ? -40.298 -11.499 50.509  1.00 25.17 ?  198 GLU   B CG  1 
ATOM   1514 C  CD  . GLU   A 1 203 ? -39.258 -12.418 49.897  1.00 32.30 ?  198 GLU   B CD  1 
ATOM   1515 O  OE1 . GLU   A 1 203 ? -38.137 -12.507 50.437  1.00 33.02 ?  198 GLU   B OE1 1 
ATOM   1516 O  OE2 . GLU   A 1 203 ? -39.554 -13.007 48.853  1.00 38.08 -1 198 GLU   B OE2 1 
ATOM   1517 N  N   . ALA   A 1 204 ? -39.868 -7.540  50.586  1.00 19.91 ?  199 ALA   B N   1 
ATOM   1518 C  CA  . ALA   A 1 204 ? -40.492 -6.568  49.651  1.00 23.58 ?  199 ALA   B CA  1 
ATOM   1519 C  C   . ALA   A 1 204 ? -39.457 -6.028  48.672  1.00 22.88 ?  199 ALA   B C   1 
ATOM   1520 O  O   . ALA   A 1 204 ? -39.858 -5.589  47.591  1.00 24.87 ?  199 ALA   B O   1 
ATOM   1521 C  CB  . ALA   A 1 204 ? -41.166 -5.423  50.382  1.00 25.98 ?  199 ALA   B CB  1 
ATOM   1522 N  N   . THR   A 1 205 ? -38.184 -5.997  49.051  1.00 20.77 ?  200 THR   B N   1 
ATOM   1523 C  CA  . THR   A 1 205 ? -37.103 -5.340  48.261  1.00 20.77 ?  200 THR   B CA  1 
ATOM   1524 C  C   . THR   A 1 205 ? -36.063 -6.358  47.782  1.00 19.88 ?  200 THR   B C   1 
ATOM   1525 O  O   . THR   A 1 205 ? -35.161 -5.946  47.035  1.00 20.20 ?  200 THR   B O   1 
ATOM   1526 C  CB  . THR   A 1 205 ? -36.489 -4.200  49.077  1.00 20.28 ?  200 THR   B CB  1 
ATOM   1527 O  OG1 . THR   A 1 205 ? -36.075 -4.766  50.325  1.00 20.81 ?  200 THR   B OG1 1 
ATOM   1528 C  CG2 . THR   A 1 205 ? -37.452 -3.054  49.311  1.00 19.18 ?  200 THR   B CG2 1 
ATOM   1529 N  N   . ARG   A 1 206 ? -36.214 -7.631  48.108  1.00 20.01 ?  201 ARG   B N   1 
ATOM   1530 C  CA  . ARG   A 1 206 ? -35.190 -8.658  47.808  1.00 20.34 ?  201 ARG   B CA  1 
ATOM   1531 C  C   . ARG   A 1 206 ? -34.991 -8.825  46.286  1.00 19.47 ?  201 ARG   B C   1 
ATOM   1532 O  O   . ARG   A 1 206 ? -33.809 -9.002  45.853  1.00 19.49 ?  201 ARG   B O   1 
ATOM   1533 C  CB  . ARG   A 1 206 ? -35.549 -10.000 48.437  1.00 23.39 ?  201 ARG   B CB  1 
ATOM   1534 C  CG  . ARG   A 1 206 ? -34.385 -10.969 48.309  1.00 24.95 ?  201 ARG   B CG  1 
ATOM   1535 C  CD  . ARG   A 1 206 ? -34.563 -12.175 49.203  1.00 26.65 ?  201 ARG   B CD  1 
ATOM   1536 N  NE  . ARG   A 1 206 ? -35.782 -12.880 48.877  1.00 30.73 ?  201 ARG   B NE  1 
ATOM   1537 C  CZ  . ARG   A 1 206 ? -35.864 -13.911 48.042  1.00 35.39 ?  201 ARG   B CZ  1 
ATOM   1538 N  NH1 . ARG   A 1 206 ? -34.787 -14.380 47.432  1.00 38.45 1  201 ARG   B NH1 1 
ATOM   1539 N  NH2 . ARG   A 1 206 ? -37.030 -14.478 47.831  1.00 38.52 ?  201 ARG   B NH2 1 
ATOM   1540 N  N   . ALA   A 1 207 ? -36.046 -8.688  45.488  1.00 18.18 ?  202 ALA   B N   1 
ATOM   1541 C  CA  . ALA   A 1 207 ? -35.966 -8.846  44.017  1.00 19.99 ?  202 ALA   B CA  1 
ATOM   1542 C  C   . ALA   A 1 207 ? -35.094 -7.752  43.438  1.00 18.90 ?  202 ALA   B C   1 
ATOM   1543 O  O   . ALA   A 1 207 ? -34.330 -8.056  42.492  1.00 20.93 ?  202 ALA   B O   1 
ATOM   1544 C  CB  . ALA   A 1 207 ? -37.327 -8.823  43.387  1.00 20.14 ?  202 ALA   B CB  1 
ATOM   1545 N  N   . VAL   A 1 208 ? -35.176 -6.530  43.974  1.00 18.62 ?  203 VAL   B N   1 
ATOM   1546 C  CA  . VAL   A 1 208 ? -34.328 -5.409  43.498  1.00 18.71 ?  203 VAL   B CA  1 
ATOM   1547 C  C   . VAL   A 1 208 ? -32.890 -5.740  43.881  1.00 17.96 ?  203 VAL   B C   1 
ATOM   1548 O  O   . VAL   A 1 208 ? -31.996 -5.578  43.076  1.00 19.41 ?  203 VAL   B O   1 
ATOM   1549 C  CB  . VAL   A 1 208 ? -34.752 -4.062  44.099  1.00 19.73 ?  203 VAL   B CB  1 
ATOM   1550 C  CG1 . VAL   A 1 208 ? -33.767 -2.944  43.746  1.00 20.58 ?  203 VAL   B CG1 1 
ATOM   1551 C  CG2 . VAL   A 1 208 ? -36.160 -3.702  43.638  1.00 19.50 ?  203 VAL   B CG2 1 
ATOM   1552 N  N   . ALA   A 1 209 ? -32.663 -6.197  45.118  1.00 17.14 ?  204 ALA   B N   1 
ATOM   1553 C  CA  . ALA   A 1 209 ? -31.306 -6.579  45.570  1.00 17.78 ?  204 ALA   B CA  1 
ATOM   1554 C  C   . ALA   A 1 209 ? -30.748 -7.657  44.646  1.00 19.54 ?  204 ALA   B C   1 
ATOM   1555 O  O   . ALA   A 1 209 ? -29.527 -7.637  44.386  1.00 19.48 ?  204 ALA   B O   1 
ATOM   1556 C  CB  . ALA   A 1 209 ? -31.326 -7.069  46.995  1.00 18.66 ?  204 ALA   B CB  1 
ATOM   1557 N  N   . GLY   A 1 210 ? -31.573 -8.618  44.252  1.00 20.53 ?  205 GLY   B N   1 
ATOM   1558 C  CA  . GLY   A 1 210 ? -31.201 -9.720  43.336  1.00 21.77 ?  205 GLY   B CA  1 
ATOM   1559 C  C   . GLY   A 1 210 ? -30.679 -9.181  42.008  1.00 22.76 ?  205 GLY   B C   1 
ATOM   1560 O  O   . GLY   A 1 210 ? -29.644 -9.653  41.518  1.00 25.01 ?  205 GLY   B O   1 
ATOM   1561 N  N   . LEU   A 1 211 ? -31.379 -8.221  41.411  1.00 22.70 ?  206 LEU   B N   1 
ATOM   1562 C  CA  . LEU   A 1 211 ? -30.905 -7.604  40.148  1.00 23.70 ?  206 LEU   B CA  1 
ATOM   1563 C  C   . LEU   A 1 211 ? -29.613 -6.852  40.410  1.00 21.55 ?  206 LEU   B C   1 
ATOM   1564 O  O   . LEU   A 1 211 ? -28.703 -6.993  39.603  1.00 24.12 ?  206 LEU   B O   1 
ATOM   1565 C  CB  . LEU   A 1 211 ? -31.990 -6.689  39.597  1.00 22.12 ?  206 LEU   B CB  1 
ATOM   1566 C  CG  . LEU   A 1 211 ? -33.212 -7.432  39.084  1.00 24.62 ?  206 LEU   B CG  1 
ATOM   1567 C  CD1 . LEU   A 1 211 ? -34.314 -6.446  38.786  1.00 26.92 ?  206 LEU   B CD1 1 
ATOM   1568 C  CD2 . LEU   A 1 211 ? -32.871 -8.232  37.839  1.00 26.82 ?  206 LEU   B CD2 1 
ATOM   1569 N  N   . MET   A 1 212 ? -29.520 -6.102  41.508  1.00 19.88 ?  207 MET   B N   1 
ATOM   1570 C  CA  . MET   A 1 212 ? -28.277 -5.334  41.811  1.00 20.61 ?  207 MET   B CA  1 
ATOM   1571 C  C   . MET   A 1 212 ? -27.097 -6.281  41.965  1.00 23.72 ?  207 MET   B C   1 
ATOM   1572 O  O   . MET   A 1 212 ? -25.997 -5.935  41.518  1.00 23.85 ?  207 MET   B O   1 
ATOM   1573 C  CB  . MET   A 1 212 ? -28.387 -4.488  43.084  1.00 20.48 ?  207 MET   B CB  1 
ATOM   1574 C  CG  . MET   A 1 212 ? -29.436 -3.398  42.935  1.00 24.10 ?  207 MET   B CG  1 
ATOM   1575 S  SD  . MET   A 1 212 ? -29.786 -2.450  44.428  1.00 22.80 ?  207 MET   B SD  1 
ATOM   1576 C  CE  . MET   A 1 212 ? -28.198 -1.604  44.527  1.00 24.53 ?  207 MET   B CE  1 
ATOM   1577 N  N   . ASP   A 1 213 ? -27.332 -7.456  42.527  1.00 23.13 ?  208 ASP   B N   1 
ATOM   1578 C  CA  . ASP   A 1 213 ? -26.271 -8.463  42.740  1.00 27.04 ?  208 ASP   B CA  1 
ATOM   1579 C  C   . ASP   A 1 213 ? -25.778 -9.024  41.400  1.00 29.34 ?  208 ASP   B C   1 
ATOM   1580 O  O   . ASP   A 1 213 ? -24.655 -9.494  41.367  1.00 29.10 ?  208 ASP   B O   1 
ATOM   1581 C  CB  . ASP   A 1 213 ? -26.800 -9.593  43.620  1.00 30.93 ?  208 ASP   B CB  1 
ATOM   1582 C  CG  . ASP   A 1 213 ? -25.692 -10.390 44.276  1.00 39.64 ?  208 ASP   B CG  1 
ATOM   1583 O  OD1 . ASP   A 1 213 ? -24.716 -9.762  44.749  1.00 46.91 ?  208 ASP   B OD1 1 
ATOM   1584 O  OD2 . ASP   A 1 213 ? -25.810 -11.622 44.295  1.00 44.09 -1 208 ASP   B OD2 1 
ATOM   1585 N  N   . ARG   A 1 214 ? -26.591 -9.002  40.353  1.00 24.60 ?  209 ARG   B N   1 
ATOM   1586 C  CA  . ARG   A 1 214 ? -26.256 -9.563  39.013  1.00 28.36 ?  209 ARG   B CA  1 
ATOM   1587 C  C   . ARG   A 1 214 ? -25.640 -8.511  38.084  1.00 27.90 ?  209 ARG   B C   1 
ATOM   1588 O  O   . ARG   A 1 214 ? -25.233 -8.894  36.974  1.00 28.27 ?  209 ARG   B O   1 
ATOM   1589 C  CB  . ARG   A 1 214 ? -27.519 -10.181 38.422  1.00 30.17 ?  209 ARG   B CB  1 
ATOM   1590 C  CG  . ARG   A 1 214 ? -27.996 -11.405 39.191  1.00 32.14 ?  209 ARG   B CG  1 
ATOM   1591 C  CD  . ARG   A 1 214 ? -29.269 -11.967 38.593  1.00 38.73 ?  209 ARG   B CD  1 
ATOM   1592 N  NE  . ARG   A 1 214 ? -29.072 -12.223 37.168  1.00 46.82 ?  209 ARG   B NE  1 
ATOM   1593 C  CZ  . ARG   A 1 214 ? -29.985 -12.042 36.207  1.00 50.63 ?  209 ARG   B CZ  1 
ATOM   1594 N  NH1 . ARG   A 1 214 ? -29.673 -12.308 34.945  1.00 48.91 1  209 ARG   B NH1 1 
ATOM   1595 N  NH2 . ARG   A 1 214 ? -31.201 -11.606 36.504  1.00 49.21 ?  209 ARG   B NH2 1 
ATOM   1596 N  N   . LEU   A 1 215 ? -25.505 -7.253  38.502  1.00 28.28 ?  210 LEU   B N   1 
ATOM   1597 C  CA  . LEU   A 1 215 ? -24.823 -6.235  37.666  1.00 30.62 ?  210 LEU   B CA  1 
ATOM   1598 C  C   . LEU   A 1 215 ? -23.328 -6.529  37.705  1.00 36.74 ?  210 LEU   B C   1 
ATOM   1599 O  O   . LEU   A 1 215 ? -22.834 -6.991  38.735  1.00 32.83 ?  210 LEU   B O   1 
ATOM   1600 C  CB  . LEU   A 1 215 ? -25.071 -4.829  38.202  1.00 30.31 ?  210 LEU   B CB  1 
ATOM   1601 C  CG  . LEU   A 1 215 ? -26.521 -4.374  38.141  1.00 27.09 ?  210 LEU   B CG  1 
ATOM   1602 C  CD1 . LEU   A 1 215 ? -26.662 -3.068  38.882  1.00 25.63 ?  210 LEU   B CD1 1 
ATOM   1603 C  CD2 . LEU   A 1 215 ? -26.971 -4.235  36.711  1.00 30.48 ?  210 LEU   B CD2 1 
ATOM   1604 N  N   . PRO   A 1 216 ? -22.599 -6.241  36.596  1.00 40.46 ?  211 PRO   B N   1 
ATOM   1605 C  CA  . PRO   A 1 216 ? -21.162 -6.530  36.490  1.00 46.45 ?  211 PRO   B CA  1 
ATOM   1606 C  C   . PRO   A 1 216 ? -20.317 -6.091  37.693  1.00 44.09 ?  211 PRO   B C   1 
ATOM   1607 O  O   . PRO   A 1 216 ? -20.527 -4.957  38.122  1.00 51.18 ?  211 PRO   B O   1 
ATOM   1608 C  CB  . PRO   A 1 216 ? -20.732 -5.710  35.260  1.00 48.19 ?  211 PRO   B CB  1 
ATOM   1609 C  CG  . PRO   A 1 216 ? -21.978 -5.629  34.395  1.00 45.82 ?  211 PRO   B CG  1 
ATOM   1610 C  CD  . PRO   A 1 216 ? -23.140 -5.631  35.369  1.00 43.84 ?  211 PRO   B CD  1 
ATOM   1611 N  N   . ALA   B 1 5   ? -62.979 7.223   30.307  1.00 37.88 ?  0   ALA   C N   1 
ATOM   1612 C  CA  . ALA   B 1 5   ? -61.674 7.195   29.558  1.00 38.72 ?  0   ALA   C CA  1 
ATOM   1613 C  C   . ALA   B 1 5   ? -60.838 5.969   29.959  1.00 34.95 ?  0   ALA   C C   1 
ATOM   1614 O  O   . ALA   B 1 5   ? -59.934 5.602   29.192  1.00 38.61 ?  0   ALA   C O   1 
ATOM   1615 C  CB  . ALA   B 1 5   ? -60.899 8.469   29.782  1.00 38.72 ?  0   ALA   C CB  1 
ATOM   1616 N  N   . MET   B 1 6   ? -61.079 5.392   31.132  1.00 33.81 ?  1   MET   C N   1 
ATOM   1617 C  CA  . MET   B 1 6   ? -60.531 4.061   31.486  1.00 31.53 ?  1   MET   C CA  1 
ATOM   1618 C  C   . MET   B 1 6   ? -61.699 3.082   31.563  1.00 28.47 ?  1   MET   C C   1 
ATOM   1619 O  O   . MET   B 1 6   ? -62.694 3.384   32.239  1.00 32.90 ?  1   MET   C O   1 
ATOM   1620 C  CB  . MET   B 1 6   ? -59.844 4.104   32.845  1.00 31.64 ?  1   MET   C CB  1 
ATOM   1621 C  CG  . MET   B 1 6   ? -59.174 2.831   33.218  1.00 32.05 ?  1   MET   C CG  1 
ATOM   1622 S  SD  . MET   B 1 6   ? -58.638 2.964   34.933  1.00 35.21 ?  1   MET   C SD  1 
ATOM   1623 C  CE  . MET   B 1 6   ? -57.860 1.362   35.065  1.00 33.79 ?  1   MET   C CE  1 
ATOM   1624 N  N   . PHE   B 1 7   ? -61.571 1.905   30.964  1.00 28.87 ?  2   PHE   C N   1 
ATOM   1625 C  CA  . PHE   B 1 7   ? -62.657 0.895   31.033  1.00 29.49 ?  2   PHE   C CA  1 
ATOM   1626 C  C   . PHE   B 1 7   ? -62.540 0.111   32.338  1.00 27.56 ?  2   PHE   C C   1 
ATOM   1627 O  O   . PHE   B 1 7   ? -61.548 -0.652  32.520  1.00 31.09 ?  2   PHE   C O   1 
ATOM   1628 C  CB  . PHE   B 1 7   ? -62.592 -0.062  29.845  1.00 29.73 ?  2   PHE   C CB  1 
ATOM   1629 C  CG  . PHE   B 1 7   ? -63.686 -1.085  29.877  1.00 31.65 ?  2   PHE   C CG  1 
ATOM   1630 C  CD1 . PHE   B 1 7   ? -65.009 -0.687  29.767  1.00 36.73 ?  2   PHE   C CD1 1 
ATOM   1631 C  CD2 . PHE   B 1 7   ? -63.402 -2.422  30.072  1.00 35.81 ?  2   PHE   C CD2 1 
ATOM   1632 C  CE1 . PHE   B 1 7   ? -66.034 -1.627  29.799  1.00 36.02 ?  2   PHE   C CE1 1 
ATOM   1633 C  CE2 . PHE   B 1 7   ? -64.425 -3.356  30.107  1.00 38.38 ?  2   PHE   C CE2 1 
ATOM   1634 C  CZ  . PHE   B 1 7   ? -65.737 -2.956  29.972  1.00 37.97 ?  2   PHE   C CZ  1 
ATOM   1635 N  N   . VAL   B 1 8   ? -63.521 0.247   33.220  1.00 24.72 ?  3   VAL   C N   1 
ATOM   1636 C  CA  . VAL   B 1 8   ? -63.555 -0.538  34.485  1.00 22.17 ?  3   VAL   C CA  1 
ATOM   1637 C  C   . VAL   B 1 8   ? -64.883 -1.255  34.557  1.00 25.38 ?  3   VAL   C C   1 
ATOM   1638 O  O   . VAL   B 1 8   ? -65.909 -0.587  34.687  1.00 22.00 ?  3   VAL   C O   1 
ATOM   1639 C  CB  . VAL   B 1 8   ? -63.360 0.364   35.717  1.00 22.13 ?  3   VAL   C CB  1 
ATOM   1640 C  CG1 . VAL   B 1 8   ? -63.330 -0.458  36.986  1.00 23.49 ?  3   VAL   C CG1 1 
ATOM   1641 C  CG2 . VAL   B 1 8   ? -62.084 1.198   35.588  1.00 23.19 ?  3   VAL   C CG2 1 
ATOM   1642 N  N   . PRO   B 1 9   ? -64.897 -2.597  34.443  1.00 25.51 ?  4   PRO   C N   1 
ATOM   1643 C  CA  . PRO   B 1 9   ? -66.124 -3.360  34.662  1.00 25.22 ?  4   PRO   C CA  1 
ATOM   1644 C  C   . PRO   B 1 9   ? -66.726 -3.074  36.044  1.00 28.66 ?  4   PRO   C C   1 
ATOM   1645 O  O   . PRO   B 1 9   ? -66.007 -2.903  37.012  1.00 26.38 ?  4   PRO   C O   1 
ATOM   1646 C  CB  . PRO   B 1 9   ? -65.698 -4.830  34.491  1.00 27.14 ?  4   PRO   C CB  1 
ATOM   1647 C  CG  . PRO   B 1 9   ? -64.375 -4.762  33.703  1.00 27.02 ?  4   PRO   C CG  1 
ATOM   1648 C  CD  . PRO   B 1 9   ? -63.746 -3.452  34.149  1.00 25.26 ?  4   PRO   C CD  1 
ATOM   1649 N  N   . GLY   B 1 10  ? -68.062 -3.019  36.109  1.00 30.78 ?  5   GLY   C N   1 
ATOM   1650 C  CA  . GLY   B 1 10  ? -68.815 -2.660  37.326  1.00 30.80 ?  5   GLY   C CA  1 
ATOM   1651 C  C   . GLY   B 1 10  ? -68.286 -3.301  38.605  1.00 29.75 ?  5   GLY   C C   1 
ATOM   1652 O  O   . GLY   B 1 10  ? -68.086 -2.585  39.597  1.00 29.58 ?  5   GLY   C O   1 
ATOM   1653 N  N   . PRO   B 1 11  ? -68.027 -4.641  38.639  1.00 28.82 ?  6   PRO   C N   1 
ATOM   1654 C  CA  . PRO   B 1 11  ? -67.642 -5.317  39.864  1.00 27.83 ?  6   PRO   C CA  1 
ATOM   1655 C  C   . PRO   B 1 11  ? -66.257 -4.867  40.346  1.00 23.53 ?  6   PRO   C C   1 
ATOM   1656 O  O   . PRO   B 1 11  ? -65.963 -5.157  41.477  1.00 22.50 ?  6   PRO   C O   1 
ATOM   1657 C  CB  . PRO   B 1 11  ? -67.589 -6.812  39.522  1.00 31.27 ?  6   PRO   C CB  1 
ATOM   1658 C  CG  . PRO   B 1 11  ? -68.312 -6.920  38.220  1.00 32.93 ?  6   PRO   C CG  1 
ATOM   1659 C  CD  . PRO   B 1 11  ? -68.114 -5.594  37.520  1.00 32.30 ?  6   PRO   C CD  1 
ATOM   1660 N  N   . TYR   B 1 12  ? -65.486 -4.159  39.515  1.00 22.83 ?  7   TYR   C N   1 
ATOM   1661 C  CA  . TYR   B 1 12  ? -64.086 -3.804  39.871  1.00 20.61 ?  7   TYR   C CA  1 
ATOM   1662 C  C   . TYR   B 1 12  ? -63.999 -2.329  40.286  1.00 23.24 ?  7   TYR   C C   1 
ATOM   1663 O  O   . TYR   B 1 12  ? -62.863 -1.788  40.475  1.00 21.10 ?  7   TYR   C O   1 
ATOM   1664 C  CB  . TYR   B 1 12  ? -63.132 -4.155  38.725  1.00 21.52 ?  7   TYR   C CB  1 
ATOM   1665 C  CG  . TYR   B 1 12  ? -63.136 -5.610  38.323  1.00 19.43 ?  7   TYR   C CG  1 
ATOM   1666 C  CD1 . TYR   B 1 12  ? -63.335 -6.608  39.262  1.00 20.96 ?  7   TYR   C CD1 1 
ATOM   1667 C  CD2 . TYR   B 1 12  ? -62.959 -5.994  37.008  1.00 22.43 ?  7   TYR   C CD2 1 
ATOM   1668 C  CE1 . TYR   B 1 12  ? -63.366 -7.934  38.893  1.00 22.38 ?  7   TYR   C CE1 1 
ATOM   1669 C  CE2 . TYR   B 1 12  ? -62.981 -7.324  36.616  1.00 22.52 ?  7   TYR   C CE2 1 
ATOM   1670 C  CZ  . TYR   B 1 12  ? -63.212 -8.295  37.574  1.00 21.79 ?  7   TYR   C CZ  1 
ATOM   1671 O  OH  . TYR   B 1 12  ? -63.249 -9.634  37.282  1.00 25.52 ?  7   TYR   C OH  1 
ATOM   1672 N  N   . HIS   B 1 13  ? -65.137 -1.668  40.509  1.00 21.04 ?  8   HIS   C N   1 
ATOM   1673 C  CA  . HIS   B 1 13  ? -65.112 -0.281  41.040  1.00 22.77 ?  8   HIS   C CA  1 
ATOM   1674 C  C   . HIS   B 1 13  ? -64.715 -0.308  42.505  1.00 23.29 ?  8   HIS   C C   1 
ATOM   1675 O  O   . HIS   B 1 13  ? -65.157 -1.189  43.241  1.00 26.13 ?  8   HIS   C O   1 
ATOM   1676 C  CB  . HIS   B 1 13  ? -66.463 0.417   40.811  1.00 24.56 ?  8   HIS   C CB  1 
ATOM   1677 C  CG  . HIS   B 1 13  ? -66.678 0.740   39.380  1.00 30.08 ?  8   HIS   C CG  1 
ATOM   1678 N  ND1 . HIS   B 1 13  ? -66.924 2.028   38.939  1.00 42.03 ?  8   HIS   C ND1 1 
ATOM   1679 C  CD2 . HIS   B 1 13  ? -66.605 -0.016  38.265  1.00 32.66 ?  8   HIS   C CD2 1 
ATOM   1680 C  CE1 . HIS   B 1 13  ? -67.014 2.034   37.619  1.00 37.90 ?  8   HIS   C CE1 1 
ATOM   1681 N  NE2 . HIS   B 1 13  ? -66.834 0.799   37.190  1.00 33.98 ?  8   HIS   C NE2 1 
ATOM   1682 N  N   . ALA   B 1 14  ? -63.943 0.684   42.942  1.00 23.64 ?  9   ALA   C N   1 
ATOM   1683 C  CA  . ALA   B 1 14  ? -63.648 0.832   44.379  1.00 26.60 ?  9   ALA   C CA  1 
ATOM   1684 C  C   . ALA   B 1 14  ? -64.965 1.043   45.117  1.00 26.02 ?  9   ALA   C C   1 
ATOM   1685 O  O   . ALA   B 1 14  ? -65.863 1.712   44.605  1.00 25.33 ?  9   ALA   C O   1 
ATOM   1686 C  CB  . ALA   B 1 14  ? -62.706 1.981   44.611  1.00 30.28 ?  9   ALA   C CB  1 
ATOM   1687 N  N   . PRO   B 1 15  ? -65.087 0.539   46.353  1.00 27.46 ?  10  PRO   C N   1 
ATOM   1688 C  CA  . PRO   B 1 15  ? -66.257 0.842   47.178  1.00 29.45 ?  10  PRO   C CA  1 
ATOM   1689 C  C   . PRO   B 1 15  ? -66.384 2.328   47.545  1.00 29.39 ?  10  PRO   C C   1 
ATOM   1690 O  O   . PRO   B 1 15  ? -67.482 2.762   47.761  1.00 28.62 ?  10  PRO   C O   1 
ATOM   1691 C  CB  . PRO   B 1 15  ? -66.057 0.029   48.464  1.00 30.35 ?  10  PRO   C CB  1 
ATOM   1692 C  CG  . PRO   B 1 15  ? -64.600 -0.377  48.456  1.00 33.79 ?  10  PRO   C CG  1 
ATOM   1693 C  CD  . PRO   B 1 15  ? -64.149 -0.377  47.013  1.00 29.15 ?  10  PRO   C CD  1 
ATOM   1694 N  N   . GLU   B 1 16  ? -65.273 3.067   47.649  1.00 28.43 ?  11  GLU   C N   1 
ATOM   1695 C  CA  . GLU   B 1 16  ? -65.250 4.507   48.035  1.00 29.44 ?  11  GLU   C CA  1 
ATOM   1696 C  C   . GLU   B 1 16  ? -64.214 5.247   47.185  1.00 27.15 ?  11  GLU   C C   1 
ATOM   1697 O  O   . GLU   B 1 16  ? -63.178 4.642   46.857  1.00 23.35 ?  11  GLU   C O   1 
ATOM   1698 C  CB  . GLU   B 1 16  ? -64.857 4.697   49.509  1.00 36.84 ?  11  GLU   C CB  1 
ATOM   1699 C  CG  . GLU   B 1 16  ? -65.866 4.155   50.517  1.00 42.60 ?  11  GLU   C CG  1 
ATOM   1700 C  CD  . GLU   B 1 16  ? -67.250 4.801   50.485  1.00 56.45 ?  11  GLU   C CD  1 
ATOM   1701 O  OE1 . GLU   B 1 16  ? -67.333 5.997   50.108  1.00 61.99 ?  11  GLU   C OE1 1 
ATOM   1702 O  OE2 . GLU   B 1 16  ? -68.256 4.107   50.835  1.00 61.91 -1 11  GLU   C OE2 1 
ATOM   1703 N  N   . ASP   B 1 17  ? -64.452 6.525   46.903  1.00 26.07 ?  12  ASP   C N   1 
ATOM   1704 C  CA  . ASP   B 1 17  ? -63.497 7.394   46.171  1.00 26.57 ?  12  ASP   C CA  1 
ATOM   1705 C  C   . ASP   B 1 17  ? -62.130 7.392   46.874  1.00 24.10 ?  12  ASP   C C   1 
ATOM   1706 O  O   . ASP   B 1 17  ? -61.121 7.511   46.173  1.00 21.26 ?  12  ASP   C O   1 
ATOM   1707 C  CB  . ASP   B 1 17  ? -64.007 8.822   46.051  1.00 30.59 ?  12  ASP   C CB  1 
ATOM   1708 C  CG  . ASP   B 1 17  ? -65.222 8.977   45.145  1.00 32.90 ?  12  ASP   C CG  1 
ATOM   1709 O  OD1 . ASP   B 1 17  ? -65.377 8.181   44.198  1.00 32.33 ?  12  ASP   C OD1 1 
ATOM   1710 O  OD2 . ASP   B 1 17  ? -66.008 9.912   45.398  1.00 40.76 -1 12  ASP   C OD2 1 
ATOM   1711 N  N   . ARG   B 1 18  ? -62.102 7.273   48.194  1.00 23.58 ?  13  ARG   C N   1 
ATOM   1712 C  CA  . ARG   B 1 18  ? -60.837 7.366   48.967  1.00 24.10 ?  13  ARG   C CA  1 
ATOM   1713 C  C   . ARG   B 1 18  ? -59.860 6.257   48.557  1.00 23.08 ?  13  ARG   C C   1 
ATOM   1714 O  O   . ARG   B 1 18  ? -58.600 6.489   48.659  1.00 23.26 ?  13  ARG   C O   1 
ATOM   1715 C  CB  . ARG   B 1 18  ? -61.160 7.400   50.464  1.00 28.37 ?  13  ARG   C CB  1 
ATOM   1716 C  CG  . ARG   B 1 18  ? -60.002 7.068   51.377  1.00 37.21 ?  13  ARG   C CG  1 
ATOM   1717 C  CD  . ARG   B 1 18  ? -58.980 8.172   51.312  1.00 43.68 ?  13  ARG   C CD  1 
ATOM   1718 N  NE  . ARG   B 1 18  ? -59.222 9.191   52.311  1.00 57.33 ?  13  ARG   C NE  1 
ATOM   1719 C  CZ  . ARG   B 1 18  ? -58.408 9.484   53.323  1.00 60.07 ?  13  ARG   C CZ  1 
ATOM   1720 N  NH1 . ARG   B 1 18  ? -57.263 8.839   53.497  1.00 58.82 1  13  ARG   C NH1 1 
ATOM   1721 N  NH2 . ARG   B 1 18  ? -58.754 10.443  54.163  1.00 67.60 ?  13  ARG   C NH2 1 
ATOM   1722 N  N   . TRP   B 1 19  ? -60.361 5.136   48.042  1.00 21.48 ?  14  TRP   C N   1 
ATOM   1723 C  CA  . TRP   B 1 19  ? -59.469 4.019   47.632  1.00 22.14 ?  14  TRP   C CA  1 
ATOM   1724 C  C   . TRP   B 1 19  ? -58.532 4.507   46.523  1.00 19.68 ?  14  TRP   C C   1 
ATOM   1725 O  O   . TRP   B 1 19  ? -57.351 4.066   46.512  1.00 20.01 ?  14  TRP   C O   1 
ATOM   1726 C  CB  . TRP   B 1 19  ? -60.274 2.819   47.170  1.00 22.60 ?  14  TRP   C CB  1 
ATOM   1727 C  CG  . TRP   B 1 19  ? -60.865 1.994   48.273  1.00 23.76 ?  14  TRP   C CG  1 
ATOM   1728 C  CD1 . TRP   B 1 19  ? -61.527 2.424   49.390  1.00 25.71 ?  14  TRP   C CD1 1 
ATOM   1729 C  CD2 . TRP   B 1 19  ? -60.825 0.559   48.347  1.00 24.51 ?  14  TRP   C CD2 1 
ATOM   1730 N  NE1 . TRP   B 1 19  ? -61.874 1.351   50.171  1.00 26.00 ?  14  TRP   C NE1 1 
ATOM   1731 C  CE2 . TRP   B 1 19  ? -61.482 0.192   49.545  1.00 25.49 ?  14  TRP   C CE2 1 
ATOM   1732 C  CE3 . TRP   B 1 19  ? -60.303 -0.443  47.519  1.00 25.35 ?  14  TRP   C CE3 1 
ATOM   1733 C  CZ2 . TRP   B 1 19  ? -61.602 -1.144  49.936  1.00 25.84 ?  14  TRP   C CZ2 1 
ATOM   1734 C  CZ3 . TRP   B 1 19  ? -60.422 -1.757  47.910  1.00 26.60 ?  14  TRP   C CZ3 1 
ATOM   1735 C  CH2 . TRP   B 1 19  ? -61.084 -2.103  49.085  1.00 26.05 ?  14  TRP   C CH2 1 
ATOM   1736 N  N   . LEU   B 1 20  ? -59.015 5.371   45.628  1.00 19.15 ?  15  LEU   C N   1 
ATOM   1737 C  CA  . LEU   B 1 20  ? -58.185 5.818   44.492  1.00 19.79 ?  15  LEU   C CA  1 
ATOM   1738 C  C   . LEU   B 1 20  ? -57.088 6.712   45.054  1.00 19.44 ?  15  LEU   C C   1 
ATOM   1739 O  O   . LEU   B 1 20  ? -55.944 6.558   44.646  1.00 18.65 ?  15  LEU   C O   1 
ATOM   1740 C  CB  . LEU   B 1 20  ? -59.004 6.571   43.463  1.00 22.43 ?  15  LEU   C CB  1 
ATOM   1741 C  CG  . LEU   B 1 20  ? -59.888 5.724   42.551  1.00 22.08 ?  15  LEU   C CG  1 
ATOM   1742 C  CD1 . LEU   B 1 20  ? -61.100 5.196   43.311  1.00 21.63 ?  15  LEU   C CD1 1 
ATOM   1743 C  CD2 . LEU   B 1 20  ? -60.302 6.554   41.323  1.00 23.18 ?  15  LEU   C CD2 1 
ATOM   1744 N  N   . VAL   B 1 21  ? -57.424 7.590   46.016  1.00 17.33 ?  16  VAL   C N   1 
ATOM   1745 C  CA  . VAL   B 1 21  ? -56.409 8.480   46.642  1.00 19.76 ?  16  VAL   C CA  1 
ATOM   1746 C  C   . VAL   B 1 21  ? -55.369 7.623   47.364  1.00 17.55 ?  16  VAL   C C   1 
ATOM   1747 O  O   . VAL   B 1 21  ? -54.164 7.891   47.231  1.00 18.36 ?  16  VAL   C O   1 
ATOM   1748 C  CB  . VAL   B 1 21  ? -57.072 9.484   47.611  1.00 21.58 ?  16  VAL   C CB  1 
ATOM   1749 C  CG1 . VAL   B 1 21  ? -56.046 10.432  48.225  1.00 22.67 ?  16  VAL   C CG1 1 
ATOM   1750 C  CG2 . VAL   B 1 21  ? -58.149 10.265  46.923  1.00 22.84 ?  16  VAL   C CG2 1 
ATOM   1751 N  N   . ASP   B 1 22  ? -55.811 6.613   48.126  1.00 20.47 ?  17  ASP   C N   1 
ATOM   1752 C  CA  . ASP   B 1 22  ? -54.916 5.680   48.884  1.00 21.18 ?  17  ASP   C CA  1 
ATOM   1753 C  C   . ASP   B 1 22  ? -53.944 4.980   47.934  1.00 20.66 ?  17  ASP   C C   1 
ATOM   1754 O  O   . ASP   B 1 22  ? -52.745 4.850   48.283  1.00 19.59 ?  17  ASP   C O   1 
ATOM   1755 C  CB  . ASP   B 1 22  ? -55.676 4.612   49.684  1.00 25.29 ?  17  ASP   C CB  1 
ATOM   1756 C  CG  . ASP   B 1 22  ? -56.564 5.124   50.815  1.00 32.43 ?  17  ASP   C CG  1 
ATOM   1757 O  OD1 . ASP   B 1 22  ? -56.412 6.294   51.200  1.00 35.30 ?  17  ASP   C OD1 1 
ATOM   1758 O  OD2 . ASP   B 1 22  ? -57.411 4.339   51.293  1.00 42.22 -1 17  ASP   C OD2 1 
ATOM   1759 N  N   . LEU   B 1 23  ? -54.409 4.586   46.749  1.00 18.87 ?  18  LEU   C N   1 
ATOM   1760 C  CA  . LEU   B 1 23  ? -53.508 3.905   45.776  1.00 20.06 ?  18  LEU   C CA  1 
ATOM   1761 C  C   . LEU   B 1 23  ? -52.459 4.890   45.272  1.00 18.03 ?  18  LEU   C C   1 
ATOM   1762 O  O   . LEU   B 1 23  ? -51.269 4.498   45.212  1.00 18.38 ?  18  LEU   C O   1 
ATOM   1763 C  CB  . LEU   B 1 23  ? -54.293 3.297   44.613  1.00 22.83 ?  18  LEU   C CB  1 
ATOM   1764 C  CG  . LEU   B 1 23  ? -53.497 2.283   43.787  1.00 26.67 ?  18  LEU   C CG  1 
ATOM   1765 C  CD1 . LEU   B 1 23  ? -54.418 1.431   42.937  1.00 30.19 ?  18  LEU   C CD1 1 
ATOM   1766 C  CD2 . LEU   B 1 23  ? -52.518 2.986   42.879  1.00 31.79 ?  18  LEU   C CD2 1 
ATOM   1767 N  N   . VAL   B 1 24  ? -52.856 6.118   44.917  1.00 19.24 ?  19  VAL   C N   1 
ATOM   1768 C  CA  . VAL   B 1 24  ? -51.904 7.155   44.418  1.00 19.64 ?  19  VAL   C CA  1 
ATOM   1769 C  C   . VAL   B 1 24  ? -50.877 7.399   45.514  1.00 19.58 ?  19  VAL   C C   1 
ATOM   1770 O  O   . VAL   B 1 24  ? -49.661 7.442   45.224  1.00 18.06 ?  19  VAL   C O   1 
ATOM   1771 C  CB  . VAL   B 1 24  ? -52.640 8.458   44.060  1.00 23.32 ?  19  VAL   C CB  1 
ATOM   1772 C  CG1 . VAL   B 1 24  ? -51.650 9.614   43.954  1.00 22.70 ?  19  VAL   C CG1 1 
ATOM   1773 C  CG2 . VAL   B 1 24  ? -53.469 8.291   42.791  1.00 22.31 ?  19  VAL   C CG2 1 
ATOM   1774 N  N   . ARG   B 1 25  ? -51.307 7.574   46.750  1.00 18.20 ?  20  ARG   C N   1 
ATOM   1775 C  CA  . ARG   B 1 25  ? -50.312 7.828   47.838  1.00 20.51 ?  20  ARG   C CA  1 
ATOM   1776 C  C   . ARG   B 1 25  ? -49.383 6.641   48.044  1.00 19.81 ?  20  ARG   C C   1 
ATOM   1777 O  O   . ARG   B 1 25  ? -48.189 6.848   48.381  1.00 19.59 ?  20  ARG   C O   1 
ATOM   1778 C  CB  . ARG   B 1 25  ? -51.010 8.186   49.147  1.00 21.33 ?  20  ARG   C CB  1 
ATOM   1779 C  CG  . ARG   B 1 25  ? -51.786 9.496   49.085  1.00 25.17 ?  20  ARG   C CG  1 
ATOM   1780 C  CD  . ARG   B 1 25  ? -52.284 9.818   50.496  1.00 29.03 ?  20  ARG   C CD  1 
ATOM   1781 N  NE  . ARG   B 1 25  ? -53.060 11.038  50.634  1.00 31.43 ?  20  ARG   C NE  1 
ATOM   1782 C  CZ  . ARG   B 1 25  ? -52.586 12.291  50.597  1.00 36.51 ?  20  ARG   C CZ  1 
ATOM   1783 N  NH1 . ARG   B 1 25  ? -51.301 12.563  50.384  1.00 38.99 1  20  ARG   C NH1 1 
ATOM   1784 N  NH2 . ARG   B 1 25  ? -53.436 13.291  50.747  1.00 42.98 ?  20  ARG   C NH2 1 
ATOM   1785 N  N   . GLY   B 1 26  ? -49.882 5.417   47.922  1.00 17.97 ?  21  GLY   C N   1 
ATOM   1786 C  CA  . GLY   B 1 26  ? -49.090 4.216   48.215  1.00 17.71 ?  21  GLY   C CA  1 
ATOM   1787 C  C   . GLY   B 1 26  ? -48.155 3.810   47.081  1.00 17.37 ?  21  GLY   C C   1 
ATOM   1788 O  O   . GLY   B 1 26  ? -47.313 2.909   47.345  1.00 19.70 ?  21  GLY   C O   1 
ATOM   1789 N  N   . HIS   B 1 27  ? -48.343 4.361   45.863  1.00 17.22 ?  22  HIS   C N   1 
ATOM   1790 C  CA  . HIS   B 1 27  ? -47.661 3.922   44.620  1.00 18.18 ?  22  HIS   C CA  1 
ATOM   1791 C  C   . HIS   B 1 27  ? -47.334 5.141   43.762  1.00 18.36 ?  22  HIS   C C   1 
ATOM   1792 O  O   . HIS   B 1 27  ? -47.745 5.244   42.620  1.00 17.63 ?  22  HIS   C O   1 
ATOM   1793 C  CB  . HIS   B 1 27  ? -48.453 2.828   43.893  1.00 18.31 ?  22  HIS   C CB  1 
ATOM   1794 C  CG  . HIS   B 1 27  ? -48.866 1.739   44.810  1.00 18.66 ?  22  HIS   C CG  1 
ATOM   1795 N  ND1 . HIS   B 1 27  ? -48.052 0.683   45.080  1.00 20.49 ?  22  HIS   C ND1 1 
ATOM   1796 C  CD2 . HIS   B 1 27  ? -49.950 1.586   45.588  1.00 19.22 ?  22  HIS   C CD2 1 
ATOM   1797 C  CE1 . HIS   B 1 27  ? -48.622 -0.080  45.986  1.00 21.06 ?  22  HIS   C CE1 1 
ATOM   1798 N  NE2 . HIS   B 1 27  ? -49.791 0.431   46.298  1.00 20.86 ?  22  HIS   C NE2 1 
ATOM   1799 N  N   . PRO   B 1 28  ? -46.492 6.055   44.286  1.00 17.12 ?  23  PRO   C N   1 
ATOM   1800 C  CA  . PRO   B 1 28  ? -46.264 7.348   43.634  1.00 17.43 ?  23  PRO   C CA  1 
ATOM   1801 C  C   . PRO   B 1 28  ? -45.474 7.335   42.326  1.00 17.91 ?  23  PRO   C C   1 
ATOM   1802 O  O   . PRO   B 1 28  ? -45.499 8.350   41.633  1.00 17.78 ?  23  PRO   C O   1 
ATOM   1803 C  CB  . PRO   B 1 28  ? -45.477 8.136   44.705  1.00 17.61 ?  23  PRO   C CB  1 
ATOM   1804 C  CG  . PRO   B 1 28  ? -44.814 7.082   45.520  1.00 18.53 ?  23  PRO   C CG  1 
ATOM   1805 C  CD  . PRO   B 1 28  ? -45.771 5.917   45.568  1.00 17.23 ?  23  PRO   C CD  1 
ATOM   1806 N  N   . LEU   B 1 29  ? -44.710 6.259   42.055  1.00 17.99 ?  24  LEU   C N   1 
ATOM   1807 C  CA  . LEU   B 1 29  ? -43.977 6.197   40.775  1.00 17.78 ?  24  LEU   C CA  1 
ATOM   1808 C  C   . LEU   B 1 29  ? -44.953 5.771   39.675  1.00 17.16 ?  24  LEU   C C   1 
ATOM   1809 O  O   . LEU   B 1 29  ? -45.148 4.553   39.420  1.00 18.36 ?  24  LEU   C O   1 
ATOM   1810 C  CB  . LEU   B 1 29  ? -42.757 5.286   40.875  1.00 17.49 ?  24  LEU   C CB  1 
ATOM   1811 C  CG  . LEU   B 1 29  ? -41.757 5.449   39.713  1.00 21.62 ?  24  LEU   C CG  1 
ATOM   1812 C  CD1 . LEU   B 1 29  ? -40.980 6.769   39.803  1.00 24.26 ?  24  LEU   C CD1 1 
ATOM   1813 C  CD2 . LEU   B 1 29  ? -40.821 4.239   39.630  1.00 21.22 ?  24  LEU   C CD2 1 
ATOM   1814 N  N   . ALA   B 1 30  ? -45.522 6.783   39.026  1.00 17.04 ?  25  ALA   C N   1 
ATOM   1815 C  CA  . ALA   B 1 30  ? -46.589 6.669   38.032  1.00 16.85 ?  25  ALA   C CA  1 
ATOM   1816 C  C   . ALA   B 1 30  ? -45.972 6.511   36.651  1.00 18.62 ?  25  ALA   C C   1 
ATOM   1817 O  O   . ALA   B 1 30  ? -44.844 6.931   36.462  1.00 20.34 ?  25  ALA   C O   1 
ATOM   1818 C  CB  . ALA   B 1 30  ? -47.472 7.885   38.111  1.00 18.53 ?  25  ALA   C CB  1 
ATOM   1819 N  N   . GLN   B 1 31  ? -46.704 5.930   35.726  1.00 16.92 ?  26  GLN   C N   1 
ATOM   1820 C  CA  . GLN   B 1 31  ? -46.346 6.005   34.289  1.00 16.60 ?  26  GLN   C CA  1 
ATOM   1821 C  C   . GLN   B 1 31  ? -47.135 7.173   33.704  1.00 17.35 ?  26  GLN   C C   1 
ATOM   1822 O  O   . GLN   B 1 31  ? -48.395 7.079   33.601  1.00 18.52 ?  26  GLN   C O   1 
ATOM   1823 C  CB  . GLN   B 1 31  ? -46.641 4.679   33.596  1.00 15.06 ?  26  GLN   C CB  1 
ATOM   1824 C  CG  . GLN   B 1 31  ? -45.767 3.521   34.043  1.00 18.12 ?  26  GLN   C CG  1 
ATOM   1825 C  CD  . GLN   B 1 31  ? -45.977 2.219   33.288  1.00 16.30 ?  26  GLN   C CD  1 
ATOM   1826 O  OE1 . GLN   B 1 31  ? -46.347 2.196   32.114  1.00 19.62 ?  26  GLN   C OE1 1 
ATOM   1827 N  NE2 . GLN   B 1 31  ? -45.790 1.117   33.986  1.00 17.11 ?  26  GLN   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 32  ? -46.424 8.204   33.307  1.00 18.40 ?  27  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 32  ? -47.018 9.399   32.687  1.00 17.07 ?  27  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 32  ? -47.027 9.159   31.182  1.00 17.57 ?  27  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 32  ? -45.932 8.914   30.617  1.00 14.52 ?  27  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 32  ? -46.217 10.632  33.049  1.00 16.76 ?  27  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 32  ? -46.690 11.932  32.365  1.00 18.71 ?  27  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 32  ? -48.085 12.351  32.800  1.00 19.66 ?  27  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 32  ? -45.730 13.073  32.616  1.00 22.71 ?  27  LEU   C CD2 1 
ATOM   1836 N  N   . ALA   B 1 33  ? -48.219 9.183   30.565  1.00 13.71 ?  28  ALA   C N   1 
ATOM   1837 C  CA  . ALA   B 1 33  ? -48.340 8.969   29.112  1.00 16.24 ?  28  ALA   C CA  1 
ATOM   1838 C  C   . ALA   B 1 33  ? -48.884 10.228  28.427  1.00 16.32 ?  28  ALA   C C   1 
ATOM   1839 O  O   . ALA   B 1 33  ? -49.920 10.751  28.862  1.00 17.16 ?  28  ALA   C O   1 
ATOM   1840 C  CB  . ALA   B 1 33  ? -49.197 7.757   28.795  1.00 17.16 ?  28  ALA   C CB  1 
ATOM   1841 N  N   . SER   B 1 34  ? -48.330 10.522  27.260  1.00 18.17 ?  29  SER   C N   1 
ATOM   1842 C  CA  . SER   B 1 34  ? -48.894 11.518  26.330  1.00 17.12 ?  29  SER   C CA  1 
ATOM   1843 C  C   . SER   B 1 34  ? -48.786 11.053  24.877  1.00 18.57 ?  29  SER   C C   1 
ATOM   1844 O  O   . SER   B 1 34  ? -48.047 10.129  24.581  1.00 21.31 ?  29  SER   C O   1 
ATOM   1845 C  CB  . SER   B 1 34  ? -48.276 12.863  26.543  1.00 19.57 ?  29  SER   C CB  1 
ATOM   1846 O  OG  . SER   B 1 34  ? -46.919 12.821  26.190  1.00 20.44 ?  29  SER   C OG  1 
ATOM   1847 N  N   . ASN   B 1 35  ? -49.606 11.630  24.012  1.00 21.67 ?  30  ASN   C N   1 
ATOM   1848 C  CA  . ASN   B 1 35  ? -49.698 11.162  22.608  1.00 24.08 ?  30  ASN   C CA  1 
ATOM   1849 C  C   . ASN   B 1 35  ? -48.373 11.334  21.869  1.00 24.37 ?  30  ASN   C C   1 
ATOM   1850 O  O   . ASN   B 1 35  ? -47.636 12.364  22.089  1.00 24.92 ?  30  ASN   C O   1 
ATOM   1851 C  CB  . ASN   B 1 35  ? -50.820 11.849  21.840  1.00 25.51 ?  30  ASN   C CB  1 
ATOM   1852 C  CG  . ASN   B 1 35  ? -52.201 11.422  22.272  1.00 27.53 ?  30  ASN   C CG  1 
ATOM   1853 O  OD1 . ASN   B 1 35  ? -52.400 10.373  22.871  1.00 24.69 ?  30  ASN   C OD1 1 
ATOM   1854 N  ND2 . ASN   B 1 35  ? -53.188 12.259  21.969  1.00 33.50 ?  30  ASN   C ND2 1 
ATOM   1855 N  N   . GLY   B 1 36  ? -48.078 10.358  20.994  1.00 22.44 ?  31  GLY   C N   1 
ATOM   1856 C  CA  . GLY   B 1 36  ? -46.902 10.398  20.118  1.00 24.30 ?  31  GLY   C CA  1 
ATOM   1857 C  C   . GLY   B 1 36  ? -47.279 11.241  18.903  1.00 26.78 ?  31  GLY   C C   1 
ATOM   1858 O  O   . GLY   B 1 36  ? -48.439 11.180  18.499  1.00 32.07 ?  31  GLY   C O   1 
ATOM   1859 N  N   . ALA   B 1 37  ? -46.373 12.055  18.406  1.00 30.12 ?  32  ALA   C N   1 
ATOM   1860 C  CA  . ALA   B 1 37  ? -46.626 12.952  17.256  1.00 33.69 ?  32  ALA   C CA  1 
ATOM   1861 C  C   . ALA   B 1 37  ? -46.671 12.084  16.003  1.00 35.62 ?  32  ALA   C C   1 
ATOM   1862 O  O   . ALA   B 1 37  ? -45.892 11.094  15.954  1.00 34.03 ?  32  ALA   C O   1 
ATOM   1863 C  CB  . ALA   B 1 37  ? -45.560 14.005  17.180  1.00 35.43 ?  32  ALA   C CB  1 
ATOM   1864 N  N   . GLY   B 1 38  ? -47.594 12.412  15.086  1.00 40.22 ?  33  GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 38  ? -47.677 11.821  13.739  1.00 42.08 ?  33  GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 38  ? -48.071 10.362  13.814  1.00 41.79 ?  33  GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 38  ? -47.487 9.576   13.089  1.00 41.04 ?  33  GLY   C O   1 
ATOM   1868 N  N   . GLY   B 1 39  ? -49.042 10.042  14.672  1.00 45.65 ?  34  GLY   C N   1 
ATOM   1869 C  CA  . GLY   B 1 39  ? -49.556 8.679   14.910  1.00 43.96 ?  34  GLY   C CA  1 
ATOM   1870 C  C   . GLY   B 1 39  ? -48.517 7.721   15.481  1.00 39.15 ?  34  GLY   C C   1 
ATOM   1871 O  O   . GLY   B 1 39  ? -48.790 6.502   15.476  1.00 43.66 ?  34  GLY   C O   1 
ATOM   1872 N  N   . ALA   B 1 40  ? -47.391 8.211   15.989  1.00 28.24 ?  35  ALA   C N   1 
ATOM   1873 C  CA  . ALA   B 1 40  ? -46.400 7.374   16.701  1.00 30.74 ?  35  ALA   C CA  1 
ATOM   1874 C  C   . ALA   B 1 40  ? -46.996 6.934   18.052  1.00 27.63 ?  35  ALA   C C   1 
ATOM   1875 O  O   . ALA   B 1 40  ? -48.002 7.501   18.509  1.00 28.67 ?  35  ALA   C O   1 
ATOM   1876 C  CB  . ALA   B 1 40  ? -45.065 8.071   16.842  1.00 30.36 ?  35  ALA   C CB  1 
ATOM   1877 N  N   . ALA   B 1 41  ? -46.481 5.850   18.616  1.00 25.51 ?  36  ALA   C N   1 
ATOM   1878 C  CA  . ALA   B 1 41  ? -46.919 5.350   19.934  1.00 23.80 ?  36  ALA   C CA  1 
ATOM   1879 C  C   . ALA   B 1 41  ? -46.747 6.469   20.967  1.00 23.24 ?  36  ALA   C C   1 
ATOM   1880 O  O   . ALA   B 1 41  ? -45.823 7.279   20.892  1.00 20.41 ?  36  ALA   C O   1 
ATOM   1881 C  CB  . ALA   B 1 41  ? -46.090 4.154   20.303  1.00 24.11 ?  36  ALA   C CB  1 
ATOM   1882 N  N   . PRO   B 1 42  ? -47.560 6.464   22.032  1.00 19.97 ?  37  PRO   C N   1 
ATOM   1883 C  CA  . PRO   B 1 42  ? -47.335 7.362   23.147  1.00 19.30 ?  37  PRO   C CA  1 
ATOM   1884 C  C   . PRO   B 1 42  ? -45.915 7.377   23.722  1.00 18.14 ?  37  PRO   C C   1 
ATOM   1885 O  O   . PRO   B 1 42  ? -45.222 6.389   23.667  1.00 19.07 ?  37  PRO   C O   1 
ATOM   1886 C  CB  . PRO   B 1 42  ? -48.316 6.876   24.200  1.00 20.46 ?  37  PRO   C CB  1 
ATOM   1887 C  CG  . PRO   B 1 42  ? -49.466 6.307   23.396  1.00 21.71 ?  37  PRO   C CG  1 
ATOM   1888 C  CD  . PRO   B 1 42  ? -48.788 5.677   22.199  1.00 20.93 ?  37  PRO   C CD  1 
ATOM   1889 N  N   . HIS   B 1 43  ? -45.541 8.544   24.276  1.00 20.08 ?  38  HIS   C N   1 
ATOM   1890 C  CA  . HIS   B 1 43  ? -44.400 8.742   25.204  1.00 19.39 ?  38  HIS   C CA  1 
ATOM   1891 C  C   . HIS   B 1 43  ? -44.832 8.265   26.600  1.00 17.33 ?  38  HIS   C C   1 
ATOM   1892 O  O   . HIS   B 1 43  ? -45.991 8.525   26.973  1.00 18.97 ?  38  HIS   C O   1 
ATOM   1893 C  CB  . HIS   B 1 43  ? -44.021 10.207  25.321  1.00 22.50 ?  38  HIS   C CB  1 
ATOM   1894 C  CG  . HIS   B 1 43  ? -43.703 10.826  24.005  1.00 26.15 ?  38  HIS   C CG  1 
ATOM   1895 N  ND1 . HIS   B 1 43  ? -42.472 10.685  23.435  1.00 30.23 ?  38  HIS   C ND1 1 
ATOM   1896 C  CD2 . HIS   B 1 43  ? -44.435 11.593  23.174  1.00 30.30 ?  38  HIS   C CD2 1 
ATOM   1897 C  CE1 . HIS   B 1 43  ? -42.436 11.348  22.294  1.00 32.10 ?  38  HIS   C CE1 1 
ATOM   1898 N  NE2 . HIS   B 1 43  ? -43.630 11.906  22.105  1.00 33.60 ?  38  HIS   C NE2 1 
ATOM   1899 N  N   . ILE   B 1 44  ? -43.974 7.512   27.266  1.00 18.25 ?  39  ILE   C N   1 
ATOM   1900 C  CA  . ILE   B 1 44  ? -44.169 6.925   28.627  1.00 14.93 ?  39  ILE   C CA  1 
ATOM   1901 C  C   . ILE   B 1 44  ? -42.953 7.253   29.466  1.00 18.48 ?  39  ILE   C C   1 
ATOM   1902 O  O   . ILE   B 1 44  ? -41.861 6.827   29.070  1.00 17.57 ?  39  ILE   C O   1 
ATOM   1903 C  CB  . ILE   B 1 44  ? -44.328 5.391   28.576  1.00 19.26 ?  39  ILE   C CB  1 
ATOM   1904 C  CG1 . ILE   B 1 44  ? -45.379 4.931   27.585  1.00 18.72 ?  39  ILE   C CG1 1 
ATOM   1905 C  CG2 . ILE   B 1 44  ? -44.598 4.832   29.945  1.00 19.48 ?  39  ILE   C CG2 1 
ATOM   1906 C  CD1 . ILE   B 1 44  ? -46.762 5.358   27.897  1.00 20.06 ?  39  ILE   C CD1 1 
ATOM   1907 N  N   . THR   B 1 45  ? -43.149 7.916   30.614  1.00 16.47 ?  40  THR   C N   1 
ATOM   1908 C  CA  . THR   B 1 45  ? -42.036 8.144   31.558  1.00 18.47 ?  40  THR   C CA  1 
ATOM   1909 C  C   . THR   B 1 45  ? -42.520 7.797   32.953  1.00 16.62 ?  40  THR   C C   1 
ATOM   1910 O  O   . THR   B 1 45  ? -43.654 8.139   33.320  1.00 16.77 ?  40  THR   C O   1 
ATOM   1911 C  CB  . THR   B 1 45  ? -41.500 9.585   31.537  1.00 17.57 ?  40  THR   C CB  1 
ATOM   1912 O  OG1 . THR   B 1 45  ? -41.171 9.922   30.173  1.00 18.66 ?  40  THR   C OG1 1 
ATOM   1913 C  CG2 . THR   B 1 45  ? -40.293 9.723   32.444  1.00 18.72 ?  40  THR   C CG2 1 
ATOM   1914 N  N   . HIS   B 1 46  ? -41.679 7.059   33.672  1.00 16.81 ?  41  HIS   C N   1 
ATOM   1915 C  CA  . HIS   B 1 46  ? -41.894 6.758   35.108  1.00 17.34 ?  41  HIS   C CA  1 
ATOM   1916 C  C   . HIS   B 1 46  ? -41.518 7.999   35.922  1.00 15.99 ?  41  HIS   C C   1 
ATOM   1917 O  O   . HIS   B 1 46  ? -40.369 8.411   35.912  1.00 16.24 ?  41  HIS   C O   1 
ATOM   1918 C  CB  . HIS   B 1 46  ? -41.129 5.509   35.551  1.00 17.15 ?  41  HIS   C CB  1 
ATOM   1919 C  CG  . HIS   B 1 46  ? -41.632 4.228   34.951  1.00 23.80 ?  41  HIS   C CG  1 
ATOM   1920 N  ND1 . HIS   B 1 46  ? -42.450 3.371   35.636  1.00 29.00 ?  41  HIS   C ND1 1 
ATOM   1921 C  CD2 . HIS   B 1 46  ? -41.488 3.705   33.724  1.00 28.61 ?  41  HIS   C CD2 1 
ATOM   1922 C  CE1 . HIS   B 1 46  ? -42.756 2.348   34.874  1.00 29.43 ?  41  HIS   C CE1 1 
ATOM   1923 N  NE2 . HIS   B 1 46  ? -42.154 2.510   33.702  1.00 30.37 ?  41  HIS   C NE2 1 
ATOM   1924 N  N   . VAL   B 1 47  ? -42.484 8.588   36.586  1.00 14.53 ?  42  VAL   C N   1 
ATOM   1925 C  CA  . VAL   B 1 47  ? -42.283 9.856   37.328  1.00 15.29 ?  42  VAL   C CA  1 
ATOM   1926 C  C   . VAL   B 1 47  ? -42.908 9.769   38.711  1.00 15.30 ?  42  VAL   C C   1 
ATOM   1927 O  O   . VAL   B 1 47  ? -44.029 9.259   38.852  1.00 14.55 ?  42  VAL   C O   1 
ATOM   1928 C  CB  . VAL   B 1 47  ? -42.830 11.064  36.563  1.00 15.07 ?  42  VAL   C CB  1 
ATOM   1929 C  CG1 . VAL   B 1 47  ? -42.060 11.350  35.287  1.00 17.48 ?  42  VAL   C CG1 1 
ATOM   1930 C  CG2 . VAL   B 1 47  ? -44.323 10.886  36.218  1.00 16.44 ?  42  VAL   C CG2 1 
ATOM   1931 N  N   . PRO   B 1 48  ? -42.306 10.428  39.727  1.00 16.60 ?  43  PRO   C N   1 
ATOM   1932 C  CA  . PRO   B 1 48  ? -42.840 10.510  41.088  1.00 16.66 ?  43  PRO   C CA  1 
ATOM   1933 C  C   . PRO   B 1 48  ? -43.893 11.615  41.175  1.00 17.97 ?  43  PRO   C C   1 
ATOM   1934 O  O   . PRO   B 1 48  ? -43.612 12.769  40.904  1.00 17.78 ?  43  PRO   C O   1 
ATOM   1935 C  CB  . PRO   B 1 48  ? -41.616 10.824  41.978  1.00 18.28 ?  43  PRO   C CB  1 
ATOM   1936 C  CG  . PRO   B 1 48  ? -40.768 11.625  41.046  1.00 17.00 ?  43  PRO   C CG  1 
ATOM   1937 C  CD  . PRO   B 1 48  ? -40.952 11.020  39.665  1.00 16.98 ?  43  PRO   C CD  1 
ATOM   1938 N  N   . ILE   B 1 49  ? -45.138 11.207  41.433  1.00 15.72 ?  44  ILE   C N   1 
ATOM   1939 C  CA  . ILE   B 1 49  ? -46.289 12.121  41.528  1.00 16.27 ?  44  ILE   C CA  1 
ATOM   1940 C  C   . ILE   B 1 49  ? -46.879 12.019  42.928  1.00 15.30 ?  44  ILE   C C   1 
ATOM   1941 O  O   . ILE   B 1 49  ? -47.073 10.906  43.453  1.00 16.70 ?  44  ILE   C O   1 
ATOM   1942 C  CB  . ILE   B 1 49  ? -47.293 11.852  40.415  1.00 18.36 ?  44  ILE   C CB  1 
ATOM   1943 C  CG1 . ILE   B 1 49  ? -46.625 12.068  39.049  1.00 19.89 ?  44  ILE   C CG1 1 
ATOM   1944 C  CG2 . ILE   B 1 49  ? -48.483 12.763  40.636  1.00 18.91 ?  44  ILE   C CG2 1 
ATOM   1945 C  CD1 . ILE   B 1 49  ? -47.498 11.715  37.834  1.00 19.75 ?  44  ILE   C CD1 1 
ATOM   1946 N  N   . ILE   B 1 50  ? -47.150 13.187  43.508  1.00 15.87 ?  45  ILE   C N   1 
ATOM   1947 C  CA  . ILE   B 1 50  ? -47.833 13.294  44.828  1.00 19.14 ?  45  ILE   C CA  1 
ATOM   1948 C  C   . ILE   B 1 50  ? -49.088 14.164  44.729  1.00 17.48 ?  45  ILE   C C   1 
ATOM   1949 O  O   . ILE   B 1 50  ? -49.233 15.030  43.837  1.00 17.29 ?  45  ILE   C O   1 
ATOM   1950 C  CB  . ILE   B 1 50  ? -46.848 13.881  45.862  1.00 20.01 ?  45  ILE   C CB  1 
ATOM   1951 C  CG1 . ILE   B 1 50  ? -46.386 15.275  45.440  1.00 20.25 ?  45  ILE   C CG1 1 
ATOM   1952 C  CG2 . ILE   B 1 50  ? -45.651 12.967  46.110  1.00 18.55 ?  45  ILE   C CG2 1 
ATOM   1953 C  CD1 . ILE   B 1 50  ? -45.708 16.074  46.562  1.00 22.43 ?  45  ILE   C CD1 1 
ATOM   1954 N  N   . VAL   B 1 51  ? -49.955 14.003  45.706  1.00 19.24 ?  46  VAL   C N   1 
ATOM   1955 C  CA  . VAL   B 1 51  ? -51.104 14.927  45.906  1.00 22.53 ?  46  VAL   C CA  1 
ATOM   1956 C  C   . VAL   B 1 51  ? -50.604 16.295  46.421  1.00 22.57 ?  46  VAL   C C   1 
ATOM   1957 O  O   . VAL   B 1 51  ? -49.698 16.346  47.293  1.00 22.60 ?  46  VAL   C O   1 
ATOM   1958 C  CB  . VAL   B 1 51  ? -52.096 14.285  46.892  1.00 25.64 ?  46  VAL   C CB  1 
ATOM   1959 C  CG1 . VAL   B 1 51  ? -53.124 15.285  47.415  1.00 29.97 ?  46  VAL   C CG1 1 
ATOM   1960 C  CG2 . VAL   B 1 51  ? -52.735 13.053  46.279  1.00 28.07 ?  46  VAL   C CG2 1 
ATOM   1961 N  N   . ASP   B 1 52  ? -51.176 17.372  45.883  1.00 24.12 ?  47  ASP   C N   1 
ATOM   1962 C  CA  . ASP   B 1 52  ? -50.977 18.784  46.326  1.00 23.25 ?  47  ASP   C CA  1 
ATOM   1963 C  C   . ASP   B 1 52  ? -50.738 18.844  47.836  1.00 23.87 ?  47  ASP   C C   1 
ATOM   1964 O  O   . ASP   B 1 52  ? -51.623 18.528  48.621  1.00 23.61 ?  47  ASP   C O   1 
ATOM   1965 C  CB  . ASP   B 1 52  ? -52.202 19.620  45.971  1.00 27.85 ?  47  ASP   C CB  1 
ATOM   1966 C  CG  . ASP   B 1 52  ? -52.143 21.073  46.411  1.00 30.55 ?  47  ASP   C CG  1 
ATOM   1967 O  OD1 . ASP   B 1 52  ? -51.136 21.494  47.035  1.00 25.75 ?  47  ASP   C OD1 1 
ATOM   1968 O  OD2 . ASP   B 1 52  ? -53.095 21.774  46.093  1.00 30.63 -1 47  ASP   C OD2 1 
ATOM   1969 N  N   . PRO   B 1 53  ? -49.496 19.119  48.299  1.00 22.94 ?  48  PRO   C N   1 
ATOM   1970 C  CA  . PRO   B 1 53  ? -49.187 19.051  49.727  1.00 26.68 ?  48  PRO   C CA  1 
ATOM   1971 C  C   . PRO   B 1 53  ? -49.819 20.191  50.542  1.00 27.98 ?  48  PRO   C C   1 
ATOM   1972 O  O   . PRO   B 1 53  ? -49.737 20.154  51.767  1.00 31.37 ?  48  PRO   C O   1 
ATOM   1973 C  CB  . PRO   B 1 53  ? -47.653 19.214  49.736  1.00 26.40 ?  48  PRO   C CB  1 
ATOM   1974 C  CG  . PRO   B 1 53  ? -47.377 20.089  48.523  1.00 26.48 ?  48  PRO   C CG  1 
ATOM   1975 C  CD  . PRO   B 1 53  ? -48.310 19.477  47.500  1.00 26.72 ?  48  PRO   C CD  1 
ATOM   1976 N  N   . GLU   B 1 54  ? -50.394 21.183  49.853  1.00 30.25 ?  49  GLU   C N   1 
ATOM   1977 C  CA  . GLU   B 1 54  ? -51.038 22.372  50.483  1.00 32.78 ?  49  GLU   C CA  1 
ATOM   1978 C  C   . GLU   B 1 54  ? -52.493 22.051  50.856  1.00 33.07 ?  49  GLU   C C   1 
ATOM   1979 O  O   . GLU   B 1 54  ? -53.123 22.871  51.513  1.00 32.06 ?  49  GLU   C O   1 
ATOM   1980 C  CB  . GLU   B 1 54  ? -50.949 23.566  49.537  1.00 37.52 ?  49  GLU   C CB  1 
ATOM   1981 C  CG  . GLU   B 1 54  ? -49.534 24.090  49.386  1.00 42.50 ?  49  GLU   C CG  1 
ATOM   1982 C  CD  . GLU   B 1 54  ? -49.191 25.131  50.448  1.00 55.84 ?  49  GLU   C CD  1 
ATOM   1983 O  OE1 . GLU   B 1 54  ? -49.087 24.743  51.634  1.00 54.48 ?  49  GLU   C OE1 1 
ATOM   1984 O  OE2 . GLU   B 1 54  ? -49.075 26.345  50.099  1.00 63.94 -1 49  GLU   C OE2 1 
ATOM   1985 N  N   . LEU   B 1 55  ? -53.022 20.899  50.466  1.00 29.11 ?  50  LEU   C N   1 
ATOM   1986 C  CA  . LEU   B 1 55  ? -54.393 20.485  50.880  1.00 33.71 ?  50  LEU   C CA  1 
ATOM   1987 C  C   . LEU   B 1 55  ? -54.289 20.058  52.338  1.00 38.34 ?  50  LEU   C C   1 
ATOM   1988 O  O   . LEU   B 1 55  ? -53.508 19.136  52.638  1.00 37.34 ?  50  LEU   C O   1 
ATOM   1989 C  CB  . LEU   B 1 55  ? -54.931 19.341  50.013  1.00 31.21 ?  50  LEU   C CB  1 
ATOM   1990 C  CG  . LEU   B 1 55  ? -55.178 19.682  48.545  1.00 31.30 ?  50  LEU   C CG  1 
ATOM   1991 C  CD1 . LEU   B 1 55  ? -55.675 18.436  47.833  1.00 29.25 ?  50  LEU   C CD1 1 
ATOM   1992 C  CD2 . LEU   B 1 55  ? -56.171 20.833  48.394  1.00 34.73 ?  50  LEU   C CD2 1 
ATOM   1993 N  N   . ASP   B 1 56  ? -54.998 20.771  53.201  1.00 47.10 ?  51  ASP   C N   1 
ATOM   1994 C  CA  . ASP   B 1 56  ? -55.222 20.390  54.612  1.00 55.25 ?  51  ASP   C CA  1 
ATOM   1995 C  C   . ASP   B 1 56  ? -56.609 19.741  54.618  1.00 56.00 ?  51  ASP   C C   1 
ATOM   1996 O  O   . ASP   B 1 56  ? -57.460 20.137  53.766  1.00 56.03 ?  51  ASP   C O   1 
ATOM   1997 C  CB  . ASP   B 1 56  ? -55.014 21.598  55.538  1.00 63.02 ?  51  ASP   C CB  1 
ATOM   1998 C  CG  . ASP   B 1 56  ? -53.560 22.060  55.623  1.00 68.62 ?  51  ASP   C CG  1 
ATOM   1999 O  OD1 . ASP   B 1 56  ? -52.886 21.695  56.607  1.00 74.95 ?  51  ASP   C OD1 1 
ATOM   2000 O  OD2 . ASP   B 1 56  ? -53.103 22.785  54.705  1.00 69.98 -1 51  ASP   C OD2 1 
ATOM   2001 N  N   . GLY   B 1 57  ? -56.787 18.735  55.476  1.00 49.90 ?  52  GLY   C N   1 
ATOM   2002 C  CA  . GLY   B 1 57  ? -58.063 18.029  55.679  1.00 43.08 ?  52  GLY   C CA  1 
ATOM   2003 C  C   . GLY   B 1 57  ? -58.079 16.764  54.838  1.00 40.27 ?  52  GLY   C C   1 
ATOM   2004 O  O   . GLY   B 1 57  ? -57.276 16.632  53.911  1.00 34.63 ?  52  GLY   C O   1 
ATOM   2005 N  N   . PRO   B 1 58  ? -58.974 15.803  55.136  1.00 35.89 ?  53  PRO   C N   1 
ATOM   2006 C  CA  . PRO   B 1 58  ? -58.967 14.526  54.428  1.00 36.65 ?  53  PRO   C CA  1 
ATOM   2007 C  C   . PRO   B 1 58  ? -59.184 14.749  52.924  1.00 33.79 ?  53  PRO   C C   1 
ATOM   2008 O  O   . PRO   B 1 58  ? -60.009 15.573  52.531  1.00 31.48 ?  53  PRO   C O   1 
ATOM   2009 C  CB  . PRO   B 1 58  ? -60.098 13.714  55.080  1.00 39.25 ?  53  PRO   C CB  1 
ATOM   2010 C  CG  . PRO   B 1 58  ? -60.364 14.413  56.400  1.00 40.62 ?  53  PRO   C CG  1 
ATOM   2011 C  CD  . PRO   B 1 58  ? -60.023 15.870  56.167  1.00 40.90 ?  53  PRO   C CD  1 
ATOM   2012 N  N   . VAL   B 1 59  ? -58.376 14.074  52.109  1.00 29.59 ?  54  VAL   C N   1 
ATOM   2013 C  CA  . VAL   B 1 59  ? -58.523 14.119  50.629  1.00 26.85 ?  54  VAL   C CA  1 
ATOM   2014 C  C   . VAL   B 1 59  ? -59.268 12.855  50.248  1.00 27.77 ?  54  VAL   C C   1 
ATOM   2015 O  O   . VAL   B 1 59  ? -58.645 11.776  50.261  1.00 28.52 ?  54  VAL   C O   1 
ATOM   2016 C  CB  . VAL   B 1 59  ? -57.174 14.218  49.894  1.00 27.20 ?  54  VAL   C CB  1 
ATOM   2017 C  CG1 . VAL   B 1 59  ? -57.389 14.216  48.397  1.00 27.51 ?  54  VAL   C CG1 1 
ATOM   2018 C  CG2 . VAL   B 1 59  ? -56.383 15.444  50.320  1.00 27.97 ?  54  VAL   C CG2 1 
ATOM   2019 N  N   . ASP   B 1 60  ? -60.560 12.986  49.968  1.00 30.91 ?  55  ASP   C N   1 
ATOM   2020 C  CA  . ASP   B 1 60  ? -61.430 11.813  49.724  1.00 32.36 ?  55  ASP   C CA  1 
ATOM   2021 C  C   . ASP   B 1 60  ? -61.542 11.523  48.234  1.00 28.82 ?  55  ASP   C C   1 
ATOM   2022 O  O   . ASP   B 1 60  ? -61.933 10.393  47.931  1.00 36.25 ?  55  ASP   C O   1 
ATOM   2023 C  CB  . ASP   B 1 60  ? -62.793 12.030  50.376  1.00 37.31 ?  55  ASP   C CB  1 
ATOM   2024 C  CG  . ASP   B 1 60  ? -62.706 11.959  51.892  1.00 44.25 ?  55  ASP   C CG  1 
ATOM   2025 O  OD1 . ASP   B 1 60  ? -61.824 11.227  52.401  1.00 50.67 ?  55  ASP   C OD1 1 
ATOM   2026 O  OD2 . ASP   B 1 60  ? -63.482 12.669  52.553  1.00 53.03 -1 55  ASP   C OD2 1 
ATOM   2027 N  N   . ARG   B 1 61  ? -61.312 12.506  47.360  1.00 24.97 ?  56  ARG   C N   1 
ATOM   2028 C  CA  . ARG   B 1 61  ? -61.571 12.402  45.897  1.00 26.67 ?  56  ARG   C CA  1 
ATOM   2029 C  C   . ARG   B 1 61  ? -60.368 12.969  45.143  1.00 24.59 ?  56  ARG   C C   1 
ATOM   2030 O  O   . ARG   B 1 61  ? -59.880 14.026  45.548  1.00 24.12 ?  56  ARG   C O   1 
ATOM   2031 C  CB  . ARG   B 1 61  ? -62.788 13.227  45.430  1.00 33.75 ?  56  ARG   C CB  1 
ATOM   2032 C  CG  . ARG   B 1 61  ? -64.147 12.576  45.670  1.00 43.49 ?  56  ARG   C CG  1 
ATOM   2033 C  CD  . ARG   B 1 61  ? -65.337 13.528  45.576  1.00 47.85 ?  56  ARG   C CD  1 
ATOM   2034 N  NE  . ARG   B 1 61  ? -65.625 14.141  46.880  1.00 54.19 ?  56  ARG   C NE  1 
ATOM   2035 C  CZ  . ARG   B 1 61  ? -65.344 15.398  47.250  1.00 57.92 ?  56  ARG   C CZ  1 
ATOM   2036 N  NH1 . ARG   B 1 61  ? -65.635 15.794  48.479  1.00 58.82 1  56  ARG   C NH1 1 
ATOM   2037 N  NH2 . ARG   B 1 61  ? -64.782 16.265  46.414  1.00 60.10 ?  56  ARG   C NH2 1 
ATOM   2038 N  N   . LEU   B 1 62  ? -59.990 12.359  44.016  1.00 23.54 ?  57  LEU   C N   1 
ATOM   2039 C  CA  . LEU   B 1 62  ? -58.922 12.882  43.143  1.00 21.20 ?  57  LEU   C CA  1 
ATOM   2040 C  C   . LEU   B 1 62  ? -59.467 13.947  42.200  1.00 22.53 ?  57  LEU   C C   1 
ATOM   2041 O  O   . LEU   B 1 62  ? -58.725 14.868  41.871  1.00 23.70 ?  57  LEU   C O   1 
ATOM   2042 C  CB  . LEU   B 1 62  ? -58.333 11.730  42.335  1.00 23.05 ?  57  LEU   C CB  1 
ATOM   2043 C  CG  . LEU   B 1 62  ? -57.456 10.764  43.115  1.00 25.18 ?  57  LEU   C CG  1 
ATOM   2044 C  CD1 . LEU   B 1 62  ? -57.089 9.577   42.217  1.00 22.01 ?  57  LEU   C CD1 1 
ATOM   2045 C  CD2 . LEU   B 1 62  ? -56.199 11.453  43.661  1.00 24.79 ?  57  LEU   C CD2 1 
ATOM   2046 N  N   . VAL   B 1 63  ? -60.696 13.795  41.685  1.00 22.17 ?  58  VAL   C N   1 
ATOM   2047 C  CA  . VAL   B 1 63  ? -61.219 14.776  40.698  1.00 25.26 ?  58  VAL   C CA  1 
ATOM   2048 C  C   . VAL   B 1 63  ? -61.277 16.143  41.375  1.00 23.79 ?  58  VAL   C C   1 
ATOM   2049 O  O   . VAL   B 1 63  ? -61.745 16.245  42.520  1.00 25.82 ?  58  VAL   C O   1 
ATOM   2050 C  CB  . VAL   B 1 63  ? -62.561 14.355  40.078  1.00 24.40 ?  58  VAL   C CB  1 
ATOM   2051 C  CG1 . VAL   B 1 63  ? -63.174 15.489  39.266  1.00 27.15 ?  58  VAL   C CG1 1 
ATOM   2052 C  CG2 . VAL   B 1 63  ? -62.339 13.132  39.186  1.00 24.44 ?  58  VAL   C CG2 1 
ATOM   2053 N  N   . GLY   B 1 64  ? -60.667 17.124  40.719  1.00 23.68 ?  59  GLY   C N   1 
ATOM   2054 C  CA  . GLY   B 1 64  ? -60.666 18.520  41.164  1.00 25.17 ?  59  GLY   C CA  1 
ATOM   2055 C  C   . GLY   B 1 64  ? -59.400 18.926  41.886  1.00 29.06 ?  59  GLY   C C   1 
ATOM   2056 O  O   . GLY   B 1 64  ? -59.196 20.124  42.077  1.00 35.49 ?  59  GLY   C O   1 
ATOM   2057 N  N   . ILE   B 1 65  ? -58.539 18.000  42.268  1.00 24.59 ?  60  ILE   C N   1 
ATOM   2058 C  CA  . ILE   B 1 65  ? -57.272 18.368  42.947  1.00 25.14 ?  60  ILE   C CA  1 
ATOM   2059 C  C   . ILE   B 1 65  ? -56.140 18.405  41.923  1.00 22.58 ?  60  ILE   C C   1 
ATOM   2060 O  O   . ILE   B 1 65  ? -56.254 17.875  40.768  1.00 21.15 ?  60  ILE   C O   1 
ATOM   2061 C  CB  . ILE   B 1 65  ? -56.973 17.431  44.140  1.00 30.17 ?  60  ILE   C CB  1 
ATOM   2062 C  CG1 . ILE   B 1 65  ? -56.345 16.114  43.656  1.00 31.02 ?  60  ILE   C CG1 1 
ATOM   2063 C  CG2 . ILE   B 1 65  ? -58.229 17.209  44.991  1.00 29.17 ?  60  ILE   C CG2 1 
ATOM   2064 C  CD1 . ILE   B 1 65  ? -55.796 15.215  44.740  1.00 35.02 ?  60  ILE   C CD1 1 
ATOM   2065 N  N   . THR   B 1 66  ? -55.027 18.993  42.347  1.00 22.33 ?  61  THR   C N   1 
ATOM   2066 C  CA  . THR   B 1 66  ? -53.816 19.101  41.526  1.00 23.63 ?  61  THR   C CA  1 
ATOM   2067 C  C   . THR   B 1 66  ? -52.806 18.099  42.072  1.00 21.71 ?  61  THR   C C   1 
ATOM   2068 O  O   . THR   B 1 66  ? -52.605 18.032  43.304  1.00 23.96 ?  61  THR   C O   1 
ATOM   2069 C  CB  . THR   B 1 66  ? -53.290 20.540  41.476  1.00 27.85 ?  61  THR   C CB  1 
ATOM   2070 O  OG1 . THR   B 1 66  ? -54.406 21.320  41.027  1.00 28.91 ?  61  THR   C OG1 1 
ATOM   2071 C  CG2 . THR   B 1 66  ? -52.087 20.678  40.562  1.00 24.97 ?  61  THR   C CG2 1 
ATOM   2072 N  N   . LEU   B 1 67  ? -52.226 17.337  41.159  1.00 19.24 ?  62  LEU   C N   1 
ATOM   2073 C  CA  . LEU   B 1 67  ? -51.045 16.517  41.471  1.00 18.96 ?  62  LEU   C CA  1 
ATOM   2074 C  C   . LEU   B 1 67  ? -49.797 17.271  41.055  1.00 19.14 ?  62  LEU   C C   1 
ATOM   2075 O  O   . LEU   B 1 67  ? -49.885 18.037  40.081  1.00 21.12 ?  62  LEU   C O   1 
ATOM   2076 C  CB  . LEU   B 1 67  ? -51.192 15.168  40.765  1.00 18.59 ?  62  LEU   C CB  1 
ATOM   2077 C  CG  . LEU   B 1 67  ? -52.491 14.423  41.062  1.00 17.23 ?  62  LEU   C CG  1 
ATOM   2078 C  CD1 . LEU   B 1 67  ? -52.497 13.133  40.281  1.00 19.12 ?  62  LEU   C CD1 1 
ATOM   2079 C  CD2 . LEU   B 1 67  ? -52.705 14.136  42.545  1.00 19.23 ?  62  LEU   C CD2 1 
ATOM   2080 N  N   . TRP   B 1 68  ? -48.694 17.015  41.780  1.00 17.89 ?  63  TRP   C N   1 
ATOM   2081 C  CA  . TRP   B 1 68  ? -47.329 17.586  41.625  1.00 18.13 ?  63  TRP   C CA  1 
ATOM   2082 C  C   . TRP   B 1 68  ? -46.384 16.471  41.215  1.00 16.94 ?  63  TRP   C C   1 
ATOM   2083 O  O   . TRP   B 1 68  ? -46.508 15.336  41.820  1.00 16.09 ?  63  TRP   C O   1 
ATOM   2084 C  CB  . TRP   B 1 68  ? -46.818 18.210  42.922  1.00 19.11 ?  63  TRP   C CB  1 
ATOM   2085 C  CG  . TRP   B 1 68  ? -47.522 19.450  43.344  1.00 18.66 ?  63  TRP   C CG  1 
ATOM   2086 C  CD1 . TRP   B 1 68  ? -48.787 19.882  43.068  1.00 21.00 ?  63  TRP   C CD1 1 
ATOM   2087 C  CD2 . TRP   B 1 68  ? -46.972 20.370  44.266  1.00 20.50 ?  63  TRP   C CD2 1 
ATOM   2088 N  NE1 . TRP   B 1 68  ? -49.021 21.083  43.700  1.00 20.52 ?  63  TRP   C NE1 1 
ATOM   2089 C  CE2 . TRP   B 1 68  ? -47.922 21.395  44.448  1.00 21.01 ?  63  TRP   C CE2 1 
ATOM   2090 C  CE3 . TRP   B 1 68  ? -45.752 20.416  44.941  1.00 19.48 ?  63  TRP   C CE3 1 
ATOM   2091 C  CZ2 . TRP   B 1 68  ? -47.689 22.467  45.298  1.00 21.46 ?  63  TRP   C CZ2 1 
ATOM   2092 C  CZ3 . TRP   B 1 68  ? -45.525 21.502  45.771  1.00 20.79 ?  63  TRP   C CZ3 1 
ATOM   2093 C  CH2 . TRP   B 1 68  ? -46.474 22.507  45.932  1.00 23.41 ?  63  TRP   C CH2 1 
ATOM   2094 N  N   . GLY   B 1 69  ? -45.592 16.683  40.153  1.00 16.65 ?  64  GLY   C N   1 
ATOM   2095 C  CA  . GLY   B 1 69  ? -44.617 15.721  39.673  1.00 17.36 ?  64  GLY   C CA  1 
ATOM   2096 C  C   . GLY   B 1 69  ? -43.364 16.393  39.163  1.00 18.95 ?  64  GLY   C C   1 
ATOM   2097 O  O   . GLY   B 1 69  ? -43.322 17.628  39.014  1.00 16.97 ?  64  GLY   C O   1 
ATOM   2098 N  N   . HIS   B 1 70  ? -42.365 15.600  38.857  1.00 17.10 ?  65  HIS   C N   1 
ATOM   2099 C  CA  . HIS   B 1 70  ? -41.158 16.088  38.141  1.00 17.83 ?  65  HIS   C CA  1 
ATOM   2100 C  C   . HIS   B 1 70  ? -40.619 15.000  37.249  1.00 15.93 ?  65  HIS   C C   1 
ATOM   2101 O  O   . HIS   B 1 70  ? -40.837 13.764  37.509  1.00 17.08 ?  65  HIS   C O   1 
ATOM   2102 C  CB  . HIS   B 1 70  ? -40.097 16.710  39.067  1.00 18.36 ?  65  HIS   C CB  1 
ATOM   2103 C  CG  . HIS   B 1 70  ? -39.275 15.760  39.862  1.00 17.17 ?  65  HIS   C CG  1 
ATOM   2104 N  ND1 . HIS   B 1 70  ? -39.769 15.203  41.014  1.00 15.68 ?  65  HIS   C ND1 1 
ATOM   2105 C  CD2 . HIS   B 1 70  ? -37.980 15.342  39.740  1.00 17.14 ?  65  HIS   C CD2 1 
ATOM   2106 C  CE1 . HIS   B 1 70  ? -38.841 14.438  41.562  1.00 18.61 ?  65  HIS   C CE1 1 
ATOM   2107 N  NE2 . HIS   B 1 70  ? -37.754 14.455  40.776  1.00 16.20 ?  65  HIS   C NE2 1 
ATOM   2108 N  N   . MET   B 1 71  ? -39.856 15.435  36.265  1.00 17.93 ?  66  MET   C N   1 
ATOM   2109 C  CA  . MET   B 1 71  ? -39.105 14.551  35.387  1.00 18.02 ?  66  MET   C CA  1 
ATOM   2110 C  C   . MET   B 1 71  ? -37.819 15.278  35.029  1.00 17.79 ?  66  MET   C C   1 
ATOM   2111 O  O   . MET   B 1 71  ? -37.596 16.403  35.516  1.00 16.98 ?  66  MET   C O   1 
ATOM   2112 C  CB  . MET   B 1 71  ? -39.905 14.174  34.139  1.00 19.30 ?  66  MET   C CB  1 
ATOM   2113 C  CG  . MET   B 1 71  ? -40.132 15.340  33.154  1.00 20.46 ?  66  MET   C CG  1 
ATOM   2114 S  SD  . MET   B 1 71  ? -40.834 14.758  31.558  1.00 29.49 ?  66  MET   C SD  1 
ATOM   2115 C  CE  . MET   B 1 71  ? -42.480 14.864  32.198  1.00 24.84 ?  66  MET   C CE  1 
ATOM   2116 N  N   . ASN   B 1 72  ? -37.046 14.656  34.162  1.00 19.07 ?  67  ASN   C N   1 
ATOM   2117 C  CA  . ASN   B 1 72  ? -35.763 15.199  33.690  1.00 18.19 ?  67  ASN   C CA  1 
ATOM   2118 C  C   . ASN   B 1 72  ? -36.106 16.157  32.534  1.00 18.29 ?  67  ASN   C C   1 
ATOM   2119 O  O   . ASN   B 1 72  ? -36.677 15.699  31.550  1.00 18.20 ?  67  ASN   C O   1 
ATOM   2120 C  CB  . ASN   B 1 72  ? -34.847 14.097  33.231  1.00 17.34 ?  67  ASN   C CB  1 
ATOM   2121 C  CG  . ASN   B 1 72  ? -33.460 14.623  32.921  1.00 20.58 ?  67  ASN   C CG  1 
ATOM   2122 O  OD1 . ASN   B 1 72  ? -33.295 15.824  32.735  1.00 21.42 ?  67  ASN   C OD1 1 
ATOM   2123 N  ND2 . ASN   B 1 72  ? -32.472 13.739  32.915  1.00 22.63 ?  67  ASN   C ND2 1 
ATOM   2124 N  N   . ARG   B 1 73  ? -35.741 17.422  32.621  1.00 18.14 ?  68  ARG   C N   1 
ATOM   2125 C  CA  . ARG   B 1 73  ? -35.931 18.369  31.481  1.00 21.34 ?  68  ARG   C CA  1 
ATOM   2126 C  C   . ARG   B 1 73  ? -35.237 17.898  30.210  1.00 23.05 ?  68  ARG   C C   1 
ATOM   2127 O  O   . ARG   B 1 73  ? -35.626 18.330  29.173  1.00 26.23 ?  68  ARG   C O   1 
ATOM   2128 C  CB  . ARG   B 1 73  ? -35.363 19.734  31.842  1.00 24.77 ?  68  ARG   C CB  1 
ATOM   2129 C  CG  . ARG   B 1 73  ? -36.413 20.644  32.398  1.00 25.04 ?  68  ARG   C CG  1 
ATOM   2130 C  CD  . ARG   B 1 73  ? -35.863 22.035  32.588  1.00 23.04 ?  68  ARG   C CD  1 
ATOM   2131 N  NE  . ARG   B 1 73  ? -36.814 22.552  33.527  1.00 18.93 ?  68  ARG   C NE  1 
ATOM   2132 C  CZ  . ARG   B 1 73  ? -37.648 23.536  33.275  1.00 18.23 ?  68  ARG   C CZ  1 
ATOM   2133 N  NH1 . ARG   B 1 73  ? -37.676 24.101  32.072  1.00 22.22 1  68  ARG   C NH1 1 
ATOM   2134 N  NH2 . ARG   B 1 73  ? -38.464 23.946  34.216  1.00 20.08 ?  68  ARG   C NH2 1 
ATOM   2135 N  N   . ALA   B 1 74  ? -34.215 17.040  30.308  1.00 22.57 ?  69  ALA   C N   1 
ATOM   2136 C  CA  . ALA   B 1 74  ? -33.429 16.535  29.169  1.00 24.48 ?  69  ALA   C CA  1 
ATOM   2137 C  C   . ALA   B 1 74  ? -34.116 15.305  28.561  1.00 21.71 ?  69  ALA   C C   1 
ATOM   2138 O  O   . ALA   B 1 74  ? -33.743 14.853  27.449  1.00 24.63 ?  69  ALA   C O   1 
ATOM   2139 C  CB  . ALA   B 1 74  ? -32.028 16.244  29.631  1.00 25.00 ?  69  ALA   C CB  1 
ATOM   2140 N  N   . ASN   B 1 75  ? -35.103 14.737  29.242  1.00 20.41 ?  70  ASN   C N   1 
ATOM   2141 C  CA  . ASN   B 1 75  ? -35.969 13.671  28.681  1.00 20.83 ?  70  ASN   C CA  1 
ATOM   2142 C  C   . ASN   B 1 75  ? -36.750 14.285  27.514  1.00 20.55 ?  70  ASN   C C   1 
ATOM   2143 O  O   . ASN   B 1 75  ? -37.500 15.246  27.691  1.00 20.42 ?  70  ASN   C O   1 
ATOM   2144 C  CB  . ASN   B 1 75  ? -36.838 13.090  29.799  1.00 20.05 ?  70  ASN   C CB  1 
ATOM   2145 C  CG  . ASN   B 1 75  ? -37.758 11.981  29.363  1.00 20.71 ?  70  ASN   C CG  1 
ATOM   2146 O  OD1 . ASN   B 1 75  ? -38.087 11.851  28.168  1.00 17.23 ?  70  ASN   C OD1 1 
ATOM   2147 N  ND2 . ASN   B 1 75  ? -38.238 11.261  30.369  1.00 19.61 ?  70  ASN   C ND2 1 
ATOM   2148 N  N   . PRO   B 1 76  ? -36.679 13.695  26.295  1.00 19.90 ?  71  PRO   C N   1 
ATOM   2149 C  CA  . PRO   B 1 76  ? -37.434 14.246  25.164  1.00 21.32 ?  71  PRO   C CA  1 
ATOM   2150 C  C   . PRO   B 1 76  ? -38.951 14.315  25.393  1.00 19.19 ?  71  PRO   C C   1 
ATOM   2151 O  O   . PRO   B 1 76  ? -39.624 15.070  24.703  1.00 20.24 ?  71  PRO   C O   1 
ATOM   2152 C  CB  . PRO   B 1 76  ? -37.074 13.255  24.040  1.00 22.03 ?  71  PRO   C CB  1 
ATOM   2153 C  CG  . PRO   B 1 76  ? -35.693 12.807  24.399  1.00 24.08 ?  71  PRO   C CG  1 
ATOM   2154 C  CD  . PRO   B 1 76  ? -35.828 12.554  25.882  1.00 21.33 ?  71  PRO   C CD  1 
ATOM   2155 N  N   . HIS   B 1 77  ? -39.472 13.581  26.375  1.00 17.97 ?  72  HIS   C N   1 
ATOM   2156 C  CA  . HIS   B 1 77  ? -40.918 13.632  26.724  1.00 17.30 ?  72  HIS   C CA  1 
ATOM   2157 C  C   . HIS   B 1 77  ? -41.240 15.063  27.192  1.00 17.43 ?  72  HIS   C C   1 
ATOM   2158 O  O   . HIS   B 1 77  ? -42.300 15.560  26.941  1.00 17.73 ?  72  HIS   C O   1 
ATOM   2159 C  CB  . HIS   B 1 77  ? -41.183 12.557  27.762  1.00 16.88 ?  72  HIS   C CB  1 
ATOM   2160 C  CG  . HIS   B 1 77  ? -42.629 12.282  27.987  1.00 16.19 ?  72  HIS   C CG  1 
ATOM   2161 N  ND1 . HIS   B 1 77  ? -43.026 11.290  28.812  1.00 16.37 ?  72  HIS   C ND1 1 
ATOM   2162 C  CD2 . HIS   B 1 77  ? -43.742 12.841  27.484  1.00 19.23 ?  72  HIS   C CD2 1 
ATOM   2163 C  CE1 . HIS   B 1 77  ? -44.351 11.213  28.822  1.00 18.29 ?  72  HIS   C CE1 1 
ATOM   2164 N  NE2 . HIS   B 1 77  ? -44.822 12.230  28.066  1.00 18.07 ?  72  HIS   C NE2 1 
ATOM   2165 N  N   . TRP   B 1 78  ? -40.338 15.699  27.887  1.00 17.16 ?  73  TRP   C N   1 
ATOM   2166 C  CA  . TRP   B 1 78  ? -40.588 17.083  28.399  1.00 18.38 ?  73  TRP   C CA  1 
ATOM   2167 C  C   . TRP   B 1 78  ? -40.872 18.035  27.219  1.00 19.28 ?  73  TRP   C C   1 
ATOM   2168 O  O   . TRP   B 1 78  ? -41.944 18.622  27.177  1.00 20.61 ?  73  TRP   C O   1 
ATOM   2169 C  CB  . TRP   B 1 78  ? -39.434 17.521  29.280  1.00 20.67 ?  73  TRP   C CB  1 
ATOM   2170 C  CG  . TRP   B 1 78  ? -39.528 18.946  29.729  1.00 19.70 ?  73  TRP   C CG  1 
ATOM   2171 C  CD1 . TRP   B 1 78  ? -38.982 20.035  29.120  1.00 20.77 ?  73  TRP   C CD1 1 
ATOM   2172 C  CD2 . TRP   B 1 78  ? -40.225 19.420  30.885  1.00 19.15 ?  73  TRP   C CD2 1 
ATOM   2173 N  NE1 . TRP   B 1 78  ? -39.250 21.153  29.852  1.00 21.54 ?  73  TRP   C NE1 1 
ATOM   2174 C  CE2 . TRP   B 1 78  ? -40.028 20.818  30.930  1.00 20.36 ?  73  TRP   C CE2 1 
ATOM   2175 C  CE3 . TRP   B 1 78  ? -41.017 18.818  31.868  1.00 19.57 ?  73  TRP   C CE3 1 
ATOM   2176 C  CZ2 . TRP   B 1 78  ? -40.559 21.603  31.951  1.00 20.40 ?  73  TRP   C CZ2 1 
ATOM   2177 C  CZ3 . TRP   B 1 78  ? -41.548 19.602  32.875  1.00 19.16 ?  73  TRP   C CZ3 1 
ATOM   2178 C  CH2 . TRP   B 1 78  ? -41.282 20.976  32.926  1.00 18.90 ?  73  TRP   C CH2 1 
ATOM   2179 N  N   . ALA   B 1 79  ? -40.033 18.033  26.197  1.00 20.63 ?  74  ALA   C N   1 
ATOM   2180 C  CA  . ALA   B 1 79  ? -40.255 18.859  24.986  1.00 22.00 ?  74  ALA   C CA  1 
ATOM   2181 C  C   . ALA   B 1 79  ? -41.576 18.467  24.301  1.00 26.46 ?  74  ALA   C C   1 
ATOM   2182 O  O   . ALA   B 1 79  ? -42.264 19.388  23.805  1.00 26.20 ?  74  ALA   C O   1 
ATOM   2183 C  CB  . ALA   B 1 79  ? -39.067 18.748  24.089  1.00 22.93 ?  74  ALA   C CB  1 
ATOM   2184 N  N   . ALA   B 1 80  ? -41.932 17.169  24.283  1.00 23.53 ?  75  ALA   C N   1 
ATOM   2185 C  CA  . ALA   B 1 80  ? -43.051 16.647  23.507  1.00 26.30 ?  75  ALA   C CA  1 
ATOM   2186 C  C   . ALA   B 1 80  ? -44.333 17.089  24.204  1.00 28.79 ?  75  ALA   C C   1 
ATOM   2187 O  O   . ALA   B 1 80  ? -45.359 17.220  23.540  1.00 33.48 ?  75  ALA   C O   1 
ATOM   2188 C  CB  . ALA   B 1 80  ? -42.929 15.150  23.370  1.00 30.08 ?  75  ALA   C CB  1 
ATOM   2189 N  N   . LEU   B 1 81  ? -44.290 17.396  25.493  1.00 27.23 ?  76  LEU   C N   1 
ATOM   2190 C  CA  . LEU   B 1 81  ? -45.553 17.736  26.186  1.00 28.19 ?  76  LEU   C CA  1 
ATOM   2191 C  C   . LEU   B 1 81  ? -46.086 19.056  25.625  1.00 40.25 ?  76  LEU   C C   1 
ATOM   2192 O  O   . LEU   B 1 81  ? -47.347 19.179  25.465  1.00 41.96 ?  76  LEU   C O   1 
ATOM   2193 C  CB  . LEU   B 1 81  ? -45.312 17.763  27.683  1.00 27.53 ?  76  LEU   C CB  1 
ATOM   2194 C  CG  . LEU   B 1 81  ? -45.126 16.373  28.288  1.00 26.47 ?  76  LEU   C CG  1 
ATOM   2195 C  CD1 . LEU   B 1 81  ? -44.516 16.447  29.690  1.00 27.35 ?  76  LEU   C CD1 1 
ATOM   2196 C  CD2 . LEU   B 1 81  ? -46.461 15.677  28.311  1.00 24.75 ?  76  LEU   C CD2 1 
ATOM   2197 N  N   . GLY   B 1 82  ? -45.182 19.955  25.226  1.00 43.97 ?  77  GLY   C N   1 
ATOM   2198 C  CA  . GLY   B 1 82  ? -45.599 21.293  24.790  1.00 50.37 ?  77  GLY   C CA  1 
ATOM   2199 C  C   . GLY   B 1 82  ? -46.296 21.947  25.965  1.00 57.18 ?  77  GLY   C C   1 
ATOM   2200 O  O   . GLY   B 1 82  ? -45.989 21.522  27.123  1.00 56.81 ?  77  GLY   C O   1 
ATOM   2201 N  N   . GLY   B 1 83  ? -47.262 22.833  25.700  1.00 57.98 ?  78  GLY   C N   1 
ATOM   2202 C  CA  . GLY   B 1 83  ? -47.826 23.730  26.725  1.00 54.85 ?  78  GLY   C CA  1 
ATOM   2203 C  C   . GLY   B 1 83  ? -49.004 23.108  27.450  1.00 52.91 ?  78  GLY   C C   1 
ATOM   2204 O  O   . GLY   B 1 83  ? -49.062 23.198  28.686  1.00 58.84 ?  78  GLY   C O   1 
ATOM   2205 N  N   . ALA   B 1 84  ? -49.947 22.538  26.708  1.00 53.55 ?  79  ALA   C N   1 
ATOM   2206 C  CA  . ALA   B 1 84  ? -51.309 22.232  27.200  1.00 54.01 ?  79  ALA   C CA  1 
ATOM   2207 C  C   . ALA   B 1 84  ? -51.660 20.763  26.924  1.00 45.93 ?  79  ALA   C C   1 
ATOM   2208 O  O   . ALA   B 1 84  ? -52.788 20.499  26.455  1.00 46.60 ?  79  ALA   C O   1 
ATOM   2209 C  CB  . ALA   B 1 84  ? -52.278 23.178  26.539  1.00 55.90 ?  79  ALA   C CB  1 
ATOM   2210 N  N   . ALA   B 1 85  ? -50.739 19.845  27.237  1.00 42.66 ?  80  ALA   C N   1 
ATOM   2211 C  CA  . ALA   B 1 85  ? -50.847 18.411  26.865  1.00 36.46 ?  80  ALA   C CA  1 
ATOM   2212 C  C   . ALA   B 1 85  ? -51.924 17.739  27.721  1.00 33.01 ?  80  ALA   C C   1 
ATOM   2213 O  O   . ALA   B 1 85  ? -51.911 17.879  28.977  1.00 29.50 ?  80  ALA   C O   1 
ATOM   2214 C  CB  . ALA   B 1 85  ? -49.523 17.706  26.989  1.00 36.86 ?  80  ALA   C CB  1 
ATOM   2215 N  N   . ASN   B 1 86  ? -52.855 17.063  27.059  1.00 27.68 ?  81  ASN   C N   1 
ATOM   2216 C  CA  . ASN   B 1 86  ? -53.796 16.131  27.736  1.00 27.93 ?  81  ASN   C CA  1 
ATOM   2217 C  C   . ASN   B 1 86  ? -53.062 14.833  28.049  1.00 24.30 ?  81  ASN   C C   1 
ATOM   2218 O  O   . ASN   B 1 86  ? -52.579 14.183  27.097  1.00 23.83 ?  81  ASN   C O   1 
ATOM   2219 C  CB  . ASN   B 1 86  ? -55.006 15.816  26.889  1.00 29.54 ?  81  ASN   C CB  1 
ATOM   2220 C  CG  . ASN   B 1 86  ? -55.742 17.089  26.573  1.00 31.76 ?  81  ASN   C CG  1 
ATOM   2221 O  OD1 . ASN   B 1 86  ? -55.948 17.888  27.473  1.00 34.88 ?  81  ASN   C OD1 1 
ATOM   2222 N  ND2 . ASN   B 1 86  ? -56.119 17.274  25.325  1.00 36.26 ?  81  ASN   C ND2 1 
ATOM   2223 N  N   . VAL   B 1 87  ? -52.937 14.531  29.333  1.00 20.10 ?  82  VAL   C N   1 
ATOM   2224 C  CA  . VAL   B 1 87  ? -52.085 13.395  29.745  1.00 18.95 ?  82  VAL   C CA  1 
ATOM   2225 C  C   . VAL   B 1 87  ? -52.881 12.411  30.580  1.00 16.53 ?  82  VAL   C C   1 
ATOM   2226 O  O   . VAL   B 1 87  ? -53.958 12.731  31.084  1.00 17.68 ?  82  VAL   C O   1 
ATOM   2227 C  CB  . VAL   B 1 87  ? -50.803 13.832  30.460  1.00 19.17 ?  82  VAL   C CB  1 
ATOM   2228 C  CG1 . VAL   B 1 87  ? -50.017 14.811  29.608  1.00 22.82 ?  82  VAL   C CG1 1 
ATOM   2229 C  CG2 . VAL   B 1 87  ? -51.085 14.401  31.846  1.00 19.31 ?  82  VAL   C CG2 1 
ATOM   2230 N  N   . VAL   B 1 88  ? -52.352 11.198  30.651  1.00 16.49 ?  83  VAL   C N   1 
ATOM   2231 C  CA  . VAL   B 1 88  ? -52.810 10.212  31.658  1.00 15.85 ?  83  VAL   C CA  1 
ATOM   2232 C  C   . VAL   B 1 88  ? -51.640 9.830   32.544  1.00 16.69 ?  83  VAL   C C   1 
ATOM   2233 O  O   . VAL   B 1 88  ? -50.504 9.668   32.029  1.00 18.01 ?  83  VAL   C O   1 
ATOM   2234 C  CB  . VAL   B 1 88  ? -53.477 8.975   31.029  1.00 16.72 ?  83  VAL   C CB  1 
ATOM   2235 C  CG1 . VAL   B 1 88  ? -52.607 8.337   29.960  1.00 19.75 ?  83  VAL   C CG1 1 
ATOM   2236 C  CG2 . VAL   B 1 88  ? -53.847 7.965   32.100  1.00 17.36 ?  83  VAL   C CG2 1 
ATOM   2237 N  N   . ALA   B 1 89  ? -51.904 9.665   33.833  1.00 16.50 ?  84  ALA   C N   1 
ATOM   2238 C  CA  . ALA   B 1 89  ? -50.872 9.146   34.765  1.00 15.88 ?  84  ALA   C CA  1 
ATOM   2239 C  C   . ALA   B 1 89  ? -51.470 7.923   35.426  1.00 16.87 ?  84  ALA   C C   1 
ATOM   2240 O  O   . ALA   B 1 89  ? -52.622 8.006   35.931  1.00 16.86 ?  84  ALA   C O   1 
ATOM   2241 C  CB  . ALA   B 1 89  ? -50.444 10.147  35.803  1.00 16.54 ?  84  ALA   C CB  1 
ATOM   2242 N  N   . THR   B 1 90  ? -50.757 6.817   35.306  1.00 15.87 ?  85  THR   C N   1 
ATOM   2243 C  CA  . THR   B 1 90  ? -51.231 5.500   35.759  1.00 17.04 ?  85  THR   C CA  1 
ATOM   2244 C  C   . THR   B 1 90  ? -50.405 5.080   36.972  1.00 16.73 ?  85  THR   C C   1 
ATOM   2245 O  O   . THR   B 1 90  ? -49.109 5.050   36.929  1.00 18.84 ?  85  THR   C O   1 
ATOM   2246 C  CB  . THR   B 1 90  ? -51.197 4.436   34.667  1.00 17.49 ?  85  THR   C CB  1 
ATOM   2247 O  OG1 . THR   B 1 90  ? -51.948 4.943   33.565  1.00 18.98 ?  85  THR   C OG1 1 
ATOM   2248 C  CG2 . THR   B 1 90  ? -51.750 3.119   35.185  1.00 18.15 ?  85  THR   C CG2 1 
ATOM   2249 N  N   . PHE   B 1 91  ? -51.127 4.793   38.028  1.00 16.13 ?  86  PHE   C N   1 
ATOM   2250 C  CA  . PHE   B 1 91  ? -50.584 4.284   39.305  1.00 17.08 ?  86  PHE   C CA  1 
ATOM   2251 C  C   . PHE   B 1 91  ? -51.021 2.830   39.438  1.00 20.32 ?  86  PHE   C C   1 
ATOM   2252 O  O   . PHE   B 1 91  ? -52.216 2.500   39.342  1.00 20.30 ?  86  PHE   C O   1 
ATOM   2253 C  CB  . PHE   B 1 91  ? -51.069 5.105   40.492  1.00 16.94 ?  86  PHE   C CB  1 
ATOM   2254 C  CG  . PHE   B 1 91  ? -50.809 6.596   40.385  1.00 15.99 ?  86  PHE   C CG  1 
ATOM   2255 C  CD1 . PHE   B 1 91  ? -51.600 7.386   39.575  1.00 14.42 ?  86  PHE   C CD1 1 
ATOM   2256 C  CD2 . PHE   B 1 91  ? -49.798 7.237   41.114  1.00 15.84 ?  86  PHE   C CD2 1 
ATOM   2257 C  CE1 . PHE   B 1 91  ? -51.414 8.743   39.503  1.00 14.93 ?  86  PHE   C CE1 1 
ATOM   2258 C  CE2 . PHE   B 1 91  ? -49.650 8.609   41.068  1.00 16.23 ?  86  PHE   C CE2 1 
ATOM   2259 C  CZ  . PHE   B 1 91  ? -50.363 9.349   40.174  1.00 16.04 ?  86  PHE   C CZ  1 
ATOM   2260 N  N   . ALA   B 1 92  ? -50.071 1.985   39.744  1.00 17.77 ?  87  ALA   C N   1 
ATOM   2261 C  CA  . ALA   B 1 92  ? -50.273 0.532   39.807  1.00 19.45 ?  87  ALA   C CA  1 
ATOM   2262 C  C   . ALA   B 1 92  ? -49.988 0.048   41.207  1.00 18.90 ?  87  ALA   C C   1 
ATOM   2263 O  O   . ALA   B 1 92  ? -48.824 0.159   41.637  1.00 17.84 ?  87  ALA   C O   1 
ATOM   2264 C  CB  . ALA   B 1 92  ? -49.383 -0.151  38.801  1.00 21.85 ?  87  ALA   C CB  1 
ATOM   2265 N  N   . GLY   B 1 93  ? -50.978 -0.538  41.854  1.00 17.35 ?  88  GLY   C N   1 
ATOM   2266 C  CA  . GLY   B 1 93  ? -50.812 -1.155  43.169  1.00 17.99 ?  88  GLY   C CA  1 
ATOM   2267 C  C   . GLY   B 1 93  ? -50.591 -2.672  43.204  1.00 17.47 ?  88  GLY   C C   1 
ATOM   2268 O  O   . GLY   B 1 93  ? -50.079 -3.325  42.296  1.00 15.59 ?  88  GLY   C O   1 
ATOM   2269 N  N   . PRO   B 1 94  ? -50.927 -3.279  44.366  1.00 17.50 ?  89  PRO   C N   1 
ATOM   2270 C  CA  . PRO   B 1 94  ? -50.810 -4.720  44.581  1.00 18.68 ?  89  PRO   C CA  1 
ATOM   2271 C  C   . PRO   B 1 94  ? -51.461 -5.493  43.422  1.00 18.88 ?  89  PRO   C C   1 
ATOM   2272 O  O   . PRO   B 1 94  ? -52.520 -5.095  42.885  1.00 18.15 ?  89  PRO   C O   1 
ATOM   2273 C  CB  . PRO   B 1 94  ? -51.591 -4.931  45.886  1.00 19.78 ?  89  PRO   C CB  1 
ATOM   2274 C  CG  . PRO   B 1 94  ? -51.384 -3.628  46.629  1.00 19.62 ?  89  PRO   C CG  1 
ATOM   2275 C  CD  . PRO   B 1 94  ? -51.462 -2.576  45.547  1.00 18.61 ?  89  PRO   C CD  1 
ATOM   2276 N  N   . ASN   B 1 95  ? -50.877 -6.646  43.131  1.00 19.23 ?  90  ASN   C N   1 
ATOM   2277 C  CA  . ASN   B 1 95  ? -51.360 -7.505  42.033  1.00 17.36 ?  90  ASN   C CA  1 
ATOM   2278 C  C   . ASN   B 1 95  ? -50.866 -8.910  42.260  1.00 18.31 ?  90  ASN   C C   1 
ATOM   2279 O  O   . ASN   B 1 95  ? -49.767 -9.107  42.864  1.00 16.55 ?  90  ASN   C O   1 
ATOM   2280 C  CB  . ASN   B 1 95  ? -50.964 -6.957  40.662  1.00 19.41 ?  90  ASN   C CB  1 
ATOM   2281 C  CG  . ASN   B 1 95  ? -49.467 -7.042  40.444  1.00 20.37 ?  90  ASN   C CG  1 
ATOM   2282 O  OD1 . ASN   B 1 95  ? -48.987 -8.024  39.898  1.00 19.91 ?  90  ASN   C OD1 1 
ATOM   2283 N  ND2 . ASN   B 1 95  ? -48.764 -6.014  40.870  1.00 21.45 ?  90  ASN   C ND2 1 
ATOM   2284 N  N   . ALA   B 1 96  ? -51.573 -9.867  41.677  1.00 16.48 ?  91  ALA   C N   1 
ATOM   2285 C  CA  . ALA   B 1 96  ? -51.190 -11.288 41.751  1.00 14.81 ?  91  ALA   C CA  1 
ATOM   2286 C  C   . ALA   B 1 96  ? -51.931 -12.128 40.746  1.00 17.10 ?  91  ALA   C C   1 
ATOM   2287 O  O   . ALA   B 1 96  ? -53.173 -11.985 40.615  1.00 15.96 ?  91  ALA   C O   1 
ATOM   2288 C  CB  . ALA   B 1 96  ? -51.360 -11.820 43.129  1.00 16.53 ?  91  ALA   C CB  1 
ATOM   2289 N  N   . TYR   B 1 97  ? -51.208 -13.079 40.182  1.00 17.60 ?  92  TYR   C N   1 
ATOM   2290 C  CA  . TYR   B 1 97  ? -51.772 -14.151 39.336  1.00 18.16 ?  92  TYR   C CA  1 
ATOM   2291 C  C   . TYR   B 1 97  ? -52.719 -15.028 40.140  1.00 17.54 ?  92  TYR   C C   1 
ATOM   2292 O  O   . TYR   B 1 97  ? -52.408 -15.388 41.276  1.00 18.25 ?  92  TYR   C O   1 
ATOM   2293 C  CB  . TYR   B 1 97  ? -50.649 -14.955 38.703  1.00 16.59 ?  92  TYR   C CB  1 
ATOM   2294 C  CG  . TYR   B 1 97  ? -51.198 -16.066 37.843  1.00 16.49 ?  92  TYR   C CG  1 
ATOM   2295 C  CD1 . TYR   B 1 97  ? -51.669 -15.843 36.565  1.00 17.23 ?  92  TYR   C CD1 1 
ATOM   2296 C  CD2 . TYR   B 1 97  ? -51.216 -17.363 38.317  1.00 18.15 ?  92  TYR   C CD2 1 
ATOM   2297 C  CE1 . TYR   B 1 97  ? -52.139 -16.878 35.782  1.00 17.92 ?  92  TYR   C CE1 1 
ATOM   2298 C  CE2 . TYR   B 1 97  ? -51.676 -18.420 37.547  1.00 17.18 ?  92  TYR   C CE2 1 
ATOM   2299 C  CZ  . TYR   B 1 97  ? -52.126 -18.177 36.266  1.00 17.44 ?  92  TYR   C CZ  1 
ATOM   2300 O  OH  . TYR   B 1 97  ? -52.519 -19.210 35.479  1.00 17.82 ?  92  TYR   C OH  1 
ATOM   2301 N  N   . VAL   B 1 98  ? -53.915 -15.258 39.584  1.00 17.61 ?  93  VAL   C N   1 
ATOM   2302 C  CA  . VAL   B 1 98  ? -54.959 -16.165 40.143  1.00 16.60 ?  93  VAL   C CA  1 
ATOM   2303 C  C   . VAL   B 1 98  ? -54.967 -17.498 39.373  1.00 16.61 ?  93  VAL   C C   1 
ATOM   2304 O  O   . VAL   B 1 98  ? -55.497 -17.543 38.249  1.00 17.75 ?  93  VAL   C O   1 
ATOM   2305 C  CB  . VAL   B 1 98  ? -56.337 -15.524 40.110  1.00 16.51 ?  93  VAL   C CB  1 
ATOM   2306 C  CG1 . VAL   B 1 98  ? -57.366 -16.447 40.767  1.00 17.47 ?  93  VAL   C CG1 1 
ATOM   2307 C  CG2 . VAL   B 1 98  ? -56.300 -14.145 40.786  1.00 18.26 ?  93  VAL   C CG2 1 
ATOM   2308 N  N   . SER   B 1 99  ? -54.404 -18.526 39.996  1.00 16.20 ?  94  SER   C N   1 
ATOM   2309 C  CA  . SER   B 1 99  ? -54.463 -19.927 39.535  1.00 17.18 ?  94  SER   C CA  1 
ATOM   2310 C  C   . SER   B 1 99  ? -55.863 -20.458 39.823  1.00 17.64 ?  94  SER   C C   1 
ATOM   2311 O  O   . SER   B 1 99  ? -56.289 -20.453 40.984  1.00 18.45 ?  94  SER   C O   1 
ATOM   2312 C  CB  . SER   B 1 99  ? -53.489 -20.777 40.237  1.00 17.57 ?  94  SER   C CB  1 
ATOM   2313 O  OG  . SER   B 1 99  ? -53.646 -22.113 39.815  1.00 18.85 ?  94  SER   C OG  1 
ATOM   2314 N  N   . PRO   B 1 100 ? -56.577 -21.040 38.844  1.00 19.78 ?  95  PRO   C N   1 
ATOM   2315 C  CA  . PRO   B 1 100 ? -57.840 -21.717 39.160  1.00 18.46 ?  95  PRO   C CA  1 
ATOM   2316 C  C   . PRO   B 1 100 ? -57.690 -22.883 40.143  1.00 19.78 ?  95  PRO   C C   1 
ATOM   2317 O  O   . PRO   B 1 100 ? -58.701 -23.353 40.663  1.00 19.08 ?  95  PRO   C O   1 
ATOM   2318 C  CB  . PRO   B 1 100 ? -58.346 -22.168 37.788  1.00 19.84 ?  95  PRO   C CB  1 
ATOM   2319 C  CG  . PRO   B 1 100 ? -57.713 -21.235 36.837  1.00 19.18 ?  95  PRO   C CG  1 
ATOM   2320 C  CD  . PRO   B 1 100 ? -56.325 -20.974 37.392  1.00 19.05 ?  95  PRO   C CD  1 
ATOM   2321 N  N   . ALA   B 1 101 ? -56.463 -23.347 40.421  1.00 18.00 ?  96  ALA   C N   1 
ATOM   2322 C  CA  . ALA   B 1 101 ? -56.280 -24.431 41.412  1.00 21.53 ?  96  ALA   C CA  1 
ATOM   2323 C  C   . ALA   B 1 101 ? -56.868 -23.955 42.738  1.00 24.57 ?  96  ALA   C C   1 
ATOM   2324 O  O   . ALA   B 1 101 ? -57.342 -24.806 43.524  1.00 22.74 ?  96  ALA   C O   1 
ATOM   2325 C  CB  . ALA   B 1 101 ? -54.818 -24.820 41.537  1.00 21.93 ?  96  ALA   C CB  1 
ATOM   2326 N  N   . VAL   B 1 102 ? -56.781 -22.651 43.002  1.00 22.26 ?  97  VAL   C N   1 
ATOM   2327 C  CA  . VAL   B 1 102 ? -57.201 -22.021 44.284  1.00 26.03 ?  97  VAL   C CA  1 
ATOM   2328 C  C   . VAL   B 1 102 ? -58.728 -22.111 44.400  1.00 25.05 ?  97  VAL   C C   1 
ATOM   2329 O  O   . VAL   B 1 102 ? -59.233 -22.285 45.523  1.00 27.52 ?  97  VAL   C O   1 
ATOM   2330 C  CB  . VAL   B 1 102 ? -56.668 -20.586 44.346  1.00 26.73 ?  97  VAL   C CB  1 
ATOM   2331 C  CG1 . VAL   B 1 102 ? -57.161 -19.851 45.564  1.00 33.11 ?  97  VAL   C CG1 1 
ATOM   2332 C  CG2 . VAL   B 1 102 ? -55.145 -20.643 44.341  1.00 27.93 ?  97  VAL   C CG2 1 
ATOM   2333 N  N   . TYR   B 1 103 ? -59.423 -22.002 43.273  1.00 23.84 ?  98  TYR   C N   1 
ATOM   2334 C  CA  . TYR   B 1 103 ? -60.911 -21.987 43.230  1.00 24.54 ?  98  TYR   C CA  1 
ATOM   2335 C  C   . TYR   B 1 103 ? -61.452 -23.335 43.701  1.00 27.09 ?  98  TYR   C C   1 
ATOM   2336 O  O   . TYR   B 1 103 ? -62.540 -23.329 44.280  1.00 26.34 ?  98  TYR   C O   1 
ATOM   2337 C  CB  . TYR   B 1 103 ? -61.430 -21.760 41.818  1.00 23.50 ?  98  TYR   C CB  1 
ATOM   2338 C  CG  . TYR   B 1 103 ? -61.133 -20.438 41.178  1.00 23.66 ?  98  TYR   C CG  1 
ATOM   2339 C  CD1 . TYR   B 1 103 ? -60.742 -19.317 41.897  1.00 23.46 ?  98  TYR   C CD1 1 
ATOM   2340 C  CD2 . TYR   B 1 103 ? -61.314 -20.295 39.819  1.00 21.80 ?  98  TYR   C CD2 1 
ATOM   2341 C  CE1 . TYR   B 1 103 ? -60.520 -18.097 41.270  1.00 22.14 ?  98  TYR   C CE1 1 
ATOM   2342 C  CE2 . TYR   B 1 103 ? -61.050 -19.103 39.175  1.00 22.68 ?  98  TYR   C CE2 1 
ATOM   2343 C  CZ  . TYR   B 1 103 ? -60.675 -17.990 39.904  1.00 23.95 ?  98  TYR   C CZ  1 
ATOM   2344 O  OH  . TYR   B 1 103 ? -60.506 -16.810 39.266  1.00 23.85 ?  98  TYR   C OH  1 
ATOM   2345 N  N   . ARG   B 1 104 ? -60.731 -24.424 43.386  1.00 27.06 ?  99  ARG   C N   1 
ATOM   2346 C  CA  . ARG   B 1 104 ? -61.140 -25.837 43.619  1.00 30.32 ?  99  ARG   C CA  1 
ATOM   2347 C  C   . ARG   B 1 104 ? -62.473 -26.070 42.910  1.00 31.87 ?  99  ARG   C C   1 
ATOM   2348 O  O   . ARG   B 1 104 ? -63.306 -26.790 43.440  1.00 34.90 ?  99  ARG   C O   1 
ATOM   2349 C  CB  . ARG   B 1 104 ? -61.223 -26.131 45.125  1.00 30.81 ?  99  ARG   C CB  1 
ATOM   2350 C  CG  . ARG   B 1 104 ? -59.891 -26.079 45.853  1.00 35.12 ?  99  ARG   C CG  1 
ATOM   2351 C  CD  . ARG   B 1 104 ? -59.916 -26.685 47.252  1.00 37.58 ?  99  ARG   C CD  1 
ATOM   2352 N  NE  . ARG   B 1 104 ? -61.080 -26.385 48.097  1.00 43.38 ?  99  ARG   C NE  1 
ATOM   2353 C  CZ  . ARG   B 1 104 ? -61.146 -25.435 49.047  1.00 47.26 ?  99  ARG   C CZ  1 
ATOM   2354 N  NH1 . ARG   B 1 104 ? -60.129 -24.617 49.275  1.00 47.13 1  99  ARG   C NH1 1 
ATOM   2355 N  NH2 . ARG   B 1 104 ? -62.246 -25.293 49.770  1.00 48.40 ?  99  ARG   C NH2 1 
ATOM   2356 N  N   . THR   B 1 105 ? -62.720 -25.378 41.805  1.00 30.44 ?  100 THR   C N   1 
ATOM   2357 C  CA  . THR   B 1 105 ? -63.967 -25.564 41.016  1.00 31.49 ?  100 THR   C CA  1 
ATOM   2358 C  C   . THR   B 1 105 ? -63.571 -25.859 39.577  1.00 29.26 ?  100 THR   C C   1 
ATOM   2359 O  O   . THR   B 1 105 ? -62.389 -25.672 39.196  1.00 26.91 ?  100 THR   C O   1 
ATOM   2360 C  CB  . THR   B 1 105 ? -64.916 -24.359 41.072  1.00 33.77 ?  100 THR   C CB  1 
ATOM   2361 O  OG1 . THR   B 1 105 ? -64.250 -23.237 40.495  1.00 32.16 ?  100 THR   C OG1 1 
ATOM   2362 C  CG2 . THR   B 1 105 ? -65.378 -24.038 42.476  1.00 39.41 ?  100 THR   C CG2 1 
ATOM   2363 N  N   . ALA   B 1 106 ? -64.525 -26.310 38.786  1.00 25.92 ?  101 ALA   C N   1 
ATOM   2364 C  CA  . ALA   B 1 106 ? -64.262 -26.629 37.378  1.00 24.33 ?  101 ALA   C CA  1 
ATOM   2365 C  C   . ALA   B 1 106 ? -65.561 -26.490 36.632  1.00 25.78 ?  101 ALA   C C   1 
ATOM   2366 O  O   . ALA   B 1 106 ? -66.614 -26.816 37.182  1.00 27.09 ?  101 ALA   C O   1 
ATOM   2367 C  CB  . ALA   B 1 106 ? -63.678 -28.011 37.238  1.00 27.83 ?  101 ALA   C CB  1 
ATOM   2368 N  N   . PRO   B 1 107 ? -65.554 -26.054 35.359  1.00 22.15 ?  102 PRO   C N   1 
ATOM   2369 C  CA  . PRO   B 1 107 ? -64.371 -25.534 34.678  1.00 24.00 ?  102 PRO   C CA  1 
ATOM   2370 C  C   . PRO   B 1 107 ? -64.076 -24.089 35.112  1.00 23.85 ?  102 PRO   C C   1 
ATOM   2371 O  O   . PRO   B 1 107 ? -64.892 -23.477 35.823  1.00 21.47 ?  102 PRO   C O   1 
ATOM   2372 C  CB  . PRO   B 1 107 ? -64.821 -25.542 33.218  1.00 23.43 ?  102 PRO   C CB  1 
ATOM   2373 C  CG  . PRO   B 1 107 ? -66.327 -25.261 33.283  1.00 23.62 ?  102 PRO   C CG  1 
ATOM   2374 C  CD  . PRO   B 1 107 ? -66.757 -26.013 34.520  1.00 24.93 ?  102 PRO   C CD  1 
ATOM   2375 N  N   . ALA   B 1 108 ? -62.927 -23.559 34.695  1.00 21.58 ?  103 ALA   C N   1 
ATOM   2376 C  CA  . ALA   B 1 108 ? -62.478 -22.202 35.085  1.00 20.24 ?  103 ALA   C CA  1 
ATOM   2377 C  C   . ALA   B 1 108 ? -61.449 -21.674 34.105  1.00 18.53 ?  103 ALA   C C   1 
ATOM   2378 O  O   . ALA   B 1 108 ? -60.996 -22.394 33.231  1.00 17.59 ?  103 ALA   C O   1 
ATOM   2379 C  CB  . ALA   B 1 108 ? -61.898 -22.238 36.463  1.00 20.96 ?  103 ALA   C CB  1 
ATOM   2380 N  N   . ALA   B 1 109 ? -61.095 -20.405 34.240  1.00 18.14 ?  104 ALA   C N   1 
ATOM   2381 C  CA  . ALA   B 1 109 ? -59.955 -19.827 33.521  1.00 19.75 ?  104 ALA   C CA  1 
ATOM   2382 C  C   . ALA   B 1 109 ? -59.178 -18.998 34.525  1.00 18.49 ?  104 ALA   C C   1 
ATOM   2383 O  O   . ALA   B 1 109 ? -59.748 -18.414 35.440  1.00 16.87 ?  104 ALA   C O   1 
ATOM   2384 C  CB  . ALA   B 1 109 ? -60.431 -19.033 32.345  1.00 19.74 ?  104 ALA   C CB  1 
ATOM   2385 N  N   . PRO   B 1 110 ? -57.851 -18.940 34.417  1.00 18.78 ?  105 PRO   C N   1 
ATOM   2386 C  CA  . PRO   B 1 110 ? -57.093 -18.048 35.282  1.00 16.95 ?  105 PRO   C CA  1 
ATOM   2387 C  C   . PRO   B 1 110 ? -57.356 -16.566 35.000  1.00 18.70 ?  105 PRO   C C   1 
ATOM   2388 O  O   . PRO   B 1 110 ? -57.867 -16.157 33.981  1.00 19.17 ?  105 PRO   C O   1 
ATOM   2389 C  CB  . PRO   B 1 110 ? -55.627 -18.333 34.908  1.00 16.98 ?  105 PRO   C CB  1 
ATOM   2390 C  CG  . PRO   B 1 110 ? -55.677 -19.580 34.057  1.00 17.88 ?  105 PRO   C CG  1 
ATOM   2391 C  CD  . PRO   B 1 110 ? -57.021 -19.556 33.382  1.00 20.59 ?  105 PRO   C CD  1 
ATOM   2392 N  N   . THR   B 1 111 ? -56.877 -15.726 35.911  1.00 19.22 ?  106 THR   C N   1 
ATOM   2393 C  CA  . THR   B 1 111 ? -56.819 -14.275 35.661  1.00 18.50 ?  106 THR   C CA  1 
ATOM   2394 C  C   . THR   B 1 111 ? -55.680 -13.641 36.455  1.00 17.58 ?  106 THR   C C   1 
ATOM   2395 O  O   . THR   B 1 111 ? -54.771 -14.348 36.992  1.00 17.54 ?  106 THR   C O   1 
ATOM   2396 C  CB  . THR   B 1 111 ? -58.191 -13.676 35.938  1.00 16.59 ?  106 THR   C CB  1 
ATOM   2397 O  OG1 . THR   B 1 111 ? -58.234 -12.334 35.438  1.00 19.26 ?  106 THR   C OG1 1 
ATOM   2398 C  CG2 . THR   B 1 111 ? -58.465 -13.641 37.428  1.00 19.17 ?  106 THR   C CG2 1 
ATOM   2399 N  N   . TRP   B 1 112 ? -55.646 -12.328 36.404  1.00 17.59 ?  107 TRP   C N   1 
ATOM   2400 C  CA  . TRP   B 1 112 ? -54.641 -11.587 37.182  1.00 18.89 ?  107 TRP   C CA  1 
ATOM   2401 C  C   . TRP   B 1 112 ? -55.393 -10.532 37.989  1.00 17.35 ?  107 TRP   C C   1 
ATOM   2402 O  O   . TRP   B 1 112 ? -56.091 -9.735  37.396  1.00 20.11 ?  107 TRP   C O   1 
ATOM   2403 C  CB  . TRP   B 1 112 ? -53.554 -10.983 36.292  1.00 20.01 ?  107 TRP   C CB  1 
ATOM   2404 C  CG  . TRP   B 1 112 ? -52.248 -10.746 36.979  1.00 17.33 ?  107 TRP   C CG  1 
ATOM   2405 C  CD1 . TRP   B 1 112 ? -51.971 -9.841  37.956  1.00 19.76 ?  107 TRP   C CD1 1 
ATOM   2406 C  CD2 . TRP   B 1 112 ? -51.031 -11.414 36.726  1.00 17.72 ?  107 TRP   C CD2 1 
ATOM   2407 N  NE1 . TRP   B 1 112 ? -50.651 -9.898  38.326  1.00 18.19 ?  107 TRP   C NE1 1 
ATOM   2408 C  CE2 . TRP   B 1 112 ? -50.041 -10.860 37.577  1.00 18.95 ?  107 TRP   C CE2 1 
ATOM   2409 C  CE3 . TRP   B 1 112 ? -50.663 -12.436 35.855  1.00 16.67 ?  107 TRP   C CE3 1 
ATOM   2410 C  CZ2 . TRP   B 1 112 ? -48.713 -11.296 37.572  1.00 17.24 ?  107 TRP   C CZ2 1 
ATOM   2411 C  CZ3 . TRP   B 1 112 ? -49.359 -12.864 35.852  1.00 17.28 ?  107 TRP   C CZ3 1 
ATOM   2412 C  CH2 . TRP   B 1 112 ? -48.412 -12.350 36.740  1.00 17.85 ?  107 TRP   C CH2 1 
ATOM   2413 N  N   . ASN   B 1 113 ? -55.327 -10.604 39.313  1.00 16.26 ?  108 ASN   C N   1 
ATOM   2414 C  CA  . ASN   B 1 113 ? -55.916 -9.547  40.174  1.00 17.52 ?  108 ASN   C CA  1 
ATOM   2415 C  C   . ASN   B 1 113 ? -54.929 -8.406  40.165  1.00 18.51 ?  108 ASN   C C   1 
ATOM   2416 O  O   . ASN   B 1 113 ? -53.714 -8.662  40.416  1.00 17.23 ?  108 ASN   C O   1 
ATOM   2417 C  CB  . ASN   B 1 113 ? -56.248 -10.111 41.551  1.00 17.79 ?  108 ASN   C CB  1 
ATOM   2418 C  CG  . ASN   B 1 113 ? -57.538 -10.919 41.558  1.00 19.18 ?  108 ASN   C CG  1 
ATOM   2419 O  OD1 . ASN   B 1 113 ? -58.148 -11.155 40.500  1.00 19.18 ?  108 ASN   C OD1 1 
ATOM   2420 N  ND2 . ASN   B 1 113 ? -57.883 -11.426 42.723  1.00 18.18 ?  108 ASN   C ND2 1 
ATOM   2421 N  N   . PHE   B 1 114 ? -55.414 -7.183  40.065  1.00 18.07 ?  109 PHE   C N   1 
ATOM   2422 C  CA  . PHE   B 1 114 ? -54.527 -6.023  40.084  1.00 18.26 ?  109 PHE   C CA  1 
ATOM   2423 C  C   . PHE   B 1 114 ? -55.333 -4.791  40.432  1.00 17.11 ?  109 PHE   C C   1 
ATOM   2424 O  O   . PHE   B 1 114 ? -56.620 -4.769  40.376  1.00 16.58 ?  109 PHE   C O   1 
ATOM   2425 C  CB  . PHE   B 1 114 ? -53.823 -5.877  38.742  1.00 19.09 ?  109 PHE   C CB  1 
ATOM   2426 C  CG  . PHE   B 1 114 ? -54.695 -5.367  37.630  1.00 17.48 ?  109 PHE   C CG  1 
ATOM   2427 C  CD1 . PHE   B 1 114 ? -55.424 -6.231  36.830  1.00 16.25 ?  109 PHE   C CD1 1 
ATOM   2428 C  CD2 . PHE   B 1 114 ? -54.696 -4.015  37.308  1.00 18.94 ?  109 PHE   C CD2 1 
ATOM   2429 C  CE1 . PHE   B 1 114 ? -56.161 -5.741  35.754  1.00 19.01 ?  109 PHE   C CE1 1 
ATOM   2430 C  CE2 . PHE   B 1 114 ? -55.487 -3.520  36.289  1.00 20.50 ?  109 PHE   C CE2 1 
ATOM   2431 C  CZ  . PHE   B 1 114 ? -56.220 -4.389  35.500  1.00 17.69 ?  109 PHE   C CZ  1 
ATOM   2432 N  N   . THR   B 1 115 ? -54.582 -3.771  40.776  1.00 18.28 ?  110 THR   C N   1 
ATOM   2433 C  CA  . THR   B 1 115 ? -55.103 -2.437  41.180  1.00 18.55 ?  110 THR   C CA  1 
ATOM   2434 C  C   . THR   B 1 115 ? -54.464 -1.373  40.311  1.00 18.78 ?  110 THR   C C   1 
ATOM   2435 O  O   . THR   B 1 115 ? -53.248 -1.336  40.154  1.00 18.19 ?  110 THR   C O   1 
ATOM   2436 C  CB  . THR   B 1 115 ? -54.943 -2.262  42.692  1.00 19.56 ?  110 THR   C CB  1 
ATOM   2437 O  OG1 . THR   B 1 115 ? -53.554 -2.403  43.002  1.00 20.44 ?  110 THR   C OG1 1 
ATOM   2438 C  CG2 . THR   B 1 115 ? -55.846 -3.239  43.421  1.00 20.52 ?  110 THR   C CG2 1 
ATOM   2439 N  N   . SER   B 1 116 ? -55.260 -0.489  39.753  1.00 19.30 ?  111 SER   C N   1 
ATOM   2440 C  CA  . SER   B 1 116 ? -54.752 0.624   38.931  1.00 18.65 ?  111 SER   C CA  1 
ATOM   2441 C  C   . SER   B 1 116 ? -55.569 1.858   39.227  1.00 18.21 ?  111 SER   C C   1 
ATOM   2442 O  O   . SER   B 1 116 ? -56.773 1.758   39.292  1.00 18.88 ?  111 SER   C O   1 
ATOM   2443 C  CB  . SER   B 1 116 ? -54.829 0.226   37.468  1.00 20.75 ?  111 SER   C CB  1 
ATOM   2444 O  OG  . SER   B 1 116 ? -54.003 1.001   36.640  1.00 31.96 ?  111 SER   C OG  1 
ATOM   2445 N  N   . VAL   B 1 117 ? -54.919 3.017   39.237  1.00 16.35 ?  112 VAL   C N   1 
ATOM   2446 C  CA  . VAL   B 1 117 ? -55.632 4.308   39.110  1.00 15.90 ?  112 VAL   C CA  1 
ATOM   2447 C  C   . VAL   B 1 117 ? -55.081 5.011   37.858  1.00 16.80 ?  112 VAL   C C   1 
ATOM   2448 O  O   . VAL   B 1 117 ? -53.875 5.190   37.761  1.00 15.92 ?  112 VAL   C O   1 
ATOM   2449 C  CB  . VAL   B 1 117 ? -55.510 5.161   40.375  1.00 15.84 ?  112 VAL   C CB  1 
ATOM   2450 C  CG1 . VAL   B 1 117 ? -55.973 6.610   40.183  1.00 16.35 ?  112 VAL   C CG1 1 
ATOM   2451 C  CG2 . VAL   B 1 117 ? -56.279 4.529   41.503  1.00 19.24 ?  112 VAL   C CG2 1 
ATOM   2452 N  N   . GLN   B 1 118 ? -55.964 5.468   37.000  1.00 16.30 ?  113 GLN   C N   1 
ATOM   2453 C  CA  . GLN   B 1 118 ? -55.657 6.335   35.858  1.00 17.19 ?  113 GLN   C CA  1 
ATOM   2454 C  C   . GLN   B 1 118 ? -56.255 7.697   36.104  1.00 19.32 ?  113 GLN   C C   1 
ATOM   2455 O  O   . GLN   B 1 118 ? -57.501 7.810   36.249  1.00 19.66 ?  113 GLN   C O   1 
ATOM   2456 C  CB  . GLN   B 1 118 ? -56.112 5.791   34.522  1.00 17.34 ?  113 GLN   C CB  1 
ATOM   2457 C  CG  . GLN   B 1 118 ? -55.430 4.503   34.188  1.00 20.37 ?  113 GLN   C CG  1 
ATOM   2458 C  CD  . GLN   B 1 118 ? -55.919 3.959   32.869  1.00 20.58 ?  113 GLN   C CD  1 
ATOM   2459 O  OE1 . GLN   B 1 118 ? -56.480 4.666   32.048  1.00 20.47 ?  113 GLN   C OE1 1 
ATOM   2460 N  NE2 . GLN   B 1 118 ? -55.659 2.693   32.652  1.00 21.12 ?  113 GLN   C NE2 1 
ATOM   2461 N  N   . VAL   B 1 119 ? -55.394 8.683   36.208  1.00 17.86 ?  114 VAL   C N   1 
ATOM   2462 C  CA  . VAL   B 1 119 ? -55.843 10.115  36.268  1.00 18.68 ?  114 VAL   C CA  1 
ATOM   2463 C  C   . VAL   B 1 119 ? -55.554 10.822  34.948  1.00 21.58 ?  114 VAL   C C   1 
ATOM   2464 O  O   . VAL   B 1 119 ? -54.501 10.588  34.291  1.00 19.08 ?  114 VAL   C O   1 
ATOM   2465 C  CB  . VAL   B 1 119 ? -55.256 10.935  37.418  1.00 20.83 ?  114 VAL   C CB  1 
ATOM   2466 C  CG1 . VAL   B 1 119 ? -55.656 10.375  38.754  1.00 22.37 ?  114 VAL   C CG1 1 
ATOM   2467 C  CG2 . VAL   B 1 119 ? -53.767 11.060  37.305  1.00 22.74 ?  114 VAL   C CG2 1 
ATOM   2468 N  N   . ARG   B 1 120 ? -56.505 11.635  34.535  1.00 20.54 ?  115 ARG   C N   1 
ATOM   2469 C  CA  . ARG   B 1 120 ? -56.364 12.374  33.269  1.00 19.44 ?  115 ARG   C CA  1 
ATOM   2470 C  C   . ARG   B 1 120 ? -56.632 13.857  33.515  1.00 20.95 ?  115 ARG   C C   1 
ATOM   2471 O  O   . ARG   B 1 120 ? -57.569 14.223  34.339  1.00 22.01 ?  115 ARG   C O   1 
ATOM   2472 C  CB  . ARG   B 1 120 ? -57.302 11.827  32.203  1.00 20.86 ?  115 ARG   C CB  1 
ATOM   2473 C  CG  . ARG   B 1 120 ? -56.926 10.443  31.697  1.00 19.42 ?  115 ARG   C CG  1 
ATOM   2474 C  CD  . ARG   B 1 120 ? -58.023 9.881   30.791  1.00 22.02 ?  115 ARG   C CD  1 
ATOM   2475 N  NE  . ARG   B 1 120 ? -57.470 8.778   30.029  1.00 20.91 ?  115 ARG   C NE  1 
ATOM   2476 C  CZ  . ARG   B 1 120 ? -57.214 7.548   30.497  1.00 21.14 ?  115 ARG   C CZ  1 
ATOM   2477 N  NH1 . ARG   B 1 120 ? -57.436 7.160   31.752  1.00 18.19 1  115 ARG   C NH1 1 
ATOM   2478 N  NH2 . ARG   B 1 120 ? -56.683 6.683   29.654  1.00 23.33 ?  115 ARG   C NH2 1 
ATOM   2479 N  N   . GLY   B 1 121 ? -55.842 14.655  32.807  1.00 19.15 ?  116 GLY   C N   1 
ATOM   2480 C  CA  . GLY   B 1 121 ? -56.067 16.099  32.702  1.00 20.13 ?  116 GLY   C CA  1 
ATOM   2481 C  C   . GLY   B 1 121 ? -54.951 16.805  31.999  1.00 21.55 ?  116 GLY   C C   1 
ATOM   2482 O  O   . GLY   B 1 121 ? -54.136 16.154  31.296  1.00 20.27 ?  116 GLY   C O   1 
ATOM   2483 N  N   . GLU   B 1 122 ? -54.949 18.129  32.160  1.00 21.06 ?  117 GLU   C N   1 
ATOM   2484 C  CA  . GLU   B 1 122 ? -53.976 18.996  31.497  1.00 23.48 ?  117 GLU   C CA  1 
ATOM   2485 C  C   . GLU   B 1 122 ? -52.713 19.057  32.332  1.00 22.40 ?  117 GLU   C C   1 
ATOM   2486 O  O   . GLU   B 1 122 ? -52.811 19.273  33.553  1.00 27.60 ?  117 GLU   C O   1 
ATOM   2487 C  CB  . GLU   B 1 122 ? -54.546 20.389  31.334  1.00 30.08 ?  117 GLU   C CB  1 
ATOM   2488 C  CG  . GLU   B 1 122 ? -53.709 21.260  30.441  1.00 35.73 ?  117 GLU   C CG  1 
ATOM   2489 C  CD  . GLU   B 1 122 ? -54.356 22.625  30.207  1.00 47.85 ?  117 GLU   C CD  1 
ATOM   2490 O  OE1 . GLU   B 1 122 ? -55.583 22.635  29.862  1.00 51.44 ?  117 GLU   C OE1 1 
ATOM   2491 O  OE2 . GLU   B 1 122 ? -53.654 23.672  30.406  1.00 47.91 -1 117 GLU   C OE2 1 
ATOM   2492 N  N   . LEU   B 1 123 ? -51.572 18.842  31.695  1.00 20.58 ?  118 LEU   C N   1 
ATOM   2493 C  CA  . LEU   B 1 123 ? -50.283 18.998  32.363  1.00 21.47 ?  118 LEU   C CA  1 
ATOM   2494 C  C   . LEU   B 1 123 ? -49.776 20.427  32.112  1.00 22.65 ?  118 LEU   C C   1 
ATOM   2495 O  O   . LEU   B 1 123 ? -49.613 20.847  30.928  1.00 26.54 ?  118 LEU   C O   1 
ATOM   2496 C  CB  . LEU   B 1 123 ? -49.306 17.935  31.873  1.00 21.19 ?  118 LEU   C CB  1 
ATOM   2497 C  CG  . LEU   B 1 123 ? -47.964 17.966  32.613  1.00 23.70 ?  118 LEU   C CG  1 
ATOM   2498 C  CD1 . LEU   B 1 123 ? -47.382 16.582  32.798  1.00 23.23 ?  118 LEU   C CD1 1 
ATOM   2499 C  CD2 . LEU   B 1 123 ? -46.944 18.805  31.887  1.00 22.86 ?  118 LEU   C CD2 1 
ATOM   2500 N  N   . ARG   B 1 124 ? -49.449 21.132  33.179  1.00 22.46 ?  119 ARG   C N   1 
ATOM   2501 C  CA  . ARG   B 1 124 ? -48.822 22.475  33.102  1.00 20.61 ?  119 ARG   C CA  1 
ATOM   2502 C  C   . ARG   B 1 124 ? -47.362 22.355  33.585  1.00 21.93 ?  119 ARG   C C   1 
ATOM   2503 O  O   . ARG   B 1 124 ? -47.121 21.862  34.696  1.00 22.46 ?  119 ARG   C O   1 
ATOM   2504 C  CB  . ARG   B 1 124 ? -49.572 23.490  33.959  1.00 25.29 ?  119 ARG   C CB  1 
ATOM   2505 C  CG  . ARG   B 1 124 ? -49.002 24.881  33.715  1.00 32.01 ?  119 ARG   C CG  1 
ATOM   2506 C  CD  . ARG   B 1 124 ? -49.602 26.010  34.531  1.00 36.05 ?  119 ARG   C CD  1 
ATOM   2507 N  NE  . ARG   B 1 124 ? -49.517 25.866  35.983  1.00 39.93 ?  119 ARG   C NE  1 
ATOM   2508 C  CZ  . ARG   B 1 124 ? -48.398 25.946  36.715  1.00 42.80 ?  119 ARG   C CZ  1 
ATOM   2509 N  NH1 . ARG   B 1 124 ? -48.481 25.857  38.033  1.00 43.12 1  119 ARG   C NH1 1 
ATOM   2510 N  NH2 . ARG   B 1 124 ? -47.212 26.109  36.149  1.00 41.40 ?  119 ARG   C NH2 1 
ATOM   2511 N  N   . LYS   B 1 125 ? -46.429 22.767  32.760  1.00 19.43 ?  120 LYS   C N   1 
ATOM   2512 C  CA  . LYS   B 1 125 ? -45.003 22.839  33.161  1.00 20.27 ?  120 LYS   C CA  1 
ATOM   2513 C  C   . LYS   B 1 125 ? -44.801 24.028  34.101  1.00 22.30 ?  120 LYS   C C   1 
ATOM   2514 O  O   . LYS   B 1 125 ? -45.304 25.131  33.844  1.00 20.78 ?  120 LYS   C O   1 
ATOM   2515 C  CB  . LYS   B 1 125 ? -44.090 23.023  31.968  1.00 20.83 ?  120 LYS   C CB  1 
ATOM   2516 C  CG  . LYS   B 1 125 ? -44.180 21.942  30.922  1.00 21.52 ?  120 LYS   C CG  1 
ATOM   2517 C  CD  . LYS   B 1 125 ? -43.428 22.313  29.678  1.00 25.72 ?  120 LYS   C CD  1 
ATOM   2518 C  CE  . LYS   B 1 125 ? -43.101 21.100  28.858  1.00 23.75 ?  120 LYS   C CE  1 
ATOM   2519 N  NZ  . LYS   B 1 125 ? -42.441 21.429  27.565  1.00 28.34 1  120 LYS   C NZ  1 
ATOM   2520 N  N   . VAL   B 1 126 ? -44.078 23.784  35.177  1.00 19.48 ?  121 VAL   C N   1 
ATOM   2521 C  CA  . VAL   B 1 126 ? -43.615 24.767  36.177  1.00 19.83 ?  121 VAL   C CA  1 
ATOM   2522 C  C   . VAL   B 1 126 ? -42.310 25.349  35.641  1.00 19.76 ?  121 VAL   C C   1 
ATOM   2523 O  O   . VAL   B 1 126 ? -41.474 24.560  35.176  1.00 19.35 ?  121 VAL   C O   1 
ATOM   2524 C  CB  . VAL   B 1 126 ? -43.403 24.075  37.536  1.00 20.63 ?  121 VAL   C CB  1 
ATOM   2525 C  CG1 . VAL   B 1 126 ? -42.759 25.009  38.544  1.00 24.38 ?  121 VAL   C CG1 1 
ATOM   2526 C  CG2 . VAL   B 1 126 ? -44.722 23.511  38.085  1.00 22.45 ?  121 VAL   C CG2 1 
ATOM   2527 N  N   . GLU   B 1 127 ? -42.219 26.675  35.544  1.00 21.94 ?  122 GLU   C N   1 
ATOM   2528 C  CA  . GLU   B 1 127 ? -40.934 27.308  35.155  1.00 23.19 ?  122 GLU   C CA  1 
ATOM   2529 C  C   . GLU   B 1 127 ? -40.262 27.948  36.380  1.00 22.51 ?  122 GLU   C C   1 
ATOM   2530 O  O   . GLU   B 1 127 ? -39.000 28.037  36.382  1.00 26.46 ?  122 GLU   C O   1 
ATOM   2531 C  CB  . GLU   B 1 127 ? -41.189 28.271  33.998  1.00 23.43 ?  122 GLU   C CB  1 
ATOM   2532 C  CG  . GLU   B 1 127 ? -41.693 27.556  32.766  1.00 24.04 ?  122 GLU   C CG  1 
ATOM   2533 C  CD  . GLU   B 1 127 ? -40.747 26.581  32.087  1.00 25.11 ?  122 GLU   C CD  1 
ATOM   2534 O  OE1 . GLU   B 1 127 ? -39.575 26.379  32.531  1.00 24.26 ?  122 GLU   C OE1 1 
ATOM   2535 O  OE2 . GLU   B 1 127 ? -41.162 26.037  31.086  1.00 25.31 -1 122 GLU   C OE2 1 
ATOM   2536 N  N   . SER   B 1 128 ? -41.057 28.424  37.330  1.00 25.14 ?  123 SER   C N   1 
ATOM   2537 C  CA  . SER   B 1 128 ? -40.572 29.116  38.555  1.00 25.89 ?  123 SER   C CA  1 
ATOM   2538 C  C   . SER   B 1 128 ? -39.540 28.267  39.295  1.00 23.41 ?  123 SER   C C   1 
ATOM   2539 O  O   . SER   B 1 128 ? -39.808 27.098  39.572  1.00 24.19 ?  123 SER   C O   1 
ATOM   2540 C  CB  . SER   B 1 128 ? -41.731 29.483  39.431  1.00 30.48 ?  123 SER   C CB  1 
ATOM   2541 O  OG  . SER   B 1 128 ? -41.326 29.659  40.756  1.00 32.12 ?  123 SER   C OG  1 
ATOM   2542 N  N   . ALA   B 1 129 ? -38.354 28.803  39.586  1.00 25.22 ?  124 ALA   C N   1 
ATOM   2543 C  CA  . ALA   B 1 129 ? -37.373 28.088  40.425  1.00 25.91 ?  124 ALA   C CA  1 
ATOM   2544 C  C   . ALA   B 1 129 ? -37.953 27.841  41.828  1.00 26.64 ?  124 ALA   C C   1 
ATOM   2545 O  O   . ALA   B 1 129 ? -37.762 26.731  42.362  1.00 22.99 ?  124 ALA   C O   1 
ATOM   2546 C  CB  . ALA   B 1 129 ? -36.081 28.846  40.485  1.00 27.53 ?  124 ALA   C CB  1 
ATOM   2547 N  N   . ASP   B 1 130 ? -38.712 28.778  42.408  1.00 26.35 ?  125 ASP   C N   1 
ATOM   2548 C  CA  . ASP   B 1 130 ? -39.329 28.578  43.749  1.00 28.67 ?  125 ASP   C CA  1 
ATOM   2549 C  C   . ASP   B 1 130 ? -40.269 27.367  43.718  1.00 26.04 ?  125 ASP   C C   1 
ATOM   2550 O  O   . ASP   B 1 130 ? -40.137 26.480  44.612  1.00 23.59 ?  125 ASP   C O   1 
ATOM   2551 C  CB  . ASP   B 1 130 ? -40.064 29.822  44.246  1.00 33.72 ?  125 ASP   C CB  1 
ATOM   2552 C  CG  . ASP   B 1 130 ? -39.164 31.030  44.414  1.00 45.22 ?  125 ASP   C CG  1 
ATOM   2553 O  OD1 . ASP   B 1 130 ? -39.658 32.166  44.136  1.00 46.75 ?  125 ASP   C OD1 1 
ATOM   2554 O  OD2 . ASP   B 1 130 ? -37.964 30.832  44.793  1.00 46.01 -1 125 ASP   C OD2 1 
ATOM   2555 N  N   . ASP   B 1 131 ? -41.182 27.323  42.742  1.00 24.54 ?  126 ASP   C N   1 
ATOM   2556 C  CA  . ASP   B 1 131 ? -42.183 26.237  42.624  1.00 22.11 ?  126 ASP   C CA  1 
ATOM   2557 C  C   . ASP   B 1 131 ? -41.487 24.892  42.311  1.00 20.17 ?  126 ASP   C C   1 
ATOM   2558 O  O   . ASP   B 1 131 ? -41.992 23.830  42.776  1.00 20.82 ?  126 ASP   C O   1 
ATOM   2559 C  CB  . ASP   B 1 131 ? -43.268 26.619  41.633  1.00 26.82 ?  126 ASP   C CB  1 
ATOM   2560 C  CG  . ASP   B 1 131 ? -44.290 27.633  42.143  1.00 35.24 ?  126 ASP   C CG  1 
ATOM   2561 O  OD1 . ASP   B 1 131 ? -44.188 28.011  43.317  1.00 39.19 ?  126 ASP   C OD1 1 
ATOM   2562 O  OD2 . ASP   B 1 131 ? -45.244 27.983  41.362  1.00 47.87 -1 126 ASP   C OD2 1 
ATOM   2563 N  N   . THR   B 1 132 ? -40.402 24.887  41.540  1.00 21.57 ?  127 THR   C N   1 
ATOM   2564 C  CA  . THR   B 1 132 ? -39.654 23.661  41.207  1.00 20.33 ?  127 THR   C CA  1 
ATOM   2565 C  C   . THR   B 1 132 ? -39.052 23.090  42.497  1.00 19.76 ?  127 THR   C C   1 
ATOM   2566 O  O   . THR   B 1 132 ? -39.183 21.878  42.786  1.00 19.52 ?  127 THR   C O   1 
ATOM   2567 C  CB  . THR   B 1 132 ? -38.607 23.953  40.129  1.00 22.28 ?  127 THR   C CB  1 
ATOM   2568 O  OG1 . THR   B 1 132 ? -39.274 24.513  38.979  1.00 21.17 ?  127 THR   C OG1 1 
ATOM   2569 C  CG2 . THR   B 1 132 ? -37.837 22.721  39.705  1.00 20.64 ?  127 THR   C CG2 1 
ATOM   2570 N  N   . LEU   B 1 133 ? -38.359 23.934  43.248  1.00 21.37 ?  128 LEU   C N   1 
ATOM   2571 C  CA  . LEU   B 1 133 ? -37.763 23.512  44.537  1.00 18.58 ?  128 LEU   C CA  1 
ATOM   2572 C  C   . LEU   B 1 133 ? -38.868 23.083  45.528  1.00 20.21 ?  128 LEU   C C   1 
ATOM   2573 O  O   . LEU   B 1 133 ? -38.719 22.034  46.160  1.00 19.76 ?  128 LEU   C O   1 
ATOM   2574 C  CB  . LEU   B 1 133 ? -36.910 24.661  45.071  1.00 20.45 ?  128 LEU   C CB  1 
ATOM   2575 C  CG  . LEU   B 1 133 ? -36.284 24.324  46.417  1.00 24.29 ?  128 LEU   C CG  1 
ATOM   2576 C  CD1 . LEU   B 1 133 ? -35.326 23.173  46.273  1.00 22.53 ?  128 LEU   C CD1 1 
ATOM   2577 C  CD2 . LEU   B 1 133 ? -35.631 25.548  47.047  1.00 24.41 ?  128 LEU   C CD2 1 
ATOM   2578 N  N   . ALA   B 1 134 ? -40.019 23.751  45.592  1.00 18.66 ?  129 ALA   C N   1 
ATOM   2579 C  CA  . ALA   B 1 134 ? -41.165 23.300  46.422  1.00 19.43 ?  129 ALA   C CA  1 
ATOM   2580 C  C   . ALA   B 1 134 ? -41.594 21.874  46.017  1.00 17.96 ?  129 ALA   C C   1 
ATOM   2581 O  O   . ALA   B 1 134 ? -41.974 21.027  46.879  1.00 16.99 ?  129 ALA   C O   1 
ATOM   2582 C  CB  . ALA   B 1 134 ? -42.333 24.246  46.307  1.00 21.34 ?  129 ALA   C CB  1 
ATOM   2583 N  N   . THR   B 1 135 ? -41.661 21.639  44.712  1.00 18.05 ?  130 THR   C N   1 
ATOM   2584 C  CA  . THR   B 1 135 ? -42.076 20.331  44.157  1.00 17.06 ?  130 THR   C CA  1 
ATOM   2585 C  C   . THR   B 1 135 ? -41.177 19.222  44.695  1.00 17.81 ?  130 THR   C C   1 
ATOM   2586 O  O   . THR   B 1 135 ? -41.659 18.218  45.249  1.00 18.58 ?  130 THR   C O   1 
ATOM   2587 C  CB  . THR   B 1 135 ? -42.098 20.353  42.624  1.00 16.86 ?  130 THR   C CB  1 
ATOM   2588 O  OG1 . THR   B 1 135 ? -42.957 21.382  42.114  1.00 18.61 ?  130 THR   C OG1 1 
ATOM   2589 C  CG2 . THR   B 1 135 ? -42.569 19.021  42.079  1.00 16.44 ?  130 THR   C CG2 1 
ATOM   2590 N  N   . VAL   B 1 136 ? -39.870 19.368  44.522  1.00 17.71 ?  131 VAL   C N   1 
ATOM   2591 C  CA  . VAL   B 1 136 ? -38.967 18.248  44.898  1.00 16.90 ?  131 VAL   C CA  1 
ATOM   2592 C  C   . VAL   B 1 136 ? -38.905 18.140  46.426  1.00 16.85 ?  131 VAL   C C   1 
ATOM   2593 O  O   . VAL   B 1 136 ? -38.885 16.980  46.921  1.00 16.77 ?  131 VAL   C O   1 
ATOM   2594 C  CB  . VAL   B 1 136 ? -37.579 18.342  44.243  1.00 20.78 ?  131 VAL   C CB  1 
ATOM   2595 C  CG1 . VAL   B 1 136 ? -37.679 18.276  42.722  1.00 22.88 ?  131 VAL   C CG1 1 
ATOM   2596 C  CG2 . VAL   B 1 136 ? -36.841 19.577  44.691  1.00 21.16 ?  131 VAL   C CG2 1 
ATOM   2597 N  N   . ARG   B 1 137 ? -38.955 19.237  47.157  1.00 18.12 ?  132 ARG   C N   1 
ATOM   2598 C  CA  . ARG   B 1 137 ? -38.988 19.156  48.635  1.00 17.86 ?  132 ARG   C CA  1 
ATOM   2599 C  C   . ARG   B 1 137 ? -40.281 18.478  49.112  1.00 18.51 ?  132 ARG   C C   1 
ATOM   2600 O  O   . ARG   B 1 137 ? -40.215 17.683  50.089  1.00 18.86 ?  132 ARG   C O   1 
ATOM   2601 C  CB  . ARG   B 1 137 ? -38.864 20.528  49.298  1.00 22.35 ?  132 ARG   C CB  1 
ATOM   2602 C  CG  . ARG   B 1 137 ? -37.432 21.025  49.260  1.00 24.62 ?  132 ARG   C CG  1 
ATOM   2603 C  CD  . ARG   B 1 137 ? -37.309 22.398  49.821  1.00 29.59 ?  132 ARG   C CD  1 
ATOM   2604 N  NE  . ARG   B 1 137 ? -37.555 22.340  51.245  1.00 32.47 ?  132 ARG   C NE  1 
ATOM   2605 C  CZ  . ARG   B 1 137 ? -37.423 23.365  52.073  1.00 39.50 ?  132 ARG   C CZ  1 
ATOM   2606 N  NH1 . ARG   B 1 137 ? -37.015 24.542  51.614  1.00 44.95 1  132 ARG   C NH1 1 
ATOM   2607 N  NH2 . ARG   B 1 137 ? -37.694 23.192  53.353  1.00 43.63 ?  132 ARG   C NH2 1 
ATOM   2608 N  N   . ALA   B 1 138 ? -41.446 18.822  48.564  1.00 17.57 ?  133 ALA   C N   1 
ATOM   2609 C  CA  . ALA   B 1 138 ? -42.700 18.155  48.952  1.00 17.82 ?  133 ALA   C CA  1 
ATOM   2610 C  C   . ALA   B 1 138 ? -42.651 16.639  48.643  1.00 18.95 ?  133 ALA   C C   1 
ATOM   2611 O  O   . ALA   B 1 138 ? -43.222 15.822  49.422  1.00 19.58 ?  133 ALA   C O   1 
ATOM   2612 C  CB  . ALA   B 1 138 ? -43.870 18.796  48.257  1.00 19.66 ?  133 ALA   C CB  1 
ATOM   2613 N  N   . THR   B 1 139 ? -42.072 16.270  47.503  1.00 19.68 ?  134 THR   C N   1 
ATOM   2614 C  CA  . THR   B 1 139 ? -41.894 14.862  47.084  1.00 19.25 ?  134 THR   C CA  1 
ATOM   2615 C  C   . THR   B 1 139 ? -41.046 14.139  48.133  1.00 18.55 ?  134 THR   C C   1 
ATOM   2616 O  O   . THR   B 1 139 ? -41.358 13.027  48.515  1.00 17.41 ?  134 THR   C O   1 
ATOM   2617 C  CB  . THR   B 1 139 ? -41.332 14.788  45.669  1.00 16.96 ?  134 THR   C CB  1 
ATOM   2618 O  OG1 . THR   B 1 139 ? -42.235 15.533  44.884  1.00 19.74 ?  134 THR   C OG1 1 
ATOM   2619 C  CG2 . THR   B 1 139 ? -41.211 13.385  45.143  1.00 18.31 ?  134 THR   C CG2 1 
ATOM   2620 N  N   . VAL   B 1 140 ? -39.927 14.735  48.544  1.00 19.04 ?  135 VAL   C N   1 
ATOM   2621 C  CA  . VAL   B 1 140 ? -39.103 14.114  49.600  1.00 18.92 ?  135 VAL   C CA  1 
ATOM   2622 C  C   . VAL   B 1 140 ? -39.972 13.946  50.852  1.00 17.24 ?  135 VAL   C C   1 
ATOM   2623 O  O   . VAL   B 1 140 ? -39.965 12.854  51.441  1.00 14.82 ?  135 VAL   C O   1 
ATOM   2624 C  CB  . VAL   B 1 140 ? -37.828 14.933  49.870  1.00 18.36 ?  135 VAL   C CB  1 
ATOM   2625 C  CG1 . VAL   B 1 140 ? -37.206 14.407  51.154  1.00 19.45 ?  135 VAL   C CG1 1 
ATOM   2626 C  CG2 . VAL   B 1 140 ? -36.847 14.889  48.693  1.00 17.53 ?  135 VAL   C CG2 1 
ATOM   2627 N  N   . ALA   B 1 141 ? -40.686 14.994  51.263  1.00 19.85 ?  136 ALA   C N   1 
ATOM   2628 C  CA  . ALA   B 1 141 ? -41.477 14.979  52.524  1.00 21.24 ?  136 ALA   C CA  1 
ATOM   2629 C  C   . ALA   B 1 141 ? -42.477 13.815  52.495  1.00 22.65 ?  136 ALA   C C   1 
ATOM   2630 O  O   . ALA   B 1 141 ? -42.542 12.996  53.487  1.00 21.38 ?  136 ALA   C O   1 
ATOM   2631 C  CB  . ALA   B 1 141 ? -42.096 16.350  52.744  1.00 21.38 ?  136 ALA   C CB  1 
ATOM   2632 N  N   . ALA   B 1 142 ? -43.176 13.650  51.374  1.00 19.78 ?  137 ALA   C N   1 
ATOM   2633 C  CA  . ALA   B 1 142 ? -44.260 12.665  51.219  1.00 19.49 ?  137 ALA   C CA  1 
ATOM   2634 C  C   . ALA   B 1 142 ? -43.659 11.262  51.127  1.00 18.93 ?  137 ALA   C C   1 
ATOM   2635 O  O   . ALA   B 1 142 ? -44.128 10.379  51.831  1.00 19.74 ?  137 ALA   C O   1 
ATOM   2636 C  CB  . ALA   B 1 142 ? -45.105 12.996  50.024  1.00 19.55 ?  137 ALA   C CB  1 
ATOM   2637 N  N   . LEU   B 1 143 ? -42.641 11.073  50.310  1.00 18.25 ?  138 LEU   C N   1 
ATOM   2638 C  CA  . LEU   B 1 143 ? -42.103 9.712   50.046  1.00 18.77 ?  138 LEU   C CA  1 
ATOM   2639 C  C   . LEU   B 1 143 ? -41.199 9.272   51.206  1.00 16.58 ?  138 LEU   C C   1 
ATOM   2640 O  O   . LEU   B 1 143 ? -41.257 8.085   51.555  1.00 16.71 ?  138 LEU   C O   1 
ATOM   2641 C  CB  . LEU   B 1 143 ? -41.353 9.609   48.724  1.00 18.64 ?  138 LEU   C CB  1 
ATOM   2642 C  CG  . LEU   B 1 143 ? -42.049 10.004  47.425  1.00 23.45 ?  138 LEU   C CG  1 
ATOM   2643 C  CD1 . LEU   B 1 143 ? -41.581 9.208   46.253  1.00 19.52 ?  138 LEU   C CD1 1 
ATOM   2644 C  CD2 . LEU   B 1 143 ? -43.542 10.174  47.488  1.00 19.62 ?  138 LEU   C CD2 1 
ATOM   2645 N  N   . GLU   B 1 144 ? -40.356 10.132  51.754  1.00 19.02 ?  139 GLU   C N   1 
ATOM   2646 C  CA  . GLU   B 1 144 ? -39.508 9.713   52.896  1.00 21.09 ?  139 GLU   C CA  1 
ATOM   2647 C  C   . GLU   B 1 144 ? -40.424 9.333   54.077  1.00 21.31 ?  139 GLU   C C   1 
ATOM   2648 O  O   . GLU   B 1 144 ? -40.191 8.271   54.740  1.00 19.04 ?  139 GLU   C O   1 
ATOM   2649 C  CB  . GLU   B 1 144 ? -38.473 10.796  53.208  1.00 20.28 ?  139 GLU   C CB  1 
ATOM   2650 C  CG  . GLU   B 1 144 ? -37.486 10.329  54.258  1.00 21.46 ?  139 GLU   C CG  1 
ATOM   2651 C  CD  . GLU   B 1 144 ? -36.507 9.241   53.830  1.00 18.86 ?  139 GLU   C CD  1 
ATOM   2652 O  OE1 . GLU   B 1 144 ? -36.291 9.039   52.622  1.00 17.22 ?  139 GLU   C OE1 1 
ATOM   2653 O  OE2 . GLU   B 1 144 ? -35.944 8.575   54.736  1.00 19.17 -1 139 GLU   C OE2 1 
ATOM   2654 N  N   . SER   B 1 145 ? -41.537 10.034  54.278  1.00 21.76 ?  140 SER   C N   1 
ATOM   2655 C  CA  . SER   B 1 145 ? -42.491 9.678   55.354  1.00 24.22 ?  140 SER   C CA  1 
ATOM   2656 C  C   . SER   B 1 145 ? -43.095 8.270   55.154  1.00 21.86 ?  140 SER   C C   1 
ATOM   2657 O  O   . SER   B 1 145 ? -43.253 7.499   56.122  1.00 22.23 ?  140 SER   C O   1 
ATOM   2658 C  CB  . SER   B 1 145 ? -43.568 10.745  55.462  1.00 26.54 ?  140 SER   C CB  1 
ATOM   2659 O  OG  . SER   B 1 145 ? -44.594 10.316  56.349  1.00 30.54 ?  140 SER   C OG  1 
ATOM   2660 N  N   . ARG   B 1 146 ? -43.501 7.920   53.956  1.00 19.55 ?  141 ARG   C N   1 
ATOM   2661 C  CA  . ARG   B 1 146 ? -44.268 6.696   53.687  1.00 23.51 ?  141 ARG   C CA  1 
ATOM   2662 C  C   . ARG   B 1 146 ? -43.350 5.508   53.435  1.00 22.03 ?  141 ARG   C C   1 
ATOM   2663 O  O   . ARG   B 1 146 ? -43.776 4.384   53.732  1.00 22.85 ?  141 ARG   C O   1 
ATOM   2664 C  CB  . ARG   B 1 146 ? -45.161 6.933   52.475  1.00 27.22 ?  141 ARG   C CB  1 
ATOM   2665 C  CG  . ARG   B 1 146 ? -46.519 6.267   52.564  1.00 36.42 ?  141 ARG   C CG  1 
ATOM   2666 C  CD  . ARG   B 1 146 ? -47.436 6.894   51.539  1.00 39.27 ?  141 ARG   C CD  1 
ATOM   2667 N  NE  . ARG   B 1 146 ? -48.344 7.841   52.158  1.00 47.19 ?  141 ARG   C NE  1 
ATOM   2668 C  CZ  . ARG   B 1 146 ? -49.498 7.496   52.715  1.00 46.75 ?  141 ARG   C CZ  1 
ATOM   2669 N  NH1 . ARG   B 1 146 ? -49.866 6.227   52.734  1.00 51.39 1  141 ARG   C NH1 1 
ATOM   2670 N  NH2 . ARG   B 1 146 ? -50.277 8.418   53.245  1.00 58.13 ?  141 ARG   C NH2 1 
ATOM   2671 N  N   . PHE   B 1 147 ? -42.150 5.714   52.879  1.00 18.52 ?  142 PHE   C N   1 
ATOM   2672 C  CA  . PHE   B 1 147 ? -41.313 4.627   52.324  1.00 17.05 ?  142 PHE   C CA  1 
ATOM   2673 C  C   . PHE   B 1 147 ? -39.891 4.639   52.889  1.00 15.94 ?  142 PHE   C C   1 
ATOM   2674 O  O   . PHE   B 1 147 ? -39.138 3.725   52.577  1.00 19.33 ?  142 PHE   C O   1 
ATOM   2675 C  CB  . PHE   B 1 147 ? -41.187 4.758   50.800  1.00 16.86 ?  142 PHE   C CB  1 
ATOM   2676 C  CG  . PHE   B 1 147 ? -42.537 4.785   50.128  1.00 17.50 ?  142 PHE   C CG  1 
ATOM   2677 C  CD1 . PHE   B 1 147 ? -43.321 3.651   50.086  1.00 19.50 ?  142 PHE   C CD1 1 
ATOM   2678 C  CD2 . PHE   B 1 147 ? -43.039 5.954   49.581  1.00 18.42 ?  142 PHE   C CD2 1 
ATOM   2679 C  CE1 . PHE   B 1 147 ? -44.604 3.701   49.553  1.00 17.72 ?  142 PHE   C CE1 1 
ATOM   2680 C  CE2 . PHE   B 1 147 ? -44.328 6.012   49.047  1.00 16.90 ?  142 PHE   C CE2 1 
ATOM   2681 C  CZ  . PHE   B 1 147 ? -45.089 4.867   49.004  1.00 18.29 ?  142 PHE   C CZ  1 
ATOM   2682 N  N   . GLY   B 1 148 ? -39.533 5.665   53.626  1.00 16.40 ?  143 GLY   C N   1 
ATOM   2683 C  CA  . GLY   B 1 148 ? -38.107 5.852   53.971  1.00 15.64 ?  143 GLY   C CA  1 
ATOM   2684 C  C   . GLY   B 1 148 ? -37.807 5.509   55.427  1.00 18.16 ?  143 GLY   C C   1 
ATOM   2685 O  O   . GLY   B 1 148 ? -38.343 4.522   55.968  1.00 19.85 ?  143 GLY   C O   1 
ATOM   2686 N  N   . ALA   B 1 149 ? -36.860 6.246   55.993  1.00 19.66 ?  144 ALA   C N   1 
ATOM   2687 C  CA  . ALA   B 1 149 ? -36.200 5.896   57.261  1.00 20.81 ?  144 ALA   C CA  1 
ATOM   2688 C  C   . ALA   B 1 149 ? -35.809 7.190   57.992  1.00 21.86 ?  144 ALA   C C   1 
ATOM   2689 O  O   . ALA   B 1 149 ? -34.694 7.297   58.515  1.00 24.16 ?  144 ALA   C O   1 
ATOM   2690 C  CB  . ALA   B 1 149 ? -35.041 4.999   56.896  1.00 22.50 ?  144 ALA   C CB  1 
ATOM   2691 N  N   . GLY   B 1 150 ? -36.675 8.191   57.953  1.00 21.97 ?  145 GLY   C N   1 
ATOM   2692 C  CA  . GLY   B 1 150 ? -36.534 9.396   58.767  1.00 20.68 ?  145 GLY   C CA  1 
ATOM   2693 C  C   . GLY   B 1 150 ? -35.393 10.299  58.303  1.00 24.08 ?  145 GLY   C C   1 
ATOM   2694 O  O   . GLY   B 1 150 ? -34.943 11.122  59.117  1.00 24.05 ?  145 GLY   C O   1 
ATOM   2695 N  N   . TRP   B 1 151 ? -34.960 10.212  57.047  1.00 20.79 ?  146 TRP   C N   1 
ATOM   2696 C  CA  . TRP   B 1 151 ? -33.887 11.072  56.518  1.00 20.07 ?  146 TRP   C CA  1 
ATOM   2697 C  C   . TRP   B 1 151 ? -34.331 12.543  56.506  1.00 20.63 ?  146 TRP   C C   1 
ATOM   2698 O  O   . TRP   B 1 151 ? -35.457 12.884  56.062  1.00 20.54 ?  146 TRP   C O   1 
ATOM   2699 C  CB  . TRP   B 1 151 ? -33.461 10.655  55.130  1.00 19.41 ?  146 TRP   C CB  1 
ATOM   2700 C  CG  . TRP   B 1 151 ? -32.397 11.526  54.536  1.00 18.90 ?  146 TRP   C CG  1 
ATOM   2701 C  CD1 . TRP   B 1 151 ? -31.068 11.551  54.858  1.00 20.20 ?  146 TRP   C CD1 1 
ATOM   2702 C  CD2 . TRP   B 1 151 ? -32.567 12.453  53.456  1.00 20.12 ?  146 TRP   C CD2 1 
ATOM   2703 N  NE1 . TRP   B 1 151 ? -30.402 12.432  54.056  1.00 20.77 ?  146 TRP   C NE1 1 
ATOM   2704 C  CE2 . TRP   B 1 151 ? -31.294 12.994  53.169  1.00 20.16 ?  146 TRP   C CE2 1 
ATOM   2705 C  CE3 . TRP   B 1 151 ? -33.666 12.841  52.693  1.00 18.52 ?  146 TRP   C CE3 1 
ATOM   2706 C  CZ2 . TRP   B 1 151 ? -31.096 13.914  52.146  1.00 21.81 ?  146 TRP   C CZ2 1 
ATOM   2707 C  CZ3 . TRP   B 1 151 ? -33.471 13.775  51.694  1.00 18.80 ?  146 TRP   C CZ3 1 
ATOM   2708 C  CH2 . TRP   B 1 151 ? -32.198 14.272  51.407  1.00 21.09 ?  146 TRP   C CH2 1 
ATOM   2709 N  N   . ASP   B 1 152 ? -33.435 13.404  56.971  1.00 21.11 ?  147 ASP   C N   1 
ATOM   2710 C  CA  . ASP   B 1 152 ? -33.690 14.854  57.121  1.00 21.83 ?  147 ASP   C CA  1 
ATOM   2711 C  C   . ASP   B 1 152 ? -33.029 15.529  55.927  1.00 21.21 ?  147 ASP   C C   1 
ATOM   2712 O  O   . ASP   B 1 152 ? -31.777 15.443  55.776  1.00 21.27 ?  147 ASP   C O   1 
ATOM   2713 C  CB  . ASP   B 1 152 ? -33.137 15.372  58.459  1.00 23.52 ?  147 ASP   C CB  1 
ATOM   2714 C  CG  . ASP   B 1 152 ? -33.391 16.842  58.729  1.00 28.70 ?  147 ASP   C CG  1 
ATOM   2715 O  OD1 . ASP   B 1 152 ? -33.944 17.554  57.854  1.00 28.48 ?  147 ASP   C OD1 1 
ATOM   2716 O  OD2 . ASP   B 1 152 ? -32.949 17.291  59.801  1.00 35.13 -1 147 ASP   C OD2 1 
ATOM   2717 N  N   . MET   B 1 153 ? -33.823 16.131  55.046  1.00 22.48 ?  148 MET   C N   1 
ATOM   2718 C  CA  . MET   B 1 153 ? -33.289 16.797  53.822  1.00 22.67 ?  148 MET   C CA  1 
ATOM   2719 C  C   . MET   B 1 153 ? -32.576 18.133  54.131  1.00 22.46 ?  148 MET   C C   1 
ATOM   2720 O  O   . MET   B 1 153 ? -31.929 18.644  53.205  1.00 21.95 ?  148 MET   C O   1 
ATOM   2721 C  CB  . MET   B 1 153 ? -34.403 17.098  52.823  1.00 23.32 ?  148 MET   C CB  1 
ATOM   2722 C  CG  . MET   B 1 153 ? -35.338 18.163  53.251  1.00 27.90 ?  148 MET   C CG  1 
ATOM   2723 S  SD  . MET   B 1 153 ? -36.681 18.457  52.031  1.00 25.50 ?  148 MET   C SD  1 
ATOM   2724 C  CE  . MET   B 1 153 ? -38.078 17.757  52.898  1.00 26.01 ?  148 MET   C CE  1 
ATOM   2725 N  N   . THR   B 1 154 ? -32.628 18.644  55.366  1.00 23.90 ?  149 THR   C N   1 
ATOM   2726 C  CA  . THR   B 1 154 ? -32.206 20.039  55.708  1.00 25.49 ?  149 THR   C CA  1 
ATOM   2727 C  C   . THR   B 1 154 ? -30.774 20.264  55.221  1.00 26.79 ?  149 THR   C C   1 
ATOM   2728 O  O   . THR   B 1 154 ? -30.517 21.257  54.502  1.00 26.79 ?  149 THR   C O   1 
ATOM   2729 C  CB  . THR   B 1 154 ? -32.298 20.302  57.216  1.00 26.63 ?  149 THR   C CB  1 
ATOM   2730 O  OG1 . THR   B 1 154 ? -33.685 20.239  57.516  1.00 26.90 ?  149 THR   C OG1 1 
ATOM   2731 C  CG2 . THR   B 1 154 ? -31.746 21.655  57.628  1.00 29.24 ?  149 THR   C CG2 1 
ATOM   2732 N  N   . GLY   B 1 155 ? -29.870 19.368  55.562  1.00 23.48 ?  150 GLY   C N   1 
ATOM   2733 C  CA  . GLY   B 1 155 ? -28.455 19.528  55.158  1.00 23.04 ?  150 GLY   C CA  1 
ATOM   2734 C  C   . GLY   B 1 155 ? -28.185 19.316  53.668  1.00 24.87 ?  150 GLY   C C   1 
ATOM   2735 O  O   . GLY   B 1 155 ? -26.986 19.433  53.241  1.00 26.88 ?  150 GLY   C O   1 
ATOM   2736 N  N   . SER   B 1 156 ? -29.194 18.967  52.873  1.00 21.30 ?  151 SER   C N   1 
ATOM   2737 C  CA  . SER   B 1 156 ? -29.000 18.715  51.424  1.00 21.23 ?  151 SER   C CA  1 
ATOM   2738 C  C   . SER   B 1 156 ? -29.712 19.798  50.605  1.00 21.68 ?  151 SER   C C   1 
ATOM   2739 O  O   . SER   B 1 156 ? -29.636 19.691  49.362  1.00 21.84 ?  151 SER   C O   1 
ATOM   2740 C  CB  . SER   B 1 156 ? -29.454 17.325  51.028  1.00 21.50 ?  151 SER   C CB  1 
ATOM   2741 O  OG  . SER   B 1 156 ? -28.647 16.344  51.634  1.00 20.93 ?  151 SER   C OG  1 
ATOM   2742 N  N   . LEU   B 1 157 ? -30.371 20.771  51.239  1.00 23.64 ?  152 LEU   C N   1 
ATOM   2743 C  CA  . LEU   B 1 157 ? -31.113 21.823  50.470  1.00 26.84 ?  152 LEU   C CA  1 
ATOM   2744 C  C   . LEU   B 1 157 ? -30.174 22.596  49.534  1.00 27.84 ?  152 LEU   C C   1 
ATOM   2745 O  O   . LEU   B 1 157 ? -30.623 22.930  48.434  1.00 26.75 ?  152 LEU   C O   1 
ATOM   2746 C  CB  . LEU   B 1 157 ? -31.862 22.743  51.416  1.00 28.42 ?  152 LEU   C CB  1 
ATOM   2747 C  CG  . LEU   B 1 157 ? -32.921 22.065  52.271  1.00 32.50 ?  152 LEU   C CG  1 
ATOM   2748 C  CD1 . LEU   B 1 157 ? -33.560 23.074  53.223  1.00 31.76 ?  152 LEU   C CD1 1 
ATOM   2749 C  CD2 . LEU   B 1 157 ? -33.953 21.367  51.405  1.00 30.34 ?  152 LEU   C CD2 1 
ATOM   2750 N  N   . ASP   B 1 158 ? -28.931 22.910  49.914  1.00 27.19 ?  153 ASP   C N   1 
ATOM   2751 C  CA  . ASP   B 1 158 ? -28.010 23.618  48.980  1.00 29.78 ?  153 ASP   C CA  1 
ATOM   2752 C  C   . ASP   B 1 158 ? -27.735 22.726  47.768  1.00 25.33 ?  153 ASP   C C   1 
ATOM   2753 O  O   . ASP   B 1 158 ? -27.715 23.235  46.610  1.00 22.49 ?  153 ASP   C O   1 
ATOM   2754 C  CB  . ASP   B 1 158 ? -26.693 24.031  49.649  1.00 33.62 ?  153 ASP   C CB  1 
ATOM   2755 C  CG  . ASP   B 1 158 ? -26.799 25.260  50.546  1.00 39.76 ?  153 ASP   C CG  1 
ATOM   2756 O  OD1 . ASP   B 1 158 ? -27.891 25.880  50.603  1.00 39.11 ?  153 ASP   C OD1 1 
ATOM   2757 O  OD2 . ASP   B 1 158 ? -25.777 25.594  51.176  1.00 47.55 -1 153 ASP   C OD2 1 
ATOM   2758 N  N   . TYR   B 1 159 ? -27.566 21.416  47.984  1.00 22.39 ?  154 TYR   C N   1 
ATOM   2759 C  CA  . TYR   B 1 159 ? -27.351 20.435  46.899  1.00 19.91 ?  154 TYR   C CA  1 
ATOM   2760 C  C   . TYR   B 1 159 ? -28.583 20.445  45.993  1.00 18.74 ?  154 TYR   C C   1 
ATOM   2761 O  O   . TYR   B 1 159 ? -28.443 20.410  44.765  1.00 21.78 ?  154 TYR   C O   1 
ATOM   2762 C  CB  . TYR   B 1 159 ? -27.042 19.046  47.473  1.00 19.38 ?  154 TYR   C CB  1 
ATOM   2763 C  CG  . TYR   B 1 159 ? -26.969 17.971  46.434  1.00 20.22 ?  154 TYR   C CG  1 
ATOM   2764 C  CD1 . TYR   B 1 159 ? -25.974 17.952  45.463  1.00 21.79 ?  154 TYR   C CD1 1 
ATOM   2765 C  CD2 . TYR   B 1 159 ? -27.865 16.907  46.459  1.00 22.28 ?  154 TYR   C CD2 1 
ATOM   2766 C  CE1 . TYR   B 1 159 ? -25.903 16.937  44.524  1.00 25.34 ?  154 TYR   C CE1 1 
ATOM   2767 C  CE2 . TYR   B 1 159 ? -27.818 15.900  45.509  1.00 23.31 ?  154 TYR   C CE2 1 
ATOM   2768 C  CZ  . TYR   B 1 159 ? -26.845 15.920  44.533  1.00 25.04 ?  154 TYR   C CZ  1 
ATOM   2769 O  OH  . TYR   B 1 159 ? -26.796 14.935  43.603  1.00 28.07 ?  154 TYR   C OH  1 
ATOM   2770 N  N   . PHE   B 1 160 ? -29.765 20.469  46.572  1.00 19.93 ?  155 PHE   C N   1 
ATOM   2771 C  CA  . PHE   B 1 160 ? -30.975 20.454  45.746  1.00 17.73 ?  155 PHE   C CA  1 
ATOM   2772 C  C   . PHE   B 1 160 ? -30.893 21.668  44.802  1.00 19.68 ?  155 PHE   C C   1 
ATOM   2773 O  O   . PHE   B 1 160 ? -31.248 21.555  43.631  1.00 20.54 ?  155 PHE   C O   1 
ATOM   2774 C  CB  . PHE   B 1 160 ? -32.253 20.505  46.581  1.00 16.75 ?  155 PHE   C CB  1 
ATOM   2775 C  CG  . PHE   B 1 160 ? -32.601 19.294  47.433  1.00 17.17 ?  155 PHE   C CG  1 
ATOM   2776 C  CD1 . PHE   B 1 160 ? -31.782 18.187  47.539  1.00 19.14 ?  155 PHE   C CD1 1 
ATOM   2777 C  CD2 . PHE   B 1 160 ? -33.805 19.293  48.133  1.00 17.47 ?  155 PHE   C CD2 1 
ATOM   2778 C  CE1 . PHE   B 1 160 ? -32.141 17.124  48.356  1.00 17.56 ?  155 PHE   C CE1 1 
ATOM   2779 C  CE2 . PHE   B 1 160 ? -34.182 18.227  48.930  1.00 17.44 ?  155 PHE   C CE2 1 
ATOM   2780 C  CZ  . PHE   B 1 160 ? -33.381 17.125  48.992  1.00 17.13 ?  155 PHE   C CZ  1 
ATOM   2781 N  N   . ARG   B 1 161 ? -30.534 22.839  45.343  1.00 20.88 ?  156 ARG   C N   1 
ATOM   2782 C  CA  . ARG   B 1 161 ? -30.549 24.084  44.531  1.00 20.96 ?  156 ARG   C CA  1 
ATOM   2783 C  C   . ARG   B 1 161 ? -29.510 23.951  43.432  1.00 22.20 ?  156 ARG   C C   1 
ATOM   2784 O  O   . ARG   B 1 161 ? -29.761 24.418  42.290  1.00 21.88 ?  156 ARG   C O   1 
ATOM   2785 C  CB  . ARG   B 1 161 ? -30.303 25.286  45.446  1.00 24.23 ?  156 ARG   C CB  1 
ATOM   2786 C  CG  . ARG   B 1 161 ? -31.530 25.643  46.280  1.00 28.53 ?  156 ARG   C CG  1 
ATOM   2787 C  CD  . ARG   B 1 161 ? -31.131 26.707  47.289  1.00 37.66 ?  156 ARG   C CD  1 
ATOM   2788 N  NE  . ARG   B 1 161 ? -32.287 27.434  47.769  1.00 45.86 ?  156 ARG   C NE  1 
ATOM   2789 C  CZ  . ARG   B 1 161 ? -32.886 27.274  48.946  1.00 50.01 ?  156 ARG   C CZ  1 
ATOM   2790 N  NH1 . ARG   B 1 161 ? -32.447 26.381  49.821  1.00 48.28 1  156 ARG   C NH1 1 
ATOM   2791 N  NH2 . ARG   B 1 161 ? -33.938 28.029  49.233  1.00 51.32 ?  156 ARG   C NH2 1 
ATOM   2792 N  N   . ARG   B 1 162 ? -28.381 23.320  43.725  1.00 20.86 ?  157 ARG   C N   1 
ATOM   2793 C  CA  . ARG   B 1 162 ? -27.296 23.130  42.736  1.00 24.65 ?  157 ARG   C CA  1 
ATOM   2794 C  C   . ARG   B 1 162 ? -27.786 22.268  41.546  1.00 22.27 ?  157 ARG   C C   1 
ATOM   2795 O  O   . ARG   B 1 162 ? -27.396 22.557  40.389  1.00 22.16 ?  157 ARG   C O   1 
ATOM   2796 C  CB  . ARG   B 1 162 ? -26.082 22.533  43.457  1.00 28.50 ?  157 ARG   C CB  1 
ATOM   2797 C  CG  . ARG   B 1 162 ? -24.755 23.232  43.223  1.00 37.35 ?  157 ARG   C CG  1 
ATOM   2798 C  CD  . ARG   B 1 162 ? -23.936 23.279  44.503  1.00 35.69 ?  157 ARG   C CD  1 
ATOM   2799 N  NE  . ARG   B 1 162 ? -23.708 21.976  45.145  1.00 39.87 ?  157 ARG   C NE  1 
ATOM   2800 C  CZ  . ARG   B 1 162 ? -23.780 21.749  46.463  1.00 36.40 ?  157 ARG   C CZ  1 
ATOM   2801 N  NH1 . ARG   B 1 162 ? -24.094 22.722  47.306  1.00 40.23 1  157 ARG   C NH1 1 
ATOM   2802 N  NH2 . ARG   B 1 162 ? -23.550 20.535  46.931  1.00 33.11 ?  157 ARG   C NH2 1 
ATOM   2803 N  N   . ILE   B 1 163 ? -28.635 21.258  41.767  1.00 22.60 ?  158 ILE   C N   1 
ATOM   2804 C  CA  . ILE   B 1 163 ? -29.035 20.338  40.669  1.00 20.33 ?  158 ILE   C CA  1 
ATOM   2805 C  C   . ILE   B 1 163 ? -30.433 20.711  40.124  1.00 19.71 ?  158 ILE   C C   1 
ATOM   2806 O  O   . ILE   B 1 163 ? -30.807 20.148  39.105  1.00 20.05 ?  158 ILE   C O   1 
ATOM   2807 C  CB  . ILE   B 1 163 ? -28.949 18.867  41.136  1.00 21.47 ?  158 ILE   C CB  1 
ATOM   2808 C  CG1 . ILE   B 1 163 ? -29.924 18.531  42.249  1.00 20.95 ?  158 ILE   C CG1 1 
ATOM   2809 C  CG2 . ILE   B 1 163 ? -27.526 18.495  41.518  1.00 20.78 ?  158 ILE   C CG2 1 
ATOM   2810 C  CD1 . ILE   B 1 163 ? -30.048 17.022  42.495  1.00 22.31 ?  158 ILE   C CD1 1 
ATOM   2811 N  N   . LEU   B 1 164 ? -31.107 21.650  40.745  1.00 19.80 ?  159 LEU   C N   1 
ATOM   2812 C  CA  . LEU   B 1 164 ? -32.462 22.153  40.379  1.00 19.90 ?  159 LEU   C CA  1 
ATOM   2813 C  C   . LEU   B 1 164 ? -32.607 22.454  38.881  1.00 20.00 ?  159 LEU   C C   1 
ATOM   2814 O  O   . LEU   B 1 164 ? -33.687 22.238  38.320  1.00 18.10 ?  159 LEU   C O   1 
ATOM   2815 C  CB  . LEU   B 1 164 ? -32.758 23.421  41.164  1.00 20.47 ?  159 LEU   C CB  1 
ATOM   2816 C  CG  . LEU   B 1 164 ? -34.245 23.745  41.352  1.00 18.97 ?  159 LEU   C CG  1 
ATOM   2817 C  CD1 . LEU   B 1 164 ? -34.952 22.586  42.053  1.00 21.25 ?  159 LEU   C CD1 1 
ATOM   2818 C  CD2 . LEU   B 1 164 ? -34.358 25.001  42.163  1.00 22.22 ?  159 LEU   C CD2 1 
ATOM   2819 N  N   . PRO   B 1 165 ? -31.625 23.020  38.156  1.00 20.57 ?  160 PRO   C N   1 
ATOM   2820 C  CA  . PRO   B 1 165 ? -31.869 23.384  36.750  1.00 19.47 ?  160 PRO   C CA  1 
ATOM   2821 C  C   . PRO   B 1 165 ? -32.318 22.219  35.848  1.00 20.13 ?  160 PRO   C C   1 
ATOM   2822 O  O   . PRO   B 1 165 ? -32.966 22.480  34.858  1.00 19.68 ?  160 PRO   C O   1 
ATOM   2823 C  CB  . PRO   B 1 165 ? -30.494 23.939  36.357  1.00 20.95 ?  160 PRO   C CB  1 
ATOM   2824 C  CG  . PRO   B 1 165 ? -30.080 24.633  37.597  1.00 21.30 ?  160 PRO   C CG  1 
ATOM   2825 C  CD  . PRO   B 1 165 ? -30.336 23.569  38.650  1.00 22.81 ?  160 PRO   C CD  1 
ATOM   2826 N  N   . GLY   B 1 166 ? -31.988 20.984  36.209  1.00 18.48 ?  161 GLY   C N   1 
ATOM   2827 C  CA  . GLY   B 1 166 ? -32.337 19.779  35.433  1.00 17.63 ?  161 GLY   C CA  1 
ATOM   2828 C  C   . GLY   B 1 166 ? -33.790 19.358  35.657  1.00 17.43 ?  161 GLY   C C   1 
ATOM   2829 O  O   . GLY   B 1 166 ? -34.291 18.567  34.893  1.00 18.74 ?  161 GLY   C O   1 
ATOM   2830 N  N   . VAL   B 1 167 ? -34.426 19.858  36.684  1.00 16.96 ?  162 VAL   C N   1 
ATOM   2831 C  CA  . VAL   B 1 167 ? -35.791 19.424  37.053  1.00 17.36 ?  162 VAL   C CA  1 
ATOM   2832 C  C   . VAL   B 1 167 ? -36.815 20.041  36.100  1.00 16.84 ?  162 VAL   C C   1 
ATOM   2833 O  O   . VAL   B 1 167 ? -36.803 21.269  35.916  1.00 16.57 ?  162 VAL   C O   1 
ATOM   2834 C  CB  . VAL   B 1 167 ? -36.100 19.766  38.510  1.00 16.96 ?  162 VAL   C CB  1 
ATOM   2835 C  CG1 . VAL   B 1 167 ? -37.505 19.305  38.891  1.00 17.24 ?  162 VAL   C CG1 1 
ATOM   2836 C  CG2 . VAL   B 1 167 ? -35.037 19.223  39.465  1.00 18.23 ?  162 VAL   C CG2 1 
ATOM   2837 N  N   . GLY   B 1 168 ? -37.660 19.185  35.530  1.00 16.96 ?  163 GLY   C N   1 
ATOM   2838 C  CA  . GLY   B 1 168 ? -38.910 19.561  34.893  1.00 16.88 ?  163 GLY   C CA  1 
ATOM   2839 C  C   . GLY   B 1 168 ? -40.081 19.273  35.819  1.00 16.56 ?  163 GLY   C C   1 
ATOM   2840 O  O   . GLY   B 1 168 ? -40.630 18.139  35.784  1.00 18.60 ?  163 GLY   C O   1 
ATOM   2841 N  N   . ALA   B 1 169 ? -40.483 20.254  36.601  1.00 16.50 ?  164 ALA   C N   1 
ATOM   2842 C  CA  . ALA   B 1 169 ? -41.587 20.098  37.554  1.00 15.98 ?  164 ALA   C CA  1 
ATOM   2843 C  C   . ALA   B 1 169 ? -42.870 20.350  36.802  1.00 14.59 ?  164 ALA   C C   1 
ATOM   2844 O  O   . ALA   B 1 169 ? -42.898 21.134  35.843  1.00 18.28 ?  164 ALA   C O   1 
ATOM   2845 C  CB  . ALA   B 1 169 ? -41.452 20.988  38.770  1.00 18.74 ?  164 ALA   C CB  1 
ATOM   2846 N  N   . PHE   B 1 170 ? -43.940 19.706  37.232  1.00 16.91 ?  165 PHE   C N   1 
ATOM   2847 C  CA  . PHE   B 1 170 ? -45.246 19.934  36.598  1.00 16.60 ?  165 PHE   C CA  1 
ATOM   2848 C  C   . PHE   B 1 170 ? -46.384 19.838  37.599  1.00 18.75 ?  165 PHE   C C   1 
ATOM   2849 O  O   . PHE   B 1 170 ? -46.263 19.342  38.723  1.00 19.19 ?  165 PHE   C O   1 
ATOM   2850 C  CB  . PHE   B 1 170 ? -45.379 19.004  35.398  1.00 18.42 ?  165 PHE   C CB  1 
ATOM   2851 C  CG  . PHE   B 1 170 ? -45.374 17.542  35.752  1.00 19.37 ?  165 PHE   C CG  1 
ATOM   2852 C  CD1 . PHE   B 1 170 ? -46.539 16.930  36.171  1.00 20.08 ?  165 PHE   C CD1 1 
ATOM   2853 C  CD2 . PHE   B 1 170 ? -44.231 16.774  35.570  1.00 20.46 ?  165 PHE   C CD2 1 
ATOM   2854 C  CE1 . PHE   B 1 170 ? -46.524 15.579  36.509  1.00 20.95 ?  165 PHE   C CE1 1 
ATOM   2855 C  CE2 . PHE   B 1 170 ? -44.213 15.433  35.931  1.00 21.93 ?  165 PHE   C CE2 1 
ATOM   2856 C  CZ  . PHE   B 1 170 ? -45.366 14.829  36.360  1.00 22.83 ?  165 PHE   C CZ  1 
ATOM   2857 N  N   . ARG   B 1 171 ? -47.530 20.264  37.081  1.00 18.64 ?  166 ARG   C N   1 
ATOM   2858 C  CA  . ARG   B 1 171 ? -48.821 20.288  37.794  1.00 20.96 ?  166 ARG   C CA  1 
ATOM   2859 C  C   . ARG   B 1 171 ? -49.837 19.601  36.884  1.00 20.39 ?  166 ARG   C C   1 
ATOM   2860 O  O   . ARG   B 1 171 ? -49.902 19.913  35.671  1.00 23.16 ?  166 ARG   C O   1 
ATOM   2861 C  CB  . ARG   B 1 171 ? -49.243 21.716  38.133  1.00 21.07 ?  166 ARG   C CB  1 
ATOM   2862 C  CG  . ARG   B 1 171 ? -48.235 22.451  38.983  1.00 23.11 ?  166 ARG   C CG  1 
ATOM   2863 C  CD  . ARG   B 1 171 ? -48.247 21.954  40.402  1.00 22.54 ?  166 ARG   C CD  1 
ATOM   2864 N  NE  . ARG   B 1 171 ? -47.356 22.716  41.248  1.00 24.90 ?  166 ARG   C NE  1 
ATOM   2865 C  CZ  . ARG   B 1 171 ? -46.095 22.377  41.551  1.00 24.17 ?  166 ARG   C CZ  1 
ATOM   2866 N  NH1 . ARG   B 1 171 ? -45.525 21.273  41.087  1.00 23.09 1  166 ARG   C NH1 1 
ATOM   2867 N  NH2 . ARG   B 1 171 ? -45.435 23.164  42.362  1.00 25.73 ?  166 ARG   C NH2 1 
ATOM   2868 N  N   . LEU   B 1 172 ? -50.584 18.665  37.459  1.00 20.95 ?  167 LEU   C N   1 
ATOM   2869 C  CA  . LEU   B 1 172 ? -51.616 17.912  36.712  1.00 22.71 ?  167 LEU   C CA  1 
ATOM   2870 C  C   . LEU   B 1 172 ? -52.941 18.108  37.448  1.00 22.47 ?  167 LEU   C C   1 
ATOM   2871 O  O   . LEU   B 1 172 ? -53.141 17.552  38.516  1.00 20.27 ?  167 LEU   C O   1 
ATOM   2872 C  CB  . LEU   B 1 172 ? -51.209 16.443  36.593  1.00 25.69 ?  167 LEU   C CB  1 
ATOM   2873 C  CG  . LEU   B 1 172 ? -52.155 15.585  35.755  1.00 26.16 ?  167 LEU   C CG  1 
ATOM   2874 C  CD1 . LEU   B 1 172 ? -52.342 16.193  34.374  1.00 30.67 ?  167 LEU   C CD1 1 
ATOM   2875 C  CD2 . LEU   B 1 172 ? -51.631 14.172  35.631  1.00 26.55 ?  167 LEU   C CD2 1 
ATOM   2876 N  N   . ARG   B 1 173 ? -53.814 18.914  36.858  1.00 26.69 ?  168 ARG   C N   1 
ATOM   2877 C  CA  . ARG   B 1 173 ? -55.181 19.216  37.335  1.00 27.57 ?  168 ARG   C CA  1 
ATOM   2878 C  C   . ARG   B 1 173 ? -56.048 18.020  36.939  1.00 19.95 ?  168 ARG   C C   1 
ATOM   2879 O  O   . ARG   B 1 173 ? -56.136 17.754  35.780  1.00 23.22 ?  168 ARG   C O   1 
ATOM   2880 C  CB  . ARG   B 1 173 ? -55.651 20.507  36.656  1.00 32.53 ?  168 ARG   C CB  1 
ATOM   2881 C  CG  . ARG   B 1 173 ? -57.046 20.984  37.039  1.00 43.63 ?  168 ARG   C CG  1 
ATOM   2882 C  CD  . ARG   B 1 173 ? -57.350 21.045  38.522  1.00 50.32 ?  168 ARG   C CD  1 
ATOM   2883 N  NE  . ARG   B 1 173 ? -58.398 22.002  38.930  1.00 59.68 ?  168 ARG   C NE  1 
ATOM   2884 C  CZ  . ARG   B 1 173 ? -59.708 21.946  38.616  1.00 62.30 ?  168 ARG   C CZ  1 
ATOM   2885 N  NH1 . ARG   B 1 173 ? -60.196 21.011  37.815  1.00 61.73 1  168 ARG   C NH1 1 
ATOM   2886 N  NH2 . ARG   B 1 173 ? -60.538 22.858  39.092  1.00 67.11 ?  168 ARG   C NH2 1 
ATOM   2887 N  N   . VAL   B 1 174 ? -56.545 17.280  37.913  1.00 22.29 ?  169 VAL   C N   1 
ATOM   2888 C  CA  . VAL   B 1 174 ? -57.235 15.985  37.672  1.00 21.17 ?  169 VAL   C CA  1 
ATOM   2889 C  C   . VAL   B 1 174 ? -58.663 16.295  37.218  1.00 19.23 ?  169 VAL   C C   1 
ATOM   2890 O  O   . VAL   B 1 174 ? -59.429 16.754  38.042  1.00 20.29 ?  169 VAL   C O   1 
ATOM   2891 C  CB  . VAL   B 1 174 ? -57.217 15.093  38.911  1.00 21.08 ?  169 VAL   C CB  1 
ATOM   2892 C  CG1 . VAL   B 1 174 ? -57.959 13.802  38.588  1.00 22.29 ?  169 VAL   C CG1 1 
ATOM   2893 C  CG2 . VAL   B 1 174 ? -55.756 14.805  39.288  1.00 21.51 ?  169 VAL   C CG2 1 
ATOM   2894 N  N   . ALA   B 1 175 ? -58.921 16.111  35.930  1.00 21.73 ?  170 ALA   C N   1 
ATOM   2895 C  CA  . ALA   B 1 175 ? -60.272 16.250  35.327  1.00 21.83 ?  170 ALA   C CA  1 
ATOM   2896 C  C   . ALA   B 1 175 ? -61.078 14.951  35.461  1.00 24.36 ?  170 ALA   C C   1 
ATOM   2897 O  O   . ALA   B 1 175 ? -62.324 15.017  35.573  1.00 25.01 ?  170 ALA   C O   1 
ATOM   2898 C  CB  . ALA   B 1 175 ? -60.111 16.608  33.888  1.00 21.70 ?  170 ALA   C CB  1 
ATOM   2899 N  N   . GLU   B 1 176 ? -60.413 13.804  35.304  1.00 23.35 ?  171 GLU   C N   1 
ATOM   2900 C  CA  . GLU   B 1 176 ? -61.036 12.454  35.262  1.00 24.92 ?  171 GLU   C CA  1 
ATOM   2901 C  C   . GLU   B 1 176 ? -60.190 11.526  36.134  1.00 21.32 ?  171 GLU   C C   1 
ATOM   2902 O  O   . GLU   B 1 176 ? -58.955 11.582  36.043  1.00 19.57 ?  171 GLU   C O   1 
ATOM   2903 C  CB  . GLU   B 1 176 ? -61.026 11.853  33.850  1.00 30.60 ?  171 GLU   C CB  1 
ATOM   2904 C  CG  . GLU   B 1 176 ? -62.175 12.256  32.936  1.00 40.79 ?  171 GLU   C CG  1 
ATOM   2905 C  CD  . GLU   B 1 176 ? -62.466 11.165  31.905  1.00 51.48 ?  171 GLU   C CD  1 
ATOM   2906 O  OE1 . GLU   B 1 176 ? -62.238 11.410  30.691  1.00 61.02 ?  171 GLU   C OE1 1 
ATOM   2907 O  OE2 . GLU   B 1 176 ? -62.902 10.043  32.321  1.00 60.92 -1 171 GLU   C OE2 1 
ATOM   2908 N  N   . ALA   B 1 177 ? -60.793 10.665  36.920  1.00 21.34 ?  172 ALA   C N   1 
ATOM   2909 C  CA  . ALA   B 1 177 ? -60.032 9.636   37.681  1.00 22.18 ?  172 ALA   C CA  1 
ATOM   2910 C  C   . ALA   B 1 177 ? -60.830 8.354   37.686  1.00 24.46 ?  172 ALA   C C   1 
ATOM   2911 O  O   . ALA   B 1 177 ? -62.057 8.383   37.979  1.00 25.16 ?  172 ALA   C O   1 
ATOM   2912 C  CB  . ALA   B 1 177 ? -59.729 10.083  39.079  1.00 22.37 ?  172 ALA   C CB  1 
ATOM   2913 N  N   . ASP   B 1 178 ? -60.158 7.262   37.345  1.00 23.82 ?  173 ASP   C N   1 
ATOM   2914 C  CA  . ASP   B 1 178 ? -60.765 5.922   37.217  1.00 24.31 ?  173 ASP   C CA  1 
ATOM   2915 C  C   . ASP   B 1 178 ? -59.901 4.962   38.043  1.00 22.77 ?  173 ASP   C C   1 
ATOM   2916 O  O   . ASP   B 1 178 ? -58.664 5.141   38.075  1.00 22.04 ?  173 ASP   C O   1 
ATOM   2917 C  CB  . ASP   B 1 178 ? -60.873 5.569   35.727  1.00 27.64 ?  173 ASP   C CB  1 
ATOM   2918 C  CG  . ASP   B 1 178 ? -61.920 6.399   34.979  1.00 35.18 ?  173 ASP   C CG  1 
ATOM   2919 O  OD1 . ASP   B 1 178 ? -61.534 7.226   34.046  1.00 37.13 ?  173 ASP   C OD1 1 
ATOM   2920 O  OD2 . ASP   B 1 178 ? -63.126 6.229   35.336  1.00 39.77 -1 173 ASP   C OD2 1 
ATOM   2921 N  N   . GLY   B 1 179 ? -60.537 4.024   38.722  1.00 21.69 ?  174 GLY   C N   1 
ATOM   2922 C  CA  . GLY   B 1 179 ? -59.837 3.012   39.536  1.00 22.32 ?  174 GLY   C CA  1 
ATOM   2923 C  C   . GLY   B 1 179 ? -60.309 1.596   39.239  1.00 21.08 ?  174 GLY   C C   1 
ATOM   2924 O  O   . GLY   B 1 179 ? -61.516 1.335   39.301  1.00 18.92 ?  174 GLY   C O   1 
ATOM   2925 N  N   . MET   B 1 180 ? -59.393 0.764   38.813  1.00 19.09 ?  175 MET   C N   1 
ATOM   2926 C  CA  . MET   B 1 180 ? -59.566 -0.682  38.585  1.00 19.07 ?  175 MET   C CA  1 
ATOM   2927 C  C   . MET   B 1 180 ? -59.182 -1.384  39.881  1.00 17.98 ?  175 MET   C C   1 
ATOM   2928 O  O   . MET   B 1 180 ? -57.954 -1.392  40.250  1.00 20.43 ?  175 MET   C O   1 
ATOM   2929 C  CB  . MET   B 1 180 ? -58.682 -1.176  37.434  1.00 22.20 ?  175 MET   C CB  1 
ATOM   2930 C  CG  . MET   B 1 180 ? -58.719 -2.650  37.203  1.00 23.88 ?  175 MET   C CG  1 
ATOM   2931 S  SD  . MET   B 1 180 ? -60.212 -3.230  36.325  1.00 26.16 ?  175 MET   C SD  1 
ATOM   2932 C  CE  . MET   B 1 180 ? -59.825 -2.603  34.704  1.00 23.82 ?  175 MET   C CE  1 
ATOM   2933 N  N   . PHE   B 1 181 ? -60.150 -1.996  40.561  1.00 18.23 ?  176 PHE   C N   1 
ATOM   2934 C  CA  . PHE   B 1 181 ? -59.826 -2.843  41.727  1.00 19.25 ?  176 PHE   C CA  1 
ATOM   2935 C  C   . PHE   B 1 181 ? -60.271 -4.276  41.392  1.00 20.11 ?  176 PHE   C C   1 
ATOM   2936 O  O   . PHE   B 1 181 ? -61.403 -4.708  41.761  1.00 18.39 ?  176 PHE   C O   1 
ATOM   2937 C  CB  . PHE   B 1 181 ? -60.401 -2.236  42.993  1.00 19.68 ?  176 PHE   C CB  1 
ATOM   2938 C  CG  . PHE   B 1 181 ? -59.726 -0.950  43.355  1.00 19.56 ?  176 PHE   C CG  1 
ATOM   2939 C  CD1 . PHE   B 1 181 ? -60.036 0.225   42.689  1.00 22.38 ?  176 PHE   C CD1 1 
ATOM   2940 C  CD2 . PHE   B 1 181 ? -58.705 -0.941  44.286  1.00 22.66 ?  176 PHE   C CD2 1 
ATOM   2941 C  CE1 . PHE   B 1 181 ? -59.404 1.413   43.020  1.00 23.32 ?  176 PHE   C CE1 1 
ATOM   2942 C  CE2 . PHE   B 1 181 ? -58.082 0.254   44.622  1.00 21.61 ?  176 PHE   C CE2 1 
ATOM   2943 C  CZ  . PHE   B 1 181 ? -58.424 1.416   43.976  1.00 21.56 ?  176 PHE   C CZ  1 
ATOM   2944 N  N   . LYS   B 1 182 ? -59.422 -4.958  40.617  1.00 20.26 ?  177 LYS   C N   1 
ATOM   2945 C  CA  . LYS   B 1 182 ? -59.791 -6.268  40.051  1.00 20.14 ?  177 LYS   C CA  1 
ATOM   2946 C  C   . LYS   B 1 182 ? -59.398 -7.305  41.086  1.00 19.21 ?  177 LYS   C C   1 
ATOM   2947 O  O   . LYS   B 1 182 ? -58.163 -7.662  41.214  1.00 17.00 ?  177 LYS   C O   1 
ATOM   2948 C  CB  . LYS   B 1 182 ? -59.186 -6.479  38.676  1.00 20.05 ?  177 LYS   C CB  1 
ATOM   2949 C  CG  . LYS   B 1 182 ? -59.415 -7.886  38.148  1.00 21.01 ?  177 LYS   C CG  1 
ATOM   2950 C  CD  . LYS   B 1 182 ? -59.112 -8.090  36.694  1.00 23.40 ?  177 LYS   C CD  1 
ATOM   2951 C  CE  . LYS   B 1 182 ? -59.072 -9.582  36.394  1.00 28.79 ?  177 LYS   C CE  1 
ATOM   2952 N  NZ  . LYS   B 1 182 ? -60.418 -10.182 36.389  1.00 33.93 1  177 LYS   C NZ  1 
ATOM   2953 N  N   . LEU   B 1 183 ? -60.366 -7.723  41.890  1.00 16.92 ?  178 LEU   C N   1 
ATOM   2954 C  CA  . LEU   B 1 183 ? -60.083 -8.448  43.150  1.00 18.44 ?  178 LEU   C CA  1 
ATOM   2955 C  C   . LEU   B 1 183 ? -61.060 -9.619  43.318  1.00 19.20 ?  178 LEU   C C   1 
ATOM   2956 O  O   . LEU   B 1 183 ? -61.489 -9.865  44.463  1.00 19.52 ?  178 LEU   C O   1 
ATOM   2957 C  CB  . LEU   B 1 183 ? -60.167 -7.478  44.341  1.00 19.61 ?  178 LEU   C CB  1 
ATOM   2958 C  CG  . LEU   B 1 183 ? -59.149 -6.342  44.322  1.00 20.27 ?  178 LEU   C CG  1 
ATOM   2959 C  CD1 . LEU   B 1 183 ? -59.479 -5.282  45.369  1.00 20.39 ?  178 LEU   C CD1 1 
ATOM   2960 C  CD2 . LEU   B 1 183 ? -57.755 -6.922  44.565  1.00 20.75 ?  178 LEU   C CD2 1 
ATOM   2961 N  N   . SER   B 1 184 ? -61.350 -10.338 42.239  1.00 19.05 ?  179 SER   C N   1 
ATOM   2962 C  CA  . SER   B 1 184 ? -62.174 -11.580 42.274  1.00 19.65 ?  179 SER   C CA  1 
ATOM   2963 C  C   . SER   B 1 184 ? -63.628 -11.296 42.657  1.00 21.10 ?  179 SER   C C   1 
ATOM   2964 O  O   . SER   B 1 184 ? -64.340 -12.266 42.963  1.00 22.89 ?  179 SER   C O   1 
ATOM   2965 C  CB  . SER   B 1 184 ? -61.611 -12.581 43.187  1.00 20.88 ?  179 SER   C CB  1 
ATOM   2966 O  OG  . SER   B 1 184 ? -60.377 -13.040 42.693  1.00 18.55 ?  179 SER   C OG  1 
ATOM   2967 N  N   . GLN   B 1 185 ? -64.085 -10.059 42.534  1.00 20.33 ?  180 GLN   C N   1 
ATOM   2968 C  CA  . GLN   B 1 185 ? -65.507 -9.712  42.816  1.00 22.59 ?  180 GLN   C CA  1 
ATOM   2969 C  C   . GLN   B 1 185 ? -66.465 -10.460 41.871  1.00 26.13 ?  180 GLN   C C   1 
ATOM   2970 O  O   . GLN   B 1 185 ? -67.630 -10.621 42.297  1.00 25.42 ?  180 GLN   C O   1 
ATOM   2971 C  CB  . GLN   B 1 185 ? -65.769 -8.201  42.722  1.00 22.65 ?  180 GLN   C CB  1 
ATOM   2972 C  CG  . GLN   B 1 185 ? -65.019 -7.358  43.745  1.00 21.31 ?  180 GLN   C CG  1 
ATOM   2973 C  CD  . GLN   B 1 185 ? -63.705 -6.827  43.201  1.00 19.00 ?  180 GLN   C CD  1 
ATOM   2974 O  OE1 . GLN   B 1 185 ? -62.967 -7.538  42.526  1.00 19.84 ?  180 GLN   C OE1 1 
ATOM   2975 N  NE2 . GLN   B 1 185 ? -63.433 -5.539  43.431  1.00 20.40 ?  180 GLN   C NE2 1 
ATOM   2976 N  N   . GLU   B 1 186 ? -66.029 -10.872 40.671  1.00 25.39 ?  181 GLU   C N   1 
ATOM   2977 C  CA  . GLU   B 1 186 ? -66.821 -11.644 39.667  1.00 29.39 ?  181 GLU   C CA  1 
ATOM   2978 C  C   . GLU   B 1 186 ? -67.111 -13.063 40.179  1.00 30.28 ?  181 GLU   C C   1 
ATOM   2979 O  O   . GLU   B 1 186 ? -68.108 -13.634 39.733  1.00 33.20 ?  181 GLU   C O   1 
ATOM   2980 C  CB  . GLU   B 1 186 ? -66.151 -11.652 38.279  1.00 29.10 ?  181 GLU   C CB  1 
ATOM   2981 C  CG  . GLU   B 1 186 ? -65.067 -12.702 38.036  1.00 30.98 ?  181 GLU   C CG  1 
ATOM   2982 C  CD  . GLU   B 1 186 ? -63.713 -12.504 38.721  1.00 33.09 ?  181 GLU   C CD  1 
ATOM   2983 O  OE1 . GLU   B 1 186 ? -63.509 -11.423 39.391  1.00 27.81 ?  181 GLU   C OE1 1 
ATOM   2984 O  OE2 . GLU   B 1 186 ? -62.861 -13.435 38.596  1.00 27.36 -1 181 GLU   C OE2 1 
ATOM   2985 N  N   . GLN   B 1 187 ? -66.303 -13.605 41.080  1.00 25.35 ?  182 GLN   C N   1 
ATOM   2986 C  CA  . GLN   B 1 187 ? -66.486 -14.989 41.582  1.00 25.72 ?  182 GLN   C CA  1 
ATOM   2987 C  C   . GLN   B 1 187 ? -67.577 -15.015 42.665  1.00 24.22 ?  182 GLN   C C   1 
ATOM   2988 O  O   . GLN   B 1 187 ? -67.916 -13.974 43.280  1.00 26.16 ?  182 GLN   C O   1 
ATOM   2989 C  CB  . GLN   B 1 187 ? -65.175 -15.588 42.085  1.00 23.48 ?  182 GLN   C CB  1 
ATOM   2990 C  CG  . GLN   B 1 187 ? -64.063 -15.576 41.049  1.00 24.78 ?  182 GLN   C CG  1 
ATOM   2991 C  CD  . GLN   B 1 187 ? -64.337 -16.496 39.889  1.00 25.12 ?  182 GLN   C CD  1 
ATOM   2992 O  OE1 . GLN   B 1 187 ? -64.826 -17.617 40.050  1.00 26.32 ?  182 GLN   C OE1 1 
ATOM   2993 N  NE2 . GLN   B 1 187 ? -64.093 -15.985 38.704  1.00 27.66 ?  182 GLN   C NE2 1 
ATOM   2994 N  N   . GLN   B 1 188 ? -68.115 -16.201 42.890  1.00 26.13 ?  183 GLN   C N   1 
ATOM   2995 C  CA  . GLN   B 1 188 ? -69.051 -16.480 44.002  1.00 28.68 ?  183 GLN   C CA  1 
ATOM   2996 C  C   . GLN   B 1 188 ? -68.332 -16.293 45.341  1.00 27.29 ?  183 GLN   C C   1 
ATOM   2997 O  O   . GLN   B 1 188 ? -67.110 -16.515 45.453  1.00 24.75 ?  183 GLN   C O   1 
ATOM   2998 C  CB  . GLN   B 1 188 ? -69.586 -17.900 43.819  1.00 29.59 ?  183 GLN   C CB  1 
ATOM   2999 C  CG  . GLN   B 1 188 ? -70.422 -18.086 42.564  1.00 33.96 ?  183 GLN   C CG  1 
ATOM   3000 C  CD  . GLN   B 1 188 ? -71.774 -17.448 42.760  1.00 41.78 ?  183 GLN   C CD  1 
ATOM   3001 O  OE1 . GLN   B 1 188 ? -72.196 -16.616 41.966  1.00 60.44 ?  183 GLN   C OE1 1 
ATOM   3002 N  NE2 . GLN   B 1 188 ? -72.447 -17.794 43.848  1.00 43.84 ?  183 GLN   C NE2 1 
ATOM   3003 N  N   . PRO   B 1 189 ? -69.055 -15.917 46.416  1.00 32.77 ?  184 PRO   C N   1 
ATOM   3004 C  CA  . PRO   B 1 189 ? -68.434 -15.614 47.723  1.00 34.02 ?  184 PRO   C CA  1 
ATOM   3005 C  C   . PRO   B 1 189 ? -67.458 -16.645 48.309  1.00 33.51 ?  184 PRO   C C   1 
ATOM   3006 O  O   . PRO   B 1 189 ? -66.410 -16.245 48.784  1.00 33.46 ?  184 PRO   C O   1 
ATOM   3007 C  CB  . PRO   B 1 189 ? -69.645 -15.449 48.653  1.00 35.68 ?  184 PRO   C CB  1 
ATOM   3008 C  CG  . PRO   B 1 189 ? -70.715 -14.917 47.724  1.00 35.83 ?  184 PRO   C CG  1 
ATOM   3009 C  CD  . PRO   B 1 189 ? -70.521 -15.705 46.440  1.00 35.00 ?  184 PRO   C CD  1 
ATOM   3010 N  N   . ALA   B 1 190 ? -67.785 -17.934 48.284  1.00 30.47 ?  185 ALA   C N   1 
ATOM   3011 C  CA  . ALA   B 1 190 ? -66.895 -18.993 48.802  1.00 31.71 ?  185 ALA   C CA  1 
ATOM   3012 C  C   . ALA   B 1 190 ? -65.598 -19.033 47.992  1.00 29.57 ?  185 ALA   C C   1 
ATOM   3013 O  O   . ALA   B 1 190 ? -64.569 -19.431 48.546  1.00 33.56 ?  185 ALA   C O   1 
ATOM   3014 C  CB  . ALA   B 1 190 ? -67.583 -20.324 48.758  1.00 33.79 ?  185 ALA   C CB  1 
ATOM   3015 N  N   . ILE   B 1 191 ? -65.668 -18.758 46.687  1.00 27.83 ?  186 ILE   C N   1 
ATOM   3016 C  CA  . ILE   B 1 191 ? -64.468 -18.769 45.816  1.00 28.87 ?  186 ILE   C CA  1 
ATOM   3017 C  C   . ILE   B 1 191 ? -63.611 -17.536 46.155  1.00 25.32 ?  186 ILE   C C   1 
ATOM   3018 O  O   . ILE   B 1 191 ? -62.376 -17.685 46.250  1.00 24.40 ?  186 ILE   C O   1 
ATOM   3019 C  CB  . ILE   B 1 191 ? -64.867 -18.796 44.334  1.00 30.64 ?  186 ILE   C CB  1 
ATOM   3020 C  CG1 . ILE   B 1 191 ? -65.801 -19.966 44.015  1.00 36.38 ?  186 ILE   C CG1 1 
ATOM   3021 C  CG2 . ILE   B 1 191 ? -63.615 -18.794 43.480  1.00 29.85 ?  186 ILE   C CG2 1 
ATOM   3022 C  CD1 . ILE   B 1 191 ? -65.383 -21.262 44.647  1.00 38.09 ?  186 ILE   C CD1 1 
ATOM   3023 N  N   . ARG   B 1 192 ? -64.225 -16.365 46.305  1.00 26.50 ?  187 ARG   C N   1 
ATOM   3024 C  CA  . ARG   B 1 192 ? -63.503 -15.137 46.753  1.00 26.39 ?  187 ARG   C CA  1 
ATOM   3025 C  C   . ARG   B 1 192 ? -62.767 -15.429 48.065  1.00 26.07 ?  187 ARG   C C   1 
ATOM   3026 O  O   . ARG   B 1 192 ? -61.557 -15.079 48.206  1.00 22.62 ?  187 ARG   C O   1 
ATOM   3027 C  CB  . ARG   B 1 192 ? -64.445 -13.946 46.951  1.00 27.29 ?  187 ARG   C CB  1 
ATOM   3028 C  CG  . ARG   B 1 192 ? -65.170 -13.512 45.690  1.00 28.81 ?  187 ARG   C CG  1 
ATOM   3029 C  CD  . ARG   B 1 192 ? -65.812 -12.144 45.853  1.00 38.61 ?  187 ARG   C CD  1 
ATOM   3030 N  NE  . ARG   B 1 192 ? -67.172 -12.143 45.340  1.00 50.07 ?  187 ARG   C NE  1 
ATOM   3031 C  CZ  . ARG   B 1 192 ? -68.283 -12.114 46.082  1.00 59.91 ?  187 ARG   C CZ  1 
ATOM   3032 N  NH1 . ARG   B 1 192 ? -68.227 -12.056 47.406  1.00 60.79 1  187 ARG   C NH1 1 
ATOM   3033 N  NH2 . ARG   B 1 192 ? -69.464 -12.136 45.483  1.00 61.66 ?  187 ARG   C NH2 1 
ATOM   3034 N  N   . ARG   B 1 193 ? -63.411 -16.147 48.984  1.00 26.05 ?  188 ARG   C N   1 
ATOM   3035 C  CA  . ARG   B 1 193 ? -62.779 -16.527 50.283  1.00 28.35 ?  188 ARG   C CA  1 
ATOM   3036 C  C   . ARG   B 1 193 ? -61.591 -17.450 50.040  1.00 26.20 ?  188 ARG   C C   1 
ATOM   3037 O  O   . ARG   B 1 193 ? -60.569 -17.234 50.699  1.00 22.50 ?  188 ARG   C O   1 
ATOM   3038 C  CB  . ARG   B 1 193 ? -63.778 -17.135 51.270  1.00 32.47 ?  188 ARG   C CB  1 
ATOM   3039 C  CG  . ARG   B 1 193 ? -64.878 -16.165 51.678  1.00 43.41 ?  188 ARG   C CG  1 
ATOM   3040 C  CD  . ARG   B 1 193 ? -65.535 -16.527 53.005  1.00 51.51 ?  188 ARG   C CD  1 
ATOM   3041 N  NE  . ARG   B 1 193 ? -66.056 -17.891 52.991  1.00 60.39 ?  188 ARG   C NE  1 
ATOM   3042 C  CZ  . ARG   B 1 193 ? -67.246 -18.257 52.502  1.00 58.86 ?  188 ARG   C CZ  1 
ATOM   3043 N  NH1 . ARG   B 1 193 ? -67.596 -19.535 52.535  1.00 57.16 1  188 ARG   C NH1 1 
ATOM   3044 N  NH2 . ARG   B 1 193 ? -68.069 -17.355 51.983  1.00 52.84 ?  188 ARG   C NH2 1 
ATOM   3045 N  N   . ARG   B 1 194 ? -61.690 -18.392 49.091  1.00 22.11 ?  189 ARG   C N   1 
ATOM   3046 C  CA  . ARG   B 1 194 ? -60.564 -19.316 48.831  1.00 22.54 ?  189 ARG   C CA  1 
ATOM   3047 C  C   . ARG   B 1 194 ? -59.379 -18.533 48.256  1.00 22.16 ?  189 ARG   C C   1 
ATOM   3048 O  O   . ARG   B 1 194 ? -58.240 -18.851 48.627  1.00 22.76 ?  189 ARG   C O   1 
ATOM   3049 C  CB  . ARG   B 1 194 ? -60.969 -20.418 47.860  1.00 24.50 ?  189 ARG   C CB  1 
ATOM   3050 C  CG  . ARG   B 1 194 ? -61.890 -21.431 48.517  1.00 27.15 ?  189 ARG   C CG  1 
ATOM   3051 C  CD  . ARG   B 1 194 ? -62.473 -22.426 47.523  1.00 29.47 ?  189 ARG   C CD  1 
ATOM   3052 N  NE  . ARG   B 1 194 ? -63.691 -22.991 48.097  1.00 31.15 ?  189 ARG   C NE  1 
ATOM   3053 C  CZ  . ARG   B 1 194 ? -64.573 -23.743 47.456  1.00 35.64 ?  189 ARG   C CZ  1 
ATOM   3054 N  NH1 . ARG   B 1 194 ? -64.389 -24.064 46.188  1.00 35.56 1  189 ARG   C NH1 1 
ATOM   3055 N  NH2 . ARG   B 1 194 ? -65.652 -24.168 48.093  1.00 37.08 ?  189 ARG   C NH2 1 
ATOM   3056 N  N   . VAL   B 1 195 ? -59.662 -17.570 47.373  1.00 22.98 ?  190 VAL   C N   1 
ATOM   3057 C  CA  . VAL   B 1 195 ? -58.602 -16.720 46.758  1.00 22.45 ?  190 VAL   C CA  1 
ATOM   3058 C  C   . VAL   B 1 195 ? -57.928 -15.916 47.864  1.00 21.89 ?  190 VAL   C C   1 
ATOM   3059 O  O   . VAL   B 1 195 ? -56.675 -15.943 47.951  1.00 20.69 ?  190 VAL   C O   1 
ATOM   3060 C  CB  . VAL   B 1 195 ? -59.137 -15.830 45.629  1.00 22.52 ?  190 VAL   C CB  1 
ATOM   3061 C  CG1 . VAL   B 1 195 ? -58.060 -14.874 45.122  1.00 22.12 ?  190 VAL   C CG1 1 
ATOM   3062 C  CG2 . VAL   B 1 195 ? -59.706 -16.661 44.477  1.00 23.98 ?  190 VAL   C CG2 1 
ATOM   3063 N  N   . ARG   B 1 196 ? -58.729 -15.233 48.677  1.00 23.09 ?  191 ARG   C N   1 
ATOM   3064 C  CA  . ARG   B 1 196 ? -58.225 -14.381 49.788  1.00 26.02 ?  191 ARG   C CA  1 
ATOM   3065 C  C   . ARG   B 1 196 ? -57.340 -15.245 50.687  1.00 27.74 ?  191 ARG   C C   1 
ATOM   3066 O  O   . ARG   B 1 196 ? -56.230 -14.785 51.035  1.00 26.23 ?  191 ARG   C O   1 
ATOM   3067 C  CB  . ARG   B 1 196 ? -59.379 -13.744 50.563  1.00 31.30 ?  191 ARG   C CB  1 
ATOM   3068 C  CG  . ARG   B 1 196 ? -58.910 -12.936 51.769  1.00 38.76 ?  191 ARG   C CG  1 
ATOM   3069 C  CD  . ARG   B 1 196 ? -59.965 -11.964 52.271  1.00 49.10 ?  191 ARG   C CD  1 
ATOM   3070 N  NE  . ARG   B 1 196 ? -61.349 -12.449 52.258  1.00 56.52 ?  191 ARG   C NE  1 
ATOM   3071 C  CZ  . ARG   B 1 196 ? -61.880 -13.272 53.164  1.00 61.99 ?  191 ARG   C CZ  1 
ATOM   3072 N  NH1 . ARG   B 1 196 ? -61.144 -13.744 54.161  1.00 66.74 1  191 ARG   C NH1 1 
ATOM   3073 N  NH2 . ARG   B 1 196 ? -63.145 -13.637 53.055  1.00 64.03 ?  191 ARG   C NH2 1 
ATOM   3074 N  N   . HIS   B 1 197 ? -57.793 -16.453 51.053  1.00 26.17 ?  192 HIS   C N   1 
ATOM   3075 C  CA  . HIS   B 1 197 ? -57.053 -17.319 52.003  1.00 27.34 ?  192 HIS   C CA  1 
ATOM   3076 C  C   . HIS   B 1 197 ? -55.708 -17.682 51.375  1.00 27.78 ?  192 HIS   C C   1 
ATOM   3077 O  O   . HIS   B 1 197 ? -54.651 -17.635 52.067  1.00 28.94 ?  192 HIS   C O   1 
ATOM   3078 C  CB  . HIS   B 1 197 ? -57.847 -18.575 52.344  1.00 32.56 ?  192 HIS   C CB  1 
ATOM   3079 C  CG  . HIS   B 1 197 ? -57.084 -19.500 53.218  1.00 33.49 ?  192 HIS   C CG  1 
ATOM   3080 N  ND1 . HIS   B 1 197 ? -56.786 -20.800 52.842  1.00 42.87 ?  192 HIS   C ND1 1 
ATOM   3081 C  CD2 . HIS   B 1 197 ? -56.527 -19.309 54.433  1.00 37.36 ?  192 HIS   C CD2 1 
ATOM   3082 C  CE1 . HIS   B 1 197 ? -56.092 -21.378 53.803  1.00 39.90 ?  192 HIS   C CE1 1 
ATOM   3083 N  NE2 . HIS   B 1 197 ? -55.921 -20.483 54.782  1.00 41.52 ?  192 HIS   C NE2 1 
ATOM   3084 N  N   . SER   B 1 198 ? -55.747 -18.034 50.095  1.00 25.68 ?  193 SER   C N   1 
ATOM   3085 C  CA  . SER   B 1 198 ? -54.558 -18.474 49.337  1.00 26.48 ?  193 SER   C CA  1 
ATOM   3086 C  C   . SER   B 1 198 ? -53.500 -17.352 49.285  1.00 23.20 ?  193 SER   C C   1 
ATOM   3087 O  O   . SER   B 1 198 ? -52.324 -17.634 49.441  1.00 29.37 ?  193 SER   C O   1 
ATOM   3088 C  CB  . SER   B 1 198 ? -54.941 -18.896 47.986  1.00 26.12 ?  193 SER   C CB  1 
ATOM   3089 O  OG  . SER   B 1 198 ? -53.803 -19.376 47.334  1.00 36.20 ?  193 SER   C OG  1 
ATOM   3090 N  N   . PHE   B 1 199 ? -53.910 -16.113 49.119  1.00 22.63 ?  194 PHE   C N   1 
ATOM   3091 C  CA  . PHE   B 1 199 ? -52.984 -14.962 48.999  1.00 21.44 ?  194 PHE   C CA  1 
ATOM   3092 C  C   . PHE   B 1 199 ? -52.433 -14.551 50.379  1.00 23.86 ?  194 PHE   C C   1 
ATOM   3093 O  O   . PHE   B 1 199 ? -51.407 -13.863 50.424  1.00 23.20 ?  194 PHE   C O   1 
ATOM   3094 C  CB  . PHE   B 1 199 ? -53.704 -13.796 48.340  1.00 21.24 ?  194 PHE   C CB  1 
ATOM   3095 C  CG  . PHE   B 1 199 ? -53.916 -13.937 46.850  1.00 20.84 ?  194 PHE   C CG  1 
ATOM   3096 C  CD1 . PHE   B 1 199 ? -53.130 -14.790 46.074  1.00 26.50 ?  194 PHE   C CD1 1 
ATOM   3097 C  CD2 . PHE   B 1 199 ? -54.822 -13.136 46.201  1.00 22.52 ?  194 PHE   C CD2 1 
ATOM   3098 C  CE1 . PHE   B 1 199 ? -53.294 -14.857 44.689  1.00 23.06 ?  194 PHE   C CE1 1 
ATOM   3099 C  CE2 . PHE   B 1 199 ? -54.977 -13.204 44.827  1.00 21.78 ?  194 PHE   C CE2 1 
ATOM   3100 C  CZ  . PHE   B 1 199 ? -54.273 -14.114 44.089  1.00 22.56 ?  194 PHE   C CZ  1 
ATOM   3101 N  N   . GLY   B 1 200 ? -53.149 -14.890 51.451  1.00 24.70 ?  195 GLY   C N   1 
ATOM   3102 C  CA  . GLY   B 1 200 ? -52.707 -14.658 52.845  1.00 28.42 ?  195 GLY   C CA  1 
ATOM   3103 C  C   . GLY   B 1 200 ? -51.379 -15.317 53.186  1.00 33.26 ?  195 GLY   C C   1 
ATOM   3104 O  O   . GLY   B 1 200 ? -50.701 -14.822 54.096  1.00 38.15 ?  195 GLY   C O   1 
ATOM   3105 N  N   . GLY   B 1 201 ? -51.022 -16.408 52.513  1.00 38.61 ?  196 GLY   C N   1 
ATOM   3106 C  CA  . GLY   B 1 201 ? -49.953 -17.311 52.969  1.00 42.15 ?  196 GLY   C CA  1 
ATOM   3107 C  C   . GLY   B 1 201 ? -48.594 -16.974 52.380  1.00 44.24 ?  196 GLY   C C   1 
ATOM   3108 O  O   . GLY   B 1 201 ? -47.678 -17.814 52.536  1.00 44.89 ?  196 GLY   C O   1 
ATOM   3109 N  N   . ALA   B 1 202 ? -48.435 -15.821 51.724  1.00 39.44 ?  197 ALA   C N   1 
ATOM   3110 C  CA  . ALA   B 1 202 ? -47.157 -15.461 51.063  1.00 40.14 ?  197 ALA   C CA  1 
ATOM   3111 C  C   . ALA   B 1 202 ? -47.009 -13.951 50.951  1.00 34.66 ?  197 ALA   C C   1 
ATOM   3112 O  O   . ALA   B 1 202 ? -47.988 -13.279 50.665  1.00 37.52 ?  197 ALA   C O   1 
ATOM   3113 C  CB  . ALA   B 1 202 ? -47.075 -16.141 49.711  1.00 41.23 ?  197 ALA   C CB  1 
ATOM   3114 N  N   . GLU   B 1 203 ? -45.802 -13.419 51.128  1.00 34.06 ?  198 GLU   C N   1 
ATOM   3115 C  CA  . GLU   B 1 203 ? -45.547 -11.965 51.068  1.00 30.60 ?  198 GLU   C CA  1 
ATOM   3116 C  C   . GLU   B 1 203 ? -45.969 -11.325 49.731  1.00 35.64 ?  198 GLU   C C   1 
ATOM   3117 O  O   . GLU   B 1 203 ? -46.395 -10.152 49.747  1.00 35.02 ?  198 GLU   C O   1 
ATOM   3118 C  CB  . GLU   B 1 203 ? -44.064 -11.669 51.273  1.00 38.74 ?  198 GLU   C CB  1 
ATOM   3119 C  CG  . GLU   B 1 203 ? -43.747 -10.174 51.245  1.00 40.58 ?  198 GLU   C CG  1 
ATOM   3120 C  CD  . GLU   B 1 203 ? -43.531 -9.500  49.890  1.00 46.76 ?  198 GLU   C CD  1 
ATOM   3121 O  OE1 . GLU   B 1 203 ? -43.271 -10.210 48.871  1.00 53.26 ?  198 GLU   C OE1 1 
ATOM   3122 O  OE2 . GLU   B 1 203 ? -43.639 -8.253  49.839  1.00 56.82 -1 198 GLU   C OE2 1 
ATOM   3123 N  N   . ALA   B 1 204 ? -45.744 -12.013 48.604  1.00 31.62 ?  199 ALA   C N   1 
ATOM   3124 C  CA  . ALA   B 1 204 ? -45.934 -11.496 47.229  1.00 30.89 ?  199 ALA   C CA  1 
ATOM   3125 C  C   . ALA   B 1 204 ? -47.404 -11.105 47.039  1.00 26.97 ?  199 ALA   C C   1 
ATOM   3126 O  O   . ALA   B 1 204 ? -47.709 -10.306 46.138  1.00 27.33 ?  199 ALA   C O   1 
ATOM   3127 C  CB  . ALA   B 1 204 ? -45.522 -12.578 46.260  1.00 30.86 ?  199 ALA   C CB  1 
ATOM   3128 N  N   . THR   B 1 205 ? -48.280 -11.734 47.811  1.00 25.48 ?  200 THR   C N   1 
ATOM   3129 C  CA  . THR   B 1 205 ? -49.763 -11.690 47.590  1.00 23.96 ?  200 THR   C CA  1 
ATOM   3130 C  C   . THR   B 1 205 ? -50.529 -11.146 48.800  1.00 24.65 ?  200 THR   C C   1 
ATOM   3131 O  O   . THR   B 1 205 ? -51.781 -10.969 48.688  1.00 22.76 ?  200 THR   C O   1 
ATOM   3132 C  CB  . THR   B 1 205 ? -50.246 -13.092 47.214  1.00 27.42 ?  200 THR   C CB  1 
ATOM   3133 O  OG1 . THR   B 1 205 ? -49.938 -14.034 48.239  1.00 26.68 ?  200 THR   C OG1 1 
ATOM   3134 C  CG2 . THR   B 1 205 ? -49.661 -13.596 45.912  1.00 27.78 ?  200 THR   C CG2 1 
ATOM   3135 N  N   . ARG   B 1 206 ? -49.867 -10.857 49.931  1.00 23.98 ?  201 ARG   C N   1 
ATOM   3136 C  CA  . ARG   B 1 206 ? -50.600 -10.429 51.153  1.00 25.78 ?  201 ARG   C CA  1 
ATOM   3137 C  C   . ARG   B 1 206 ? -51.306 -9.076  50.986  1.00 23.55 ?  201 ARG   C C   1 
ATOM   3138 O  O   . ARG   B 1 206 ? -52.410 -8.888  51.583  1.00 24.62 ?  201 ARG   C O   1 
ATOM   3139 C  CB  . ARG   B 1 206 ? -49.656 -10.396 52.358  1.00 29.03 ?  201 ARG   C CB  1 
ATOM   3140 C  CG  . ARG   B 1 206 ? -50.012 -11.433 53.408  1.00 34.15 ?  201 ARG   C CG  1 
ATOM   3141 C  CD  . ARG   B 1 206 ? -48.969 -11.656 54.506  1.00 37.51 ?  201 ARG   C CD  1 
ATOM   3142 N  NE  . ARG   B 1 206 ? -48.881 -13.096 54.760  1.00 36.49 ?  201 ARG   C NE  1 
ATOM   3143 C  CZ  . ARG   B 1 206 ? -47.777 -13.851 54.686  1.00 39.64 ?  201 ARG   C CZ  1 
ATOM   3144 N  NH1 . ARG   B 1 206 ? -46.598 -13.318 54.420  1.00 34.87 1  201 ARG   C NH1 1 
ATOM   3145 N  NH2 . ARG   B 1 206 ? -47.857 -15.152 54.941  1.00 43.29 ?  201 ARG   C NH2 1 
ATOM   3146 N  N   . ALA   B 1 207 ? -50.736 -8.140  50.221  1.00 22.21 ?  202 ALA   C N   1 
ATOM   3147 C  CA  . ALA   B 1 207 ? -51.331 -6.807  50.025  1.00 23.88 ?  202 ALA   C CA  1 
ATOM   3148 C  C   . ALA   B 1 207 ? -52.608 -6.952  49.203  1.00 20.25 ?  202 ALA   C C   1 
ATOM   3149 O  O   . ALA   B 1 207 ? -53.492 -6.166  49.422  1.00 23.39 ?  202 ALA   C O   1 
ATOM   3150 C  CB  . ALA   B 1 207 ? -50.376 -5.863  49.340  1.00 24.95 ?  202 ALA   C CB  1 
ATOM   3151 N  N   . VAL   B 1 208 ? -52.649 -7.896  48.252  1.00 20.57 ?  203 VAL   C N   1 
ATOM   3152 C  CA  . VAL   B 1 208 ? -53.900 -8.192  47.499  1.00 20.23 ?  203 VAL   C CA  1 
ATOM   3153 C  C   . VAL   B 1 208 ? -54.936 -8.749  48.478  1.00 18.98 ?  203 VAL   C C   1 
ATOM   3154 O  O   . VAL   B 1 208 ? -56.105 -8.281  48.430  1.00 19.58 ?  203 VAL   C O   1 
ATOM   3155 C  CB  . VAL   B 1 208 ? -53.660 -9.154  46.327  1.00 22.11 ?  203 VAL   C CB  1 
ATOM   3156 C  CG1 . VAL   B 1 208 ? -54.981 -9.546  45.659  1.00 20.33 ?  203 VAL   C CG1 1 
ATOM   3157 C  CG2 . VAL   B 1 208 ? -52.704 -8.528  45.326  1.00 25.61 ?  203 VAL   C CG2 1 
ATOM   3158 N  N   . ALA   B 1 209 ? -54.555 -9.750  49.288  1.00 19.06 ?  204 ALA   C N   1 
ATOM   3159 C  CA  . ALA   B 1 209 ? -55.436 -10.355 50.305  1.00 21.28 ?  204 ALA   C CA  1 
ATOM   3160 C  C   . ALA   B 1 209 ? -55.986 -9.244  51.222  1.00 22.13 ?  204 ALA   C C   1 
ATOM   3161 O  O   . ALA   B 1 209 ? -57.175 -9.259  51.561  1.00 24.76 ?  204 ALA   C O   1 
ATOM   3162 C  CB  . ALA   B 1 209 ? -54.698 -11.423 51.063  1.00 23.68 ?  204 ALA   C CB  1 
ATOM   3163 N  N   . GLY   B 1 210 ? -55.126 -8.303  51.601  1.00 22.36 ?  205 GLY   C N   1 
ATOM   3164 C  CA  . GLY   B 1 210 ? -55.469 -7.130  52.431  1.00 25.38 ?  205 GLY   C CA  1 
ATOM   3165 C  C   . GLY   B 1 210 ? -56.592 -6.325  51.808  1.00 24.68 ?  205 GLY   C C   1 
ATOM   3166 O  O   . GLY   B 1 210 ? -57.563 -5.969  52.499  1.00 26.01 ?  205 GLY   C O   1 
ATOM   3167 N  N   . LEU   B 1 211 ? -56.510 -6.044  50.507  1.00 21.81 ?  206 LEU   C N   1 
ATOM   3168 C  CA  . LEU   B 1 211 ? -57.585 -5.257  49.865  1.00 19.82 ?  206 LEU   C CA  1 
ATOM   3169 C  C   . LEU   B 1 211 ? -58.868 -6.095  49.745  1.00 21.28 ?  206 LEU   C C   1 
ATOM   3170 O  O   . LEU   B 1 211 ? -59.999 -5.531  49.897  1.00 21.36 ?  206 LEU   C O   1 
ATOM   3171 C  CB  . LEU   B 1 211 ? -57.089 -4.827  48.473  1.00 23.22 ?  206 LEU   C CB  1 
ATOM   3172 C  CG  . LEU   B 1 211 ? -56.025 -3.725  48.472  1.00 28.82 ?  206 LEU   C CG  1 
ATOM   3173 C  CD1 . LEU   B 1 211 ? -55.407 -3.584  47.109  1.00 29.17 ?  206 LEU   C CD1 1 
ATOM   3174 C  CD2 . LEU   B 1 211 ? -56.627 -2.384  48.928  1.00 33.61 ?  206 LEU   C CD2 1 
ATOM   3175 N  N   . MET   B 1 212 ? -58.737 -7.389  49.395  1.00 22.72 ?  207 MET   C N   1 
ATOM   3176 C  CA  . MET   B 1 212 ? -59.912 -8.297  49.273  1.00 22.96 ?  207 MET   C CA  1 
ATOM   3177 C  C   . MET   B 1 212 ? -60.668 -8.330  50.607  1.00 25.64 ?  207 MET   C C   1 
ATOM   3178 O  O   . MET   B 1 212 ? -61.937 -8.328  50.605  1.00 24.54 ?  207 MET   C O   1 
ATOM   3179 C  CB  . MET   B 1 212 ? -59.435 -9.697  48.881  1.00 23.61 ?  207 MET   C CB  1 
ATOM   3180 C  CG  . MET   B 1 212 ? -58.923 -9.743  47.462  1.00 24.26 ?  207 MET   C CG  1 
ATOM   3181 S  SD  . MET   B 1 212 ? -58.406 -11.406 46.952  1.00 23.30 ?  207 MET   C SD  1 
ATOM   3182 C  CE  . MET   B 1 212 ? -60.074 -12.036 46.695  1.00 24.57 ?  207 MET   C CE  1 
ATOM   3183 N  N   . ASP   B 1 213 ? -59.938 -8.294  51.710  1.00 26.81 ?  208 ASP   C N   1 
ATOM   3184 C  CA  . ASP   B 1 213 ? -60.483 -8.263  53.094  1.00 30.10 ?  208 ASP   C CA  1 
ATOM   3185 C  C   . ASP   B 1 213 ? -61.307 -6.994  53.332  1.00 32.15 ?  208 ASP   C C   1 
ATOM   3186 O  O   . ASP   B 1 213 ? -62.278 -7.068  54.103  1.00 33.89 ?  208 ASP   C O   1 
ATOM   3187 C  CB  . ASP   B 1 213 ? -59.346 -8.353  54.109  1.00 35.86 ?  208 ASP   C CB  1 
ATOM   3188 C  CG  . ASP   B 1 213 ? -59.205 -9.718  54.740  1.00 45.70 ?  208 ASP   C CG  1 
ATOM   3189 O  OD1 . ASP   B 1 213 ? -60.265 -10.318 55.023  1.00 56.46 ?  208 ASP   C OD1 1 
ATOM   3190 O  OD2 . ASP   B 1 213 ? -58.036 -10.161 54.948  1.00 58.43 -1 208 ASP   C OD2 1 
ATOM   3191 N  N   . ARG   B 1 214 ? -60.963 -5.876  52.697  1.00 29.32 ?  209 ARG   C N   1 
ATOM   3192 C  CA  . ARG   B 1 214 ? -61.608 -4.564  52.948  1.00 33.90 ?  209 ARG   C CA  1 
ATOM   3193 C  C   . ARG   B 1 214 ? -62.804 -4.333  52.046  1.00 33.14 ?  209 ARG   C C   1 
ATOM   3194 O  O   . ARG   B 1 214 ? -63.460 -3.334  52.276  1.00 36.38 ?  209 ARG   C O   1 
ATOM   3195 C  CB  . ARG   B 1 214 ? -60.614 -3.429  52.773  1.00 37.99 ?  209 ARG   C CB  1 
ATOM   3196 C  CG  . ARG   B 1 214 ? -59.401 -3.593  53.670  1.00 43.66 ?  209 ARG   C CG  1 
ATOM   3197 C  CD  . ARG   B 1 214 ? -58.513 -2.382  53.564  1.00 49.62 ?  209 ARG   C CD  1 
ATOM   3198 N  NE  . ARG   B 1 214 ? -59.298 -1.166  53.777  1.00 55.64 ?  209 ARG   C NE  1 
ATOM   3199 C  CZ  . ARG   B 1 214 ? -59.107 -0.015  53.138  1.00 57.76 ?  209 ARG   C CZ  1 
ATOM   3200 N  NH1 . ARG   B 1 214 ? -58.168 0.088   52.207  1.00 55.36 1  209 ARG   C NH1 1 
ATOM   3201 N  NH2 . ARG   B 1 214 ? -59.873 1.023   53.428  1.00 57.79 ?  209 ARG   C NH2 1 
ATOM   3202 N  N   . LEU   B 1 215 ? -63.121 -5.228  51.101  1.00 31.69 ?  210 LEU   C N   1 
ATOM   3203 C  CA  . LEU   B 1 215 ? -64.323 -5.036  50.266  1.00 36.16 ?  210 LEU   C CA  1 
ATOM   3204 C  C   . LEU   B 1 215 ? -65.565 -5.283  51.122  1.00 40.30 ?  210 LEU   C C   1 
ATOM   3205 O  O   . LEU   B 1 215 ? -65.559 -6.142  51.987  1.00 42.79 ?  210 LEU   C O   1 
ATOM   3206 C  CB  . LEU   B 1 215 ? -64.263 -5.944  49.036  1.00 30.88 ?  210 LEU   C CB  1 
ATOM   3207 C  CG  . LEU   B 1 215 ? -63.133 -5.645  48.060  1.00 26.75 ?  210 LEU   C CG  1 
ATOM   3208 C  CD1 . LEU   B 1 215 ? -63.051 -6.744  46.994  1.00 28.23 ?  210 LEU   C CD1 1 
ATOM   3209 C  CD2 . LEU   B 1 215 ? -63.328 -4.308  47.362  1.00 29.60 ?  210 LEU   C CD2 1 
ATOM   3210 N  N   . PRO   B 1 216 ? -66.674 -4.538  50.918  1.00 52.18 ?  211 PRO   C N   1 
ATOM   3211 C  CA  . PRO   B 1 216 ? -67.866 -4.675  51.765  1.00 55.35 ?  211 PRO   C CA  1 
ATOM   3212 C  C   . PRO   B 1 216 ? -68.300 -6.129  52.026  1.00 56.37 ?  211 PRO   C C   1 
ATOM   3213 O  O   . PRO   B 1 216 ? -68.559 -6.856  51.079  1.00 56.18 ?  211 PRO   C O   1 
ATOM   3214 C  CB  . PRO   B 1 216 ? -68.973 -3.920  51.001  1.00 54.63 ?  211 PRO   C CB  1 
ATOM   3215 C  CG  . PRO   B 1 216 ? -68.347 -3.488  49.679  1.00 54.13 ?  211 PRO   C CG  1 
ATOM   3216 C  CD  . PRO   B 1 216 ? -66.844 -3.514  49.878  1.00 51.54 ?  211 PRO   C CD  1 
ATOM   3217 N  N   . GLY   C 1 4   ? -66.386 -12.670 81.319  1.00 61.90 ?  -1  GLY   D N   1 
ATOM   3218 C  CA  . GLY   C 1 4   ? -65.137 -12.324 80.567  1.00 56.92 ?  -1  GLY   D CA  1 
ATOM   3219 C  C   . GLY   C 1 4   ? -63.909 -12.297 81.471  1.00 50.77 ?  -1  GLY   D C   1 
ATOM   3220 O  O   . GLY   C 1 4   ? -63.950 -11.597 82.510  1.00 48.39 ?  -1  GLY   D O   1 
ATOM   3221 N  N   . ALA   C 1 5   ? -62.839 -13.004 81.078  1.00 39.47 ?  0   ALA   D N   1 
ATOM   3222 C  CA  . ALA   C 1 5   ? -61.534 -13.025 81.781  1.00 36.90 ?  0   ALA   D CA  1 
ATOM   3223 C  C   . ALA   C 1 5   ? -60.715 -11.787 81.400  1.00 32.65 ?  0   ALA   D C   1 
ATOM   3224 O  O   . ALA   C 1 5   ? -59.818 -11.413 82.175  1.00 32.41 ?  0   ALA   D O   1 
ATOM   3225 C  CB  . ALA   C 1 5   ? -60.804 -14.301 81.500  1.00 36.87 ?  0   ALA   D CB  1 
ATOM   3226 N  N   . MET   C 1 6   ? -61.049 -11.128 80.290  1.00 32.33 ?  1   MET   D N   1 
ATOM   3227 C  CA  . MET   C 1 6   ? -60.477 -9.808  79.923  1.00 30.71 ?  1   MET   D CA  1 
ATOM   3228 C  C   . MET   C 1 6   ? -61.610 -8.790  79.911  1.00 28.55 ?  1   MET   D C   1 
ATOM   3229 O  O   . MET   C 1 6   ? -62.659 -9.097  79.338  1.00 29.16 ?  1   MET   D O   1 
ATOM   3230 C  CB  . MET   C 1 6   ? -59.848 -9.839  78.535  1.00 31.23 ?  1   MET   D CB  1 
ATOM   3231 C  CG  . MET   C 1 6   ? -59.115 -8.571  78.211  1.00 31.11 ?  1   MET   D CG  1 
ATOM   3232 S  SD  . MET   C 1 6   ? -58.548 -8.681  76.501  1.00 33.41 ?  1   MET   D SD  1 
ATOM   3233 C  CE  . MET   C 1 6   ? -57.833 -7.064  76.330  1.00 28.75 ?  1   MET   D CE  1 
ATOM   3234 N  N   . PHE   C 1 7   ? -61.424 -7.629  80.529  1.00 26.92 ?  2   PHE   D N   1 
ATOM   3235 C  CA  . PHE   C 1 7   ? -62.453 -6.553  80.529  1.00 27.29 ?  2   PHE   D CA  1 
ATOM   3236 C  C   . PHE   C 1 7   ? -62.364 -5.775  79.209  1.00 26.33 ?  2   PHE   D C   1 
ATOM   3237 O  O   . PHE   C 1 7   ? -61.326 -5.160  78.945  1.00 29.58 ?  2   PHE   D O   1 
ATOM   3238 C  CB  . PHE   C 1 7   ? -62.299 -5.634  81.732  1.00 28.21 ?  2   PHE   D CB  1 
ATOM   3239 C  CG  . PHE   C 1 7   ? -63.283 -4.500  81.773  1.00 29.06 ?  2   PHE   D CG  1 
ATOM   3240 C  CD1 . PHE   C 1 7   ? -64.631 -4.724  82.003  1.00 31.73 ?  2   PHE   D CD1 1 
ATOM   3241 C  CD2 . PHE   C 1 7   ? -62.854 -3.194  81.579  1.00 32.05 ?  2   PHE   D CD2 1 
ATOM   3242 C  CE1 . PHE   C 1 7   ? -65.525 -3.663  82.059  1.00 31.55 ?  2   PHE   D CE1 1 
ATOM   3243 C  CE2 . PHE   C 1 7   ? -63.749 -2.139  81.611  1.00 32.93 ?  2   PHE   D CE2 1 
ATOM   3244 C  CZ  . PHE   C 1 7   ? -65.090 -2.383  81.830  1.00 32.04 ?  2   PHE   D CZ  1 
ATOM   3245 N  N   . VAL   C 1 8   ? -63.387 -5.902  78.367  1.00 23.84 ?  3   VAL   D N   1 
ATOM   3246 C  CA  . VAL   C 1 8   ? -63.482 -5.199  77.050  1.00 20.66 ?  3   VAL   D CA  1 
ATOM   3247 C  C   . VAL   C 1 8   ? -64.853 -4.572  76.958  1.00 24.08 ?  3   VAL   D C   1 
ATOM   3248 O  O   . VAL   C 1 8   ? -65.823 -5.288  76.733  1.00 25.38 ?  3   VAL   D O   1 
ATOM   3249 C  CB  . VAL   C 1 8   ? -63.293 -6.121  75.841  1.00 22.46 ?  3   VAL   D CB  1 
ATOM   3250 C  CG1 . VAL   C 1 8   ? -63.331 -5.330  74.543  1.00 21.51 ?  3   VAL   D CG1 1 
ATOM   3251 C  CG2 . VAL   C 1 8   ? -61.997 -6.920  75.958  1.00 21.63 ?  3   VAL   D CG2 1 
ATOM   3252 N  N   . PRO   C 1 9   ? -64.933 -3.241  77.061  1.00 25.51 ?  4   PRO   D N   1 
ATOM   3253 C  CA  . PRO   C 1 9   ? -66.193 -2.537  76.838  1.00 26.77 ?  4   PRO   D CA  1 
ATOM   3254 C  C   . PRO   C 1 9   ? -66.772 -2.889  75.464  1.00 28.75 ?  4   PRO   D C   1 
ATOM   3255 O  O   . PRO   C 1 9   ? -66.049 -3.039  74.482  1.00 26.51 ?  4   PRO   D O   1 
ATOM   3256 C  CB  . PRO   C 1 9   ? -65.831 -1.057  77.019  1.00 28.15 ?  4   PRO   D CB  1 
ATOM   3257 C  CG  . PRO   C 1 9   ? -64.548 -1.068  77.858  1.00 28.56 ?  4   PRO   D CG  1 
ATOM   3258 C  CD  . PRO   C 1 9   ? -63.840 -2.351  77.462  1.00 28.95 ?  4   PRO   D CD  1 
ATOM   3259 N  N   . GLY   C 1 10  ? -68.101 -3.021  75.406  1.00 28.60 ?  5   GLY   D N   1 
ATOM   3260 C  CA  . GLY   C 1 10  ? -68.845 -3.389  74.183  1.00 29.41 ?  5   GLY   D CA  1 
ATOM   3261 C  C   . GLY   C 1 10  ? -68.361 -2.666  72.921  1.00 27.86 ?  5   GLY   D C   1 
ATOM   3262 O  O   . GLY   C 1 10  ? -68.142 -3.315  71.897  1.00 28.88 ?  5   GLY   D O   1 
ATOM   3263 N  N   . PRO   C 1 11  ? -68.137 -1.330  72.957  1.00 27.77 ?  6   PRO   D N   1 
ATOM   3264 C  CA  . PRO   C 1 11  ? -67.769 -0.572  71.767  1.00 26.18 ?  6   PRO   D CA  1 
ATOM   3265 C  C   . PRO   C 1 11  ? -66.385 -0.956  71.219  1.00 23.69 ?  6   PRO   D C   1 
ATOM   3266 O  O   . PRO   C 1 11  ? -66.105 -0.589  70.105  1.00 23.36 ?  6   PRO   D O   1 
ATOM   3267 C  CB  . PRO   C 1 11  ? -67.711 0.886   72.250  1.00 31.10 ?  6   PRO   D CB  1 
ATOM   3268 C  CG  . PRO   C 1 11  ? -68.573 0.897   73.496  1.00 30.40 ?  6   PRO   D CG  1 
ATOM   3269 C  CD  . PRO   C 1 11  ? -68.318 -0.452  74.125  1.00 30.23 ?  6   PRO   D CD  1 
ATOM   3270 N  N   . TYR   C 1 12  ? -65.564 -1.625  72.027  1.00 21.29 ?  7   TYR   D N   1 
ATOM   3271 C  CA  . TYR   C 1 12  ? -64.170 -1.972  71.612  1.00 21.59 ?  7   TYR   D CA  1 
ATOM   3272 C  C   . TYR   C 1 12  ? -64.038 -3.444  71.247  1.00 23.14 ?  7   TYR   D C   1 
ATOM   3273 O  O   . TYR   C 1 12  ? -62.897 -3.973  71.082  1.00 19.66 ?  7   TYR   D O   1 
ATOM   3274 C  CB  . TYR   C 1 12  ? -63.186 -1.568  72.688  1.00 20.58 ?  7   TYR   D CB  1 
ATOM   3275 C  CG  . TYR   C 1 12  ? -63.219 -0.120  73.078  1.00 20.62 ?  7   TYR   D CG  1 
ATOM   3276 C  CD1 . TYR   C 1 12  ? -63.419 0.877   72.142  1.00 18.21 ?  7   TYR   D CD1 1 
ATOM   3277 C  CD2 . TYR   C 1 12  ? -63.045 0.250   74.399  1.00 22.66 ?  7   TYR   D CD2 1 
ATOM   3278 C  CE1 . TYR   C 1 12  ? -63.431 2.206   72.498  1.00 21.97 ?  7   TYR   D CE1 1 
ATOM   3279 C  CE2 . TYR   C 1 12  ? -63.073 1.583   74.776  1.00 23.28 ?  7   TYR   D CE2 1 
ATOM   3280 C  CZ  . TYR   C 1 12  ? -63.255 2.558   73.816  1.00 23.18 ?  7   TYR   D CZ  1 
ATOM   3281 O  OH  . TYR   C 1 12  ? -63.315 3.881   74.133  1.00 26.53 ?  7   TYR   D OH  1 
ATOM   3282 N  N   . HIS   C 1 13  ? -65.157 -4.137  71.083  1.00 21.98 ?  8   HIS   D N   1 
ATOM   3283 C  CA  . HIS   C 1 13  ? -65.169 -5.504  70.512  1.00 24.45 ?  8   HIS   D CA  1 
ATOM   3284 C  C   . HIS   C 1 13  ? -64.819 -5.467  69.017  1.00 24.66 ?  8   HIS   D C   1 
ATOM   3285 O  O   . HIS   C 1 13  ? -65.277 -4.543  68.281  1.00 23.88 ?  8   HIS   D O   1 
ATOM   3286 C  CB  . HIS   C 1 13  ? -66.538 -6.138  70.766  1.00 27.94 ?  8   HIS   D CB  1 
ATOM   3287 C  CG  . HIS   C 1 13  ? -66.733 -6.577  72.179  1.00 32.55 ?  8   HIS   D CG  1 
ATOM   3288 N  ND1 . HIS   C 1 13  ? -67.253 -7.816  72.499  1.00 42.91 ?  8   HIS   D ND1 1 
ATOM   3289 C  CD2 . HIS   C 1 13  ? -66.480 -5.963  73.353  1.00 35.77 ?  8   HIS   D CD2 1 
ATOM   3290 C  CE1 . HIS   C 1 13  ? -67.299 -7.941  73.816  1.00 44.56 ?  8   HIS   D CE1 1 
ATOM   3291 N  NE2 . HIS   C 1 13  ? -66.828 -6.816  74.363  1.00 39.42 ?  8   HIS   D NE2 1 
ATOM   3292 N  N   . ALA   C 1 14  ? -64.085 -6.484  68.529  1.00 26.93 ?  9   ALA   D N   1 
ATOM   3293 C  CA  . ALA   C 1 14  ? -63.764 -6.590  67.082  1.00 28.57 ?  9   ALA   D CA  1 
ATOM   3294 C  C   . ALA   C 1 14  ? -65.063 -6.744  66.305  1.00 28.30 ?  9   ALA   D C   1 
ATOM   3295 O  O   . ALA   C 1 14  ? -65.983 -7.375  66.791  1.00 25.30 ?  9   ALA   D O   1 
ATOM   3296 C  CB  . ALA   C 1 14  ? -62.856 -7.748  66.814  1.00 29.83 ?  9   ALA   D CB  1 
ATOM   3297 N  N   . PRO   C 1 15  ? -65.184 -6.191  65.086  1.00 29.62 ?  10  PRO   D N   1 
ATOM   3298 C  CA  . PRO   C 1 15  ? -66.379 -6.437  64.284  1.00 32.02 ?  10  PRO   D CA  1 
ATOM   3299 C  C   . PRO   C 1 15  ? -66.532 -7.916  63.882  1.00 32.78 ?  10  PRO   D C   1 
ATOM   3300 O  O   . PRO   C 1 15  ? -67.626 -8.298  63.541  1.00 32.31 ?  10  PRO   D O   1 
ATOM   3301 C  CB  . PRO   C 1 15  ? -66.169 -5.593  63.020  1.00 32.01 ?  10  PRO   D CB  1 
ATOM   3302 C  CG  . PRO   C 1 15  ? -64.693 -5.335  62.988  1.00 32.00 ?  10  PRO   D CG  1 
ATOM   3303 C  CD  . PRO   C 1 15  ? -64.234 -5.282  64.433  1.00 28.04 ?  10  PRO   D CD  1 
ATOM   3304 N  N   . GLU   C 1 16  ? -65.446 -8.693  63.846  1.00 30.33 ?  11  GLU   D N   1 
ATOM   3305 C  CA  . GLU   C 1 16  ? -65.468 -10.128 63.443  1.00 30.13 ?  11  GLU   D CA  1 
ATOM   3306 C  C   . GLU   C 1 16  ? -64.405 -10.879 64.238  1.00 28.85 ?  11  GLU   D C   1 
ATOM   3307 O  O   . GLU   C 1 16  ? -63.362 -10.278 64.503  1.00 25.51 ?  11  GLU   D O   1 
ATOM   3308 C  CB  . GLU   C 1 16  ? -65.113 -10.327 61.962  1.00 37.88 ?  11  GLU   D CB  1 
ATOM   3309 C  CG  . GLU   C 1 16  ? -66.061 -9.669  60.966  1.00 47.79 ?  11  GLU   D CG  1 
ATOM   3310 C  CD  . GLU   C 1 16  ? -67.512 -10.150 61.004  1.00 58.62 ?  11  GLU   D CD  1 
ATOM   3311 O  OE1 . GLU   C 1 16  ? -67.759 -11.244 61.575  1.00 63.84 ?  11  GLU   D OE1 1 
ATOM   3312 O  OE2 . GLU   C 1 16  ? -68.406 -9.423  60.474  1.00 62.14 -1 11  GLU   D OE2 1 
ATOM   3313 N  N   . ASP   C 1 17  ? -64.612 -12.171 64.483  1.00 26.93 ?  12  ASP   D N   1 
ATOM   3314 C  CA  . ASP   C 1 17  ? -63.647 -13.045 65.202  1.00 27.87 ?  12  ASP   D CA  1 
ATOM   3315 C  C   . ASP   C 1 17  ? -62.284 -13.048 64.489  1.00 27.91 ?  12  ASP   D C   1 
ATOM   3316 O  O   . ASP   C 1 17  ? -61.236 -13.178 65.172  1.00 23.77 ?  12  ASP   D O   1 
ATOM   3317 C  CB  . ASP   C 1 17  ? -64.177 -14.481 65.296  1.00 32.62 ?  12  ASP   D CB  1 
ATOM   3318 C  CG  . ASP   C 1 17  ? -65.367 -14.667 66.228  1.00 36.82 ?  12  ASP   D CG  1 
ATOM   3319 O  OD1 . ASP   C 1 17  ? -65.381 -14.028 67.310  1.00 34.23 ?  12  ASP   D OD1 1 
ATOM   3320 O  OD2 . ASP   C 1 17  ? -66.270 -15.468 65.865  1.00 42.83 -1 12  ASP   D OD2 1 
ATOM   3321 N  N   . ARG   C 1 18  ? -62.276 -12.956 63.159  1.00 24.97 ?  13  ARG   D N   1 
ATOM   3322 C  CA  . ARG   C 1 18  ? -61.011 -13.084 62.370  1.00 25.60 ?  13  ARG   D CA  1 
ATOM   3323 C  C   . ARG   C 1 18  ? -60.025 -11.960 62.756  1.00 24.09 ?  13  ARG   D C   1 
ATOM   3324 O  O   . ARG   C 1 18  ? -58.800 -12.190 62.618  1.00 22.85 ?  13  ARG   D O   1 
ATOM   3325 C  CB  . ARG   C 1 18  ? -61.328 -13.115 60.875  1.00 31.90 ?  13  ARG   D CB  1 
ATOM   3326 C  CG  . ARG   C 1 18  ? -60.127 -13.060 59.946  1.00 44.80 ?  13  ARG   D CG  1 
ATOM   3327 C  CD  . ARG   C 1 18  ? -59.391 -14.380 59.804  1.00 55.14 ?  13  ARG   D CD  1 
ATOM   3328 N  NE  . ARG   C 1 18  ? -58.585 -14.454 58.584  1.00 68.28 ?  13  ARG   D NE  1 
ATOM   3329 C  CZ  . ARG   C 1 18  ? -57.703 -15.417 58.288  1.00 72.38 ?  13  ARG   D CZ  1 
ATOM   3330 N  NH1 . ARG   C 1 18  ? -57.458 -16.413 59.128  1.00 67.17 1  13  ARG   D NH1 1 
ATOM   3331 N  NH2 . ARG   C 1 18  ? -57.041 -15.360 57.144  1.00 82.44 ?  13  ARG   D NH2 1 
ATOM   3332 N  N   . TRP   C 1 19  ? -60.500 -10.818 63.279  1.00 21.70 ?  14  TRP   D N   1 
ATOM   3333 C  CA  . TRP   C 1 19  ? -59.612 -9.688  63.668  1.00 22.20 ?  14  TRP   D CA  1 
ATOM   3334 C  C   . TRP   C 1 19  ? -58.646 -10.167 64.753  1.00 20.22 ?  14  TRP   D C   1 
ATOM   3335 O  O   . TRP   C 1 19  ? -57.477 -9.744  64.762  1.00 19.70 ?  14  TRP   D O   1 
ATOM   3336 C  CB  . TRP   C 1 19  ? -60.403 -8.482  64.161  1.00 23.12 ?  14  TRP   D CB  1 
ATOM   3337 C  CG  . TRP   C 1 19  ? -61.002 -7.629  63.089  1.00 23.47 ?  14  TRP   D CG  1 
ATOM   3338 C  CD1 . TRP   C 1 19  ? -61.637 -8.034  61.948  1.00 25.55 ?  14  TRP   D CD1 1 
ATOM   3339 C  CD2 . TRP   C 1 19  ? -60.951 -6.202  63.032  1.00 21.78 ?  14  TRP   D CD2 1 
ATOM   3340 N  NE1 . TRP   C 1 19  ? -62.002 -6.943  61.205  1.00 27.57 ?  14  TRP   D NE1 1 
ATOM   3341 C  CE2 . TRP   C 1 19  ? -61.596 -5.805  61.846  1.00 24.05 ?  14  TRP   D CE2 1 
ATOM   3342 C  CE3 . TRP   C 1 19  ? -60.394 -5.238  63.865  1.00 25.27 ?  14  TRP   D CE3 1 
ATOM   3343 C  CZ2 . TRP   C 1 19  ? -61.708 -4.464  61.471  1.00 25.88 ?  14  TRP   D CZ2 1 
ATOM   3344 C  CZ3 . TRP   C 1 19  ? -60.527 -3.912  63.515  1.00 29.26 ?  14  TRP   D CZ3 1 
ATOM   3345 C  CH2 . TRP   C 1 19  ? -61.184 -3.535  62.337  1.00 28.05 ?  14  TRP   D CH2 1 
ATOM   3346 N  N   . LEU   C 1 20  ? -59.115 -11.014 65.661  1.00 21.68 ?  15  LEU   D N   1 
ATOM   3347 C  CA  . LEU   C 1 20  ? -58.288 -11.526 66.775  1.00 20.62 ?  15  LEU   D CA  1 
ATOM   3348 C  C   . LEU   C 1 20  ? -57.220 -12.444 66.197  1.00 20.51 ?  15  LEU   D C   1 
ATOM   3349 O  O   . LEU   C 1 20  ? -56.076 -12.339 66.613  1.00 18.15 ?  15  LEU   D O   1 
ATOM   3350 C  CB  . LEU   C 1 20  ? -59.141 -12.256 67.816  1.00 21.86 ?  15  LEU   D CB  1 
ATOM   3351 C  CG  . LEU   C 1 20  ? -59.995 -11.396 68.768  1.00 21.63 ?  15  LEU   D CG  1 
ATOM   3352 C  CD1 . LEU   C 1 20  ? -61.265 -10.875 68.092  1.00 21.72 ?  15  LEU   D CD1 1 
ATOM   3353 C  CD2 . LEU   C 1 20  ? -60.386 -12.180 70.022  1.00 20.97 ?  15  LEU   D CD2 1 
ATOM   3354 N  N   . VAL   C 1 21  ? -57.560 -13.288 65.219  1.00 18.28 ?  16  VAL   D N   1 
ATOM   3355 C  CA  . VAL   C 1 21  ? -56.557 -14.187 64.561  1.00 21.10 ?  16  VAL   D CA  1 
ATOM   3356 C  C   . VAL   C 1 21  ? -55.514 -13.332 63.825  1.00 20.48 ?  16  VAL   D C   1 
ATOM   3357 O  O   . VAL   C 1 21  ? -54.301 -13.623 63.961  1.00 19.96 ?  16  VAL   D O   1 
ATOM   3358 C  CB  . VAL   C 1 21  ? -57.215 -15.205 63.616  1.00 22.39 ?  16  VAL   D CB  1 
ATOM   3359 C  CG1 . VAL   C 1 21  ? -56.197 -16.133 62.979  1.00 22.27 ?  16  VAL   D CG1 1 
ATOM   3360 C  CG2 . VAL   C 1 21  ? -58.299 -16.006 64.326  1.00 22.91 ?  16  VAL   D CG2 1 
ATOM   3361 N  N   . ASP   C 1 22  ? -55.968 -12.310 63.094  1.00 20.02 ?  17  ASP   D N   1 
ATOM   3362 C  CA  . ASP   C 1 22  ? -55.089 -11.367 62.356  1.00 22.12 ?  17  ASP   D CA  1 
ATOM   3363 C  C   . ASP   C 1 22  ? -54.106 -10.741 63.332  1.00 20.64 ?  17  ASP   D C   1 
ATOM   3364 O  O   . ASP   C 1 22  ? -52.901 -10.622 62.971  1.00 19.07 ?  17  ASP   D O   1 
ATOM   3365 C  CB  . ASP   C 1 22  ? -55.857 -10.262 61.627  1.00 26.05 ?  17  ASP   D CB  1 
ATOM   3366 C  CG  . ASP   C 1 22  ? -56.721 -10.722 60.474  1.00 34.09 ?  17  ASP   D CG  1 
ATOM   3367 O  OD1 . ASP   C 1 22  ? -56.499 -11.881 59.986  1.00 35.19 ?  17  ASP   D OD1 1 
ATOM   3368 O  OD2 . ASP   C 1 22  ? -57.609 -9.921  60.070  1.00 44.12 -1 17  ASP   D OD2 1 
ATOM   3369 N  N   . LEU   C 1 23  ? -54.558 -10.350 64.524  1.00 20.30 ?  18  LEU   D N   1 
ATOM   3370 C  CA  . LEU   C 1 23  ? -53.630 -9.659  65.457  1.00 20.86 ?  18  LEU   D CA  1 
ATOM   3371 C  C   . LEU   C 1 23  ? -52.600 -10.668 65.923  1.00 19.08 ?  18  LEU   D C   1 
ATOM   3372 O  O   . LEU   C 1 23  ? -51.375 -10.276 65.935  1.00 19.19 ?  18  LEU   D O   1 
ATOM   3373 C  CB  . LEU   C 1 23  ? -54.379 -9.005  66.623  1.00 22.97 ?  18  LEU   D CB  1 
ATOM   3374 C  CG  . LEU   C 1 23  ? -53.558 -8.017  67.466  1.00 25.07 ?  18  LEU   D CG  1 
ATOM   3375 C  CD1 . LEU   C 1 23  ? -54.419 -7.085  68.276  1.00 29.71 ?  18  LEU   D CD1 1 
ATOM   3376 C  CD2 . LEU   C 1 23  ? -52.712 -8.731  68.468  1.00 27.63 ?  18  LEU   D CD2 1 
ATOM   3377 N  N   . VAL   C 1 24  ? -53.015 -11.914 66.254  1.00 19.12 ?  19  VAL   D N   1 
ATOM   3378 C  CA  . VAL   C 1 24  ? -52.045 -12.958 66.703  1.00 19.92 ?  19  VAL   D CA  1 
ATOM   3379 C  C   . VAL   C 1 24  ? -50.997 -13.176 65.601  1.00 19.08 ?  19  VAL   D C   1 
ATOM   3380 O  O   . VAL   C 1 24  ? -49.786 -13.221 65.893  1.00 18.80 ?  19  VAL   D O   1 
ATOM   3381 C  CB  . VAL   C 1 24  ? -52.780 -14.254 67.102  1.00 21.58 ?  19  VAL   D CB  1 
ATOM   3382 C  CG1 . VAL   C 1 24  ? -51.796 -15.414 67.164  1.00 22.16 ?  19  VAL   D CG1 1 
ATOM   3383 C  CG2 . VAL   C 1 24  ? -53.557 -14.087 68.413  1.00 21.07 ?  19  VAL   D CG2 1 
ATOM   3384 N  N   . ARG   C 1 25  ? -51.407 -13.315 64.361  1.00 20.45 ?  20  ARG   D N   1 
ATOM   3385 C  CA  . ARG   C 1 25  ? -50.460 -13.539 63.242  1.00 21.55 ?  20  ARG   D CA  1 
ATOM   3386 C  C   . ARG   C 1 25  ? -49.561 -12.327 63.042  1.00 22.46 ?  20  ARG   D C   1 
ATOM   3387 O  O   . ARG   C 1 25  ? -48.360 -12.561 62.747  1.00 20.70 ?  20  ARG   D O   1 
ATOM   3388 C  CB  . ARG   C 1 25  ? -51.220 -13.897 61.970  1.00 23.83 ?  20  ARG   D CB  1 
ATOM   3389 C  CG  . ARG   C 1 25  ? -51.950 -15.230 61.995  1.00 27.06 ?  20  ARG   D CG  1 
ATOM   3390 C  CD  . ARG   C 1 25  ? -52.452 -15.460 60.565  1.00 28.94 ?  20  ARG   D CD  1 
ATOM   3391 N  NE  . ARG   C 1 25  ? -53.406 -16.535 60.375  1.00 32.39 ?  20  ARG   D NE  1 
ATOM   3392 C  CZ  . ARG   C 1 25  ? -53.131 -17.833 60.424  1.00 34.36 ?  20  ARG   D CZ  1 
ATOM   3393 N  NH1 . ARG   C 1 25  ? -51.899 -18.262 60.667  1.00 36.59 1  20  ARG   D NH1 1 
ATOM   3394 N  NH2 . ARG   C 1 25  ? -54.115 -18.703 60.242  1.00 37.53 ?  20  ARG   D NH2 1 
ATOM   3395 N  N   . GLY   C 1 26  ? -50.071 -11.086 63.217  1.00 18.94 ?  21  GLY   D N   1 
ATOM   3396 C  CA  . GLY   C 1 26  ? -49.302 -9.871  62.940  1.00 19.54 ?  21  GLY   D CA  1 
ATOM   3397 C  C   . GLY   C 1 26  ? -48.293 -9.554  64.019  1.00 17.82 ?  21  GLY   D C   1 
ATOM   3398 O  O   . GLY   C 1 26  ? -47.482 -8.690  63.767  1.00 19.35 ?  21  GLY   D O   1 
ATOM   3399 N  N   . HIS   C 1 27  ? -48.467 -10.117 65.230  1.00 17.22 ?  22  HIS   D N   1 
ATOM   3400 C  CA  . HIS   C 1 27  ? -47.760 -9.694  66.460  1.00 18.06 ?  22  HIS   D CA  1 
ATOM   3401 C  C   . HIS   C 1 27  ? -47.440 -10.904 67.326  1.00 19.35 ?  22  HIS   D C   1 
ATOM   3402 O  O   . HIS   C 1 27  ? -47.873 -11.032 68.485  1.00 19.10 ?  22  HIS   D O   1 
ATOM   3403 C  CB  . HIS   C 1 27  ? -48.647 -8.657  67.175  1.00 16.51 ?  22  HIS   D CB  1 
ATOM   3404 C  CG  . HIS   C 1 27  ? -48.985 -7.541  66.277  1.00 19.48 ?  22  HIS   D CG  1 
ATOM   3405 N  ND1 . HIS   C 1 27  ? -48.164 -6.467  66.139  1.00 19.29 ?  22  HIS   D ND1 1 
ATOM   3406 C  CD2 . HIS   C 1 27  ? -50.028 -7.322  65.463  1.00 19.13 ?  22  HIS   D CD2 1 
ATOM   3407 C  CE1 . HIS   C 1 27  ? -48.686 -5.627  65.268  1.00 23.17 ?  22  HIS   D CE1 1 
ATOM   3408 N  NE2 . HIS   C 1 27  ? -49.804 -6.135  64.804  1.00 19.83 ?  22  HIS   D NE2 1 
ATOM   3409 N  N   . PRO   C 1 28  ? -46.626 -11.839 66.794  1.00 17.99 ?  23  PRO   D N   1 
ATOM   3410 C  CA  . PRO   C 1 28  ? -46.427 -13.122 67.457  1.00 17.89 ?  23  PRO   D CA  1 
ATOM   3411 C  C   . PRO   C 1 28  ? -45.598 -13.117 68.743  1.00 16.85 ?  23  PRO   D C   1 
ATOM   3412 O  O   . PRO   C 1 28  ? -45.599 -14.141 69.398  1.00 16.70 ?  23  PRO   D O   1 
ATOM   3413 C  CB  . PRO   C 1 28  ? -45.680 -13.968 66.390  1.00 17.51 ?  23  PRO   D CB  1 
ATOM   3414 C  CG  . PRO   C 1 28  ? -44.958 -12.931 65.549  1.00 19.16 ?  23  PRO   D CG  1 
ATOM   3415 C  CD  . PRO   C 1 28  ? -45.928 -11.762 65.491  1.00 19.42 ?  23  PRO   D CD  1 
ATOM   3416 N  N   . LEU   C 1 29  ? -44.853 -12.046 69.022  1.00 16.81 ?  24  LEU   D N   1 
ATOM   3417 C  CA  . LEU   C 1 29  ? -44.054 -12.025 70.259  1.00 17.67 ?  24  LEU   D CA  1 
ATOM   3418 C  C   . LEU   C 1 29  ? -45.038 -11.635 71.359  1.00 17.70 ?  24  LEU   D C   1 
ATOM   3419 O  O   . LEU   C 1 29  ? -45.209 -10.417 71.573  1.00 17.24 ?  24  LEU   D O   1 
ATOM   3420 C  CB  . LEU   C 1 29  ? -42.862 -11.078 70.148  1.00 20.45 ?  24  LEU   D CB  1 
ATOM   3421 C  CG  . LEU   C 1 29  ? -41.815 -11.270 71.254  1.00 22.53 ?  24  LEU   D CG  1 
ATOM   3422 C  CD1 . LEU   C 1 29  ? -41.132 -12.618 71.151  1.00 22.23 ?  24  LEU   D CD1 1 
ATOM   3423 C  CD2 . LEU   C 1 29  ? -40.752 -10.183 71.241  1.00 25.44 ?  24  LEU   D CD2 1 
ATOM   3424 N  N   . ALA   C 1 30  ? -45.581 -12.663 72.018  1.00 18.18 ?  25  ALA   D N   1 
ATOM   3425 C  CA  . ALA   C 1 30  ? -46.626 -12.560 73.047  1.00 18.81 ?  25  ALA   D CA  1 
ATOM   3426 C  C   . ALA   C 1 30  ? -45.963 -12.403 74.422  1.00 19.53 ?  25  ALA   D C   1 
ATOM   3427 O  O   . ALA   C 1 30  ? -44.847 -12.852 74.594  1.00 20.18 ?  25  ALA   D O   1 
ATOM   3428 C  CB  . ALA   C 1 30  ? -47.497 -13.777 72.979  1.00 21.83 ?  25  ALA   D CB  1 
ATOM   3429 N  N   . GLN   C 1 31  ? -46.672 -11.773 75.355  1.00 17.77 ?  26  GLN   D N   1 
ATOM   3430 C  CA  . GLN   C 1 31  ? -46.345 -11.869 76.793  1.00 17.38 ?  26  GLN   D CA  1 
ATOM   3431 C  C   . GLN   C 1 31  ? -47.111 -13.037 77.393  1.00 18.64 ?  26  GLN   D C   1 
ATOM   3432 O  O   . GLN   C 1 31  ? -48.370 -12.965 77.482  1.00 18.96 ?  26  GLN   D O   1 
ATOM   3433 C  CB  . GLN   C 1 31  ? -46.634 -10.551 77.507  1.00 16.49 ?  26  GLN   D CB  1 
ATOM   3434 C  CG  . GLN   C 1 31  ? -45.850 -9.400  76.932  1.00 18.97 ?  26  GLN   D CG  1 
ATOM   3435 C  CD  . GLN   C 1 31  ? -45.963 -8.107  77.709  1.00 19.38 ?  26  GLN   D CD  1 
ATOM   3436 O  OE1 . GLN   C 1 31  ? -46.171 -8.107  78.924  1.00 21.24 ?  26  GLN   D OE1 1 
ATOM   3437 N  NE2 . GLN   C 1 31  ? -45.727 -7.009  77.018  1.00 19.12 ?  26  GLN   D NE2 1 
ATOM   3438 N  N   . LEU   C 1 32  ? -46.379 -14.073 77.769  1.00 17.43 ?  27  LEU   D N   1 
ATOM   3439 C  CA  . LEU   C 1 32  ? -46.982 -15.276 78.406  1.00 17.39 ?  27  LEU   D CA  1 
ATOM   3440 C  C   . LEU   C 1 32  ? -46.957 -15.029 79.913  1.00 17.68 ?  27  LEU   D C   1 
ATOM   3441 O  O   . LEU   C 1 32  ? -45.876 -14.778 80.452  1.00 16.14 ?  27  LEU   D O   1 
ATOM   3442 C  CB  . LEU   C 1 32  ? -46.194 -16.501 77.992  1.00 18.49 ?  27  LEU   D CB  1 
ATOM   3443 C  CG  . LEU   C 1 32  ? -46.635 -17.813 78.630  1.00 20.73 ?  27  LEU   D CG  1 
ATOM   3444 C  CD1 . LEU   C 1 32  ? -48.036 -18.230 78.180  1.00 22.54 ?  27  LEU   D CD1 1 
ATOM   3445 C  CD2 . LEU   C 1 32  ? -45.619 -18.892 78.319  1.00 22.24 ?  27  LEU   D CD2 1 
ATOM   3446 N  N   . ALA   C 1 33  ? -48.120 -15.040 80.560  1.00 15.95 ?  28  ALA   D N   1 
ATOM   3447 C  CA  . ALA   C 1 33  ? -48.188 -14.831 82.032  1.00 15.69 ?  28  ALA   D CA  1 
ATOM   3448 C  C   . ALA   C 1 33  ? -48.787 -16.066 82.718  1.00 16.12 ?  28  ALA   D C   1 
ATOM   3449 O  O   . ALA   C 1 33  ? -49.805 -16.616 82.283  1.00 18.60 ?  28  ALA   D O   1 
ATOM   3450 C  CB  . ALA   C 1 33  ? -48.937 -13.581 82.362  1.00 17.40 ?  28  ALA   D CB  1 
ATOM   3451 N  N   . SER   C 1 34  ? -48.224 -16.400 83.863  1.00 18.37 ?  29  SER   D N   1 
ATOM   3452 C  CA  . SER   C 1 34  ? -48.778 -17.439 84.749  1.00 20.22 ?  29  SER   D CA  1 
ATOM   3453 C  C   . SER   C 1 34  ? -48.641 -16.973 86.190  1.00 21.15 ?  29  SER   D C   1 
ATOM   3454 O  O   . SER   C 1 34  ? -47.788 -16.111 86.462  1.00 21.03 ?  29  SER   D O   1 
ATOM   3455 C  CB  . SER   C 1 34  ? -48.137 -18.759 84.510  1.00 19.96 ?  29  SER   D CB  1 
ATOM   3456 O  OG  . SER   C 1 34  ? -46.742 -18.718 84.762  1.00 22.01 ?  29  SER   D OG  1 
ATOM   3457 N  N   . ASN   C 1 35  ? -49.464 -17.530 87.073  1.00 21.13 ?  30  ASN   D N   1 
ATOM   3458 C  CA  . ASN   C 1 35  ? -49.477 -17.107 88.497  1.00 24.39 ?  30  ASN   D CA  1 
ATOM   3459 C  C   . ASN   C 1 35  ? -48.122 -17.301 89.167  1.00 25.08 ?  30  ASN   D C   1 
ATOM   3460 O  O   . ASN   C 1 35  ? -47.425 -18.288 88.911  1.00 24.43 ?  30  ASN   D O   1 
ATOM   3461 C  CB  . ASN   C 1 35  ? -50.516 -17.872 89.300  1.00 26.60 ?  30  ASN   D CB  1 
ATOM   3462 C  CG  . ASN   C 1 35  ? -51.913 -17.402 88.991  1.00 27.48 ?  30  ASN   D CG  1 
ATOM   3463 O  OD1 . ASN   C 1 35  ? -52.107 -16.334 88.413  1.00 24.44 ?  30  ASN   D OD1 1 
ATOM   3464 N  ND2 . ASN   C 1 35  ? -52.899 -18.198 89.381  1.00 34.18 ?  30  ASN   D ND2 1 
ATOM   3465 N  N   . GLY   C 1 36  ? -47.756 -16.347 90.025  1.00 25.94 ?  31  GLY   D N   1 
ATOM   3466 C  CA  . GLY   C 1 36  ? -46.558 -16.424 90.862  1.00 26.70 ?  31  GLY   D CA  1 
ATOM   3467 C  C   . GLY   C 1 36  ? -46.913 -17.249 92.081  1.00 29.09 ?  31  GLY   D C   1 
ATOM   3468 O  O   . GLY   C 1 36  ? -48.086 -17.241 92.443  1.00 32.94 ?  31  GLY   D O   1 
ATOM   3469 N  N   . ALA   C 1 37  ? -45.981 -18.041 92.582  1.00 32.32 ?  32  ALA   D N   1 
ATOM   3470 C  CA  . ALA   C 1 37  ? -46.195 -18.948 93.735  1.00 34.39 ?  32  ALA   D CA  1 
ATOM   3471 C  C   . ALA   C 1 37  ? -46.198 -18.108 95.008  1.00 36.93 ?  32  ALA   D C   1 
ATOM   3472 O  O   . ALA   C 1 37  ? -45.394 -17.177 95.064  1.00 34.12 ?  32  ALA   D O   1 
ATOM   3473 C  CB  . ALA   C 1 37  ? -45.084 -19.957 93.760  1.00 36.57 ?  32  ALA   D CB  1 
ATOM   3474 N  N   . GLY   C 1 38  ? -47.043 -18.453 95.985  1.00 41.94 ?  33  GLY   D N   1 
ATOM   3475 C  CA  . GLY   C 1 38  ? -47.101 -17.812 97.315  1.00 47.18 ?  33  GLY   D CA  1 
ATOM   3476 C  C   . GLY   C 1 38  ? -47.566 -16.367 97.218  1.00 47.52 ?  33  GLY   D C   1 
ATOM   3477 O  O   . GLY   C 1 38  ? -46.919 -15.510 97.829  1.00 48.97 ?  33  GLY   D O   1 
ATOM   3478 N  N   . GLY   C 1 39  ? -48.617 -16.105 96.431  1.00 44.98 ?  34  GLY   D N   1 
ATOM   3479 C  CA  . GLY   C 1 39  ? -49.140 -14.752 96.144  1.00 43.95 ?  34  GLY   D CA  1 
ATOM   3480 C  C   . GLY   C 1 39  ? -48.083 -13.790 95.596  1.00 40.09 ?  34  GLY   D C   1 
ATOM   3481 O  O   . GLY   C 1 39  ? -48.316 -12.564 95.677  1.00 42.86 ?  34  GLY   D O   1 
ATOM   3482 N  N   . ALA   C 1 40  ? -46.959 -14.276 95.068  1.00 34.17 ?  35  ALA   D N   1 
ATOM   3483 C  CA  . ALA   C 1 40  ? -45.979 -13.422 94.349  1.00 34.62 ?  35  ALA   D CA  1 
ATOM   3484 C  C   . ALA   C 1 40  ? -46.619 -12.959 93.031  1.00 30.68 ?  35  ALA   D C   1 
ATOM   3485 O  O   . ALA   C 1 40  ? -47.704 -13.445 92.658  1.00 32.57 ?  35  ALA   D O   1 
ATOM   3486 C  CB  . ALA   C 1 40  ? -44.659 -14.121 94.132  1.00 34.07 ?  35  ALA   D CB  1 
ATOM   3487 N  N   . ALA   C 1 41  ? -46.048 -11.921 92.430  1.00 30.29 ?  36  ALA   D N   1 
ATOM   3488 C  CA  . ALA   C 1 41  ? -46.491 -11.372 91.130  1.00 28.03 ?  36  ALA   D CA  1 
ATOM   3489 C  C   . ALA   C 1 41  ? -46.358 -12.470 90.080  1.00 23.63 ?  36  ALA   D C   1 
ATOM   3490 O  O   . ALA   C 1 41  ? -45.429 -13.287 90.131  1.00 22.39 ?  36  ALA   D O   1 
ATOM   3491 C  CB  . ALA   C 1 41  ? -45.649 -10.181 90.748  1.00 23.62 ?  36  ALA   D CB  1 
ATOM   3492 N  N   . PRO   C 1 42  ? -47.207 -12.452 89.042  1.00 22.26 ?  37  PRO   D N   1 
ATOM   3493 C  CA  . PRO   C 1 42  ? -47.015 -13.359 87.915  1.00 20.55 ?  37  PRO   D CA  1 
ATOM   3494 C  C   . PRO   C 1 42  ? -45.627 -13.346 87.274  1.00 20.28 ?  37  PRO   D C   1 
ATOM   3495 O  O   . PRO   C 1 42  ? -45.011 -12.282 87.247  1.00 20.62 ?  37  PRO   D O   1 
ATOM   3496 C  CB  . PRO   C 1 42  ? -48.007 -12.843 86.885  1.00 21.11 ?  37  PRO   D CB  1 
ATOM   3497 C  CG  . PRO   C 1 42  ? -49.141 -12.277 87.730  1.00 22.15 ?  37  PRO   D CG  1 
ATOM   3498 C  CD  . PRO   C 1 42  ? -48.420 -11.627 88.894  1.00 22.36 ?  37  PRO   D CD  1 
ATOM   3499 N  N   . HIS   C 1 43  ? -45.260 -14.508 86.724  1.00 19.39 ?  38  HIS   D N   1 
ATOM   3500 C  CA  . HIS   C 1 43  ? -44.161 -14.678 85.748  1.00 20.48 ?  38  HIS   D CA  1 
ATOM   3501 C  C   . HIS   C 1 43  ? -44.666 -14.144 84.407  1.00 17.87 ?  38  HIS   D C   1 
ATOM   3502 O  O   . HIS   C 1 43  ? -45.818 -14.414 84.042  1.00 19.27 ?  38  HIS   D O   1 
ATOM   3503 C  CB  . HIS   C 1 43  ? -43.724 -16.139 85.577  1.00 22.64 ?  38  HIS   D CB  1 
ATOM   3504 C  CG  . HIS   C 1 43  ? -43.365 -16.828 86.846  1.00 28.10 ?  38  HIS   D CG  1 
ATOM   3505 N  ND1 . HIS   C 1 43  ? -42.075 -16.879 87.313  1.00 36.58 ?  38  HIS   D ND1 1 
ATOM   3506 C  CD2 . HIS   C 1 43  ? -44.138 -17.520 87.717  1.00 32.26 ?  38  HIS   D CD2 1 
ATOM   3507 C  CE1 . HIS   C 1 43  ? -42.055 -17.573 88.442  1.00 35.99 ?  38  HIS   D CE1 1 
ATOM   3508 N  NE2 . HIS   C 1 43  ? -43.322 -17.956 88.717  1.00 35.10 ?  38  HIS   D NE2 1 
ATOM   3509 N  N   . ILE   C 1 44  ? -43.818 -13.418 83.716  1.00 19.15 ?  39  ILE   D N   1 
ATOM   3510 C  CA  . ILE   C 1 44  ? -44.077 -12.831 82.370  1.00 16.59 ?  39  ILE   D CA  1 
ATOM   3511 C  C   . ILE   C 1 44  ? -42.857 -13.148 81.508  1.00 17.68 ?  39  ILE   D C   1 
ATOM   3512 O  O   . ILE   C 1 44  ? -41.755 -12.723 81.874  1.00 19.23 ?  39  ILE   D O   1 
ATOM   3513 C  CB  . ILE   C 1 44  ? -44.252 -11.292 82.424  1.00 19.90 ?  39  ILE   D CB  1 
ATOM   3514 C  CG1 . ILE   C 1 44  ? -45.255 -10.815 83.477  1.00 19.75 ?  39  ILE   D CG1 1 
ATOM   3515 C  CG2 . ILE   C 1 44  ? -44.552 -10.695 81.066  1.00 19.86 ?  39  ILE   D CG2 1 
ATOM   3516 C  CD1 . ILE   C 1 44  ? -46.690 -11.117 83.165  1.00 21.35 ?  39  ILE   D CD1 1 
ATOM   3517 N  N   . THR   C 1 45  ? -43.050 -13.840 80.406  1.00 16.68 ?  40  THR   D N   1 
ATOM   3518 C  CA  . THR   C 1 45  ? -41.975 -14.037 79.407  1.00 17.76 ?  40  THR   D CA  1 
ATOM   3519 C  C   . THR   C 1 45  ? -42.483 -13.673 78.020  1.00 16.93 ?  40  THR   D C   1 
ATOM   3520 O  O   . THR   C 1 45  ? -43.657 -14.007 77.674  1.00 15.48 ?  40  THR   D O   1 
ATOM   3521 C  CB  . THR   C 1 45  ? -41.472 -15.482 79.421  1.00 20.10 ?  40  THR   D CB  1 
ATOM   3522 O  OG1 . THR   C 1 45  ? -41.042 -15.791 80.743  1.00 20.32 ?  40  THR   D OG1 1 
ATOM   3523 C  CG2 . THR   C 1 45  ? -40.341 -15.675 78.450  1.00 18.21 ?  40  THR   D CG2 1 
ATOM   3524 N  N   . HIS   C 1 46  ? -41.664 -12.944 77.279  1.00 18.59 ?  41  HIS   D N   1 
ATOM   3525 C  CA  . HIS   C 1 46  ? -41.885 -12.641 75.848  1.00 18.76 ?  41  HIS   D CA  1 
ATOM   3526 C  C   . HIS   C 1 46  ? -41.508 -13.865 75.013  1.00 18.68 ?  41  HIS   D C   1 
ATOM   3527 O  O   . HIS   C 1 46  ? -40.335 -14.232 75.006  1.00 15.87 ?  41  HIS   D O   1 
ATOM   3528 C  CB  . HIS   C 1 46  ? -41.125 -11.407 75.374  1.00 18.76 ?  41  HIS   D CB  1 
ATOM   3529 C  CG  . HIS   C 1 46  ? -41.590 -10.158 76.046  1.00 23.74 ?  41  HIS   D CG  1 
ATOM   3530 N  ND1 . HIS   C 1 46  ? -42.363 -9.198  75.424  1.00 30.80 ?  41  HIS   D ND1 1 
ATOM   3531 C  CD2 . HIS   C 1 46  ? -41.350 -9.713  77.291  1.00 27.43 ?  41  HIS   D CD2 1 
ATOM   3532 C  CE1 . HIS   C 1 46  ? -42.567 -8.206  76.261  1.00 28.08 ?  41  HIS   D CE1 1 
ATOM   3533 N  NE2 . HIS   C 1 46  ? -41.972 -8.506  77.422  1.00 30.05 ?  41  HIS   D NE2 1 
ATOM   3534 N  N   . VAL   C 1 47  ? -42.502 -14.470 74.367  1.00 15.90 ?  42  VAL   D N   1 
ATOM   3535 C  CA  . VAL   C 1 47  ? -42.351 -15.747 73.633  1.00 17.39 ?  42  VAL   D CA  1 
ATOM   3536 C  C   . VAL   C 1 47  ? -43.012 -15.641 72.270  1.00 17.86 ?  42  VAL   D C   1 
ATOM   3537 O  O   . VAL   C 1 47  ? -44.102 -15.057 72.134  1.00 17.14 ?  42  VAL   D O   1 
ATOM   3538 C  CB  . VAL   C 1 47  ? -42.907 -16.918 74.444  1.00 18.33 ?  42  VAL   D CB  1 
ATOM   3539 C  CG1 . VAL   C 1 47  ? -42.151 -17.081 75.743  1.00 19.36 ?  42  VAL   D CG1 1 
ATOM   3540 C  CG2 . VAL   C 1 47  ? -44.390 -16.734 74.737  1.00 18.51 ?  42  VAL   D CG2 1 
ATOM   3541 N  N   . PRO   C 1 48  ? -42.422 -16.258 71.234  1.00 17.81 ?  43  PRO   D N   1 
ATOM   3542 C  CA  . PRO   C 1 48  ? -43.017 -16.324 69.904  1.00 18.14 ?  43  PRO   D CA  1 
ATOM   3543 C  C   . PRO   C 1 48  ? -44.095 -17.405 69.845  1.00 17.68 ?  43  PRO   D C   1 
ATOM   3544 O  O   . PRO   C 1 48  ? -43.807 -18.576 70.126  1.00 18.03 ?  43  PRO   D O   1 
ATOM   3545 C  CB  . PRO   C 1 48  ? -41.833 -16.702 69.004  1.00 19.23 ?  43  PRO   D CB  1 
ATOM   3546 C  CG  . PRO   C 1 48  ? -40.939 -17.484 69.884  1.00 21.38 ?  43  PRO   D CG  1 
ATOM   3547 C  CD  . PRO   C 1 48  ? -41.107 -16.936 71.281  1.00 19.22 ?  43  PRO   D CD  1 
ATOM   3548 N  N   . ILE   C 1 49  ? -45.310 -17.001 69.471  1.00 17.80 ?  44  ILE   D N   1 
ATOM   3549 C  CA  . ILE   C 1 49  ? -46.471 -17.905 69.468  1.00 17.95 ?  44  ILE   D CA  1 
ATOM   3550 C  C   . ILE   C 1 49  ? -47.124 -17.805 68.096  1.00 18.60 ?  44  ILE   D C   1 
ATOM   3551 O  O   . ILE   C 1 49  ? -47.323 -16.681 67.595  1.00 19.11 ?  44  ILE   D O   1 
ATOM   3552 C  CB  . ILE   C 1 49  ? -47.427 -17.589 70.604  1.00 18.96 ?  44  ILE   D CB  1 
ATOM   3553 C  CG1 . ILE   C 1 49  ? -46.786 -17.870 71.959  1.00 18.85 ?  44  ILE   D CG1 1 
ATOM   3554 C  CG2 . ILE   C 1 49  ? -48.678 -18.426 70.394  1.00 17.57 ?  44  ILE   D CG2 1 
ATOM   3555 C  CD1 . ILE   C 1 49  ? -47.694 -17.566 73.164  1.00 21.16 ?  44  ILE   D CD1 1 
ATOM   3556 N  N   . ILE   C 1 50  ? -47.370 -18.974 67.491  1.00 16.93 ?  45  ILE   D N   1 
ATOM   3557 C  CA  . ILE   C 1 50  ? -48.079 -19.094 66.193  1.00 18.77 ?  45  ILE   D CA  1 
ATOM   3558 C  C   . ILE   C 1 50  ? -49.336 -19.968 66.332  1.00 18.22 ?  45  ILE   D C   1 
ATOM   3559 O  O   . ILE   C 1 50  ? -49.440 -20.837 67.249  1.00 17.92 ?  45  ILE   D O   1 
ATOM   3560 C  CB  . ILE   C 1 50  ? -47.138 -19.669 65.123  1.00 20.25 ?  45  ILE   D CB  1 
ATOM   3561 C  CG1 . ILE   C 1 50  ? -46.694 -21.103 65.462  1.00 21.67 ?  45  ILE   D CG1 1 
ATOM   3562 C  CG2 . ILE   C 1 50  ? -45.929 -18.777 64.947  1.00 20.35 ?  45  ILE   D CG2 1 
ATOM   3563 C  CD1 . ILE   C 1 50  ? -46.031 -21.808 64.305  1.00 23.17 ?  45  ILE   D CD1 1 
ATOM   3564 N  N   . VAL   C 1 51  ? -50.235 -19.762 65.395  1.00 21.31 ?  46  VAL   D N   1 
ATOM   3565 C  CA  . VAL   C 1 51  ? -51.411 -20.658 65.204  1.00 22.57 ?  46  VAL   D CA  1 
ATOM   3566 C  C   . VAL   C 1 51  ? -50.904 -22.025 64.702  1.00 23.86 ?  46  VAL   D C   1 
ATOM   3567 O  O   . VAL   C 1 51  ? -49.957 -22.072 63.878  1.00 21.06 ?  46  VAL   D O   1 
ATOM   3568 C  CB  . VAL   C 1 51  ? -52.400 -19.992 64.230  1.00 26.60 ?  46  VAL   D CB  1 
ATOM   3569 C  CG1 . VAL   C 1 51  ? -53.515 -20.940 63.830  1.00 29.44 ?  46  VAL   D CG1 1 
ATOM   3570 C  CG2 . VAL   C 1 51  ? -52.955 -18.685 64.804  1.00 27.89 ?  46  VAL   D CG2 1 
ATOM   3571 N  N   . ASP   C 1 52  ? -51.472 -23.113 65.234  1.00 23.00 ?  47  ASP   D N   1 
ATOM   3572 C  CA  . ASP   C 1 52  ? -51.254 -24.514 64.796  1.00 25.33 ?  47  ASP   D CA  1 
ATOM   3573 C  C   . ASP   C 1 52  ? -51.029 -24.547 63.286  1.00 24.61 ?  47  ASP   D C   1 
ATOM   3574 O  O   . ASP   C 1 52  ? -51.941 -24.266 62.514  1.00 22.32 ?  47  ASP   D O   1 
ATOM   3575 C  CB  . ASP   C 1 52  ? -52.482 -25.348 65.173  1.00 28.24 ?  47  ASP   D CB  1 
ATOM   3576 C  CG  . ASP   C 1 52  ? -52.428 -26.824 64.809  1.00 31.70 ?  47  ASP   D CG  1 
ATOM   3577 O  OD1 . ASP   C 1 52  ? -51.431 -27.274 64.202  1.00 28.36 ?  47  ASP   D OD1 1 
ATOM   3578 O  OD2 . ASP   C 1 52  ? -53.425 -27.501 65.135  1.00 30.54 -1 47  ASP   D OD2 1 
ATOM   3579 N  N   . PRO   C 1 53  ? -49.812 -24.845 62.807  1.00 24.60 ?  48  PRO   D N   1 
ATOM   3580 C  CA  . PRO   C 1 53  ? -49.544 -24.792 61.371  1.00 27.22 ?  48  PRO   D CA  1 
ATOM   3581 C  C   . PRO   C 1 53  ? -50.211 -25.915 60.567  1.00 29.91 ?  48  PRO   D C   1 
ATOM   3582 O  O   . PRO   C 1 53  ? -50.153 -25.848 59.351  1.00 30.04 ?  48  PRO   D O   1 
ATOM   3583 C  CB  . PRO   C 1 53  ? -48.030 -24.975 61.300  1.00 28.46 ?  48  PRO   D CB  1 
ATOM   3584 C  CG  . PRO   C 1 53  ? -47.717 -25.779 62.540  1.00 27.61 ?  48  PRO   D CG  1 
ATOM   3585 C  CD  . PRO   C 1 53  ? -48.605 -25.156 63.585  1.00 25.66 ?  48  PRO   D CD  1 
ATOM   3586 N  N   . GLU   C 1 54  ? -50.771 -26.923 61.250  1.00 30.18 ?  49  GLU   D N   1 
ATOM   3587 C  CA  . GLU   C 1 54  ? -51.418 -28.098 60.593  1.00 30.93 ?  49  GLU   D CA  1 
ATOM   3588 C  C   . GLU   C 1 54  ? -52.857 -27.749 60.214  1.00 35.55 ?  49  GLU   D C   1 
ATOM   3589 O  O   . GLU   C 1 54  ? -53.468 -28.525 59.473  1.00 35.26 ?  49  GLU   D O   1 
ATOM   3590 C  CB  . GLU   C 1 54  ? -51.352 -29.329 61.496  1.00 34.92 ?  49  GLU   D CB  1 
ATOM   3591 C  CG  . GLU   C 1 54  ? -49.932 -29.773 61.788  1.00 40.74 ?  49  GLU   D CG  1 
ATOM   3592 C  CD  . GLU   C 1 54  ? -49.330 -30.707 60.737  1.00 55.61 ?  49  GLU   D CD  1 
ATOM   3593 O  OE1 . GLU   C 1 54  ? -48.864 -31.795 61.138  1.00 69.01 ?  49  GLU   D OE1 1 
ATOM   3594 O  OE2 . GLU   C 1 54  ? -49.328 -30.363 59.514  1.00 55.45 -1 49  GLU   D OE2 1 
ATOM   3595 N  N   . LEU   C 1 55  ? -53.400 -26.635 60.705  1.00 32.57 ?  50  LEU   D N   1 
ATOM   3596 C  CA  . LEU   C 1 55  ? -54.740 -26.182 60.257  1.00 37.82 ?  50  LEU   D CA  1 
ATOM   3597 C  C   . LEU   C 1 55  ? -54.592 -25.713 58.810  1.00 44.95 ?  50  LEU   D C   1 
ATOM   3598 O  O   . LEU   C 1 55  ? -53.845 -24.758 58.558  1.00 45.97 ?  50  LEU   D O   1 
ATOM   3599 C  CB  . LEU   C 1 55  ? -55.269 -25.071 61.163  1.00 36.32 ?  50  LEU   D CB  1 
ATOM   3600 C  CG  . LEU   C 1 55  ? -55.483 -25.483 62.616  1.00 37.04 ?  50  LEU   D CG  1 
ATOM   3601 C  CD1 . LEU   C 1 55  ? -55.839 -24.267 63.452  1.00 37.69 ?  50  LEU   D CD1 1 
ATOM   3602 C  CD2 . LEU   C 1 55  ? -56.571 -26.546 62.725  1.00 39.63 ?  50  LEU   D CD2 1 
ATOM   3603 N  N   . ASP   C 1 56  ? -55.216 -26.448 57.899  1.00 52.16 ?  51  ASP   D N   1 
ATOM   3604 C  CA  . ASP   C 1 56  ? -55.450 -26.016 56.502  1.00 59.32 ?  51  ASP   D CA  1 
ATOM   3605 C  C   . ASP   C 1 56  ? -56.806 -25.295 56.503  1.00 55.25 ?  51  ASP   D C   1 
ATOM   3606 O  O   . ASP   C 1 56  ? -57.691 -25.671 57.310  1.00 59.73 ?  51  ASP   D O   1 
ATOM   3607 C  CB  . ASP   C 1 56  ? -55.319 -27.206 55.539  1.00 64.66 ?  51  ASP   D CB  1 
ATOM   3608 C  CG  . ASP   C 1 56  ? -53.922 -27.824 55.517  1.00 71.37 ?  51  ASP   D CG  1 
ATOM   3609 O  OD1 . ASP   C 1 56  ? -53.183 -27.582 54.534  1.00 73.16 ?  51  ASP   D OD1 1 
ATOM   3610 O  OD2 . ASP   C 1 56  ? -53.573 -28.553 56.481  1.00 75.16 -1 51  ASP   D OD2 1 
ATOM   3611 N  N   . GLY   C 1 57  ? -56.944 -24.267 55.669  1.00 52.37 ?  52  GLY   D N   1 
ATOM   3612 C  CA  . GLY   C 1 57  ? -58.205 -23.514 55.517  1.00 46.57 ?  52  GLY   D CA  1 
ATOM   3613 C  C   . GLY   C 1 57  ? -58.215 -22.301 56.438  1.00 41.54 ?  52  GLY   D C   1 
ATOM   3614 O  O   . GLY   C 1 57  ? -57.430 -22.233 57.385  1.00 38.91 ?  52  GLY   D O   1 
ATOM   3615 N  N   . PRO   C 1 58  ? -59.107 -21.321 56.185  1.00 39.68 ?  53  PRO   D N   1 
ATOM   3616 C  CA  . PRO   C 1 58  ? -59.122 -20.079 56.953  1.00 37.65 ?  53  PRO   D CA  1 
ATOM   3617 C  C   . PRO   C 1 58  ? -59.382 -20.406 58.429  1.00 35.70 ?  53  PRO   D C   1 
ATOM   3618 O  O   . PRO   C 1 58  ? -60.202 -21.259 58.707  1.00 33.04 ?  53  PRO   D O   1 
ATOM   3619 C  CB  . PRO   C 1 58  ? -60.265 -19.236 56.370  1.00 35.86 ?  53  PRO   D CB  1 
ATOM   3620 C  CG  . PRO   C 1 58  ? -60.670 -19.930 55.084  1.00 40.30 ?  53  PRO   D CG  1 
ATOM   3621 C  CD  . PRO   C 1 58  ? -60.159 -21.355 55.155  1.00 40.66 ?  53  PRO   D CD  1 
ATOM   3622 N  N   . VAL   C 1 59  ? -58.621 -19.768 59.313  1.00 31.68 ?  54  VAL   D N   1 
ATOM   3623 C  CA  . VAL   C 1 59  ? -58.819 -19.821 60.784  1.00 29.43 ?  54  VAL   D CA  1 
ATOM   3624 C  C   . VAL   C 1 59  ? -59.562 -18.540 61.135  1.00 29.79 ?  54  VAL   D C   1 
ATOM   3625 O  O   . VAL   C 1 59  ? -58.952 -17.459 61.086  1.00 29.89 ?  54  VAL   D O   1 
ATOM   3626 C  CB  . VAL   C 1 59  ? -57.466 -19.948 61.507  1.00 28.24 ?  54  VAL   D CB  1 
ATOM   3627 C  CG1 . VAL   C 1 59  ? -57.634 -20.049 63.006  1.00 29.89 ?  54  VAL   D CG1 1 
ATOM   3628 C  CG2 . VAL   C 1 59  ? -56.669 -21.127 60.967  1.00 30.31 ?  54  VAL   D CG2 1 
ATOM   3629 N  N   . ASP   C 1 60  ? -60.852 -18.658 61.395  1.00 32.54 ?  55  ASP   D N   1 
ATOM   3630 C  CA  . ASP   C 1 60  ? -61.760 -17.506 61.633  1.00 34.96 ?  55  ASP   D CA  1 
ATOM   3631 C  C   . ASP   C 1 60  ? -61.897 -17.201 63.125  1.00 30.07 ?  55  ASP   D C   1 
ATOM   3632 O  O   . ASP   C 1 60  ? -62.321 -16.087 63.430  1.00 32.28 ?  55  ASP   D O   1 
ATOM   3633 C  CB  . ASP   C 1 60  ? -63.124 -17.781 60.995  1.00 40.34 ?  55  ASP   D CB  1 
ATOM   3634 C  CG  . ASP   C 1 60  ? -63.066 -17.732 59.476  1.00 47.90 ?  55  ASP   D CG  1 
ATOM   3635 O  OD1 . ASP   C 1 60  ? -62.215 -16.973 58.945  1.00 48.85 ?  55  ASP   D OD1 1 
ATOM   3636 O  OD2 . ASP   C 1 60  ? -63.849 -18.463 58.838  1.00 56.16 -1 55  ASP   D OD2 1 
ATOM   3637 N  N   . ARG   C 1 61  ? -61.609 -18.159 64.003  1.00 25.99 ?  56  ARG   D N   1 
ATOM   3638 C  CA  . ARG   C 1 61  ? -61.793 -18.045 65.472  1.00 28.97 ?  56  ARG   D CA  1 
ATOM   3639 C  C   . ARG   C 1 61  ? -60.569 -18.635 66.185  1.00 25.00 ?  56  ARG   D C   1 
ATOM   3640 O  O   . ARG   C 1 61  ? -60.074 -19.715 65.781  1.00 27.45 ?  56  ARG   D O   1 
ATOM   3641 C  CB  . ARG   C 1 61  ? -62.999 -18.861 65.965  1.00 34.74 ?  56  ARG   D CB  1 
ATOM   3642 C  CG  . ARG   C 1 61  ? -64.348 -18.210 65.732  1.00 45.74 ?  56  ARG   D CG  1 
ATOM   3643 C  CD  . ARG   C 1 61  ? -65.514 -19.135 66.052  1.00 51.81 ?  56  ARG   D CD  1 
ATOM   3644 N  NE  . ARG   C 1 61  ? -66.006 -19.755 64.826  1.00 59.94 ?  56  ARG   D NE  1 
ATOM   3645 C  CZ  . ARG   C 1 61  ? -65.739 -20.995 64.413  1.00 68.24 ?  56  ARG   D CZ  1 
ATOM   3646 N  NH1 . ARG   C 1 61  ? -64.996 -21.823 65.135  1.00 74.18 1  56  ARG   D NH1 1 
ATOM   3647 N  NH2 . ARG   C 1 61  ? -66.236 -21.410 63.264  1.00 69.64 ?  56  ARG   D NH2 1 
ATOM   3648 N  N   . LEU   C 1 62  ? -60.171 -18.023 67.290  1.00 23.46 ?  57  LEU   D N   1 
ATOM   3649 C  CA  . LEU   C 1 62  ? -59.112 -18.546 68.171  1.00 23.29 ?  57  LEU   D CA  1 
ATOM   3650 C  C   . LEU   C 1 62  ? -59.643 -19.621 69.125  1.00 24.28 ?  57  LEU   D C   1 
ATOM   3651 O  O   . LEU   C 1 62  ? -58.909 -20.546 69.397  1.00 23.44 ?  57  LEU   D O   1 
ATOM   3652 C  CB  . LEU   C 1 62  ? -58.491 -17.385 68.955  1.00 23.87 ?  57  LEU   D CB  1 
ATOM   3653 C  CG  . LEU   C 1 62  ? -57.560 -16.472 68.161  1.00 24.27 ?  57  LEU   D CG  1 
ATOM   3654 C  CD1 . LEU   C 1 62  ? -57.058 -15.326 69.026  1.00 23.73 ?  57  LEU   D CD1 1 
ATOM   3655 C  CD2 . LEU   C 1 62  ? -56.399 -17.220 67.501  1.00 24.73 ?  57  LEU   D CD2 1 
ATOM   3656 N  N   . VAL   C 1 63  ? -60.871 -19.506 69.634  1.00 23.97 ?  58  VAL   D N   1 
ATOM   3657 C  CA  . VAL   C 1 63  ? -61.359 -20.462 70.662  1.00 24.25 ?  58  VAL   D CA  1 
ATOM   3658 C  C   . VAL   C 1 63  ? -61.432 -21.831 69.991  1.00 22.94 ?  58  VAL   D C   1 
ATOM   3659 O  O   . VAL   C 1 63  ? -61.957 -21.941 68.880  1.00 26.62 ?  58  VAL   D O   1 
ATOM   3660 C  CB  . VAL   C 1 63  ? -62.710 -20.053 71.285  1.00 26.07 ?  58  VAL   D CB  1 
ATOM   3661 C  CG1 . VAL   C 1 63  ? -63.272 -21.184 72.153  1.00 27.96 ?  58  VAL   D CG1 1 
ATOM   3662 C  CG2 . VAL   C 1 63  ? -62.568 -18.775 72.110  1.00 24.92 ?  58  VAL   D CG2 1 
ATOM   3663 N  N   . GLY   C 1 64  ? -60.868 -22.831 70.648  1.00 24.77 ?  59  GLY   D N   1 
ATOM   3664 C  CA  . GLY   C 1 64  ? -60.885 -24.219 70.189  1.00 25.84 ?  59  GLY   D CA  1 
ATOM   3665 C  C   . GLY   C 1 64  ? -59.656 -24.592 69.380  1.00 27.62 ?  59  GLY   D C   1 
ATOM   3666 O  O   . GLY   C 1 64  ? -59.516 -25.770 69.107  1.00 34.26 ?  59  GLY   D O   1 
ATOM   3667 N  N   . ILE   C 1 65  ? -58.803 -23.665 68.964  1.00 25.96 ?  60  ILE   D N   1 
ATOM   3668 C  CA  . ILE   C 1 65  ? -57.534 -24.041 68.273  1.00 25.33 ?  60  ILE   D CA  1 
ATOM   3669 C  C   . ILE   C 1 65  ? -56.397 -24.120 69.282  1.00 23.61 ?  60  ILE   D C   1 
ATOM   3670 O  O   . ILE   C 1 65  ? -56.538 -23.642 70.407  1.00 22.93 ?  60  ILE   D O   1 
ATOM   3671 C  CB  . ILE   C 1 65  ? -57.187 -23.132 67.086  1.00 29.39 ?  60  ILE   D CB  1 
ATOM   3672 C  CG1 . ILE   C 1 65  ? -56.689 -21.759 67.542  1.00 29.61 ?  60  ILE   D CG1 1 
ATOM   3673 C  CG2 . ILE   C 1 65  ? -58.365 -23.045 66.114  1.00 32.77 ?  60  ILE   D CG2 1 
ATOM   3674 C  CD1 . ILE   C 1 65  ? -56.134 -20.905 66.436  1.00 34.08 ?  60  ILE   D CD1 1 
ATOM   3675 N  N   . THR   C 1 66  ? -55.282 -24.708 68.853  1.00 22.19 ?  61  THR   D N   1 
ATOM   3676 C  CA  . THR   C 1 66  ? -54.064 -24.833 69.666  1.00 22.30 ?  61  THR   D CA  1 
ATOM   3677 C  C   . THR   C 1 66  ? -53.042 -23.845 69.115  1.00 22.85 ?  61  THR   D C   1 
ATOM   3678 O  O   . THR   C 1 66  ? -52.894 -23.758 67.886  1.00 23.26 ?  61  THR   D O   1 
ATOM   3679 C  CB  . THR   C 1 66  ? -53.547 -26.279 69.670  1.00 27.02 ?  61  THR   D CB  1 
ATOM   3680 O  OG1 . THR   C 1 66  ? -54.563 -27.098 70.236  1.00 28.35 ?  61  THR   D OG1 1 
ATOM   3681 C  CG2 . THR   C 1 66  ? -52.304 -26.472 70.500  1.00 24.44 ?  61  THR   D CG2 1 
ATOM   3682 N  N   . LEU   C 1 67  ? -52.408 -23.104 70.022  1.00 19.80 ?  62  LEU   D N   1 
ATOM   3683 C  CA  . LEU   C 1 67  ? -51.259 -22.244 69.652  1.00 19.02 ?  62  LEU   D CA  1 
ATOM   3684 C  C   . LEU   C 1 67  ? -49.986 -23.004 70.015  1.00 18.16 ?  62  LEU   D C   1 
ATOM   3685 O  O   . LEU   C 1 67  ? -50.023 -23.813 70.942  1.00 20.64 ?  62  LEU   D O   1 
ATOM   3686 C  CB  . LEU   C 1 67  ? -51.365 -20.908 70.377  1.00 18.23 ?  62  LEU   D CB  1 
ATOM   3687 C  CG  . LEU   C 1 67  ? -52.650 -20.114 70.146  1.00 19.87 ?  62  LEU   D CG  1 
ATOM   3688 C  CD1 . LEU   C 1 67  ? -52.554 -18.780 70.876  1.00 20.50 ?  62  LEU   D CD1 1 
ATOM   3689 C  CD2 . LEU   C 1 67  ? -52.923 -19.878 68.674  1.00 21.85 ?  62  LEU   D CD2 1 
ATOM   3690 N  N   . TRP   C 1 68  ? -48.931 -22.774 69.246  1.00 18.51 ?  63  TRP   D N   1 
ATOM   3691 C  CA  . TRP   C 1 68  ? -47.570 -23.323 69.442  1.00 17.69 ?  63  TRP   D CA  1 
ATOM   3692 C  C   . TRP   C 1 68  ? -46.629 -22.189 69.820  1.00 19.78 ?  63  TRP   D C   1 
ATOM   3693 O  O   . TRP   C 1 68  ? -46.685 -21.100 69.188  1.00 17.66 ?  63  TRP   D O   1 
ATOM   3694 C  CB  . TRP   C 1 68  ? -47.088 -23.982 68.168  1.00 19.37 ?  63  TRP   D CB  1 
ATOM   3695 C  CG  . TRP   C 1 68  ? -47.836 -25.186 67.723  1.00 19.54 ?  63  TRP   D CG  1 
ATOM   3696 C  CD1 . TRP   C 1 68  ? -49.115 -25.587 68.017  1.00 23.58 ?  63  TRP   D CD1 1 
ATOM   3697 C  CD2 . TRP   C 1 68  ? -47.333 -26.125 66.774  1.00 22.24 ?  63  TRP   D CD2 1 
ATOM   3698 N  NE1 . TRP   C 1 68  ? -49.409 -26.749 67.334  1.00 22.59 ?  63  TRP   D NE1 1 
ATOM   3699 C  CE2 . TRP   C 1 68  ? -48.321 -27.103 66.583  1.00 23.61 ?  63  TRP   D CE2 1 
ATOM   3700 C  CE3 . TRP   C 1 68  ? -46.117 -26.230 66.100  1.00 21.79 ?  63  TRP   D CE3 1 
ATOM   3701 C  CZ2 . TRP   C 1 68  ? -48.135 -28.186 65.714  1.00 23.53 ?  63  TRP   D CZ2 1 
ATOM   3702 C  CZ3 . TRP   C 1 68  ? -45.937 -27.290 65.242  1.00 22.70 ?  63  TRP   D CZ3 1 
ATOM   3703 C  CH2 . TRP   C 1 68  ? -46.928 -28.245 65.053  1.00 24.23 ?  63  TRP   D CH2 1 
ATOM   3704 N  N   . GLY   C 1 69  ? -45.778 -22.445 70.796  1.00 17.65 ?  64  GLY   D N   1 
ATOM   3705 C  CA  . GLY   C 1 69  ? -44.723 -21.508 71.188  1.00 18.49 ?  64  GLY   D CA  1 
ATOM   3706 C  C   . GLY   C 1 69  ? -43.547 -22.218 71.775  1.00 16.53 ?  64  GLY   D C   1 
ATOM   3707 O  O   . GLY   C 1 69  ? -43.567 -23.452 71.897  1.00 18.21 ?  64  GLY   D O   1 
ATOM   3708 N  N   . HIS   C 1 70  ? -42.485 -21.471 72.040  1.00 18.25 ?  65  HIS   D N   1 
ATOM   3709 C  CA  . HIS   C 1 70  ? -41.328 -21.953 72.825  1.00 18.53 ?  65  HIS   D CA  1 
ATOM   3710 C  C   . HIS   C 1 70  ? -40.742 -20.849 73.686  1.00 19.37 ?  65  HIS   D C   1 
ATOM   3711 O  O   . HIS   C 1 70  ? -40.986 -19.629 73.445  1.00 18.76 ?  65  HIS   D O   1 
ATOM   3712 C  CB  . HIS   C 1 70  ? -40.247 -22.541 71.900  1.00 19.37 ?  65  HIS   D CB  1 
ATOM   3713 C  CG  . HIS   C 1 70  ? -39.460 -21.574 71.090  1.00 17.15 ?  65  HIS   D CG  1 
ATOM   3714 N  ND1 . HIS   C 1 70  ? -39.942 -21.017 69.924  1.00 18.78 ?  65  HIS   D ND1 1 
ATOM   3715 C  CD2 . HIS   C 1 70  ? -38.151 -21.192 71.149  1.00 20.45 ?  65  HIS   D CD2 1 
ATOM   3716 C  CE1 . HIS   C 1 70  ? -39.011 -20.261 69.368  1.00 19.04 ?  65  HIS   D CE1 1 
ATOM   3717 N  NE2 . HIS   C 1 70  ? -37.918 -20.340 70.068  1.00 17.82 ?  65  HIS   D NE2 1 
ATOM   3718 N  N   . MET   C 1 71  ? -39.975 -21.293 74.659  1.00 19.52 ?  66  MET   D N   1 
ATOM   3719 C  CA  . MET   C 1 71  ? -39.209 -20.419 75.555  1.00 20.46 ?  66  MET   D CA  1 
ATOM   3720 C  C   . MET   C 1 71  ? -37.913 -21.164 75.870  1.00 18.00 ?  66  MET   D C   1 
ATOM   3721 O  O   . MET   C 1 71  ? -37.741 -22.316 75.397  1.00 19.50 ?  66  MET   D O   1 
ATOM   3722 C  CB  . MET   C 1 71  ? -39.987 -20.083 76.826  1.00 19.62 ?  66  MET   D CB  1 
ATOM   3723 C  CG  . MET   C 1 71  ? -40.042 -21.191 77.865  1.00 22.44 ?  66  MET   D CG  1 
ATOM   3724 S  SD  . MET   C 1 71  ? -40.792 -20.639 79.433  1.00 29.28 ?  66  MET   D SD  1 
ATOM   3725 C  CE  . MET   C 1 71  ? -42.365 -20.761 78.662  1.00 22.26 ?  66  MET   D CE  1 
ATOM   3726 N  N   . ASN   C 1 72  ? -37.130 -20.569 76.728  1.00 18.69 ?  67  ASN   D N   1 
ATOM   3727 C  CA  . ASN   C 1 72  ? -35.828 -21.117 77.171  1.00 18.53 ?  67  ASN   D CA  1 
ATOM   3728 C  C   . ASN   C 1 72  ? -36.119 -22.062 78.348  1.00 17.83 ?  67  ASN   D C   1 
ATOM   3729 O  O   . ASN   C 1 72  ? -36.764 -21.617 79.308  1.00 16.43 ?  67  ASN   D O   1 
ATOM   3730 C  CB  . ASN   C 1 72  ? -34.880 -19.991 77.486  1.00 17.72 ?  67  ASN   D CB  1 
ATOM   3731 C  CG  . ASN   C 1 72  ? -33.511 -20.504 77.814  1.00 22.27 ?  67  ASN   D CG  1 
ATOM   3732 O  OD1 . ASN   C 1 72  ? -33.305 -21.710 78.061  1.00 20.14 ?  67  ASN   D OD1 1 
ATOM   3733 N  ND2 . ASN   C 1 72  ? -32.565 -19.591 77.772  1.00 22.31 ?  67  ASN   D ND2 1 
ATOM   3734 N  N   . ARG   C 1 73  ? -35.769 -23.348 78.241  1.00 18.46 ?  68  ARG   D N   1 
ATOM   3735 C  CA  . ARG   C 1 73  ? -35.909 -24.272 79.407  1.00 21.80 ?  68  ARG   D CA  1 
ATOM   3736 C  C   . ARG   C 1 73  ? -35.213 -23.716 80.633  1.00 24.23 ?  68  ARG   D C   1 
ATOM   3737 O  O   . ARG   C 1 73  ? -35.604 -24.111 81.705  1.00 26.42 ?  68  ARG   D O   1 
ATOM   3738 C  CB  . ARG   C 1 73  ? -35.350 -25.649 79.091  1.00 24.24 ?  68  ARG   D CB  1 
ATOM   3739 C  CG  . ARG   C 1 73  ? -36.305 -26.451 78.251  1.00 23.42 ?  68  ARG   D CG  1 
ATOM   3740 C  CD  . ARG   C 1 73  ? -36.023 -27.924 78.175  1.00 22.92 ?  68  ARG   D CD  1 
ATOM   3741 N  NE  . ARG   C 1 73  ? -37.014 -28.491 77.300  1.00 20.74 ?  68  ARG   D NE  1 
ATOM   3742 C  CZ  . ARG   C 1 73  ? -37.809 -29.497 77.599  1.00 22.49 ?  68  ARG   D CZ  1 
ATOM   3743 N  NH1 . ARG   C 1 73  ? -37.733 -30.080 78.788  1.00 20.36 1  68  ARG   D NH1 1 
ATOM   3744 N  NH2 . ARG   C 1 73  ? -38.688 -29.904 76.725  1.00 23.82 ?  68  ARG   D NH2 1 
ATOM   3745 N  N   . ALA   C 1 74  ? -34.151 -22.931 80.475  1.00 22.52 ?  69  ALA   D N   1 
ATOM   3746 C  CA  . ALA   C 1 74  ? -33.348 -22.358 81.585  1.00 24.50 ?  69  ALA   D CA  1 
ATOM   3747 C  C   . ALA   C 1 74  ? -34.064 -21.176 82.226  1.00 23.38 ?  69  ALA   D C   1 
ATOM   3748 O  O   . ALA   C 1 74  ? -33.680 -20.740 83.326  1.00 22.63 ?  69  ALA   D O   1 
ATOM   3749 C  CB  . ALA   C 1 74  ? -31.964 -21.945 81.117  1.00 24.48 ?  69  ALA   D CB  1 
ATOM   3750 N  N   . ASN   C 1 75  ? -35.083 -20.643 81.575  1.00 23.22 ?  70  ASN   D N   1 
ATOM   3751 C  CA  . ASN   C 1 75  ? -35.910 -19.581 82.173  1.00 21.20 ?  70  ASN   D CA  1 
ATOM   3752 C  C   . ASN   C 1 75  ? -36.650 -20.206 83.347  1.00 19.77 ?  70  ASN   D C   1 
ATOM   3753 O  O   . ASN   C 1 75  ? -37.423 -21.144 83.151  1.00 20.77 ?  70  ASN   D O   1 
ATOM   3754 C  CB  . ASN   C 1 75  ? -36.798 -19.004 81.085  1.00 20.81 ?  70  ASN   D CB  1 
ATOM   3755 C  CG  . ASN   C 1 75  ? -37.694 -17.871 81.496  1.00 21.12 ?  70  ASN   D CG  1 
ATOM   3756 O  OD1 . ASN   C 1 75  ? -38.002 -17.690 82.669  1.00 19.70 ?  70  ASN   D OD1 1 
ATOM   3757 N  ND2 . ASN   C 1 75  ? -38.201 -17.188 80.483  1.00 20.41 ?  70  ASN   D ND2 1 
ATOM   3758 N  N   . PRO   C 1 76  ? -36.546 -19.655 84.562  1.00 19.32 ?  71  PRO   D N   1 
ATOM   3759 C  CA  . PRO   C 1 76  ? -37.337 -20.181 85.687  1.00 20.89 ?  71  PRO   D CA  1 
ATOM   3760 C  C   . PRO   C 1 76  ? -38.846 -20.265 85.473  1.00 20.42 ?  71  PRO   D C   1 
ATOM   3761 O  O   . PRO   C 1 76  ? -39.513 -21.004 86.184  1.00 20.50 ?  71  PRO   D O   1 
ATOM   3762 C  CB  . PRO   C 1 76  ? -37.006 -19.142 86.781  1.00 20.00 ?  71  PRO   D CB  1 
ATOM   3763 C  CG  . PRO   C 1 76  ? -35.571 -18.792 86.473  1.00 20.42 ?  71  PRO   D CG  1 
ATOM   3764 C  CD  . PRO   C 1 76  ? -35.670 -18.539 84.980  1.00 19.49 ?  71  PRO   D CD  1 
ATOM   3765 N  N   . HIS   C 1 77  ? -39.380 -19.476 84.538  1.00 20.41 ?  72  HIS   D N   1 
ATOM   3766 C  CA  . HIS   C 1 77  ? -40.825 -19.545 84.167  1.00 18.70 ?  72  HIS   D CA  1 
ATOM   3767 C  C   . HIS   C 1 77  ? -41.160 -20.968 83.697  1.00 18.72 ?  72  HIS   D C   1 
ATOM   3768 O  O   . HIS   C 1 77  ? -42.247 -21.493 83.980  1.00 19.14 ?  72  HIS   D O   1 
ATOM   3769 C  CB  . HIS   C 1 77  ? -41.126 -18.450 83.134  1.00 18.56 ?  72  HIS   D CB  1 
ATOM   3770 C  CG  . HIS   C 1 77  ? -42.579 -18.203 82.921  1.00 18.57 ?  72  HIS   D CG  1 
ATOM   3771 N  ND1 . HIS   C 1 77  ? -43.035 -17.148 82.137  1.00 18.49 ?  72  HIS   D ND1 1 
ATOM   3772 C  CD2 . HIS   C 1 77  ? -43.661 -18.786 83.461  1.00 19.85 ?  72  HIS   D CD2 1 
ATOM   3773 C  CE1 . HIS   C 1 77  ? -44.357 -17.150 82.166  1.00 19.42 ?  72  HIS   D CE1 1 
ATOM   3774 N  NE2 . HIS   C 1 77  ? -44.765 -18.156 82.972  1.00 20.75 ?  72  HIS   D NE2 1 
ATOM   3775 N  N   . TRP   C 1 78  ? -40.264 -21.575 82.974  1.00 19.32 ?  73  TRP   D N   1 
ATOM   3776 C  CA  . TRP   C 1 78  ? -40.496 -22.943 82.443  1.00 20.33 ?  73  TRP   D CA  1 
ATOM   3777 C  C   . TRP   C 1 78  ? -40.756 -23.887 83.634  1.00 22.50 ?  73  TRP   D C   1 
ATOM   3778 O  O   . TRP   C 1 78  ? -41.723 -24.639 83.573  1.00 23.98 ?  73  TRP   D O   1 
ATOM   3779 C  CB  . TRP   C 1 78  ? -39.319 -23.402 81.581  1.00 20.92 ?  73  TRP   D CB  1 
ATOM   3780 C  CG  . TRP   C 1 78  ? -39.453 -24.801 81.045  1.00 20.18 ?  73  TRP   D CG  1 
ATOM   3781 C  CD1 . TRP   C 1 78  ? -38.899 -25.909 81.617  1.00 22.80 ?  73  TRP   D CD1 1 
ATOM   3782 C  CD2 . TRP   C 1 78  ? -40.247 -25.287 79.951  1.00 18.31 ?  73  TRP   D CD2 1 
ATOM   3783 N  NE1 . TRP   C 1 78  ? -39.178 -27.019 80.901  1.00 23.04 ?  73  TRP   D NE1 1 
ATOM   3784 C  CE2 . TRP   C 1 78  ? -40.001 -26.677 79.862  1.00 20.54 ?  73  TRP   D CE2 1 
ATOM   3785 C  CE3 . TRP   C 1 78  ? -41.083 -24.717 79.003  1.00 18.43 ?  73  TRP   D CE3 1 
ATOM   3786 C  CZ2 . TRP   C 1 78  ? -40.581 -27.485 78.889  1.00 21.66 ?  73  TRP   D CZ2 1 
ATOM   3787 C  CZ3 . TRP   C 1 78  ? -41.627 -25.512 78.017  1.00 18.16 ?  73  TRP   D CZ3 1 
ATOM   3788 C  CH2 . TRP   C 1 78  ? -41.403 -26.883 77.984  1.00 19.37 ?  73  TRP   D CH2 1 
ATOM   3789 N  N   . ALA   C 1 79  ? -39.929 -23.838 84.677  1.00 20.59 ?  74  ALA   D N   1 
ATOM   3790 C  CA  . ALA   C 1 79  ? -40.037 -24.777 85.825  1.00 25.37 ?  74  ALA   D CA  1 
ATOM   3791 C  C   . ALA   C 1 79  ? -41.308 -24.449 86.603  1.00 27.32 ?  74  ALA   D C   1 
ATOM   3792 O  O   . ALA   C 1 79  ? -41.991 -25.390 87.083  1.00 30.65 ?  74  ALA   D O   1 
ATOM   3793 C  CB  . ALA   C 1 79  ? -38.802 -24.731 86.660  1.00 25.13 ?  74  ALA   D CB  1 
ATOM   3794 N  N   . ALA   C 1 80  ? -41.722 -23.174 86.569  1.00 28.04 ?  75  ALA   D N   1 
ATOM   3795 C  CA  . ALA   C 1 80  ? -42.870 -22.653 87.344  1.00 25.00 ?  75  ALA   D CA  1 
ATOM   3796 C  C   . ALA   C 1 80  ? -44.158 -23.055 86.673  1.00 29.52 ?  75  ALA   D C   1 
ATOM   3797 O  O   . ALA   C 1 80  ? -45.193 -23.191 87.391  1.00 30.92 ?  75  ALA   D O   1 
ATOM   3798 C  CB  . ALA   C 1 80  ? -42.774 -21.163 87.536  1.00 27.21 ?  75  ALA   D CB  1 
ATOM   3799 N  N   . LEU   C 1 81  ? -44.119 -23.348 85.382  1.00 29.35 ?  76  LEU   D N   1 
ATOM   3800 C  CA  . LEU   C 1 81  ? -45.348 -23.747 84.671  1.00 31.53 ?  76  LEU   D CA  1 
ATOM   3801 C  C   . LEU   C 1 81  ? -45.789 -25.134 85.149  1.00 44.66 ?  76  LEU   D C   1 
ATOM   3802 O  O   . LEU   C 1 81  ? -47.006 -25.314 85.423  1.00 48.23 ?  76  LEU   D O   1 
ATOM   3803 C  CB  . LEU   C 1 81  ? -45.099 -23.673 83.167  1.00 30.67 ?  76  LEU   D CB  1 
ATOM   3804 C  CG  . LEU   C 1 81  ? -45.061 -22.233 82.649  1.00 29.39 ?  76  LEU   D CG  1 
ATOM   3805 C  CD1 . LEU   C 1 81  ? -44.539 -22.195 81.221  1.00 29.01 ?  76  LEU   D CD1 1 
ATOM   3806 C  CD2 . LEU   C 1 81  ? -46.454 -21.598 82.762  1.00 28.02 ?  76  LEU   D CD2 1 
ATOM   3807 N  N   . GLY   C 1 82  ? -44.844 -26.054 85.309  1.00 47.10 ?  77  GLY   D N   1 
ATOM   3808 C  CA  . GLY   C 1 82  ? -45.176 -27.414 85.767  1.00 58.82 ?  77  GLY   D CA  1 
ATOM   3809 C  C   . GLY   C 1 82  ? -46.265 -28.021 84.900  1.00 65.88 ?  77  GLY   D C   1 
ATOM   3810 O  O   . GLY   C 1 82  ? -46.322 -27.697 83.679  1.00 70.08 ?  77  GLY   D O   1 
ATOM   3811 N  N   . GLY   C 1 83  ? -47.123 -28.837 85.510  1.00 72.03 ?  78  GLY   D N   1 
ATOM   3812 C  CA  . GLY   C 1 83  ? -47.962 -29.814 84.796  1.00 72.74 ?  78  GLY   D CA  1 
ATOM   3813 C  C   . GLY   C 1 83  ? -48.863 -29.152 83.776  1.00 69.72 ?  78  GLY   D C   1 
ATOM   3814 O  O   . GLY   C 1 83  ? -48.605 -29.313 82.568  1.00 77.60 ?  78  GLY   D O   1 
ATOM   3815 N  N   . ALA   C 1 84  ? -49.876 -28.431 84.256  1.00 61.97 ?  79  ALA   D N   1 
ATOM   3816 C  CA  . ALA   C 1 84  ? -51.079 -28.048 83.484  1.00 52.76 ?  79  ALA   D CA  1 
ATOM   3817 C  C   . ALA   C 1 84  ? -51.482 -26.625 83.881  1.00 50.94 ?  79  ALA   D C   1 
ATOM   3818 O  O   . ALA   C 1 84  ? -52.629 -26.417 84.324  1.00 49.26 ?  79  ALA   D O   1 
ATOM   3819 C  CB  . ALA   C 1 84  ? -52.170 -29.044 83.770  1.00 49.13 ?  79  ALA   D CB  1 
ATOM   3820 N  N   . ALA   C 1 85  ? -50.553 -25.678 83.746  1.00 42.47 ?  80  ALA   D N   1 
ATOM   3821 C  CA  . ALA   C 1 85  ? -50.753 -24.283 84.200  1.00 36.66 ?  80  ALA   D CA  1 
ATOM   3822 C  C   . ALA   C 1 85  ? -51.851 -23.622 83.361  1.00 32.28 ?  80  ALA   D C   1 
ATOM   3823 O  O   . ALA   C 1 85  ? -51.891 -23.828 82.108  1.00 30.64 ?  80  ALA   D O   1 
ATOM   3824 C  CB  . ALA   C 1 85  ? -49.466 -23.525 84.131  1.00 35.32 ?  80  ALA   D CB  1 
ATOM   3825 N  N   . ASN   C 1 86  ? -52.734 -22.874 84.023  1.00 29.67 ?  81  ASN   D N   1 
ATOM   3826 C  CA  . ASN   C 1 86  ? -53.721 -21.981 83.355  1.00 28.96 ?  81  ASN   D CA  1 
ATOM   3827 C  C   . ASN   C 1 86  ? -53.016 -20.665 83.054  1.00 24.71 ?  81  ASN   D C   1 
ATOM   3828 O  O   . ASN   C 1 86  ? -52.514 -20.042 84.004  1.00 25.88 ?  81  ASN   D O   1 
ATOM   3829 C  CB  . ASN   C 1 86  ? -54.924 -21.747 84.241  1.00 31.56 ?  81  ASN   D CB  1 
ATOM   3830 C  CG  . ASN   C 1 86  ? -55.653 -23.038 84.488  1.00 34.50 ?  81  ASN   D CG  1 
ATOM   3831 O  OD1 . ASN   C 1 86  ? -55.902 -23.791 83.549  1.00 36.44 ?  81  ASN   D OD1 1 
ATOM   3832 N  ND2 . ASN   C 1 86  ? -55.967 -23.297 85.740  1.00 36.82 ?  81  ASN   D ND2 1 
ATOM   3833 N  N   . VAL   C 1 87  ? -52.883 -20.314 81.779  1.00 21.97 ?  82  VAL   D N   1 
ATOM   3834 C  CA  . VAL   C 1 87  ? -52.003 -19.173 81.423  1.00 21.66 ?  82  VAL   D CA  1 
ATOM   3835 C  C   . VAL   C 1 87  ? -52.819 -18.182 80.618  1.00 19.37 ?  82  VAL   D C   1 
ATOM   3836 O  O   . VAL   C 1 87  ? -53.914 -18.517 80.154  1.00 19.84 ?  82  VAL   D O   1 
ATOM   3837 C  CB  . VAL   C 1 87  ? -50.753 -19.624 80.651  1.00 22.31 ?  82  VAL   D CB  1 
ATOM   3838 C  CG1 . VAL   C 1 87  ? -49.917 -20.597 81.452  1.00 25.19 ?  82  VAL   D CG1 1 
ATOM   3839 C  CG2 . VAL   C 1 87  ? -51.097 -20.205 79.293  1.00 22.15 ?  82  VAL   D CG2 1 
ATOM   3840 N  N   . VAL   C 1 88  ? -52.258 -16.993 80.468  1.00 18.52 ?  83  VAL   D N   1 
ATOM   3841 C  CA  . VAL   C 1 88  ? -52.743 -15.999 79.474  1.00 17.19 ?  83  VAL   D CA  1 
ATOM   3842 C  C   . VAL   C 1 88  ? -51.562 -15.648 78.594  1.00 15.76 ?  83  VAL   D C   1 
ATOM   3843 O  O   . VAL   C 1 88  ? -50.409 -15.476 79.108  1.00 17.95 ?  83  VAL   D O   1 
ATOM   3844 C  CB  . VAL   C 1 88  ? -53.412 -14.772 80.118  1.00 18.56 ?  83  VAL   D CB  1 
ATOM   3845 C  CG1 . VAL   C 1 88  ? -52.526 -14.130 81.183  1.00 18.69 ?  83  VAL   D CG1 1 
ATOM   3846 C  CG2 . VAL   C 1 88  ? -53.823 -13.738 79.094  1.00 19.11 ?  83  VAL   D CG2 1 
ATOM   3847 N  N   . ALA   C 1 89  ? -51.840 -15.513 77.304  1.00 16.55 ?  84  ALA   D N   1 
ATOM   3848 C  CA  . ALA   C 1 89  ? -50.886 -14.964 76.313  1.00 17.81 ?  84  ALA   D CA  1 
ATOM   3849 C  C   . ALA   C 1 89  ? -51.537 -13.746 75.697  1.00 16.44 ?  84  ALA   D C   1 
ATOM   3850 O  O   . ALA   C 1 89  ? -52.687 -13.805 75.180  1.00 19.36 ?  84  ALA   D O   1 
ATOM   3851 C  CB  . ALA   C 1 89  ? -50.464 -15.974 75.286  1.00 18.73 ?  84  ALA   D CB  1 
ATOM   3852 N  N   . THR   C 1 90  ? -50.839 -12.647 75.835  1.00 16.49 ?  85  THR   D N   1 
ATOM   3853 C  CA  . THR   C 1 90  ? -51.299 -11.326 75.370  1.00 16.16 ?  85  THR   D CA  1 
ATOM   3854 C  C   . THR   C 1 90  ? -50.507 -10.904 74.156  1.00 15.83 ?  85  THR   D C   1 
ATOM   3855 O  O   . THR   C 1 90  ? -49.232 -10.874 74.201  1.00 15.94 ?  85  THR   D O   1 
ATOM   3856 C  CB  . THR   C 1 90  ? -51.224 -10.267 76.481  1.00 17.53 ?  85  THR   D CB  1 
ATOM   3857 O  OG1 . THR   C 1 90  ? -51.996 -10.729 77.592  1.00 19.60 ?  85  THR   D OG1 1 
ATOM   3858 C  CG2 . THR   C 1 90  ? -51.704 -8.935  75.970  1.00 18.94 ?  85  THR   D CG2 1 
ATOM   3859 N  N   . PHE   C 1 91  ? -51.243 -10.558 73.129  1.00 14.64 ?  86  PHE   D N   1 
ATOM   3860 C  CA  . PHE   C 1 91  ? -50.712 -10.050 71.848  1.00 16.98 ?  86  PHE   D CA  1 
ATOM   3861 C  C   . PHE   C 1 91  ? -51.106 -8.598  71.687  1.00 17.09 ?  86  PHE   D C   1 
ATOM   3862 O  O   . PHE   C 1 91  ? -52.293 -8.229  71.711  1.00 19.08 ?  86  PHE   D O   1 
ATOM   3863 C  CB  . PHE   C 1 91  ? -51.161 -10.867 70.661  1.00 15.34 ?  86  PHE   D CB  1 
ATOM   3864 C  CG  . PHE   C 1 91  ? -50.867 -12.338 70.779  1.00 16.34 ?  86  PHE   D CG  1 
ATOM   3865 C  CD1 . PHE   C 1 91  ? -51.660 -13.140 71.585  1.00 16.75 ?  86  PHE   D CD1 1 
ATOM   3866 C  CD2 . PHE   C 1 91  ? -49.846 -12.926 70.064  1.00 17.41 ?  86  PHE   D CD2 1 
ATOM   3867 C  CE1 . PHE   C 1 91  ? -51.458 -14.499 71.665  1.00 17.84 ?  86  PHE   D CE1 1 
ATOM   3868 C  CE2 . PHE   C 1 91  ? -49.661 -14.297 70.120  1.00 18.02 ?  86  PHE   D CE2 1 
ATOM   3869 C  CZ  . PHE   C 1 91  ? -50.450 -15.086 70.924  1.00 17.99 ?  86  PHE   D CZ  1 
ATOM   3870 N  N   . ALA   C 1 92  ? -50.117 -7.767  71.472  1.00 17.70 ?  87  ALA   D N   1 
ATOM   3871 C  CA  . ALA   C 1 92  ? -50.333 -6.290  71.416  1.00 19.54 ?  87  ALA   D CA  1 
ATOM   3872 C  C   . ALA   C 1 92  ? -50.055 -5.780  70.024  1.00 20.83 ?  87  ALA   D C   1 
ATOM   3873 O  O   . ALA   C 1 92  ? -48.929 -5.966  69.530  1.00 19.08 ?  87  ALA   D O   1 
ATOM   3874 C  CB  . ALA   C 1 92  ? -49.453 -5.551  72.388  1.00 22.26 ?  87  ALA   D CB  1 
ATOM   3875 N  N   . GLY   C 1 93  ? -51.047 -5.158  69.438  1.00 18.45 ?  88  GLY   D N   1 
ATOM   3876 C  CA  . GLY   C 1 93  ? -50.961 -4.595  68.088  1.00 17.98 ?  88  GLY   D CA  1 
ATOM   3877 C  C   . GLY   C 1 93  ? -50.690 -3.106  68.043  1.00 17.04 ?  88  GLY   D C   1 
ATOM   3878 O  O   . GLY   C 1 93  ? -50.115 -2.489  68.960  1.00 17.88 ?  88  GLY   D O   1 
ATOM   3879 N  N   . PRO   C 1 94  ? -51.020 -2.514  66.883  1.00 19.23 ?  89  PRO   D N   1 
ATOM   3880 C  CA  . PRO   C 1 94  ? -50.883 -1.085  66.693  1.00 19.81 ?  89  PRO   D CA  1 
ATOM   3881 C  C   . PRO   C 1 94  ? -51.521 -0.305  67.854  1.00 17.50 ?  89  PRO   D C   1 
ATOM   3882 O  O   . PRO   C 1 94  ? -52.597 -0.661  68.401  1.00 17.41 ?  89  PRO   D O   1 
ATOM   3883 C  CB  . PRO   C 1 94  ? -51.549 -0.840  65.343  1.00 21.83 ?  89  PRO   D CB  1 
ATOM   3884 C  CG  . PRO   C 1 94  ? -51.323 -2.103  64.623  1.00 20.25 ?  89  PRO   D CG  1 
ATOM   3885 C  CD  . PRO   C 1 94  ? -51.515 -3.180  65.676  1.00 20.59 ?  89  PRO   D CD  1 
ATOM   3886 N  N   . ASN   C 1 95  ? -50.924 0.849   68.115  1.00 18.27 ?  90  ASN   D N   1 
ATOM   3887 C  CA  . ASN   C 1 95  ? -51.405 1.725   69.218  1.00 16.30 ?  90  ASN   D CA  1 
ATOM   3888 C  C   . ASN   C 1 95  ? -50.911 3.143   68.963  1.00 17.12 ?  90  ASN   D C   1 
ATOM   3889 O  O   . ASN   C 1 95  ? -49.798 3.324   68.432  1.00 17.42 ?  90  ASN   D O   1 
ATOM   3890 C  CB  . ASN   C 1 95  ? -51.023 1.136   70.600  1.00 15.84 ?  90  ASN   D CB  1 
ATOM   3891 C  CG  . ASN   C 1 95  ? -49.525 1.182   70.844  1.00 20.01 ?  90  ASN   D CG  1 
ATOM   3892 O  OD1 . ASN   C 1 95  ? -48.981 2.182   71.329  1.00 20.34 ?  90  ASN   D OD1 1 
ATOM   3893 N  ND2 . ASN   C 1 95  ? -48.825 0.132   70.409  1.00 21.84 ?  90  ASN   D ND2 1 
ATOM   3894 N  N   . ALA   C 1 96  ? -51.601 4.135   69.514  1.00 17.22 ?  91  ALA   D N   1 
ATOM   3895 C  CA  . ALA   C 1 96  ? -51.130 5.533   69.487  1.00 17.66 ?  91  ALA   D CA  1 
ATOM   3896 C  C   . ALA   C 1 96  ? -51.856 6.366   70.531  1.00 19.08 ?  91  ALA   D C   1 
ATOM   3897 O  O   . ALA   C 1 96  ? -53.091 6.194   70.699  1.00 17.22 ?  91  ALA   D O   1 
ATOM   3898 C  CB  . ALA   C 1 96  ? -51.343 6.120   68.130  1.00 16.80 ?  91  ALA   D CB  1 
ATOM   3899 N  N   . TYR   C 1 97  ? -51.126 7.302   71.113  1.00 19.74 ?  92  TYR   D N   1 
ATOM   3900 C  CA  . TYR   C 1 97  ? -51.711 8.349   71.988  1.00 18.96 ?  92  TYR   D CA  1 
ATOM   3901 C  C   . TYR   C 1 97  ? -52.696 9.223   71.222  1.00 18.23 ?  92  TYR   D C   1 
ATOM   3902 O  O   . TYR   C 1 97  ? -52.418 9.589   70.069  1.00 17.28 ?  92  TYR   D O   1 
ATOM   3903 C  CB  . TYR   C 1 97  ? -50.600 9.185   72.600  1.00 17.63 ?  92  TYR   D CB  1 
ATOM   3904 C  CG  . TYR   C 1 97  ? -51.120 10.258  73.502  1.00 17.24 ?  92  TYR   D CG  1 
ATOM   3905 C  CD1 . TYR   C 1 97  ? -51.591 9.982   74.771  1.00 17.26 ?  92  TYR   D CD1 1 
ATOM   3906 C  CD2 . TYR   C 1 97  ? -51.113 11.571  73.082  1.00 16.45 ?  92  TYR   D CD2 1 
ATOM   3907 C  CE1 . TYR   C 1 97  ? -52.108 10.975  75.576  1.00 18.10 ?  92  TYR   D CE1 1 
ATOM   3908 C  CE2 . TYR   C 1 97  ? -51.631 12.572  73.871  1.00 16.45 ?  92  TYR   D CE2 1 
ATOM   3909 C  CZ  . TYR   C 1 97  ? -52.061 12.283  75.153  1.00 15.67 ?  92  TYR   D CZ  1 
ATOM   3910 O  OH  . TYR   C 1 97  ? -52.519 13.257  75.956  1.00 17.22 ?  92  TYR   D OH  1 
ATOM   3911 N  N   . VAL   C 1 98  ? -53.884 9.458   71.812  1.00 18.43 ?  93  VAL   D N   1 
ATOM   3912 C  CA  . VAL   C 1 98  ? -54.921 10.360  71.245  1.00 16.30 ?  93  VAL   D CA  1 
ATOM   3913 C  C   . VAL   C 1 98  ? -54.908 11.667  72.034  1.00 17.94 ?  93  VAL   D C   1 
ATOM   3914 O  O   . VAL   C 1 98  ? -55.363 11.702  73.210  1.00 17.84 ?  93  VAL   D O   1 
ATOM   3915 C  CB  . VAL   C 1 98  ? -56.321 9.758   71.244  1.00 16.82 ?  93  VAL   D CB  1 
ATOM   3916 C  CG1 . VAL   C 1 98  ? -57.200 10.706  70.535  1.00 18.04 ?  93  VAL   D CG1 1 
ATOM   3917 C  CG2 . VAL   C 1 98  ? -56.344 8.386   70.586  1.00 17.12 ?  93  VAL   D CG2 1 
ATOM   3918 N  N   . SER   C 1 99  ? -54.444 12.721  71.388  1.00 17.21 ?  94  SER   D N   1 
ATOM   3919 C  CA  . SER   C 1 99  ? -54.509 14.114  71.909  1.00 17.14 ?  94  SER   D CA  1 
ATOM   3920 C  C   . SER   C 1 99  ? -55.901 14.686  71.681  1.00 16.76 ?  94  SER   D C   1 
ATOM   3921 O  O   . SER   C 1 99  ? -56.325 14.810  70.543  1.00 18.22 ?  94  SER   D O   1 
ATOM   3922 C  CB  . SER   C 1 99  ? -53.553 15.015  71.273  1.00 16.45 ?  94  SER   D CB  1 
ATOM   3923 O  OG  . SER   C 1 99  ? -53.771 16.363  71.690  1.00 18.65 ?  94  SER   D OG  1 
ATOM   3924 N  N   . PRO   C 1 100 ? -56.592 15.206  72.717  1.00 18.67 ?  95  PRO   D N   1 
ATOM   3925 C  CA  . PRO   C 1 100 ? -57.910 15.801  72.456  1.00 18.68 ?  95  PRO   D CA  1 
ATOM   3926 C  C   . PRO   C 1 100 ? -57.770 17.005  71.506  1.00 18.00 ?  95  PRO   D C   1 
ATOM   3927 O  O   . PRO   C 1 100 ? -58.730 17.500  71.025  1.00 18.86 ?  95  PRO   D O   1 
ATOM   3928 C  CB  . PRO   C 1 100 ? -58.339 16.243  73.849  1.00 19.60 ?  95  PRO   D CB  1 
ATOM   3929 C  CG  . PRO   C 1 100 ? -57.703 15.249  74.757  1.00 19.88 ?  95  PRO   D CG  1 
ATOM   3930 C  CD  . PRO   C 1 100 ? -56.297 15.150  74.154  1.00 17.42 ?  95  PRO   D CD  1 
ATOM   3931 N  N   . ALA   C 1 101 ? -56.551 17.538  71.302  1.00 17.58 ?  96  ALA   D N   1 
ATOM   3932 C  CA  . ALA   C 1 101 ? -56.425 18.659  70.331  1.00 19.81 ?  96  ALA   D CA  1 
ATOM   3933 C  C   . ALA   C 1 101 ? -56.977 18.202  68.973  1.00 23.03 ?  96  ALA   D C   1 
ATOM   3934 O  O   . ALA   C 1 101 ? -57.392 19.060  68.201  1.00 23.40 ?  96  ALA   D O   1 
ATOM   3935 C  CB  . ALA   C 1 101 ? -54.996 19.108  70.203  1.00 20.59 ?  96  ALA   D CB  1 
ATOM   3936 N  N   . VAL   C 1 102 ? -56.954 16.897  68.673  1.00 20.86 ?  97  VAL   D N   1 
ATOM   3937 C  CA  . VAL   C 1 102 ? -57.282 16.377  67.314  1.00 21.46 ?  97  VAL   D CA  1 
ATOM   3938 C  C   . VAL   C 1 102 ? -58.815 16.397  67.227  1.00 21.94 ?  97  VAL   D C   1 
ATOM   3939 O  O   . VAL   C 1 102 ? -59.342 16.576  66.141  1.00 26.84 ?  97  VAL   D O   1 
ATOM   3940 C  CB  . VAL   C 1 102 ? -56.691 14.969  67.133  1.00 25.00 ?  97  VAL   D CB  1 
ATOM   3941 C  CG1 . VAL   C 1 102 ? -57.176 14.269  65.879  1.00 30.24 ?  97  VAL   D CG1 1 
ATOM   3942 C  CG2 . VAL   C 1 102 ? -55.168 15.021  67.147  1.00 25.87 ?  97  VAL   D CG2 1 
ATOM   3943 N  N   . TYR   C 1 103 ? -59.492 16.216  68.350  1.00 21.28 ?  98  TYR   D N   1 
ATOM   3944 C  CA  . TYR   C 1 103 ? -60.997 16.194  68.398  1.00 18.84 ?  98  TYR   D CA  1 
ATOM   3945 C  C   . TYR   C 1 103 ? -61.605 17.546  68.023  1.00 22.99 ?  98  TYR   D C   1 
ATOM   3946 O  O   . TYR   C 1 103 ? -62.711 17.526  67.446  1.00 26.23 ?  98  TYR   D O   1 
ATOM   3947 C  CB  . TYR   C 1 103 ? -61.466 15.881  69.804  1.00 18.26 ?  98  TYR   D CB  1 
ATOM   3948 C  CG  . TYR   C 1 103 ? -61.147 14.544  70.405  1.00 19.46 ?  98  TYR   D CG  1 
ATOM   3949 C  CD1 . TYR   C 1 103 ? -60.745 13.444  69.658  1.00 19.28 ?  98  TYR   D CD1 1 
ATOM   3950 C  CD2 . TYR   C 1 103 ? -61.210 14.393  71.774  1.00 19.89 ?  98  TYR   D CD2 1 
ATOM   3951 C  CE1 . TYR   C 1 103 ? -60.508 12.224  70.251  1.00 20.30 ?  98  TYR   D CE1 1 
ATOM   3952 C  CE2 . TYR   C 1 103 ? -60.934 13.180  72.390  1.00 20.29 ?  98  TYR   D CE2 1 
ATOM   3953 C  CZ  . TYR   C 1 103 ? -60.568 12.088  71.627  1.00 19.16 ?  98  TYR   D CZ  1 
ATOM   3954 O  OH  . TYR   C 1 103 ? -60.389 10.873  72.204  1.00 19.67 ?  98  TYR   D OH  1 
ATOM   3955 N  N   . ARG   C 1 104 ? -60.946 18.659  68.353  1.00 22.11 ?  99  ARG   D N   1 
ATOM   3956 C  CA  . ARG   C 1 104 ? -61.460 20.052  68.214  1.00 28.88 ?  99  ARG   D CA  1 
ATOM   3957 C  C   . ARG   C 1 104 ? -62.799 20.188  68.961  1.00 30.83 ?  99  ARG   D C   1 
ATOM   3958 O  O   . ARG   C 1 104 ? -63.716 20.813  68.444  1.00 35.07 ?  99  ARG   D O   1 
ATOM   3959 C  CB  . ARG   C 1 104 ? -61.535 20.428  66.729  1.00 31.31 ?  99  ARG   D CB  1 
ATOM   3960 C  CG  . ARG   C 1 104 ? -60.194 20.311  66.005  1.00 35.86 ?  99  ARG   D CG  1 
ATOM   3961 C  CD  . ARG   C 1 104 ? -60.070 21.156  64.746  1.00 41.85 ?  99  ARG   D CD  1 
ATOM   3962 N  NE  . ARG   C 1 104 ? -61.174 20.933  63.815  1.00 46.39 ?  99  ARG   D NE  1 
ATOM   3963 C  CZ  . ARG   C 1 104 ? -61.195 20.035  62.832  1.00 50.06 ?  99  ARG   D CZ  1 
ATOM   3964 N  NH1 . ARG   C 1 104 ? -60.161 19.234  62.611  1.00 48.66 1  99  ARG   D NH1 1 
ATOM   3965 N  NH2 . ARG   C 1 104 ? -62.272 19.931  62.071  1.00 54.86 ?  99  ARG   D NH2 1 
ATOM   3966 N  N   . THR   C 1 105 ? -62.919 19.562  70.131  1.00 32.34 ?  100 THR   D N   1 
ATOM   3967 C  CA  . THR   C 1 105 ? -64.135 19.603  70.973  1.00 30.97 ?  100 THR   D CA  1 
ATOM   3968 C  C   . THR   C 1 105 ? -63.719 19.881  72.409  1.00 30.86 ?  100 THR   D C   1 
ATOM   3969 O  O   . THR   C 1 105 ? -62.540 19.696  72.744  1.00 25.01 ?  100 THR   D O   1 
ATOM   3970 C  CB  . THR   C 1 105 ? -64.899 18.279  70.954  1.00 36.76 ?  100 THR   D CB  1 
ATOM   3971 O  OG1 . THR   C 1 105 ? -64.005 17.292  71.468  1.00 31.19 ?  100 THR   D OG1 1 
ATOM   3972 C  CG2 . THR   C 1 105 ? -65.411 17.920  69.579  1.00 45.35 ?  100 THR   D CG2 1 
ATOM   3973 N  N   . ALA   C 1 106 ? -64.669 20.307  73.216  1.00 26.30 ?  101 ALA   D N   1 
ATOM   3974 C  CA  . ALA   C 1 106 ? -64.458 20.607  74.644  1.00 25.63 ?  101 ALA   D CA  1 
ATOM   3975 C  C   . ALA   C 1 106 ? -65.771 20.367  75.345  1.00 25.87 ?  101 ALA   D C   1 
ATOM   3976 O  O   . ALA   C 1 106 ? -66.814 20.567  74.730  1.00 27.96 ?  101 ALA   D O   1 
ATOM   3977 C  CB  . ALA   C 1 106 ? -63.992 22.023  74.813  1.00 28.28 ?  101 ALA   D CB  1 
ATOM   3978 N  N   . PRO   C 1 107 ? -65.763 19.790  76.557  1.00 24.62 ?  102 PRO   D N   1 
ATOM   3979 C  CA  . PRO   C 1 107 ? -64.543 19.309  77.176  1.00 23.00 ?  102 PRO   D CA  1 
ATOM   3980 C  C   . PRO   C 1 107 ? -64.189 17.897  76.688  1.00 22.29 ?  102 PRO   D C   1 
ATOM   3981 O  O   . PRO   C 1 107 ? -64.944 17.293  75.917  1.00 19.01 ?  102 PRO   D O   1 
ATOM   3982 C  CB  . PRO   C 1 107 ? -64.923 19.254  78.652  1.00 23.80 ?  102 PRO   D CB  1 
ATOM   3983 C  CG  . PRO   C 1 107 ? -66.399 18.909  78.625  1.00 24.25 ?  102 PRO   D CG  1 
ATOM   3984 C  CD  . PRO   C 1 107 ? -66.957 19.480  77.352  1.00 23.30 ?  102 PRO   D CD  1 
ATOM   3985 N  N   . ALA   C 1 108 ? -63.001 17.442  77.050  1.00 21.69 ?  103 ALA   D N   1 
ATOM   3986 C  CA  . ALA   C 1 108 ? -62.472 16.131  76.592  1.00 20.03 ?  103 ALA   D CA  1 
ATOM   3987 C  C   . ALA   C 1 108 ? -61.412 15.621  77.557  1.00 18.84 ?  103 ALA   D C   1 
ATOM   3988 O  O   . ALA   C 1 108 ? -61.034 16.299  78.527  1.00 17.72 ?  103 ALA   D O   1 
ATOM   3989 C  CB  . ALA   C 1 108 ? -61.913 16.308  75.209  1.00 22.08 ?  103 ALA   D CB  1 
ATOM   3990 N  N   . ALA   C 1 109 ? -61.006 14.381  77.372  1.00 19.20 ?  104 ALA   D N   1 
ATOM   3991 C  CA  . ALA   C 1 109 ? -59.827 13.831  78.066  1.00 20.11 ?  104 ALA   D CA  1 
ATOM   3992 C  C   . ALA   C 1 109 ? -59.060 12.986  77.056  1.00 18.78 ?  104 ALA   D C   1 
ATOM   3993 O  O   . ALA   C 1 109 ? -59.641 12.471  76.121  1.00 17.13 ?  104 ALA   D O   1 
ATOM   3994 C  CB  . ALA   C 1 109 ? -60.248 13.049  79.293  1.00 20.15 ?  104 ALA   D CB  1 
ATOM   3995 N  N   . PRO   C 1 110 ? -57.715 12.876  77.181  1.00 17.18 ?  105 PRO   D N   1 
ATOM   3996 C  CA  . PRO   C 1 110 ? -56.939 12.098  76.237  1.00 16.61 ?  105 PRO   D CA  1 
ATOM   3997 C  C   . PRO   C 1 110 ? -57.205 10.616  76.467  1.00 17.39 ?  105 PRO   D C   1 
ATOM   3998 O  O   . PRO   C 1 110 ? -57.793 10.172  77.505  1.00 19.14 ?  105 PRO   D O   1 
ATOM   3999 C  CB  . PRO   C 1 110 ? -55.466 12.390  76.598  1.00 18.73 ?  105 PRO   D CB  1 
ATOM   4000 C  CG  . PRO   C 1 110 ? -55.556 13.582  77.501  1.00 19.62 ?  105 PRO   D CG  1 
ATOM   4001 C  CD  . PRO   C 1 110 ? -56.887 13.454  78.232  1.00 19.12 ?  105 PRO   D CD  1 
ATOM   4002 N  N   . THR   C 1 111 ? -56.785 9.843   75.492  1.00 16.20 ?  106 THR   D N   1 
ATOM   4003 C  CA  . THR   C 1 111 ? -56.784 8.373   75.655  1.00 17.88 ?  106 THR   D CA  1 
ATOM   4004 C  C   . THR   C 1 111 ? -55.604 7.764   74.893  1.00 18.32 ?  106 THR   D C   1 
ATOM   4005 O  O   . THR   C 1 111 ? -54.776 8.489   74.342  1.00 18.99 ?  106 THR   D O   1 
ATOM   4006 C  CB  . THR   C 1 111 ? -58.151 7.779   75.303  1.00 17.78 ?  106 THR   D CB  1 
ATOM   4007 O  OG1 . THR   C 1 111 ? -58.175 6.430   75.783  1.00 18.95 ?  106 THR   D OG1 1 
ATOM   4008 C  CG2 . THR   C 1 111 ? -58.497 7.785   73.839  1.00 17.50 ?  106 THR   D CG2 1 
ATOM   4009 N  N   . TRP   C 1 112 ? -55.502 6.445   74.954  1.00 17.98 ?  107 TRP   D N   1 
ATOM   4010 C  CA  . TRP   C 1 112 ? -54.528 5.721   74.116  1.00 17.38 ?  107 TRP   D CA  1 
ATOM   4011 C  C   . TRP   C 1 112 ? -55.333 4.721   73.329  1.00 19.67 ?  107 TRP   D C   1 
ATOM   4012 O  O   . TRP   C 1 112 ? -56.000 3.880   73.953  1.00 20.73 ?  107 TRP   D O   1 
ATOM   4013 C  CB  . TRP   C 1 112 ? -53.451 5.089   74.971  1.00 17.87 ?  107 TRP   D CB  1 
ATOM   4014 C  CG  . TRP   C 1 112 ? -52.144 4.891   74.272  1.00 17.07 ?  107 TRP   D CG  1 
ATOM   4015 C  CD1 . TRP   C 1 112 ? -51.899 4.015   73.250  1.00 18.26 ?  107 TRP   D CD1 1 
ATOM   4016 C  CD2 . TRP   C 1 112 ? -50.912 5.576   74.534  1.00 17.86 ?  107 TRP   D CD2 1 
ATOM   4017 N  NE1 . TRP   C 1 112 ? -50.573 4.088   72.880  1.00 18.30 ?  107 TRP   D NE1 1 
ATOM   4018 C  CE2 . TRP   C 1 112 ? -49.955 5.043   73.639  1.00 17.54 ?  107 TRP   D CE2 1 
ATOM   4019 C  CE3 . TRP   C 1 112 ? -50.516 6.589   75.424  1.00 16.83 ?  107 TRP   D CE3 1 
ATOM   4020 C  CZ2 . TRP   C 1 112 ? -48.640 5.501   73.595  1.00 16.80 ?  107 TRP   D CZ2 1 
ATOM   4021 C  CZ3 . TRP   C 1 112 ? -49.200 7.027   75.392  1.00 17.93 ?  107 TRP   D CZ3 1 
ATOM   4022 C  CH2 . TRP   C 1 112 ? -48.290 6.491   74.487  1.00 18.82 ?  107 TRP   D CH2 1 
ATOM   4023 N  N   . ASN   C 1 113 ? -55.304 4.828   72.015  1.00 17.08 ?  108 ASN   D N   1 
ATOM   4024 C  CA  . ASN   C 1 113 ? -55.958 3.812   71.184  1.00 15.50 ?  108 ASN   D CA  1 
ATOM   4025 C  C   . ASN   C 1 113 ? -54.998 2.628   71.115  1.00 17.11 ?  108 ASN   D C   1 
ATOM   4026 O  O   . ASN   C 1 113 ? -53.780 2.854   70.857  1.00 17.58 ?  108 ASN   D O   1 
ATOM   4027 C  CB  . ASN   C 1 113 ? -56.309 4.314   69.784  1.00 16.91 ?  108 ASN   D CB  1 
ATOM   4028 C  CG  . ASN   C 1 113 ? -57.593 5.111   69.757  1.00 17.02 ?  108 ASN   D CG  1 
ATOM   4029 O  OD1 . ASN   C 1 113 ? -58.192 5.332   70.820  1.00 18.50 ?  108 ASN   D OD1 1 
ATOM   4030 N  ND2 . ASN   C 1 113 ? -57.938 5.639   68.594  1.00 18.68 ?  108 ASN   D ND2 1 
ATOM   4031 N  N   . PHE   C 1 114 ? -55.512 1.406   71.210  1.00 16.09 ?  109 PHE   D N   1 
ATOM   4032 C  CA  . PHE   C 1 114 ? -54.619 0.231   71.185  1.00 17.66 ?  109 PHE   D CA  1 
ATOM   4033 C  C   . PHE   C 1 114 ? -55.408 -1.017  70.856  1.00 17.08 ?  109 PHE   D C   1 
ATOM   4034 O  O   . PHE   C 1 114 ? -56.646 -1.012  70.927  1.00 16.82 ?  109 PHE   D O   1 
ATOM   4035 C  CB  . PHE   C 1 114 ? -53.876 0.097   72.528  1.00 17.31 ?  109 PHE   D CB  1 
ATOM   4036 C  CG  . PHE   C 1 114 ? -54.719 -0.432  73.643  1.00 16.89 ?  109 PHE   D CG  1 
ATOM   4037 C  CD1 . PHE   C 1 114 ? -55.492 0.415   74.429  1.00 17.62 ?  109 PHE   D CD1 1 
ATOM   4038 C  CD2 . PHE   C 1 114 ? -54.723 -1.781  73.926  1.00 18.30 ?  109 PHE   D CD2 1 
ATOM   4039 C  CE1 . PHE   C 1 114 ? -56.143 -0.084  75.533  1.00 20.24 ?  109 PHE   D CE1 1 
ATOM   4040 C  CE2 . PHE   C 1 114 ? -55.463 -2.295  74.982  1.00 18.83 ?  109 PHE   D CE2 1 
ATOM   4041 C  CZ  . PHE   C 1 114 ? -56.162 -1.435  75.789  1.00 18.35 ?  109 PHE   D CZ  1 
ATOM   4042 N  N   . THR   C 1 115 ? -54.642 -2.039  70.470  1.00 17.01 ?  110 THR   D N   1 
ATOM   4043 C  CA  . THR   C 1 115 ? -55.160 -3.353  70.071  1.00 18.62 ?  110 THR   D CA  1 
ATOM   4044 C  C   . THR   C 1 115 ? -54.526 -4.391  70.957  1.00 18.31 ?  110 THR   D C   1 
ATOM   4045 O  O   . THR   C 1 115 ? -53.289 -4.373  71.141  1.00 15.13 ?  110 THR   D O   1 
ATOM   4046 C  CB  . THR   C 1 115 ? -54.977 -3.576  68.569  1.00 18.48 ?  110 THR   D CB  1 
ATOM   4047 O  OG1 . THR   C 1 115 ? -53.600 -3.350  68.268  1.00 20.87 ?  110 THR   D OG1 1 
ATOM   4048 C  CG2 . THR   C 1 115 ? -55.923 -2.666  67.817  1.00 20.42 ?  110 THR   D CG2 1 
ATOM   4049 N  N   . SER   C 1 116 ? -55.327 -5.280  71.502  1.00 18.06 ?  111 SER   D N   1 
ATOM   4050 C  CA  . SER   C 1 116 ? -54.806 -6.374  72.339  1.00 19.86 ?  111 SER   D CA  1 
ATOM   4051 C  C   . SER   C 1 116 ? -55.701 -7.596  72.145  1.00 19.68 ?  111 SER   D C   1 
ATOM   4052 O  O   . SER   C 1 116 ? -56.917 -7.469  72.145  1.00 22.86 ?  111 SER   D O   1 
ATOM   4053 C  CB  . SER   C 1 116 ? -54.766 -5.937  73.798  1.00 21.49 ?  111 SER   D CB  1 
ATOM   4054 O  OG  . SER   C 1 116 ? -54.245 -6.953  74.637  1.00 28.18 ?  111 SER   D OG  1 
ATOM   4055 N  N   . VAL   C 1 117 ? -55.065 -8.744  72.098  1.00 17.08 ?  112 VAL   D N   1 
ATOM   4056 C  CA  . VAL   C 1 117 ? -55.729 -10.059 72.186  1.00 17.95 ?  112 VAL   D CA  1 
ATOM   4057 C  C   . VAL   C 1 117 ? -55.154 -10.781 73.392  1.00 17.39 ?  112 VAL   D C   1 
ATOM   4058 O  O   . VAL   C 1 117 ? -53.907 -10.893 73.506  1.00 15.85 ?  112 VAL   D O   1 
ATOM   4059 C  CB  . VAL   C 1 117 ? -55.597 -10.838 70.867  1.00 17.02 ?  112 VAL   D CB  1 
ATOM   4060 C  CG1 . VAL   C 1 117 ? -56.075 -12.262 70.969  1.00 18.14 ?  112 VAL   D CG1 1 
ATOM   4061 C  CG2 . VAL   C 1 117 ? -56.343 -10.130 69.756  1.00 19.18 ?  112 VAL   D CG2 1 
ATOM   4062 N  N   . GLN   C 1 118 ? -56.060 -11.269 74.231  1.00 15.65 ?  113 GLN   D N   1 
ATOM   4063 C  CA  . GLN   C 1 118 ? -55.744 -12.131 75.373  1.00 16.15 ?  113 GLN   D CA  1 
ATOM   4064 C  C   . GLN   C 1 118 ? -56.370 -13.494 75.160  1.00 19.02 ?  113 GLN   D C   1 
ATOM   4065 O  O   . GLN   C 1 118 ? -57.601 -13.602 75.034  1.00 18.75 ?  113 GLN   D O   1 
ATOM   4066 C  CB  . GLN   C 1 118 ? -56.120 -11.571 76.722  1.00 16.72 ?  113 GLN   D CB  1 
ATOM   4067 C  CG  . GLN   C 1 118 ? -55.399 -10.274 77.042  1.00 17.71 ?  113 GLN   D CG  1 
ATOM   4068 C  CD  . GLN   C 1 118 ? -55.838 -9.723  78.372  1.00 18.36 ?  113 GLN   D CD  1 
ATOM   4069 O  OE1 . GLN   C 1 118 ? -56.394 -10.431 79.194  1.00 20.74 ?  113 GLN   D OE1 1 
ATOM   4070 N  NE2 . GLN   C 1 118 ? -55.573 -8.460  78.579  1.00 19.50 ?  113 GLN   D NE2 1 
ATOM   4071 N  N   . VAL   C 1 119 ? -55.519 -14.486 75.073  1.00 17.72 ?  114 VAL   D N   1 
ATOM   4072 C  CA  . VAL   C 1 119 ? -55.923 -15.912 74.991  1.00 18.89 ?  114 VAL   D CA  1 
ATOM   4073 C  C   . VAL   C 1 119 ? -55.578 -16.614 76.308  1.00 19.36 ?  114 VAL   D C   1 
ATOM   4074 O  O   . VAL   C 1 119 ? -54.470 -16.466 76.881  1.00 19.68 ?  114 VAL   D O   1 
ATOM   4075 C  CB  . VAL   C 1 119 ? -55.349 -16.673 73.789  1.00 20.91 ?  114 VAL   D CB  1 
ATOM   4076 C  CG1 . VAL   C 1 119 ? -55.815 -16.076 72.481  1.00 23.83 ?  114 VAL   D CG1 1 
ATOM   4077 C  CG2 . VAL   C 1 119 ? -53.854 -16.784 73.855  1.00 23.23 ?  114 VAL   D CG2 1 
ATOM   4078 N  N   . ARG   C 1 120 ? -56.529 -17.388 76.772  1.00 21.00 ?  115 ARG   D N   1 
ATOM   4079 C  CA  . ARG   C 1 120 ? -56.382 -18.159 78.015  1.00 19.80 ?  115 ARG   D CA  1 
ATOM   4080 C  C   . ARG   C 1 120 ? -56.652 -19.632 77.729  1.00 21.86 ?  115 ARG   D C   1 
ATOM   4081 O  O   . ARG   C 1 120 ? -57.587 -19.960 76.948  1.00 21.01 ?  115 ARG   D O   1 
ATOM   4082 C  CB  . ARG   C 1 120 ? -57.325 -17.621 79.089  1.00 21.10 ?  115 ARG   D CB  1 
ATOM   4083 C  CG  . ARG   C 1 120 ? -56.903 -16.266 79.609  1.00 21.95 ?  115 ARG   D CG  1 
ATOM   4084 C  CD  . ARG   C 1 120 ? -57.953 -15.630 80.531  1.00 24.49 ?  115 ARG   D CD  1 
ATOM   4085 N  NE  . ARG   C 1 120 ? -57.350 -14.536 81.268  1.00 22.19 ?  115 ARG   D NE  1 
ATOM   4086 C  CZ  . ARG   C 1 120 ? -57.106 -13.316 80.775  1.00 21.60 ?  115 ARG   D CZ  1 
ATOM   4087 N  NH1 . ARG   C 1 120 ? -57.483 -12.967 79.555  1.00 20.54 1  115 ARG   D NH1 1 
ATOM   4088 N  NH2 . ARG   C 1 120 ? -56.518 -12.415 81.536  1.00 24.15 ?  115 ARG   D NH2 1 
ATOM   4089 N  N   . GLY   C 1 121 ? -55.854 -20.458 78.380  1.00 20.25 ?  116 GLY   D N   1 
ATOM   4090 C  CA  . GLY   C 1 121 ? -56.100 -21.902 78.450  1.00 21.01 ?  116 GLY   D CA  1 
ATOM   4091 C  C   . GLY   C 1 121 ? -55.000 -22.625 79.178  1.00 23.34 ?  116 GLY   D C   1 
ATOM   4092 O  O   . GLY   C 1 121 ? -54.166 -21.997 79.870  1.00 22.34 ?  116 GLY   D O   1 
ATOM   4093 N  N   . GLU   C 1 122 ? -54.984 -23.938 78.985  1.00 25.11 ?  117 GLU   D N   1 
ATOM   4094 C  CA  . GLU   C 1 122 ? -54.027 -24.851 79.641  1.00 27.91 ?  117 GLU   D CA  1 
ATOM   4095 C  C   . GLU   C 1 122 ? -52.757 -24.895 78.807  1.00 24.58 ?  117 GLU   D C   1 
ATOM   4096 O  O   . GLU   C 1 122 ? -52.835 -25.122 77.605  1.00 28.61 ?  117 GLU   D O   1 
ATOM   4097 C  CB  . GLU   C 1 122 ? -54.588 -26.272 79.759  1.00 33.14 ?  117 GLU   D CB  1 
ATOM   4098 C  CG  . GLU   C 1 122 ? -55.302 -26.541 81.066  1.00 44.02 ?  117 GLU   D CG  1 
ATOM   4099 C  CD  . GLU   C 1 122 ? -55.375 -28.023 81.454  1.00 53.04 ?  117 GLU   D CD  1 
ATOM   4100 O  OE1 . GLU   C 1 122 ? -55.603 -28.306 82.668  1.00 55.18 ?  117 GLU   D OE1 1 
ATOM   4101 O  OE2 . GLU   C 1 122 ? -55.171 -28.899 80.552  1.00 53.61 -1 117 GLU   D OE2 1 
ATOM   4102 N  N   . LEU   C 1 123 ? -51.620 -24.697 79.430  1.00 23.16 ?  118 LEU   D N   1 
ATOM   4103 C  CA  . LEU   C 1 123 ? -50.343 -24.850 78.723  1.00 22.85 ?  118 LEU   D CA  1 
ATOM   4104 C  C   . LEU   C 1 123 ? -49.804 -26.249 78.996  1.00 23.04 ?  118 LEU   D C   1 
ATOM   4105 O  O   . LEU   C 1 123 ? -49.669 -26.623 80.169  1.00 24.33 ?  118 LEU   D O   1 
ATOM   4106 C  CB  . LEU   C 1 123 ? -49.356 -23.797 79.187  1.00 25.83 ?  118 LEU   D CB  1 
ATOM   4107 C  CG  . LEU   C 1 123 ? -48.031 -23.812 78.423  1.00 25.60 ?  118 LEU   D CG  1 
ATOM   4108 C  CD1 . LEU   C 1 123 ? -47.474 -22.419 78.363  1.00 27.25 ?  118 LEU   D CD1 1 
ATOM   4109 C  CD2 . LEU   C 1 123 ? -47.028 -24.731 79.072  1.00 26.00 ?  118 LEU   D CD2 1 
ATOM   4110 N  N   . ARG   C 1 124 ? -49.518 -26.980 77.930  1.00 23.07 ?  119 ARG   D N   1 
ATOM   4111 C  CA  . ARG   C 1 124 ? -48.892 -28.327 78.013  1.00 22.97 ?  119 ARG   D CA  1 
ATOM   4112 C  C   . ARG   C 1 124 ? -47.457 -28.207 77.510  1.00 25.35 ?  119 ARG   D C   1 
ATOM   4113 O  O   . ARG   C 1 124 ? -47.284 -27.666 76.431  1.00 23.67 ?  119 ARG   D O   1 
ATOM   4114 C  CB  . ARG   C 1 124 ? -49.641 -29.365 77.195  1.00 26.67 ?  119 ARG   D CB  1 
ATOM   4115 C  CG  . ARG   C 1 124 ? -49.032 -30.755 77.382  1.00 36.29 ?  119 ARG   D CG  1 
ATOM   4116 C  CD  . ARG   C 1 124 ? -49.650 -31.941 76.654  1.00 43.20 ?  119 ARG   D CD  1 
ATOM   4117 N  NE  . ARG   C 1 124 ? -49.608 -31.812 75.201  1.00 49.33 ?  119 ARG   D NE  1 
ATOM   4118 C  CZ  . ARG   C 1 124 ? -48.511 -31.942 74.443  1.00 48.41 ?  119 ARG   D CZ  1 
ATOM   4119 N  NH1 . ARG   C 1 124 ? -47.329 -32.223 74.979  1.00 46.87 1  119 ARG   D NH1 1 
ATOM   4120 N  NH2 . ARG   C 1 124 ? -48.626 -31.822 73.134  1.00 46.75 ?  119 ARG   D NH2 1 
ATOM   4121 N  N   . LYS   C 1 125 ? -46.491 -28.684 78.288  1.00 23.95 ?  120 LYS   D N   1 
ATOM   4122 C  CA  . LYS   C 1 125 ? -45.079 -28.737 77.841  1.00 24.92 ?  120 LYS   D CA  1 
ATOM   4123 C  C   . LYS   C 1 125 ? -44.907 -29.875 76.850  1.00 27.90 ?  120 LYS   D C   1 
ATOM   4124 O  O   . LYS   C 1 125 ? -45.363 -31.004 77.110  1.00 28.14 ?  120 LYS   D O   1 
ATOM   4125 C  CB  . LYS   C 1 125 ? -44.140 -28.978 79.005  1.00 27.52 ?  120 LYS   D CB  1 
ATOM   4126 C  CG  . LYS   C 1 125 ? -44.105 -27.849 80.008  1.00 26.11 ?  120 LYS   D CG  1 
ATOM   4127 C  CD  . LYS   C 1 125 ? -43.258 -28.241 81.170  1.00 27.82 ?  120 LYS   D CD  1 
ATOM   4128 C  CE  . LYS   C 1 125 ? -43.014 -27.057 82.065  1.00 26.08 ?  120 LYS   D CE  1 
ATOM   4129 N  NZ  . LYS   C 1 125 ? -42.196 -27.369 83.261  1.00 28.41 1  120 LYS   D NZ  1 
ATOM   4130 N  N   . VAL   C 1 126 ? -44.218 -29.598 75.761  1.00 23.63 ?  121 VAL   D N   1 
ATOM   4131 C  CA  . VAL   C 1 126 ? -43.768 -30.594 74.776  1.00 22.77 ?  121 VAL   D CA  1 
ATOM   4132 C  C   . VAL   C 1 126 ? -42.471 -31.168 75.306  1.00 22.06 ?  121 VAL   D C   1 
ATOM   4133 O  O   . VAL   C 1 126 ? -41.613 -30.403 75.753  1.00 22.12 ?  121 VAL   D O   1 
ATOM   4134 C  CB  . VAL   C 1 126 ? -43.615 -29.974 73.387  1.00 23.90 ?  121 VAL   D CB  1 
ATOM   4135 C  CG1 . VAL   C 1 126 ? -43.146 -30.995 72.355  1.00 25.45 ?  121 VAL   D CG1 1 
ATOM   4136 C  CG2 . VAL   C 1 126 ? -44.934 -29.349 72.922  1.00 25.34 ?  121 VAL   D CG2 1 
ATOM   4137 N  N   . GLU   C 1 127 ? -42.389 -32.503 75.349  1.00 25.65 ?  122 GLU   D N   1 
ATOM   4138 C  CA  . GLU   C 1 127 ? -41.117 -33.167 75.693  1.00 26.34 ?  122 GLU   D CA  1 
ATOM   4139 C  C   . GLU   C 1 127 ? -40.543 -33.863 74.462  1.00 26.93 ?  122 GLU   D C   1 
ATOM   4140 O  O   . GLU   C 1 127 ? -39.298 -33.966 74.425  1.00 27.30 ?  122 GLU   D O   1 
ATOM   4141 C  CB  . GLU   C 1 127 ? -41.289 -34.144 76.868  1.00 29.82 ?  122 GLU   D CB  1 
ATOM   4142 C  CG  . GLU   C 1 127 ? -41.861 -33.472 78.089  1.00 31.26 ?  122 GLU   D CG  1 
ATOM   4143 C  CD  . GLU   C 1 127 ? -40.932 -32.567 78.871  1.00 30.56 ?  122 GLU   D CD  1 
ATOM   4144 O  OE1 . GLU   C 1 127 ? -39.779 -32.285 78.421  1.00 28.27 ?  122 GLU   D OE1 1 
ATOM   4145 O  OE2 . GLU   C 1 127 ? -41.367 -32.121 79.948  1.00 34.94 -1 122 GLU   D OE2 1 
ATOM   4146 N  N   . SER   C 1 128 ? -41.384 -34.361 73.552  1.00 24.19 ?  123 SER   D N   1 
ATOM   4147 C  CA  . SER   C 1 128 ? -40.954 -35.002 72.290  1.00 25.22 ?  123 SER   D CA  1 
ATOM   4148 C  C   . SER   C 1 128 ? -39.929 -34.137 71.560  1.00 30.11 ?  123 SER   D C   1 
ATOM   4149 O  O   . SER   C 1 128 ? -40.146 -32.926 71.480  1.00 28.56 ?  123 SER   D O   1 
ATOM   4150 C  CB  . SER   C 1 128 ? -42.110 -35.300 71.424  1.00 31.75 ?  123 SER   D CB  1 
ATOM   4151 O  OG  . SER   C 1 128 ? -41.674 -35.556 70.105  1.00 38.99 ?  123 SER   D OG  1 
ATOM   4152 N  N   . ALA   C 1 129 ? -38.841 -34.734 71.069  1.00 29.54 ?  124 ALA   D N   1 
ATOM   4153 C  CA  . ALA   C 1 129 ? -37.825 -34.035 70.247  1.00 32.61 ?  124 ALA   D CA  1 
ATOM   4154 C  C   . ALA   C 1 129 ? -38.432 -33.703 68.888  1.00 29.88 ?  124 ALA   D C   1 
ATOM   4155 O  O   . ALA   C 1 129 ? -38.166 -32.601 68.357  1.00 28.69 ?  124 ALA   D O   1 
ATOM   4156 C  CB  . ALA   C 1 129 ? -36.589 -34.875 70.079  1.00 35.15 ?  124 ALA   D CB  1 
ATOM   4157 N  N   . ASP   C 1 130 ? -39.193 -34.630 68.312  1.00 30.85 ?  125 ASP   D N   1 
ATOM   4158 C  CA  . ASP   C 1 130 ? -39.825 -34.403 66.987  1.00 36.15 ?  125 ASP   D CA  1 
ATOM   4159 C  C   . ASP   C 1 130 ? -40.745 -33.168 67.076  1.00 31.13 ?  125 ASP   D C   1 
ATOM   4160 O  O   . ASP   C 1 130 ? -40.680 -32.307 66.150  1.00 27.11 ?  125 ASP   D O   1 
ATOM   4161 C  CB  . ASP   C 1 130 ? -40.544 -35.661 66.498  1.00 40.28 ?  125 ASP   D CB  1 
ATOM   4162 C  CG  . ASP   C 1 130 ? -39.580 -36.825 66.309  1.00 52.52 ?  125 ASP   D CG  1 
ATOM   4163 O  OD1 . ASP   C 1 130 ? -38.680 -36.693 65.455  1.00 59.45 ?  125 ASP   D OD1 1 
ATOM   4164 O  OD2 . ASP   C 1 130 ? -39.686 -37.831 67.072  1.00 62.49 -1 125 ASP   D OD2 1 
ATOM   4165 N  N   . ASP   C 1 131 ? -41.571 -33.090 68.117  1.00 25.89 ?  126 ASP   D N   1 
ATOM   4166 C  CA  . ASP   C 1 131 ? -42.595 -32.023 68.253  1.00 26.82 ?  126 ASP   D CA  1 
ATOM   4167 C  C   . ASP   C 1 131 ? -41.885 -30.712 68.600  1.00 23.22 ?  126 ASP   D C   1 
ATOM   4168 O  O   . ASP   C 1 131 ? -42.356 -29.647 68.152  1.00 21.78 ?  126 ASP   D O   1 
ATOM   4169 C  CB  . ASP   C 1 131 ? -43.690 -32.396 69.258  1.00 30.51 ?  126 ASP   D CB  1 
ATOM   4170 C  CG  . ASP   C 1 131 ? -44.617 -33.522 68.812  1.00 37.89 ?  126 ASP   D CG  1 
ATOM   4171 O  OD1 . ASP   C 1 131 ? -44.760 -33.705 67.610  1.00 43.09 ?  126 ASP   D OD1 1 
ATOM   4172 O  OD2 . ASP   C 1 131 ? -45.228 -34.180 69.683  1.00 45.30 -1 126 ASP   D OD2 1 
ATOM   4173 N  N   . THR   C 1 132 ? -40.758 -30.777 69.293  1.00 22.01 ?  127 THR   D N   1 
ATOM   4174 C  CA  . THR   C 1 132 ? -39.974 -29.564 69.631  1.00 21.91 ?  127 THR   D CA  1 
ATOM   4175 C  C   . THR   C 1 132 ? -39.391 -29.005 68.334  1.00 21.24 ?  127 THR   D C   1 
ATOM   4176 O  O   . THR   C 1 132 ? -39.517 -27.806 68.063  1.00 19.39 ?  127 THR   D O   1 
ATOM   4177 C  CB  . THR   C 1 132 ? -38.910 -29.845 70.698  1.00 22.31 ?  127 THR   D CB  1 
ATOM   4178 O  OG1 . THR   C 1 132 ? -39.561 -30.367 71.860  1.00 23.33 ?  127 THR   D OG1 1 
ATOM   4179 C  CG2 . THR   C 1 132 ? -38.188 -28.589 71.126  1.00 20.52 ?  127 THR   D CG2 1 
ATOM   4180 N  N   . LEU   C 1 133 ? -38.754 -29.852 67.539  1.00 22.50 ?  128 LEU   D N   1 
ATOM   4181 C  CA  . LEU   C 1 133 ? -38.154 -29.383 66.272  1.00 22.96 ?  128 LEU   D CA  1 
ATOM   4182 C  C   . LEU   C 1 133 ? -39.264 -28.881 65.356  1.00 22.01 ?  128 LEU   D C   1 
ATOM   4183 O  O   . LEU   C 1 133 ? -39.081 -27.850 64.714  1.00 20.38 ?  128 LEU   D O   1 
ATOM   4184 C  CB  . LEU   C 1 133 ? -37.344 -30.500 65.619  1.00 24.72 ?  128 LEU   D CB  1 
ATOM   4185 C  CG  . LEU   C 1 133 ? -36.764 -30.137 64.257  1.00 26.02 ?  128 LEU   D CG  1 
ATOM   4186 C  CD1 . LEU   C 1 133 ? -35.692 -29.049 64.400  1.00 24.60 ?  128 LEU   D CD1 1 
ATOM   4187 C  CD2 . LEU   C 1 133 ? -36.186 -31.385 63.580  1.00 27.35 ?  128 LEU   D CD2 1 
ATOM   4188 N  N   . ALA   C 1 134 ? -40.393 -29.565 65.292  1.00 20.76 ?  129 ALA   D N   1 
ATOM   4189 C  CA  . ALA   C 1 134 ? -41.542 -29.097 64.486  1.00 22.11 ?  129 ALA   D CA  1 
ATOM   4190 C  C   . ALA   C 1 134 ? -41.958 -27.676 64.914  1.00 20.69 ?  129 ALA   D C   1 
ATOM   4191 O  O   . ALA   C 1 134 ? -42.335 -26.854 64.028  1.00 18.74 ?  129 ALA   D O   1 
ATOM   4192 C  CB  . ALA   C 1 134 ? -42.688 -30.064 64.572  1.00 21.13 ?  129 ALA   D CB  1 
ATOM   4193 N  N   . THR   C 1 135 ? -41.968 -27.396 66.211  1.00 19.90 ?  130 THR   D N   1 
ATOM   4194 C  CA  . THR   C 1 135 ? -42.442 -26.102 66.742  1.00 17.25 ?  130 THR   D CA  1 
ATOM   4195 C  C   . THR   C 1 135 ? -41.554 -24.984 66.189  1.00 19.38 ?  130 THR   D C   1 
ATOM   4196 O  O   . THR   C 1 135 ? -42.054 -24.008 65.636  1.00 19.21 ?  130 THR   D O   1 
ATOM   4197 C  CB  . THR   C 1 135 ? -42.393 -26.111 68.273  1.00 19.91 ?  130 THR   D CB  1 
ATOM   4198 O  OG1 . THR   C 1 135 ? -43.280 -27.123 68.764  1.00 21.05 ?  130 THR   D OG1 1 
ATOM   4199 C  CG2 . THR   C 1 135 ? -42.804 -24.765 68.817  1.00 18.40 ?  130 THR   D CG2 1 
ATOM   4200 N  N   . VAL   C 1 136 ? -40.238 -25.167 66.306  1.00 18.31 ?  131 VAL   D N   1 
ATOM   4201 C  CA  . VAL   C 1 136 ? -39.313 -24.067 65.930  1.00 19.69 ?  131 VAL   D CA  1 
ATOM   4202 C  C   . VAL   C 1 136 ? -39.270 -23.926 64.401  1.00 17.90 ?  131 VAL   D C   1 
ATOM   4203 O  O   . VAL   C 1 136 ? -39.202 -22.776 63.933  1.00 19.13 ?  131 VAL   D O   1 
ATOM   4204 C  CB  . VAL   C 1 136 ? -37.923 -24.263 66.528  1.00 19.41 ?  131 VAL   D CB  1 
ATOM   4205 C  CG1 . VAL   C 1 136 ? -37.941 -24.135 68.049  1.00 21.66 ?  131 VAL   D CG1 1 
ATOM   4206 C  CG2 . VAL   C 1 136 ? -37.245 -25.546 66.070  1.00 23.28 ?  131 VAL   D CG2 1 
ATOM   4207 N  N   . ARG   C 1 137 ? -39.362 -25.019 63.659  1.00 19.39 ?  132 ARG   D N   1 
ATOM   4208 C  CA  . ARG   C 1 137 ? -39.427 -24.950 62.184  1.00 20.15 ?  132 ARG   D CA  1 
ATOM   4209 C  C   . ARG   C 1 137 ? -40.697 -24.254 61.722  1.00 20.68 ?  132 ARG   D C   1 
ATOM   4210 O  O   . ARG   C 1 137 ? -40.646 -23.427 60.776  1.00 22.48 ?  132 ARG   D O   1 
ATOM   4211 C  CB  . ARG   C 1 137 ? -39.361 -26.350 61.564  1.00 24.04 ?  132 ARG   D CB  1 
ATOM   4212 C  CG  . ARG   C 1 137 ? -38.041 -27.040 61.804  1.00 29.24 ?  132 ARG   D CG  1 
ATOM   4213 C  CD  . ARG   C 1 137 ? -37.527 -27.458 60.467  1.00 42.48 ?  132 ARG   D CD  1 
ATOM   4214 N  NE  . ARG   C 1 137 ? -38.049 -28.688 59.953  1.00 40.36 ?  132 ARG   D NE  1 
ATOM   4215 C  CZ  . ARG   C 1 137 ? -37.995 -29.046 58.669  1.00 48.90 ?  132 ARG   D CZ  1 
ATOM   4216 N  NH1 . ARG   C 1 137 ? -38.406 -30.241 58.301  1.00 51.20 1  132 ARG   D NH1 1 
ATOM   4217 N  NH2 . ARG   C 1 137 ? -37.571 -28.208 57.740  1.00 56.56 ?  132 ARG   D NH2 1 
ATOM   4218 N  N   . ALA   C 1 138 ? -41.817 -24.550 62.343  1.00 18.27 ?  133 ALA   D N   1 
ATOM   4219 C  CA  . ALA   C 1 138 ? -43.072 -23.896 61.946  1.00 18.46 ?  133 ALA   D CA  1 
ATOM   4220 C  C   . ALA   C 1 138 ? -42.948 -22.404 62.294  1.00 19.11 ?  133 ALA   D C   1 
ATOM   4221 O  O   . ALA   C 1 138 ? -43.550 -21.566 61.603  1.00 19.01 ?  133 ALA   D O   1 
ATOM   4222 C  CB  . ALA   C 1 138 ? -44.220 -24.534 62.649  1.00 18.35 ?  133 ALA   D CB  1 
ATOM   4223 N  N   . THR   C 1 139 ? -42.272 -22.090 63.393  1.00 17.28 ?  134 THR   D N   1 
ATOM   4224 C  CA  . THR   C 1 139 ? -42.165 -20.669 63.833  1.00 18.04 ?  134 THR   D CA  1 
ATOM   4225 C  C   . THR   C 1 139 ? -41.328 -19.920 62.797  1.00 19.16 ?  134 THR   D C   1 
ATOM   4226 O  O   . THR   C 1 139 ? -41.692 -18.807 62.376  1.00 19.27 ?  134 THR   D O   1 
ATOM   4227 C  CB  . THR   C 1 139 ? -41.616 -20.586 65.255  1.00 19.42 ?  134 THR   D CB  1 
ATOM   4228 O  OG1 . THR   C 1 139 ? -42.510 -21.340 66.080  1.00 18.31 ?  134 THR   D OG1 1 
ATOM   4229 C  CG2 . THR   C 1 139 ? -41.479 -19.171 65.754  1.00 19.56 ?  134 THR   D CG2 1 
ATOM   4230 N  N   . VAL   C 1 140 ? -40.192 -20.509 62.395  1.00 18.22 ?  135 VAL   D N   1 
ATOM   4231 C  CA  . VAL   C 1 140 ? -39.409 -19.901 61.294  1.00 18.69 ?  135 VAL   D CA  1 
ATOM   4232 C  C   . VAL   C 1 140 ? -40.304 -19.733 60.056  1.00 20.50 ?  135 VAL   D C   1 
ATOM   4233 O  O   . VAL   C 1 140 ? -40.315 -18.650 59.452  1.00 18.99 ?  135 VAL   D O   1 
ATOM   4234 C  CB  . VAL   C 1 140 ? -38.183 -20.756 60.948  1.00 21.77 ?  135 VAL   D CB  1 
ATOM   4235 C  CG1 . VAL   C 1 140 ? -37.571 -20.238 59.653  1.00 23.26 ?  135 VAL   D CG1 1 
ATOM   4236 C  CG2 . VAL   C 1 140 ? -37.221 -20.774 62.104  1.00 21.49 ?  135 VAL   D CG2 1 
ATOM   4237 N  N   . ALA   C 1 141 ? -41.011 -20.771 59.633  1.00 20.14 ?  136 ALA   D N   1 
ATOM   4238 C  CA  . ALA   C 1 141 ? -41.826 -20.700 58.402  1.00 22.40 ?  136 ALA   D CA  1 
ATOM   4239 C  C   . ALA   C 1 141 ? -42.807 -19.516 58.470  1.00 23.01 ?  136 ALA   D C   1 
ATOM   4240 O  O   . ALA   C 1 141 ? -42.877 -18.694 57.497  1.00 21.55 ?  136 ALA   D O   1 
ATOM   4241 C  CB  . ALA   C 1 141 ? -42.542 -22.008 58.162  1.00 23.82 ?  136 ALA   D CB  1 
ATOM   4242 N  N   . ALA   C 1 142 ? -43.506 -19.372 59.591  1.00 21.54 ?  137 ALA   D N   1 
ATOM   4243 C  CA  . ALA   C 1 142 ? -44.560 -18.347 59.750  1.00 20.29 ?  137 ALA   D CA  1 
ATOM   4244 C  C   . ALA   C 1 142 ? -43.926 -16.954 59.844  1.00 20.86 ?  137 ALA   D C   1 
ATOM   4245 O  O   . ALA   C 1 142 ? -44.418 -16.027 59.187  1.00 19.93 ?  137 ALA   D O   1 
ATOM   4246 C  CB  . ALA   C 1 142 ? -45.400 -18.680 60.956  1.00 21.88 ?  137 ALA   D CB  1 
ATOM   4247 N  N   . LEU   C 1 143 ? -42.886 -16.793 60.660  1.00 18.00 ?  138 LEU   D N   1 
ATOM   4248 C  CA  . LEU   C 1 143 ? -42.331 -15.448 60.941  1.00 18.32 ?  138 LEU   D CA  1 
ATOM   4249 C  C   . LEU   C 1 143 ? -41.448 -14.987 59.782  1.00 17.59 ?  138 LEU   D C   1 
ATOM   4250 O  O   . LEU   C 1 143 ? -41.494 -13.793 59.434  1.00 16.41 ?  138 LEU   D O   1 
ATOM   4251 C  CB  . LEU   C 1 143 ? -41.528 -15.443 62.228  1.00 17.81 ?  138 LEU   D CB  1 
ATOM   4252 C  CG  . LEU   C 1 143 ? -42.258 -15.785 63.520  1.00 22.05 ?  138 LEU   D CG  1 
ATOM   4253 C  CD1 . LEU   C 1 143 ? -41.746 -15.064 64.698  1.00 16.80 ?  138 LEU   D CD1 1 
ATOM   4254 C  CD2 . LEU   C 1 143 ? -43.757 -15.853 63.452  1.00 22.23 ?  138 LEU   D CD2 1 
ATOM   4255 N  N   . GLU   C 1 144 ? -40.638 -15.880 59.210  1.00 19.01 ?  139 GLU   D N   1 
ATOM   4256 C  CA  . GLU   C 1 144 ? -39.768 -15.458 58.071  1.00 18.92 ?  139 GLU   D CA  1 
ATOM   4257 C  C   . GLU   C 1 144 ? -40.674 -15.034 56.906  1.00 20.20 ?  139 GLU   D C   1 
ATOM   4258 O  O   . GLU   C 1 144 ? -40.411 -13.996 56.246  1.00 19.10 ?  139 GLU   D O   1 
ATOM   4259 C  CB  . GLU   C 1 144 ? -38.809 -16.572 57.686  1.00 20.37 ?  139 GLU   D CB  1 
ATOM   4260 C  CG  . GLU   C 1 144 ? -37.768 -16.139 56.662  1.00 21.21 ?  139 GLU   D CG  1 
ATOM   4261 C  CD  . GLU   C 1 144 ? -36.768 -15.088 57.104  1.00 19.68 ?  139 GLU   D CD  1 
ATOM   4262 O  OE1 . GLU   C 1 144 ? -36.537 -14.946 58.310  1.00 19.45 ?  139 GLU   D OE1 1 
ATOM   4263 O  OE2 . GLU   C 1 144 ? -36.246 -14.346 56.203  1.00 18.06 -1 139 GLU   D OE2 1 
ATOM   4264 N  N   . SER   C 1 145 ? -41.765 -15.746 56.668  1.00 19.70 ?  140 SER   D N   1 
ATOM   4265 C  CA  . SER   C 1 145 ? -42.743 -15.378 55.610  1.00 23.40 ?  140 SER   D CA  1 
ATOM   4266 C  C   . SER   C 1 145 ? -43.320 -13.971 55.839  1.00 20.11 ?  140 SER   D C   1 
ATOM   4267 O  O   . SER   C 1 145 ? -43.430 -13.166 54.901  1.00 21.50 ?  140 SER   D O   1 
ATOM   4268 C  CB  . SER   C 1 145 ? -43.869 -16.394 55.523  1.00 24.50 ?  140 SER   D CB  1 
ATOM   4269 O  OG  . SER   C 1 145 ? -44.854 -15.923 54.603  1.00 28.65 ?  140 SER   D OG  1 
ATOM   4270 N  N   . ARG   C 1 146 ? -43.726 -13.660 57.052  1.00 19.31 ?  141 ARG   D N   1 
ATOM   4271 C  CA  . ARG   C 1 146 ? -44.460 -12.432 57.360  1.00 21.36 ?  141 ARG   D CA  1 
ATOM   4272 C  C   . ARG   C 1 146 ? -43.517 -11.272 57.634  1.00 18.79 ?  141 ARG   D C   1 
ATOM   4273 O  O   . ARG   C 1 146 ? -43.882 -10.134 57.273  1.00 21.65 ?  141 ARG   D O   1 
ATOM   4274 C  CB  . ARG   C 1 146 ? -45.397 -12.760 58.525  1.00 24.87 ?  141 ARG   D CB  1 
ATOM   4275 C  CG  . ARG   C 1 146 ? -46.683 -11.961 58.567  1.00 33.48 ?  141 ARG   D CG  1 
ATOM   4276 C  CD  . ARG   C 1 146 ? -47.625 -12.638 59.562  1.00 34.88 ?  141 ARG   D CD  1 
ATOM   4277 N  NE  . ARG   C 1 146 ? -48.471 -13.667 58.968  1.00 39.22 ?  141 ARG   D NE  1 
ATOM   4278 C  CZ  . ARG   C 1 146 ? -49.625 -13.432 58.356  1.00 41.83 ?  141 ARG   D CZ  1 
ATOM   4279 N  NH1 . ARG   C 1 146 ? -50.058 -12.189 58.209  1.00 44.85 1  141 ARG   D NH1 1 
ATOM   4280 N  NH2 . ARG   C 1 146 ? -50.313 -14.436 57.854  1.00 46.24 ?  141 ARG   D NH2 1 
ATOM   4281 N  N   . PHE   C 1 147 ? -42.327 -11.463 58.216  1.00 17.45 ?  142 PHE   D N   1 
ATOM   4282 C  CA  . PHE   C 1 147 ? -41.524 -10.337 58.737  1.00 16.78 ?  142 PHE   D CA  1 
ATOM   4283 C  C   . PHE   C 1 147 ? -40.092 -10.365 58.144  1.00 17.23 ?  142 PHE   D C   1 
ATOM   4284 O  O   . PHE   C 1 147 ? -39.310 -9.477  58.446  1.00 18.54 ?  142 PHE   D O   1 
ATOM   4285 C  CB  . PHE   C 1 147 ? -41.449 -10.451 60.253  1.00 17.29 ?  142 PHE   D CB  1 
ATOM   4286 C  CG  . PHE   C 1 147 ? -42.804 -10.512 60.939  1.00 17.59 ?  142 PHE   D CG  1 
ATOM   4287 C  CD1 . PHE   C 1 147 ? -43.593 -9.396  61.009  1.00 19.22 ?  142 PHE   D CD1 1 
ATOM   4288 C  CD2 . PHE   C 1 147 ? -43.270 -11.694 61.489  1.00 19.02 ?  142 PHE   D CD2 1 
ATOM   4289 C  CE1 . PHE   C 1 147 ? -44.872 -9.463  61.551  1.00 21.13 ?  142 PHE   D CE1 1 
ATOM   4290 C  CE2 . PHE   C 1 147 ? -44.546 -11.782 62.039  1.00 19.97 ?  142 PHE   D CE2 1 
ATOM   4291 C  CZ  . PHE   C 1 147 ? -45.334 -10.653 62.077  1.00 18.97 ?  142 PHE   D CZ  1 
ATOM   4292 N  N   . GLY   C 1 148 ? -39.775 -11.365 57.342  1.00 18.48 ?  143 GLY   D N   1 
ATOM   4293 C  CA  . GLY   C 1 148 ? -38.377 -11.685 57.002  1.00 17.46 ?  143 GLY   D CA  1 
ATOM   4294 C  C   . GLY   C 1 148 ? -37.996 -11.274 55.587  1.00 19.62 ?  143 GLY   D C   1 
ATOM   4295 O  O   . GLY   C 1 148 ? -38.537 -10.281 55.045  1.00 19.54 ?  143 GLY   D O   1 
ATOM   4296 N  N   . ALA   C 1 149 ? -37.039 -12.008 55.020  1.00 19.45 ?  144 ALA   D N   1 
ATOM   4297 C  CA  . ALA   C 1 149 ? -36.393 -11.655 53.738  1.00 20.45 ?  144 ALA   D CA  1 
ATOM   4298 C  C   . ALA   C 1 149 ? -36.050 -12.958 52.980  1.00 22.22 ?  144 ALA   D C   1 
ATOM   4299 O  O   . ALA   C 1 149 ? -34.920 -13.102 52.459  1.00 21.91 ?  144 ALA   D O   1 
ATOM   4300 C  CB  . ALA   C 1 149 ? -35.171 -10.832 54.080  1.00 20.03 ?  144 ALA   D CB  1 
ATOM   4301 N  N   . GLY   C 1 150 ? -36.975 -13.906 52.953  1.00 22.06 ?  145 GLY   D N   1 
ATOM   4302 C  CA  . GLY   C 1 150 ? -36.822 -15.141 52.159  1.00 21.96 ?  145 GLY   D CA  1 
ATOM   4303 C  C   . GLY   C 1 150 ? -35.667 -16.039 52.591  1.00 23.55 ?  145 GLY   D C   1 
ATOM   4304 O  O   . GLY   C 1 150 ? -35.234 -16.881 51.782  1.00 23.88 ?  145 GLY   D O   1 
ATOM   4305 N  N   . TRP   C 1 151 ? -35.235 -15.975 53.847  1.00 20.96 ?  146 TRP   D N   1 
ATOM   4306 C  CA  . TRP   C 1 151 ? -34.226 -16.910 54.395  1.00 20.30 ?  146 TRP   D CA  1 
ATOM   4307 C  C   . TRP   C 1 151 ? -34.735 -18.353 54.356  1.00 19.55 ?  146 TRP   D C   1 
ATOM   4308 O  O   . TRP   C 1 151 ? -35.876 -18.641 54.737  1.00 22.19 ?  146 TRP   D O   1 
ATOM   4309 C  CB  . TRP   C 1 151 ? -33.821 -16.527 55.802  1.00 19.52 ?  146 TRP   D CB  1 
ATOM   4310 C  CG  . TRP   C 1 151 ? -32.741 -17.371 56.375  1.00 19.69 ?  146 TRP   D CG  1 
ATOM   4311 C  CD1 . TRP   C 1 151 ? -31.430 -17.426 55.992  1.00 19.74 ?  146 TRP   D CD1 1 
ATOM   4312 C  CD2 . TRP   C 1 151 ? -32.897 -18.327 57.435  1.00 18.63 ?  146 TRP   D CD2 1 
ATOM   4313 N  NE1 . TRP   C 1 151 ? -30.750 -18.318 56.772  1.00 20.68 ?  146 TRP   D NE1 1 
ATOM   4314 C  CE2 . TRP   C 1 151 ? -31.623 -18.901 57.656  1.00 19.92 ?  146 TRP   D CE2 1 
ATOM   4315 C  CE3 . TRP   C 1 151 ? -33.995 -18.727 58.196  1.00 19.21 ?  146 TRP   D CE3 1 
ATOM   4316 C  CZ2 . TRP   C 1 151 ? -31.414 -19.847 58.658  1.00 21.75 ?  146 TRP   D CZ2 1 
ATOM   4317 C  CZ3 . TRP   C 1 151 ? -33.781 -19.652 59.198  1.00 20.69 ?  146 TRP   D CZ3 1 
ATOM   4318 C  CH2 . TRP   C 1 151 ? -32.510 -20.187 59.416  1.00 21.76 ?  146 TRP   D CH2 1 
ATOM   4319 N  N   . ASP   C 1 152 ? -33.895 -19.222 53.821  1.00 24.62 ?  147 ASP   D N   1 
ATOM   4320 C  CA  . ASP   C 1 152 ? -34.171 -20.669 53.667  1.00 23.28 ?  147 ASP   D CA  1 
ATOM   4321 C  C   . ASP   C 1 152 ? -33.497 -21.389 54.830  1.00 22.76 ?  147 ASP   D C   1 
ATOM   4322 O  O   . ASP   C 1 152 ? -32.259 -21.349 54.934  1.00 20.44 ?  147 ASP   D O   1 
ATOM   4323 C  CB  . ASP   C 1 152 ? -33.664 -21.168 52.316  1.00 26.35 ?  147 ASP   D CB  1 
ATOM   4324 C  CG  . ASP   C 1 152 ? -33.898 -22.635 52.035  1.00 31.34 ?  147 ASP   D CG  1 
ATOM   4325 O  OD1 . ASP   C 1 152 ? -34.444 -23.335 52.918  1.00 27.50 ?  147 ASP   D OD1 1 
ATOM   4326 O  OD2 . ASP   C 1 152 ? -33.543 -23.056 50.907  1.00 34.44 -1 147 ASP   D OD2 1 
ATOM   4327 N  N   . MET   C 1 153 ? -34.283 -21.995 55.712  1.00 23.01 ?  148 MET   D N   1 
ATOM   4328 C  CA  . MET   C 1 153 ? -33.742 -22.670 56.919  1.00 24.03 ?  148 MET   D CA  1 
ATOM   4329 C  C   . MET   C 1 153 ? -33.024 -23.992 56.569  1.00 23.66 ?  148 MET   D C   1 
ATOM   4330 O  O   . MET   C 1 153 ? -32.375 -24.515 57.469  1.00 22.67 ?  148 MET   D O   1 
ATOM   4331 C  CB  . MET   C 1 153 ? -34.844 -22.986 57.926  1.00 26.01 ?  148 MET   D CB  1 
ATOM   4332 C  CG  . MET   C 1 153 ? -35.945 -23.864 57.383  1.00 29.55 ?  148 MET   D CG  1 
ATOM   4333 S  SD  . MET   C 1 153 ? -37.113 -24.188 58.732  1.00 27.02 ?  148 MET   D SD  1 
ATOM   4334 C  CE  . MET   C 1 153 ? -38.623 -23.586 57.988  1.00 27.11 ?  148 MET   D CE  1 
ATOM   4335 N  N   . THR   C 1 154 ? -33.151 -24.498 55.341  1.00 26.29 ?  149 THR   D N   1 
ATOM   4336 C  CA  . THR   C 1 154 ? -32.728 -25.872 54.957  1.00 27.77 ?  149 THR   D CA  1 
ATOM   4337 C  C   . THR   C 1 154 ? -31.285 -26.122 55.406  1.00 27.60 ?  149 THR   D C   1 
ATOM   4338 O  O   . THR   C 1 154 ? -31.064 -27.130 56.139  1.00 27.82 ?  149 THR   D O   1 
ATOM   4339 C  CB  . THR   C 1 154 ? -32.911 -26.142 53.456  1.00 28.97 ?  149 THR   D CB  1 
ATOM   4340 O  OG1 . THR   C 1 154 ? -34.301 -25.966 53.165  1.00 31.59 ?  149 THR   D OG1 1 
ATOM   4341 C  CG2 . THR   C 1 154 ? -32.447 -27.539 53.096  1.00 33.54 ?  149 THR   D CG2 1 
ATOM   4342 N  N   . GLY   C 1 155 ? -30.351 -25.214 55.097  1.00 25.06 ?  150 GLY   D N   1 
ATOM   4343 C  CA  . GLY   C 1 155 ? -28.933 -25.349 55.481  1.00 24.37 ?  150 GLY   D CA  1 
ATOM   4344 C  C   . GLY   C 1 155 ? -28.673 -25.239 56.977  1.00 26.74 ?  150 GLY   D C   1 
ATOM   4345 O  O   . GLY   C 1 155 ? -27.510 -25.426 57.418  1.00 26.74 ?  150 GLY   D O   1 
ATOM   4346 N  N   . SER   C 1 156 ? -29.683 -24.898 57.784  1.00 24.48 ?  151 SER   D N   1 
ATOM   4347 C  CA  . SER   C 1 156 ? -29.472 -24.687 59.233  1.00 23.80 ?  151 SER   D CA  1 
ATOM   4348 C  C   . SER   C 1 156 ? -30.188 -25.758 60.051  1.00 23.55 ?  151 SER   D C   1 
ATOM   4349 O  O   . SER   C 1 156 ? -30.130 -25.639 61.281  1.00 23.25 ?  151 SER   D O   1 
ATOM   4350 C  CB  . SER   C 1 156 ? -29.912 -23.274 59.662  1.00 23.76 ?  151 SER   D CB  1 
ATOM   4351 O  OG  . SER   C 1 156 ? -29.060 -22.299 59.095  1.00 24.72 ?  151 SER   D OG  1 
ATOM   4352 N  N   . LEU   C 1 157 ? -30.843 -26.721 59.408  1.00 27.02 ?  152 LEU   D N   1 
ATOM   4353 C  CA  . LEU   C 1 157 ? -31.677 -27.714 60.143  1.00 29.15 ?  152 LEU   D CA  1 
ATOM   4354 C  C   . LEU   C 1 157 ? -30.781 -28.532 61.062  1.00 30.57 ?  152 LEU   D C   1 
ATOM   4355 O  O   . LEU   C 1 157 ? -31.227 -28.832 62.188  1.00 28.12 ?  152 LEU   D O   1 
ATOM   4356 C  CB  . LEU   C 1 157 ? -32.481 -28.587 59.189  1.00 30.27 ?  152 LEU   D CB  1 
ATOM   4357 C  CG  . LEU   C 1 157 ? -33.558 -27.870 58.380  1.00 33.24 ?  152 LEU   D CG  1 
ATOM   4358 C  CD1 . LEU   C 1 157 ? -34.204 -28.815 57.371  1.00 33.17 ?  152 LEU   D CD1 1 
ATOM   4359 C  CD2 . LEU   C 1 157 ? -34.619 -27.256 59.293  1.00 33.45 ?  152 LEU   D CD2 1 
ATOM   4360 N  N   . ASP   C 1 158 ? -29.553 -28.879 60.654  1.00 32.19 ?  153 ASP   D N   1 
ATOM   4361 C  CA  . ASP   C 1 158 ? -28.648 -29.628 61.556  1.00 31.92 ?  153 ASP   D CA  1 
ATOM   4362 C  C   . ASP   C 1 158 ? -28.316 -28.748 62.752  1.00 28.87 ?  153 ASP   D C   1 
ATOM   4363 O  O   . ASP   C 1 158 ? -28.140 -29.270 63.883  1.00 28.05 ?  153 ASP   D O   1 
ATOM   4364 C  CB  . ASP   C 1 158 ? -27.391 -30.138 60.834  1.00 39.12 ?  153 ASP   D CB  1 
ATOM   4365 C  CG  . ASP   C 1 158 ? -27.662 -31.310 59.898  1.00 46.19 ?  153 ASP   D CG  1 
ATOM   4366 O  OD1 . ASP   C 1 158 ? -28.771 -31.930 60.003  1.00 46.21 ?  153 ASP   D OD1 1 
ATOM   4367 O  OD2 . ASP   C 1 158 ? -26.782 -31.585 59.043  1.00 56.12 -1 153 ASP   D OD2 1 
ATOM   4368 N  N   . TYR   C 1 159 ? -28.177 -27.436 62.552  1.00 25.30 ?  154 TYR   D N   1 
ATOM   4369 C  CA  . TYR   C 1 159 ? -27.861 -26.515 63.658  1.00 21.23 ?  154 TYR   D CA  1 
ATOM   4370 C  C   . TYR   C 1 159 ? -29.045 -26.460 64.622  1.00 17.92 ?  154 TYR   D C   1 
ATOM   4371 O  O   . TYR   C 1 159 ? -28.790 -26.439 65.821  1.00 21.95 ?  154 TYR   D O   1 
ATOM   4372 C  CB  . TYR   C 1 159 ? -27.476 -25.123 63.144  1.00 25.65 ?  154 TYR   D CB  1 
ATOM   4373 C  CG  . TYR   C 1 159 ? -27.358 -24.049 64.198  1.00 24.24 ?  154 TYR   D CG  1 
ATOM   4374 C  CD1 . TYR   C 1 159 ? -26.357 -24.068 65.154  1.00 24.20 ?  154 TYR   D CD1 1 
ATOM   4375 C  CD2 . TYR   C 1 159 ? -28.250 -22.970 64.206  1.00 25.20 ?  154 TYR   D CD2 1 
ATOM   4376 C  CE1 . TYR   C 1 159 ? -26.234 -23.084 66.107  1.00 26.37 ?  154 TYR   D CE1 1 
ATOM   4377 C  CE2 . TYR   C 1 159 ? -28.135 -21.962 65.140  1.00 24.00 ?  154 TYR   D CE2 1 
ATOM   4378 C  CZ  . TYR   C 1 159 ? -27.118 -22.012 66.086  1.00 29.49 ?  154 TYR   D CZ  1 
ATOM   4379 O  OH  . TYR   C 1 159 ? -27.012 -21.059 67.044  1.00 29.47 ?  154 TYR   D OH  1 
ATOM   4380 N  N   . PHE   C 1 160 ? -30.275 -26.417 64.106  1.00 20.16 ?  155 PHE   D N   1 
ATOM   4381 C  CA  . PHE   C 1 160 ? -31.489 -26.416 64.952  1.00 18.26 ?  155 PHE   D CA  1 
ATOM   4382 C  C   . PHE   C 1 160 ? -31.440 -27.660 65.862  1.00 21.06 ?  155 PHE   D C   1 
ATOM   4383 O  O   . PHE   C 1 160 ? -31.551 -27.522 67.100  1.00 21.35 ?  155 PHE   D O   1 
ATOM   4384 C  CB  . PHE   C 1 160 ? -32.752 -26.426 64.110  1.00 17.91 ?  155 PHE   D CB  1 
ATOM   4385 C  CG  . PHE   C 1 160 ? -33.073 -25.194 63.282  1.00 17.75 ?  155 PHE   D CG  1 
ATOM   4386 C  CD1 . PHE   C 1 160 ? -32.223 -24.115 63.183  1.00 21.34 ?  155 PHE   D CD1 1 
ATOM   4387 C  CD2 . PHE   C 1 160 ? -34.272 -25.166 62.581  1.00 18.97 ?  155 PHE   D CD2 1 
ATOM   4388 C  CE1 . PHE   C 1 160 ? -32.589 -23.023 62.395  1.00 20.81 ?  155 PHE   D CE1 1 
ATOM   4389 C  CE2 . PHE   C 1 160 ? -34.642 -24.073 61.811  1.00 19.70 ?  155 PHE   D CE2 1 
ATOM   4390 C  CZ  . PHE   C 1 160 ? -33.811 -22.990 61.746  1.00 18.35 ?  155 PHE   D CZ  1 
ATOM   4391 N  N   . ARG   C 1 161 ? -31.135 -28.831 65.288  1.00 25.50 ?  156 ARG   D N   1 
ATOM   4392 C  CA  . ARG   C 1 161 ? -31.064 -30.096 66.082  1.00 25.28 ?  156 ARG   D CA  1 
ATOM   4393 C  C   . ARG   C 1 161 ? -29.984 -29.977 67.158  1.00 25.09 ?  156 ARG   D C   1 
ATOM   4394 O  O   . ARG   C 1 161 ? -30.209 -30.435 68.315  1.00 24.60 ?  156 ARG   D O   1 
ATOM   4395 C  CB  . ARG   C 1 161 ? -30.833 -31.316 65.177  1.00 28.39 ?  156 ARG   D CB  1 
ATOM   4396 C  CG  . ARG   C 1 161 ? -32.017 -31.647 64.290  1.00 33.48 ?  156 ARG   D CG  1 
ATOM   4397 C  CD  . ARG   C 1 161 ? -31.788 -32.875 63.396  1.00 40.44 ?  156 ARG   D CD  1 
ATOM   4398 N  NE  . ARG   C 1 161 ? -32.858 -32.988 62.415  1.00 44.06 ?  156 ARG   D NE  1 
ATOM   4399 C  CZ  . ARG   C 1 161 ? -32.796 -32.584 61.143  1.00 48.01 ?  156 ARG   D CZ  1 
ATOM   4400 N  NH1 . ARG   C 1 161 ? -33.867 -32.699 60.369  1.00 50.11 1  156 ARG   D NH1 1 
ATOM   4401 N  NH2 . ARG   C 1 161 ? -31.673 -32.098 60.635  1.00 48.21 ?  156 ARG   D NH2 1 
ATOM   4402 N  N   . ARG   C 1 162 ? -28.857 -29.364 66.843  1.00 22.75 ?  157 ARG   D N   1 
ATOM   4403 C  CA  . ARG   C 1 162 ? -27.751 -29.150 67.804  1.00 24.99 ?  157 ARG   D CA  1 
ATOM   4404 C  C   . ARG   C 1 162 ? -28.153 -28.314 69.022  1.00 25.13 ?  157 ARG   D C   1 
ATOM   4405 O  O   . ARG   C 1 162 ? -27.725 -28.657 70.149  1.00 23.53 ?  157 ARG   D O   1 
ATOM   4406 C  CB  . ARG   C 1 162 ? -26.528 -28.515 67.131  1.00 29.43 ?  157 ARG   D CB  1 
ATOM   4407 C  CG  . ARG   C 1 162 ? -25.290 -29.400 67.072  1.00 39.59 ?  157 ARG   D CG  1 
ATOM   4408 C  CD  . ARG   C 1 162 ? -24.589 -29.429 65.716  1.00 33.39 ?  157 ARG   D CD  1 
ATOM   4409 N  NE  . ARG   C 1 162 ? -24.241 -28.104 65.215  1.00 32.75 ?  157 ARG   D NE  1 
ATOM   4410 C  CZ  . ARG   C 1 162 ? -24.314 -27.725 63.951  1.00 29.81 ?  157 ARG   D CZ  1 
ATOM   4411 N  NH1 . ARG   C 1 162 ? -23.922 -26.511 63.626  1.00 33.44 1  157 ARG   D NH1 1 
ATOM   4412 N  NH2 . ARG   C 1 162 ? -24.760 -28.551 63.012  1.00 32.97 ?  157 ARG   D NH2 1 
ATOM   4413 N  N   . ILE   C 1 163 ? -28.948 -27.259 68.861  1.00 23.82 ?  158 ILE   D N   1 
ATOM   4414 C  CA  . ILE   C 1 163 ? -29.275 -26.380 70.018  1.00 21.55 ?  158 ILE   D CA  1 
ATOM   4415 C  C   . ILE   C 1 163 ? -30.666 -26.713 70.590  1.00 20.24 ?  158 ILE   D C   1 
ATOM   4416 O  O   . ILE   C 1 163 ? -31.000 -26.081 71.638  1.00 20.11 ?  158 ILE   D O   1 
ATOM   4417 C  CB  . ILE   C 1 163 ? -29.153 -24.906 69.587  1.00 21.52 ?  158 ILE   D CB  1 
ATOM   4418 C  CG1 . ILE   C 1 163 ? -30.186 -24.537 68.533  1.00 21.75 ?  158 ILE   D CG1 1 
ATOM   4419 C  CG2 . ILE   C 1 163 ? -27.721 -24.627 69.131  1.00 23.51 ?  158 ILE   D CG2 1 
ATOM   4420 C  CD1 . ILE   C 1 163 ? -30.339 -23.006 68.319  1.00 23.29 ?  158 ILE   D CD1 1 
ATOM   4421 N  N   . LEU   C 1 164 ? -31.346 -27.684 69.979  1.00 23.19 ?  159 LEU   D N   1 
ATOM   4422 C  CA  . LEU   C 1 164 ? -32.718 -28.126 70.320  1.00 23.10 ?  159 LEU   D CA  1 
ATOM   4423 C  C   . LEU   C 1 164 ? -32.877 -28.438 71.821  1.00 24.29 ?  159 LEU   D C   1 
ATOM   4424 O  O   . LEU   C 1 164 ? -33.965 -28.183 72.382  1.00 20.97 ?  159 LEU   D O   1 
ATOM   4425 C  CB  . LEU   C 1 164 ? -33.147 -29.312 69.456  1.00 22.46 ?  159 LEU   D CB  1 
ATOM   4426 C  CG  . LEU   C 1 164 ? -34.661 -29.558 69.412  1.00 24.37 ?  159 LEU   D CG  1 
ATOM   4427 C  CD1 . LEU   C 1 164 ? -35.386 -28.428 68.705  1.00 22.51 ?  159 LEU   D CD1 1 
ATOM   4428 C  CD2 . LEU   C 1 164 ? -35.000 -30.894 68.775  1.00 26.35 ?  159 LEU   D CD2 1 
ATOM   4429 N  N   . PRO   C 1 165 ? -31.901 -29.023 72.544  1.00 21.32 ?  160 PRO   D N   1 
ATOM   4430 C  CA  . PRO   C 1 165 ? -32.159 -29.379 73.966  1.00 20.70 ?  160 PRO   D CA  1 
ATOM   4431 C  C   . PRO   C 1 165 ? -32.596 -28.227 74.897  1.00 19.74 ?  160 PRO   D C   1 
ATOM   4432 O  O   . PRO   C 1 165 ? -33.247 -28.410 75.923  1.00 18.71 ?  160 PRO   D O   1 
ATOM   4433 C  CB  . PRO   C 1 165 ? -30.817 -29.964 74.432  1.00 19.47 ?  160 PRO   D CB  1 
ATOM   4434 C  CG  . PRO   C 1 165 ? -30.258 -30.556 73.183  1.00 21.93 ?  160 PRO   D CG  1 
ATOM   4435 C  CD  . PRO   C 1 165 ? -30.611 -29.570 72.072  1.00 21.60 ?  160 PRO   D CD  1 
ATOM   4436 N  N   . GLY   C 1 166 ? -32.194 -27.000 74.564  1.00 20.66 ?  161 GLY   D N   1 
ATOM   4437 C  CA  . GLY   C 1 166 ? -32.554 -25.832 75.377  1.00 20.33 ?  161 GLY   D CA  1 
ATOM   4438 C  C   . GLY   C 1 166 ? -33.966 -25.324 75.117  1.00 18.71 ?  161 GLY   D C   1 
ATOM   4439 O  O   . GLY   C 1 166 ? -34.432 -24.521 75.951  1.00 20.02 ?  161 GLY   D O   1 
ATOM   4440 N  N   . VAL   C 1 167 ? -34.649 -25.819 74.090  1.00 17.82 ?  162 VAL   D N   1 
ATOM   4441 C  CA  . VAL   C 1 167 ? -35.994 -25.331 73.677  1.00 19.29 ?  162 VAL   D CA  1 
ATOM   4442 C  C   . VAL   C 1 167 ? -37.043 -25.912 74.607  1.00 20.98 ?  162 VAL   D C   1 
ATOM   4443 O  O   . VAL   C 1 167 ? -37.121 -27.147 74.704  1.00 20.72 ?  162 VAL   D O   1 
ATOM   4444 C  CB  . VAL   C 1 167 ? -36.349 -25.657 72.229  1.00 19.03 ?  162 VAL   D CB  1 
ATOM   4445 C  CG1 . VAL   C 1 167 ? -37.758 -25.172 71.879  1.00 18.10 ?  162 VAL   D CG1 1 
ATOM   4446 C  CG2 . VAL   C 1 167 ? -35.275 -25.132 71.255  1.00 20.35 ?  162 VAL   D CG2 1 
ATOM   4447 N  N   . GLY   C 1 168 ? -37.823 -25.050 75.244  1.00 18.99 ?  163 GLY   D N   1 
ATOM   4448 C  CA  . GLY   C 1 168 ? -39.062 -25.461 75.928  1.00 19.71 ?  163 GLY   D CA  1 
ATOM   4449 C  C   . GLY   C 1 168 ? -40.264 -25.175 75.056  1.00 18.82 ?  163 GLY   D C   1 
ATOM   4450 O  O   . GLY   C 1 168 ? -40.744 -24.055 75.103  1.00 20.49 ?  163 GLY   D O   1 
ATOM   4451 N  N   . ALA   C 1 169 ? -40.654 -26.118 74.223  1.00 17.80 ?  164 ALA   D N   1 
ATOM   4452 C  CA  . ALA   C 1 169 ? -41.800 -25.927 73.318  1.00 18.23 ?  164 ALA   D CA  1 
ATOM   4453 C  C   . ALA   C 1 169 ? -43.049 -26.213 74.141  1.00 17.70 ?  164 ALA   D C   1 
ATOM   4454 O  O   . ALA   C 1 169 ? -43.001 -27.046 75.066  1.00 19.82 ?  164 ALA   D O   1 
ATOM   4455 C  CB  . ALA   C 1 169 ? -41.673 -26.757 72.074  1.00 18.44 ?  164 ALA   D CB  1 
ATOM   4456 N  N   . PHE   C 1 170 ? -44.156 -25.587 73.781  1.00 18.45 ?  165 PHE   D N   1 
ATOM   4457 C  CA  . PHE   C 1 170 ? -45.439 -25.758 74.495  1.00 17.44 ?  165 PHE   D CA  1 
ATOM   4458 C  C   . PHE   C 1 170 ? -46.573 -25.659 73.498  1.00 19.39 ?  165 PHE   D C   1 
ATOM   4459 O  O   . PHE   C 1 170 ? -46.436 -25.175 72.350  1.00 17.25 ?  165 PHE   D O   1 
ATOM   4460 C  CB  . PHE   C 1 170 ? -45.568 -24.763 75.650  1.00 18.52 ?  165 PHE   D CB  1 
ATOM   4461 C  CG  . PHE   C 1 170 ? -45.483 -23.304 75.274  1.00 18.56 ?  165 PHE   D CG  1 
ATOM   4462 C  CD1 . PHE   C 1 170 ? -46.607 -22.626 74.810  1.00 20.70 ?  165 PHE   D CD1 1 
ATOM   4463 C  CD2 . PHE   C 1 170 ? -44.287 -22.616 75.395  1.00 20.74 ?  165 PHE   D CD2 1 
ATOM   4464 C  CE1 . PHE   C 1 170 ? -46.512 -21.281 74.452  1.00 20.25 ?  165 PHE   D CE1 1 
ATOM   4465 C  CE2 . PHE   C 1 170 ? -44.213 -21.271 75.066  1.00 22.13 ?  165 PHE   D CE2 1 
ATOM   4466 C  CZ  . PHE   C 1 170 ? -45.323 -20.604 74.617  1.00 20.86 ?  165 PHE   D CZ  1 
ATOM   4467 N  N   . ARG   C 1 171 ? -47.728 -26.102 73.989  1.00 19.11 ?  166 ARG   D N   1 
ATOM   4468 C  CA  . ARG   C 1 171 ? -49.012 -26.059 73.269  1.00 20.38 ?  166 ARG   D CA  1 
ATOM   4469 C  C   . ARG   C 1 171 ? -49.997 -25.365 74.196  1.00 21.13 ?  166 ARG   D C   1 
ATOM   4470 O  O   . ARG   C 1 171 ? -49.971 -25.624 75.391  1.00 20.07 ?  166 ARG   D O   1 
ATOM   4471 C  CB  . ARG   C 1 171 ? -49.482 -27.461 72.878  1.00 21.98 ?  166 ARG   D CB  1 
ATOM   4472 C  CG  . ARG   C 1 171 ? -48.497 -28.207 72.004  1.00 24.18 ?  166 ARG   D CG  1 
ATOM   4473 C  CD  . ARG   C 1 171 ? -48.477 -27.582 70.634  1.00 23.54 ?  166 ARG   D CD  1 
ATOM   4474 N  NE  . ARG   C 1 171 ? -47.678 -28.346 69.704  1.00 24.41 ?  166 ARG   D NE  1 
ATOM   4475 C  CZ  . ARG   C 1 171 ? -46.402 -28.104 69.405  1.00 23.38 ?  166 ARG   D CZ  1 
ATOM   4476 N  NH1 . ARG   C 1 171 ? -45.774 -27.066 69.907  1.00 23.30 1  166 ARG   D NH1 1 
ATOM   4477 N  NH2 . ARG   C 1 171 ? -45.804 -28.864 68.503  1.00 25.98 ?  166 ARG   D NH2 1 
ATOM   4478 N  N   . LEU   C 1 172 ? -50.820 -24.483 73.654  1.00 22.62 ?  167 LEU   D N   1 
ATOM   4479 C  CA  . LEU   C 1 172 ? -51.824 -23.720 74.445  1.00 23.78 ?  167 LEU   D CA  1 
ATOM   4480 C  C   . LEU   C 1 172 ? -53.160 -23.919 73.741  1.00 24.84 ?  167 LEU   D C   1 
ATOM   4481 O  O   . LEU   C 1 172 ? -53.367 -23.338 72.654  1.00 20.95 ?  167 LEU   D O   1 
ATOM   4482 C  CB  . LEU   C 1 172 ? -51.380 -22.256 74.482  1.00 25.22 ?  167 LEU   D CB  1 
ATOM   4483 C  CG  . LEU   C 1 172 ? -52.280 -21.281 75.244  1.00 30.04 ?  167 LEU   D CG  1 
ATOM   4484 C  CD1 . LEU   C 1 172 ? -52.683 -21.830 76.594  1.00 33.46 ?  167 LEU   D CD1 1 
ATOM   4485 C  CD2 . LEU   C 1 172 ? -51.584 -19.945 75.393  1.00 30.36 ?  167 LEU   D CD2 1 
ATOM   4486 N  N   . ARG   C 1 173 ? -54.007 -24.792 74.278  1.00 26.69 ?  168 ARG   D N   1 
ATOM   4487 C  CA  . ARG   C 1 173 ? -55.375 -24.982 73.754  1.00 29.20 ?  168 ARG   D CA  1 
ATOM   4488 C  C   . ARG   C 1 173 ? -56.193 -23.782 74.224  1.00 23.09 ?  168 ARG   D C   1 
ATOM   4489 O  O   . ARG   C 1 173 ? -56.312 -23.557 75.435  1.00 26.19 ?  168 ARG   D O   1 
ATOM   4490 C  CB  . ARG   C 1 173 ? -56.006 -26.302 74.209  1.00 34.03 ?  168 ARG   D CB  1 
ATOM   4491 C  CG  . ARG   C 1 173 ? -57.455 -26.473 73.759  1.00 44.62 ?  168 ARG   D CG  1 
ATOM   4492 C  CD  . ARG   C 1 173 ? -57.709 -26.532 72.254  1.00 49.15 ?  168 ARG   D CD  1 
ATOM   4493 N  NE  . ARG   C 1 173 ? -57.792 -27.915 71.777  1.00 61.71 ?  168 ARG   D NE  1 
ATOM   4494 C  CZ  . ARG   C 1 173 ? -57.612 -28.331 70.513  1.00 66.34 ?  168 ARG   D CZ  1 
ATOM   4495 N  NH1 . ARG   C 1 173 ? -57.320 -27.485 69.529  1.00 59.38 1  168 ARG   D NH1 1 
ATOM   4496 N  NH2 . ARG   C 1 173 ? -57.710 -29.624 70.244  1.00 71.57 ?  168 ARG   D NH2 1 
ATOM   4497 N  N   . VAL   C 1 174 ? -56.693 -22.997 73.282  1.00 24.21 ?  169 VAL   D N   1 
ATOM   4498 C  CA  . VAL   C 1 174 ? -57.409 -21.741 73.600  1.00 22.07 ?  169 VAL   D CA  1 
ATOM   4499 C  C   . VAL   C 1 174 ? -58.829 -22.077 74.082  1.00 21.32 ?  169 VAL   D C   1 
ATOM   4500 O  O   . VAL   C 1 174 ? -59.562 -22.614 73.288  1.00 22.11 ?  169 VAL   D O   1 
ATOM   4501 C  CB  . VAL   C 1 174 ? -57.397 -20.786 72.403  1.00 19.83 ?  169 VAL   D CB  1 
ATOM   4502 C  CG1 . VAL   C 1 174 ? -58.147 -19.491 72.675  1.00 22.24 ?  169 VAL   D CG1 1 
ATOM   4503 C  CG2 . VAL   C 1 174 ? -55.943 -20.505 71.979  1.00 21.28 ?  169 VAL   D CG2 1 
ATOM   4504 N  N   . ALA   C 1 175 ? -59.100 -21.808 75.361  1.00 22.77 ?  170 ALA   D N   1 
ATOM   4505 C  CA  . ALA   C 1 175 ? -60.426 -21.952 76.006  1.00 23.44 ?  170 ALA   D CA  1 
ATOM   4506 C  C   . ALA   C 1 175 ? -61.192 -20.635 75.890  1.00 23.20 ?  170 ALA   D C   1 
ATOM   4507 O  O   . ALA   C 1 175 ? -62.421 -20.661 75.778  1.00 24.25 ?  170 ALA   D O   1 
ATOM   4508 C  CB  . ALA   C 1 175 ? -60.230 -22.343 77.437  1.00 24.04 ?  170 ALA   D CB  1 
ATOM   4509 N  N   . GLU   C 1 176 ? -60.502 -19.500 75.975  1.00 23.91 ?  171 GLU   D N   1 
ATOM   4510 C  CA  . GLU   C 1 176 ? -61.143 -18.158 75.913  1.00 26.11 ?  171 GLU   D CA  1 
ATOM   4511 C  C   . GLU   C 1 176 ? -60.254 -17.248 75.089  1.00 22.20 ?  171 GLU   D C   1 
ATOM   4512 O  O   . GLU   C 1 176 ? -59.029 -17.390 75.194  1.00 21.99 ?  171 GLU   D O   1 
ATOM   4513 C  CB  . GLU   C 1 176 ? -61.334 -17.515 77.291  1.00 30.99 ?  171 GLU   D CB  1 
ATOM   4514 C  CG  . GLU   C 1 176 ? -61.871 -18.422 78.379  1.00 39.60 ?  171 GLU   D CG  1 
ATOM   4515 C  CD  . GLU   C 1 176 ? -61.964 -17.686 79.713  1.00 51.69 ?  171 GLU   D CD  1 
ATOM   4516 O  OE1 . GLU   C 1 176 ? -62.813 -16.773 79.804  1.00 59.40 ?  171 GLU   D OE1 1 
ATOM   4517 O  OE2 . GLU   C 1 176 ? -61.149 -17.984 80.647  1.00 60.59 -1 171 GLU   D OE2 1 
ATOM   4518 N  N   . ALA   C 1 177 ? -60.858 -16.350 74.328  1.00 22.69 ?  172 ALA   D N   1 
ATOM   4519 C  CA  . ALA   C 1 177 ? -60.132 -15.364 73.495  1.00 21.85 ?  172 ALA   D CA  1 
ATOM   4520 C  C   . ALA   C 1 177 ? -60.878 -14.056 73.589  1.00 23.66 ?  172 ALA   D C   1 
ATOM   4521 O  O   . ALA   C 1 177 ? -62.096 -14.043 73.310  1.00 25.01 ?  172 ALA   D O   1 
ATOM   4522 C  CB  . ALA   C 1 177 ? -60.036 -15.808 72.066  1.00 21.75 ?  172 ALA   D CB  1 
ATOM   4523 N  N   . ASP   C 1 178 ? -60.196 -13.026 74.062  1.00 22.37 ?  173 ASP   D N   1 
ATOM   4524 C  CA  . ASP   C 1 178 ? -60.777 -11.675 74.213  1.00 23.69 ?  173 ASP   D CA  1 
ATOM   4525 C  C   . ASP   C 1 178 ? -59.943 -10.722 73.373  1.00 20.80 ?  173 ASP   D C   1 
ATOM   4526 O  O   . ASP   C 1 178 ? -58.733 -10.862 73.369  1.00 20.91 ?  173 ASP   D O   1 
ATOM   4527 C  CB  . ASP   C 1 178 ? -60.830 -11.312 75.701  1.00 26.20 ?  173 ASP   D CB  1 
ATOM   4528 C  CG  . ASP   C 1 178 ? -61.862 -12.120 76.487  1.00 32.35 ?  173 ASP   D CG  1 
ATOM   4529 O  OD1 . ASP   C 1 178 ? -61.452 -12.940 77.398  1.00 30.91 ?  173 ASP   D OD1 1 
ATOM   4530 O  OD2 . ASP   C 1 178 ? -63.092 -11.950 76.173  1.00 37.14 -1 173 ASP   D OD2 1 
ATOM   4531 N  N   . GLY   C 1 179 ? -60.587 -9.738  72.757  1.00 21.41 ?  174 GLY   D N   1 
ATOM   4532 C  CA  . GLY   C 1 179 ? -59.933 -8.764  71.879  1.00 22.26 ?  174 GLY   D CA  1 
ATOM   4533 C  C   . GLY   C 1 179 ? -60.367 -7.360  72.221  1.00 24.03 ?  174 GLY   D C   1 
ATOM   4534 O  O   . GLY   C 1 179 ? -61.572 -7.080  72.149  1.00 23.96 ?  174 GLY   D O   1 
ATOM   4535 N  N   . MET   C 1 180 ? -59.406 -6.527  72.600  1.00 20.73 ?  175 MET   D N   1 
ATOM   4536 C  CA  . MET   C 1 180 ? -59.598 -5.075  72.783  1.00 21.75 ?  175 MET   D CA  1 
ATOM   4537 C  C   . MET   C 1 180 ? -59.191 -4.337  71.518  1.00 19.68 ?  175 MET   D C   1 
ATOM   4538 O  O   . MET   C 1 180 ? -57.985 -4.360  71.156  1.00 20.55 ?  175 MET   D O   1 
ATOM   4539 C  CB  . MET   C 1 180 ? -58.776 -4.584  73.968  1.00 22.95 ?  175 MET   D CB  1 
ATOM   4540 C  CG  . MET   C 1 180 ? -58.884 -3.110  74.210  1.00 23.91 ?  175 MET   D CG  1 
ATOM   4541 S  SD  . MET   C 1 180 ? -60.341 -2.522  75.116  1.00 25.54 ?  175 MET   D SD  1 
ATOM   4542 C  CE  . MET   C 1 180 ? -59.924 -3.176  76.726  1.00 26.16 ?  175 MET   D CE  1 
ATOM   4543 N  N   . PHE   C 1 181 ? -60.167 -3.766  70.823  1.00 19.07 ?  176 PHE   D N   1 
ATOM   4544 C  CA  . PHE   C 1 181 ? -59.906 -2.902  69.646  1.00 17.95 ?  176 PHE   D CA  1 
ATOM   4545 C  C   . PHE   C 1 181 ? -60.326 -1.485  70.027  1.00 18.93 ?  176 PHE   D C   1 
ATOM   4546 O  O   . PHE   C 1 181 ? -61.409 -1.066  69.662  1.00 19.34 ?  176 PHE   D O   1 
ATOM   4547 C  CB  . PHE   C 1 181 ? -60.499 -3.481  68.353  1.00 19.22 ?  176 PHE   D CB  1 
ATOM   4548 C  CG  . PHE   C 1 181 ? -59.845 -4.780  67.948  1.00 18.81 ?  176 PHE   D CG  1 
ATOM   4549 C  CD1 . PHE   C 1 181 ? -60.162 -5.969  68.600  1.00 21.55 ?  176 PHE   D CD1 1 
ATOM   4550 C  CD2 . PHE   C 1 181 ? -58.770 -4.779  67.051  1.00 19.63 ?  176 PHE   D CD2 1 
ATOM   4551 C  CE1 . PHE   C 1 181 ? -59.525 -7.165  68.275  1.00 22.28 ?  176 PHE   D CE1 1 
ATOM   4552 C  CE2 . PHE   C 1 181 ? -58.169 -5.978  66.713  1.00 21.17 ?  176 PHE   D CE2 1 
ATOM   4553 C  CZ  . PHE   C 1 181 ? -58.531 -7.154  67.335  1.00 19.93 ?  176 PHE   D CZ  1 
ATOM   4554 N  N   . LYS   C 1 182 ? -59.454 -0.795  70.745  1.00 17.79 ?  177 LYS   D N   1 
ATOM   4555 C  CA  . LYS   C 1 182 ? -59.757 0.535   71.320  1.00 18.90 ?  177 LYS   D CA  1 
ATOM   4556 C  C   . LYS   C 1 182 ? -59.381 1.566   70.261  1.00 18.27 ?  177 LYS   D C   1 
ATOM   4557 O  O   . LYS   C 1 182 ? -58.185 1.910   70.169  1.00 19.45 ?  177 LYS   D O   1 
ATOM   4558 C  CB  . LYS   C 1 182 ? -59.090 0.718   72.670  1.00 18.72 ?  177 LYS   D CB  1 
ATOM   4559 C  CG  . LYS   C 1 182 ? -59.433 2.060   73.280  1.00 22.19 ?  177 LYS   D CG  1 
ATOM   4560 C  CD  . LYS   C 1 182 ? -59.062 2.212   74.717  1.00 25.98 ?  177 LYS   D CD  1 
ATOM   4561 C  CE  . LYS   C 1 182 ? -59.062 3.668   75.128  1.00 29.33 ?  177 LYS   D CE  1 
ATOM   4562 N  NZ  . LYS   C 1 182 ? -60.380 4.305   74.925  1.00 31.31 1  177 LYS   D NZ  1 
ATOM   4563 N  N   . LEU   C 1 183 ? -60.367 1.959   69.441  1.00 17.72 ?  178 LEU   D N   1 
ATOM   4564 C  CA  . LEU   C 1 183 ? -60.126 2.684   68.178  1.00 18.41 ?  178 LEU   D CA  1 
ATOM   4565 C  C   . LEU   C 1 183 ? -61.150 3.825   68.038  1.00 19.06 ?  178 LEU   D C   1 
ATOM   4566 O  O   . LEU   C 1 183 ? -61.533 4.137   66.908  1.00 21.30 ?  178 LEU   D O   1 
ATOM   4567 C  CB  . LEU   C 1 183 ? -60.138 1.704   66.991  1.00 18.98 ?  178 LEU   D CB  1 
ATOM   4568 C  CG  . LEU   C 1 183 ? -59.089 0.578   66.949  1.00 19.70 ?  178 LEU   D CG  1 
ATOM   4569 C  CD1 . LEU   C 1 183 ? -59.419 -0.381  65.818  1.00 19.93 ?  178 LEU   D CD1 1 
ATOM   4570 C  CD2 . LEU   C 1 183 ? -57.666 1.099   66.821  1.00 20.03 ?  178 LEU   D CD2 1 
ATOM   4571 N  N   . SER   C 1 184 ? -61.459 4.518   69.127  1.00 18.67 ?  179 SER   D N   1 
ATOM   4572 C  CA  . SER   C 1 184 ? -62.262 5.775   69.123  1.00 20.01 ?  179 SER   D CA  1 
ATOM   4573 C  C   . SER   C 1 184 ? -63.737 5.495   68.735  1.00 20.31 ?  179 SER   D C   1 
ATOM   4574 O  O   . SER   C 1 184 ? -64.484 6.471   68.446  1.00 21.46 ?  179 SER   D O   1 
ATOM   4575 C  CB  . SER   C 1 184 ? -61.679 6.840   68.215  1.00 20.41 ?  179 SER   D CB  1 
ATOM   4576 O  OG  . SER   C 1 184 ? -60.365 7.274   68.624  1.00 21.28 ?  179 SER   D OG  1 
ATOM   4577 N  N   . GLN   C 1 185 ? -64.187 4.256   68.825  1.00 19.69 ?  180 GLN   D N   1 
ATOM   4578 C  CA  . GLN   C 1 185 ? -65.612 3.886   68.546  1.00 22.11 ?  180 GLN   D CA  1 
ATOM   4579 C  C   . GLN   C 1 185 ? -66.588 4.648   69.448  1.00 22.66 ?  180 GLN   D C   1 
ATOM   4580 O  O   . GLN   C 1 185 ? -67.752 4.802   68.990  1.00 26.17 ?  180 GLN   D O   1 
ATOM   4581 C  CB  . GLN   C 1 185 ? -65.851 2.378   68.651  1.00 22.54 ?  180 GLN   D CB  1 
ATOM   4582 C  CG  . GLN   C 1 185 ? -65.076 1.547   67.634  1.00 22.89 ?  180 GLN   D CG  1 
ATOM   4583 C  CD  . GLN   C 1 185 ? -63.801 0.991   68.236  1.00 22.62 ?  180 GLN   D CD  1 
ATOM   4584 O  OE1 . GLN   C 1 185 ? -63.071 1.723   68.913  1.00 21.41 ?  180 GLN   D OE1 1 
ATOM   4585 N  NE2 . GLN   C 1 185 ? -63.523 -0.294  67.991  1.00 20.96 ?  180 GLN   D NE2 1 
ATOM   4586 N  N   . GLU   C 1 186 ? -66.172 5.076   70.641  1.00 22.21 ?  181 GLU   D N   1 
ATOM   4587 C  CA  . GLU   C 1 186 ? -66.945 5.855   71.652  1.00 25.44 ?  181 GLU   D CA  1 
ATOM   4588 C  C   . GLU   C 1 186 ? -67.183 7.285   71.154  1.00 27.36 ?  181 GLU   D C   1 
ATOM   4589 O  O   . GLU   C 1 186 ? -68.173 7.923   71.625  1.00 28.81 ?  181 GLU   D O   1 
ATOM   4590 C  CB  . GLU   C 1 186 ? -66.276 5.804   73.036  1.00 26.88 ?  181 GLU   D CB  1 
ATOM   4591 C  CG  . GLU   C 1 186 ? -65.154 6.839   73.323  1.00 29.28 ?  181 GLU   D CG  1 
ATOM   4592 C  CD  . GLU   C 1 186 ? -63.796 6.650   72.650  1.00 36.62 ?  181 GLU   D CD  1 
ATOM   4593 O  OE1 . GLU   C 1 186 ? -63.627 5.622   71.959  1.00 30.17 ?  181 GLU   D OE1 1 
ATOM   4594 O  OE2 . GLU   C 1 186 ? -62.913 7.565   72.768  1.00 34.96 -1 181 GLU   D OE2 1 
ATOM   4595 N  N   . GLN   C 1 187 ? -66.361 7.797   70.229  1.00 24.64 ?  182 GLN   D N   1 
ATOM   4596 C  CA  . GLN   C 1 187 ? -66.539 9.192   69.758  1.00 23.75 ?  182 GLN   D CA  1 
ATOM   4597 C  C   . GLN   C 1 187 ? -67.636 9.270   68.680  1.00 22.18 ?  182 GLN   D C   1 
ATOM   4598 O  O   . GLN   C 1 187 ? -67.980 8.241   68.046  1.00 22.88 ?  182 GLN   D O   1 
ATOM   4599 C  CB  . GLN   C 1 187 ? -65.207 9.762   69.278  1.00 23.41 ?  182 GLN   D CB  1 
ATOM   4600 C  CG  . GLN   C 1 187 ? -64.143 9.743   70.370  1.00 22.95 ?  182 GLN   D CG  1 
ATOM   4601 C  CD  . GLN   C 1 187 ? -64.449 10.710  71.492  1.00 25.60 ?  182 GLN   D CD  1 
ATOM   4602 O  OE1 . GLN   C 1 187 ? -64.825 11.877  71.283  1.00 26.83 ?  182 GLN   D OE1 1 
ATOM   4603 N  NE2 . GLN   C 1 187 ? -64.275 10.233  72.701  1.00 25.04 ?  182 GLN   D NE2 1 
ATOM   4604 N  N   . GLN   C 1 188 ? -68.145 10.481  68.467  1.00 22.98 ?  183 GLN   D N   1 
ATOM   4605 C  CA  . GLN   C 1 188 ? -69.081 10.783  67.366  1.00 25.58 ?  183 GLN   D CA  1 
ATOM   4606 C  C   . GLN   C 1 188 ? -68.330 10.588  66.042  1.00 27.36 ?  183 GLN   D C   1 
ATOM   4607 O  O   . GLN   C 1 188 ? -67.108 10.741  65.965  1.00 24.20 ?  183 GLN   D O   1 
ATOM   4608 C  CB  . GLN   C 1 188 ? -69.655 12.191  67.525  1.00 28.01 ?  183 GLN   D CB  1 
ATOM   4609 C  CG  . GLN   C 1 188 ? -70.459 12.419  68.804  1.00 29.44 ?  183 GLN   D CG  1 
ATOM   4610 C  CD  . GLN   C 1 188 ? -71.621 11.460  68.904  1.00 31.61 ?  183 GLN   D CD  1 
ATOM   4611 O  OE1 . GLN   C 1 188 ? -72.250 11.110  67.914  1.00 32.37 ?  183 GLN   D OE1 1 
ATOM   4612 N  NE2 . GLN   C 1 188 ? -71.916 10.998  70.108  1.00 33.49 ?  183 GLN   D NE2 1 
ATOM   4613 N  N   . PRO   C 1 189 ? -69.046 10.231  64.961  1.00 29.87 ?  184 PRO   D N   1 
ATOM   4614 C  CA  . PRO   C 1 189 ? -68.447 10.039  63.631  1.00 29.68 ?  184 PRO   D CA  1 
ATOM   4615 C  C   . PRO   C 1 189 ? -67.475 11.130  63.158  1.00 28.94 ?  184 PRO   D C   1 
ATOM   4616 O  O   . PRO   C 1 189 ? -66.418 10.771  62.671  1.00 28.11 ?  184 PRO   D O   1 
ATOM   4617 C  CB  . PRO   C 1 189 ? -69.687 10.034  62.725  1.00 32.88 ?  184 PRO   D CB  1 
ATOM   4618 C  CG  . PRO   C 1 189 ? -70.755 9.394   63.588  1.00 30.95 ?  184 PRO   D CG  1 
ATOM   4619 C  CD  . PRO   C 1 189 ? -70.501 9.967   64.965  1.00 31.78 ?  184 PRO   D CD  1 
ATOM   4620 N  N   . ALA   C 1 190 ? -67.833 12.412  63.306  1.00 29.48 ?  185 ALA   D N   1 
ATOM   4621 C  CA  . ALA   C 1 190 ? -66.989 13.545  62.874  1.00 30.62 ?  185 ALA   D CA  1 
ATOM   4622 C  C   . ALA   C 1 190 ? -65.680 13.498  63.661  1.00 29.45 ?  185 ALA   D C   1 
ATOM   4623 O  O   . ALA   C 1 190 ? -64.643 13.838  63.087  1.00 28.31 ?  185 ALA   D O   1 
ATOM   4624 C  CB  . ALA   C 1 190 ? -67.689 14.856  63.082  1.00 33.15 ?  185 ALA   D CB  1 
ATOM   4625 N  N   . ILE   C 1 191 ? -65.727 13.107  64.943  1.00 28.25 ?  186 ILE   D N   1 
ATOM   4626 C  CA  . ILE   C 1 191 ? -64.492 13.066  65.783  1.00 27.24 ?  186 ILE   D CA  1 
ATOM   4627 C  C   . ILE   C 1 191 ? -63.647 11.883  65.321  1.00 24.57 ?  186 ILE   D C   1 
ATOM   4628 O  O   . ILE   C 1 191 ? -62.419 12.043  65.180  1.00 22.20 ?  186 ILE   D O   1 
ATOM   4629 C  CB  . ILE   C 1 191 ? -64.778 13.006  67.296  1.00 28.08 ?  186 ILE   D CB  1 
ATOM   4630 C  CG1 . ILE   C 1 191 ? -65.638 14.185  67.764  1.00 34.00 ?  186 ILE   D CG1 1 
ATOM   4631 C  CG2 . ILE   C 1 191 ? -63.474 12.894  68.074  1.00 27.36 ?  186 ILE   D CG2 1 
ATOM   4632 C  CD1 . ILE   C 1 191 ? -65.099 15.519  67.388  1.00 37.53 ?  186 ILE   D CD1 1 
ATOM   4633 N  N   . ARG   C 1 192 ? -64.263 10.725  65.135  1.00 24.50 ?  187 ARG   D N   1 
ATOM   4634 C  CA  . ARG   C 1 192 ? -63.563 9.507   64.649  1.00 25.74 ?  187 ARG   D CA  1 
ATOM   4635 C  C   . ARG   C 1 192 ? -62.842 9.831   63.338  1.00 24.13 ?  187 ARG   D C   1 
ATOM   4636 O  O   . ARG   C 1 192 ? -61.669 9.409   63.204  1.00 22.82 ?  187 ARG   D O   1 
ATOM   4637 C  CB  . ARG   C 1 192 ? -64.509 8.331   64.408  1.00 26.20 ?  187 ARG   D CB  1 
ATOM   4638 C  CG  . ARG   C 1 192 ? -65.177 7.795   65.657  1.00 28.46 ?  187 ARG   D CG  1 
ATOM   4639 C  CD  . ARG   C 1 192 ? -65.844 6.466   65.356  1.00 34.79 ?  187 ARG   D CD  1 
ATOM   4640 N  NE  . ARG   C 1 192 ? -67.179 6.532   65.894  1.00 42.53 ?  187 ARG   D NE  1 
ATOM   4641 C  CZ  . ARG   C 1 192 ? -68.314 6.443   65.196  1.00 49.97 ?  187 ARG   D CZ  1 
ATOM   4642 N  NH1 . ARG   C 1 192 ? -68.311 6.201   63.893  1.00 51.96 1  187 ARG   D NH1 1 
ATOM   4643 N  NH2 . ARG   C 1 192 ? -69.465 6.555   65.835  1.00 46.84 ?  187 ARG   D NH2 1 
ATOM   4644 N  N   . ARG   C 1 193 ? -63.457 10.621  62.458  1.00 25.46 ?  188 ARG   D N   1 
ATOM   4645 C  CA  . ARG   C 1 193 ? -62.827 10.950  61.153  1.00 26.48 ?  188 ARG   D CA  1 
ATOM   4646 C  C   . ARG   C 1 193 ? -61.640 11.879  61.393  1.00 24.22 ?  188 ARG   D C   1 
ATOM   4647 O  O   . ARG   C 1 193 ? -60.569 11.631  60.773  1.00 23.14 ?  188 ARG   D O   1 
ATOM   4648 C  CB  . ARG   C 1 193 ? -63.816 11.582  60.184  1.00 32.18 ?  188 ARG   D CB  1 
ATOM   4649 C  CG  . ARG   C 1 193 ? -64.998 10.677  59.865  1.00 40.76 ?  188 ARG   D CG  1 
ATOM   4650 C  CD  . ARG   C 1 193 ? -65.734 11.142  58.619  1.00 45.96 ?  188 ARG   D CD  1 
ATOM   4651 N  NE  . ARG   C 1 193 ? -66.588 12.287  58.901  1.00 48.70 ?  188 ARG   D NE  1 
ATOM   4652 C  CZ  . ARG   C 1 193 ? -67.834 12.221  59.364  1.00 48.66 ?  188 ARG   D CZ  1 
ATOM   4653 N  NH1 . ARG   C 1 193 ? -68.508 13.334  59.580  1.00 53.46 1  188 ARG   D NH1 1 
ATOM   4654 N  NH2 . ARG   C 1 193 ? -68.396 11.055  59.627  1.00 49.88 ?  188 ARG   D NH2 1 
ATOM   4655 N  N   . ARG   C 1 194 ? -61.736 12.795  62.369  1.00 21.23 ?  189 ARG   D N   1 
ATOM   4656 C  CA  . ARG   C 1 194 ? -60.589 13.690  62.672  1.00 21.31 ?  189 ARG   D CA  1 
ATOM   4657 C  C   . ARG   C 1 194 ? -59.438 12.882  63.253  1.00 21.39 ?  189 ARG   D C   1 
ATOM   4658 O  O   . ARG   C 1 194 ? -58.306 13.112  62.839  1.00 21.14 ?  189 ARG   D O   1 
ATOM   4659 C  CB  . ARG   C 1 194 ? -60.988 14.803  63.639  1.00 25.92 ?  189 ARG   D CB  1 
ATOM   4660 C  CG  . ARG   C 1 194 ? -61.962 15.802  63.035  1.00 27.39 ?  189 ARG   D CG  1 
ATOM   4661 C  CD  . ARG   C 1 194 ? -62.525 16.704  64.117  1.00 30.38 ?  189 ARG   D CD  1 
ATOM   4662 N  NE  . ARG   C 1 194 ? -63.624 17.469  63.546  1.00 38.02 ?  189 ARG   D NE  1 
ATOM   4663 C  CZ  . ARG   C 1 194 ? -64.540 18.168  64.217  1.00 42.62 ?  189 ARG   D CZ  1 
ATOM   4664 N  NH1 . ARG   C 1 194 ? -64.550 18.212  65.541  1.00 39.33 1  189 ARG   D NH1 1 
ATOM   4665 N  NH2 . ARG   C 1 194 ? -65.476 18.813  63.538  1.00 43.65 ?  189 ARG   D NH2 1 
ATOM   4666 N  N   . VAL   C 1 195 ? -59.722 11.942  64.149  1.00 21.64 ?  190 VAL   D N   1 
ATOM   4667 C  CA  . VAL   C 1 195 ? -58.662 11.051  64.686  1.00 22.46 ?  190 VAL   D CA  1 
ATOM   4668 C  C   . VAL   C 1 195 ? -57.983 10.284  63.543  1.00 20.76 ?  190 VAL   D C   1 
ATOM   4669 O  O   . VAL   C 1 195 ? -56.732 10.280  63.447  1.00 21.73 ?  190 VAL   D O   1 
ATOM   4670 C  CB  . VAL   C 1 195 ? -59.191 10.118  65.778  1.00 21.29 ?  190 VAL   D CB  1 
ATOM   4671 C  CG1 . VAL   C 1 195 ? -58.095 9.176   66.235  1.00 21.21 ?  190 VAL   D CG1 1 
ATOM   4672 C  CG2 . VAL   C 1 195 ? -59.727 10.919  66.945  1.00 22.78 ?  190 VAL   D CG2 1 
ATOM   4673 N  N   . ARG   C 1 196 ? -58.766 9.574   62.759  1.00 23.55 ?  191 ARG   D N   1 
ATOM   4674 C  CA  . ARG   C 1 196 ? -58.242 8.763   61.626  1.00 28.80 ?  191 ARG   D CA  1 
ATOM   4675 C  C   . ARG   C 1 196 ? -57.339 9.632   60.744  1.00 26.92 ?  191 ARG   D C   1 
ATOM   4676 O  O   . ARG   C 1 196 ? -56.236 9.161   60.378  1.00 27.49 ?  191 ARG   D O   1 
ATOM   4677 C  CB  . ARG   C 1 196 ? -59.395 8.220   60.785  1.00 33.51 ?  191 ARG   D CB  1 
ATOM   4678 C  CG  . ARG   C 1 196 ? -58.953 7.297   59.658  1.00 42.58 ?  191 ARG   D CG  1 
ATOM   4679 C  CD  . ARG   C 1 196 ? -60.123 6.414   59.275  1.00 54.09 ?  191 ARG   D CD  1 
ATOM   4680 N  NE  . ARG   C 1 196 ? -61.301 7.136   58.778  1.00 60.98 ?  191 ARG   D NE  1 
ATOM   4681 C  CZ  . ARG   C 1 196 ? -62.441 7.335   59.449  1.00 66.95 ?  191 ARG   D CZ  1 
ATOM   4682 N  NH1 . ARG   C 1 196 ? -62.612 6.880   60.685  1.00 68.82 1  191 ARG   D NH1 1 
ATOM   4683 N  NH2 . ARG   C 1 196 ? -63.425 7.996   58.864  1.00 66.20 ?  191 ARG   D NH2 1 
ATOM   4684 N  N   . HIS   C 1 197 ? -57.775 10.847  60.420  1.00 26.03 ?  192 HIS   D N   1 
ATOM   4685 C  CA  . HIS   C 1 197 ? -57.053 11.752  59.480  1.00 25.00 ?  192 HIS   D CA  1 
ATOM   4686 C  C   . HIS   C 1 197 ? -55.754 12.145  60.149  1.00 27.26 ?  192 HIS   D C   1 
ATOM   4687 O  O   . HIS   C 1 197 ? -54.705 12.105  59.469  1.00 31.86 ?  192 HIS   D O   1 
ATOM   4688 C  CB  . HIS   C 1 197 ? -57.884 12.958  59.092  1.00 29.64 ?  192 HIS   D CB  1 
ATOM   4689 C  CG  . HIS   C 1 197 ? -57.112 14.005  58.368  1.00 31.55 ?  192 HIS   D CG  1 
ATOM   4690 N  ND1 . HIS   C 1 197 ? -56.537 13.765  57.131  1.00 34.68 ?  192 HIS   D ND1 1 
ATOM   4691 C  CD2 . HIS   C 1 197 ? -56.834 15.285  58.684  1.00 34.19 ?  192 HIS   D CD2 1 
ATOM   4692 C  CE1 . HIS   C 1 197 ? -55.929 14.859  56.720  1.00 34.15 ?  192 HIS   D CE1 1 
ATOM   4693 N  NE2 . HIS   C 1 197 ? -56.115 15.816  57.639  1.00 34.96 ?  192 HIS   D NE2 1 
ATOM   4694 N  N   . SER   C 1 198 ? -55.790 12.407  61.452  1.00 25.43 ?  193 SER   D N   1 
ATOM   4695 C  CA  . SER   C 1 198 ? -54.591 12.782  62.238  1.00 26.41 ?  193 SER   D CA  1 
ATOM   4696 C  C   . SER   C 1 198 ? -53.533 11.698  62.178  1.00 23.73 ?  193 SER   D C   1 
ATOM   4697 O  O   . SER   C 1 198 ? -52.369 12.055  62.178  1.00 29.72 ?  193 SER   D O   1 
ATOM   4698 C  CB  . SER   C 1 198 ? -54.927 13.071  63.665  1.00 29.29 ?  193 SER   D CB  1 
ATOM   4699 O  OG  . SER   C 1 198 ? -53.808 13.665  64.282  1.00 38.29 ?  193 SER   D OG  1 
ATOM   4700 N  N   . PHE   C 1 199 ? -53.926 10.442  62.258  1.00 22.19 ?  194 PHE   D N   1 
ATOM   4701 C  CA  . PHE   C 1 199 ? -53.026 9.264   62.327  1.00 20.78 ?  194 PHE   D CA  1 
ATOM   4702 C  C   . PHE   C 1 199 ? -52.491 8.897   60.940  1.00 23.32 ?  194 PHE   D C   1 
ATOM   4703 O  O   . PHE   C 1 199 ? -51.490 8.173   60.865  1.00 22.46 ?  194 PHE   D O   1 
ATOM   4704 C  CB  . PHE   C 1 199 ? -53.733 8.078   62.972  1.00 20.79 ?  194 PHE   D CB  1 
ATOM   4705 C  CG  . PHE   C 1 199 ? -53.895 8.183   64.477  1.00 19.75 ?  194 PHE   D CG  1 
ATOM   4706 C  CD1 . PHE   C 1 199 ? -53.115 9.053   65.236  1.00 21.46 ?  194 PHE   D CD1 1 
ATOM   4707 C  CD2 . PHE   C 1 199 ? -54.798 7.373   65.149  1.00 21.34 ?  194 PHE   D CD2 1 
ATOM   4708 C  CE1 . PHE   C 1 199 ? -53.241 9.120   66.626  1.00 21.56 ?  194 PHE   D CE1 1 
ATOM   4709 C  CE2 . PHE   C 1 199 ? -54.922 7.445   66.532  1.00 20.69 ?  194 PHE   D CE2 1 
ATOM   4710 C  CZ  . PHE   C 1 199 ? -54.145 8.318   67.276  1.00 21.07 ?  194 PHE   D CZ  1 
ATOM   4711 N  N   . GLY   C 1 200 ? -53.171 9.310   59.879  1.00 26.08 ?  195 GLY   D N   1 
ATOM   4712 C  CA  . GLY   C 1 200 ? -52.755 8.951   58.500  1.00 29.18 ?  195 GLY   D CA  1 
ATOM   4713 C  C   . GLY   C 1 200 ? -51.468 9.642   58.074  1.00 32.56 ?  195 GLY   D C   1 
ATOM   4714 O  O   . GLY   C 1 200 ? -50.822 9.159   57.096  1.00 37.38 ?  195 GLY   D O   1 
ATOM   4715 N  N   . GLY   C 1 201 ? -51.084 10.719  58.758  1.00 35.75 ?  196 GLY   D N   1 
ATOM   4716 C  CA  . GLY   C 1 201 ? -49.978 11.599  58.340  1.00 41.49 ?  196 GLY   D CA  1 
ATOM   4717 C  C   . GLY   C 1 201 ? -48.604 11.142  58.808  1.00 45.68 ?  196 GLY   D C   1 
ATOM   4718 O  O   . GLY   C 1 201 ? -47.664 11.932  58.596  1.00 52.91 ?  196 GLY   D O   1 
ATOM   4719 N  N   . ALA   C 1 202 ? -48.449 9.969   59.441  1.00 41.60 ?  197 ALA   D N   1 
ATOM   4720 C  CA  . ALA   C 1 202 ? -47.151 9.571   60.049  1.00 39.18 ?  197 ALA   D CA  1 
ATOM   4721 C  C   . ALA   C 1 202 ? -46.991 8.052   60.164  1.00 37.75 ?  197 ALA   D C   1 
ATOM   4722 O  O   . ALA   C 1 202 ? -47.957 7.344   60.502  1.00 39.62 ?  197 ALA   D O   1 
ATOM   4723 C  CB  . ALA   C 1 202 ? -46.980 10.249  61.389  1.00 39.36 ?  197 ALA   D CB  1 
ATOM   4724 N  N   . GLU   C 1 203 ? -45.782 7.552   59.905  1.00 37.26 ?  198 GLU   D N   1 
ATOM   4725 C  CA  . GLU   C 1 203 ? -45.466 6.110   59.973  1.00 34.58 ?  198 GLU   D CA  1 
ATOM   4726 C  C   . GLU   C 1 203 ? -45.867 5.535   61.332  1.00 32.77 ?  198 GLU   D C   1 
ATOM   4727 O  O   . GLU   C 1 203 ? -46.421 4.439   61.339  1.00 35.57 ?  198 GLU   D O   1 
ATOM   4728 C  CB  . GLU   C 1 203 ? -43.982 5.852   59.707  1.00 40.93 ?  198 GLU   D CB  1 
ATOM   4729 C  CG  . GLU   C 1 203 ? -43.624 4.380   59.729  1.00 44.63 ?  198 GLU   D CG  1 
ATOM   4730 C  CD  . GLU   C 1 203 ? -43.404 3.722   61.091  1.00 48.88 ?  198 GLU   D CD  1 
ATOM   4731 O  OE1 . GLU   C 1 203 ? -43.147 4.458   62.100  1.00 58.30 ?  198 GLU   D OE1 1 
ATOM   4732 O  OE2 . GLU   C 1 203 ? -43.512 2.465   61.158  1.00 44.37 -1 198 GLU   D OE2 1 
ATOM   4733 N  N   . ALA   C 1 204 ? -45.598 6.248   62.435  1.00 30.73 ?  199 ALA   D N   1 
ATOM   4734 C  CA  . ALA   C 1 204 ? -45.818 5.766   63.818  1.00 30.26 ?  199 ALA   D CA  1 
ATOM   4735 C  C   . ALA   C 1 204 ? -47.286 5.369   64.032  1.00 27.04 ?  199 ALA   D C   1 
ATOM   4736 O  O   . ALA   C 1 204 ? -47.566 4.557   64.933  1.00 27.09 ?  199 ALA   D O   1 
ATOM   4737 C  CB  . ALA   C 1 204 ? -45.408 6.837   64.798  1.00 30.84 ?  199 ALA   D CB  1 
ATOM   4738 N  N   . THR   C 1 205 ? -48.198 5.969   63.279  1.00 25.25 ?  200 THR   D N   1 
ATOM   4739 C  CA  . THR   C 1 205 ? -49.668 5.885   63.556  1.00 23.33 ?  200 THR   D CA  1 
ATOM   4740 C  C   . THR   C 1 205 ? -50.468 5.355   62.365  1.00 22.53 ?  200 THR   D C   1 
ATOM   4741 O  O   . THR   C 1 205 ? -51.690 5.235   62.476  1.00 20.10 ?  200 THR   D O   1 
ATOM   4742 C  CB  . THR   C 1 205 ? -50.159 7.266   63.986  1.00 23.72 ?  200 THR   D CB  1 
ATOM   4743 O  OG1 . THR   C 1 205 ? -49.881 8.271   62.998  1.00 23.63 ?  200 THR   D OG1 1 
ATOM   4744 C  CG2 . THR   C 1 205 ? -49.544 7.691   65.301  1.00 24.60 ?  200 THR   D CG2 1 
ATOM   4745 N  N   . ARG   C 1 206 ? -49.852 5.147   61.208  1.00 22.65 ?  201 ARG   D N   1 
ATOM   4746 C  CA  . ARG   C 1 206 ? -50.586 4.718   59.985  1.00 26.21 ?  201 ARG   D CA  1 
ATOM   4747 C  C   . ARG   C 1 206 ? -51.286 3.361   60.207  1.00 22.68 ?  201 ARG   D C   1 
ATOM   4748 O  O   . ARG   C 1 206 ? -52.413 3.164   59.666  1.00 23.54 ?  201 ARG   D O   1 
ATOM   4749 C  CB  . ARG   C 1 206 ? -49.596 4.727   58.803  1.00 30.83 ?  201 ARG   D CB  1 
ATOM   4750 C  CG  . ARG   C 1 206 ? -50.173 5.101   57.446  1.00 42.92 ?  201 ARG   D CG  1 
ATOM   4751 C  CD  . ARG   C 1 206 ? -49.666 6.373   56.756  1.00 48.85 ?  201 ARG   D CD  1 
ATOM   4752 N  NE  . ARG   C 1 206 ? -48.215 6.507   56.718  1.00 48.82 ?  201 ARG   D NE  1 
ATOM   4753 C  CZ  . ARG   C 1 206 ? -47.531 7.640   56.504  1.00 45.36 ?  201 ARG   D CZ  1 
ATOM   4754 N  NH1 . ARG   C 1 206 ? -46.209 7.616   56.558  1.00 37.59 1  201 ARG   D NH1 1 
ATOM   4755 N  NH2 . ARG   C 1 206 ? -48.139 8.788   56.262  1.00 47.99 ?  201 ARG   D NH2 1 
ATOM   4756 N  N   . ALA   C 1 207 ? -50.729 2.438   60.987  1.00 21.80 ?  202 ALA   D N   1 
ATOM   4757 C  CA  . ALA   C 1 207 ? -51.315 1.094   61.228  1.00 22.47 ?  202 ALA   D CA  1 
ATOM   4758 C  C   . ALA   C 1 207 ? -52.603 1.247   62.064  1.00 20.76 ?  202 ALA   D C   1 
ATOM   4759 O  O   . ALA   C 1 207 ? -53.593 0.562   61.809  1.00 23.33 ?  202 ALA   D O   1 
ATOM   4760 C  CB  . ALA   C 1 207 ? -50.310 0.207   61.925  1.00 22.10 ?  202 ALA   D CB  1 
ATOM   4761 N  N   . VAL   C 1 208 ? -52.591 2.190   63.012  1.00 22.34 ?  203 VAL   D N   1 
ATOM   4762 C  CA  . VAL   C 1 208 ? -53.843 2.509   63.741  1.00 22.13 ?  203 VAL   D CA  1 
ATOM   4763 C  C   . VAL   C 1 208 ? -54.866 3.101   62.780  1.00 20.30 ?  203 VAL   D C   1 
ATOM   4764 O  O   . VAL   C 1 208 ? -56.034 2.610   62.781  1.00 23.52 ?  203 VAL   D O   1 
ATOM   4765 C  CB  . VAL   C 1 208 ? -53.609 3.417   64.951  1.00 24.77 ?  203 VAL   D CB  1 
ATOM   4766 C  CG1 . VAL   C 1 208 ? -54.945 3.779   65.588  1.00 22.08 ?  203 VAL   D CG1 1 
ATOM   4767 C  CG2 . VAL   C 1 208 ? -52.767 2.699   65.957  1.00 26.71 ?  203 VAL   D CG2 1 
ATOM   4768 N  N   . ALA   C 1 209 ? -54.483 4.095   61.988  1.00 20.97 ?  204 ALA   D N   1 
ATOM   4769 C  CA  . ALA   C 1 209 ? -55.378 4.704   60.975  1.00 22.63 ?  204 ALA   D CA  1 
ATOM   4770 C  C   . ALA   C 1 209 ? -55.971 3.597   60.082  1.00 24.65 ?  204 ALA   D C   1 
ATOM   4771 O  O   . ALA   C 1 209 ? -57.208 3.600   59.821  1.00 23.41 ?  204 ALA   D O   1 
ATOM   4772 C  CB  . ALA   C 1 209 ? -54.644 5.737   60.160  1.00 23.60 ?  204 ALA   D CB  1 
ATOM   4773 N  N   . GLY   C 1 210 ? -55.134 2.660   59.630  1.00 24.72 ?  205 GLY   D N   1 
ATOM   4774 C  CA  . GLY   C 1 210 ? -55.597 1.536   58.781  1.00 27.15 ?  205 GLY   D CA  1 
ATOM   4775 C  C   . GLY   C 1 210 ? -56.677 0.685   59.447  1.00 24.73 ?  205 GLY   D C   1 
ATOM   4776 O  O   . GLY   C 1 210 ? -57.654 0.309   58.760  1.00 26.74 ?  205 GLY   D O   1 
ATOM   4777 N  N   . LEU   C 1 211 ? -56.541 0.345   60.734  1.00 21.77 ?  206 LEU   D N   1 
ATOM   4778 C  CA  . LEU   C 1 211 ? -57.600 -0.408  61.446  1.00 22.30 ?  206 LEU   D CA  1 
ATOM   4779 C  C   . LEU   C 1 211 ? -58.870 0.440   61.594  1.00 22.39 ?  206 LEU   D C   1 
ATOM   4780 O  O   . LEU   C 1 211 ? -59.950 -0.107  61.464  1.00 21.67 ?  206 LEU   D O   1 
ATOM   4781 C  CB  . LEU   C 1 211 ? -57.048 -0.857  62.802  1.00 25.60 ?  206 LEU   D CB  1 
ATOM   4782 C  CG  . LEU   C 1 211 ? -55.994 -1.953  62.708  1.00 26.97 ?  206 LEU   D CG  1 
ATOM   4783 C  CD1 . LEU   C 1 211 ? -55.175 -2.038  63.984  1.00 26.48 ?  206 LEU   D CD1 1 
ATOM   4784 C  CD2 . LEU   C 1 211 ? -56.618 -3.299  62.358  1.00 29.08 ?  206 LEU   D CD2 1 
ATOM   4785 N  N   . MET   C 1 212 ? -58.758 1.708   61.981  1.00 23.08 ?  207 MET   D N   1 
ATOM   4786 C  CA  . MET   C 1 212 ? -59.932 2.603   62.087  1.00 24.85 ?  207 MET   D CA  1 
ATOM   4787 C  C   . MET   C 1 212 ? -60.666 2.671   60.741  1.00 27.42 ?  207 MET   D C   1 
ATOM   4788 O  O   . MET   C 1 212 ? -61.896 2.690   60.768  1.00 26.69 ?  207 MET   D O   1 
ATOM   4789 C  CB  . MET   C 1 212 ? -59.487 3.993   62.533  1.00 23.67 ?  207 MET   D CB  1 
ATOM   4790 C  CG  . MET   C 1 212 ? -58.909 3.977   63.929  1.00 24.08 ?  207 MET   D CG  1 
ATOM   4791 S  SD  . MET   C 1 212 ? -58.428 5.653   64.463  1.00 24.84 ?  207 MET   D SD  1 
ATOM   4792 C  CE  . MET   C 1 212 ? -60.108 6.278   64.640  1.00 25.48 ?  207 MET   D CE  1 
ATOM   4793 N  N   . ASP   C 1 213 ? -59.943 2.645   59.621  1.00 26.51 ?  208 ASP   D N   1 
ATOM   4794 C  CA  . ASP   C 1 213 ? -60.519 2.608   58.245  1.00 30.39 ?  208 ASP   D CA  1 
ATOM   4795 C  C   . ASP   C 1 213 ? -61.381 1.364   58.001  1.00 30.95 ?  208 ASP   D C   1 
ATOM   4796 O  O   . ASP   C 1 213 ? -62.271 1.465   57.153  1.00 33.37 ?  208 ASP   D O   1 
ATOM   4797 C  CB  . ASP   C 1 213 ? -59.421 2.654   57.184  1.00 33.02 ?  208 ASP   D CB  1 
ATOM   4798 C  CG  . ASP   C 1 213 ? -58.996 4.056   56.814  1.00 42.32 ?  208 ASP   D CG  1 
ATOM   4799 O  OD1 . ASP   C 1 213 ? -57.782 4.257   56.526  1.00 50.51 ?  208 ASP   D OD1 1 
ATOM   4800 O  OD2 . ASP   C 1 213 ? -59.879 4.940   56.818  1.00 56.22 -1 208 ASP   D OD2 1 
ATOM   4801 N  N   . ARG   C 1 214 ? -61.119 0.244   58.663  1.00 30.64 ?  209 ARG   D N   1 
ATOM   4802 C  CA  . ARG   C 1 214 ? -61.788 -1.069  58.412  1.00 35.83 ?  209 ARG   D CA  1 
ATOM   4803 C  C   . ARG   C 1 214 ? -63.011 -1.261  59.306  1.00 37.31 ?  209 ARG   D C   1 
ATOM   4804 O  O   . ARG   C 1 214 ? -63.718 -2.251  59.069  1.00 37.77 ?  209 ARG   D O   1 
ATOM   4805 C  CB  . ARG   C 1 214 ? -60.830 -2.247  58.598  1.00 39.21 ?  209 ARG   D CB  1 
ATOM   4806 C  CG  . ARG   C 1 214 ? -59.482 -2.042  57.924  1.00 46.69 ?  209 ARG   D CG  1 
ATOM   4807 C  CD  . ARG   C 1 214 ? -58.723 -3.259  57.415  1.00 51.41 ?  209 ARG   D CD  1 
ATOM   4808 N  NE  . ARG   C 1 214 ? -58.855 -4.531  58.131  1.00 63.45 ?  209 ARG   D NE  1 
ATOM   4809 C  CZ  . ARG   C 1 214 ? -59.764 -5.482  57.882  1.00 66.10 ?  209 ARG   D CZ  1 
ATOM   4810 N  NH1 . ARG   C 1 214 ? -59.750 -6.606  58.584  1.00 63.87 1  209 ARG   D NH1 1 
ATOM   4811 N  NH2 . ARG   C 1 214 ? -60.701 -5.308  56.962  1.00 65.32 ?  209 ARG   D NH2 1 
ATOM   4812 N  N   . LEU   C 1 215 ? -63.256 -0.376  60.283  1.00 34.26 ?  210 LEU   D N   1 
ATOM   4813 C  CA  . LEU   C 1 215 ? -64.424 -0.505  61.182  1.00 36.93 ?  210 LEU   D CA  1 
ATOM   4814 C  C   . LEU   C 1 215 ? -65.670 -0.196  60.369  1.00 42.61 ?  210 LEU   D C   1 
ATOM   4815 O  O   . LEU   C 1 215 ? -65.642 0.741   59.577  1.00 47.70 ?  210 LEU   D O   1 
ATOM   4816 C  CB  . LEU   C 1 215 ? -64.305 0.460   62.363  1.00 32.91 ?  210 LEU   D CB  1 
ATOM   4817 C  CG  . LEU   C 1 215 ? -63.210 0.106   63.359  1.00 29.45 ?  210 LEU   D CG  1 
ATOM   4818 C  CD1 . LEU   C 1 215 ? -63.104 1.193   64.407  1.00 25.70 ?  210 LEU   D CD1 1 
ATOM   4819 C  CD2 . LEU   C 1 215 ? -63.449 -1.235  64.019  1.00 30.85 ?  210 LEU   D CD2 1 
ATOM   4820 N  N   . PRO   C 1 216 ? -66.780 -0.948  60.556  1.00 52.45 ?  211 PRO   D N   1 
ATOM   4821 C  CA  . PRO   C 1 216 ? -68.009 -0.722  59.790  1.00 56.14 ?  211 PRO   D CA  1 
ATOM   4822 C  C   . PRO   C 1 216 ? -68.515 0.729   59.865  1.00 57.96 ?  211 PRO   D C   1 
ATOM   4823 O  O   . PRO   C 1 216 ? -68.461 1.313   60.945  1.00 58.78 ?  211 PRO   D O   1 
ATOM   4824 C  CB  . PRO   C 1 216 ? -69.043 -1.684  60.407  1.00 56.60 ?  211 PRO   D CB  1 
ATOM   4825 C  CG  . PRO   C 1 216 ? -68.385 -2.289  61.641  1.00 54.08 ?  211 PRO   D CG  1 
ATOM   4826 C  CD  . PRO   C 1 216 ? -66.894 -2.088  61.478  1.00 54.09 ?  211 PRO   D CD  1 
ATOM   4827 N  N   . GLY   D 1 4   ? -33.593 -13.648 89.923  1.00 51.36 ?  -1  GLY   A N   1 
ATOM   4828 C  CA  . GLY   D 1 4   ? -34.458 -12.565 89.356  1.00 48.83 ?  -1  GLY   A CA  1 
ATOM   4829 C  C   . GLY   D 1 4   ? -35.913 -12.993 89.247  1.00 40.72 ?  -1  GLY   A C   1 
ATOM   4830 O  O   . GLY   D 1 4   ? -36.183 -14.223 89.180  1.00 39.82 ?  -1  GLY   A O   1 
ATOM   4831 N  N   . ALA   D 1 5   ? -36.839 -12.026 89.258  1.00 34.81 ?  0   ALA   A N   1 
ATOM   4832 C  CA  . ALA   D 1 5   ? -38.279 -12.263 89.002  1.00 36.30 ?  0   ALA   A CA  1 
ATOM   4833 C  C   . ALA   D 1 5   ? -38.509 -12.322 87.482  1.00 32.41 ?  0   ALA   A C   1 
ATOM   4834 O  O   . ALA   D 1 5   ? -39.477 -12.932 87.051  1.00 30.22 ?  0   ALA   A O   1 
ATOM   4835 C  CB  . ALA   D 1 5   ? -39.108 -11.209 89.654  1.00 35.79 ?  0   ALA   A CB  1 
ATOM   4836 N  N   . MET   D 1 6   ? -37.641 -11.683 86.712  1.00 31.79 ?  1   MET   A N   1 
ATOM   4837 C  CA  . MET   D 1 6   ? -37.657 -11.714 85.225  1.00 28.44 ?  1   MET   A CA  1 
ATOM   4838 C  C   . MET   D 1 6   ? -36.355 -12.354 84.760  1.00 30.10 ?  1   MET   A C   1 
ATOM   4839 O  O   . MET   D 1 6   ? -35.286 -12.013 85.313  1.00 32.52 ?  1   MET   A O   1 
ATOM   4840 C  CB  . MET   D 1 6   ? -37.818 -10.319 84.632  1.00 32.34 ?  1   MET   A CB  1 
ATOM   4841 C  CG  . MET   D 1 6   ? -37.681 -10.278 83.143  1.00 31.67 ?  1   MET   A CG  1 
ATOM   4842 S  SD  . MET   D 1 6   ? -37.745 -8.572  82.599  1.00 33.61 ?  1   MET   A SD  1 
ATOM   4843 C  CE  . MET   D 1 6   ? -38.037 -8.813  80.852  1.00 31.07 ?  1   MET   A CE  1 
ATOM   4844 N  N   . PHE   D 1 7   ? -36.451 -13.310 83.838  1.00 27.78 ?  2   PHE   A N   1 
ATOM   4845 C  CA  . PHE   D 1 7   ? -35.273 -13.994 83.271  1.00 27.42 ?  2   PHE   A CA  1 
ATOM   4846 C  C   . PHE   D 1 7   ? -34.651 -13.089 82.205  1.00 27.87 ?  2   PHE   A C   1 
ATOM   4847 O  O   . PHE   D 1 7   ? -35.340 -12.793 81.193  1.00 27.29 ?  2   PHE   A O   1 
ATOM   4848 C  CB  . PHE   D 1 7   ? -35.659 -15.350 82.693  1.00 25.87 ?  2   PHE   A CB  1 
ATOM   4849 C  CG  . PHE   D 1 7   ? -34.474 -16.089 82.113  1.00 27.94 ?  2   PHE   A CG  1 
ATOM   4850 C  CD1 . PHE   D 1 7   ? -33.482 -16.573 82.950  1.00 29.55 ?  2   PHE   A CD1 1 
ATOM   4851 C  CD2 . PHE   D 1 7   ? -34.364 -16.335 80.750  1.00 31.29 ?  2   PHE   A CD2 1 
ATOM   4852 C  CE1 . PHE   D 1 7   ? -32.416 -17.306 82.454  1.00 28.29 ?  2   PHE   A CE1 1 
ATOM   4853 C  CE2 . PHE   D 1 7   ? -33.272 -17.032 80.247  1.00 30.88 ?  2   PHE   A CE2 1 
ATOM   4854 C  CZ  . PHE   D 1 7   ? -32.322 -17.544 81.098  1.00 33.74 ?  2   PHE   A CZ  1 
ATOM   4855 N  N   . VAL   D 1 8   ? -33.399 -12.653 82.417  1.00 25.89 ?  3   VAL   A N   1 
ATOM   4856 C  CA  . VAL   D 1 8   ? -32.701 -11.799 81.425  1.00 24.44 ?  3   VAL   A CA  1 
ATOM   4857 C  C   . VAL   D 1 8   ? -31.289 -12.325 81.262  1.00 25.60 ?  3   VAL   A C   1 
ATOM   4858 O  O   . VAL   D 1 8   ? -30.482 -12.130 82.156  1.00 27.24 ?  3   VAL   A O   1 
ATOM   4859 C  CB  . VAL   D 1 8   ? -32.679 -10.313 81.815  1.00 24.01 ?  3   VAL   A CB  1 
ATOM   4860 C  CG1 . VAL   D 1 8   ? -32.067 -9.494  80.673  1.00 25.21 ?  3   VAL   A CG1 1 
ATOM   4861 C  CG2 . VAL   D 1 8   ? -34.062 -9.781  82.207  1.00 25.90 ?  3   VAL   A CG2 1 
ATOM   4862 N  N   . PRO   D 1 9   ? -30.968 -13.002 80.143  1.00 26.63 ?  4   PRO   A N   1 
ATOM   4863 C  CA  . PRO   D 1 9   ? -29.582 -13.361 79.845  1.00 27.95 ?  4   PRO   A CA  1 
ATOM   4864 C  C   . PRO   D 1 9   ? -28.640 -12.163 80.012  1.00 30.38 ?  4   PRO   A C   1 
ATOM   4865 O  O   . PRO   D 1 9   ? -28.987 -11.041 79.639  1.00 28.76 ?  4   PRO   A O   1 
ATOM   4866 C  CB  . PRO   D 1 9   ? -29.642 -13.818 78.387  1.00 26.35 ?  4   PRO   A CB  1 
ATOM   4867 C  CG  . PRO   D 1 9   ? -31.059 -14.324 78.218  1.00 28.61 ?  4   PRO   A CG  1 
ATOM   4868 C  CD  . PRO   D 1 9   ? -31.900 -13.443 79.101  1.00 27.29 ?  4   PRO   A CD  1 
ATOM   4869 N  N   . GLY   D 1 10  ? -27.439 -12.431 80.533  1.00 32.40 ?  5   GLY   A N   1 
ATOM   4870 C  CA  . GLY   D 1 10  ? -26.373 -11.434 80.764  1.00 33.24 ?  5   GLY   A CA  1 
ATOM   4871 C  C   . GLY   D 1 10  ? -26.179 -10.463 79.599  1.00 28.19 ?  5   GLY   A C   1 
ATOM   4872 O  O   . GLY   D 1 10  ? -26.123 -9.260  79.824  1.00 31.45 ?  5   GLY   A O   1 
ATOM   4873 N  N   . PRO   D 1 11  ? -26.106 -10.926 78.333  1.00 28.29 ?  6   PRO   A N   1 
ATOM   4874 C  CA  . PRO   D 1 11  ? -25.794 -10.043 77.218  1.00 27.86 ?  6   PRO   A CA  1 
ATOM   4875 C  C   . PRO   D 1 11  ? -26.879 -8.987  77.000  1.00 26.90 ?  6   PRO   A C   1 
ATOM   4876 O  O   . PRO   D 1 11  ? -26.595 -7.997  76.368  1.00 23.61 ?  6   PRO   A O   1 
ATOM   4877 C  CB  . PRO   D 1 11  ? -25.736 -10.962 75.985  1.00 31.21 ?  6   PRO   A CB  1 
ATOM   4878 C  CG  . PRO   D 1 11  ? -25.619 -12.367 76.543  1.00 31.81 ?  6   PRO   A CG  1 
ATOM   4879 C  CD  . PRO   D 1 11  ? -26.265 -12.315 77.903  1.00 31.49 ?  6   PRO   A CD  1 
ATOM   4880 N  N   . TYR   D 1 12  ? -28.098 -9.244  77.494  1.00 23.47 ?  7   TYR   A N   1 
ATOM   4881 C  CA  . TYR   D 1 12  ? -29.275 -8.382  77.222  1.00 24.31 ?  7   TYR   A CA  1 
ATOM   4882 C  C   . TYR   D 1 12  ? -29.606 -7.454  78.389  1.00 24.94 ?  7   TYR   A C   1 
ATOM   4883 O  O   . TYR   D 1 12  ? -30.703 -6.849  78.381  1.00 24.30 ?  7   TYR   A O   1 
ATOM   4884 C  CB  . TYR   D 1 12  ? -30.454 -9.266  76.844  1.00 20.85 ?  7   TYR   A CB  1 
ATOM   4885 C  CG  . TYR   D 1 12  ? -30.186 -10.168 75.676  1.00 21.94 ?  7   TYR   A CG  1 
ATOM   4886 C  CD1 . TYR   D 1 12  ? -29.396 -9.759  74.607  1.00 22.37 ?  7   TYR   A CD1 1 
ATOM   4887 C  CD2 . TYR   D 1 12  ? -30.732 -11.439 75.637  1.00 24.07 ?  7   TYR   A CD2 1 
ATOM   4888 C  CE1 . TYR   D 1 12  ? -29.162 -10.608 73.542  1.00 22.95 ?  7   TYR   A CE1 1 
ATOM   4889 C  CE2 . TYR   D 1 12  ? -30.490 -12.313 74.598  1.00 24.40 ?  7   TYR   A CE2 1 
ATOM   4890 C  CZ  . TYR   D 1 12  ? -29.688 -11.893 73.547  1.00 23.08 ?  7   TYR   A CZ  1 
ATOM   4891 O  OH  . TYR   D 1 12  ? -29.501 -12.732 72.494  1.00 24.68 ?  7   TYR   A OH  1 
ATOM   4892 N  N   . HIS   D 1 13  ? -28.702 -7.298  79.360  1.00 26.93 ?  8   HIS   A N   1 
ATOM   4893 C  CA  . HIS   D 1 13  ? -28.832 -6.274  80.430  1.00 27.55 ?  8   HIS   A CA  1 
ATOM   4894 C  C   . HIS   D 1 13  ? -28.605 -4.896  79.807  1.00 26.39 ?  8   HIS   A C   1 
ATOM   4895 O  O   . HIS   D 1 13  ? -27.735 -4.783  78.920  1.00 27.48 ?  8   HIS   A O   1 
ATOM   4896 C  CB  . HIS   D 1 13  ? -27.868 -6.571  81.587  1.00 30.39 ?  8   HIS   A CB  1 
ATOM   4897 C  CG  . HIS   D 1 13  ? -28.293 -7.720  82.435  1.00 36.90 ?  8   HIS   A CG  1 
ATOM   4898 N  ND1 . HIS   D 1 13  ? -28.508 -7.598  83.797  1.00 45.25 ?  8   HIS   A ND1 1 
ATOM   4899 C  CD2 . HIS   D 1 13  ? -28.556 -9.004  82.124  1.00 36.54 ?  8   HIS   A CD2 1 
ATOM   4900 C  CE1 . HIS   D 1 13  ? -28.888 -8.765  84.279  1.00 46.47 ?  8   HIS   A CE1 1 
ATOM   4901 N  NE2 . HIS   D 1 13  ? -28.927 -9.641  83.271  1.00 41.55 ?  8   HIS   A NE2 1 
ATOM   4902 N  N   . ALA   D 1 14  ? -29.379 -3.880  80.222  1.00 27.77 ?  9   ALA   A N   1 
ATOM   4903 C  CA  . ALA   D 1 14  ? -29.143 -2.467  79.852  1.00 26.54 ?  9   ALA   A CA  1 
ATOM   4904 C  C   . ALA   D 1 14  ? -27.726 -2.082  80.275  1.00 29.29 ?  9   ALA   A C   1 
ATOM   4905 O  O   . ALA   D 1 14  ? -27.211 -2.589  81.285  1.00 29.55 ?  9   ALA   A O   1 
ATOM   4906 C  CB  . ALA   D 1 14  ? -30.173 -1.570  80.462  1.00 26.68 ?  9   ALA   A CB  1 
ATOM   4907 N  N   . PRO   D 1 15  ? -27.045 -1.254  79.461  1.00 29.92 ?  10  PRO   A N   1 
ATOM   4908 C  CA  . PRO   D 1 15  ? -25.753 -0.668  79.816  1.00 35.68 ?  10  PRO   A CA  1 
ATOM   4909 C  C   . PRO   D 1 15  ? -25.814 0.213   81.080  1.00 35.79 ?  10  PRO   A C   1 
ATOM   4910 O  O   . PRO   D 1 15  ? -24.811 0.332   81.760  1.00 38.81 ?  10  PRO   A O   1 
ATOM   4911 C  CB  . PRO   D 1 15  ? -25.407 0.258   78.634  1.00 36.45 ?  10  PRO   A CB  1 
ATOM   4912 C  CG  . PRO   D 1 15  ? -26.276 -0.175  77.503  1.00 36.95 ?  10  PRO   A CG  1 
ATOM   4913 C  CD  . PRO   D 1 15  ? -27.483 -0.841  78.115  1.00 36.55 ?  10  PRO   A CD  1 
ATOM   4914 N  N   . GLU   D 1 16  ? -26.973 0.820   81.347  1.00 31.75 ?  11  GLU   A N   1 
ATOM   4915 C  CA  . GLU   D 1 16  ? -27.185 1.863   82.387  1.00 34.53 ?  11  GLU   A CA  1 
ATOM   4916 C  C   . GLU   D 1 16  ? -28.578 1.686   82.979  1.00 32.12 ?  11  GLU   A C   1 
ATOM   4917 O  O   . GLU   D 1 16  ? -29.516 1.426   82.206  1.00 27.38 ?  11  GLU   A O   1 
ATOM   4918 C  CB  . GLU   D 1 16  ? -27.111 3.283   81.805  1.00 41.59 ?  11  GLU   A CB  1 
ATOM   4919 C  CG  . GLU   D 1 16  ? -25.841 3.606   81.021  1.00 50.76 ?  11  GLU   A CG  1 
ATOM   4920 C  CD  . GLU   D 1 16  ? -24.602 3.922   81.854  1.00 59.54 ?  11  GLU   A CD  1 
ATOM   4921 O  OE1 . GLU   D 1 16  ? -24.636 3.677   83.077  1.00 67.33 ?  11  GLU   A OE1 1 
ATOM   4922 O  OE2 . GLU   D 1 16  ? -23.595 4.409   81.275  1.00 70.72 -1 11  GLU   A OE2 1 
ATOM   4923 N  N   . ASP   D 1 17  ? -28.733 1.886   84.283  1.00 28.42 ?  12  ASP   A N   1 
ATOM   4924 C  CA  . ASP   D 1 17  ? -30.072 1.824   84.921  1.00 28.65 ?  12  ASP   A CA  1 
ATOM   4925 C  C   . ASP   D 1 17  ? -31.046 2.795   84.235  1.00 28.47 ?  12  ASP   A C   1 
ATOM   4926 O  O   . ASP   D 1 17  ? -32.266 2.501   84.221  1.00 24.15 ?  12  ASP   A O   1 
ATOM   4927 C  CB  . ASP   D 1 17  ? -29.991 2.164   86.412  1.00 33.37 ?  12  ASP   A CB  1 
ATOM   4928 C  CG  . ASP   D 1 17  ? -29.370 1.059   87.249  1.00 39.41 ?  12  ASP   A CG  1 
ATOM   4929 O  OD1 . ASP   D 1 17  ? -29.674 -0.119  86.986  1.00 39.06 ?  12  ASP   A OD1 1 
ATOM   4930 O  OD2 . ASP   D 1 17  ? -28.616 1.402   88.180  1.00 41.96 -1 12  ASP   A OD2 1 
ATOM   4931 N  N   . ARG   D 1 18  ? -30.564 3.957   83.789  1.00 24.46 ?  13  ARG   A N   1 
ATOM   4932 C  CA  . ARG   D 1 18  ? -31.417 5.008   83.182  1.00 24.78 ?  13  ARG   A CA  1 
ATOM   4933 C  C   . ARG   D 1 18  ? -32.188 4.482   81.952  1.00 23.91 ?  13  ARG   A C   1 
ATOM   4934 O  O   . ARG   D 1 18  ? -33.294 5.065   81.632  1.00 22.09 ?  13  ARG   A O   1 
ATOM   4935 C  CB  . ARG   D 1 18  ? -30.544 6.202   82.813  1.00 28.31 ?  13  ARG   A CB  1 
ATOM   4936 C  CG  . ARG   D 1 18  ? -31.223 7.245   81.942  1.00 33.28 ?  13  ARG   A CG  1 
ATOM   4937 C  CD  . ARG   D 1 18  ? -32.294 7.978   82.697  1.00 37.73 ?  13  ARG   A CD  1 
ATOM   4938 N  NE  . ARG   D 1 18  ? -31.693 8.984   83.549  1.00 52.34 ?  13  ARG   A NE  1 
ATOM   4939 C  CZ  . ARG   D 1 18  ? -31.761 10.299  83.345  1.00 54.19 ?  13  ARG   A CZ  1 
ATOM   4940 N  NH1 . ARG   D 1 18  ? -32.432 10.787  82.312  1.00 57.58 1  13  ARG   A NH1 1 
ATOM   4941 N  NH2 . ARG   D 1 18  ? -31.156 11.117  84.191  1.00 60.79 ?  13  ARG   A NH2 1 
ATOM   4942 N  N   . TRP   D 1 19  ? -31.683 3.446   81.280  1.00 21.82 ?  14  TRP   A N   1 
ATOM   4943 C  CA  . TRP   D 1 19  ? -32.371 2.894   80.092  1.00 22.34 ?  14  TRP   A CA  1 
ATOM   4944 C  C   . TRP   D 1 19  ? -33.740 2.372   80.513  1.00 20.54 ?  14  TRP   A C   1 
ATOM   4945 O  O   . TRP   D 1 19  ? -34.641 2.445   79.662  1.00 23.54 ?  14  TRP   A O   1 
ATOM   4946 C  CB  . TRP   D 1 19  ? -31.606 1.787   79.395  1.00 23.79 ?  14  TRP   A CB  1 
ATOM   4947 C  CG  . TRP   D 1 19  ? -30.468 2.267   78.549  1.00 26.66 ?  14  TRP   A CG  1 
ATOM   4948 C  CD1 . TRP   D 1 19  ? -29.559 3.245   78.863  1.00 30.77 ?  14  TRP   A CD1 1 
ATOM   4949 C  CD2 . TRP   D 1 19  ? -30.101 1.774   77.250  1.00 26.31 ?  14  TRP   A CD2 1 
ATOM   4950 N  NE1 . TRP   D 1 19  ? -28.677 3.412   77.835  1.00 31.50 ?  14  TRP   A NE1 1 
ATOM   4951 C  CE2 . TRP   D 1 19  ? -28.960 2.505   76.845  1.00 29.17 ?  14  TRP   A CE2 1 
ATOM   4952 C  CE3 . TRP   D 1 19  ? -30.619 0.795   76.394  1.00 25.97 ?  14  TRP   A CE3 1 
ATOM   4953 C  CZ2 . TRP   D 1 19  ? -28.348 2.282   75.611  1.00 30.23 ?  14  TRP   A CZ2 1 
ATOM   4954 C  CZ3 . TRP   D 1 19  ? -29.996 0.558   75.193  1.00 28.95 ?  14  TRP   A CZ3 1 
ATOM   4955 C  CH2 . TRP   D 1 19  ? -28.877 1.296   74.808  1.00 27.95 ?  14  TRP   A CH2 1 
ATOM   4956 N  N   . LEU   D 1 20  ? -33.876 1.812   81.727  1.00 21.09 ?  15  LEU   A N   1 
ATOM   4957 C  CA  . LEU   D 1 20  ? -35.161 1.217   82.126  1.00 21.18 ?  15  LEU   A CA  1 
ATOM   4958 C  C   . LEU   D 1 20  ? -36.136 2.372   82.344  1.00 20.27 ?  15  LEU   A C   1 
ATOM   4959 O  O   . LEU   D 1 20  ? -37.346 2.248   82.026  1.00 20.29 ?  15  LEU   A O   1 
ATOM   4960 C  CB  . LEU   D 1 20  ? -34.979 0.350   83.371  1.00 20.91 ?  15  LEU   A CB  1 
ATOM   4961 C  CG  . LEU   D 1 20  ? -34.332 -1.010  83.131  1.00 21.26 ?  15  LEU   A CG  1 
ATOM   4962 C  CD1 . LEU   D 1 20  ? -32.841 -0.893  82.945  1.00 23.53 ?  15  LEU   A CD1 1 
ATOM   4963 C  CD2 . LEU   D 1 20  ? -34.677 -1.985  84.245  1.00 23.95 ?  15  LEU   A CD2 1 
ATOM   4964 N  N   . VAL   D 1 21  ? -35.669 3.448   82.986  1.00 21.20 ?  16  VAL   A N   1 
ATOM   4965 C  CA  . VAL   D 1 21  ? -36.529 4.640   83.212  1.00 19.98 ?  16  VAL   A CA  1 
ATOM   4966 C  C   . VAL   D 1 21  ? -36.936 5.184   81.840  1.00 17.25 ?  16  VAL   A C   1 
ATOM   4967 O  O   . VAL   D 1 21  ? -38.162 5.515   81.678  1.00 20.94 ?  16  VAL   A O   1 
ATOM   4968 C  CB  . VAL   D 1 21  ? -35.876 5.739   84.070  1.00 21.17 ?  16  VAL   A CB  1 
ATOM   4969 C  CG1 . VAL   D 1 21  ? -36.867 6.881   84.233  1.00 20.32 ?  16  VAL   A CG1 1 
ATOM   4970 C  CG2 . VAL   D 1 21  ? -35.408 5.212   85.432  1.00 22.97 ?  16  VAL   A CG2 1 
ATOM   4971 N  N   . ASP   D 1 22  ? -35.992 5.307   80.911  1.00 20.84 ?  17  ASP   A N   1 
ATOM   4972 C  CA  . ASP   D 1 22  ? -36.275 5.878   79.570  1.00 21.29 ?  17  ASP   A CA  1 
ATOM   4973 C  C   . ASP   D 1 22  ? -37.399 5.041   78.928  1.00 21.62 ?  17  ASP   A C   1 
ATOM   4974 O  O   . ASP   D 1 22  ? -38.328 5.640   78.283  1.00 22.45 ?  17  ASP   A O   1 
ATOM   4975 C  CB  . ASP   D 1 22  ? -35.032 5.880   78.688  1.00 26.32 ?  17  ASP   A CB  1 
ATOM   4976 C  CG  . ASP   D 1 22  ? -33.954 6.875   79.086  1.00 31.79 ?  17  ASP   A CG  1 
ATOM   4977 O  OD1 . ASP   D 1 22  ? -34.259 7.816   79.875  1.00 33.08 ?  17  ASP   A OD1 1 
ATOM   4978 O  OD2 . ASP   D 1 22  ? -32.809 6.679   78.615  1.00 36.39 -1 17  ASP   A OD2 1 
ATOM   4979 N  N   . LEU   D 1 23  ? -37.346 3.708   79.057  1.00 21.01 ?  18  LEU   A N   1 
ATOM   4980 C  CA  . LEU   D 1 23  ? -38.367 2.834   78.380  1.00 19.94 ?  18  LEU   A CA  1 
ATOM   4981 C  C   . LEU   D 1 23  ? -39.739 3.052   79.040  1.00 19.55 ?  18  LEU   A C   1 
ATOM   4982 O  O   . LEU   D 1 23  ? -40.766 3.167   78.306  1.00 18.29 ?  18  LEU   A O   1 
ATOM   4983 C  CB  . LEU   D 1 23  ? -37.957 1.353   78.425  1.00 21.15 ?  18  LEU   A CB  1 
ATOM   4984 C  CG  . LEU   D 1 23  ? -38.692 0.426   77.449  1.00 23.39 ?  18  LEU   A CG  1 
ATOM   4985 C  CD1 . LEU   D 1 23  ? -37.960 -0.885  77.237  1.00 28.33 ?  18  LEU   A CD1 1 
ATOM   4986 C  CD2 . LEU   D 1 23  ? -40.078 0.092   77.955  1.00 28.90 ?  18  LEU   A CD2 1 
ATOM   4987 N  N   . VAL   D 1 24  ? -39.801 3.140   80.372  1.00 18.74 ?  19  VAL   A N   1 
ATOM   4988 C  CA  . VAL   D 1 24  ? -41.080 3.384   81.083  1.00 19.49 ?  19  VAL   A CA  1 
ATOM   4989 C  C   . VAL   D 1 24  ? -41.650 4.719   80.602  1.00 19.74 ?  19  VAL   A C   1 
ATOM   4990 O  O   . VAL   D 1 24  ? -42.876 4.818   80.358  1.00 18.55 ?  19  VAL   A O   1 
ATOM   4991 C  CB  . VAL   D 1 24  ? -40.911 3.371   82.617  1.00 20.49 ?  19  VAL   A CB  1 
ATOM   4992 C  CG1 . VAL   D 1 24  ? -41.969 4.154   83.331  1.00 21.41 ?  19  VAL   A CG1 1 
ATOM   4993 C  CG2 . VAL   D 1 24  ? -40.879 1.978   83.154  1.00 21.79 ?  19  VAL   A CG2 1 
ATOM   4994 N  N   . ARG   D 1 25  ? -40.814 5.760   80.496  1.00 18.95 ?  20  ARG   A N   1 
ATOM   4995 C  CA  . ARG   D 1 25  ? -41.274 7.098   80.060  1.00 20.35 ?  20  ARG   A CA  1 
ATOM   4996 C  C   . ARG   D 1 25  ? -41.768 7.026   78.609  1.00 18.81 ?  20  ARG   A C   1 
ATOM   4997 O  O   . ARG   D 1 25  ? -42.721 7.725   78.276  1.00 20.69 ?  20  ARG   A O   1 
ATOM   4998 C  CB  . ARG   D 1 25  ? -40.154 8.139   80.208  1.00 20.34 ?  20  ARG   A CB  1 
ATOM   4999 C  CG  . ARG   D 1 25  ? -39.871 8.473   81.659  1.00 24.11 ?  20  ARG   A CG  1 
ATOM   5000 C  CD  . ARG   D 1 25  ? -39.101 9.747   81.659  1.00 26.63 ?  20  ARG   A CD  1 
ATOM   5001 N  NE  . ARG   D 1 25  ? -38.421 10.000  82.898  1.00 28.62 ?  20  ARG   A NE  1 
ATOM   5002 C  CZ  . ARG   D 1 25  ? -38.918 10.612  83.932  1.00 29.22 ?  20  ARG   A CZ  1 
ATOM   5003 N  NH1 . ARG   D 1 25  ? -40.192 10.965  83.970  1.00 31.41 1  20  ARG   A NH1 1 
ATOM   5004 N  NH2 . ARG   D 1 25  ? -38.124 10.840  84.966  1.00 36.06 ?  20  ARG   A NH2 1 
ATOM   5005 N  N   . GLY   D 1 26  ? -41.115 6.227   77.778  1.00 20.37 ?  21  GLY   A N   1 
ATOM   5006 C  CA  . GLY   D 1 26  ? -41.372 6.224   76.323  1.00 18.96 ?  21  GLY   A CA  1 
ATOM   5007 C  C   . GLY   D 1 26  ? -42.596 5.411   75.963  1.00 20.13 ?  21  GLY   A C   1 
ATOM   5008 O  O   . GLY   D 1 26  ? -43.095 5.578   74.852  1.00 18.49 ?  21  GLY   A O   1 
ATOM   5009 N  N   . HIS   D 1 27  ? -43.018 4.496   76.847  1.00 17.78 ?  22  HIS   A N   1 
ATOM   5010 C  CA  . HIS   D 1 27  ? -44.005 3.435   76.529  1.00 18.66 ?  22  HIS   A CA  1 
ATOM   5011 C  C   . HIS   D 1 27  ? -44.967 3.255   77.688  1.00 19.41 ?  22  HIS   A C   1 
ATOM   5012 O  O   . HIS   D 1 27  ? -44.956 2.220   78.331  1.00 18.49 ?  22  HIS   A O   1 
ATOM   5013 C  CB  . HIS   D 1 27  ? -43.218 2.180   76.154  1.00 20.31 ?  22  HIS   A CB  1 
ATOM   5014 C  CG  . HIS   D 1 27  ? -42.291 2.453   75.045  1.00 19.69 ?  22  HIS   A CG  1 
ATOM   5015 N  ND1 . HIS   D 1 27  ? -42.714 2.448   73.727  1.00 21.42 ?  22  HIS   A ND1 1 
ATOM   5016 C  CD2 . HIS   D 1 27  ? -40.987 2.782   75.023  1.00 19.85 ?  22  HIS   A CD2 1 
ATOM   5017 C  CE1 . HIS   D 1 27  ? -41.687 2.757   72.947  1.00 21.73 ?  22  HIS   A CE1 1 
ATOM   5018 N  NE2 . HIS   D 1 27  ? -40.636 2.956   73.709  1.00 20.77 ?  22  HIS   A NE2 1 
ATOM   5019 N  N   . PRO   D 1 28  ? -45.745 4.293   78.048  1.00 17.11 ?  23  PRO   A N   1 
ATOM   5020 C  CA  . PRO   D 1 28  ? -46.472 4.304   79.324  1.00 18.55 ?  23  PRO   A CA  1 
ATOM   5021 C  C   . PRO   D 1 28  ? -47.699 3.377   79.392  1.00 20.26 ?  23  PRO   A C   1 
ATOM   5022 O  O   . PRO   D 1 28  ? -48.209 3.130   80.484  1.00 16.48 ?  23  PRO   A O   1 
ATOM   5023 C  CB  . PRO   D 1 28  ? -46.954 5.758   79.472  1.00 20.14 ?  23  PRO   A CB  1 
ATOM   5024 C  CG  . PRO   D 1 28  ? -46.994 6.276   78.048  1.00 20.69 ?  23  PRO   A CG  1 
ATOM   5025 C  CD  . PRO   D 1 28  ? -45.853 5.571   77.346  1.00 18.61 ?  23  PRO   A CD  1 
ATOM   5026 N  N   . LEU   D 1 29  ? -48.168 2.854   78.256  1.00 15.97 ?  24  LEU   A N   1 
ATOM   5027 C  CA  . LEU   D 1 29  ? -49.337 1.953   78.307  1.00 17.63 ?  24  LEU   A CA  1 
ATOM   5028 C  C   . LEU   D 1 29  ? -48.804 0.555   78.636  1.00 17.45 ?  24  LEU   A C   1 
ATOM   5029 O  O   . LEU   D 1 29  ? -48.382 -0.197  77.753  1.00 17.98 ?  24  LEU   A O   1 
ATOM   5030 C  CB  . LEU   D 1 29  ? -50.143 1.968   77.013  1.00 17.30 ?  24  LEU   A CB  1 
ATOM   5031 C  CG  . LEU   D 1 29  ? -51.492 1.286   77.152  1.00 19.14 ?  24  LEU   A CG  1 
ATOM   5032 C  CD1 . LEU   D 1 29  ? -52.412 2.164   77.969  1.00 19.83 ?  24  LEU   A CD1 1 
ATOM   5033 C  CD2 . LEU   D 1 29  ? -52.027 0.988   75.763  1.00 21.45 ?  24  LEU   A CD2 1 
ATOM   5034 N  N   . ALA   D 1 30  ? -48.711 0.262   79.938  1.00 17.32 ?  25  ALA   A N   1 
ATOM   5035 C  CA  . ALA   D 1 30  ? -48.141 -0.964  80.497  1.00 17.14 ?  25  ALA   A CA  1 
ATOM   5036 C  C   . ALA   D 1 30  ? -49.187 -2.068  80.570  1.00 17.69 ?  25  ALA   A C   1 
ATOM   5037 O  O   . ALA   D 1 30  ? -50.412 -1.755  80.578  1.00 17.89 ?  25  ALA   A O   1 
ATOM   5038 C  CB  . ALA   D 1 30  ? -47.656 -0.675  81.877  1.00 18.36 ?  25  ALA   A CB  1 
ATOM   5039 N  N   . GLN   D 1 31  ? -48.703 -3.301  80.574  1.00 15.19 ?  26  GLN   A N   1 
ATOM   5040 C  CA  . GLN   D 1 31  ? -49.585 -4.458  80.898  1.00 17.16 ?  26  GLN   A CA  1 
ATOM   5041 C  C   . GLN   D 1 31  ? -49.474 -4.749  82.387  1.00 15.10 ?  26  GLN   A C   1 
ATOM   5042 O  O   . GLN   D 1 31  ? -48.386 -5.104  82.869  1.00 18.91 ?  26  GLN   A O   1 
ATOM   5043 C  CB  . GLN   D 1 31  ? -49.263 -5.690  80.066  1.00 16.53 ?  26  GLN   A CB  1 
ATOM   5044 C  CG  . GLN   D 1 31  ? -49.548 -5.461  78.579  1.00 17.58 ?  26  GLN   A CG  1 
ATOM   5045 C  CD  . GLN   D 1 31  ? -49.354 -6.702  77.727  1.00 18.60 ?  26  GLN   A CD  1 
ATOM   5046 O  OE1 . GLN   D 1 31  ? -49.577 -7.832  78.177  1.00 21.11 ?  26  GLN   A OE1 1 
ATOM   5047 N  NE2 . GLN   D 1 31  ? -49.006 -6.507  76.460  1.00 19.00 ?  26  GLN   A NE2 1 
ATOM   5048 N  N   . LEU   D 1 32  ? -50.521 -4.468  83.117  1.00 17.45 ?  27  LEU   A N   1 
ATOM   5049 C  CA  . LEU   D 1 32  ? -50.562 -4.725  84.593  1.00 17.26 ?  27  LEU   A CA  1 
ATOM   5050 C  C   . LEU   D 1 32  ? -51.090 -6.151  84.804  1.00 18.96 ?  27  LEU   A C   1 
ATOM   5051 O  O   . LEU   D 1 32  ? -52.205 -6.454  84.338  1.00 18.44 ?  27  LEU   A O   1 
ATOM   5052 C  CB  . LEU   D 1 32  ? -51.448 -3.683  85.274  1.00 17.74 ?  27  LEU   A CB  1 
ATOM   5053 C  CG  . LEU   D 1 32  ? -51.571 -3.844  86.793  1.00 19.51 ?  27  LEU   A CG  1 
ATOM   5054 C  CD1 . LEU   D 1 32  ? -50.270 -3.482  87.465  1.00 20.72 ?  27  LEU   A CD1 1 
ATOM   5055 C  CD2 . LEU   D 1 32  ? -52.680 -2.971  87.351  1.00 21.89 ?  27  LEU   A CD2 1 
ATOM   5056 N  N   . ALA   D 1 33  ? -50.336 -6.986  85.495  1.00 18.93 ?  28  ALA   A N   1 
ATOM   5057 C  CA  . ALA   D 1 33  ? -50.693 -8.404  85.726  1.00 18.14 ?  28  ALA   A CA  1 
ATOM   5058 C  C   . ALA   D 1 33  ? -50.710 -8.702  87.224  1.00 18.15 ?  28  ALA   A C   1 
ATOM   5059 O  O   . ALA   D 1 33  ? -49.800 -8.287  87.956  1.00 19.65 ?  28  ALA   A O   1 
ATOM   5060 C  CB  . ALA   D 1 33  ? -49.757 -9.337  85.001  1.00 18.65 ?  28  ALA   A CB  1 
ATOM   5061 N  N   . SER   D 1 34  ? -51.722 -9.427  87.644  1.00 18.69 ?  29  SER   A N   1 
ATOM   5062 C  CA  . SER   D 1 34  ? -51.792 -9.971  89.020  1.00 19.86 ?  29  SER   A CA  1 
ATOM   5063 C  C   . SER   D 1 34  ? -52.394 -11.380 88.967  1.00 21.11 ?  29  SER   A C   1 
ATOM   5064 O  O   . SER   D 1 34  ? -53.055 -11.740 87.978  1.00 19.90 ?  29  SER   A O   1 
ATOM   5065 C  CB  . SER   D 1 34  ? -52.572 -9.040  89.878  1.00 21.24 ?  29  SER   A CB  1 
ATOM   5066 O  OG  . SER   D 1 34  ? -53.930 -8.968  89.490  1.00 21.79 ?  29  SER   A OG  1 
ATOM   5067 N  N   . ASN   D 1 35  ? -52.175 -12.139 90.020  1.00 20.90 ?  30  ASN   A N   1 
ATOM   5068 C  CA  . ASN   D 1 35  ? -52.545 -13.566 90.040  1.00 23.88 ?  30  ASN   A CA  1 
ATOM   5069 C  C   . ASN   D 1 35  ? -54.061 -13.711 89.888  1.00 25.11 ?  30  ASN   A C   1 
ATOM   5070 O  O   . ASN   D 1 35  ? -54.817 -12.873 90.427  1.00 25.67 ?  30  ASN   A O   1 
ATOM   5071 C  CB  . ASN   D 1 35  ? -52.120 -14.260 91.316  1.00 23.70 ?  30  ASN   A CB  1 
ATOM   5072 C  CG  . ASN   D 1 35  ? -50.631 -14.476 91.394  1.00 24.40 ?  30  ASN   A CG  1 
ATOM   5073 O  OD1 . ASN   D 1 35  ? -49.920 -14.398 90.407  1.00 24.14 ?  30  ASN   A OD1 1 
ATOM   5074 N  ND2 . ASN   D 1 35  ? -50.156 -14.859 92.567  1.00 30.10 ?  30  ASN   A ND2 1 
ATOM   5075 N  N   . GLY   D 1 36  ? -54.469 -14.745 89.164  1.00 24.25 ?  31  GLY   A N   1 
ATOM   5076 C  CA  . GLY   D 1 36  ? -55.870 -15.189 89.081  1.00 25.26 ?  31  GLY   A CA  1 
ATOM   5077 C  C   . GLY   D 1 36  ? -56.212 -15.979 90.342  1.00 28.73 ?  31  GLY   A C   1 
ATOM   5078 O  O   . GLY   D 1 36  ? -55.336 -16.672 90.861  1.00 31.11 ?  31  GLY   A O   1 
ATOM   5079 N  N   . ALA   D 1 37  ? -57.444 -15.861 90.818  1.00 33.22 ?  32  ALA   A N   1 
ATOM   5080 C  CA  . ALA   D 1 37  ? -57.938 -16.593 92.011  1.00 35.85 ?  32  ALA   A CA  1 
ATOM   5081 C  C   . ALA   D 1 37  ? -58.066 -18.072 91.649  1.00 38.12 ?  32  ALA   A C   1 
ATOM   5082 O  O   . ALA   D 1 37  ? -58.625 -18.344 90.563  1.00 38.14 ?  32  ALA   A O   1 
ATOM   5083 C  CB  . ALA   D 1 37  ? -59.276 -16.029 92.448  1.00 35.61 ?  32  ALA   A CB  1 
ATOM   5084 N  N   . GLY   D 1 38  ? -57.611 -18.955 92.551  1.00 42.39 ?  33  GLY   A N   1 
ATOM   5085 C  CA  . GLY   D 1 38  ? -57.779 -20.422 92.502  1.00 46.71 ?  33  GLY   A CA  1 
ATOM   5086 C  C   . GLY   D 1 38  ? -57.199 -21.009 91.232  1.00 49.37 ?  33  GLY   A C   1 
ATOM   5087 O  O   . GLY   D 1 38  ? -57.974 -21.588 90.447  1.00 53.44 ?  33  GLY   A O   1 
ATOM   5088 N  N   . GLY   D 1 39  ? -55.905 -20.766 90.991  1.00 47.94 ?  34  GLY   A N   1 
ATOM   5089 C  CA  . GLY   D 1 39  ? -55.142 -21.335 89.862  1.00 48.32 ?  34  GLY   A CA  1 
ATOM   5090 C  C   . GLY   D 1 39  ? -55.599 -20.867 88.477  1.00 44.79 ?  34  GLY   A C   1 
ATOM   5091 O  O   . GLY   D 1 39  ? -55.056 -21.428 87.495  1.00 47.49 ?  34  GLY   A O   1 
ATOM   5092 N  N   . ALA   D 1 40  ? -56.540 -19.912 88.365  1.00 39.24 ?  35  ALA   A N   1 
ATOM   5093 C  CA  . ALA   D 1 40  ? -56.961 -19.292 87.079  1.00 36.09 ?  35  ALA   A CA  1 
ATOM   5094 C  C   . ALA   D 1 40  ? -55.793 -18.478 86.526  1.00 27.61 ?  35  ALA   A C   1 
ATOM   5095 O  O   . ALA   D 1 40  ? -54.867 -18.143 87.293  1.00 29.06 ?  35  ALA   A O   1 
ATOM   5096 C  CB  . ALA   D 1 40  ? -58.171 -18.406 87.207  1.00 33.56 ?  35  ALA   A CB  1 
ATOM   5097 N  N   . ALA   D 1 41  ? -55.835 -18.167 85.226  1.00 27.11 ?  36  ALA   A N   1 
ATOM   5098 C  CA  . ALA   D 1 41  ? -54.774 -17.361 84.578  1.00 24.47 ?  36  ALA   A CA  1 
ATOM   5099 C  C   . ALA   D 1 41  ? -54.735 -15.970 85.226  1.00 22.11 ?  36  ALA   A C   1 
ATOM   5100 O  O   . ALA   D 1 41  ? -55.750 -15.456 85.689  1.00 21.46 ?  36  ALA   A O   1 
ATOM   5101 C  CB  . ALA   D 1 41  ? -55.007 -17.268 83.098  1.00 24.20 ?  36  ALA   A CB  1 
ATOM   5102 N  N   . PRO   D 1 42  ? -53.571 -15.302 85.258  1.00 19.07 ?  37  PRO   A N   1 
ATOM   5103 C  CA  . PRO   D 1 42  ? -53.509 -13.901 85.656  1.00 18.57 ?  37  PRO   A CA  1 
ATOM   5104 C  C   . PRO   D 1 42  ? -54.528 -12.988 84.960  1.00 19.46 ?  37  PRO   A C   1 
ATOM   5105 O  O   . PRO   D 1 42  ? -54.927 -13.172 83.796  1.00 18.75 ?  37  PRO   A O   1 
ATOM   5106 C  CB  . PRO   D 1 42  ? -52.061 -13.504 85.311  1.00 20.16 ?  37  PRO   A CB  1 
ATOM   5107 C  CG  . PRO   D 1 42  ? -51.304 -14.784 85.396  1.00 19.60 ?  37  PRO   A CG  1 
ATOM   5108 C  CD  . PRO   D 1 42  ? -52.249 -15.827 84.868  1.00 20.04 ?  37  PRO   A CD  1 
ATOM   5109 N  N   . HIS   D 1 43  ? -54.960 -11.972 85.708  1.00 21.14 ?  38  HIS   A N   1 
ATOM   5110 C  CA  . HIS   D 1 43  ? -55.636 -10.776 85.184  1.00 21.41 ?  38  HIS   A CA  1 
ATOM   5111 C  C   . HIS   D 1 43  ? -54.600 -9.911  84.488  1.00 18.48 ?  38  HIS   A C   1 
ATOM   5112 O  O   . HIS   D 1 43  ? -53.529 -9.699  85.062  1.00 22.73 ?  38  HIS   A O   1 
ATOM   5113 C  CB  . HIS   D 1 43  ? -56.247 -9.940  86.316  1.00 27.22 ?  38  HIS   A CB  1 
ATOM   5114 C  CG  . HIS   D 1 43  ? -57.364 -10.618 87.031  1.00 31.59 ?  38  HIS   A CG  1 
ATOM   5115 N  ND1 . HIS   D 1 43  ? -58.685 -10.343 86.735  1.00 39.72 ?  38  HIS   A ND1 1 
ATOM   5116 C  CD2 . HIS   D 1 43  ? -57.365 -11.462 88.078  1.00 37.03 ?  38  HIS   A CD2 1 
ATOM   5117 C  CE1 . HIS   D 1 43  ? -59.450 -11.062 87.528  1.00 38.60 ?  38  HIS   A CE1 1 
ATOM   5118 N  NE2 . HIS   D 1 43  ? -58.665 -11.755 88.352  1.00 36.88 ?  38  HIS   A NE2 1 
ATOM   5119 N  N   . ILE   D 1 44  ? -54.924 -9.408  83.307  1.00 19.18 ?  39  ILE   A N   1 
ATOM   5120 C  CA  . ILE   D 1 44  ? -54.022 -8.474  82.553  1.00 19.12 ?  39  ILE   A CA  1 
ATOM   5121 C  C   . ILE   D 1 44  ? -54.863 -7.287  82.109  1.00 18.55 ?  39  ILE   A C   1 
ATOM   5122 O  O   . ILE   D 1 44  ? -55.879 -7.499  81.413  1.00 19.39 ?  39  ILE   A O   1 
ATOM   5123 C  CB  . ILE   D 1 44  ? -53.374 -9.130  81.313  1.00 20.02 ?  39  ILE   A CB  1 
ATOM   5124 C  CG1 . ILE   D 1 44  ? -52.758 -10.491 81.591  1.00 21.27 ?  39  ILE   A CG1 1 
ATOM   5125 C  CG2 . ILE   D 1 44  ? -52.404 -8.183  80.656  1.00 23.53 ?  39  ILE   A CG2 1 
ATOM   5126 C  CD1 . ILE   D 1 44  ? -51.412 -10.434 82.242  1.00 21.02 ?  39  ILE   A CD1 1 
ATOM   5127 N  N   . THR   D 1 45  ? -54.441 -6.082  82.461  1.00 17.26 ?  40  THR   A N   1 
ATOM   5128 C  CA  . THR   D 1 45  ? -55.062 -4.831  81.971  1.00 18.64 ?  40  THR   A CA  1 
ATOM   5129 C  C   . THR   D 1 45  ? -53.983 -3.913  81.421  1.00 16.55 ?  40  THR   A C   1 
ATOM   5130 O  O   . THR   D 1 45  ? -52.938 -3.727  82.100  1.00 19.10 ?  40  THR   A O   1 
ATOM   5131 C  CB  . THR   D 1 45  ? -55.894 -4.155  83.060  1.00 19.38 ?  40  THR   A CB  1 
ATOM   5132 O  OG1 . THR   D 1 45  ? -56.869 -5.075  83.547  1.00 20.17 ?  40  THR   A OG1 1 
ATOM   5133 C  CG2 . THR   D 1 45  ? -56.609 -2.922  82.547  1.00 19.04 ?  40  THR   A CG2 1 
ATOM   5134 N  N   . HIS   D 1 46  ? -54.230 -3.344  80.237  1.00 17.46 ?  41  HIS   A N   1 
ATOM   5135 C  CA  . HIS   D 1 46  ? -53.470 -2.197  79.710  1.00 17.18 ?  41  HIS   A CA  1 
ATOM   5136 C  C   . HIS   D 1 46  ? -53.874 -0.914  80.449  1.00 17.34 ?  41  HIS   A C   1 
ATOM   5137 O  O   . HIS   D 1 46  ? -55.021 -0.490  80.323  1.00 18.96 ?  41  HIS   A O   1 
ATOM   5138 C  CB  . HIS   D 1 46  ? -53.609 -2.079  78.213  1.00 18.21 ?  41  HIS   A CB  1 
ATOM   5139 C  CG  . HIS   D 1 46  ? -53.191 -3.314  77.495  1.00 24.98 ?  41  HIS   A CG  1 
ATOM   5140 N  ND1 . HIS   D 1 46  ? -51.964 -3.445  76.913  1.00 29.02 ?  41  HIS   A ND1 1 
ATOM   5141 C  CD2 . HIS   D 1 46  ? -53.867 -4.463  77.269  1.00 31.07 ?  41  HIS   A CD2 1 
ATOM   5142 C  CE1 . HIS   D 1 46  ? -51.889 -4.628  76.343  1.00 28.23 ?  41  HIS   A CE1 1 
ATOM   5143 N  NE2 . HIS   D 1 46  ? -53.036 -5.290  76.566  1.00 34.34 ?  41  HIS   A NE2 1 
ATOM   5144 N  N   . VAL   D 1 47  ? -52.895 -0.294  81.089  1.00 17.72 ?  42  VAL   A N   1 
ATOM   5145 C  CA  . VAL   D 1 47  ? -53.104 0.893   81.966  1.00 17.12 ?  42  VAL   A CA  1 
ATOM   5146 C  C   . VAL   D 1 47  ? -51.988 1.891   81.734  1.00 17.12 ?  42  VAL   A C   1 
ATOM   5147 O  O   . VAL   D 1 47  ? -50.806 1.528   81.620  1.00 15.47 ?  42  VAL   A O   1 
ATOM   5148 C  CB  . VAL   D 1 47  ? -53.202 0.431   83.437  1.00 17.34 ?  42  VAL   A CB  1 
ATOM   5149 C  CG1 . VAL   D 1 47  ? -54.391 -0.484  83.690  1.00 18.80 ?  42  VAL   A CG1 1 
ATOM   5150 C  CG2 . VAL   D 1 47  ? -51.953 -0.267  83.906  1.00 17.96 ?  42  VAL   A CG2 1 
ATOM   5151 N  N   . PRO   D 1 48  ? -52.340 3.204   81.768  1.00 16.05 ?  43  PRO   A N   1 
ATOM   5152 C  CA  . PRO   D 1 48  ? -51.372 4.286   81.702  1.00 18.38 ?  43  PRO   A CA  1 
ATOM   5153 C  C   . PRO   D 1 48  ? -50.652 4.468   83.040  1.00 18.74 ?  43  PRO   A C   1 
ATOM   5154 O  O   . PRO   D 1 48  ? -51.329 4.708   84.034  1.00 18.74 ?  43  PRO   A O   1 
ATOM   5155 C  CB  . PRO   D 1 48  ? -52.228 5.520   81.359  1.00 17.08 ?  43  PRO   A CB  1 
ATOM   5156 C  CG  . PRO   D 1 48  ? -53.627 5.199   81.920  1.00 16.27 ?  43  PRO   A CG  1 
ATOM   5157 C  CD  . PRO   D 1 48  ? -53.732 3.675   81.956  1.00 16.10 ?  43  PRO   A CD  1 
ATOM   5158 N  N   . ILE   D 1 49  ? -49.319 4.345   83.005  1.00 18.65 ?  44  ILE   A N   1 
ATOM   5159 C  CA  . ILE   D 1 49  ? -48.458 4.425   84.218  1.00 19.21 ?  44  ILE   A CA  1 
ATOM   5160 C  C   . ILE   D 1 49  ? -47.321 5.418   83.971  1.00 20.22 ?  44  ILE   A C   1 
ATOM   5161 O  O   . ILE   D 1 49  ? -46.670 5.340   82.943  1.00 18.79 ?  44  ILE   A O   1 
ATOM   5162 C  CB  . ILE   D 1 49  ? -47.924 3.043   84.643  1.00 19.32 ?  44  ILE   A CB  1 
ATOM   5163 C  CG1 . ILE   D 1 49  ? -49.083 2.098   84.968  1.00 20.02 ?  44  ILE   A CG1 1 
ATOM   5164 C  CG2 . ILE   D 1 49  ? -46.964 3.169   85.814  1.00 18.74 ?  44  ILE   A CG2 1 
ATOM   5165 C  CD1 . ILE   D 1 49  ? -48.629 0.704   85.361  1.00 21.17 ?  44  ILE   A CD1 1 
ATOM   5166 N  N   . ILE   D 1 50  ? -47.147 6.333   84.927  1.00 20.83 ?  45  ILE   A N   1 
ATOM   5167 C  CA  . ILE   D 1 50  ? -46.110 7.387   84.891  1.00 20.50 ?  45  ILE   A CA  1 
ATOM   5168 C  C   . ILE   D 1 50  ? -45.240 7.310   86.127  1.00 22.13 ?  45  ILE   A C   1 
ATOM   5169 O  O   . ILE   D 1 50  ? -45.701 6.800   87.148  1.00 20.04 ?  45  ILE   A O   1 
ATOM   5170 C  CB  . ILE   D 1 50  ? -46.707 8.794   84.756  1.00 19.64 ?  45  ILE   A CB  1 
ATOM   5171 C  CG1 . ILE   D 1 50  ? -47.572 9.163   85.954  1.00 20.37 ?  45  ILE   A CG1 1 
ATOM   5172 C  CG2 . ILE   D 1 50  ? -47.399 8.927   83.397  1.00 20.84 ?  45  ILE   A CG2 1 
ATOM   5173 C  CD1 . ILE   D 1 50  ? -47.941 10.639  86.013  1.00 21.94 ?  45  ILE   A CD1 1 
ATOM   5174 N  N   . VAL   D 1 51  ? -44.027 7.851   85.996  1.00 22.84 ?  46  VAL   A N   1 
ATOM   5175 C  CA  . VAL   D 1 51  ? -43.122 8.084   87.152  1.00 23.92 ?  46  VAL   A CA  1 
ATOM   5176 C  C   . VAL   D 1 51  ? -43.714 9.203   88.031  1.00 24.39 ?  46  VAL   A C   1 
ATOM   5177 O  O   . VAL   D 1 51  ? -44.244 10.173  87.488  1.00 24.96 ?  46  VAL   A O   1 
ATOM   5178 C  CB  . VAL   D 1 51  ? -41.707 8.392   86.625  1.00 24.75 ?  46  VAL   A CB  1 
ATOM   5179 C  CG1 . VAL   D 1 51  ? -40.800 8.910   87.726  1.00 28.75 ?  46  VAL   A CG1 1 
ATOM   5180 C  CG2 . VAL   D 1 51  ? -41.111 7.181   85.940  1.00 24.78 ?  46  VAL   A CG2 1 
ATOM   5181 N  N   . ASP   D 1 52  ? -43.689 9.011   89.364  1.00 22.34 ?  47  ASP   A N   1 
ATOM   5182 C  CA  . ASP   D 1 52  ? -44.034 10.014  90.404  1.00 23.24 ?  47  ASP   A CA  1 
ATOM   5183 C  C   . ASP   D 1 52  ? -43.713 11.409  89.882  1.00 21.12 ?  47  ASP   A C   1 
ATOM   5184 O  O   . ASP   D 1 52  ? -42.546 11.745  89.727  1.00 23.12 ?  47  ASP   A O   1 
ATOM   5185 C  CB  . ASP   D 1 52  ? -43.257 9.744   91.700  1.00 27.35 ?  47  ASP   A CB  1 
ATOM   5186 C  CG  . ASP   D 1 52  ? -43.526 10.705  92.852  1.00 29.06 ?  47  ASP   A CG  1 
ATOM   5187 O  OD1 . ASP   D 1 52  ? -44.302 11.652  92.653  1.00 29.06 ?  47  ASP   A OD1 1 
ATOM   5188 O  OD2 . ASP   D 1 52  ? -43.014 10.456  93.984  1.00 29.68 -1 47  ASP   A OD2 1 
ATOM   5189 N  N   . PRO   D 1 53  ? -44.708 12.264  89.621  1.00 21.94 ?  48  PRO   A N   1 
ATOM   5190 C  CA  . PRO   D 1 53  ? -44.452 13.613  89.088  1.00 23.99 ?  48  PRO   A CA  1 
ATOM   5191 C  C   . PRO   D 1 53  ? -43.755 14.560  90.073  1.00 27.62 ?  48  PRO   A C   1 
ATOM   5192 O  O   . PRO   D 1 53  ? -43.262 15.586  89.634  1.00 28.28 ?  48  PRO   A O   1 
ATOM   5193 C  CB  . PRO   D 1 53  ? -45.865 14.116  88.770  1.00 26.40 ?  48  PRO   A CB  1 
ATOM   5194 C  CG  . PRO   D 1 53  ? -46.721 13.411  89.751  1.00 25.41 ?  48  PRO   A CG  1 
ATOM   5195 C  CD  . PRO   D 1 53  ? -46.141 12.012  89.828  1.00 25.10 ?  48  PRO   A CD  1 
ATOM   5196 N  N   . GLU   D 1 54  ? -43.673 14.179  91.350  1.00 29.67 ?  49  GLU   A N   1 
ATOM   5197 C  CA  . GLU   D 1 54  ? -43.098 15.043  92.416  1.00 31.62 ?  49  GLU   A CA  1 
ATOM   5198 C  C   . GLU   D 1 54  ? -41.581 14.834  92.541  1.00 32.60 ?  49  GLU   A C   1 
ATOM   5199 O  O   . GLU   D 1 54  ? -41.006 15.572  93.329  1.00 28.98 ?  49  GLU   A O   1 
ATOM   5200 C  CB  . GLU   D 1 54  ? -43.824 14.830  93.743  1.00 35.90 ?  49  GLU   A CB  1 
ATOM   5201 C  CG  . GLU   D 1 54  ? -45.334 15.020  93.681  1.00 37.06 ?  49  GLU   A CG  1 
ATOM   5202 C  CD  . GLU   D 1 54  ? -45.801 16.415  93.271  1.00 46.23 ?  49  GLU   A CD  1 
ATOM   5203 O  OE1 . GLU   D 1 54  ? -45.103 17.408  93.627  1.00 46.68 ?  49  GLU   A OE1 1 
ATOM   5204 O  OE2 . GLU   D 1 54  ? -46.865 16.514  92.592  1.00 41.49 -1 49  GLU   A OE2 1 
ATOM   5205 N  N   . LEU   D 1 55  ? -40.945 13.939  91.763  1.00 30.76 ?  50  LEU   A N   1 
ATOM   5206 C  CA  . LEU   D 1 55  ? -39.464 13.700  91.830  1.00 35.03 ?  50  LEU   A CA  1 
ATOM   5207 C  C   . LEU   D 1 55  ? -38.702 14.843  91.150  1.00 38.49 ?  50  LEU   A C   1 
ATOM   5208 O  O   . LEU   D 1 55  ? -39.076 15.242  90.056  1.00 39.24 ?  50  LEU   A O   1 
ATOM   5209 C  CB  . LEU   D 1 55  ? -39.114 12.348  91.196  1.00 35.69 ?  50  LEU   A CB  1 
ATOM   5210 C  CG  . LEU   D 1 55  ? -39.800 11.152  91.840  1.00 36.52 ?  50  LEU   A CG  1 
ATOM   5211 C  CD1 . LEU   D 1 55  ? -39.401 9.877   91.126  1.00 36.05 ?  50  LEU   A CD1 1 
ATOM   5212 C  CD2 . LEU   D 1 55  ? -39.481 11.049  93.331  1.00 36.66 ?  50  LEU   A CD2 1 
ATOM   5213 N  N   . ASP   D 1 56  ? -37.676 15.372  91.805  1.00 51.57 ?  51  ASP   A N   1 
ATOM   5214 C  CA  . ASP   D 1 56  ? -36.849 16.486  91.266  1.00 58.30 ?  51  ASP   A CA  1 
ATOM   5215 C  C   . ASP   D 1 56  ? -35.463 15.941  90.914  1.00 61.78 ?  51  ASP   A C   1 
ATOM   5216 O  O   . ASP   D 1 56  ? -35.038 14.941  91.533  1.00 63.22 ?  51  ASP   A O   1 
ATOM   5217 C  CB  . ASP   D 1 56  ? -36.771 17.649  92.261  1.00 65.68 ?  51  ASP   A CB  1 
ATOM   5218 C  CG  . ASP   D 1 56  ? -38.114 18.312  92.524  1.00 69.97 ?  51  ASP   A CG  1 
ATOM   5219 O  OD1 . ASP   D 1 56  ? -38.617 18.994  91.601  1.00 59.76 ?  51  ASP   A OD1 1 
ATOM   5220 O  OD2 . ASP   D 1 56  ? -38.660 18.124  93.641  1.00 73.93 -1 51  ASP   A OD2 1 
ATOM   5221 N  N   . GLY   D 1 57  ? -34.782 16.585  89.965  1.00 64.23 ?  52  GLY   A N   1 
ATOM   5222 C  CA  . GLY   D 1 57  ? -33.433 16.177  89.527  1.00 60.80 ?  52  GLY   A CA  1 
ATOM   5223 C  C   . GLY   D 1 57  ? -33.501 14.802  88.875  1.00 62.43 ?  52  GLY   A C   1 
ATOM   5224 O  O   . GLY   D 1 57  ? -34.597 14.236  88.763  1.00 55.92 ?  52  GLY   A O   1 
ATOM   5225 N  N   . PRO   D 1 58  ? -32.344 14.231  88.459  1.00 57.43 ?  53  PRO   A N   1 
ATOM   5226 C  CA  . PRO   D 1 58  ? -32.324 13.149  87.471  1.00 57.38 ?  53  PRO   A CA  1 
ATOM   5227 C  C   . PRO   D 1 58  ? -32.894 11.855  88.072  1.00 45.38 ?  53  PRO   A C   1 
ATOM   5228 O  O   . PRO   D 1 58  ? -32.654 11.600  89.241  1.00 48.39 ?  53  PRO   A O   1 
ATOM   5229 C  CB  . PRO   D 1 58  ? -30.831 13.006  87.094  1.00 61.18 ?  53  PRO   A CB  1 
ATOM   5230 C  CG  . PRO   D 1 58  ? -30.129 14.192  87.743  1.00 57.64 ?  53  PRO   A CG  1 
ATOM   5231 C  CD  . PRO   D 1 58  ? -30.993 14.578  88.925  1.00 58.98 ?  53  PRO   A CD  1 
ATOM   5232 N  N   . VAL   D 1 59  ? -33.689 11.102  87.308  1.00 39.53 ?  54  VAL   A N   1 
ATOM   5233 C  CA  . VAL   D 1 59  ? -34.265 9.815   87.798  1.00 35.34 ?  54  VAL   A CA  1 
ATOM   5234 C  C   . VAL   D 1 59  ? -33.497 8.708   87.072  1.00 30.47 ?  54  VAL   A C   1 
ATOM   5235 O  O   . VAL   D 1 59  ? -33.730 8.533   85.898  1.00 30.53 ?  54  VAL   A O   1 
ATOM   5236 C  CB  . VAL   D 1 59  ? -35.799 9.756   87.606  1.00 35.36 ?  54  VAL   A CB  1 
ATOM   5237 C  CG1 . VAL   D 1 59  ? -36.382 8.434   88.069  1.00 35.58 ?  54  VAL   A CG1 1 
ATOM   5238 C  CG2 . VAL   D 1 59  ? -36.490 10.909  88.329  1.00 38.46 ?  54  VAL   A CG2 1 
ATOM   5239 N  N   . ASP   D 1 60  ? -32.532 8.066   87.716  1.00 32.33 ?  55  ASP   A N   1 
ATOM   5240 C  CA  . ASP   D 1 60  ? -31.667 7.062   87.033  1.00 34.74 ?  55  ASP   A CA  1 
ATOM   5241 C  C   . ASP   D 1 60  ? -32.125 5.631   87.331  1.00 31.86 ?  55  ASP   A C   1 
ATOM   5242 O  O   . ASP   D 1 60  ? -31.797 4.727   86.546  1.00 33.36 ?  55  ASP   A O   1 
ATOM   5243 C  CB  . ASP   D 1 60  ? -30.186 7.289   87.366  1.00 40.72 ?  55  ASP   A CB  1 
ATOM   5244 C  CG  . ASP   D 1 60  ? -29.658 8.621   86.857  1.00 49.10 ?  55  ASP   A CG  1 
ATOM   5245 O  OD1 . ASP   D 1 60  ? -30.104 9.062   85.769  1.00 49.07 ?  55  ASP   A OD1 1 
ATOM   5246 O  OD2 . ASP   D 1 60  ? -28.825 9.228   87.559  1.00 61.21 -1 55  ASP   A OD2 1 
ATOM   5247 N  N   . ARG   D 1 61  ? -32.826 5.391   88.426  1.00 29.98 ?  56  ARG   A N   1 
ATOM   5248 C  CA  . ARG   D 1 61  ? -33.136 4.021   88.867  1.00 33.59 ?  56  ARG   A CA  1 
ATOM   5249 C  C   . ARG   D 1 61  ? -34.632 3.958   89.105  1.00 29.35 ?  56  ARG   A C   1 
ATOM   5250 O  O   . ARG   D 1 61  ? -35.172 4.874   89.733  1.00 31.66 ?  56  ARG   A O   1 
ATOM   5251 C  CB  . ARG   D 1 61  ? -32.380 3.634   90.145  1.00 39.74 ?  56  ARG   A CB  1 
ATOM   5252 C  CG  . ARG   D 1 61  ? -30.944 3.183   89.902  1.00 47.33 ?  56  ARG   A CG  1 
ATOM   5253 C  CD  . ARG   D 1 61  ? -30.094 3.140   91.164  1.00 55.00 ?  56  ARG   A CD  1 
ATOM   5254 N  NE  . ARG   D 1 61  ? -30.165 4.406   91.895  1.00 67.26 ?  56  ARG   A NE  1 
ATOM   5255 C  CZ  . ARG   D 1 61  ? -29.491 5.527   91.594  1.00 70.83 ?  56  ARG   A CZ  1 
ATOM   5256 N  NH1 . ARG   D 1 61  ? -29.668 6.613   92.332  1.00 73.42 1  56  ARG   A NH1 1 
ATOM   5257 N  NH2 . ARG   D 1 61  ? -28.649 5.569   90.570  1.00 63.92 ?  56  ARG   A NH2 1 
ATOM   5258 N  N   . LEU   D 1 62  ? -35.269 2.873   88.688  1.00 27.02 ?  57  LEU   A N   1 
ATOM   5259 C  CA  . LEU   D 1 62  ? -36.710 2.658   88.999  1.00 23.08 ?  57  LEU   A CA  1 
ATOM   5260 C  C   . LEU   D 1 62  ? -36.882 2.141   90.433  1.00 24.18 ?  57  LEU   A C   1 
ATOM   5261 O  O   . LEU   D 1 62  ? -37.911 2.437   91.059  1.00 25.36 ?  57  LEU   A O   1 
ATOM   5262 C  CB  . LEU   D 1 62  ? -37.289 1.643   88.005  1.00 26.02 ?  57  LEU   A CB  1 
ATOM   5263 C  CG  . LEU   D 1 62  ? -37.551 2.165   86.603  1.00 23.68 ?  57  LEU   A CG  1 
ATOM   5264 C  CD1 . LEU   D 1 62  ? -37.885 0.995   85.654  1.00 22.90 ?  57  LEU   A CD1 1 
ATOM   5265 C  CD2 . LEU   D 1 62  ? -38.679 3.190   86.636  1.00 24.83 ?  57  LEU   A CD2 1 
ATOM   5266 N  N   . VAL   D 1 63  ? -35.968 1.307   90.922  1.00 26.28 ?  58  VAL   A N   1 
ATOM   5267 C  CA  . VAL   D 1 63  ? -36.156 0.647   92.251  1.00 28.53 ?  58  VAL   A CA  1 
ATOM   5268 C  C   . VAL   D 1 63  ? -36.235 1.738   93.324  1.00 26.91 ?  58  VAL   A C   1 
ATOM   5269 O  O   . VAL   D 1 63  ? -35.308 2.570   93.374  1.00 29.36 ?  58  VAL   A O   1 
ATOM   5270 C  CB  . VAL   D 1 63  ? -35.049 -0.372  92.575  1.00 28.97 ?  58  VAL   A CB  1 
ATOM   5271 C  CG1 . VAL   D 1 63  ? -35.098 -0.802  94.044  1.00 29.78 ?  58  VAL   A CG1 1 
ATOM   5272 C  CG2 . VAL   D 1 63  ? -35.159 -1.602  91.671  1.00 29.73 ?  58  VAL   A CG2 1 
ATOM   5273 N  N   . GLY   D 1 64  ? -37.292 1.722   94.126  1.00 26.18 ?  59  GLY   A N   1 
ATOM   5274 C  CA  . GLY   D 1 64  ? -37.501 2.686   95.216  1.00 29.17 ?  59  GLY   A CA  1 
ATOM   5275 C  C   . GLY   D 1 64  ? -38.340 3.876   94.822  1.00 30.94 ?  59  GLY   A C   1 
ATOM   5276 O  O   . GLY   D 1 64  ? -38.699 4.639   95.733  1.00 37.14 ?  59  GLY   A O   1 
ATOM   5277 N  N   . ILE   D 1 65  ? -38.667 4.065   93.540  1.00 25.57 ?  60  ILE   A N   1 
ATOM   5278 C  CA  . ILE   D 1 65  ? -39.619 5.149   93.191  1.00 27.27 ?  60  ILE   A CA  1 
ATOM   5279 C  C   . ILE   D 1 65  ? -41.028 4.568   93.165  1.00 24.38 ?  60  ILE   A C   1 
ATOM   5280 O  O   . ILE   D 1 65  ? -41.213 3.327   93.102  1.00 25.69 ?  60  ILE   A O   1 
ATOM   5281 C  CB  . ILE   D 1 65  ? -39.261 5.885   91.896  1.00 28.25 ?  60  ILE   A CB  1 
ATOM   5282 C  CG1 . ILE   D 1 65  ? -39.496 5.037   90.652  1.00 31.82 ?  60  ILE   A CG1 1 
ATOM   5283 C  CG2 . ILE   D 1 65  ? -37.857 6.446   91.946  1.00 26.62 ?  60  ILE   A CG2 1 
ATOM   5284 C  CD1 . ILE   D 1 65  ? -39.129 5.754   89.363  1.00 35.57 ?  60  ILE   A CD1 1 
ATOM   5285 N  N   . THR   D 1 66  ? -41.975 5.468   93.239  1.00 23.65 ?  61  THR   A N   1 
ATOM   5286 C  CA  . THR   D 1 66  ? -43.413 5.142   93.184  1.00 24.31 ?  61  THR   A CA  1 
ATOM   5287 C  C   . THR   D 1 66  ? -43.902 5.477   91.781  1.00 24.28 ?  61  THR   A C   1 
ATOM   5288 O  O   . THR   D 1 66  ? -43.664 6.590   91.307  1.00 25.32 ?  61  THR   A O   1 
ATOM   5289 C  CB  . THR   D 1 66  ? -44.199 5.834   94.289  1.00 26.86 ?  61  THR   A CB  1 
ATOM   5290 O  OG1 . THR   D 1 66  ? -43.603 5.362   95.499  1.00 31.28 ?  61  THR   A OG1 1 
ATOM   5291 C  CG2 . THR   D 1 66  ? -45.664 5.459   94.241  1.00 27.95 ?  61  THR   A CG2 1 
ATOM   5292 N  N   . LEU   D 1 67  ? -44.589 4.532   91.159  1.00 22.69 ?  62  LEU   A N   1 
ATOM   5293 C  CA  . LEU   D 1 67  ? -45.285 4.784   89.893  1.00 21.07 ?  62  LEU   A CA  1 
ATOM   5294 C  C   . LEU   D 1 67  ? -46.756 5.052   90.160  1.00 18.21 ?  62  LEU   A C   1 
ATOM   5295 O  O   . LEU   D 1 67  ? -47.358 4.523   91.080  1.00 20.38 ?  62  LEU   A O   1 
ATOM   5296 C  CB  . LEU   D 1 67  ? -45.120 3.624   88.889  1.00 19.04 ?  62  LEU   A CB  1 
ATOM   5297 C  CG  . LEU   D 1 67  ? -43.700 3.179   88.626  1.00 20.85 ?  62  LEU   A CG  1 
ATOM   5298 C  CD1 . LEU   D 1 67  ? -43.739 1.944   87.719  1.00 22.12 ?  62  LEU   A CD1 1 
ATOM   5299 C  CD2 . LEU   D 1 67  ? -42.853 4.301   88.054  1.00 20.28 ?  62  LEU   A CD2 1 
ATOM   5300 N  N   . TRP   D 1 68  ? -47.293 5.945   89.361  1.00 18.53 ?  63  TRP   A N   1 
ATOM   5301 C  CA  . TRP   D 1 68  ? -48.720 6.352   89.423  1.00 17.74 ?  63  TRP   A CA  1 
ATOM   5302 C  C   . TRP   D 1 68  ? -49.460 5.758   88.227  1.00 19.50 ?  63  TRP   A C   1 
ATOM   5303 O  O   . TRP   D 1 68  ? -48.953 5.857   87.116  1.00 18.81 ?  63  TRP   A O   1 
ATOM   5304 C  CB  . TRP   D 1 68  ? -48.843 7.872   89.343  1.00 19.05 ?  63  TRP   A CB  1 
ATOM   5305 C  CG  . TRP   D 1 68  ? -48.369 8.612   90.553  1.00 20.46 ?  63  TRP   A CG  1 
ATOM   5306 C  CD1 . TRP   D 1 68  ? -47.436 8.239   91.481  1.00 21.47 ?  63  TRP   A CD1 1 
ATOM   5307 C  CD2 . TRP   D 1 68  ? -48.808 9.923   90.918  1.00 21.99 ?  63  TRP   A CD2 1 
ATOM   5308 N  NE1 . TRP   D 1 68  ? -47.303 9.227   92.433  1.00 23.75 ?  63  TRP   A NE1 1 
ATOM   5309 C  CE2 . TRP   D 1 68  ? -48.109 10.279  92.096  1.00 22.56 ?  63  TRP   A CE2 1 
ATOM   5310 C  CE3 . TRP   D 1 68  ? -49.689 10.834  90.331  1.00 22.14 ?  63  TRP   A CE3 1 
ATOM   5311 C  CZ2 . TRP   D 1 68  ? -48.310 11.523  92.711  1.00 23.42 ?  63  TRP   A CZ2 1 
ATOM   5312 C  CZ3 . TRP   D 1 68  ? -49.889 12.056  90.930  1.00 24.52 ?  63  TRP   A CZ3 1 
ATOM   5313 C  CH2 . TRP   D 1 68  ? -49.218 12.374  92.120  1.00 26.30 ?  63  TRP   A CH2 1 
ATOM   5314 N  N   . GLY   D 1 69  ? -50.719 5.339   88.408  1.00 17.70 ?  64  GLY   A N   1 
ATOM   5315 C  CA  . GLY   D 1 69  ? -51.466 4.776   87.276  1.00 17.42 ?  64  GLY   A CA  1 
ATOM   5316 C  C   . GLY   D 1 69  ? -52.926 4.712   87.582  1.00 17.28 ?  64  GLY   A C   1 
ATOM   5317 O  O   . GLY   D 1 69  ? -53.308 5.065   88.737  1.00 17.67 ?  64  GLY   A O   1 
ATOM   5318 N  N   . HIS   D 1 70  ? -53.744 4.438   86.577  1.00 17.62 ?  65  HIS   A N   1 
ATOM   5319 C  CA  . HIS   D 1 70  ? -55.206 4.283   86.791  1.00 17.71 ?  65  HIS   A CA  1 
ATOM   5320 C  C   . HIS   D 1 70  ? -55.750 3.221   85.848  1.00 22.35 ?  65  HIS   A C   1 
ATOM   5321 O  O   . HIS   D 1 70  ? -55.125 2.904   84.860  1.00 19.91 ?  65  HIS   A O   1 
ATOM   5322 C  CB  . HIS   D 1 70  ? -56.024 5.554   86.675  1.00 18.50 ?  65  HIS   A CB  1 
ATOM   5323 C  CG  . HIS   D 1 70  ? -56.212 6.129   85.327  1.00 16.41 ?  65  HIS   A CG  1 
ATOM   5324 N  ND1 . HIS   D 1 70  ? -55.219 6.846   84.672  1.00 18.07 ?  65  HIS   A ND1 1 
ATOM   5325 C  CD2 . HIS   D 1 70  ? -57.289 6.154   84.523  1.00 18.16 ?  65  HIS   A CD2 1 
ATOM   5326 C  CE1 . HIS   D 1 70  ? -55.723 7.264   83.501  1.00 17.36 ?  65  HIS   A CE1 1 
ATOM   5327 N  NE2 . HIS   D 1 70  ? -56.990 6.813   83.371  1.00 15.57 ?  65  HIS   A NE2 1 
ATOM   5328 N  N   . MET   D 1 71  ? -56.917 2.707   86.217  1.00 20.67 ?  66  MET   A N   1 
ATOM   5329 C  CA  . MET   D 1 71  ? -57.673 1.734   85.438  1.00 20.62 ?  66  MET   A CA  1 
ATOM   5330 C  C   . MET   D 1 71  ? -59.138 2.025   85.733  1.00 19.36 ?  66  MET   A C   1 
ATOM   5331 O  O   . MET   D 1 71  ? -59.436 3.000   86.460  1.00 20.99 ?  66  MET   A O   1 
ATOM   5332 C  CB  . MET   D 1 71  ? -57.309 0.296   85.791  1.00 23.39 ?  66  MET   A CB  1 
ATOM   5333 C  CG  . MET   D 1 71  ? -57.793 -0.138  87.144  1.00 23.95 ?  66  MET   A CG  1 
ATOM   5334 S  SD  . MET   D 1 71  ? -57.709 -1.938  87.347  1.00 31.69 ?  66  MET   A SD  1 
ATOM   5335 C  CE  . MET   D 1 71  ? -55.966 -1.948  87.710  1.00 28.59 ?  66  MET   A CE  1 
ATOM   5336 N  N   . ASN   D 1 72  ? -60.012 1.325   85.043  1.00 19.08 ?  67  ASN   A N   1 
ATOM   5337 C  CA  . ASN   D 1 72  ? -61.479 1.434   85.215  1.00 18.57 ?  67  ASN   A CA  1 
ATOM   5338 C  C   . ASN   D 1 72  ? -61.896 0.688   86.486  1.00 20.14 ?  67  ASN   A C   1 
ATOM   5339 O  O   . ASN   D 1 72  ? -61.623 -0.497  86.614  1.00 21.34 ?  67  ASN   A O   1 
ATOM   5340 C  CB  . ASN   D 1 72  ? -62.153 0.896   83.961  1.00 19.29 ?  67  ASN   A CB  1 
ATOM   5341 C  CG  . ASN   D 1 72  ? -63.647 1.110   83.933  1.00 22.87 ?  67  ASN   A CG  1 
ATOM   5342 O  OD1 . ASN   D 1 72  ? -64.231 1.481   84.952  1.00 25.48 ?  67  ASN   A OD1 1 
ATOM   5343 N  ND2 . ASN   D 1 72  ? -64.217 1.017   82.744  1.00 24.53 ?  67  ASN   A ND2 1 
ATOM   5344 N  N   . ARG   D 1 73  ? -62.525 1.374   87.437  1.00 24.20 ?  68  ARG   A N   1 
ATOM   5345 C  CA  . ARG   D 1 73  ? -63.057 0.743   88.670  1.00 27.40 ?  68  ARG   A CA  1 
ATOM   5346 C  C   . ARG   D 1 73  ? -64.044 -0.369  88.342  1.00 28.64 ?  68  ARG   A C   1 
ATOM   5347 O  O   . ARG   D 1 73  ? -64.195 -1.290  89.184  1.00 29.68 ?  68  ARG   A O   1 
ATOM   5348 C  CB  . ARG   D 1 73  ? -63.776 1.797   89.514  1.00 31.46 ?  68  ARG   A CB  1 
ATOM   5349 C  CG  . ARG   D 1 73  ? -62.966 2.233   90.703  1.00 32.66 ?  68  ARG   A CG  1 
ATOM   5350 C  CD  . ARG   D 1 73  ? -63.695 3.250   91.530  1.00 34.59 ?  68  ARG   A CD  1 
ATOM   5351 N  NE  . ARG   D 1 73  ? -62.644 3.982   92.177  1.00 34.97 ?  68  ARG   A NE  1 
ATOM   5352 C  CZ  . ARG   D 1 73  ? -62.168 3.712   93.376  1.00 37.09 ?  68  ARG   A CZ  1 
ATOM   5353 N  NH1 . ARG   D 1 73  ? -62.704 2.741   94.102  1.00 41.93 1  68  ARG   A NH1 1 
ATOM   5354 N  NH2 . ARG   D 1 73  ? -61.206 4.469   93.873  1.00 32.79 ?  68  ARG   A NH2 1 
ATOM   5355 N  N   . ALA   D 1 74  ? -64.685 -0.329  87.182  1.00 26.52 ?  69  ALA   A N   1 
ATOM   5356 C  CA  . ALA   D 1 74  ? -65.675 -1.346  86.764  1.00 29.56 ?  69  ALA   A CA  1 
ATOM   5357 C  C   . ALA   D 1 74  ? -64.975 -2.582  86.200  1.00 28.20 ?  69  ALA   A C   1 
ATOM   5358 O  O   . ALA   D 1 74  ? -65.622 -3.612  86.001  1.00 28.56 ?  69  ALA   A O   1 
ATOM   5359 C  CB  . ALA   D 1 74  ? -66.612 -0.770  85.745  1.00 31.17 ?  69  ALA   A CB  1 
ATOM   5360 N  N   . ASN   D 1 75  ? -63.683 -2.478  85.895  1.00 25.82 ?  70  ASN   A N   1 
ATOM   5361 C  CA  . ASN   D 1 75  ? -62.885 -3.625  85.438  1.00 21.49 ?  70  ASN   A CA  1 
ATOM   5362 C  C   . ASN   D 1 75  ? -62.828 -4.594  86.605  1.00 21.63 ?  70  ASN   A C   1 
ATOM   5363 O  O   . ASN   D 1 75  ? -62.382 -4.215  87.663  1.00 23.63 ?  70  ASN   A O   1 
ATOM   5364 C  CB  . ASN   D 1 75  ? -61.477 -3.149  85.083  1.00 23.37 ?  70  ASN   A CB  1 
ATOM   5365 C  CG  . ASN   D 1 75  ? -60.603 -4.220  84.486  1.00 22.30 ?  70  ASN   A CG  1 
ATOM   5366 O  OD1 . ASN   D 1 75  ? -60.789 -5.410  84.740  1.00 22.25 ?  70  ASN   A OD1 1 
ATOM   5367 N  ND2 . ASN   D 1 75  ? -59.657 -3.786  83.664  1.00 20.61 ?  70  ASN   A ND2 1 
ATOM   5368 N  N   . PRO   D 1 76  ? -63.259 -5.867  86.469  1.00 22.99 ?  71  PRO   A N   1 
ATOM   5369 C  CA  . PRO   D 1 76  ? -63.121 -6.852  87.560  1.00 22.09 ?  71  PRO   A CA  1 
ATOM   5370 C  C   . PRO   D 1 76  ? -61.726 -6.981  88.147  1.00 21.53 ?  71  PRO   A C   1 
ATOM   5371 O  O   . PRO   D 1 76  ? -61.546 -7.392  89.279  1.00 23.34 ?  71  PRO   A O   1 
ATOM   5372 C  CB  . PRO   D 1 76  ? -63.496 -8.190  86.876  1.00 23.83 ?  71  PRO   A CB  1 
ATOM   5373 C  CG  . PRO   D 1 76  ? -64.375 -7.794  85.723  1.00 27.17 ?  71  PRO   A CG  1 
ATOM   5374 C  CD  . PRO   D 1 76  ? -63.871 -6.429  85.271  1.00 25.23 ?  71  PRO   A CD  1 
ATOM   5375 N  N   . HIS   D 1 77  ? -60.726 -6.595  87.365  1.00 21.94 ?  72  HIS   A N   1 
ATOM   5376 C  CA  . HIS   D 1 77  ? -59.322 -6.628  87.821  1.00 19.43 ?  72  HIS   A CA  1 
ATOM   5377 C  C   . HIS   D 1 77  ? -59.221 -5.732  89.065  1.00 19.62 ?  72  HIS   A C   1 
ATOM   5378 O  O   . HIS   D 1 77  ? -58.487 -6.076  90.002  1.00 22.38 ?  72  HIS   A O   1 
ATOM   5379 C  CB  . HIS   D 1 77  ? -58.424 -6.258  86.641  1.00 19.46 ?  72  HIS   A CB  1 
ATOM   5380 C  CG  . HIS   D 1 77  ? -56.963 -6.489  86.876  1.00 20.23 ?  72  HIS   A CG  1 
ATOM   5381 N  ND1 . HIS   D 1 77  ? -56.035 -6.321  85.868  1.00 19.70 ?  72  HIS   A ND1 1 
ATOM   5382 C  CD2 . HIS   D 1 77  ? -56.289 -7.011  87.911  1.00 19.38 ?  72  HIS   A CD2 1 
ATOM   5383 C  CE1 . HIS   D 1 77  ? -54.841 -6.568  86.335  1.00 20.23 ?  72  HIS   A CE1 1 
ATOM   5384 N  NE2 . HIS   D 1 77  ? -54.968 -7.011  87.576  1.00 20.60 ?  72  HIS   A NE2 1 
ATOM   5385 N  N   . TRP   D 1 78  ? -59.943 -4.615  89.072  1.00 20.51 ?  73  TRP   A N   1 
ATOM   5386 C  CA  . TRP   D 1 78  ? -59.858 -3.641  90.204  1.00 22.10 ?  73  TRP   A CA  1 
ATOM   5387 C  C   . TRP   D 1 78  ? -60.253 -4.324  91.523  1.00 21.90 ?  73  TRP   A C   1 
ATOM   5388 O  O   . TRP   D 1 78  ? -59.492 -4.267  92.464  1.00 23.39 ?  73  TRP   A O   1 
ATOM   5389 C  CB  . TRP   D 1 78  ? -60.704 -2.416  89.899  1.00 23.46 ?  73  TRP   A CB  1 
ATOM   5390 C  CG  . TRP   D 1 78  ? -60.735 -1.433  91.027  1.00 25.15 ?  73  TRP   A CG  1 
ATOM   5391 C  CD1 . TRP   D 1 78  ? -61.763 -1.238  91.900  1.00 23.97 ?  73  TRP   A CD1 1 
ATOM   5392 C  CD2 . TRP   D 1 78  ? -59.691 -0.525  91.416  1.00 23.48 ?  73  TRP   A CD2 1 
ATOM   5393 N  NE1 . TRP   D 1 78  ? -61.441 -0.263  92.794  1.00 24.42 ?  73  TRP   A NE1 1 
ATOM   5394 C  CE2 . TRP   D 1 78  ? -60.186 0.202   92.526  1.00 25.63 ?  73  TRP   A CE2 1 
ATOM   5395 C  CE3 . TRP   D 1 78  ? -58.406 -0.234  90.950  1.00 24.29 ?  73  TRP   A CE3 1 
ATOM   5396 C  CZ2 . TRP   D 1 78  ? -59.470 1.225   93.132  1.00 24.91 ?  73  TRP   A CZ2 1 
ATOM   5397 C  CZ3 . TRP   D 1 78  ? -57.691 0.775   91.556  1.00 24.77 ?  73  TRP   A CZ3 1 
ATOM   5398 C  CH2 . TRP   D 1 78  ? -58.196 1.473   92.658  1.00 24.70 ?  73  TRP   A CH2 1 
ATOM   5399 N  N   . ALA   D 1 79  ? -61.392 -5.014  91.547  1.00 25.91 ?  74  ALA   A N   1 
ATOM   5400 C  CA  . ALA   D 1 79  ? -61.880 -5.771  92.734  1.00 26.70 ?  74  ALA   A CA  1 
ATOM   5401 C  C   . ALA   D 1 79  ? -60.878 -6.873  93.071  1.00 31.19 ?  74  ALA   A C   1 
ATOM   5402 O  O   . ALA   D 1 79  ? -60.604 -7.121  94.253  1.00 31.47 ?  74  ALA   A O   1 
ATOM   5403 C  CB  . ALA   D 1 79  ? -63.271 -6.292  92.440  1.00 27.52 ?  74  ALA   A CB  1 
ATOM   5404 N  N   . ALA   D 1 80  ? -60.280 -7.493  92.058  1.00 29.74 ?  75  ALA   A N   1 
ATOM   5405 C  CA  . ALA   D 1 80  ? -59.422 -8.683  92.245  1.00 30.41 ?  75  ALA   A CA  1 
ATOM   5406 C  C   . ALA   D 1 80  ? -58.122 -8.260  92.912  1.00 31.00 ?  75  ALA   A C   1 
ATOM   5407 O  O   . ALA   D 1 80  ? -57.517 -9.081  93.623  1.00 35.63 ?  75  ALA   A O   1 
ATOM   5408 C  CB  . ALA   D 1 80  ? -59.203 -9.389  90.925  1.00 30.31 ?  75  ALA   A CB  1 
ATOM   5409 N  N   . LEU   D 1 81  ? -57.722 -7.000  92.773  1.00 30.98 ?  76  LEU   A N   1 
ATOM   5410 C  CA  . LEU   D 1 81  ? -56.446 -6.537  93.372  1.00 35.12 ?  76  LEU   A CA  1 
ATOM   5411 C  C   . LEU   D 1 81  ? -56.611 -6.431  94.896  1.00 45.25 ?  76  LEU   A C   1 
ATOM   5412 O  O   . LEU   D 1 81  ? -55.576 -6.405  95.589  1.00 43.59 ?  76  LEU   A O   1 
ATOM   5413 C  CB  . LEU   D 1 81  ? -56.025 -5.204  92.749  1.00 32.70 ?  76  LEU   A CB  1 
ATOM   5414 C  CG  . LEU   D 1 81  ? -55.514 -5.327  91.310  1.00 26.60 ?  76  LEU   A CG  1 
ATOM   5415 C  CD1 . LEU   D 1 81  ? -55.680 -4.024  90.591  1.00 26.42 ?  76  LEU   A CD1 1 
ATOM   5416 C  CD2 . LEU   D 1 81  ? -54.067 -5.821  91.264  1.00 27.91 ?  76  LEU   A CD2 1 
ATOM   5417 N  N   . GLY   D 1 82  ? -57.858 -6.350  95.384  1.00 44.72 ?  77  GLY   A N   1 
ATOM   5418 C  CA  . GLY   D 1 82  ? -58.158 -6.283  96.826  1.00 54.35 ?  77  GLY   A CA  1 
ATOM   5419 C  C   . GLY   D 1 82  ? -57.357 -5.174  97.485  1.00 62.77 ?  77  GLY   A C   1 
ATOM   5420 O  O   . GLY   D 1 82  ? -57.502 -4.017  97.045  1.00 68.46 ?  77  GLY   A O   1 
ATOM   5421 N  N   . GLY   D 1 83  ? -56.515 -5.512  98.469  1.00 66.18 ?  78  GLY   A N   1 
ATOM   5422 C  CA  . GLY   D 1 83  ? -55.695 -4.544  99.220  1.00 66.22 ?  78  GLY   A CA  1 
ATOM   5423 C  C   . GLY   D 1 83  ? -54.303 -4.413  98.625  1.00 71.59 ?  78  GLY   A C   1 
ATOM   5424 O  O   . GLY   D 1 83  ? -54.140 -3.658  97.640  1.00 85.88 ?  78  GLY   A O   1 
ATOM   5425 N  N   . ALA   D 1 84  ? -53.346 -5.156  99.182  1.00 66.53 ?  79  ALA   A N   1 
ATOM   5426 C  CA  . ALA   D 1 84  ? -51.893 -5.038  98.920  1.00 63.06 ?  79  ALA   A CA  1 
ATOM   5427 C  C   . ALA   D 1 84  ? -51.447 -6.147  97.957  1.00 56.24 ?  79  ALA   A C   1 
ATOM   5428 O  O   . ALA   D 1 84  ? -50.634 -7.017  98.374  1.00 55.05 ?  79  ALA   A O   1 
ATOM   5429 C  CB  . ALA   D 1 84  ? -51.142 -5.109  100.230 1.00 67.39 ?  79  ALA   A CB  1 
ATOM   5430 N  N   . ALA   D 1 85  ? -51.933 -6.103  96.711  1.00 43.67 ?  80  ALA   A N   1 
ATOM   5431 C  CA  . ALA   D 1 85  ? -51.633 -7.116  95.665  1.00 37.64 ?  80  ALA   A CA  1 
ATOM   5432 C  C   . ALA   D 1 85  ? -50.174 -6.990  95.201  1.00 32.50 ?  80  ALA   A C   1 
ATOM   5433 O  O   . ALA   D 1 85  ? -49.728 -5.871  94.907  1.00 28.49 ?  80  ALA   A O   1 
ATOM   5434 C  CB  . ALA   D 1 85  ? -52.588 -6.977  94.517  1.00 38.66 ?  80  ALA   A CB  1 
ATOM   5435 N  N   . ASN   D 1 86  ? -49.478 -8.115  95.081  1.00 27.51 ?  81  ASN   A N   1 
ATOM   5436 C  CA  . ASN   D 1 86  ? -48.140 -8.168  94.444  1.00 29.90 ?  81  ASN   A CA  1 
ATOM   5437 C  C   . ASN   D 1 86  ? -48.363 -8.200  92.939  1.00 26.37 ?  81  ASN   A C   1 
ATOM   5438 O  O   . ASN   D 1 86  ? -49.057 -9.124  92.489  1.00 28.56 ?  81  ASN   A O   1 
ATOM   5439 C  CB  . ASN   D 1 86  ? -47.366 -9.377  94.943  1.00 30.48 ?  81  ASN   A CB  1 
ATOM   5440 C  CG  . ASN   D 1 86  ? -47.059 -9.201  96.405  1.00 34.79 ?  81  ASN   A CG  1 
ATOM   5441 O  OD1 . ASN   D 1 86  ? -46.732 -8.087  96.805  1.00 32.25 ?  81  ASN   A OD1 1 
ATOM   5442 N  ND2 . ASN   D 1 86  ? -47.152 -10.274 97.177  1.00 34.75 ?  81  ASN   A ND2 1 
ATOM   5443 N  N   . VAL   D 1 87  ? -47.884 -7.188  92.217  1.00 22.95 ?  82  VAL   A N   1 
ATOM   5444 C  CA  . VAL   D 1 87  ? -48.185 -7.057  90.757  1.00 21.20 ?  82  VAL   A CA  1 
ATOM   5445 C  C   . VAL   D 1 87  ? -46.887 -6.911  89.991  1.00 18.38 ?  82  VAL   A C   1 
ATOM   5446 O  O   . VAL   D 1 87  ? -45.805 -6.699  90.578  1.00 19.79 ?  82  VAL   A O   1 
ATOM   5447 C  CB  . VAL   D 1 87  ? -49.137 -5.902  90.404  1.00 21.16 ?  82  VAL   A CB  1 
ATOM   5448 C  CG1 . VAL   D 1 87  ? -50.446 -5.981  91.170  1.00 24.25 ?  82  VAL   A CG1 1 
ATOM   5449 C  CG2 . VAL   D 1 87  ? -48.465 -4.556  90.561  1.00 21.17 ?  82  VAL   A CG2 1 
ATOM   5450 N  N   . VAL   D 1 88  ? -46.991 -7.171  88.699  1.00 20.23 ?  83  VAL   A N   1 
ATOM   5451 C  CA  . VAL   D 1 88  ? -45.926 -6.852  87.713  1.00 20.58 ?  83  VAL   A CA  1 
ATOM   5452 C  C   . VAL   D 1 88  ? -46.566 -5.918  86.685  1.00 20.68 ?  83  VAL   A C   1 
ATOM   5453 O  O   . VAL   D 1 88  ? -47.747 -6.157  86.305  1.00 18.95 ?  83  VAL   A O   1 
ATOM   5454 C  CB  . VAL   D 1 88  ? -45.339 -8.099  87.059  1.00 21.37 ?  83  VAL   A CB  1 
ATOM   5455 C  CG1 . VAL   D 1 88  ? -46.399 -8.997  86.447  1.00 23.10 ?  83  VAL   A CG1 1 
ATOM   5456 C  CG2 . VAL   D 1 88  ? -44.291 -7.711  86.033  1.00 22.21 ?  83  VAL   A CG2 1 
ATOM   5457 N  N   . ALA   D 1 89  ? -45.841 -4.862  86.307  1.00 19.84 ?  84  ALA   A N   1 
ATOM   5458 C  CA  . ALA   D 1 89  ? -46.215 -3.968  85.192  1.00 18.47 ?  84  ALA   A CA  1 
ATOM   5459 C  C   . ALA   D 1 89  ? -45.127 -4.050  84.151  1.00 18.86 ?  84  ALA   A C   1 
ATOM   5460 O  O   . ALA   D 1 89  ? -43.906 -3.936  84.511  1.00 17.63 ?  84  ALA   A O   1 
ATOM   5461 C  CB  . ALA   D 1 89  ? -46.475 -2.548  85.655  1.00 21.17 ?  84  ALA   A CB  1 
ATOM   5462 N  N   . THR   D 1 90  ? -45.540 -4.421  82.939  1.00 19.06 ?  85  THR   A N   1 
ATOM   5463 C  CA  . THR   D 1 90  ? -44.616 -4.700  81.829  1.00 17.42 ?  85  THR   A CA  1 
ATOM   5464 C  C   . THR   D 1 90  ? -44.746 -3.559  80.829  1.00 16.55 ?  85  THR   A C   1 
ATOM   5465 O  O   . THR   D 1 90  ? -45.905 -3.240  80.378  1.00 14.32 ?  85  THR   A O   1 
ATOM   5466 C  CB  . THR   D 1 90  ? -44.845 -6.094  81.227  1.00 16.97 ?  85  THR   A CB  1 
ATOM   5467 O  OG1 . THR   D 1 90  ? -44.729 -7.070  82.283  1.00 18.40 ?  85  THR   A OG1 1 
ATOM   5468 C  CG2 . THR   D 1 90  ? -43.862 -6.335  80.105  1.00 18.34 ?  85  THR   A CG2 1 
ATOM   5469 N  N   . PHE   D 1 91  ? -43.598 -2.952  80.523  1.00 15.89 ?  86  PHE   A N   1 
ATOM   5470 C  CA  . PHE   D 1 91  ? -43.463 -1.849  79.560  1.00 18.37 ?  86  PHE   A CA  1 
ATOM   5471 C  C   . PHE   D 1 91  ? -42.719 -2.417  78.350  1.00 17.16 ?  86  PHE   A C   1 
ATOM   5472 O  O   . PHE   D 1 91  ? -41.607 -2.973  78.533  1.00 22.56 ?  86  PHE   A O   1 
ATOM   5473 C  CB  . PHE   D 1 91  ? -42.774 -0.648  80.181  1.00 17.78 ?  86  PHE   A CB  1 
ATOM   5474 C  CG  . PHE   D 1 91  ? -43.434 -0.069  81.396  1.00 17.51 ?  86  PHE   A CG  1 
ATOM   5475 C  CD1 . PHE   D 1 91  ? -43.296 -0.726  82.616  1.00 19.83 ?  86  PHE   A CD1 1 
ATOM   5476 C  CD2 . PHE   D 1 91  ? -44.281 1.043   81.324  1.00 16.22 ?  86  PHE   A CD2 1 
ATOM   5477 C  CE1 . PHE   D 1 91  ? -43.907 -0.230  83.745  1.00 17.80 ?  86  PHE   A CE1 1 
ATOM   5478 C  CE2 . PHE   D 1 91  ? -44.890 1.536   82.463  1.00 16.83 ?  86  PHE   A CE2 1 
ATOM   5479 C  CZ  . PHE   D 1 91  ? -44.698 0.907   83.669  1.00 17.44 ?  86  PHE   A CZ  1 
ATOM   5480 N  N   . ALA   D 1 92  ? -43.306 -2.335  77.168  1.00 16.20 ?  87  ALA   A N   1 
ATOM   5481 C  CA  . ALA   D 1 92  ? -42.737 -2.919  75.926  1.00 18.07 ?  87  ALA   A CA  1 
ATOM   5482 C  C   . ALA   D 1 92  ? -42.289 -1.796  74.995  1.00 19.85 ?  87  ALA   A C   1 
ATOM   5483 O  O   . ALA   D 1 92  ? -43.139 -0.947  74.613  1.00 21.27 ?  87  ALA   A O   1 
ATOM   5484 C  CB  . ALA   D 1 92  ? -43.692 -3.864  75.226  1.00 19.35 ?  87  ALA   A CB  1 
ATOM   5485 N  N   . GLY   D 1 93  ? -41.006 -1.792  74.643  1.00 16.69 ?  88  GLY   A N   1 
ATOM   5486 C  CA  . GLY   D 1 93  ? -40.483 -0.754  73.755  1.00 20.14 ?  88  GLY   A CA  1 
ATOM   5487 C  C   . GLY   D 1 93  ? -40.246 -1.242  72.321  1.00 18.43 ?  88  GLY   A C   1 
ATOM   5488 O  O   . GLY   D 1 93  ? -40.864 -2.183  71.871  1.00 19.72 ?  88  GLY   A O   1 
ATOM   5489 N  N   . PRO   D 1 94  ? -39.327 -0.563  71.603  1.00 19.03 ?  89  PRO   A N   1 
ATOM   5490 C  CA  . PRO   D 1 94  ? -38.956 -0.901  70.231  1.00 19.70 ?  89  PRO   A CA  1 
ATOM   5491 C  C   . PRO   D 1 94  ? -38.638 -2.386  70.085  1.00 17.45 ?  89  PRO   A C   1 
ATOM   5492 O  O   . PRO   D 1 94  ? -38.051 -2.964  71.006  1.00 17.48 ?  89  PRO   A O   1 
ATOM   5493 C  CB  . PRO   D 1 94  ? -37.653 -0.098  70.062  1.00 20.74 ?  89  PRO   A CB  1 
ATOM   5494 C  CG  . PRO   D 1 94  ? -37.927 1.138   70.865  1.00 20.64 ?  89  PRO   A CG  1 
ATOM   5495 C  CD  . PRO   D 1 94  ? -38.570 0.590   72.119  1.00 20.45 ?  89  PRO   A CD  1 
ATOM   5496 N  N   . ASN   D 1 95  ? -38.971 -2.954  68.937  1.00 17.67 ?  90  ASN   A N   1 
ATOM   5497 C  CA  . ASN   D 1 95  ? -38.771 -4.397  68.719  1.00 18.25 ?  90  ASN   A CA  1 
ATOM   5498 C  C   . ASN   D 1 95  ? -38.791 -4.630  67.223  1.00 17.94 ?  90  ASN   A C   1 
ATOM   5499 O  O   . ASN   D 1 95  ? -39.492 -3.874  66.535  1.00 17.46 ?  90  ASN   A O   1 
ATOM   5500 C  CB  . ASN   D 1 95  ? -39.822 -5.240  69.447  1.00 17.73 ?  90  ASN   A CB  1 
ATOM   5501 C  CG  . ASN   D 1 95  ? -41.229 -5.069  68.898  1.00 18.89 ?  90  ASN   A CG  1 
ATOM   5502 O  OD1 . ASN   D 1 95  ? -41.606 -5.794  67.983  1.00 19.31 ?  90  ASN   A OD1 1 
ATOM   5503 N  ND2 . ASN   D 1 95  ? -41.997 -4.153  69.465  1.00 18.88 ?  90  ASN   A ND2 1 
ATOM   5504 N  N   . ALA   D 1 96  ? -38.094 -5.646  66.756  1.00 16.31 ?  91  ALA   A N   1 
ATOM   5505 C  CA  . ALA   D 1 96  ? -38.149 -6.028  65.328  1.00 16.33 ?  91  ALA   A CA  1 
ATOM   5506 C  C   . ALA   D 1 96  ? -37.638 -7.435  65.149  1.00 16.99 ?  91  ALA   A C   1 
ATOM   5507 O  O   . ALA   D 1 96  ? -36.646 -7.818  65.810  1.00 16.55 ?  91  ALA   A O   1 
ATOM   5508 C  CB  . ALA   D 1 96  ? -37.360 -5.081  64.479  1.00 18.78 ?  91  ALA   A CB  1 
ATOM   5509 N  N   . TYR   D 1 97  ? -38.294 -8.154  64.257  1.00 15.46 ?  92  TYR   A N   1 
ATOM   5510 C  CA  . TYR   D 1 97  ? -37.864 -9.485  63.768  1.00 14.45 ?  92  TYR   A CA  1 
ATOM   5511 C  C   . TYR   D 1 97  ? -36.523 -9.381  63.065  1.00 14.67 ?  92  TYR   A C   1 
ATOM   5512 O  O   . TYR   D 1 97  ? -36.291 -8.402  62.301  1.00 15.36 ?  92  TYR   A O   1 
ATOM   5513 C  CB  . TYR   D 1 97  ? -38.894 -10.051 62.810  1.00 14.97 ?  92  TYR   A CB  1 
ATOM   5514 C  CG  . TYR   D 1 97  ? -38.506 -11.381 62.251  1.00 15.03 ?  92  TYR   A CG  1 
ATOM   5515 C  CD1 . TYR   D 1 97  ? -38.662 -12.535 63.014  1.00 16.98 ?  92  TYR   A CD1 1 
ATOM   5516 C  CD2 . TYR   D 1 97  ? -38.022 -11.534 60.964  1.00 14.60 ?  92  TYR   A CD2 1 
ATOM   5517 C  CE1 . TYR   D 1 97  ? -38.388 -13.792 62.516  1.00 16.97 ?  92  TYR   A CE1 1 
ATOM   5518 C  CE2 . TYR   D 1 97  ? -37.768 -12.800 60.444  1.00 14.77 ?  92  TYR   A CE2 1 
ATOM   5519 C  CZ  . TYR   D 1 97  ? -37.911 -13.933 61.225  1.00 15.80 ?  92  TYR   A CZ  1 
ATOM   5520 O  OH  . TYR   D 1 97  ? -37.613 -15.194 60.769  1.00 17.11 ?  92  TYR   A OH  1 
ATOM   5521 N  N   . VAL   D 1 98  ? -35.640 -10.301 63.414  1.00 16.23 ?  93  VAL   A N   1 
ATOM   5522 C  CA  . VAL   D 1 98  ? -34.293 -10.438 62.780  1.00 15.30 ?  93  VAL   A CA  1 
ATOM   5523 C  C   . VAL   D 1 98  ? -34.265 -11.664 61.868  1.00 14.26 ?  93  VAL   A C   1 
ATOM   5524 O  O   . VAL   D 1 98  ? -34.253 -12.834 62.349  1.00 14.64 ?  93  VAL   A O   1 
ATOM   5525 C  CB  . VAL   D 1 98  ? -33.202 -10.536 63.846  1.00 17.77 ?  93  VAL   A CB  1 
ATOM   5526 C  CG1 . VAL   D 1 98  ? -31.858 -10.650 63.150  1.00 16.92 ?  93  VAL   A CG1 1 
ATOM   5527 C  CG2 . VAL   D 1 98  ? -33.261 -9.396  64.848  1.00 16.94 ?  93  VAL   A CG2 1 
ATOM   5528 N  N   . SER   D 1 99  ? -34.275 -11.420 60.562  1.00 15.73 ?  94  SER   A N   1 
ATOM   5529 C  CA  . SER   D 1 99  ? -34.091 -12.459 59.528  1.00 16.37 ?  94  SER   A CA  1 
ATOM   5530 C  C   . SER   D 1 99  ? -32.623 -12.841 59.469  1.00 17.98 ?  94  SER   A C   1 
ATOM   5531 O  O   . SER   D 1 99  ? -31.835 -11.944 59.298  1.00 18.08 ?  94  SER   A O   1 
ATOM   5532 C  CB  . SER   D 1 99  ? -34.497 -11.963 58.190  1.00 15.44 ?  94  SER   A CB  1 
ATOM   5533 O  OG  . SER   D 1 99  ? -34.217 -12.992 57.235  1.00 17.30 ?  94  SER   A OG  1 
ATOM   5534 N  N   . PRO   D 1 100 ? -32.207 -14.125 59.512  1.00 19.82 ?  95  PRO   A N   1 
ATOM   5535 C  CA  . PRO   D 1 100 ? -30.783 -14.442 59.288  1.00 19.72 ?  95  PRO   A CA  1 
ATOM   5536 C  C   . PRO   D 1 100 ? -30.237 -14.066 57.894  1.00 20.35 ?  95  PRO   A C   1 
ATOM   5537 O  O   . PRO   D 1 100 ? -28.993 -14.041 57.731  1.00 19.76 ?  95  PRO   A O   1 
ATOM   5538 C  CB  . PRO   D 1 100 ? -30.722 -15.960 59.373  1.00 19.97 ?  95  PRO   A CB  1 
ATOM   5539 C  CG  . PRO   D 1 100 ? -31.932 -16.342 60.181  1.00 19.87 ?  95  PRO   A CG  1 
ATOM   5540 C  CD  . PRO   D 1 100 ? -33.008 -15.338 59.778  1.00 19.93 ?  95  PRO   A CD  1 
ATOM   5541 N  N   . ALA   D 1 101 ? -31.100 -13.694 56.947  1.00 19.76 ?  96  ALA   A N   1 
ATOM   5542 C  CA  . ALA   D 1 101 ? -30.673 -13.051 55.672  1.00 21.67 ?  96  ALA   A CA  1 
ATOM   5543 C  C   . ALA   D 1 101 ? -29.808 -11.817 55.949  1.00 21.60 ?  96  ALA   A C   1 
ATOM   5544 O  O   . ALA   D 1 101 ? -28.857 -11.627 55.187  1.00 23.36 ?  96  ALA   A O   1 
ATOM   5545 C  CB  . ALA   D 1 101 ? -31.875 -12.675 54.818  1.00 21.47 ?  96  ALA   A CB  1 
ATOM   5546 N  N   . VAL   D 1 102 ? -30.054 -11.073 57.033  1.00 16.91 ?  97  VAL   A N   1 
ATOM   5547 C  CA  . VAL   D 1 102 ? -29.378 -9.807  57.353  1.00 18.83 ?  97  VAL   A CA  1 
ATOM   5548 C  C   . VAL   D 1 102 ? -27.973 -10.203 57.796  1.00 20.80 ?  97  VAL   A C   1 
ATOM   5549 O  O   . VAL   D 1 102 ? -27.050 -9.442  57.574  1.00 22.78 ?  97  VAL   A O   1 
ATOM   5550 C  CB  . VAL   D 1 102 ? -30.148 -9.044  58.442  1.00 21.02 ?  97  VAL   A CB  1 
ATOM   5551 C  CG1 . VAL   D 1 102 ? -29.378 -7.852  58.966  1.00 23.66 ?  97  VAL   A CG1 1 
ATOM   5552 C  CG2 . VAL   D 1 102 ? -31.537 -8.641  57.947  1.00 22.76 ?  97  VAL   A CG2 1 
ATOM   5553 N  N   . TYR   D 1 103 ? -27.833 -11.361 58.469  1.00 19.68 ?  98  TYR   A N   1 
ATOM   5554 C  CA  . TYR   D 1 103 ? -26.516 -11.802 58.994  1.00 20.20 ?  98  TYR   A CA  1 
ATOM   5555 C  C   . TYR   D 1 103 ? -25.543 -12.091 57.857  1.00 19.63 ?  98  TYR   A C   1 
ATOM   5556 O  O   . TYR   D 1 103 ? -24.311 -11.842 58.056  1.00 24.91 ?  98  TYR   A O   1 
ATOM   5557 C  CB  . TYR   D 1 103 ? -26.652 -13.081 59.829  1.00 21.01 ?  98  TYR   A CB  1 
ATOM   5558 C  CG  . TYR   D 1 103 ? -27.506 -12.989 61.061  1.00 21.51 ?  98  TYR   A CG  1 
ATOM   5559 C  CD1 . TYR   D 1 103 ? -27.740 -11.808 61.731  1.00 21.89 ?  98  TYR   A CD1 1 
ATOM   5560 C  CD2 . TYR   D 1 103 ? -28.001 -14.153 61.633  1.00 26.32 ?  98  TYR   A CD2 1 
ATOM   5561 C  CE1 . TYR   D 1 103 ? -28.445 -11.773 62.925  1.00 21.32 ?  98  TYR   A CE1 1 
ATOM   5562 C  CE2 . TYR   D 1 103 ? -28.740 -14.130 62.805  1.00 25.10 ?  98  TYR   A CE2 1 
ATOM   5563 C  CZ  . TYR   D 1 103 ? -28.929 -12.948 63.478  1.00 22.26 ?  98  TYR   A CZ  1 
ATOM   5564 O  OH  . TYR   D 1 103 ? -29.627 -12.954 64.657  1.00 22.44 ?  98  TYR   A OH  1 
ATOM   5565 N  N   . ARG   D 1 104 ? -26.020 -12.709 56.768  1.00 22.73 ?  99  ARG   A N   1 
ATOM   5566 C  CA  . ARG   D 1 104 ? -25.230 -13.220 55.607  1.00 26.15 ?  99  ARG   A CA  1 
ATOM   5567 C  C   . ARG   D 1 104 ? -24.219 -14.279 56.082  1.00 32.03 ?  99  ARG   A C   1 
ATOM   5568 O  O   . ARG   D 1 104 ? -23.079 -14.362 55.534  1.00 31.27 ?  99  ARG   A O   1 
ATOM   5569 C  CB  . ARG   D 1 104 ? -24.559 -12.061 54.858  1.00 25.62 ?  99  ARG   A CB  1 
ATOM   5570 C  CG  . ARG   D 1 104 ? -25.452 -10.837 54.746  1.00 25.26 ?  99  ARG   A CG  1 
ATOM   5571 C  CD  . ARG   D 1 104 ? -25.039 -9.908  53.639  1.00 26.88 ?  99  ARG   A CD  1 
ATOM   5572 N  NE  . ARG   D 1 104 ? -23.653 -9.452  53.695  1.00 27.94 ?  99  ARG   A NE  1 
ATOM   5573 C  CZ  . ARG   D 1 104 ? -23.237 -8.305  54.223  1.00 27.64 ?  99  ARG   A CZ  1 
ATOM   5574 N  NH1 . ARG   D 1 104 ? -24.067 -7.476  54.827  1.00 25.87 1  99  ARG   A NH1 1 
ATOM   5575 N  NH2 . ARG   D 1 104 ? -21.950 -7.995  54.173  1.00 30.24 ?  99  ARG   A NH2 1 
ATOM   5576 N  N   . THR   D 1 105 ? -24.609 -15.038 57.092  1.00 26.90 ?  100 THR   A N   1 
ATOM   5577 C  CA  . THR   D 1 105 ? -23.820 -16.155 57.676  1.00 29.92 ?  100 THR   A CA  1 
ATOM   5578 C  C   . THR   D 1 105 ? -24.681 -17.407 57.666  1.00 28.77 ?  100 THR   A C   1 
ATOM   5579 O  O   . THR   D 1 105 ? -25.901 -17.299 57.518  1.00 26.60 ?  100 THR   A O   1 
ATOM   5580 C  CB  . THR   D 1 105 ? -23.350 -15.832 59.096  1.00 30.71 ?  100 THR   A CB  1 
ATOM   5581 O  OG1 . THR   D 1 105 ? -24.524 -15.632 59.884  1.00 33.55 ?  100 THR   A OG1 1 
ATOM   5582 C  CG2 . THR   D 1 105 ? -22.435 -14.632 59.148  1.00 37.73 ?  100 THR   A CG2 1 
ATOM   5583 N  N   . ALA   D 1 106 ? -24.049 -18.558 57.840  1.00 29.34 ?  101 ALA   A N   1 
ATOM   5584 C  CA  . ALA   D 1 106 ? -24.712 -19.876 57.903  1.00 29.13 ?  101 ALA   A CA  1 
ATOM   5585 C  C   . ALA   D 1 106 ? -23.861 -20.768 58.795  1.00 29.33 ?  101 ALA   A C   1 
ATOM   5586 O  O   . ALA   D 1 106 ? -22.627 -20.646 58.809  1.00 25.37 ?  101 ALA   A O   1 
ATOM   5587 C  CB  . ALA   D 1 106 ? -24.905 -20.458 56.515  1.00 31.00 ?  101 ALA   A CB  1 
ATOM   5588 N  N   . PRO   D 1 107 ? -24.472 -21.591 59.669  1.00 26.19 ?  102 PRO   A N   1 
ATOM   5589 C  CA  . PRO   D 1 107 ? -25.923 -21.663 59.834  1.00 23.81 ?  102 PRO   A CA  1 
ATOM   5590 C  C   . PRO   D 1 107 ? -26.382 -20.568 60.809  1.00 21.95 ?  102 PRO   A C   1 
ATOM   5591 O  O   . PRO   D 1 107 ? -25.581 -19.852 61.379  1.00 23.79 ?  102 PRO   A O   1 
ATOM   5592 C  CB  . PRO   D 1 107 ? -26.082 -23.078 60.411  1.00 25.09 ?  102 PRO   A CB  1 
ATOM   5593 C  CG  . PRO   D 1 107 ? -24.907 -23.176 61.332  1.00 25.86 ?  102 PRO   A CG  1 
ATOM   5594 C  CD  . PRO   D 1 107 ? -23.769 -22.487 60.604  1.00 27.70 ?  102 PRO   A CD  1 
ATOM   5595 N  N   . ALA   D 1 108 ? -27.692 -20.469 61.033  1.00 21.14 ?  103 ALA   A N   1 
ATOM   5596 C  CA  . ALA   D 1 108 ? -28.242 -19.432 61.908  1.00 20.90 ?  103 ALA   A CA  1 
ATOM   5597 C  C   . ALA   D 1 108 ? -29.676 -19.837 62.215  1.00 18.91 ?  103 ALA   A C   1 
ATOM   5598 O  O   . ALA   D 1 108 ? -30.183 -20.808 61.647  1.00 21.38 ?  103 ALA   A O   1 
ATOM   5599 C  CB  . ALA   D 1 108 ? -28.209 -18.064 61.219  1.00 22.84 ?  103 ALA   A CB  1 
ATOM   5600 N  N   . ALA   D 1 109 ? -30.255 -19.074 63.112  1.00 20.80 ?  104 ALA   A N   1 
ATOM   5601 C  CA  . ALA   D 1 109 ? -31.687 -19.138 63.460  1.00 20.25 ?  104 ALA   A CA  1 
ATOM   5602 C  C   . ALA   D 1 109 ? -32.147 -17.695 63.580  1.00 18.94 ?  104 ALA   A C   1 
ATOM   5603 O  O   . ALA   D 1 109 ? -31.378 -16.813 63.961  1.00 19.57 ?  104 ALA   A O   1 
ATOM   5604 C  CB  . ALA   D 1 109 ? -31.842 -19.872 64.774  1.00 20.93 ?  104 ALA   A CB  1 
ATOM   5605 N  N   . PRO   D 1 110 ? -33.420 -17.416 63.259  1.00 18.91 ?  105 PRO   A N   1 
ATOM   5606 C  CA  . PRO   D 1 110 ? -33.940 -16.069 63.389  1.00 17.89 ?  105 PRO   A CA  1 
ATOM   5607 C  C   . PRO   D 1 110 ? -34.106 -15.725 64.872  1.00 16.11 ?  105 PRO   A C   1 
ATOM   5608 O  O   . PRO   D 1 110 ? -34.064 -16.614 65.760  1.00 20.58 ?  105 PRO   A O   1 
ATOM   5609 C  CB  . PRO   D 1 110 ? -35.305 -16.141 62.699  1.00 17.02 ?  105 PRO   A CB  1 
ATOM   5610 C  CG  . PRO   D 1 110 ? -35.310 -17.466 61.968  1.00 19.32 ?  105 PRO   A CG  1 
ATOM   5611 C  CD  . PRO   D 1 110 ? -34.426 -18.363 62.798  1.00 19.35 ?  105 PRO   A CD  1 
ATOM   5612 N  N   . THR   D 1 111 ? -34.365 -14.451 65.155  1.00 17.86 ?  106 THR   A N   1 
ATOM   5613 C  CA  . THR   D 1 111 ? -34.738 -14.039 66.522  1.00 18.47 ?  106 THR   A CA  1 
ATOM   5614 C  C   . THR   D 1 111 ? -35.692 -12.850 66.411  1.00 18.59 ?  106 THR   A C   1 
ATOM   5615 O  O   . THR   D 1 111 ? -36.012 -12.388 65.285  1.00 17.29 ?  106 THR   A O   1 
ATOM   5616 C  CB  . THR   D 1 111 ? -33.524 -13.837 67.438  1.00 21.12 ?  106 THR   A CB  1 
ATOM   5617 O  OG1 . THR   D 1 111 ? -33.947 -13.860 68.802  1.00 20.27 ?  106 THR   A OG1 1 
ATOM   5618 C  CG2 . THR   D 1 111 ? -32.837 -12.508 67.229  1.00 21.31 ?  106 THR   A CG2 1 
ATOM   5619 N  N   . TRP   D 1 112 ? -36.073 -12.320 67.553  1.00 18.27 ?  107 TRP   A N   1 
ATOM   5620 C  CA  . TRP   D 1 112 ? -36.832 -11.061 67.621  1.00 17.67 ?  107 TRP   A CA  1 
ATOM   5621 C  C   . TRP   D 1 112 ? -36.097 -10.150 68.586  1.00 19.52 ?  107 TRP   A C   1 
ATOM   5622 O  O   . TRP   D 1 112 ? -36.006 -10.513 69.777  1.00 18.92 ?  107 TRP   A O   1 
ATOM   5623 C  CB  . TRP   D 1 112 ? -38.264 -11.386 68.069  1.00 18.72 ?  107 TRP   A CB  1 
ATOM   5624 C  CG  . TRP   D 1 112 ? -39.213 -10.335 67.608  1.00 17.60 ?  107 TRP   A CG  1 
ATOM   5625 C  CD1 . TRP   D 1 112 ? -39.246 -9.022  67.988  1.00 17.77 ?  107 TRP   A CD1 1 
ATOM   5626 C  CD2 . TRP   D 1 112 ? -40.253 -10.502 66.625  1.00 17.29 ?  107 TRP   A CD2 1 
ATOM   5627 N  NE1 . TRP   D 1 112 ? -40.257 -8.369  67.346  1.00 18.16 ?  107 TRP   A NE1 1 
ATOM   5628 C  CE2 . TRP   D 1 112 ? -40.862 -9.233  66.468  1.00 18.02 ?  107 TRP   A CE2 1 
ATOM   5629 C  CE3 . TRP   D 1 112 ? -40.709 -11.573 65.860  1.00 17.20 ?  107 TRP   A CE3 1 
ATOM   5630 C  CZ2 . TRP   D 1 112 ? -41.921 -9.047  65.595  1.00 17.83 ?  107 TRP   A CZ2 1 
ATOM   5631 C  CZ3 . TRP   D 1 112 ? -41.737 -11.369 64.982  1.00 18.84 ?  107 TRP   A CZ3 1 
ATOM   5632 C  CH2 . TRP   D 1 112 ? -42.324 -10.119 64.838  1.00 18.84 ?  107 TRP   A CH2 1 
ATOM   5633 N  N   . ASN   D 1 113 ? -35.484 -9.078  68.093  1.00 15.39 ?  108 ASN   A N   1 
ATOM   5634 C  CA  . ASN   D 1 113 ? -34.902 -8.107  69.010  1.00 15.78 ?  108 ASN   A CA  1 
ATOM   5635 C  C   . ASN   D 1 113 ? -36.038 -7.430  69.713  1.00 11.00 ?  108 ASN   A C   1 
ATOM   5636 O  O   . ASN   D 1 113 ? -36.946 -6.869  69.014  1.00 15.37 ?  108 ASN   A O   1 
ATOM   5637 C  CB  . ASN   D 1 113 ? -33.988 -7.157  68.286  1.00 16.88 ?  108 ASN   A CB  1 
ATOM   5638 C  CG  . ASN   D 1 113 ? -32.634 -7.775  68.078  1.00 19.67 ?  108 ASN   A CG  1 
ATOM   5639 O  OD1 . ASN   D 1 113 ? -32.455 -8.947  68.400  1.00 20.15 ?  108 ASN   A OD1 1 
ATOM   5640 N  ND2 . ASN   D 1 113 ? -31.715 -7.032  67.478  1.00 18.74 ?  108 ASN   A ND2 1 
ATOM   5641 N  N   . PHE   D 1 114 ? -35.967 -7.230  70.979  1.00 13.05 ?  109 PHE   A N   1 
ATOM   5642 C  CA  . PHE   D 1 114 ? -37.004 -6.455  71.647  1.00 15.20 ?  109 PHE   A CA  1 
ATOM   5643 C  C   . PHE   D 1 114 ? -36.495 -5.861  72.945  1.00 17.00 ?  109 PHE   A C   1 
ATOM   5644 O  O   . PHE   D 1 114 ? -35.443 -6.265  73.457  1.00 16.11 ?  109 PHE   A O   1 
ATOM   5645 C  CB  . PHE   D 1 114 ? -38.241 -7.327  71.934  1.00 15.71 ?  109 PHE   A CB  1 
ATOM   5646 C  CG  . PHE   D 1 114 ? -38.093 -8.372  73.047  1.00 16.87 ?  109 PHE   A CG  1 
ATOM   5647 C  CD1 . PHE   D 1 114 ? -37.513 -9.620  72.810  1.00 17.66 ?  109 PHE   A CD1 1 
ATOM   5648 C  CD2 . PHE   D 1 114 ? -38.473 -8.082  74.354  1.00 18.50 ?  109 PHE   A CD2 1 
ATOM   5649 C  CE1 . PHE   D 1 114 ? -37.396 -10.555 73.843  1.00 18.81 ?  109 PHE   A CE1 1 
ATOM   5650 C  CE2 . PHE   D 1 114 ? -38.381 -9.016  75.379  1.00 17.92 ?  109 PHE   A CE2 1 
ATOM   5651 C  CZ  . PHE   D 1 114 ? -37.759 -10.241 75.143  1.00 17.82 ?  109 PHE   A CZ  1 
ATOM   5652 N  N   . THR   D 1 115 ? -37.307 -4.972  73.481  1.00 16.97 ?  110 THR   A N   1 
ATOM   5653 C  CA  . THR   D 1 115 ? -37.026 -4.256  74.756  1.00 17.41 ?  110 THR   A CA  1 
ATOM   5654 C  C   . THR   D 1 115 ? -38.218 -4.381  75.700  1.00 18.99 ?  110 THR   A C   1 
ATOM   5655 O  O   . THR   D 1 115 ? -39.354 -4.162  75.283  1.00 16.91 ?  110 THR   A O   1 
ATOM   5656 C  CB  . THR   D 1 115 ? -36.636 -2.803  74.477  1.00 19.33 ?  110 THR   A CB  1 
ATOM   5657 O  OG1 . THR   D 1 115 ? -37.675 -2.143  73.781  1.00 21.36 ?  110 THR   A OG1 1 
ATOM   5658 C  CG2 . THR   D 1 115 ? -35.366 -2.703  73.670  1.00 18.50 ?  110 THR   A CG2 1 
ATOM   5659 N  N   . SER   D 1 116 ? -37.960 -4.656  76.971  1.00 19.72 ?  111 SER   A N   1 
ATOM   5660 C  CA  . SER   D 1 116 ? -39.057 -4.846  77.943  1.00 20.01 ?  111 SER   A CA  1 
ATOM   5661 C  C   . SER   D 1 116 ? -38.529 -4.432  79.310  1.00 19.82 ?  111 SER   A C   1 
ATOM   5662 O  O   . SER   D 1 116 ? -37.344 -4.702  79.613  1.00 19.84 ?  111 SER   A O   1 
ATOM   5663 C  CB  . SER   D 1 116 ? -39.472 -6.291  77.942  1.00 24.11 ?  111 SER   A CB  1 
ATOM   5664 O  OG  . SER   D 1 116 ? -40.418 -6.508  78.953  1.00 30.42 ?  111 SER   A OG  1 
ATOM   5665 N  N   . VAL   D 1 117 ? -39.309 -3.690  80.043  1.00 17.50 ?  112 VAL   A N   1 
ATOM   5666 C  CA  . VAL   D 1 117 ? -39.056 -3.523  81.499  1.00 16.73 ?  112 VAL   A CA  1 
ATOM   5667 C  C   . VAL   D 1 117 ? -40.212 -4.182  82.235  1.00 18.19 ?  112 VAL   A C   1 
ATOM   5668 O  O   . VAL   D 1 117 ? -41.335 -3.854  81.909  1.00 18.27 ?  112 VAL   A O   1 
ATOM   5669 C  CB  . VAL   D 1 117 ? -38.916 -2.033  81.805  1.00 17.77 ?  112 VAL   A CB  1 
ATOM   5670 C  CG1 . VAL   D 1 117 ? -38.908 -1.741  83.271  1.00 18.56 ?  112 VAL   A CG1 1 
ATOM   5671 C  CG2 . VAL   D 1 117 ? -37.701 -1.471  81.103  1.00 19.81 ?  112 VAL   A CG2 1 
ATOM   5672 N  N   . GLN   D 1 118 ? -39.913 -4.934  83.290  1.00 18.87 ?  113 GLN   A N   1 
ATOM   5673 C  CA  . GLN   D 1 118 ? -40.946 -5.464  84.206  1.00 17.57 ?  113 GLN   A CA  1 
ATOM   5674 C  C   . GLN   D 1 118 ? -40.626 -4.902  85.585  1.00 19.96 ?  113 GLN   A C   1 
ATOM   5675 O  O   . GLN   D 1 118 ? -39.481 -5.037  86.091  1.00 20.35 ?  113 GLN   A O   1 
ATOM   5676 C  CB  . GLN   D 1 118 ? -40.928 -6.979  84.249  1.00 18.13 ?  113 GLN   A CB  1 
ATOM   5677 C  CG  . GLN   D 1 118 ? -41.287 -7.611  82.925  1.00 17.89 ?  113 GLN   A CG  1 
ATOM   5678 C  CD  . GLN   D 1 118 ? -41.194 -9.110  83.004  1.00 21.98 ?  113 GLN   A CD  1 
ATOM   5679 O  OE1 . GLN   D 1 118 ? -41.151 -9.703  84.079  1.00 21.37 ?  113 GLN   A OE1 1 
ATOM   5680 N  NE2 . GLN   D 1 118 ? -41.176 -9.729  81.835  1.00 23.65 ?  113 GLN   A NE2 1 
ATOM   5681 N  N   . VAL   D 1 119 ? -41.549 -4.161  86.114  1.00 18.89 ?  114 VAL   A N   1 
ATOM   5682 C  CA  . VAL   D 1 119 ? -41.400 -3.689  87.517  1.00 20.50 ?  114 VAL   A CA  1 
ATOM   5683 C  C   . VAL   D 1 119 ? -42.359 -4.478  88.373  1.00 20.59 ?  114 VAL   A C   1 
ATOM   5684 O  O   . VAL   D 1 119 ? -43.492 -4.728  87.963  1.00 21.81 ?  114 VAL   A O   1 
ATOM   5685 C  CB  . VAL   D 1 119 ? -41.642 -2.186  87.692  1.00 20.78 ?  114 VAL   A CB  1 
ATOM   5686 C  CG1 . VAL   D 1 119 ? -40.666 -1.352  86.890  1.00 22.31 ?  114 VAL   A CG1 1 
ATOM   5687 C  CG2 . VAL   D 1 119 ? -43.065 -1.845  87.342  1.00 20.82 ?  114 VAL   A CG2 1 
ATOM   5688 N  N   . ARG   D 1 120 ? -41.908 -4.771  89.574  1.00 22.42 ?  115 ARG   A N   1 
ATOM   5689 C  CA  . ARG   D 1 120 ? -42.687 -5.550  90.540  1.00 23.63 ?  115 ARG   A CA  1 
ATOM   5690 C  C   . ARG   D 1 120 ? -42.762 -4.769  91.838  1.00 21.86 ?  115 ARG   A C   1 
ATOM   5691 O  O   . ARG   D 1 120 ? -41.739 -4.221  92.286  1.00 22.56 ?  115 ARG   A O   1 
ATOM   5692 C  CB  . ARG   D 1 120 ? -42.023 -6.912  90.729  1.00 22.76 ?  115 ARG   A CB  1 
ATOM   5693 C  CG  . ARG   D 1 120 ? -42.366 -7.897  89.624  1.00 23.91 ?  115 ARG   A CG  1 
ATOM   5694 C  CD  . ARG   D 1 120 ? -41.653 -9.221  89.689  1.00 25.60 ?  115 ARG   A CD  1 
ATOM   5695 N  NE  . ARG   D 1 120 ? -42.254 -10.126 88.716  1.00 25.11 ?  115 ARG   A NE  1 
ATOM   5696 C  CZ  . ARG   D 1 120 ? -41.970 -10.177 87.424  1.00 25.02 ?  115 ARG   A CZ  1 
ATOM   5697 N  NH1 . ARG   D 1 120 ? -40.992 -9.446  86.897  1.00 24.58 1  115 ARG   A NH1 1 
ATOM   5698 N  NH2 . ARG   D 1 120 ? -42.611 -11.044 86.678  1.00 24.23 ?  115 ARG   A NH2 1 
ATOM   5699 N  N   . GLY   D 1 121 ? -43.939 -4.772  92.419  1.00 22.02 ?  116 GLY   A N   1 
ATOM   5700 C  CA  . GLY   D 1 121 ? -44.071 -4.369  93.821  1.00 25.56 ?  116 GLY   A CA  1 
ATOM   5701 C  C   . GLY   D 1 121 ? -45.489 -4.534  94.262  1.00 26.39 ?  116 GLY   A C   1 
ATOM   5702 O  O   . GLY   D 1 121 ? -46.273 -5.239  93.604  1.00 27.04 ?  116 GLY   A O   1 
ATOM   5703 N  N   . GLU   D 1 122 ? -45.805 -3.874  95.347  1.00 24.87 ?  117 GLU   A N   1 
ATOM   5704 C  CA  . GLU   D 1 122 ? -47.151 -3.906  95.933  1.00 27.49 ?  117 GLU   A CA  1 
ATOM   5705 C  C   . GLU   D 1 122 ? -47.961 -2.751  95.347  1.00 26.65 ?  117 GLU   A C   1 
ATOM   5706 O  O   . GLU   D 1 122 ? -47.518 -1.576  95.399  1.00 31.16 ?  117 GLU   A O   1 
ATOM   5707 C  CB  . GLU   D 1 122 ? -46.971 -3.876  97.456  1.00 34.36 ?  117 GLU   A CB  1 
ATOM   5708 C  CG  . GLU   D 1 122 ? -48.258 -3.914  98.231  1.00 41.87 ?  117 GLU   A CG  1 
ATOM   5709 C  CD  . GLU   D 1 122 ? -48.033 -3.825  99.739  1.00 51.91 ?  117 GLU   A CD  1 
ATOM   5710 O  OE1 . GLU   D 1 122 ? -48.864 -3.156  100.413 1.00 60.58 ?  117 GLU   A OE1 1 
ATOM   5711 O  OE2 . GLU   D 1 122 ? -47.020 -4.422  100.235 1.00 49.87 -1 117 GLU   A OE2 1 
ATOM   5712 N  N   . LEU   D 1 123 ? -49.156 -3.059  94.852  1.00 27.68 ?  118 LEU   A N   1 
ATOM   5713 C  CA  . LEU   D 1 123 ? -50.044 -2.049  94.264  1.00 26.39 ?  118 LEU   A CA  1 
ATOM   5714 C  C   . LEU   D 1 123 ? -50.949 -1.589  95.399  1.00 29.51 ?  118 LEU   A C   1 
ATOM   5715 O  O   . LEU   D 1 123 ? -51.550 -2.435  96.063  1.00 28.86 ?  118 LEU   A O   1 
ATOM   5716 C  CB  . LEU   D 1 123 ? -50.803 -2.623  93.059  1.00 26.44 ?  118 LEU   A CB  1 
ATOM   5717 C  CG  . LEU   D 1 123 ? -51.723 -1.651  92.316  1.00 27.14 ?  118 LEU   A CG  1 
ATOM   5718 C  CD1 . LEU   D 1 123 ? -51.966 -2.100  90.894  1.00 27.83 ?  118 LEU   A CD1 1 
ATOM   5719 C  CD2 . LEU   D 1 123 ? -53.059 -1.505  93.000  1.00 27.62 ?  118 LEU   A CD2 1 
ATOM   5720 N  N   . ARG   D 1 124 ? -50.956 -0.290  95.665  1.00 26.17 ?  119 ARG   A N   1 
ATOM   5721 C  CA  . ARG   D 1 124 ? -51.831 0.307   96.689  1.00 28.50 ?  119 ARG   A CA  1 
ATOM   5722 C  C   . ARG   D 1 124 ? -52.898 1.106   95.975  1.00 25.19 ?  119 ARG   A C   1 
ATOM   5723 O  O   . ARG   D 1 124 ? -52.557 1.974   95.171  1.00 22.67 ?  119 ARG   A O   1 
ATOM   5724 C  CB  . ARG   D 1 124 ? -51.004 1.127   97.674  1.00 34.92 ?  119 ARG   A CB  1 
ATOM   5725 C  CG  . ARG   D 1 124 ? -50.134 0.282   98.598  1.00 43.95 ?  119 ARG   A CG  1 
ATOM   5726 C  CD  . ARG   D 1 124 ? -49.754 1.120   99.811  1.00 54.96 ?  119 ARG   A CD  1 
ATOM   5727 N  NE  . ARG   D 1 124 ? -48.542 0.718   100.514 1.00 66.05 ?  119 ARG   A NE  1 
ATOM   5728 C  CZ  . ARG   D 1 124 ? -48.486 -0.158  101.521 1.00 74.09 ?  119 ARG   A CZ  1 
ATOM   5729 N  NH1 . ARG   D 1 124 ? -49.578 -0.780  101.950 1.00 72.21 1  119 ARG   A NH1 1 
ATOM   5730 N  NH2 . ARG   D 1 124 ? -47.320 -0.413  102.093 1.00 72.84 ?  119 ARG   A NH2 1 
ATOM   5731 N  N   . LYS   D 1 125 ? -54.161 0.837   96.278  1.00 25.07 ?  120 LYS   A N   1 
ATOM   5732 C  CA  . LYS   D 1 125 ? -55.271 1.597   95.710  1.00 25.11 ?  120 LYS   A CA  1 
ATOM   5733 C  C   . LYS   D 1 125 ? -55.335 2.973   96.358  1.00 28.54 ?  120 LYS   A C   1 
ATOM   5734 O  O   . LYS   D 1 125 ? -55.117 3.090   97.593  1.00 28.90 ?  120 LYS   A O   1 
ATOM   5735 C  CB  . LYS   D 1 125 ? -56.567 0.833   95.914  1.00 28.86 ?  120 LYS   A CB  1 
ATOM   5736 C  CG  . LYS   D 1 125 ? -56.641 -0.477  95.155  1.00 27.69 ?  120 LYS   A CG  1 
ATOM   5737 C  CD  . LYS   D 1 125 ? -58.032 -1.004  95.282  1.00 31.77 ?  120 LYS   A CD  1 
ATOM   5738 C  CE  . LYS   D 1 125 ? -58.221 -2.302  94.559  1.00 33.99 ?  120 LYS   A CE  1 
ATOM   5739 N  NZ  . LYS   D 1 125 ? -59.515 -2.897  94.948  1.00 37.84 1  120 LYS   A NZ  1 
ATOM   5740 N  N   . VAL   D 1 126 ? -55.546 3.991   95.532  1.00 25.44 ?  121 VAL   A N   1 
ATOM   5741 C  CA  . VAL   D 1 126 ? -55.879 5.352   95.981  1.00 25.64 ?  121 VAL   A CA  1 
ATOM   5742 C  C   . VAL   D 1 126 ? -57.403 5.372   96.201  1.00 30.57 ?  121 VAL   A C   1 
ATOM   5743 O  O   . VAL   D 1 126 ? -58.193 5.080   95.248  1.00 31.83 ?  121 VAL   A O   1 
ATOM   5744 C  CB  . VAL   D 1 126 ? -55.378 6.392   94.966  1.00 26.60 ?  121 VAL   A CB  1 
ATOM   5745 C  CG1 . VAL   D 1 126 ? -55.711 7.782   95.419  1.00 29.43 ?  121 VAL   A CG1 1 
ATOM   5746 C  CG2 . VAL   D 1 126 ? -53.884 6.270   94.701  1.00 28.43 ?  121 VAL   A CG2 1 
ATOM   5747 N  N   . GLU   D 1 127 ? -57.821 5.688   97.427  1.00 34.23 ?  122 GLU   A N   1 
ATOM   5748 C  CA  . GLU   D 1 127 ? -59.269 5.821   97.748  1.00 41.58 ?  122 GLU   A CA  1 
ATOM   5749 C  C   . GLU   D 1 127 ? -59.533 7.216   98.339  1.00 44.90 ?  122 GLU   A C   1 
ATOM   5750 O  O   . GLU   D 1 127 ? -60.470 7.328   99.127  1.00 48.85 ?  122 GLU   A O   1 
ATOM   5751 C  CB  . GLU   D 1 127 ? -59.763 4.725   98.709  1.00 45.64 ?  122 GLU   A CB  1 
ATOM   5752 C  CG  . GLU   D 1 127 ? -59.430 3.278   98.315  1.00 44.93 ?  122 GLU   A CG  1 
ATOM   5753 C  CD  . GLU   D 1 127 ? -60.289 2.593   97.254  1.00 45.17 ?  122 GLU   A CD  1 
ATOM   5754 O  OE1 . GLU   D 1 127 ? -61.187 3.230   96.696  1.00 45.04 ?  122 GLU   A OE1 1 
ATOM   5755 O  OE2 . GLU   D 1 127 ? -60.044 1.389   96.991  1.00 44.49 -1 122 GLU   A OE2 1 
ATOM   5756 N  N   . SER   D 1 128 ? -58.738 8.233   97.994  1.00 39.92 ?  123 SER   A N   1 
ATOM   5757 C  CA  . SER   D 1 128 ? -59.103 9.673   98.142  1.00 37.30 ?  123 SER   A CA  1 
ATOM   5758 C  C   . SER   D 1 128 ? -59.391 10.252  96.745  1.00 32.43 ?  123 SER   A C   1 
ATOM   5759 O  O   . SER   D 1 128 ? -58.538 10.112  95.867  1.00 31.56 ?  123 SER   A O   1 
ATOM   5760 C  CB  . SER   D 1 128 ? -58.013 10.451  98.882  1.00 42.60 ?  123 SER   A CB  1 
ATOM   5761 O  OG  . SER   D 1 128 ? -57.693 11.720  98.269  1.00 44.02 ?  123 SER   A OG  1 
ATOM   5762 N  N   . ALA   D 1 129 ? -60.562 10.834  96.526  1.00 29.99 ?  124 ALA   A N   1 
ATOM   5763 C  CA  . ALA   D 1 129 ? -60.911 11.620  95.316  1.00 30.53 ?  124 ALA   A CA  1 
ATOM   5764 C  C   . ALA   D 1 129 ? -59.815 12.650  94.975  1.00 32.60 ?  124 ALA   A C   1 
ATOM   5765 O  O   . ALA   D 1 129 ? -59.482 12.806  93.788  1.00 30.16 ?  124 ALA   A O   1 
ATOM   5766 C  CB  . ALA   D 1 129 ? -62.250 12.292  95.485  1.00 32.80 ?  124 ALA   A CB  1 
ATOM   5767 N  N   . ASP   D 1 130 ? -59.259 13.357  95.954  1.00 31.72 ?  125 ASP   A N   1 
ATOM   5768 C  CA  . ASP   D 1 130 ? -58.215 14.377  95.656  1.00 32.41 ?  125 ASP   A CA  1 
ATOM   5769 C  C   . ASP   D 1 130 ? -56.982 13.697  95.021  1.00 31.24 ?  125 ASP   A C   1 
ATOM   5770 O  O   . ASP   D 1 130 ? -56.405 14.277  94.066  1.00 25.69 ?  125 ASP   A O   1 
ATOM   5771 C  CB  . ASP   D 1 130 ? -57.959 15.253  96.891  1.00 38.71 ?  125 ASP   A CB  1 
ATOM   5772 C  CG  . ASP   D 1 130 ? -59.098 16.266  97.109  1.00 50.55 ?  125 ASP   A CG  1 
ATOM   5773 O  OD1 . ASP   D 1 130 ? -58.944 17.454  96.654  1.00 55.43 ?  125 ASP   A OD1 1 
ATOM   5774 O  OD2 . ASP   D 1 130 ? -60.168 15.871  97.702  1.00 57.54 -1 125 ASP   A OD2 1 
ATOM   5775 N  N   . ASP   D 1 131 ? -56.641 12.485  95.436  1.00 25.96 ?  126 ASP   A N   1 
ATOM   5776 C  CA  . ASP   D 1 131 ? -55.409 11.785  94.970  1.00 28.56 ?  126 ASP   A CA  1 
ATOM   5777 C  C   . ASP   D 1 131 ? -55.698 11.132  93.605  1.00 25.72 ?  126 ASP   A C   1 
ATOM   5778 O  O   . ASP   D 1 131 ? -54.774 10.941  92.809  1.00 23.86 ?  126 ASP   A O   1 
ATOM   5779 C  CB  . ASP   D 1 131 ? -54.944 10.760  95.997  1.00 30.30 ?  126 ASP   A CB  1 
ATOM   5780 C  CG  . ASP   D 1 131 ? -54.399 11.368  97.278  1.00 41.25 ?  126 ASP   A CG  1 
ATOM   5781 O  OD1 . ASP   D 1 131 ? -53.934 12.526  97.223  1.00 41.63 ?  126 ASP   A OD1 1 
ATOM   5782 O  OD2 . ASP   D 1 131 ? -54.473 10.677  98.322  1.00 43.30 -1 126 ASP   A OD2 1 
ATOM   5783 N  N   . THR   D 1 132 ? -56.952 10.823  93.354  1.00 22.28 ?  127 THR   A N   1 
ATOM   5784 C  CA  . THR   D 1 132 ? -57.443 10.235  92.080  1.00 21.82 ?  127 THR   A CA  1 
ATOM   5785 C  C   . THR   D 1 132 ? -57.401 11.329  91.013  1.00 21.76 ?  127 THR   A C   1 
ATOM   5786 O  O   . THR   D 1 132 ? -56.940 11.076  89.896  1.00 20.25 ?  127 THR   A O   1 
ATOM   5787 C  CB  . THR   D 1 132 ? -58.858 9.673   92.252  1.00 20.87 ?  127 THR   A CB  1 
ATOM   5788 O  OG1 . THR   D 1 132 ? -58.809 8.643   93.250  1.00 20.44 ?  127 THR   A OG1 1 
ATOM   5789 C  CG2 . THR   D 1 132 ? -59.407 9.136   90.958  1.00 22.47 ?  127 THR   A CG2 1 
ATOM   5790 N  N   . LEU   D 1 133 ? -57.871 12.533  91.353  1.00 20.33 ?  128 LEU   A N   1 
ATOM   5791 C  CA  . LEU   D 1 133 ? -57.745 13.703  90.464  1.00 20.48 ?  128 LEU   A CA  1 
ATOM   5792 C  C   . LEU   D 1 133 ? -56.276 14.013  90.183  1.00 18.83 ?  128 LEU   A C   1 
ATOM   5793 O  O   . LEU   D 1 133 ? -55.931 14.230  89.006  1.00 20.51 ?  128 LEU   A O   1 
ATOM   5794 C  CB  . LEU   D 1 133 ? -58.428 14.922  91.101  1.00 23.15 ?  128 LEU   A CB  1 
ATOM   5795 C  CG  . LEU   D 1 133 ? -58.413 16.153  90.194  1.00 19.80 ?  128 LEU   A CG  1 
ATOM   5796 C  CD1 . LEU   D 1 133 ? -59.252 15.911  88.941  1.00 22.76 ?  128 LEU   A CD1 1 
ATOM   5797 C  CD2 . LEU   D 1 133 ? -58.940 17.392  90.920  1.00 22.68 ?  128 LEU   A CD2 1 
ATOM   5798 N  N   . ALA   D 1 134 ? -55.426 14.037  91.197  1.00 17.72 ?  129 ALA   A N   1 
ATOM   5799 C  CA  . ALA   D 1 134 ? -53.966 14.261  91.025  1.00 17.66 ?  129 ALA   A CA  1 
ATOM   5800 C  C   . ALA   D 1 134 ? -53.401 13.263  89.997  1.00 18.73 ?  129 ALA   A C   1 
ATOM   5801 O  O   . ALA   D 1 134 ? -52.609 13.659  89.122  1.00 21.88 ?  129 ALA   A O   1 
ATOM   5802 C  CB  . ALA   D 1 134 ? -53.308 14.153  92.313  1.00 18.34 ?  129 ALA   A CB  1 
ATOM   5803 N  N   . THR   D 1 135 ? -53.742 11.975  90.154  1.00 18.71 ?  130 THR   A N   1 
ATOM   5804 C  CA  . THR   D 1 135 ? -53.248 10.895  89.284  1.00 17.09 ?  130 THR   A CA  1 
ATOM   5805 C  C   . THR   D 1 135 ? -53.578 11.244  87.827  1.00 17.13 ?  130 THR   A C   1 
ATOM   5806 O  O   . THR   D 1 135 ? -52.662 11.214  87.003  1.00 19.40 ?  130 THR   A O   1 
ATOM   5807 C  CB  . THR   D 1 135 ? -53.788 9.522   89.688  1.00 17.19 ?  130 THR   A CB  1 
ATOM   5808 O  OG1 . THR   D 1 135 ? -53.491 9.294   91.051  1.00 19.41 ?  130 THR   A OG1 1 
ATOM   5809 C  CG2 . THR   D 1 135 ? -53.183 8.445   88.836  1.00 17.30 ?  130 THR   A CG2 1 
ATOM   5810 N  N   . VAL   D 1 136 ? -54.836 11.521  87.495  1.00 17.22 ?  131 VAL   A N   1 
ATOM   5811 C  CA  . VAL   D 1 136 ? -55.206 11.730  86.068  1.00 18.07 ?  131 VAL   A CA  1 
ATOM   5812 C  C   . VAL   D 1 136 ? -54.635 13.052  85.520  1.00 18.77 ?  131 VAL   A C   1 
ATOM   5813 O  O   . VAL   D 1 136 ? -54.236 13.093  84.317  1.00 16.83 ?  131 VAL   A O   1 
ATOM   5814 C  CB  . VAL   D 1 136 ? -56.722 11.596  85.806  1.00 18.96 ?  131 VAL   A CB  1 
ATOM   5815 C  CG1 . VAL   D 1 136 ? -57.207 10.192  86.205  1.00 22.31 ?  131 VAL   A CG1 1 
ATOM   5816 C  CG2 . VAL   D 1 136 ? -57.586 12.642  86.467  1.00 20.96 ?  131 VAL   A CG2 1 
ATOM   5817 N  N   . ARG   D 1 137 ? -54.517 14.098  86.341  1.00 17.04 ?  132 ARG   A N   1 
ATOM   5818 C  CA  . ARG   D 1 137 ? -54.001 15.390  85.818  1.00 16.85 ?  132 ARG   A CA  1 
ATOM   5819 C  C   . ARG   D 1 137 ? -52.511 15.224  85.580  1.00 15.79 ?  132 ARG   A C   1 
ATOM   5820 O  O   . ARG   D 1 137 ? -51.993 15.809  84.612  1.00 16.52 ?  132 ARG   A O   1 
ATOM   5821 C  CB  . ARG   D 1 137 ? -54.331 16.535  86.759  1.00 16.56 ?  132 ARG   A CB  1 
ATOM   5822 C  CG  . ARG   D 1 137 ? -55.828 16.839  86.803  1.00 15.91 ?  132 ARG   A CG  1 
ATOM   5823 C  CD  . ARG   D 1 137 ? -56.161 18.172  87.462  1.00 17.66 ?  132 ARG   A CD  1 
ATOM   5824 N  NE  . ARG   D 1 137 ? -55.615 18.359  88.788  1.00 18.93 ?  132 ARG   A NE  1 
ATOM   5825 C  CZ  . ARG   D 1 137 ? -55.982 19.361  89.628  1.00 20.45 ?  132 ARG   A CZ  1 
ATOM   5826 N  NH1 . ARG   D 1 137 ? -56.924 20.213  89.288  1.00 22.72 1  132 ARG   A NH1 1 
ATOM   5827 N  NH2 . ARG   D 1 137 ? -55.454 19.450  90.821  1.00 21.00 ?  132 ARG   A NH2 1 
ATOM   5828 N  N   . ALA   D 1 138 ? -51.854 14.497  86.472  1.00 16.06 ?  133 ALA   A N   1 
ATOM   5829 C  CA  . ALA   D 1 138 ? -50.401 14.286  86.359  1.00 15.94 ?  133 ALA   A CA  1 
ATOM   5830 C  C   . ALA   D 1 138 ? -50.189 13.474  85.078  1.00 17.53 ?  133 ALA   A C   1 
ATOM   5831 O  O   . ALA   D 1 138 ? -49.194 13.709  84.401  1.00 17.09 ?  133 ALA   A O   1 
ATOM   5832 C  CB  . ALA   D 1 138 ? -49.867 13.619  87.573  1.00 16.84 ?  133 ALA   A CB  1 
ATOM   5833 N  N   . THR   D 1 139 ? -51.137 12.576  84.769  1.00 16.75 ?  134 THR   A N   1 
ATOM   5834 C  CA  . THR   D 1 139 ? -51.018 11.669  83.591  1.00 16.93 ?  134 THR   A CA  1 
ATOM   5835 C  C   . THR   D 1 139 ? -51.138 12.532  82.327  1.00 16.18 ?  134 THR   A C   1 
ATOM   5836 O  O   . THR   D 1 139 ? -50.378 12.333  81.377  1.00 15.59 ?  134 THR   A O   1 
ATOM   5837 C  CB  . THR   D 1 139 ? -51.981 10.480  83.703  1.00 16.60 ?  134 THR   A CB  1 
ATOM   5838 O  OG1 . THR   D 1 139 ? -51.649 9.713   84.885  1.00 17.85 ?  134 THR   A OG1 1 
ATOM   5839 C  CG2 . THR   D 1 139 ? -51.877 9.569   82.493  1.00 17.15 ?  134 THR   A CG2 1 
ATOM   5840 N  N   . VAL   D 1 140 ? -52.131 13.410  82.295  1.00 15.60 ?  135 VAL   A N   1 
ATOM   5841 C  CA  . VAL   D 1 140 ? -52.334 14.333  81.163  1.00 15.13 ?  135 VAL   A CA  1 
ATOM   5842 C  C   . VAL   D 1 140 ? -51.057 15.154  80.970  1.00 19.30 ?  135 VAL   A C   1 
ATOM   5843 O  O   . VAL   D 1 140 ? -50.538 15.198  79.797  1.00 17.97 ?  135 VAL   A O   1 
ATOM   5844 C  CB  . VAL   D 1 140 ? -53.563 15.213  81.333  1.00 17.34 ?  135 VAL   A CB  1 
ATOM   5845 C  CG1 . VAL   D 1 140 ? -53.599 16.232  80.193  1.00 17.71 ?  135 VAL   A CG1 1 
ATOM   5846 C  CG2 . VAL   D 1 140 ? -54.802 14.373  81.345  1.00 17.73 ?  135 VAL   A CG2 1 
ATOM   5847 N  N   . ALA   D 1 141 ? -50.566 15.783  82.027  1.00 17.92 ?  136 ALA   A N   1 
ATOM   5848 C  CA  . ALA   D 1 141 ? -49.378 16.635  81.909  1.00 20.22 ?  136 ALA   A CA  1 
ATOM   5849 C  C   . ALA   D 1 141 ? -48.204 15.862  81.268  1.00 21.68 ?  136 ALA   A C   1 
ATOM   5850 O  O   . ALA   D 1 141 ? -47.546 16.390  80.291  1.00 23.35 ?  136 ALA   A O   1 
ATOM   5851 C  CB  . ALA   D 1 141 ? -49.069 17.260  83.241  1.00 22.77 ?  136 ALA   A CB  1 
ATOM   5852 N  N   . ALA   D 1 142 ? -47.957 14.646  81.731  1.00 18.57 ?  137 ALA   A N   1 
ATOM   5853 C  CA  . ALA   D 1 142 ? -46.803 13.812  81.334  1.00 19.33 ?  137 ALA   A CA  1 
ATOM   5854 C  C   . ALA   D 1 142 ? -47.022 13.329  79.894  1.00 17.92 ?  137 ALA   A C   1 
ATOM   5855 O  O   . ALA   D 1 142 ? -46.080 13.441  79.077  1.00 21.26 ?  137 ALA   A O   1 
ATOM   5856 C  CB  . ALA   D 1 142 ? -46.628 12.620  82.263  1.00 20.35 ?  137 ALA   A CB  1 
ATOM   5857 N  N   . LEU   D 1 143 ? -48.222 12.822  79.569  1.00 16.10 ?  138 LEU   A N   1 
ATOM   5858 C  CA  . LEU   D 1 143 ? -48.410 12.181  78.244  1.00 16.12 ?  138 LEU   A CA  1 
ATOM   5859 C  C   . LEU   D 1 143 ? -48.677 13.240  77.177  1.00 19.18 ?  138 LEU   A C   1 
ATOM   5860 O  O   . LEU   D 1 143 ? -48.215 13.024  76.017  1.00 16.78 ?  138 LEU   A O   1 
ATOM   5861 C  CB  . LEU   D 1 143 ? -49.510 11.132  78.217  1.00 17.44 ?  138 LEU   A CB  1 
ATOM   5862 C  CG  . LEU   D 1 143 ? -49.502 9.977   79.209  1.00 24.85 ?  138 LEU   A CG  1 
ATOM   5863 C  CD1 . LEU   D 1 143 ? -50.189 8.777   78.639  1.00 19.89 ?  138 LEU   A CD1 1 
ATOM   5864 C  CD2 . LEU   D 1 143 ? -48.165 9.678   79.852  1.00 22.24 ?  138 LEU   A CD2 1 
ATOM   5865 N  N   . GLU   D 1 144 ? -49.472 14.267  77.461  1.00 18.54 ?  139 GLU   A N   1 
ATOM   5866 C  CA  . GLU   D 1 144 ? -49.748 15.289  76.419  1.00 18.67 ?  139 GLU   A CA  1 
ATOM   5867 C  C   . GLU   D 1 144 ? -48.429 15.979  76.038  1.00 20.24 ?  139 GLU   A C   1 
ATOM   5868 O  O   . GLU   D 1 144 ? -48.209 16.230  74.847  1.00 20.58 ?  139 GLU   A O   1 
ATOM   5869 C  CB  . GLU   D 1 144 ? -50.848 16.266  76.831  1.00 19.58 ?  139 GLU   A CB  1 
ATOM   5870 C  CG  . GLU   D 1 144 ? -51.232 17.227  75.727  1.00 19.44 ?  139 GLU   A CG  1 
ATOM   5871 C  CD  . GLU   D 1 144 ? -51.993 16.649  74.542  1.00 17.60 ?  139 GLU   A CD  1 
ATOM   5872 O  OE1 . GLU   D 1 144 ? -52.530 15.539  74.637  1.00 19.33 ?  139 GLU   A OE1 1 
ATOM   5873 O  OE2 . GLU   D 1 144 ? -51.967 17.296  73.491  1.00 20.07 -1 139 GLU   A OE2 1 
ATOM   5874 N  N   . SER   D 1 145 ? -47.546 16.246  76.981  1.00 20.89 ?  140 SER   A N   1 
ATOM   5875 C  CA  . SER   D 1 145 ? -46.249 16.912  76.659  1.00 23.87 ?  140 SER   A CA  1 
ATOM   5876 C  C   . SER   D 1 145 ? -45.412 15.988  75.771  1.00 24.35 ?  140 SER   A C   1 
ATOM   5877 O  O   . SER   D 1 145 ? -44.923 16.427  74.723  1.00 26.44 ?  140 SER   A O   1 
ATOM   5878 C  CB  . SER   D 1 145 ? -45.515 17.291  77.866  1.00 23.74 ?  140 SER   A CB  1 
ATOM   5879 O  OG  . SER   D 1 145 ? -45.470 16.188  78.706  1.00 33.13 ?  140 SER   A OG  1 
ATOM   5880 N  N   . ARG   D 1 146 ? -45.298 14.715  76.127  1.00 24.07 ?  141 ARG   A N   1 
ATOM   5881 C  CA  . ARG   D 1 146 ? -44.398 13.765  75.417  1.00 23.09 ?  141 ARG   A CA  1 
ATOM   5882 C  C   . ARG   D 1 146 ? -44.989 13.240  74.105  1.00 21.70 ?  141 ARG   A C   1 
ATOM   5883 O  O   . ARG   D 1 146 ? -44.207 12.992  73.175  1.00 23.24 ?  141 ARG   A O   1 
ATOM   5884 C  CB  . ARG   D 1 146 ? -44.042 12.586  76.311  1.00 22.90 ?  141 ARG   A CB  1 
ATOM   5885 C  CG  . ARG   D 1 146 ? -43.024 11.646  75.675  1.00 28.22 ?  141 ARG   A CG  1 
ATOM   5886 C  CD  . ARG   D 1 146 ? -42.445 10.658  76.667  1.00 30.91 ?  141 ARG   A CD  1 
ATOM   5887 N  NE  . ARG   D 1 146 ? -41.883 11.320  77.836  1.00 35.57 ?  141 ARG   A NE  1 
ATOM   5888 C  CZ  . ARG   D 1 146 ? -40.586 11.417  78.108  1.00 40.57 ?  141 ARG   A CZ  1 
ATOM   5889 N  NH1 . ARG   D 1 146 ? -39.678 10.865  77.315  1.00 43.13 1  141 ARG   A NH1 1 
ATOM   5890 N  NH2 . ARG   D 1 146 ? -40.215 12.048  79.199  1.00 38.36 ?  141 ARG   A NH2 1 
ATOM   5891 N  N   . PHE   D 1 147 ? -46.305 13.019  73.991  1.00 18.76 ?  142 PHE   A N   1 
ATOM   5892 C  CA  . PHE   D 1 147 ? -46.916 12.334  72.820  1.00 19.73 ?  142 PHE   A CA  1 
ATOM   5893 C  C   . PHE   D 1 147 ? -48.012 13.166  72.130  1.00 19.08 ?  142 PHE   A C   1 
ATOM   5894 O  O   . PHE   D 1 147 ? -48.518 12.712  71.073  1.00 19.78 ?  142 PHE   A O   1 
ATOM   5895 C  CB  . PHE   D 1 147 ? -47.572 11.026  73.267  1.00 19.40 ?  142 PHE   A CB  1 
ATOM   5896 C  CG  . PHE   D 1 147 ? -46.631 10.105  74.006  1.00 19.53 ?  142 PHE   A CG  1 
ATOM   5897 C  CD1 . PHE   D 1 147 ? -45.691 9.348   73.317  1.00 20.69 ?  142 PHE   A CD1 1 
ATOM   5898 C  CD2 . PHE   D 1 147 ? -46.665 9.990   75.384  1.00 17.17 ?  142 PHE   A CD2 1 
ATOM   5899 C  CE1 . PHE   D 1 147 ? -44.810 8.526   73.993  1.00 19.63 ?  142 PHE   A CE1 1 
ATOM   5900 C  CE2 . PHE   D 1 147 ? -45.755 9.196   76.055  1.00 18.82 ?  142 PHE   A CE2 1 
ATOM   5901 C  CZ  . PHE   D 1 147 ? -44.801 8.491   75.363  1.00 18.43 ?  142 PHE   A CZ  1 
ATOM   5902 N  N   . GLY   D 1 148 ? -48.363 14.312  72.690  1.00 19.19 ?  143 GLY   A N   1 
ATOM   5903 C  CA  . GLY   D 1 148 ? -49.611 15.009  72.291  1.00 20.36 ?  143 GLY   A CA  1 
ATOM   5904 C  C   . GLY   D 1 148 ? -49.367 16.124  71.287  1.00 23.90 ?  143 GLY   A C   1 
ATOM   5905 O  O   . GLY   D 1 148 ? -48.306 16.135  70.612  1.00 22.63 ?  143 GLY   A O   1 
ATOM   5906 N  N   . ALA   D 1 149 ? -50.340 17.031  71.187  1.00 21.79 ?  144 ALA   A N   1 
ATOM   5907 C  CA  . ALA   D 1 149 ? -50.424 18.094  70.158  1.00 23.13 ?  144 ALA   A CA  1 
ATOM   5908 C  C   . ALA   D 1 149 ? -50.812 19.429  70.811  1.00 21.95 ?  144 ALA   A C   1 
ATOM   5909 O  O   . ALA   D 1 149 ? -51.537 20.227  70.196  1.00 29.56 ?  144 ALA   A O   1 
ATOM   5910 C  CB  . ALA   D 1 149 ? -51.342 17.617  69.062  1.00 25.02 ?  144 ALA   A CB  1 
ATOM   5911 N  N   . GLY   D 1 150 ? -50.352 19.695  72.031  1.00 22.96 ?  145 GLY   A N   1 
ATOM   5912 C  CA  . GLY   D 1 150 ? -50.487 21.001  72.680  1.00 20.77 ?  145 GLY   A CA  1 
ATOM   5913 C  C   . GLY   D 1 150 ? -51.847 21.223  73.297  1.00 25.72 ?  145 GLY   A C   1 
ATOM   5914 O  O   . GLY   D 1 150 ? -52.190 22.367  73.536  1.00 26.52 ?  145 GLY   A O   1 
ATOM   5915 N  N   . TRP   D 1 151 ? -52.612 20.163  73.576  1.00 22.08 ?  146 TRP   A N   1 
ATOM   5916 C  CA  . TRP   D 1 151 ? -53.962 20.329  74.196  1.00 19.90 ?  146 TRP   A CA  1 
ATOM   5917 C  C   . TRP   D 1 151 ? -53.808 20.891  75.615  1.00 20.40 ?  146 TRP   A C   1 
ATOM   5918 O  O   . TRP   D 1 151 ? -52.887 20.465  76.383  1.00 21.18 ?  146 TRP   A O   1 
ATOM   5919 C  CB  . TRP   D 1 151 ? -54.647 18.984  74.259  1.00 19.94 ?  146 TRP   A CB  1 
ATOM   5920 C  CG  . TRP   D 1 151 ? -56.036 19.013  74.808  1.00 16.96 ?  146 TRP   A CG  1 
ATOM   5921 C  CD1 . TRP   D 1 151 ? -57.118 19.642  74.287  1.00 21.72 ?  146 TRP   A CD1 1 
ATOM   5922 C  CD2 . TRP   D 1 151 ? -56.469 18.428  76.039  1.00 18.69 ?  146 TRP   A CD2 1 
ATOM   5923 N  NE1 . TRP   D 1 151 ? -58.213 19.488  75.099  1.00 16.88 ?  146 TRP   A NE1 1 
ATOM   5924 C  CE2 . TRP   D 1 151 ? -57.873 18.691  76.144  1.00 16.96 ?  146 TRP   A CE2 1 
ATOM   5925 C  CE3 . TRP   D 1 151 ? -55.860 17.643  77.020  1.00 16.94 ?  146 TRP   A CE3 1 
ATOM   5926 C  CZ2 . TRP   D 1 151 ? -58.614 18.237  77.233  1.00 18.99 ?  146 TRP   A CZ2 1 
ATOM   5927 C  CZ3 . TRP   D 1 151 ? -56.598 17.191  78.079  1.00 16.85 ?  146 TRP   A CZ3 1 
ATOM   5928 C  CH2 . TRP   D 1 151 ? -57.970 17.482  78.172  1.00 18.51 ?  146 TRP   A CH2 1 
ATOM   5929 N  N   . ASP   D 1 152 ? -54.718 21.786  75.970  1.00 21.62 ?  147 ASP   A N   1 
ATOM   5930 C  CA  . ASP   D 1 152 ? -54.795 22.422  77.300  1.00 20.02 ?  147 ASP   A CA  1 
ATOM   5931 C  C   . ASP   D 1 152 ? -55.988 21.810  78.023  1.00 21.61 ?  147 ASP   A C   1 
ATOM   5932 O  O   . ASP   D 1 152 ? -57.146 22.020  77.536  1.00 21.47 ?  147 ASP   A O   1 
ATOM   5933 C  CB  . ASP   D 1 152 ? -54.875 23.943  77.110  1.00 20.83 ?  147 ASP   A CB  1 
ATOM   5934 C  CG  . ASP   D 1 152 ? -55.118 24.705  78.390  1.00 23.01 ?  147 ASP   A CG  1 
ATOM   5935 O  OD1 . ASP   D 1 152 ? -55.031 24.094  79.465  1.00 21.57 ?  147 ASP   A OD1 1 
ATOM   5936 O  OD2 . ASP   D 1 152 ? -55.455 25.922  78.285  1.00 30.21 -1 147 ASP   A OD2 1 
ATOM   5937 N  N   . MET   D 1 153 ? -55.711 21.093  79.112  1.00 21.03 ?  148 MET   A N   1 
ATOM   5938 C  CA  . MET   D 1 153 ? -56.758 20.426  79.922  1.00 20.57 ?  148 MET   A CA  1 
ATOM   5939 C  C   . MET   D 1 153 ? -57.612 21.453  80.722  1.00 20.16 ?  148 MET   A C   1 
ATOM   5940 O  O   . MET   D 1 153 ? -58.631 21.039  81.369  1.00 22.19 ?  148 MET   A O   1 
ATOM   5941 C  CB  . MET   D 1 153 ? -56.109 19.412  80.836  1.00 23.06 ?  148 MET   A CB  1 
ATOM   5942 C  CG  . MET   D 1 153 ? -55.355 20.027  82.017  1.00 23.19 ?  148 MET   A CG  1 
ATOM   5943 S  SD  . MET   D 1 153 ? -54.771 18.779  83.223  1.00 28.13 ?  148 MET   A SD  1 
ATOM   5944 C  CE  . MET   D 1 153 ? -52.993 18.753  82.939  1.00 25.41 ?  148 MET   A CE  1 
ATOM   5945 N  N   . THR   D 1 154 ? -57.268 22.724  80.721  1.00 23.64 ?  149 THR   A N   1 
ATOM   5946 C  CA  . THR   D 1 154 ? -57.866 23.685  81.703  1.00 22.52 ?  149 THR   A CA  1 
ATOM   5947 C  C   . THR   D 1 154 ? -59.398 23.663  81.648  1.00 23.52 ?  149 THR   A C   1 
ATOM   5948 O  O   . THR   D 1 154 ? -60.012 23.499  82.716  1.00 25.98 ?  149 THR   A O   1 
ATOM   5949 C  CB  . THR   D 1 154 ? -57.352 25.107  81.447  1.00 23.80 ?  149 THR   A CB  1 
ATOM   5950 O  OG1 . THR   D 1 154 ? -55.913 25.094  81.530  1.00 28.21 ?  149 THR   A OG1 1 
ATOM   5951 C  CG2 . THR   D 1 154 ? -57.982 26.087  82.414  1.00 26.95 ?  149 THR   A CG2 1 
ATOM   5952 N  N   . GLY   D 1 155 ? -59.974 23.786  80.458  1.00 23.84 ?  150 GLY   A N   1 
ATOM   5953 C  CA  . GLY   D 1 155 ? -61.445 23.801  80.232  1.00 26.35 ?  150 GLY   A CA  1 
ATOM   5954 C  C   . GLY   D 1 155 ? -62.161 22.492  80.557  1.00 25.91 ?  150 GLY   A C   1 
ATOM   5955 O  O   . GLY   D 1 155 ? -63.427 22.454  80.491  1.00 27.86 ?  150 GLY   A O   1 
ATOM   5956 N  N   . SER   D 1 156 ? -61.419 21.423  80.836  1.00 23.20 ?  151 SER   A N   1 
ATOM   5957 C  CA  . SER   D 1 156 ? -61.927 20.060  81.084  1.00 18.12 ?  151 SER   A CA  1 
ATOM   5958 C  C   . SER   D 1 156 ? -61.718 19.654  82.537  1.00 17.49 ?  151 SER   A C   1 
ATOM   5959 O  O   . SER   D 1 156 ? -62.129 18.536  82.861  1.00 17.63 ?  151 SER   A O   1 
ATOM   5960 C  CB  . SER   D 1 156 ? -61.334 19.062  80.090  1.00 20.68 ?  151 SER   A CB  1 
ATOM   5961 O  OG  . SER   D 1 156 ? -61.658 19.440  78.764  1.00 19.46 ?  151 SER   A OG  1 
ATOM   5962 N  N   . LEU   D 1 157 ? -61.321 20.569  83.441  1.00 19.24 ?  152 LEU   A N   1 
ATOM   5963 C  CA  . LEU   D 1 157 ? -61.174 20.202  84.895  1.00 20.07 ?  152 LEU   A CA  1 
ATOM   5964 C  C   . LEU   D 1 157 ? -62.508 19.778  85.481  1.00 20.18 ?  152 LEU   A C   1 
ATOM   5965 O  O   . LEU   D 1 157 ? -62.579 18.763  86.233  1.00 21.78 ?  152 LEU   A O   1 
ATOM   5966 C  CB  . LEU   D 1 157 ? -60.558 21.324  85.750  1.00 23.43 ?  152 LEU   A CB  1 
ATOM   5967 C  CG  . LEU   D 1 157 ? -60.631 21.068  87.279  1.00 26.98 ?  152 LEU   A CG  1 
ATOM   5968 C  CD1 . LEU   D 1 157 ? -59.927 19.763  87.715  1.00 24.84 ?  152 LEU   A CD1 1 
ATOM   5969 C  CD2 . LEU   D 1 157 ? -60.151 22.252  88.144  1.00 28.04 ?  152 LEU   A CD2 1 
ATOM   5970 N  N   . ASP   D 1 158 ? -63.589 20.481  85.141  1.00 21.49 ?  153 ASP   A N   1 
ATOM   5971 C  CA  . ASP   D 1 158 ? -64.919 20.125  85.710  1.00 22.34 ?  153 ASP   A CA  1 
ATOM   5972 C  C   . ASP   D 1 158 ? -65.340 18.740  85.219  1.00 19.26 ?  153 ASP   A C   1 
ATOM   5973 O  O   . ASP   D 1 158 ? -65.860 17.943  86.014  1.00 21.22 ?  153 ASP   A O   1 
ATOM   5974 C  CB  . ASP   D 1 158 ? -65.894 21.254  85.417  1.00 23.34 ?  153 ASP   A CB  1 
ATOM   5975 C  CG  . ASP   D 1 158 ? -65.645 22.470  86.281  1.00 29.44 ?  153 ASP   A CG  1 
ATOM   5976 O  OD1 . ASP   D 1 158 ? -65.101 22.306  87.451  1.00 31.15 ?  153 ASP   A OD1 1 
ATOM   5977 O  OD2 . ASP   D 1 158 ? -65.996 23.545  85.810  1.00 32.14 -1 153 ASP   A OD2 1 
ATOM   5978 N  N   . TYR   D 1 159 ? -65.128 18.475  83.935  1.00 20.30 ?  154 TYR   A N   1 
ATOM   5979 C  CA  . TYR   D 1 159 ? -65.370 17.162  83.300  1.00 21.06 ?  154 TYR   A CA  1 
ATOM   5980 C  C   . TYR   D 1 159 ? -64.593 16.074  84.037  1.00 19.57 ?  154 TYR   A C   1 
ATOM   5981 O  O   . TYR   D 1 159 ? -65.157 15.038  84.432  1.00 20.15 ?  154 TYR   A O   1 
ATOM   5982 C  CB  . TYR   D 1 159 ? -65.061 17.252  81.800  1.00 20.05 ?  154 TYR   A CB  1 
ATOM   5983 C  CG  . TYR   D 1 159 ? -65.159 15.897  81.130  1.00 23.02 ?  154 TYR   A CG  1 
ATOM   5984 C  CD1 . TYR   D 1 159 ? -66.326 15.140  81.147  1.00 25.02 ?  154 TYR   A CD1 1 
ATOM   5985 C  CD2 . TYR   D 1 159 ? -64.087 15.377  80.432  1.00 23.82 ?  154 TYR   A CD2 1 
ATOM   5986 C  CE1 . TYR   D 1 159 ? -66.423 13.912  80.495  1.00 24.79 ?  154 TYR   A CE1 1 
ATOM   5987 C  CE2 . TYR   D 1 159 ? -64.177 14.163  79.755  1.00 22.59 ?  154 TYR   A CE2 1 
ATOM   5988 C  CZ  . TYR   D 1 159 ? -65.346 13.426  79.787  1.00 23.44 ?  154 TYR   A CZ  1 
ATOM   5989 O  OH  . TYR   D 1 159 ? -65.420 12.213  79.155  1.00 24.94 ?  154 TYR   A OH  1 
ATOM   5990 N  N   . PHE   D 1 160 ? -63.264 16.269  84.239  1.00 18.79 ?  155 PHE   A N   1 
ATOM   5991 C  CA  . PHE   D 1 160 ? -62.464 15.276  84.965  1.00 18.08 ?  155 PHE   A CA  1 
ATOM   5992 C  C   . PHE   D 1 160 ? -63.101 14.962  86.332  1.00 19.71 ?  155 PHE   A C   1 
ATOM   5993 O  O   . PHE   D 1 160 ? -63.113 13.758  86.771  1.00 18.86 ?  155 PHE   A O   1 
ATOM   5994 C  CB  . PHE   D 1 160 ? -61.022 15.796  85.159  1.00 17.02 ?  155 PHE   A CB  1 
ATOM   5995 C  CG  . PHE   D 1 160 ? -60.126 16.001  83.957  1.00 16.65 ?  155 PHE   A CG  1 
ATOM   5996 C  CD1 . PHE   D 1 160 ? -60.534 15.867  82.636  1.00 15.61 ?  155 PHE   A CD1 1 
ATOM   5997 C  CD2 . PHE   D 1 160 ? -58.771 16.252  84.180  1.00 19.66 ?  155 PHE   A CD2 1 
ATOM   5998 C  CE1 . PHE   D 1 160 ? -59.649 16.014  81.581  1.00 15.26 ?  155 PHE   A CE1 1 
ATOM   5999 C  CE2 . PHE   D 1 160 ? -57.884 16.411  83.115  1.00 17.64 ?  155 PHE   A CE2 1 
ATOM   6000 C  CZ  . PHE   D 1 160 ? -58.332 16.324  81.812  1.00 17.20 ?  155 PHE   A CZ  1 
ATOM   6001 N  N   . ARG   D 1 161 ? -63.545 16.006  87.038  1.00 18.97 ?  156 ARG   A N   1 
ATOM   6002 C  CA  . ARG   D 1 161 ? -64.017 15.822  88.434  1.00 20.71 ?  156 ARG   A CA  1 
ATOM   6003 C  C   . ARG   D 1 161 ? -65.338 15.039  88.406  1.00 22.01 ?  156 ARG   A C   1 
ATOM   6004 O  O   . ARG   D 1 161 ? -65.586 14.239  89.320  1.00 24.75 ?  156 ARG   A O   1 
ATOM   6005 C  CB  . ARG   D 1 161 ? -64.183 17.164  89.139  1.00 20.99 ?  156 ARG   A CB  1 
ATOM   6006 C  CG  . ARG   D 1 161 ? -62.843 17.886  89.344  1.00 25.38 ?  156 ARG   A CG  1 
ATOM   6007 C  CD  . ARG   D 1 161 ? -63.091 19.229  90.035  1.00 23.72 ?  156 ARG   A CD  1 
ATOM   6008 N  NE  . ARG   D 1 161 ? -63.528 18.891  91.379  1.00 27.79 ?  156 ARG   A NE  1 
ATOM   6009 C  CZ  . ARG   D 1 161 ? -64.122 19.704  92.252  1.00 34.19 ?  156 ARG   A CZ  1 
ATOM   6010 N  NH1 . ARG   D 1 161 ? -64.271 20.991  92.004  1.00 33.76 1  156 ARG   A NH1 1 
ATOM   6011 N  NH2 . ARG   D 1 161 ? -64.458 19.224  93.434  1.00 34.15 ?  156 ARG   A NH2 1 
ATOM   6012 N  N   . ARG   D 1 162 ? -66.100 15.237  87.356  1.00 18.47 ?  157 ARG   A N   1 
ATOM   6013 C  CA  . ARG   D 1 162 ? -67.400 14.557  87.218  1.00 22.19 ?  157 ARG   A CA  1 
ATOM   6014 C  C   . ARG   D 1 162 ? -67.169 13.069  86.930  1.00 23.52 ?  157 ARG   A C   1 
ATOM   6015 O  O   . ARG   D 1 162 ? -67.965 12.260  87.502  1.00 23.67 ?  157 ARG   A O   1 
ATOM   6016 C  CB  . ARG   D 1 162 ? -68.258 15.216  86.151  1.00 20.89 ?  157 ARG   A CB  1 
ATOM   6017 C  CG  . ARG   D 1 162 ? -69.630 14.565  86.034  1.00 22.52 ?  157 ARG   A CG  1 
ATOM   6018 C  CD  . ARG   D 1 162 ? -70.599 15.026  87.107  1.00 25.07 ?  157 ARG   A CD  1 
ATOM   6019 N  NE  . ARG   D 1 162 ? -71.830 14.225  87.082  1.00 25.90 ?  157 ARG   A NE  1 
ATOM   6020 C  CZ  . ARG   D 1 162 ? -73.042 14.593  87.530  1.00 26.20 ?  157 ARG   A CZ  1 
ATOM   6021 N  NH1 . ARG   D 1 162 ? -73.233 15.809  87.999  1.00 27.29 1  157 ARG   A NH1 1 
ATOM   6022 N  NH2 . ARG   D 1 162 ? -74.070 13.747  87.464  1.00 26.43 ?  157 ARG   A NH2 1 
ATOM   6023 N  N   . ILE   D 1 163 ? -66.146 12.684  86.128  1.00 23.49 ?  158 ILE   A N   1 
ATOM   6024 C  CA  . ILE   D 1 163 ? -65.982 11.256  85.713  1.00 20.95 ?  158 ILE   A CA  1 
ATOM   6025 C  C   . ILE   D 1 163 ? -65.085 10.520  86.707  1.00 22.84 ?  158 ILE   A C   1 
ATOM   6026 O  O   . ILE   D 1 163 ? -65.040 9.275   86.658  1.00 24.65 ?  158 ILE   A O   1 
ATOM   6027 C  CB  . ILE   D 1 163 ? -65.528 11.107  84.265  1.00 21.17 ?  158 ILE   A CB  1 
ATOM   6028 C  CG1 . ILE   D 1 163 ? -64.125 11.657  83.998  1.00 23.89 ?  158 ILE   A CG1 1 
ATOM   6029 C  CG2 . ILE   D 1 163 ? -66.513 11.739  83.334  1.00 20.20 ?  158 ILE   A CG2 1 
ATOM   6030 C  CD1 . ILE   D 1 163 ? -63.701 11.440  82.575  1.00 21.00 ?  158 ILE   A CD1 1 
ATOM   6031 N  N   . LEU   D 1 164 ? -64.560 11.238  87.667  1.00 19.06 ?  159 LEU   A N   1 
ATOM   6032 C  CA  . LEU   D 1 164 ? -63.535 10.738  88.597  1.00 23.70 ?  159 LEU   A CA  1 
ATOM   6033 C  C   . LEU   D 1 164 ? -64.012 9.485   89.332  1.00 22.76 ?  159 LEU   A C   1 
ATOM   6034 O  O   . LEU   D 1 164 ? -63.168 8.668   89.670  1.00 22.58 ?  159 LEU   A O   1 
ATOM   6035 C  CB  . LEU   D 1 164 ? -63.142 11.851  89.566  1.00 22.77 ?  159 LEU   A CB  1 
ATOM   6036 C  CG  . LEU   D 1 164 ? -61.782 11.663  90.203  1.00 25.35 ?  159 LEU   A CG  1 
ATOM   6037 C  CD1 . LEU   D 1 164 ? -60.677 11.932  89.186  1.00 24.17 ?  159 LEU   A CD1 1 
ATOM   6038 C  CD2 . LEU   D 1 164 ? -61.663 12.579  91.414  1.00 26.63 ?  159 LEU   A CD2 1 
ATOM   6039 N  N   . PRO   D 1 165 ? -65.323 9.312   89.691  1.00 23.69 ?  160 PRO   A N   1 
ATOM   6040 C  CA  . PRO   D 1 165 ? -65.791 8.100   90.374  1.00 24.26 ?  160 PRO   A CA  1 
ATOM   6041 C  C   . PRO   D 1 165 ? -65.488 6.781   89.642  1.00 23.15 ?  160 PRO   A C   1 
ATOM   6042 O  O   . PRO   D 1 165 ? -65.411 5.792   90.321  1.00 25.22 ?  160 PRO   A O   1 
ATOM   6043 C  CB  . PRO   D 1 165 ? -67.331 8.286   90.463  1.00 26.70 ?  160 PRO   A CB  1 
ATOM   6044 C  CG  . PRO   D 1 165 ? -67.488 9.797   90.514  1.00 28.90 ?  160 PRO   A CG  1 
ATOM   6045 C  CD  . PRO   D 1 165 ? -66.424 10.282  89.541  1.00 28.64 ?  160 PRO   A CD  1 
ATOM   6046 N  N   . GLY   D 1 166 ? -65.337 6.811   88.314  1.00 22.31 ?  161 GLY   A N   1 
ATOM   6047 C  CA  . GLY   D 1 166 ? -65.006 5.674   87.437  1.00 22.26 ?  161 GLY   A CA  1 
ATOM   6048 C  C   . GLY   D 1 166 ? -63.542 5.287   87.479  1.00 22.24 ?  161 GLY   A C   1 
ATOM   6049 O  O   . GLY   D 1 166 ? -63.213 4.198   86.989  1.00 20.84 ?  161 GLY   A O   1 
ATOM   6050 N  N   . VAL   D 1 167 ? -62.696 6.140   88.054  1.00 21.47 ?  162 VAL   A N   1 
ATOM   6051 C  CA  . VAL   D 1 167 ? -61.219 5.928   88.056  1.00 18.68 ?  162 VAL   A CA  1 
ATOM   6052 C  C   . VAL   D 1 167 ? -60.826 5.087   89.270  1.00 21.11 ?  162 VAL   A C   1 
ATOM   6053 O  O   . VAL   D 1 167 ? -61.083 5.517   90.446  1.00 21.57 ?  162 VAL   A O   1 
ATOM   6054 C  CB  . VAL   D 1 167 ? -60.472 7.271   88.065  1.00 17.75 ?  162 VAL   A CB  1 
ATOM   6055 C  CG1 . VAL   D 1 167 ? -58.958 7.054   88.033  1.00 20.37 ?  162 VAL   A CG1 1 
ATOM   6056 C  CG2 . VAL   D 1 167 ? -60.887 8.189   86.922  1.00 19.60 ?  162 VAL   A CG2 1 
ATOM   6057 N  N   . GLY   D 1 168 ? -60.102 3.993   89.020  1.00 21.22 ?  163 GLY   A N   1 
ATOM   6058 C  CA  . GLY   D 1 168 ? -59.301 3.293   90.026  1.00 20.00 ?  163 GLY   A CA  1 
ATOM   6059 C  C   . GLY   D 1 168 ? -57.850 3.742   89.942  1.00 20.98 ?  163 GLY   A C   1 
ATOM   6060 O  O   . GLY   D 1 168 ? -57.104 3.159   89.155  1.00 19.28 ?  163 GLY   A O   1 
ATOM   6061 N  N   . ALA   D 1 169 ? -57.445 4.744   90.723  1.00 20.79 ?  164 ALA   A N   1 
ATOM   6062 C  CA  . ALA   D 1 169 ? -56.046 5.208   90.745  1.00 19.11 ?  164 ALA   A CA  1 
ATOM   6063 C  C   . ALA   D 1 169 ? -55.232 4.337   91.683  1.00 19.95 ?  164 ALA   A C   1 
ATOM   6064 O  O   . ALA   D 1 169 ? -55.760 3.800   92.685  1.00 21.71 ?  164 ALA   A O   1 
ATOM   6065 C  CB  . ALA   D 1 169 ? -55.984 6.689   91.093  1.00 18.35 ?  164 ALA   A CB  1 
ATOM   6066 N  N   . PHE   D 1 170 ? -53.922 4.241   91.457  1.00 19.74 ?  165 PHE   A N   1 
ATOM   6067 C  CA  . PHE   D 1 170 ? -53.088 3.363   92.271  1.00 19.00 ?  165 PHE   A CA  1 
ATOM   6068 C  C   . PHE   D 1 170 ? -51.676 3.907   92.249  1.00 19.81 ?  165 PHE   A C   1 
ATOM   6069 O  O   . PHE   D 1 170 ? -51.377 4.804   91.457  1.00 18.94 ?  165 PHE   A O   1 
ATOM   6070 C  CB  . PHE   D 1 170 ? -53.247 1.918   91.788  1.00 20.34 ?  165 PHE   A CB  1 
ATOM   6071 C  CG  . PHE   D 1 170 ? -52.799 1.677   90.368  1.00 20.63 ?  165 PHE   A CG  1 
ATOM   6072 C  CD1 . PHE   D 1 170 ? -51.460 1.581   90.058  1.00 23.04 ?  165 PHE   A CD1 1 
ATOM   6073 C  CD2 . PHE   D 1 170 ? -53.714 1.532   89.357  1.00 22.00 ?  165 PHE   A CD2 1 
ATOM   6074 C  CE1 . PHE   D 1 170 ? -51.050 1.364   88.755  1.00 23.87 ?  165 PHE   A CE1 1 
ATOM   6075 C  CE2 . PHE   D 1 170 ? -53.299 1.230   88.068  1.00 21.99 ?  165 PHE   A CE2 1 
ATOM   6076 C  CZ  . PHE   D 1 170 ? -51.973 1.228   87.762  1.00 23.36 ?  165 PHE   A CZ  1 
ATOM   6077 N  N   . ARG   D 1 171 ? -50.921 3.428   93.199  1.00 19.16 ?  166 ARG   A N   1 
ATOM   6078 C  CA  . ARG   D 1 171 ? -49.476 3.679   93.394  1.00 20.42 ?  166 ARG   A CA  1 
ATOM   6079 C  C   . ARG   D 1 171 ? -48.771 2.342   93.403  1.00 23.01 ?  166 ARG   A C   1 
ATOM   6080 O  O   . ARG   D 1 171 ? -49.208 1.379   94.121  1.00 23.62 ?  166 ARG   A O   1 
ATOM   6081 C  CB  . ARG   D 1 171 ? -49.332 4.457   94.708  1.00 22.21 ?  166 ARG   A CB  1 
ATOM   6082 C  CG  . ARG   D 1 171 ? -50.106 5.773   94.717  1.00 23.61 ?  166 ARG   A CG  1 
ATOM   6083 C  CD  . ARG   D 1 171 ? -49.350 6.772   93.885  1.00 24.37 ?  166 ARG   A CD  1 
ATOM   6084 N  NE  . ARG   D 1 171 ? -49.945 8.106   93.925  1.00 24.08 ?  166 ARG   A NE  1 
ATOM   6085 C  CZ  . ARG   D 1 171 ? -50.967 8.492   93.167  1.00 22.26 ?  166 ARG   A CZ  1 
ATOM   6086 N  NH1 . ARG   D 1 171 ? -51.474 7.690   92.243  1.00 23.27 1  166 ARG   A NH1 1 
ATOM   6087 N  NH2 . ARG   D 1 171 ? -51.442 9.708   93.301  1.00 23.59 ?  166 ARG   A NH2 1 
ATOM   6088 N  N   . LEU   D 1 172 ? -47.628 2.261   92.746  1.00 23.81 ?  167 LEU   A N   1 
ATOM   6089 C  CA  . LEU   D 1 172 ? -46.837 1.027   92.733  1.00 22.87 ?  167 LEU   A CA  1 
ATOM   6090 C  C   . LEU   D 1 172 ? -45.419 1.405   93.120  1.00 25.74 ?  167 LEU   A C   1 
ATOM   6091 O  O   . LEU   D 1 172 ? -44.741 2.049   92.316  1.00 25.33 ?  167 LEU   A O   1 
ATOM   6092 C  CB  . LEU   D 1 172 ? -46.948 0.455   91.316  1.00 22.02 ?  167 LEU   A CB  1 
ATOM   6093 C  CG  . LEU   D 1 172 ? -46.229 -0.847  91.051  1.00 25.88 ?  167 LEU   A CG  1 
ATOM   6094 C  CD1 . LEU   D 1 172 ? -46.613 -1.895  92.096  1.00 31.08 ?  167 LEU   A CD1 1 
ATOM   6095 C  CD2 . LEU   D 1 172 ? -46.566 -1.299  89.647  1.00 23.74 ?  167 LEU   A CD2 1 
ATOM   6096 N  N   . ARG   D 1 173 ? -45.025 1.107   94.355  1.00 24.17 ?  168 ARG   A N   1 
ATOM   6097 C  CA  . ARG   D 1 173 ? -43.638 1.340   94.786  1.00 26.77 ?  168 ARG   A CA  1 
ATOM   6098 C  C   . ARG   D 1 173 ? -42.847 0.206   94.166  1.00 22.73 ?  168 ARG   A C   1 
ATOM   6099 O  O   . ARG   D 1 173 ? -43.137 -0.951  94.471  1.00 24.31 ?  168 ARG   A O   1 
ATOM   6100 C  CB  . ARG   D 1 173 ? -43.510 1.369   96.319  1.00 33.78 ?  168 ARG   A CB  1 
ATOM   6101 C  CG  . ARG   D 1 173 ? -42.077 1.497   96.830  1.00 39.40 ?  168 ARG   A CG  1 
ATOM   6102 C  CD  . ARG   D 1 173 ? -41.666 2.941   96.994  1.00 52.93 ?  168 ARG   A CD  1 
ATOM   6103 N  NE  . ARG   D 1 173 ? -40.570 3.139   97.935  1.00 63.76 ?  168 ARG   A NE  1 
ATOM   6104 C  CZ  . ARG   D 1 173 ? -40.115 4.328   98.329  1.00 73.38 ?  168 ARG   A CZ  1 
ATOM   6105 N  NH1 . ARG   D 1 173 ? -39.104 4.402   99.183  1.00 78.83 1  168 ARG   A NH1 1 
ATOM   6106 N  NH2 . ARG   D 1 173 ? -40.663 5.439   97.860  1.00 77.33 ?  168 ARG   A NH2 1 
ATOM   6107 N  N   . VAL   D 1 174 ? -41.838 0.539   93.389  1.00 25.39 ?  169 VAL   A N   1 
ATOM   6108 C  CA  . VAL   D 1 174 ? -41.021 -0.455  92.676  1.00 24.20 ?  169 VAL   A CA  1 
ATOM   6109 C  C   . VAL   D 1 174 ? -40.070 -1.125  93.674  1.00 26.06 ?  169 VAL   A C   1 
ATOM   6110 O  O   . VAL   D 1 174 ? -39.149 -0.454  94.147  1.00 27.96 ?  169 VAL   A O   1 
ATOM   6111 C  CB  . VAL   D 1 174 ? -40.295 0.227   91.516  1.00 25.93 ?  169 VAL   A CB  1 
ATOM   6112 C  CG1 . VAL   D 1 174 ? -39.357 -0.710  90.785  1.00 25.32 ?  169 VAL   A CG1 1 
ATOM   6113 C  CG2 . VAL   D 1 174 ? -41.310 0.860   90.560  1.00 25.14 ?  169 VAL   A CG2 1 
ATOM   6114 N  N   . ALA   D 1 175 ? -40.284 -2.412  93.941  1.00 26.65 ?  170 ALA   A N   1 
ATOM   6115 C  CA  . ALA   D 1 175 ? -39.399 -3.265  94.771  1.00 27.90 ?  170 ALA   A CA  1 
ATOM   6116 C  C   . ALA   D 1 175 ? -38.310 -3.890  93.905  1.00 28.66 ?  170 ALA   A C   1 
ATOM   6117 O  O   . ALA   D 1 175 ? -37.140 -3.953  94.338  1.00 28.72 ?  170 ALA   A O   1 
ATOM   6118 C  CB  . ALA   D 1 175 ? -40.227 -4.315  95.453  1.00 29.76 ?  170 ALA   A CB  1 
ATOM   6119 N  N   . GLU   D 1 176 ? -38.663 -4.301  92.680  1.00 26.83 ?  171 GLU   A N   1 
ATOM   6120 C  CA  . GLU   D 1 176 ? -37.704 -4.884  91.723  1.00 28.99 ?  171 GLU   A CA  1 
ATOM   6121 C  C   . GLU   D 1 176 ? -37.999 -4.339  90.322  1.00 25.28 ?  171 GLU   A C   1 
ATOM   6122 O  O   . GLU   D 1 176 ? -39.168 -4.184  89.938  1.00 21.53 ?  171 GLU   A O   1 
ATOM   6123 C  CB  . GLU   D 1 176 ? -37.779 -6.412  91.604  1.00 35.75 ?  171 GLU   A CB  1 
ATOM   6124 C  CG  . GLU   D 1 176 ? -38.002 -7.134  92.914  1.00 42.51 ?  171 GLU   A CG  1 
ATOM   6125 C  CD  . GLU   D 1 176 ? -38.023 -8.641  92.735  1.00 54.22 ?  171 GLU   A CD  1 
ATOM   6126 O  OE1 . GLU   D 1 176 ? -36.930 -9.211  92.539  1.00 57.65 ?  171 GLU   A OE1 1 
ATOM   6127 O  OE2 . GLU   D 1 176 ? -39.138 -9.236  92.755  1.00 62.82 -1 171 GLU   A OE2 1 
ATOM   6128 N  N   . ALA   D 1 177 ? -36.949 -4.144  89.567  1.00 22.72 ?  172 ALA   A N   1 
ATOM   6129 C  CA  . ALA   D 1 177 ? -37.091 -3.727  88.159  1.00 24.83 ?  172 ALA   A CA  1 
ATOM   6130 C  C   . ALA   D 1 177 ? -36.084 -4.493  87.328  1.00 27.94 ?  172 ALA   A C   1 
ATOM   6131 O  O   . ALA   D 1 177 ? -34.879 -4.473  87.653  1.00 30.21 ?  172 ALA   A O   1 
ATOM   6132 C  CB  . ALA   D 1 177 ? -36.878 -2.250  88.030  1.00 25.46 ?  172 ALA   A CB  1 
ATOM   6133 N  N   . ASP   D 1 178 ? -36.558 -5.107  86.263  1.00 23.92 ?  173 ASP   A N   1 
ATOM   6134 C  CA  . ASP   D 1 178 ? -35.698 -5.901  85.362  1.00 23.61 ?  173 ASP   A CA  1 
ATOM   6135 C  C   . ASP   D 1 178 ? -35.892 -5.379  83.941  1.00 23.23 ?  173 ASP   A C   1 
ATOM   6136 O  O   . ASP   D 1 178 ? -37.043 -5.040  83.589  1.00 21.75 ?  173 ASP   A O   1 
ATOM   6137 C  CB  . ASP   D 1 178 ? -36.078 -7.361  85.459  1.00 25.38 ?  173 ASP   A CB  1 
ATOM   6138 C  CG  . ASP   D 1 178 ? -35.737 -7.908  86.826  1.00 33.36 ?  173 ASP   A CG  1 
ATOM   6139 O  OD1 . ASP   D 1 178 ? -36.698 -8.136  87.625  1.00 31.64 ?  173 ASP   A OD1 1 
ATOM   6140 O  OD2 . ASP   D 1 178 ? -34.493 -8.083  87.076  1.00 32.73 -1 173 ASP   A OD2 1 
ATOM   6141 N  N   . GLY   D 1 179 ? -34.802 -5.264  83.196  1.00 21.89 ?  174 GLY   A N   1 
ATOM   6142 C  CA  . GLY   D 1 179 ? -34.830 -4.783  81.807  1.00 21.76 ?  174 GLY   A CA  1 
ATOM   6143 C  C   . GLY   D 1 179 ? -34.255 -5.828  80.879  1.00 24.72 ?  174 GLY   A C   1 
ATOM   6144 O  O   . GLY   D 1 179 ? -33.073 -6.214  81.060  1.00 24.99 ?  174 GLY   A O   1 
ATOM   6145 N  N   . MET   D 1 180 ? -35.027 -6.218  79.877  1.00 21.39 ?  175 MET   A N   1 
ATOM   6146 C  CA  . MET   D 1 180 ? -34.552 -7.020  78.735  1.00 20.83 ?  175 MET   A CA  1 
ATOM   6147 C  C   . MET   D 1 180 ? -34.258 -6.084  77.557  1.00 20.23 ?  175 MET   A C   1 
ATOM   6148 O  O   . MET   D 1 180 ? -35.211 -5.445  77.060  1.00 20.56 ?  175 MET   A O   1 
ATOM   6149 C  CB  . MET   D 1 180 ? -35.586 -8.072  78.354  1.00 23.27 ?  175 MET   A CB  1 
ATOM   6150 C  CG  . MET   D 1 180 ? -35.220 -8.859  77.137  1.00 26.57 ?  175 MET   A CG  1 
ATOM   6151 S  SD  . MET   D 1 180 ? -34.188 -10.308 77.414  1.00 27.58 ?  175 MET   A SD  1 
ATOM   6152 C  CE  . MET   D 1 180 ? -35.373 -11.381 78.237  1.00 22.65 ?  175 MET   A CE  1 
ATOM   6153 N  N   . PHE   D 1 181 ? -32.982 -5.917  77.187  1.00 18.03 ?  176 PHE   A N   1 
ATOM   6154 C  CA  . PHE   D 1 181 ? -32.591 -5.129  76.006  1.00 20.62 ?  176 PHE   A CA  1 
ATOM   6155 C  C   . PHE   D 1 181 ? -31.970 -6.085  74.982  1.00 20.17 ?  176 PHE   A C   1 
ATOM   6156 O  O   . PHE   D 1 181 ? -30.711 -6.244  74.928  1.00 20.91 ?  176 PHE   A O   1 
ATOM   6157 C  CB  . PHE   D 1 181 ? -31.704 -3.961  76.426  1.00 21.94 ?  176 PHE   A CB  1 
ATOM   6158 C  CG  . PHE   D 1 181 ? -32.482 -2.936  77.189  1.00 23.98 ?  176 PHE   A CG  1 
ATOM   6159 C  CD1 . PHE   D 1 181 ? -32.762 -3.096  78.542  1.00 25.14 ?  176 PHE   A CD1 1 
ATOM   6160 C  CD2 . PHE   D 1 181 ? -33.077 -1.890  76.503  1.00 24.13 ?  176 PHE   A CD2 1 
ATOM   6161 C  CE1 . PHE   D 1 181 ? -33.561 -2.170  79.200  1.00 25.80 ?  176 PHE   A CE1 1 
ATOM   6162 C  CE2 . PHE   D 1 181 ? -33.856 -0.963  77.169  1.00 21.28 ?  176 PHE   A CE2 1 
ATOM   6163 C  CZ  . PHE   D 1 181 ? -34.080 -1.092  78.511  1.00 23.78 ?  176 PHE   A CZ  1 
ATOM   6164 N  N   . LYS   D 1 182 ? -32.826 -6.822  74.281  1.00 19.91 ?  177 LYS   A N   1 
ATOM   6165 C  CA  . LYS   D 1 182 ? -32.389 -7.915  73.372  1.00 17.30 ?  177 LYS   A CA  1 
ATOM   6166 C  C   . LYS   D 1 182 ? -32.108 -7.298  71.996  1.00 19.21 ?  177 LYS   A C   1 
ATOM   6167 O  O   . LYS   D 1 182 ? -33.047 -7.020  71.262  1.00 14.76 ?  177 LYS   A O   1 
ATOM   6168 C  CB  . LYS   D 1 182 ? -33.380 -9.065  73.399  1.00 17.66 ?  177 LYS   A CB  1 
ATOM   6169 C  CG  . LYS   D 1 182 ? -33.094 -10.181 72.420  1.00 19.22 ?  177 LYS   A CG  1 
ATOM   6170 C  CD  . LYS   D 1 182 ? -33.942 -11.384 72.627  1.00 23.70 ?  177 LYS   A CD  1 
ATOM   6171 C  CE  . LYS   D 1 182 ? -33.758 -12.431 71.558  1.00 27.34 ?  177 LYS   A CE  1 
ATOM   6172 N  NZ  . LYS   D 1 182 ? -32.334 -12.694 71.268  1.00 31.15 1  177 LYS   A NZ  1 
ATOM   6173 N  N   . LEU   D 1 183 ? -30.816 -6.993  71.739  1.00 18.17 ?  178 LEU   A N   1 
ATOM   6174 C  CA  . LEU   D 1 183 ? -30.373 -6.068  70.661  1.00 20.11 ?  178 LEU   A CA  1 
ATOM   6175 C  C   . LEU   D 1 183 ? -29.123 -6.640  69.970  1.00 18.89 ?  178 LEU   A C   1 
ATOM   6176 O  O   . LEU   D 1 183 ? -28.267 -5.846  69.553  1.00 21.87 ?  178 LEU   A O   1 
ATOM   6177 C  CB  . LEU   D 1 183 ? -30.063 -4.715  71.302  1.00 19.34 ?  178 LEU   A CB  1 
ATOM   6178 C  CG  . LEU   D 1 183 ? -31.256 -3.944  71.875  1.00 20.90 ?  178 LEU   A CG  1 
ATOM   6179 C  CD1 . LEU   D 1 183 ? -30.749 -2.687  72.583  1.00 21.63 ?  178 LEU   A CD1 1 
ATOM   6180 C  CD2 . LEU   D 1 183 ? -32.268 -3.582  70.781  1.00 21.54 ?  178 LEU   A CD2 1 
ATOM   6181 N  N   . SER   D 1 184 ? -29.109 -7.947  69.762  1.00 18.98 ?  179 SER   A N   1 
ATOM   6182 C  CA  . SER   D 1 184 ? -28.120 -8.703  68.950  1.00 20.55 ?  179 SER   A CA  1 
ATOM   6183 C  C   . SER   D 1 184 ? -26.773 -8.711  69.665  1.00 21.09 ?  179 SER   A C   1 
ATOM   6184 O  O   . SER   D 1 184 ? -25.766 -9.015  68.985  1.00 22.21 ?  179 SER   A O   1 
ATOM   6185 C  CB  . SER   D 1 184 ? -28.004 -8.159  67.538  1.00 21.85 ?  179 SER   A CB  1 
ATOM   6186 O  OG  . SER   D 1 184 ? -29.231 -8.353  66.826  1.00 19.60 ?  179 SER   A OG  1 
ATOM   6187 N  N   . GLN   D 1 185 ? -26.746 -8.466  70.979  1.00 20.44 ?  180 GLN   A N   1 
ATOM   6188 C  CA  . GLN   D 1 185 ? -25.444 -8.440  71.727  1.00 22.40 ?  180 GLN   A CA  1 
ATOM   6189 C  C   . GLN   D 1 185 ? -24.749 -9.808  71.652  1.00 25.25 ?  180 GLN   A C   1 
ATOM   6190 O  O   . GLN   D 1 185 ? -23.471 -9.854  71.742  1.00 26.39 ?  180 GLN   A O   1 
ATOM   6191 C  CB  . GLN   D 1 185 ? -25.557 -7.938  73.173  1.00 20.64 ?  180 GLN   A CB  1 
ATOM   6192 C  CG  . GLN   D 1 185 ? -26.034 -6.500  73.326  1.00 20.85 ?  180 GLN   A CG  1 
ATOM   6193 C  CD  . GLN   D 1 185 ? -27.545 -6.492  73.517  1.00 20.59 ?  180 GLN   A CD  1 
ATOM   6194 O  OE1 . GLN   D 1 185 ? -28.260 -7.215  72.816  1.00 21.00 ?  180 GLN   A OE1 1 
ATOM   6195 N  NE2 . GLN   D 1 185 ? -28.001 -5.749  74.512  1.00 21.30 ?  180 GLN   A NE2 1 
ATOM   6196 N  N   . GLU   D 1 186 ? -25.474 -10.891 71.420  1.00 25.06 ?  181 GLU   A N   1 
ATOM   6197 C  CA  . GLU   D 1 186 ? -24.912 -12.264 71.365  1.00 28.35 ?  181 GLU   A CA  1 
ATOM   6198 C  C   . GLU   D 1 186 ? -24.133 -12.475 70.058  1.00 28.50 ?  181 GLU   A C   1 
ATOM   6199 O  O   . GLU   D 1 186 ? -23.446 -13.492 69.929  1.00 29.01 ?  181 GLU   A O   1 
ATOM   6200 C  CB  . GLU   D 1 186 ? -26.049 -13.273 71.496  1.00 26.95 ?  181 GLU   A CB  1 
ATOM   6201 C  CG  . GLU   D 1 186 ? -26.848 -13.525 70.213  1.00 27.31 ?  181 GLU   A CG  1 
ATOM   6202 C  CD  . GLU   D 1 186 ? -27.847 -12.482 69.747  1.00 25.01 ?  181 GLU   A CD  1 
ATOM   6203 O  OE1 . GLU   D 1 186 ? -28.061 -11.513 70.494  1.00 24.80 ?  181 GLU   A OE1 1 
ATOM   6204 O  OE2 . GLU   D 1 186 ? -28.477 -12.692 68.656  1.00 27.22 -1 181 GLU   A OE2 1 
ATOM   6205 N  N   . GLN   D 1 187 ? -24.337 -11.631 69.051  1.00 25.97 ?  182 GLN   A N   1 
ATOM   6206 C  CA  . GLN   D 1 187 ? -23.706 -11.838 67.722  1.00 24.48 ?  182 GLN   A CA  1 
ATOM   6207 C  C   . GLN   D 1 187 ? -22.286 -11.271 67.768  1.00 24.16 ?  182 GLN   A C   1 
ATOM   6208 O  O   . GLN   D 1 187 ? -22.024 -10.440 68.649  1.00 25.15 ?  182 GLN   A O   1 
ATOM   6209 C  CB  . GLN   D 1 187 ? -24.499 -11.167 66.607  1.00 24.92 ?  182 GLN   A CB  1 
ATOM   6210 C  CG  . GLN   D 1 187 ? -25.870 -11.756 66.337  1.00 22.61 ?  182 GLN   A CG  1 
ATOM   6211 C  CD  . GLN   D 1 187 ? -25.877 -13.220 65.983  1.00 28.34 ?  182 GLN   A CD  1 
ATOM   6212 O  OE1 . GLN   D 1 187 ? -25.055 -13.698 65.188  1.00 26.65 ?  182 GLN   A OE1 1 
ATOM   6213 N  NE2 . GLN   D 1 187 ? -26.816 -13.960 66.571  1.00 27.97 ?  182 GLN   A NE2 1 
ATOM   6214 N  N   . GLN   D 1 188 ? -21.440 -11.705 66.836  1.00 25.59 ?  183 GLN   A N   1 
ATOM   6215 C  CA  . GLN   D 1 188 ? -20.090 -11.135 66.589  1.00 27.79 ?  183 GLN   A CA  1 
ATOM   6216 C  C   . GLN   D 1 188 ? -20.273 -9.685  66.135  1.00 30.28 ?  183 GLN   A C   1 
ATOM   6217 O  O   . GLN   D 1 188 ? -21.272 -9.360  65.495  1.00 28.95 ?  183 GLN   A O   1 
ATOM   6218 C  CB  . GLN   D 1 188 ? -19.353 -11.998 65.574  1.00 30.66 ?  183 GLN   A CB  1 
ATOM   6219 C  CG  . GLN   D 1 188 ? -18.980 -13.378 66.106  1.00 38.24 ?  183 GLN   A CG  1 
ATOM   6220 C  CD  . GLN   D 1 188 ? -18.007 -13.282 67.264  1.00 46.81 ?  183 GLN   A CD  1 
ATOM   6221 O  OE1 . GLN   D 1 188 ? -18.240 -13.828 68.339  1.00 55.29 ?  183 GLN   A OE1 1 
ATOM   6222 N  NE2 . GLN   D 1 188 ? -16.932 -12.524 67.091  1.00 53.93 ?  183 GLN   A NE2 1 
ATOM   6223 N  N   . PRO   D 1 189 ? -19.349 -8.761  66.476  1.00 33.33 ?  184 PRO   A N   1 
ATOM   6224 C  CA  . PRO   D 1 189 ? -19.549 -7.333  66.217  1.00 33.41 ?  184 PRO   A CA  1 
ATOM   6225 C  C   . PRO   D 1 189 ? -19.849 -6.965  64.749  1.00 32.73 ?  184 PRO   A C   1 
ATOM   6226 O  O   . PRO   D 1 189 ? -20.628 -6.041  64.552  1.00 32.59 ?  184 PRO   A O   1 
ATOM   6227 C  CB  . PRO   D 1 189 ? -18.210 -6.693  66.645  1.00 36.56 ?  184 PRO   A CB  1 
ATOM   6228 C  CG  . PRO   D 1 189 ? -17.609 -7.686  67.606  1.00 33.95 ?  184 PRO   A CG  1 
ATOM   6229 C  CD  . PRO   D 1 189 ? -18.025 -9.038  67.079  1.00 33.33 ?  184 PRO   A CD  1 
ATOM   6230 N  N   . ALA   D 1 190 ? -19.253 -7.659  63.771  1.00 30.85 ?  185 ALA   A N   1 
ATOM   6231 C  CA  . ALA   D 1 190 ? -19.525 -7.460  62.327  1.00 29.27 ?  185 ALA   A CA  1 
ATOM   6232 C  C   . ALA   D 1 190 ? -20.993 -7.799  62.010  1.00 28.01 ?  185 ALA   A C   1 
ATOM   6233 O  O   . ALA   D 1 190 ? -21.621 -7.069  61.218  1.00 25.20 ?  185 ALA   A O   1 
ATOM   6234 C  CB  . ALA   D 1 190 ? -18.597 -8.278  61.487  1.00 33.90 ?  185 ALA   A CB  1 
ATOM   6235 N  N   . ILE   D 1 191 ? -21.533 -8.845  62.617  1.00 24.36 ?  186 ILE   A N   1 
ATOM   6236 C  CA  . ILE   D 1 191 ? -22.961 -9.239  62.388  1.00 23.78 ?  186 ILE   A CA  1 
ATOM   6237 C  C   . ILE   D 1 191 ? -23.869 -8.218  63.079  1.00 23.74 ?  186 ILE   A C   1 
ATOM   6238 O  O   . ILE   D 1 191 ? -24.902 -7.832  62.457  1.00 22.64 ?  186 ILE   A O   1 
ATOM   6239 C  CB  . ILE   D 1 191 ? -23.236 -10.683 62.840  1.00 25.68 ?  186 ILE   A CB  1 
ATOM   6240 C  CG1 . ILE   D 1 191 ? -22.269 -11.703 62.230  1.00 31.15 ?  186 ILE   A CG1 1 
ATOM   6241 C  CG2 . ILE   D 1 191 ? -24.686 -11.053 62.605  1.00 25.91 ?  186 ILE   A CG2 1 
ATOM   6242 C  CD1 . ILE   D 1 191 ? -22.097 -11.590 60.759  1.00 30.97 ?  186 ILE   A CD1 1 
ATOM   6243 N  N   . ARG   D 1 192 ? -23.549 -7.810  64.303  1.00 20.48 ?  187 ARG   A N   1 
ATOM   6244 C  CA  . ARG   D 1 192 ? -24.300 -6.758  65.040  1.00 23.48 ?  187 ARG   A CA  1 
ATOM   6245 C  C   . ARG   D 1 192 ? -24.402 -5.502  64.178  1.00 23.93 ?  187 ARG   A C   1 
ATOM   6246 O  O   . ARG   D 1 192 ? -25.473 -4.890  64.112  1.00 22.05 ?  187 ARG   A O   1 
ATOM   6247 C  CB  . ARG   D 1 192 ? -23.622 -6.318  66.326  1.00 25.72 ?  187 ARG   A CB  1 
ATOM   6248 C  CG  . ARG   D 1 192 ? -23.550 -7.395  67.381  1.00 30.84 ?  187 ARG   A CG  1 
ATOM   6249 C  CD  . ARG   D 1 192 ? -23.204 -6.759  68.723  1.00 34.75 ?  187 ARG   A CD  1 
ATOM   6250 N  NE  . ARG   D 1 192 ? -22.209 -7.641  69.280  1.00 49.45 ?  187 ARG   A NE  1 
ATOM   6251 C  CZ  . ARG   D 1 192 ? -20.970 -7.291  69.629  1.00 55.82 ?  187 ARG   A CZ  1 
ATOM   6252 N  NH1 . ARG   D 1 192 ? -20.568 -6.026  69.580  1.00 57.52 1  187 ARG   A NH1 1 
ATOM   6253 N  NH2 . ARG   D 1 192 ? -20.154 -8.229  70.077  1.00 55.28 ?  187 ARG   A NH2 1 
ATOM   6254 N  N   . ARG   D 1 193 ? -23.298 -5.127  63.539  1.00 23.68 ?  188 ARG   A N   1 
ATOM   6255 C  CA  . ARG   D 1 193 ? -23.258 -3.972  62.614  1.00 24.17 ?  188 ARG   A CA  1 
ATOM   6256 C  C   . ARG   D 1 193 ? -24.231 -4.197  61.450  1.00 20.62 ?  188 ARG   A C   1 
ATOM   6257 O  O   . ARG   D 1 193 ? -24.925 -3.233  61.090  1.00 21.61 ?  188 ARG   A O   1 
ATOM   6258 C  CB  . ARG   D 1 193 ? -21.810 -3.777  62.143  1.00 27.46 ?  188 ARG   A CB  1 
ATOM   6259 C  CG  . ARG   D 1 193 ? -21.531 -2.425  61.505  1.00 35.22 ?  188 ARG   A CG  1 
ATOM   6260 C  CD  . ARG   D 1 193 ? -20.061 -2.303  61.090  1.00 40.46 ?  188 ARG   A CD  1 
ATOM   6261 N  NE  . ARG   D 1 193 ? -19.812 -1.051  60.373  1.00 45.69 ?  188 ARG   A NE  1 
ATOM   6262 C  CZ  . ARG   D 1 193 ? -19.756 -0.892  59.048  1.00 53.08 ?  188 ARG   A CZ  1 
ATOM   6263 N  NH1 . ARG   D 1 193 ? -19.933 -1.903  58.204  1.00 51.54 1  188 ARG   A NH1 1 
ATOM   6264 N  NH2 . ARG   D 1 193 ? -19.520 0.316   58.569  1.00 55.17 ?  188 ARG   A NH2 1 
ATOM   6265 N  N   . ARG   D 1 194 ? -24.270 -5.402  60.870  1.00 20.06 ?  189 ARG   A N   1 
ATOM   6266 C  CA  . ARG   D 1 194 ? -25.134 -5.672  59.695  1.00 19.29 ?  189 ARG   A CA  1 
ATOM   6267 C  C   . ARG   D 1 194 ? -26.600 -5.545  60.128  1.00 18.85 ?  189 ARG   A C   1 
ATOM   6268 O  O   . ARG   D 1 194 ? -27.412 -4.999  59.383  1.00 20.34 ?  189 ARG   A O   1 
ATOM   6269 C  CB  . ARG   D 1 194 ? -24.901 -7.070  59.133  1.00 20.18 ?  189 ARG   A CB  1 
ATOM   6270 C  CG  . ARG   D 1 194 ? -23.588 -7.188  58.389  1.00 21.80 ?  189 ARG   A CG  1 
ATOM   6271 C  CD  . ARG   D 1 194 ? -23.280 -8.622  58.082  1.00 22.96 ?  189 ARG   A CD  1 
ATOM   6272 N  NE  . ARG   D 1 194 ? -21.908 -8.633  57.568  1.00 25.03 ?  189 ARG   A NE  1 
ATOM   6273 C  CZ  . ARG   D 1 194 ? -21.223 -9.711  57.241  1.00 30.01 ?  189 ARG   A CZ  1 
ATOM   6274 N  NH1 . ARG   D 1 194 ? -21.725 -10.923 57.417  1.00 28.46 1  189 ARG   A NH1 1 
ATOM   6275 N  NH2 . ARG   D 1 194 ? -19.992 -9.554  56.762  1.00 31.16 ?  189 ARG   A NH2 1 
ATOM   6276 N  N   . VAL   D 1 195 ? -26.923 -5.978  61.337  1.00 17.80 ?  190 VAL   A N   1 
ATOM   6277 C  CA  . VAL   D 1 195 ? -28.324 -5.854  61.838  1.00 16.99 ?  190 VAL   A CA  1 
ATOM   6278 C  C   . VAL   D 1 195 ? -28.660 -4.370  62.068  1.00 17.63 ?  190 VAL   A C   1 
ATOM   6279 O  O   . VAL   D 1 195 ? -29.739 -3.885  61.652  1.00 18.10 ?  190 VAL   A O   1 
ATOM   6280 C  CB  . VAL   D 1 195 ? -28.522 -6.682  63.121  1.00 17.34 ?  190 VAL   A CB  1 
ATOM   6281 C  CG1 . VAL   D 1 195 ? -29.889 -6.480  63.732  1.00 17.96 ?  190 VAL   A CG1 1 
ATOM   6282 C  CG2 . VAL   D 1 195 ? -28.300 -8.153  62.856  1.00 19.17 ?  190 VAL   A CG2 1 
ATOM   6283 N  N   . ARG   D 1 196 ? -27.759 -3.617  62.678  1.00 18.89 ?  191 ARG   A N   1 
ATOM   6284 C  CA  . ARG   D 1 196 ? -27.992 -2.193  62.975  1.00 18.63 ?  191 ARG   A CA  1 
ATOM   6285 C  C   . ARG   D 1 196 ? -28.157 -1.424  61.654  1.00 19.68 ?  191 ARG   A C   1 
ATOM   6286 O  O   . ARG   D 1 196 ? -29.126 -0.654  61.557  1.00 19.05 ?  191 ARG   A O   1 
ATOM   6287 C  CB  . ARG   D 1 196 ? -26.842 -1.618  63.810  1.00 20.31 ?  191 ARG   A CB  1 
ATOM   6288 C  CG  . ARG   D 1 196 ? -26.988 -0.144  64.116  1.00 21.56 ?  191 ARG   A CG  1 
ATOM   6289 C  CD  . ARG   D 1 196 ? -25.946 0.292   65.122  1.00 25.80 ?  191 ARG   A CD  1 
ATOM   6290 N  NE  . ARG   D 1 196 ? -24.587 0.120   64.600  1.00 30.43 ?  191 ARG   A NE  1 
ATOM   6291 C  CZ  . ARG   D 1 196 ? -23.945 0.995   63.808  1.00 33.75 ?  191 ARG   A CZ  1 
ATOM   6292 N  NH1 . ARG   D 1 196 ? -24.538 2.107   63.410  1.00 37.28 1  191 ARG   A NH1 1 
ATOM   6293 N  NH2 . ARG   D 1 196 ? -22.710 0.743   63.416  1.00 35.87 ?  191 ARG   A NH2 1 
ATOM   6294 N  N   . HIS   D 1 197 ? -27.274 -1.593  60.664  1.00 21.54 ?  192 HIS   A N   1 
ATOM   6295 C  CA  . HIS   D 1 197 ? -27.446 -0.972  59.315  1.00 22.22 ?  192 HIS   A CA  1 
ATOM   6296 C  C   . HIS   D 1 197 ? -28.785 -1.370  58.662  1.00 21.05 ?  192 HIS   A C   1 
ATOM   6297 O  O   . HIS   D 1 197 ? -29.469 -0.476  58.155  1.00 19.93 ?  192 HIS   A O   1 
ATOM   6298 C  CB  . HIS   D 1 197 ? -26.231 -1.186  58.405  1.00 23.98 ?  192 HIS   A CB  1 
ATOM   6299 C  CG  . HIS   D 1 197 ? -25.065 -0.395  58.866  1.00 24.32 ?  192 HIS   A CG  1 
ATOM   6300 N  ND1 . HIS   D 1 197 ? -25.214 0.849   59.431  1.00 29.46 ?  192 HIS   A ND1 1 
ATOM   6301 C  CD2 . HIS   D 1 197 ? -23.742 -0.657  58.874  1.00 28.29 ?  192 HIS   A CD2 1 
ATOM   6302 C  CE1 . HIS   D 1 197 ? -24.036 1.309   59.811  1.00 29.56 ?  192 HIS   A CE1 1 
ATOM   6303 N  NE2 . HIS   D 1 197 ? -23.132 0.432   59.453  1.00 27.02 ?  192 HIS   A NE2 1 
ATOM   6304 N  N   . SER   D 1 198 ? -29.177 -2.631  58.644  1.00 18.43 ?  193 SER   A N   1 
ATOM   6305 C  CA  . SER   D 1 198 ? -30.494 -3.084  58.124  1.00 20.75 ?  193 SER   A CA  1 
ATOM   6306 C  C   . SER   D 1 198 ? -31.640 -2.321  58.796  1.00 20.79 ?  193 SER   A C   1 
ATOM   6307 O  O   . SER   D 1 198 ? -32.490 -1.745  58.112  1.00 22.13 ?  193 SER   A O   1 
ATOM   6308 C  CB  . SER   D 1 198 ? -30.669 -4.569  58.316  1.00 19.24 ?  193 SER   A CB  1 
ATOM   6309 O  OG  . SER   D 1 198 ? -31.863 -4.999  57.685  1.00 22.77 ?  193 SER   A OG  1 
ATOM   6310 N  N   . PHE   D 1 199 ? -31.681 -2.290  60.099  1.00 17.82 ?  194 PHE   A N   1 
ATOM   6311 C  CA  . PHE   D 1 199 ? -32.793 -1.660  60.852  1.00 18.77 ?  194 PHE   A CA  1 
ATOM   6312 C  C   . PHE   D 1 199 ? -32.782 -0.148  60.657  1.00 18.83 ?  194 PHE   A C   1 
ATOM   6313 O  O   . PHE   D 1 199 ? -33.860 0.439   60.725  1.00 15.22 ?  194 PHE   A O   1 
ATOM   6314 C  CB  . PHE   D 1 199 ? -32.773 -2.046  62.328  1.00 17.71 ?  194 PHE   A CB  1 
ATOM   6315 C  CG  . PHE   D 1 199 ? -33.154 -3.480  62.600  1.00 18.34 ?  194 PHE   A CG  1 
ATOM   6316 C  CD1 . PHE   D 1 199 ? -33.872 -4.212  61.665  1.00 19.55 ?  194 PHE   A CD1 1 
ATOM   6317 C  CD2 . PHE   D 1 199 ? -32.904 -4.064  63.819  1.00 18.56 ?  194 PHE   A CD2 1 
ATOM   6318 C  CE1 . PHE   D 1 199 ? -34.339 -5.495  61.936  1.00 21.85 ?  194 PHE   A CE1 1 
ATOM   6319 C  CE2 . PHE   D 1 199 ? -33.278 -5.392  64.041  1.00 18.54 ?  194 PHE   A CE2 1 
ATOM   6320 C  CZ  . PHE   D 1 199 ? -34.005 -6.097  63.121  1.00 19.28 ?  194 PHE   A CZ  1 
ATOM   6321 N  N   . GLY   D 1 200 ? -31.634 0.447   60.298  1.00 18.71 ?  195 GLY   A N   1 
ATOM   6322 C  CA  . GLY   D 1 200 ? -31.607 1.899   60.046  1.00 19.57 ?  195 GLY   A CA  1 
ATOM   6323 C  C   . GLY   D 1 200 ? -32.168 2.270   58.684  1.00 21.25 ?  195 GLY   A C   1 
ATOM   6324 O  O   . GLY   D 1 200 ? -32.335 3.488   58.435  1.00 20.89 ?  195 GLY   A O   1 
ATOM   6325 N  N   . GLY   D 1 201 ? -32.533 1.281   57.870  1.00 19.00 ?  196 GLY   A N   1 
ATOM   6326 C  CA  . GLY   D 1 201 ? -32.977 1.487   56.481  1.00 19.00 ?  196 GLY   A CA  1 
ATOM   6327 C  C   . GLY   D 1 201 ? -34.485 1.569   56.355  1.00 21.37 ?  196 GLY   A C   1 
ATOM   6328 O  O   . GLY   D 1 201 ? -34.952 1.699   55.206  1.00 23.13 ?  196 GLY   A O   1 
ATOM   6329 N  N   . ALA   D 1 202 ? -35.234 1.452   57.453  1.00 17.92 ?  197 ALA   A N   1 
ATOM   6330 C  CA  . ALA   D 1 202 ? -36.711 1.651   57.408  1.00 20.28 ?  197 ALA   A CA  1 
ATOM   6331 C  C   . ALA   D 1 202 ? -37.184 2.311   58.686  1.00 22.20 ?  197 ALA   A C   1 
ATOM   6332 O  O   . ALA   D 1 202 ? -36.702 1.949   59.799  1.00 20.49 ?  197 ALA   A O   1 
ATOM   6333 C  CB  . ALA   D 1 202 ? -37.425 0.345   57.199  1.00 20.82 ?  197 ALA   A CB  1 
ATOM   6334 N  N   . GLU   D 1 203 ? -38.177 3.189   58.563  1.00 19.87 ?  198 GLU   A N   1 
ATOM   6335 C  CA  . GLU   D 1 203 ? -38.692 3.937   59.724  1.00 21.77 ?  198 GLU   A CA  1 
ATOM   6336 C  C   . GLU   D 1 203 ? -39.174 2.952   60.809  1.00 21.69 ?  198 GLU   A C   1 
ATOM   6337 O  O   . GLU   D 1 203 ? -38.985 3.238   61.967  1.00 22.27 ?  198 GLU   A O   1 
ATOM   6338 C  CB  . GLU   D 1 203 ? -39.855 4.830   59.329  1.00 23.81 ?  198 GLU   A CB  1 
ATOM   6339 C  CG  . GLU   D 1 203 ? -40.274 5.749   60.456  1.00 27.55 ?  198 GLU   A CG  1 
ATOM   6340 C  CD  . GLU   D 1 203 ? -39.194 6.645   61.045  1.00 35.27 ?  198 GLU   A CD  1 
ATOM   6341 O  OE1 . GLU   D 1 203 ? -38.043 6.638   60.540  1.00 32.34 ?  198 GLU   A OE1 1 
ATOM   6342 O  OE2 . GLU   D 1 203 ? -39.500 7.320   62.040  1.00 37.59 -1 198 GLU   A OE2 1 
ATOM   6343 N  N   . ALA   D 1 204 ? -39.797 1.850   60.427  1.00 21.00 ?  199 ALA   A N   1 
ATOM   6344 C  CA  . ALA   D 1 204 ? -40.427 0.884   61.355  1.00 23.65 ?  199 ALA   A CA  1 
ATOM   6345 C  C   . ALA   D 1 204 ? -39.386 0.312   62.328  1.00 23.13 ?  199 ALA   A C   1 
ATOM   6346 O  O   . ALA   D 1 204 ? -39.767 -0.120  63.427  1.00 23.56 ?  199 ALA   A O   1 
ATOM   6347 C  CB  . ALA   D 1 204 ? -41.073 -0.229  60.586  1.00 25.45 ?  199 ALA   A CB  1 
ATOM   6348 N  N   . THR   D 1 205 ? -38.134 0.246   61.911  1.00 19.36 ?  200 THR   A N   1 
ATOM   6349 C  CA  . THR   D 1 205 ? -37.064 -0.427  62.699  1.00 21.23 ?  200 THR   A CA  1 
ATOM   6350 C  C   . THR   D 1 205 ? -36.017 0.570   63.193  1.00 18.42 ?  200 THR   A C   1 
ATOM   6351 O  O   . THR   D 1 205 ? -35.093 0.127   63.879  1.00 19.79 ?  200 THR   A O   1 
ATOM   6352 C  CB  . THR   D 1 205 ? -36.478 -1.587  61.881  1.00 19.86 ?  200 THR   A CB  1 
ATOM   6353 O  OG1 . THR   D 1 205 ? -36.080 -1.057  60.619  1.00 19.21 ?  200 THR   A OG1 1 
ATOM   6354 C  CG2 . THR   D 1 205 ? -37.440 -2.726  61.621  1.00 19.01 ?  200 THR   A CG2 1 
ATOM   6355 N  N   . ARG   D 1 206 ? -36.152 1.848   62.867  1.00 19.17 ?  201 ARG   A N   1 
ATOM   6356 C  CA  . ARG   D 1 206 ? -35.123 2.854   63.182  1.00 21.95 ?  201 ARG   A CA  1 
ATOM   6357 C  C   . ARG   D 1 206 ? -34.925 3.007   64.703  1.00 19.04 ?  201 ARG   A C   1 
ATOM   6358 O  O   . ARG   D 1 206 ? -33.771 3.125   65.126  1.00 21.08 ?  201 ARG   A O   1 
ATOM   6359 C  CB  . ARG   D 1 206 ? -35.463 4.195   62.521  1.00 23.67 ?  201 ARG   A CB  1 
ATOM   6360 C  CG  . ARG   D 1 206 ? -34.371 5.219   62.791  1.00 24.18 ?  201 ARG   A CG  1 
ATOM   6361 C  CD  . ARG   D 1 206 ? -34.377 6.404   61.849  1.00 27.00 ?  201 ARG   A CD  1 
ATOM   6362 N  NE  . ARG   D 1 206 ? -35.607 7.156   62.000  1.00 29.23 ?  201 ARG   A NE  1 
ATOM   6363 C  CZ  . ARG   D 1 206 ? -35.798 8.118   62.902  1.00 38.11 ?  201 ARG   A CZ  1 
ATOM   6364 N  NH1 . ARG   D 1 206 ? -34.863 8.393   63.804  1.00 41.01 1  201 ARG   A NH1 1 
ATOM   6365 N  NH2 . ARG   D 1 206 ? -36.946 8.773   62.919  1.00 41.30 ?  201 ARG   A NH2 1 
ATOM   6366 N  N   . ALA   D 1 207 ? -35.974 2.892   65.522  1.00 18.66 ?  202 ALA   A N   1 
ATOM   6367 C  CA  . ALA   D 1 207 ? -35.837 3.022   66.996  1.00 21.72 ?  202 ALA   A CA  1 
ATOM   6368 C  C   . ALA   D 1 207 ? -34.972 1.886   67.528  1.00 19.25 ?  202 ALA   A C   1 
ATOM   6369 O  O   . ALA   D 1 207 ? -34.225 2.096   68.472  1.00 22.65 ?  202 ALA   A O   1 
ATOM   6370 C  CB  . ALA   D 1 207 ? -37.188 3.044   67.630  1.00 20.78 ?  202 ALA   A CB  1 
ATOM   6371 N  N   . VAL   D 1 208 ? -35.082 0.679   66.964  1.00 20.05 ?  203 VAL   A N   1 
ATOM   6372 C  CA  . VAL   D 1 208 ? -34.254 -0.466  67.398  1.00 20.58 ?  203 VAL   A CA  1 
ATOM   6373 C  C   . VAL   D 1 208 ? -32.820 -0.138  67.003  1.00 17.27 ?  203 VAL   A C   1 
ATOM   6374 O  O   . VAL   D 1 208 ? -31.941 -0.352  67.798  1.00 18.60 ?  203 VAL   A O   1 
ATOM   6375 C  CB  . VAL   D 1 208 ? -34.736 -1.806  66.810  1.00 19.98 ?  203 VAL   A CB  1 
ATOM   6376 C  CG1 . VAL   D 1 208 ? -33.764 -2.911  67.159  1.00 21.58 ?  203 VAL   A CG1 1 
ATOM   6377 C  CG2 . VAL   D 1 208 ? -36.126 -2.134  67.344  1.00 21.89 ?  203 VAL   A CG2 1 
ATOM   6378 N  N   . ALA   D 1 209 ? -32.603 0.360   65.792  1.00 18.22 ?  204 ALA   A N   1 
ATOM   6379 C  CA  . ALA   D 1 209 ? -31.237 0.708   65.317  1.00 18.27 ?  204 ALA   A CA  1 
ATOM   6380 C  C   . ALA   D 1 209 ? -30.626 1.762   66.260  1.00 19.23 ?  204 ALA   A C   1 
ATOM   6381 O  O   . ALA   D 1 209 ? -29.422 1.625   66.580  1.00 21.86 ?  204 ALA   A O   1 
ATOM   6382 C  CB  . ALA   D 1 209 ? -31.296 1.156   63.861  1.00 19.92 ?  204 ALA   A CB  1 
ATOM   6383 N  N   . GLY   D 1 210 ? -31.419 2.747   66.688  1.00 21.33 ?  205 GLY   A N   1 
ATOM   6384 C  CA  . GLY   D 1 210 ? -31.059 3.831   67.644  1.00 22.78 ?  205 GLY   A CA  1 
ATOM   6385 C  C   . GLY   D 1 210 ? -30.499 3.258   68.934  1.00 23.61 ?  205 GLY   A C   1 
ATOM   6386 O  O   . GLY   D 1 210 ? -29.379 3.698   69.439  1.00 23.57 ?  205 GLY   A O   1 
ATOM   6387 N  N   . LEU   D 1 211 ? -31.212 2.272   69.496  1.00 22.58 ?  206 LEU   A N   1 
ATOM   6388 C  CA  . LEU   D 1 211 ? -30.745 1.623   70.746  1.00 20.98 ?  206 LEU   A CA  1 
ATOM   6389 C  C   . LEU   D 1 211 ? -29.468 0.849   70.481  1.00 23.15 ?  206 LEU   A C   1 
ATOM   6390 O  O   . LEU   D 1 211 ? -28.541 0.939   71.314  1.00 22.60 ?  206 LEU   A O   1 
ATOM   6391 C  CB  . LEU   D 1 211 ? -31.860 0.753   71.334  1.00 24.40 ?  206 LEU   A CB  1 
ATOM   6392 C  CG  . LEU   D 1 211 ? -33.069 1.519   71.868  1.00 22.53 ?  206 LEU   A CG  1 
ATOM   6393 C  CD1 . LEU   D 1 211 ? -34.196 0.548   72.142  1.00 23.82 ?  206 LEU   A CD1 1 
ATOM   6394 C  CD2 . LEU   D 1 211 ? -32.761 2.281   73.150  1.00 25.99 ?  206 LEU   A CD2 1 
ATOM   6395 N  N   . MET   D 1 212 ? -29.381 0.144   69.358  1.00 19.93 ?  207 MET   A N   1 
ATOM   6396 C  CA  . MET   D 1 212 ? -28.181 -0.656  69.049  1.00 19.49 ?  207 MET   A CA  1 
ATOM   6397 C  C   . MET   D 1 212 ? -26.995 0.295   68.914  1.00 21.78 ?  207 MET   A C   1 
ATOM   6398 O  O   . MET   D 1 212 ? -25.856 -0.084  69.305  1.00 22.34 ?  207 MET   A O   1 
ATOM   6399 C  CB  . MET   D 1 212 ? -28.371 -1.459  67.764  1.00 20.92 ?  207 MET   A CB  1 
ATOM   6400 C  CG  . MET   D 1 212 ? -29.379 -2.601  67.928  1.00 19.98 ?  207 MET   A CG  1 
ATOM   6401 S  SD  . MET   D 1 212 ? -29.721 -3.510  66.420  1.00 21.89 ?  207 MET   A SD  1 
ATOM   6402 C  CE  . MET   D 1 212 ? -28.197 -4.457  66.353  1.00 24.96 ?  207 MET   A CE  1 
ATOM   6403 N  N   . ASP   D 1 213 ? -27.223 1.482   68.358  1.00 23.98 ?  208 ASP   A N   1 
ATOM   6404 C  CA  . ASP   D 1 213 ? -26.138 2.469   68.132  1.00 28.00 ?  208 ASP   A CA  1 
ATOM   6405 C  C   . ASP   D 1 213 ? -25.638 3.010   69.477  1.00 25.73 ?  208 ASP   A C   1 
ATOM   6406 O  O   . ASP   D 1 213 ? -24.497 3.483   69.485  1.00 30.53 ?  208 ASP   A O   1 
ATOM   6407 C  CB  . ASP   D 1 213 ? -26.585 3.576   67.168  1.00 30.41 ?  208 ASP   A CB  1 
ATOM   6408 C  CG  . ASP   D 1 213 ? -25.413 4.312   66.528  1.00 41.72 ?  208 ASP   A CG  1 
ATOM   6409 O  OD1 . ASP   D 1 213 ? -24.425 3.636   66.152  1.00 40.30 ?  208 ASP   A OD1 1 
ATOM   6410 O  OD2 . ASP   D 1 213 ? -25.499 5.547   66.394  1.00 49.53 -1 208 ASP   A OD2 1 
ATOM   6411 N  N   . ARG   D 1 214 ? -26.457 3.002   70.536  1.00 23.40 ?  209 ARG   A N   1 
ATOM   6412 C  CA  . ARG   D 1 214 ? -26.169 3.619   71.843  1.00 25.21 ?  209 ARG   A CA  1 
ATOM   6413 C  C   . ARG   D 1 214 ? -25.498 2.589   72.756  1.00 28.77 ?  209 ARG   A C   1 
ATOM   6414 O  O   . ARG   D 1 214 ? -25.114 2.986   73.870  1.00 34.04 ?  209 ARG   A O   1 
ATOM   6415 C  CB  . ARG   D 1 214 ? -27.445 4.211   72.452  1.00 29.34 ?  209 ARG   A CB  1 
ATOM   6416 C  CG  . ARG   D 1 214 ? -27.826 5.547   71.835  1.00 31.41 ?  209 ARG   A CG  1 
ATOM   6417 C  CD  . ARG   D 1 214 ? -29.058 6.233   72.373  1.00 36.09 ?  209 ARG   A CD  1 
ATOM   6418 N  NE  . ARG   D 1 214 ? -30.271 5.568   71.915  1.00 49.39 ?  209 ARG   A NE  1 
ATOM   6419 C  CZ  . ARG   D 1 214 ? -31.471 6.133   71.798  1.00 55.05 ?  209 ARG   A CZ  1 
ATOM   6420 N  NH1 . ARG   D 1 214 ? -32.503 5.410   71.386  1.00 44.59 1  209 ARG   A NH1 1 
ATOM   6421 N  NH2 . ARG   D 1 214 ? -31.634 7.418   72.090  1.00 60.97 ?  209 ARG   A NH2 1 
ATOM   6422 N  N   . LEU   D 1 215 ? -25.385 1.325   72.333  1.00 26.71 ?  210 LEU   A N   1 
ATOM   6423 C  CA  . LEU   D 1 215 ? -24.739 0.266   73.146  1.00 31.19 ?  210 LEU   A CA  1 
ATOM   6424 C  C   . LEU   D 1 215 ? -23.235 0.486   73.135  1.00 35.89 ?  210 LEU   A C   1 
ATOM   6425 O  O   . LEU   D 1 215 ? -22.692 0.855   72.106  1.00 35.13 ?  210 LEU   A O   1 
ATOM   6426 C  CB  . LEU   D 1 215 ? -25.016 -1.120  72.577  1.00 29.77 ?  210 LEU   A CB  1 
ATOM   6427 C  CG  . LEU   D 1 215 ? -26.437 -1.629  72.740  1.00 27.22 ?  210 LEU   A CG  1 
ATOM   6428 C  CD1 . LEU   D 1 215 ? -26.567 -2.925  71.991  1.00 28.54 ?  210 LEU   A CD1 1 
ATOM   6429 C  CD2 . LEU   D 1 215 ? -26.822 -1.804  74.198  1.00 31.15 ?  210 LEU   A CD2 1 
ATOM   6430 N  N   . PRO   D 1 216 ? -22.528 0.200   74.252  1.00 41.27 ?  211 PRO   A N   1 
ATOM   6431 C  CA  . PRO   D 1 216 ? -21.069 0.354   74.289  1.00 48.32 ?  211 PRO   A CA  1 
ATOM   6432 C  C   . PRO   D 1 216 ? -20.356 -0.606  73.318  1.00 52.28 ?  211 PRO   A C   1 
ATOM   6433 O  O   . PRO   D 1 216 ? -20.917 -1.642  73.023  1.00 52.22 ?  211 PRO   A O   1 
ATOM   6434 C  CB  . PRO   D 1 216 ? -20.718 0.086   75.766  1.00 45.33 ?  211 PRO   A CB  1 
ATOM   6435 C  CG  . PRO   D 1 216 ? -21.864 -0.750  76.299  1.00 46.44 ?  211 PRO   A CG  1 
ATOM   6436 C  CD  . PRO   D 1 216 ? -23.083 -0.324  75.507  1.00 43.99 ?  211 PRO   A CD  1 
ATOM   6437 N  N   . THR   D 1 217 ? -19.146 -0.230  72.869  1.00 64.26 ?  212 THR   A N   1 
ATOM   6438 C  CA  . THR   D 1 217 ? -18.317 -0.885  71.808  1.00 71.62 ?  212 THR   A CA  1 
ATOM   6439 C  C   . THR   D 1 217 ? -19.021 -0.732  70.456  1.00 73.35 ?  212 THR   A C   1 
ATOM   6440 O  O   . THR   D 1 217 ? -18.788 0.272   69.798  1.00 73.57 ?  212 THR   A O   1 
ATOM   6441 C  CB  . THR   D 1 217 ? -18.012 -2.365  72.094  1.00 74.94 ?  212 THR   A CB  1 
ATOM   6442 O  OG1 . THR   D 1 217 ? -17.490 -2.490  73.416  1.00 73.50 ?  212 THR   A OG1 1 
ATOM   6443 C  CG2 . THR   D 1 217 ? -17.018 -2.969  71.122  1.00 74.60 ?  212 THR   A CG2 1 
HETATM 6444 C  CHA . HEM   E 2 .   ? -60.088 -10.215 29.332  1.00 19.84 ?  301 HEM   B CHA 1 
HETATM 6445 C  CHB . HEM   E 2 .   ? -56.154 -11.536 31.829  1.00 18.01 ?  301 HEM   B CHB 1 
HETATM 6446 C  CHC . HEM   E 2 .   ? -56.668 -16.181 30.410  1.00 19.02 ?  301 HEM   B CHC 1 
HETATM 6447 C  CHD . HEM   E 2 .   ? -60.988 -15.009 28.471  1.00 19.21 ?  301 HEM   B CHD 1 
HETATM 6448 C  C1A . HEM   E 2 .   ? -58.909 -10.168 30.043  1.00 18.51 ?  301 HEM   B C1A 1 
HETATM 6449 C  C2A . HEM   E 2 .   ? -58.455 -9.012  30.772  1.00 20.14 ?  301 HEM   B C2A 1 
HETATM 6450 C  C3A . HEM   E 2 .   ? -57.333 -9.371  31.476  1.00 20.75 ?  301 HEM   B C3A 1 
HETATM 6451 C  C4A . HEM   E 2 .   ? -57.164 -10.795 31.261  1.00 20.39 ?  301 HEM   B C4A 1 
HETATM 6452 C  CMA . HEM   E 2 .   ? -56.519 -8.403  32.360  1.00 21.54 ?  301 HEM   B CMA 1 
HETATM 6453 C  CAA . HEM   E 2 .   ? -59.046 -7.611  30.655  1.00 20.12 ?  301 HEM   B CAA 1 
HETATM 6454 C  CBA . HEM   E 2 .   ? -58.430 -6.771  29.556  1.00 18.93 ?  301 HEM   B CBA 1 
HETATM 6455 C  CGA . HEM   E 2 .   ? -59.180 -5.467  29.388  1.00 17.92 ?  301 HEM   B CGA 1 
HETATM 6456 O  O1A . HEM   E 2 .   ? -59.405 -4.659  30.368  1.00 19.53 ?  301 HEM   B O1A 1 
HETATM 6457 O  O2A . HEM   E 2 .   ? -59.509 -5.157  28.231  1.00 18.02 ?  301 HEM   B O2A 1 
HETATM 6458 C  C1B . HEM   E 2 .   ? -55.974 -12.903 31.698  1.00 18.82 ?  301 HEM   B C1B 1 
HETATM 6459 C  C2B . HEM   E 2 .   ? -54.889 -13.617 32.270  1.00 18.77 ?  301 HEM   B C2B 1 
HETATM 6460 C  C3B . HEM   E 2 .   ? -55.010 -14.934 31.899  1.00 18.46 ?  301 HEM   B C3B 1 
HETATM 6461 C  C4B . HEM   E 2 .   ? -56.204 -15.028 31.048  1.00 16.40 ?  301 HEM   B C4B 1 
HETATM 6462 C  CMB . HEM   E 2 .   ? -53.832 -13.034 33.180  1.00 17.90 ?  301 HEM   B CMB 1 
HETATM 6463 C  CAB . HEM   E 2 .   ? -54.019 -15.952 32.287  1.00 20.20 ?  301 HEM   B CAB 1 
HETATM 6464 C  CBB . HEM   E 2 .   ? -53.748 -17.020 31.668  1.00 21.16 ?  301 HEM   B CBB 1 
HETATM 6465 C  C1C . HEM   E 2 .   ? -57.892 -16.256 29.784  1.00 18.46 ?  301 HEM   B C1C 1 
HETATM 6466 C  C2C . HEM   E 2 .   ? -58.449 -17.433 29.252  1.00 18.59 ?  301 HEM   B C2C 1 
HETATM 6467 C  C3C . HEM   E 2 .   ? -59.711 -17.126 28.709  1.00 20.26 ?  301 HEM   B C3C 1 
HETATM 6468 C  C4C . HEM   E 2 .   ? -59.842 -15.689 28.857  1.00 20.03 ?  301 HEM   B C4C 1 
HETATM 6469 C  CMC . HEM   E 2 .   ? -57.826 -18.799 29.318  1.00 19.58 ?  301 HEM   B CMC 1 
HETATM 6470 C  CAC . HEM   E 2 .   ? -60.568 -18.084 27.965  1.00 20.31 ?  301 HEM   B CAC 1 
HETATM 6471 C  CBC . HEM   E 2 .   ? -61.320 -17.752 26.905  1.00 20.08 ?  301 HEM   B CBC 1 
HETATM 6472 C  C1D . HEM   E 2 .   ? -61.067 -13.619 28.621  1.00 19.07 ?  301 HEM   B C1D 1 
HETATM 6473 C  C2D . HEM   E 2 .   ? -62.263 -12.910 28.236  1.00 17.61 ?  301 HEM   B C2D 1 
HETATM 6474 C  C3D . HEM   E 2 .   ? -62.020 -11.626 28.416  1.00 18.72 ?  301 HEM   B C3D 1 
HETATM 6475 C  C4D . HEM   E 2 .   ? -60.624 -11.474 28.943  1.00 17.90 ?  301 HEM   B C4D 1 
HETATM 6476 C  CMD . HEM   E 2 .   ? -63.548 -13.495 27.628  1.00 20.46 ?  301 HEM   B CMD 1 
HETATM 6477 C  CAD . HEM   E 2 .   ? -63.009 -10.483 28.125  1.00 21.48 ?  301 HEM   B CAD 1 
HETATM 6478 C  CBD . HEM   E 2 .   ? -63.526 -9.825  29.425  1.00 24.05 ?  301 HEM   B CBD 1 
HETATM 6479 C  CGD . HEM   E 2 .   ? -63.994 -10.790 30.473  1.00 29.43 ?  301 HEM   B CGD 1 
HETATM 6480 O  O1D . HEM   E 2 .   ? -64.910 -11.572 30.153  1.00 25.97 ?  301 HEM   B O1D 1 
HETATM 6481 O  O2D . HEM   E 2 .   ? -63.435 -10.851 31.598  1.00 29.79 ?  301 HEM   B O2D 1 
HETATM 6482 N  NA  . HEM   E 2 .   ? -58.144 -11.268 30.450  1.00 18.59 ?  301 HEM   B NA  1 
HETATM 6483 N  NB  . HEM   E 2 .   ? -56.628 -13.740 30.869  1.00 17.87 ?  301 HEM   B NB  1 
HETATM 6484 N  NC  . HEM   E 2 .   ? -58.706 -15.196 29.512  1.00 16.46 ?  301 HEM   B NC  1 
HETATM 6485 N  ND  . HEM   E 2 .   ? -60.111 -12.735 29.089  1.00 18.94 ?  301 HEM   B ND  1 
HETATM 6486 FE FE  . HEM   E 2 .   ? -58.326 -13.171 29.786  1.00 18.85 ?  301 HEM   B FE  1 
HETATM 6487 O  OXT . A1ECN F 3 .   ? -31.495 9.308   40.537  1.00 32.62 ?  302 A1ECN B OXT 1 
HETATM 6488 C  C   . A1ECN F 3 .   ? -32.362 10.188  40.519  1.00 35.94 ?  302 A1ECN B C   1 
HETATM 6489 O  O   . A1ECN F 3 .   ? -33.602 9.985   40.669  1.00 35.50 ?  302 A1ECN B O   1 
HETATM 6490 C  CA  . A1ECN F 3 .   ? -31.913 11.687  40.236  1.00 37.20 ?  302 A1ECN B CA  1 
HETATM 6491 C  CB  . A1ECN F 3 .   ? -30.936 12.226  41.178  1.00 36.15 ?  302 A1ECN B CB  1 
HETATM 6492 C  CAC . A1ECN F 3 .   ? -31.640 12.547  42.564  1.00 34.07 ?  302 A1ECN B CAC 1 
HETATM 6493 C  CAD . A1ECN F 3 .   ? -33.081 12.434  42.731  1.00 37.08 ?  302 A1ECN B CAD 1 
HETATM 6494 N  NAG . A1ECN F 3 .   ? -33.837 12.566  41.484  1.00 37.31 ?  302 A1ECN B NAG 1 
HETATM 6495 N  N   . A1ECN F 3 .   ? -33.107 12.538  40.287  1.00 33.50 ?  302 A1ECN B N   1 
HETATM 6496 C  CHA . HEM   G 2 .   ? -35.234 13.242  37.642  1.00 20.34 ?  301 HEM   C CHA 1 
HETATM 6497 C  CHB . HEM   G 2 .   ? -37.284 10.486  40.963  1.00 17.10 ?  301 HEM   C CHB 1 
HETATM 6498 C  CHC . HEM   G 2 .   ? -36.377 13.835  44.455  1.00 16.38 ?  301 HEM   C CHC 1 
HETATM 6499 C  CHD . HEM   G 2 .   ? -33.725 16.292  41.089  1.00 17.14 ?  301 HEM   C CHD 1 
HETATM 6500 C  C1A . HEM   G 2 .   ? -35.943 12.251  38.252  1.00 17.97 ?  301 HEM   C C1A 1 
HETATM 6501 C  C2A . HEM   G 2 .   ? -36.399 11.084  37.589  1.00 18.32 ?  301 HEM   C C2A 1 
HETATM 6502 C  C3A . HEM   G 2 .   ? -36.922 10.299  38.519  1.00 19.94 ?  301 HEM   C C3A 1 
HETATM 6503 C  C4A . HEM   G 2 .   ? -36.813 10.999  39.755  1.00 18.25 ?  301 HEM   C C4A 1 
HETATM 6504 C  CMA . HEM   G 2 .   ? -37.628 8.924   38.366  1.00 21.42 ?  301 HEM   C CMA 1 
HETATM 6505 C  CAA . HEM   G 2 .   ? -36.324 10.729  36.121  1.00 20.32 ?  301 HEM   C CAA 1 
HETATM 6506 C  CBA . HEM   G 2 .   ? -37.571 11.146  35.317  1.00 18.52 ?  301 HEM   C CBA 1 
HETATM 6507 C  CGA . HEM   G 2 .   ? -37.319 10.950  33.858  1.00 17.65 ?  301 HEM   C CGA 1 
HETATM 6508 O  O1A . HEM   G 2 .   ? -36.995 9.828   33.399  1.00 19.25 ?  301 HEM   C O1A 1 
HETATM 6509 O  O2A . HEM   G 2 .   ? -37.398 11.970  33.112  1.00 16.67 ?  301 HEM   C O2A 1 
HETATM 6510 C  C1B . HEM   G 2 .   ? -37.217 11.143  42.209  1.00 16.25 ?  301 HEM   C C1B 1 
HETATM 6511 C  C2B . HEM   G 2 .   ? -37.716 10.584  43.429  1.00 17.71 ?  301 HEM   C C2B 1 
HETATM 6512 C  C3B . HEM   G 2 .   ? -37.547 11.520  44.395  1.00 16.51 ?  301 HEM   C C3B 1 
HETATM 6513 C  C4B . HEM   G 2 .   ? -36.840 12.683  43.762  1.00 17.21 ?  301 HEM   C C4B 1 
HETATM 6514 C  CMB . HEM   G 2 .   ? -38.413 9.238   43.554  1.00 20.37 ?  301 HEM   C CMB 1 
HETATM 6515 C  CAB . HEM   G 2 .   ? -37.921 11.331  45.780  1.00 16.94 ?  301 HEM   C CAB 1 
HETATM 6516 C  CBB . HEM   G 2 .   ? -38.091 12.213  46.672  1.00 18.89 ?  301 HEM   C CBB 1 
HETATM 6517 C  C1C . HEM   G 2 .   ? -35.548 14.801  43.796  1.00 17.26 ?  301 HEM   C C1C 1 
HETATM 6518 C  C2C . HEM   G 2 .   ? -34.927 15.858  44.445  1.00 17.25 ?  301 HEM   C C2C 1 
HETATM 6519 C  C3C . HEM   G 2 .   ? -34.183 16.603  43.542  1.00 16.54 ?  301 HEM   C C3C 1 
HETATM 6520 C  C4C . HEM   G 2 .   ? -34.327 15.898  42.267  1.00 18.30 ?  301 HEM   C C4C 1 
HETATM 6521 C  CMC . HEM   G 2 .   ? -35.120 16.118  45.929  1.00 17.03 ?  301 HEM   C CMC 1 
HETATM 6522 C  CAC . HEM   G 2 .   ? -33.493 17.863  43.925  1.00 17.87 ?  301 HEM   C CAC 1 
HETATM 6523 C  CBC . HEM   G 2 .   ? -33.311 18.904  43.097  1.00 18.64 ?  301 HEM   C CBC 1 
HETATM 6524 C  C1D . HEM   G 2 .   ? -33.898 15.651  39.890  1.00 17.33 ?  301 HEM   C C1D 1 
HETATM 6525 C  C2D . HEM   G 2 .   ? -33.183 16.047  38.691  1.00 18.08 ?  301 HEM   C C2D 1 
HETATM 6526 C  C3D . HEM   G 2 .   ? -33.584 15.200  37.734  1.00 19.27 ?  301 HEM   C C3D 1 
HETATM 6527 C  C4D . HEM   G 2 .   ? -34.595 14.310  38.366  1.00 17.81 ?  301 HEM   C C4D 1 
HETATM 6528 C  CMD . HEM   G 2 .   ? -32.160 17.128  38.612  1.00 19.24 ?  301 HEM   C CMD 1 
HETATM 6529 C  CAD . HEM   G 2 .   ? -33.175 15.212  36.304  1.00 21.34 ?  301 HEM   C CAD 1 
HETATM 6530 C  CBD . HEM   G 2 .   ? -31.748 14.743  36.164  1.00 31.48 ?  301 HEM   C CBD 1 
HETATM 6531 C  CGD . HEM   G 2 .   ? -31.627 13.389  36.717  1.00 41.42 ?  301 HEM   C CGD 1 
HETATM 6532 O  O1D . HEM   G 2 .   ? -30.525 13.041  37.204  1.00 49.43 ?  301 HEM   C O1D 1 
HETATM 6533 O  O2D . HEM   G 2 .   ? -32.622 12.642  36.696  1.00 52.87 ?  301 HEM   C O2D 1 
HETATM 6534 N  NA  . HEM   G 2 .   ? -36.199 12.205  39.623  1.00 17.46 ?  301 HEM   C NA  1 
HETATM 6535 N  NB  . HEM   G 2 .   ? -36.695 12.353  42.468  1.00 15.65 ?  301 HEM   C NB  1 
HETATM 6536 N  NC  . HEM   G 2 .   ? -35.223 14.833  42.481  1.00 18.81 ?  301 HEM   C NC  1 
HETATM 6537 N  ND  . HEM   G 2 .   ? -34.764 14.610  39.657  1.00 17.81 ?  301 HEM   C ND  1 
HETATM 6538 FE FE  . HEM   G 2 .   ? -35.864 13.595  40.986  1.00 17.46 ?  301 HEM   C FE  1 
HETATM 6539 C  CHA . HEM   H 2 .   ? -35.280 -19.206 73.181  1.00 20.83 ?  301 HEM   D CHA 1 
HETATM 6540 C  CHB . HEM   H 2 .   ? -37.386 -16.358 69.881  1.00 18.08 ?  301 HEM   D CHB 1 
HETATM 6541 C  CHC . HEM   H 2 .   ? -36.584 -19.671 66.418  1.00 18.59 ?  301 HEM   D CHC 1 
HETATM 6542 C  CHD . HEM   H 2 .   ? -33.970 -22.183 69.608  1.00 18.22 ?  301 HEM   D CHD 1 
HETATM 6543 C  C1A . HEM   H 2 .   ? -35.950 -18.144 72.588  1.00 20.70 ?  301 HEM   D C1A 1 
HETATM 6544 C  C2A . HEM   H 2 .   ? -36.418 -16.976 73.260  1.00 21.07 ?  301 HEM   D C2A 1 
HETATM 6545 C  C3A . HEM   H 2 .   ? -36.988 -16.173 72.320  1.00 21.93 ?  301 HEM   D C3A 1 
HETATM 6546 C  C4A . HEM   H 2 .   ? -36.923 -16.862 71.091  1.00 18.03 ?  301 HEM   D C4A 1 
HETATM 6547 C  CMA . HEM   H 2 .   ? -37.628 -14.793 72.553  1.00 24.26 ?  301 HEM   D CMA 1 
HETATM 6548 C  CAA . HEM   H 2 .   ? -36.266 -16.615 74.745  1.00 20.24 ?  301 HEM   D CAA 1 
HETATM 6549 C  CBA . HEM   H 2 .   ? -37.517 -17.026 75.579  1.00 19.58 ?  301 HEM   D CBA 1 
HETATM 6550 C  CGA . HEM   H 2 .   ? -37.275 -16.884 77.061  1.00 17.01 ?  301 HEM   D CGA 1 
HETATM 6551 O  O1A . HEM   H 2 .   ? -37.493 -17.846 77.827  1.00 17.32 ?  301 HEM   D O1A 1 
HETATM 6552 O  O2A . HEM   H 2 .   ? -36.952 -15.795 77.498  1.00 18.58 ?  301 HEM   D O2A 1 
HETATM 6553 C  C1B . HEM   H 2 .   ? -37.349 -17.040 68.668  1.00 18.84 ?  301 HEM   D C1B 1 
HETATM 6554 C  C2B . HEM   H 2 .   ? -37.866 -16.499 67.456  1.00 19.99 ?  301 HEM   D C2B 1 
HETATM 6555 C  C3B . HEM   H 2 .   ? -37.721 -17.405 66.449  1.00 18.94 ?  301 HEM   D C3B 1 
HETATM 6556 C  C4B . HEM   H 2 .   ? -36.971 -18.526 67.068  1.00 18.68 ?  301 HEM   D C4B 1 
HETATM 6557 C  CMB . HEM   H 2 .   ? -38.551 -15.137 67.278  1.00 18.56 ?  301 HEM   D CMB 1 
HETATM 6558 C  CAB . HEM   H 2 .   ? -38.219 -17.075 65.086  1.00 20.00 ?  301 HEM   D CAB 1 
HETATM 6559 C  CBB . HEM   H 2 .   ? -38.266 -17.928 64.072  1.00 21.11 ?  301 HEM   D CBB 1 
HETATM 6560 C  C1C . HEM   H 2 .   ? -35.771 -20.670 66.977  1.00 18.88 ?  301 HEM   D C1C 1 
HETATM 6561 C  C2C . HEM   H 2 .   ? -35.240 -21.758 66.317  1.00 19.61 ?  301 HEM   D C2C 1 
HETATM 6562 C  C3C . HEM   H 2 .   ? -34.467 -22.493 67.220  1.00 18.95 ?  301 HEM   D C3C 1 
HETATM 6563 C  C4C . HEM   H 2 .   ? -34.594 -21.814 68.451  1.00 19.85 ?  301 HEM   D C4C 1 
HETATM 6564 C  CMC . HEM   H 2 .   ? -35.453 -22.038 64.865  1.00 20.63 ?  301 HEM   D CMC 1 
HETATM 6565 C  CAC . HEM   H 2 .   ? -33.821 -23.773 66.862  1.00 19.50 ?  301 HEM   D CAC 1 
HETATM 6566 C  CBC . HEM   H 2 .   ? -33.654 -24.793 67.648  1.00 21.25 ?  301 HEM   D CBC 1 
HETATM 6567 C  C1D . HEM   H 2 .   ? -34.090 -21.558 70.820  1.00 18.89 ?  301 HEM   D C1D 1 
HETATM 6568 C  C2D . HEM   H 2 .   ? -33.325 -22.014 71.972  1.00 22.67 ?  301 HEM   D C2D 1 
HETATM 6569 C  C3D . HEM   H 2 .   ? -33.718 -21.174 72.995  1.00 23.32 ?  301 HEM   D C3D 1 
HETATM 6570 C  C4D . HEM   H 2 .   ? -34.719 -20.253 72.432  1.00 20.25 ?  301 HEM   D C4D 1 
HETATM 6571 C  CMD . HEM   H 2 .   ? -32.309 -23.164 72.046  1.00 21.04 ?  301 HEM   D CMD 1 
HETATM 6572 C  CAD . HEM   H 2 .   ? -33.296 -21.184 74.448  1.00 26.44 ?  301 HEM   D CAD 1 
HETATM 6573 C  CBD . HEM   H 2 .   ? -31.863 -20.761 74.683  1.00 34.56 ?  301 HEM   D CBD 1 
HETATM 6574 C  CGD . HEM   H 2 .   ? -31.563 -19.390 74.166  1.00 44.36 ?  301 HEM   D CGD 1 
HETATM 6575 O  O1D . HEM   H 2 .   ? -30.533 -19.203 73.431  1.00 42.74 ?  301 HEM   D O1D 1 
HETATM 6576 O  O2D . HEM   H 2 .   ? -32.327 -18.442 74.493  1.00 53.51 ?  301 HEM   D O2D 1 
HETATM 6577 N  NA  . HEM   H 2 .   ? -36.285 -18.093 71.244  1.00 18.72 ?  301 HEM   D NA  1 
HETATM 6578 N  NB  . HEM   H 2 .   ? -36.828 -18.236 68.387  1.00 19.11 ?  301 HEM   D NB  1 
HETATM 6579 N  NC  . HEM   H 2 .   ? -35.391 -20.716 68.274  1.00 18.94 ?  301 HEM   D NC  1 
HETATM 6580 N  ND  . HEM   H 2 .   ? -34.916 -20.522 71.118  1.00 20.98 ?  301 HEM   D ND  1 
HETATM 6581 FE FE  . HEM   H 2 .   ? -36.011 -19.492 69.843  1.00 18.92 ?  301 HEM   D FE  1 
HETATM 6582 O  OXT . A1ECN I 3 .   ? -61.249 6.260   76.553  1.00 36.54 ?  302 A1ECN D OXT 1 
HETATM 6583 C  C   . A1ECN I 3 .   ? -60.705 6.286   77.686  1.00 44.70 ?  302 A1ECN D C   1 
HETATM 6584 O  O   . A1ECN I 3 .   ? -59.506 5.916   77.928  1.00 40.45 ?  302 A1ECN D O   1 
HETATM 6585 C  CA  . A1ECN I 3 .   ? -61.539 6.843   78.875  1.00 43.05 ?  302 A1ECN D CA  1 
HETATM 6586 C  CB  . A1ECN I 3 .   ? -62.191 8.175   78.561  1.00 44.34 ?  302 A1ECN D CB  1 
HETATM 6587 C  CAC . A1ECN I 3 .   ? -61.492 9.184   79.419  1.00 47.34 ?  302 A1ECN D CAC 1 
HETATM 6588 C  CAD . A1ECN I 3 .   ? -59.993 9.085   79.225  1.00 44.22 ?  302 A1ECN D CAD 1 
HETATM 6589 N  NAG . A1ECN I 3 .   ? -59.518 7.798   79.862  1.00 46.10 ?  302 A1ECN D NAG 1 
HETATM 6590 N  N   . A1ECN I 3 .   ? -60.564 6.900   79.997  1.00 49.99 ?  302 A1ECN D N   1 
HETATM 6591 C  CHA . HEM   J 2 .   ? -59.983 4.322   82.113  1.00 23.03 ?  301 HEM   A CHA 1 
HETATM 6592 C  CHB . HEM   J 2 .   ? -56.075 5.611   79.559  1.00 19.40 ?  301 HEM   A CHB 1 
HETATM 6593 C  CHC . HEM   J 2 .   ? -56.554 10.138  81.214  1.00 19.46 ?  301 HEM   A CHC 1 
HETATM 6594 C  CHD . HEM   J 2 .   ? -60.706 8.920   83.402  1.00 21.76 ?  301 HEM   A CHD 1 
HETATM 6595 C  C1A . HEM   J 2 .   ? -58.842 4.303   81.371  1.00 20.24 ?  301 HEM   A C1A 1 
HETATM 6596 C  C2A . HEM   J 2 .   ? -58.424 3.125   80.654  1.00 21.50 ?  301 HEM   A C2A 1 
HETATM 6597 C  C3A . HEM   J 2 .   ? -57.299 3.487   79.915  1.00 20.65 ?  301 HEM   A C3A 1 
HETATM 6598 C  C4A . HEM   J 2 .   ? -57.110 4.902   80.128  1.00 19.35 ?  301 HEM   A C4A 1 
HETATM 6599 C  CMA . HEM   J 2 .   ? -56.482 2.533   79.004  1.00 23.02 ?  301 HEM   A CMA 1 
HETATM 6600 C  CAA . HEM   J 2 .   ? -59.071 1.713   80.730  1.00 20.45 ?  301 HEM   A CAA 1 
HETATM 6601 C  CBA . HEM   J 2 .   ? -58.440 0.941   81.858  1.00 19.33 ?  301 HEM   A CBA 1 
HETATM 6602 C  CGA . HEM   J 2 .   ? -59.130 -0.450  82.057  1.00 17.15 ?  301 HEM   A CGA 1 
HETATM 6603 O  O1A . HEM   J 2 .   ? -59.446 -0.826  83.228  1.00 18.24 ?  301 HEM   A O1A 1 
HETATM 6604 O  O2A . HEM   J 2 .   ? -59.286 -1.287  81.077  1.00 19.75 ?  301 HEM   A O2A 1 
HETATM 6605 C  C1B . HEM   J 2 .   ? -55.928 6.974   79.754  1.00 19.93 ?  301 HEM   A C1B 1 
HETATM 6606 C  C2B . HEM   J 2 .   ? -54.837 7.669   79.204  1.00 19.51 ?  301 HEM   A C2B 1 
HETATM 6607 C  C3B . HEM   J 2 .   ? -54.926 8.932   79.615  1.00 19.49 ?  301 HEM   A C3B 1 
HETATM 6608 C  C4B . HEM   J 2 .   ? -56.120 9.032   80.529  1.00 19.41 ?  301 HEM   A C4B 1 
HETATM 6609 C  CMB . HEM   J 2 .   ? -53.872 7.086   78.187  1.00 17.99 ?  301 HEM   A CMB 1 
HETATM 6610 C  CAB . HEM   J 2 .   ? -53.947 9.923   79.157  1.00 20.25 ?  301 HEM   A CAB 1 
HETATM 6611 C  CBB . HEM   J 2 .   ? -53.867 11.049  79.757  1.00 21.65 ?  301 HEM   A CBB 1 
HETATM 6612 C  C1C . HEM   J 2 .   ? -57.739 10.246  81.925  1.00 20.06 ?  301 HEM   A C1C 1 
HETATM 6613 C  C2C . HEM   J 2 .   ? -58.321 11.417  82.496  1.00 20.61 ?  301 HEM   A C2C 1 
HETATM 6614 C  C3C . HEM   J 2 .   ? -59.506 11.072  83.117  1.00 18.89 ?  301 HEM   A C3C 1 
HETATM 6615 C  C4C . HEM   J 2 .   ? -59.644 9.659   82.964  1.00 21.70 ?  301 HEM   A C4C 1 
HETATM 6616 C  CMC . HEM   J 2 .   ? -57.805 12.815  82.411  1.00 18.04 ?  301 HEM   A CMC 1 
HETATM 6617 C  CAC . HEM   J 2 .   ? -60.274 12.042  83.955  1.00 22.17 ?  301 HEM   A CAC 1 
HETATM 6618 C  CBC . HEM   J 2 .   ? -60.947 11.593  85.012  1.00 22.24 ?  301 HEM   A CBC 1 
HETATM 6619 C  C1D . HEM   J 2 .   ? -60.791 7.559   83.213  1.00 22.71 ?  301 HEM   A C1D 1 
HETATM 6620 C  C2D . HEM   J 2 .   ? -62.005 6.834   83.589  1.00 22.13 ?  301 HEM   A C2D 1 
HETATM 6621 C  C3D . HEM   J 2 .   ? -61.825 5.564   83.235  1.00 25.53 ?  301 HEM   A C3D 1 
HETATM 6622 C  C4D . HEM   J 2 .   ? -60.495 5.504   82.652  1.00 22.34 ?  301 HEM   A C4D 1 
HETATM 6623 C  CMD . HEM   J 2 .   ? -63.237 7.392   84.300  1.00 22.92 ?  301 HEM   A CMD 1 
HETATM 6624 C  CAD . HEM   J 2 .   ? -62.843 4.470   83.501  1.00 25.72 ?  301 HEM   A CAD 1 
HETATM 6625 C  CBD . HEM   J 2 .   ? -63.718 4.080   82.317  1.00 34.87 ?  301 HEM   A CBD 1 
HETATM 6626 C  CGD . HEM   J 2 .   ? -64.143 5.053   81.253  1.00 42.24 ?  301 HEM   A CGD 1 
HETATM 6627 O  O1D . HEM   J 2 .   ? -63.543 4.985   80.156  1.00 47.28 ?  301 HEM   A O1D 1 
HETATM 6628 O  O2D . HEM   J 2 .   ? -65.097 5.872   81.432  1.00 42.50 ?  301 HEM   A O2D 1 
HETATM 6629 N  NA  . HEM   J 2 .   ? -58.048 5.385   80.998  1.00 19.78 ?  301 HEM   A NA  1 
HETATM 6630 N  NB  . HEM   J 2 .   ? -56.599 7.774   80.611  1.00 21.10 ?  301 HEM   A NB  1 
HETATM 6631 N  NC  . HEM   J 2 .   ? -58.514 9.202   82.265  1.00 19.60 ?  301 HEM   A NC  1 
HETATM 6632 N  ND  . HEM   J 2 .   ? -59.979 6.785   82.539  1.00 18.72 ?  301 HEM   A ND  1 
HETATM 6633 FE FE  . HEM   J 2 .   ? -58.237 7.225   81.783  1.00 18.83 ?  301 HEM   A FE  1 
HETATM 6634 O  OXT . A1ECN K 3 .   ? -31.392 -15.281 70.384  1.00 34.97 ?  302 A1ECN A OXT 1 
HETATM 6635 C  C   . A1ECN K 3 .   ? -32.334 -16.136 70.402  1.00 39.32 ?  302 A1ECN A C   1 
HETATM 6636 O  O   . A1ECN K 3 .   ? -33.562 -15.892 70.234  1.00 37.44 ?  302 A1ECN A O   1 
HETATM 6637 C  CA  . A1ECN K 3 .   ? -31.988 -17.648 70.556  1.00 38.06 ?  302 A1ECN A CA  1 
HETATM 6638 C  CB  . A1ECN K 3 .   ? -30.972 -18.074 69.551  1.00 40.70 ?  302 A1ECN A CB  1 
HETATM 6639 C  CAC . A1ECN K 3 .   ? -31.683 -18.894 68.488  1.00 44.69 ?  302 A1ECN A CAC 1 
HETATM 6640 C  CAD . A1ECN K 3 .   ? -32.987 -18.293 68.090  1.00 38.93 ?  302 A1ECN A CAD 1 
HETATM 6641 N  NAG . A1ECN K 3 .   ? -33.935 -18.465 69.245  1.00 38.76 ?  302 A1ECN A NAG 1 
HETATM 6642 N  N   . A1ECN K 3 .   ? -33.278 -18.380 70.480  1.00 39.02 ?  302 A1ECN A N   1 
HETATM 6643 O  O   . HOH   L 4 .   ? -58.160 -1.263  29.392  1.00 30.64 ?  401 HOH   B O   1 
HETATM 6644 O  O   . HOH   L 4 .   ? -36.609 3.514   20.759  1.00 39.46 ?  402 HOH   B O   1 
HETATM 6645 O  O   . HOH   L 4 .   ? -45.277 1.154   15.132  1.00 44.06 ?  403 HOH   B O   1 
HETATM 6646 O  O   . HOH   L 4 .   ? -24.236 11.134  49.057  1.00 35.18 ?  404 HOH   B O   1 
HETATM 6647 O  O   . HOH   L 4 .   ? -59.782 -6.492  12.788  1.00 42.68 ?  405 HOH   B O   1 
HETATM 6648 O  O   . HOH   L 4 .   ? -44.283 -24.245 15.766  1.00 38.28 ?  406 HOH   B O   1 
HETATM 6649 O  O   . HOH   L 4 .   ? -52.982 -19.324 16.073  1.00 26.19 ?  407 HOH   B O   1 
HETATM 6650 O  O   . HOH   L 4 .   ? -15.645 5.176   45.193  1.00 46.96 ?  408 HOH   B O   1 
HETATM 6651 O  O   . HOH   L 4 .   ? -34.132 4.621   24.037  1.00 41.08 ?  409 HOH   B O   1 
HETATM 6652 O  O   . HOH   L 4 .   ? -28.691 5.686   58.198  1.00 39.97 ?  410 HOH   B O   1 
HETATM 6653 O  O   . HOH   L 4 .   ? -24.369 1.090   34.321  1.00 36.96 ?  411 HOH   B O   1 
HETATM 6654 O  O   . HOH   L 4 .   ? -47.486 -6.668  14.666  1.00 41.03 ?  412 HOH   B O   1 
HETATM 6655 O  O   . HOH   L 4 .   ? -33.861 1.122   21.526  1.00 45.16 ?  413 HOH   B O   1 
HETATM 6656 O  O   . HOH   L 4 .   ? -32.879 -2.438  23.853  1.00 32.91 ?  414 HOH   B O   1 
HETATM 6657 O  O   . HOH   L 4 .   ? -55.093 -33.912 32.015  1.00 24.06 ?  415 HOH   B O   1 
HETATM 6658 O  O   . HOH   L 4 .   ? -29.381 4.968   44.128  1.00 24.54 ?  416 HOH   B O   1 
HETATM 6659 O  O   . HOH   L 4 .   ? -57.330 -18.931 11.907  1.00 50.64 ?  417 HOH   B O   1 
HETATM 6660 O  O   . HOH   L 4 .   ? -68.774 -18.611 32.662  1.00 24.81 ?  418 HOH   B O   1 
HETATM 6661 O  O   . HOH   L 4 .   ? -34.621 -10.231 41.121  1.00 25.64 ?  419 HOH   B O   1 
HETATM 6662 O  O   . HOH   L 4 .   ? -42.181 -17.772 15.390  1.00 34.39 ?  420 HOH   B O   1 
HETATM 6663 O  O   . HOH   L 4 .   ? -32.703 -10.766 34.327  1.00 38.57 ?  421 HOH   B O   1 
HETATM 6664 O  O   . HOH   L 4 .   ? -45.767 -5.237  36.675  1.00 30.46 ?  422 HOH   B O   1 
HETATM 6665 O  O   . HOH   L 4 .   ? -57.951 9.144   27.144  1.00 28.35 ?  423 HOH   B O   1 
HETATM 6666 O  O   . HOH   L 4 .   ? -64.536 -17.731 33.876  1.00 25.87 ?  424 HOH   B O   1 
HETATM 6667 O  O   . HOH   L 4 .   ? -62.619 -6.337  15.925  1.00 38.55 ?  425 HOH   B O   1 
HETATM 6668 O  O   . HOH   L 4 .   ? -65.702 -20.667 20.648  1.00 30.66 ?  426 HOH   B O   1 
HETATM 6669 O  O   . HOH   L 4 .   ? -44.326 -3.676  14.455  1.00 29.83 ?  427 HOH   B O   1 
HETATM 6670 O  O   . HOH   L 4 .   ? -29.742 8.940   42.488  1.00 31.68 ?  428 HOH   B O   1 
HETATM 6671 O  O   . HOH   L 4 .   ? -22.397 7.893   45.444  1.00 31.55 ?  429 HOH   B O   1 
HETATM 6672 O  O   . HOH   L 4 .   ? -26.674 -1.433  34.162  1.00 36.27 ?  430 HOH   B O   1 
HETATM 6673 O  O   . HOH   L 4 .   ? -41.789 -11.851 14.645  1.00 44.42 ?  431 HOH   B O   1 
HETATM 6674 O  O   . HOH   L 4 .   ? -25.820 -0.891  41.605  1.00 36.51 ?  432 HOH   B O   1 
HETATM 6675 O  O   . HOH   L 4 .   ? -44.698 -14.749 31.446  1.00 21.06 ?  433 HOH   B O   1 
HETATM 6676 O  O   . HOH   L 4 .   ? -47.913 -16.077 41.496  1.00 27.91 ?  434 HOH   B O   1 
HETATM 6677 O  O   . HOH   L 4 .   ? -33.130 -8.278  17.032  1.00 41.61 ?  435 HOH   B O   1 
HETATM 6678 O  O   . HOH   L 4 .   ? -41.287 -19.027 23.116  1.00 30.25 ?  436 HOH   B O   1 
HETATM 6679 O  O   . HOH   L 4 .   ? -37.443 7.941   30.972  1.00 26.24 ?  437 HOH   B O   1 
HETATM 6680 O  O   . HOH   L 4 .   ? -35.256 -11.103 17.071  1.00 45.53 ?  438 HOH   B O   1 
HETATM 6681 O  O   . HOH   L 4 .   ? -27.469 9.707   54.705  1.00 29.84 ?  439 HOH   B O   1 
HETATM 6682 O  O   . HOH   L 4 .   ? -41.733 -12.427 38.294  1.00 28.37 ?  440 HOH   B O   1 
HETATM 6683 O  O   . HOH   L 4 .   ? -32.735 -13.958 20.548  1.00 42.49 ?  441 HOH   B O   1 
HETATM 6684 O  O   . HOH   L 4 .   ? -57.930 -22.841 11.859  1.00 44.20 ?  442 HOH   B O   1 
HETATM 6685 O  O   . HOH   L 4 .   ? -27.037 -12.345 34.695  1.00 49.85 ?  443 HOH   B O   1 
HETATM 6686 O  O   . HOH   L 4 .   ? -55.050 -4.939  13.123  1.00 38.75 ?  444 HOH   B O   1 
HETATM 6687 O  O   . HOH   L 4 .   ? -64.352 -27.723 29.659  1.00 30.17 ?  445 HOH   B O   1 
HETATM 6688 O  O   . HOH   L 4 .   ? -48.058 -24.282 38.048  1.00 27.43 ?  446 HOH   B O   1 
HETATM 6689 O  O   . HOH   L 4 .   ? -40.018 -15.506 49.644  1.00 44.11 ?  447 HOH   B O   1 
HETATM 6690 O  O   . HOH   L 4 .   ? -47.342 -20.959 25.864  1.00 29.21 ?  448 HOH   B O   1 
HETATM 6691 O  O   . HOH   L 4 .   ? -45.862 -10.912 13.594  1.00 37.85 ?  449 HOH   B O   1 
HETATM 6692 O  O   . HOH   L 4 .   ? -50.712 5.460   18.966  1.00 29.55 ?  450 HOH   B O   1 
HETATM 6693 O  O   . HOH   L 4 .   ? -43.566 -22.296 24.102  1.00 36.99 ?  451 HOH   B O   1 
HETATM 6694 O  O   . HOH   L 4 .   ? -38.935 -8.701  46.342  1.00 21.57 ?  452 HOH   B O   1 
HETATM 6695 O  O   . HOH   L 4 .   ? -58.611 1.127   29.823  1.00 33.83 ?  453 HOH   B O   1 
HETATM 6696 O  O   . HOH   L 4 .   ? -46.098 -17.874 16.241  1.00 32.49 ?  454 HOH   B O   1 
HETATM 6697 O  O   . HOH   L 4 .   ? -59.517 -11.985 18.793  1.00 18.59 ?  455 HOH   B O   1 
HETATM 6698 O  O   . HOH   L 4 .   ? -66.355 -11.467 27.903  1.00 24.91 ?  456 HOH   B O   1 
HETATM 6699 O  O   . HOH   L 4 .   ? -41.238 6.864   26.235  1.00 25.82 ?  457 HOH   B O   1 
HETATM 6700 O  O   . HOH   L 4 .   ? -29.851 9.330   45.035  1.00 19.24 ?  458 HOH   B O   1 
HETATM 6701 O  O   . HOH   L 4 .   ? -43.654 -20.119 31.629  1.00 40.71 ?  459 HOH   B O   1 
HETATM 6702 O  O   . HOH   L 4 .   ? -50.212 -26.892 35.497  1.00 30.19 ?  460 HOH   B O   1 
HETATM 6703 O  O   . HOH   L 4 .   ? -63.582 3.270   21.234  1.00 29.03 ?  461 HOH   B O   1 
HETATM 6704 O  O   . HOH   L 4 .   ? -41.999 -12.461 47.861  1.00 40.26 ?  462 HOH   B O   1 
HETATM 6705 O  O   . HOH   L 4 .   ? -52.576 -25.677 32.733  1.00 31.97 ?  463 HOH   B O   1 
HETATM 6706 O  O   . HOH   L 4 .   ? -41.749 -14.147 16.949  1.00 27.47 ?  464 HOH   B O   1 
HETATM 6707 O  O   . HOH   L 4 .   ? -38.064 -13.900 34.036  1.00 36.89 ?  465 HOH   B O   1 
HETATM 6708 O  O   . HOH   L 4 .   ? -64.079 -29.689 33.973  1.00 42.50 ?  466 HOH   B O   1 
HETATM 6709 O  O   . HOH   L 4 .   ? -61.401 -19.988 13.453  1.00 31.24 ?  467 HOH   B O   1 
HETATM 6710 O  O   . HOH   L 4 .   ? -31.564 -1.626  28.852  1.00 25.89 ?  468 HOH   B O   1 
HETATM 6711 O  O   . HOH   L 4 .   ? -63.227 -13.563 20.217  1.00 33.88 ?  469 HOH   B O   1 
HETATM 6712 O  O   . HOH   L 4 .   ? -71.360 -20.619 26.528  1.00 23.58 ?  470 HOH   B O   1 
HETATM 6713 O  O   . HOH   L 4 .   ? -31.342 -11.397 51.144  1.00 27.12 ?  471 HOH   B O   1 
HETATM 6714 O  O   . HOH   L 4 .   ? -44.780 -12.528 29.426  1.00 19.32 ?  472 HOH   B O   1 
HETATM 6715 O  O   . HOH   L 4 .   ? -22.152 1.492   38.363  1.00 42.41 ?  473 HOH   B O   1 
HETATM 6716 O  O   . HOH   L 4 .   ? -35.996 -15.006 29.414  1.00 36.59 ?  474 HOH   B O   1 
HETATM 6717 O  O   . HOH   L 4 .   ? -61.314 13.155  21.846  1.00 43.64 ?  475 HOH   B O   1 
HETATM 6718 O  O   . HOH   L 4 .   ? -66.840 -13.738 26.370  1.00 24.73 ?  476 HOH   B O   1 
HETATM 6719 O  O   . HOH   L 4 .   ? -57.448 -4.690  32.261  1.00 19.56 ?  477 HOH   B O   1 
HETATM 6720 O  O   . HOH   L 4 .   ? -40.255 -2.934  46.934  1.00 31.43 ?  478 HOH   B O   1 
HETATM 6721 O  O   . HOH   L 4 .   ? -44.222 -17.677 25.858  1.00 29.42 ?  479 HOH   B O   1 
HETATM 6722 O  O   . HOH   L 4 .   ? -26.727 1.675   55.250  1.00 23.44 ?  480 HOH   B O   1 
HETATM 6723 O  O   . HOH   L 4 .   ? -49.451 -14.645 14.090  1.00 52.91 ?  481 HOH   B O   1 
HETATM 6724 O  O   . HOH   L 4 .   ? -26.807 -1.008  54.164  1.00 20.30 ?  482 HOH   B O   1 
HETATM 6725 O  O   . HOH   L 4 .   ? -52.667 -13.065 26.380  1.00 17.53 ?  483 HOH   B O   1 
HETATM 6726 O  O   . HOH   L 4 .   ? -66.670 -8.972  27.022  1.00 33.00 ?  484 HOH   B O   1 
HETATM 6727 O  O   . HOH   L 4 .   ? -59.667 -27.589 34.078  1.00 28.99 ?  485 HOH   B O   1 
HETATM 6728 O  O   . HOH   L 4 .   ? -35.095 -1.022  17.110  1.00 41.42 ?  486 HOH   B O   1 
HETATM 6729 O  O   . HOH   L 4 .   ? -36.354 -9.018  57.567  1.00 28.06 ?  487 HOH   B O   1 
HETATM 6730 O  O   . HOH   L 4 .   ? -60.174 2.001   27.642  1.00 33.63 ?  488 HOH   B O   1 
HETATM 6731 O  O   . HOH   L 4 .   ? -35.372 -15.924 26.966  1.00 35.27 ?  489 HOH   B O   1 
HETATM 6732 O  O   . HOH   L 4 .   ? -45.738 -5.534  33.677  1.00 19.66 ?  490 HOH   B O   1 
HETATM 6733 O  O   . HOH   L 4 .   ? -40.726 -1.136  38.174  1.00 17.16 ?  491 HOH   B O   1 
HETATM 6734 O  O   . HOH   L 4 .   ? -20.230 -0.591  51.454  1.00 34.78 ?  492 HOH   B O   1 
HETATM 6735 O  O   . HOH   L 4 .   ? -28.735 -7.925  53.706  1.00 32.36 ?  493 HOH   B O   1 
HETATM 6736 O  O   . HOH   L 4 .   ? -56.820 -22.986 18.485  1.00 27.43 ?  494 HOH   B O   1 
HETATM 6737 O  O   . HOH   L 4 .   ? -30.681 4.552   40.876  1.00 21.67 ?  495 HOH   B O   1 
HETATM 6738 O  O   . HOH   L 4 .   ? -51.037 -17.113 15.893  1.00 35.34 ?  496 HOH   B O   1 
HETATM 6739 O  O   . HOH   L 4 .   ? -39.529 1.317   23.034  1.00 23.93 ?  497 HOH   B O   1 
HETATM 6740 O  O   . HOH   L 4 .   ? -57.904 13.369  27.654  1.00 31.29 ?  498 HOH   B O   1 
HETATM 6741 O  O   . HOH   L 4 .   ? -34.486 -8.624  34.102  1.00 24.70 ?  499 HOH   B O   1 
HETATM 6742 O  O   . HOH   L 4 .   ? -64.334 -1.776  21.796  1.00 28.58 ?  500 HOH   B O   1 
HETATM 6743 O  O   . HOH   L 4 .   ? -61.087 -9.980  32.876  1.00 33.19 ?  501 HOH   B O   1 
HETATM 6744 O  O   . HOH   L 4 .   ? -62.652 -6.373  31.167  1.00 42.77 ?  502 HOH   B O   1 
HETATM 6745 O  O   . HOH   L 4 .   ? -47.526 1.912   28.433  1.00 23.77 ?  503 HOH   B O   1 
HETATM 6746 O  O   . HOH   L 4 .   ? -22.614 -8.656  43.119  1.00 52.84 ?  504 HOH   B O   1 
HETATM 6747 O  O   . HOH   L 4 .   ? -26.844 9.171   29.885  1.00 39.68 ?  505 HOH   B O   1 
HETATM 6748 O  O   . HOH   L 4 .   ? -28.648 -8.081  49.284  1.00 25.15 ?  506 HOH   B O   1 
HETATM 6749 O  O   . HOH   L 4 .   ? -46.276 -1.609  33.352  1.00 23.07 ?  507 HOH   B O   1 
HETATM 6750 O  O   . HOH   L 4 .   ? -44.641 -2.197  42.184  1.00 46.53 ?  508 HOH   B O   1 
HETATM 6751 O  O   . HOH   L 4 .   ? -36.414 -3.052  52.546  1.00 22.72 ?  509 HOH   B O   1 
HETATM 6752 O  O   . HOH   L 4 .   ? -34.772 2.784   51.084  1.00 18.71 ?  510 HOH   B O   1 
HETATM 6753 O  O   . HOH   L 4 .   ? -27.145 -9.119  47.397  1.00 46.83 ?  511 HOH   B O   1 
HETATM 6754 O  O   . HOH   L 4 .   ? -36.909 9.410   24.501  1.00 38.91 ?  512 HOH   B O   1 
HETATM 6755 O  O   . HOH   L 4 .   ? -54.730 -30.001 27.773  1.00 30.60 ?  513 HOH   B O   1 
HETATM 6756 O  O   . HOH   L 4 .   ? -43.932 1.310   42.032  1.00 45.65 ?  514 HOH   B O   1 
HETATM 6757 O  O   . HOH   L 4 .   ? -66.614 -4.194  20.566  1.00 40.26 ?  515 HOH   B O   1 
HETATM 6758 O  O   . HOH   L 4 .   ? -45.460 -10.556 37.688  1.00 25.44 ?  516 HOH   B O   1 
HETATM 6759 O  O   . HOH   L 4 .   ? -32.717 -5.459  23.739  1.00 34.52 ?  517 HOH   B O   1 
HETATM 6760 O  O   . HOH   L 4 .   ? -45.624 -20.409 41.097  1.00 42.78 ?  518 HOH   B O   1 
HETATM 6761 O  O   . HOH   L 4 .   ? -32.647 0.241   26.454  1.00 42.95 ?  519 HOH   B O   1 
HETATM 6762 O  O   . HOH   L 4 .   ? -43.459 -14.352 27.854  1.00 23.14 ?  520 HOH   B O   1 
HETATM 6763 O  O   . HOH   L 4 .   ? -41.042 -7.148  53.183  1.00 22.62 ?  521 HOH   B O   1 
HETATM 6764 O  O   . HOH   L 4 .   ? -42.214 -0.887  45.569  1.00 37.02 ?  522 HOH   B O   1 
HETATM 6765 O  O   . HOH   L 4 .   ? -37.761 0.638   49.876  1.00 17.40 ?  523 HOH   B O   1 
HETATM 6766 O  O   . HOH   L 4 .   ? -23.952 14.058  46.662  1.00 50.41 ?  524 HOH   B O   1 
HETATM 6767 O  O   . HOH   L 4 .   ? -50.439 -19.268 42.213  1.00 27.65 ?  525 HOH   B O   1 
HETATM 6768 O  O   . HOH   L 4 .   ? -20.865 11.967  53.371  1.00 35.60 ?  526 HOH   B O   1 
HETATM 6769 O  O   . HOH   L 4 .   ? -58.067 -30.706 34.160  1.00 33.11 ?  527 HOH   B O   1 
HETATM 6770 O  O   . HOH   L 4 .   ? -55.328 0.085   34.215  1.00 41.08 ?  528 HOH   B O   1 
HETATM 6771 O  O   . HOH   L 4 .   ? -40.445 -4.734  43.739  1.00 24.67 ?  529 HOH   B O   1 
HETATM 6772 O  O   . HOH   L 4 .   ? -56.013 -29.091 37.971  1.00 28.54 ?  530 HOH   B O   1 
HETATM 6773 O  O   . HOH   L 4 .   ? -28.403 -11.046 25.851  1.00 32.50 ?  531 HOH   B O   1 
HETATM 6774 O  O   . HOH   L 4 .   ? -63.143 -17.598 13.094  1.00 44.55 ?  532 HOH   B O   1 
HETATM 6775 O  O   . HOH   L 4 .   ? -46.452 -15.211 16.253  1.00 28.57 ?  533 HOH   B O   1 
HETATM 6776 O  O   . HOH   L 4 .   ? -29.270 -12.497 42.069  1.00 38.89 ?  534 HOH   B O   1 
HETATM 6777 O  O   . HOH   L 4 .   ? -32.377 7.482   25.810  1.00 35.48 ?  535 HOH   B O   1 
HETATM 6778 O  O   . HOH   L 4 .   ? -64.167 -11.334 34.403  1.00 41.40 ?  536 HOH   B O   1 
HETATM 6779 O  O   . HOH   L 4 .   ? -59.834 -25.856 23.680  1.00 22.52 ?  537 HOH   B O   1 
HETATM 6780 O  O   . HOH   L 4 .   ? -42.898 -16.907 28.499  1.00 35.14 ?  538 HOH   B O   1 
HETATM 6781 O  O   . HOH   L 4 .   ? -34.084 -7.501  24.395  1.00 25.46 ?  539 HOH   B O   1 
HETATM 6782 O  O   . HOH   L 4 .   ? -16.854 3.365   46.807  1.00 32.37 ?  540 HOH   B O   1 
HETATM 6783 O  O   . HOH   L 4 .   ? -23.336 -3.773  44.972  1.00 38.03 ?  541 HOH   B O   1 
HETATM 6784 O  O   . HOH   L 4 .   ? -44.033 -17.166 31.124  1.00 34.11 ?  542 HOH   B O   1 
HETATM 6785 O  O   . HOH   L 4 .   ? -57.642 -24.738 16.875  1.00 40.01 ?  543 HOH   B O   1 
HETATM 6786 O  O   . HOH   L 4 .   ? -28.642 -12.337 44.845  1.00 49.78 ?  544 HOH   B O   1 
HETATM 6787 O  O   . HOH   L 4 .   ? -47.158 -8.820  35.676  1.00 21.23 ?  545 HOH   B O   1 
HETATM 6788 O  O   . HOH   L 4 .   ? -59.432 6.887   20.307  1.00 49.98 ?  546 HOH   B O   1 
HETATM 6789 O  O   . HOH   L 4 .   ? -40.577 1.240   48.207  1.00 22.52 ?  547 HOH   B O   1 
HETATM 6790 O  O   . HOH   L 4 .   ? -64.427 -14.663 15.534  1.00 46.03 ?  548 HOH   B O   1 
HETATM 6791 O  O   . HOH   L 4 .   ? -34.571 -3.940  54.920  1.00 32.82 ?  549 HOH   B O   1 
HETATM 6792 O  O   . HOH   L 4 .   ? -51.271 4.630   15.271  1.00 41.10 ?  550 HOH   B O   1 
HETATM 6793 O  O   . HOH   L 4 .   ? -63.352 -22.190 19.577  1.00 37.27 ?  551 HOH   B O   1 
HETATM 6794 O  O   . HOH   L 4 .   ? -56.933 -1.925  32.516  1.00 20.71 ?  552 HOH   B O   1 
HETATM 6795 O  O   . HOH   L 4 .   ? -67.183 -28.925 29.626  1.00 42.91 ?  553 HOH   B O   1 
HETATM 6796 O  O   . HOH   L 4 .   ? -45.643 -7.896  38.013  1.00 41.45 ?  554 HOH   B O   1 
HETATM 6797 O  O   . HOH   L 4 .   ? -48.031 -2.045  35.486  1.00 25.80 ?  555 HOH   B O   1 
HETATM 6798 O  O   . HOH   L 4 .   ? -25.483 10.390  46.755  1.00 28.12 ?  556 HOH   B O   1 
HETATM 6799 O  O   . HOH   L 4 .   ? -28.034 11.223  46.122  1.00 24.15 ?  557 HOH   B O   1 
HETATM 6800 O  O   . HOH   L 4 .   ? -34.739 -1.010  19.875  1.00 27.12 ?  558 HOH   B O   1 
HETATM 6801 O  O   . HOH   L 4 .   ? -70.125 -26.874 32.172  1.00 48.37 ?  559 HOH   B O   1 
HETATM 6802 O  O   . HOH   L 4 .   ? -38.156 -6.101  45.042  1.00 26.29 ?  560 HOH   B O   1 
HETATM 6803 O  O   . HOH   L 4 .   ? -27.524 -8.935  51.395  1.00 34.52 ?  561 HOH   B O   1 
HETATM 6804 O  O   . HOH   L 4 .   ? -52.270 -28.302 31.648  1.00 40.20 ?  562 HOH   B O   1 
HETATM 6805 O  O   . HOH   L 4 .   ? -45.059 1.886   17.896  1.00 27.00 ?  563 HOH   B O   1 
HETATM 6806 O  O   . HOH   L 4 .   ? -33.754 -6.130  21.350  1.00 29.58 ?  564 HOH   B O   1 
HETATM 6807 O  O   . HOH   L 4 .   ? -31.582 -11.127 46.525  1.00 44.84 ?  565 HOH   B O   1 
HETATM 6808 O  O   . HOH   L 4 .   ? -38.263 -11.591 46.337  1.00 37.57 ?  566 HOH   B O   1 
HETATM 6809 O  O   . HOH   L 4 .   ? -32.257 -11.485 39.490  1.00 43.26 ?  567 HOH   B O   1 
HETATM 6810 O  O   . HOH   L 4 .   ? -34.354 -11.920 36.636  1.00 43.73 ?  568 HOH   B O   1 
HETATM 6811 O  O   . HOH   L 4 .   ? -67.887 -6.501  23.357  1.00 39.43 ?  569 HOH   B O   1 
HETATM 6812 O  O   . HOH   L 4 .   ? -22.315 -9.284  49.450  1.00 42.52 ?  570 HOH   B O   1 
HETATM 6813 O  O   . HOH   L 4 .   ? -29.838 8.930   27.284  1.00 44.77 ?  571 HOH   B O   1 
HETATM 6814 O  O   . HOH   L 4 .   ? -68.827 -27.107 24.651  1.00 32.38 ?  572 HOH   B O   1 
HETATM 6815 O  O   . HOH   L 4 .   ? -28.734 -4.339  26.607  1.00 48.09 ?  573 HOH   B O   1 
HETATM 6816 O  O   . HOH   L 4 .   ? -21.699 9.432   42.854  1.00 47.91 ?  574 HOH   B O   1 
HETATM 6817 O  O   . HOH   L 4 .   ? -39.584 -14.067 15.635  1.00 39.40 ?  575 HOH   B O   1 
HETATM 6818 O  O   . HOH   L 4 .   ? -34.294 9.188   24.343  1.00 36.90 ?  576 HOH   B O   1 
HETATM 6819 O  O   . HOH   L 4 .   ? -23.523 -1.133  39.533  1.00 35.90 ?  577 HOH   B O   1 
HETATM 6820 O  O   . HOH   L 4 .   ? -38.760 10.932  21.547  1.00 39.17 ?  578 HOH   B O   1 
HETATM 6821 O  O   . HOH   L 4 .   ? -42.129 5.724   18.303  1.00 34.31 ?  579 HOH   B O   1 
HETATM 6822 O  O   . HOH   L 4 .   ? -62.096 -22.170 17.816  1.00 47.99 ?  580 HOH   B O   1 
HETATM 6823 O  O   . HOH   L 4 .   ? -24.341 -1.818  54.770  1.00 35.37 ?  581 HOH   B O   1 
HETATM 6824 O  O   . HOH   L 4 .   ? -42.657 0.507   38.840  1.00 27.91 ?  582 HOH   B O   1 
HETATM 6825 O  O   . HOH   L 4 .   ? -63.549 3.673   18.597  1.00 50.76 ?  583 HOH   B O   1 
HETATM 6826 O  O   . HOH   L 4 .   ? -62.448 5.590   25.386  1.00 52.66 ?  584 HOH   B O   1 
HETATM 6827 O  O   . HOH   L 4 .   ? -59.183 11.780  27.917  1.00 46.35 ?  585 HOH   B O   1 
HETATM 6828 O  O   . HOH   L 4 .   ? -27.929 10.992  42.017  1.00 34.59 ?  586 HOH   B O   1 
HETATM 6829 O  O   . HOH   L 4 .   ? -49.255 -20.259 44.425  1.00 45.00 ?  587 HOH   B O   1 
HETATM 6830 O  O   . HOH   L 4 .   ? -63.511 -15.300 18.424  1.00 40.08 ?  588 HOH   B O   1 
HETATM 6831 O  O   . HOH   L 4 .   ? -57.308 -34.839 32.146  1.00 37.66 ?  589 HOH   B O   1 
HETATM 6832 O  O   . HOH   L 4 .   ? -68.693 -23.767 22.268  1.00 43.44 ?  590 HOH   B O   1 
HETATM 6833 O  O   . HOH   L 4 .   ? -59.429 -5.931  34.200  1.00 27.31 ?  591 HOH   B O   1 
HETATM 6834 O  O   . HOH   L 4 .   ? -38.967 -12.478 37.908  1.00 43.74 ?  592 HOH   B O   1 
HETATM 6835 O  O   . HOH   L 4 .   ? -36.202 -9.796  35.763  1.00 45.79 ?  593 HOH   B O   1 
HETATM 6836 O  O   . HOH   L 4 .   ? -36.488 -5.498  58.985  1.00 25.26 ?  594 HOH   B O   1 
HETATM 6837 O  O   . HOH   L 4 .   ? -40.271 8.957   20.408  1.00 44.77 ?  595 HOH   B O   1 
HETATM 6838 O  O   . HOH   L 4 .   ? -60.463 -28.988 36.084  1.00 41.03 ?  596 HOH   B O   1 
HETATM 6839 O  O   . HOH   L 4 .   ? -41.067 -15.308 52.000  1.00 36.48 ?  597 HOH   B O   1 
HETATM 6840 O  O   . HOH   L 4 .   ? -63.116 5.406   22.749  1.00 41.27 ?  598 HOH   B O   1 
HETATM 6841 O  O   . HOH   L 4 .   ? -55.847 -27.867 40.246  1.00 33.25 ?  599 HOH   B O   1 
HETATM 6842 O  O   . HOH   L 4 .   ? -28.011 9.656   57.208  1.00 38.15 ?  600 HOH   B O   1 
HETATM 6843 O  O   . HOH   L 4 .   ? -54.594 18.613  20.837  1.00 45.39 ?  601 HOH   B O   1 
HETATM 6844 O  O   . HOH   L 4 .   ? -30.590 -10.412 48.768  1.00 37.56 ?  602 HOH   B O   1 
HETATM 6845 O  O   . HOH   L 4 .   ? -62.605 -30.697 35.567  1.00 45.46 ?  603 HOH   B O   1 
HETATM 6846 O  O   . HOH   L 4 .   ? -45.240 -0.522  38.978  1.00 34.38 ?  604 HOH   B O   1 
HETATM 6847 O  O   . HOH   L 4 .   ? -64.555 -2.946  16.732  1.00 47.99 ?  605 HOH   B O   1 
HETATM 6848 O  O   . HOH   L 4 .   ? -44.951 -20.322 26.019  1.00 30.51 ?  606 HOH   B O   1 
HETATM 6849 O  O   . HOH   L 4 .   ? -39.339 -2.876  53.010  1.00 35.62 ?  607 HOH   B O   1 
HETATM 6850 O  O   . HOH   L 4 .   ? -61.258 6.462   18.721  1.00 40.85 ?  608 HOH   B O   1 
HETATM 6851 O  O   . HOH   L 4 .   ? -46.044 -11.936 40.006  1.00 28.08 ?  609 HOH   B O   1 
HETATM 6852 O  O   . HOH   L 4 .   ? -31.910 -5.467  19.162  1.00 46.86 ?  610 HOH   B O   1 
HETATM 6853 O  O   . HOH   L 4 .   ? -40.810 -4.416  54.251  1.00 30.00 ?  611 HOH   B O   1 
HETATM 6854 O  O   . HOH   L 4 .   ? -52.135 18.515  21.098  1.00 46.56 ?  612 HOH   B O   1 
HETATM 6855 O  O   . HOH   L 4 .   ? -40.886 -1.873  51.251  1.00 29.87 ?  613 HOH   B O   1 
HETATM 6856 O  O   . HOH   L 4 .   ? -35.126 13.387  20.789  1.00 43.53 ?  614 HOH   B O   1 
HETATM 6857 O  O   . HOH   M 4 .   ? -60.774 19.041  37.343  1.00 40.36 ?  401 HOH   C O   1 
HETATM 6858 O  O   . HOH   M 4 .   ? -47.719 -9.668  43.729  1.00 29.19 ?  402 HOH   C O   1 
HETATM 6859 O  O   . HOH   M 4 .   ? -64.809 -22.028 38.617  1.00 36.64 ?  403 HOH   C O   1 
HETATM 6860 O  O   . HOH   M 4 .   ? -30.121 26.487  49.759  1.00 46.18 ?  404 HOH   C O   1 
HETATM 6861 O  O   . HOH   M 4 .   ? -56.872 16.874  29.407  1.00 35.54 ?  405 HOH   C O   1 
HETATM 6862 O  O   . HOH   M 4 .   ? -41.888 32.801  44.645  1.00 50.64 ?  406 HOH   C O   1 
HETATM 6863 O  O   . HOH   M 4 .   ? -43.482 3.020   37.774  1.00 34.36 ?  407 HOH   C O   1 
HETATM 6864 O  O   . HOH   M 4 .   ? -34.033 12.184  61.069  1.00 37.69 ?  408 HOH   C O   1 
HETATM 6865 O  O   . HOH   M 4 .   ? -36.060 25.277  41.390  1.00 25.15 ?  409 HOH   C O   1 
HETATM 6866 O  O   . HOH   M 4 .   ? -57.471 1.601   50.399  1.00 44.07 ?  410 HOH   C O   1 
HETATM 6867 O  O   . HOH   M 4 .   ? -67.993 -0.351  33.374  1.00 38.89 ?  411 HOH   C O   1 
HETATM 6868 O  O   . HOH   M 4 .   ? -45.824 26.818  32.105  1.00 33.02 ?  412 HOH   C O   1 
HETATM 6869 O  O   . HOH   M 4 .   ? -31.937 14.797  25.725  1.00 39.57 ?  413 HOH   C O   1 
HETATM 6870 O  O   . HOH   M 4 .   ? -63.617 7.735   39.820  1.00 39.81 ?  414 HOH   C O   1 
HETATM 6871 O  O   . HOH   M 4 .   ? -50.148 11.549  16.333  1.00 41.52 ?  415 HOH   C O   1 
HETATM 6872 O  O   . HOH   M 4 .   ? -51.724 13.509  24.824  1.00 30.12 ?  416 HOH   C O   1 
HETATM 6873 O  O   . HOH   M 4 .   ? -68.010 -5.009  42.972  1.00 41.77 ?  417 HOH   C O   1 
HETATM 6874 O  O   . HOH   M 4 .   ? -43.361 6.613   20.956  1.00 27.45 ?  418 HOH   C O   1 
HETATM 6875 O  O   . HOH   M 4 .   ? -59.129 6.745   27.055  1.00 45.65 ?  419 HOH   C O   1 
HETATM 6876 O  O   . HOH   M 4 .   ? -48.808 15.040  49.308  1.00 34.47 ?  420 HOH   C O   1 
HETATM 6877 O  O   . HOH   M 4 .   ? -32.406 8.059   59.385  1.00 26.49 ?  421 HOH   C O   1 
HETATM 6878 O  O   . HOH   M 4 .   ? -58.220 -23.329 47.640  1.00 29.92 ?  422 HOH   C O   1 
HETATM 6879 O  O   . HOH   M 4 .   ? -46.399 0.777   41.051  1.00 30.74 ?  423 HOH   C O   1 
HETATM 6880 O  O   . HOH   M 4 .   ? -65.575 -3.595  44.053  1.00 31.62 ?  424 HOH   C O   1 
HETATM 6881 O  O   . HOH   M 4 .   ? -47.452 1.354   49.392  1.00 31.91 ?  425 HOH   C O   1 
HETATM 6882 O  O   . HOH   M 4 .   ? -46.757 14.326  24.084  1.00 32.75 ?  426 HOH   C O   1 
HETATM 6883 O  O   . HOH   M 4 .   ? -61.048 -16.550 36.743  1.00 20.81 ?  427 HOH   C O   1 
HETATM 6884 O  O   . HOH   M 4 .   ? -40.106 10.562  24.506  1.00 47.91 ?  428 HOH   C O   1 
HETATM 6885 O  O   . HOH   M 4 .   ? -46.977 9.147   48.262  1.00 25.93 ?  429 HOH   C O   1 
HETATM 6886 O  O   . HOH   M 4 .   ? -74.076 -16.678 45.543  1.00 49.41 ?  430 HOH   C O   1 
HETATM 6887 O  O   . HOH   M 4 .   ? -29.325 18.996  37.294  1.00 30.04 ?  431 HOH   C O   1 
HETATM 6888 O  O   . HOH   M 4 .   ? -28.395 12.894  43.906  1.00 37.78 ?  432 HOH   C O   1 
HETATM 6889 O  O   . HOH   M 4 .   ? -57.112 21.693  41.937  1.00 40.14 ?  433 HOH   C O   1 
HETATM 6890 O  O   . HOH   M 4 .   ? -47.984 -8.139  49.215  1.00 34.42 ?  434 HOH   C O   1 
HETATM 6891 O  O   . HOH   M 4 .   ? -62.913 2.573   41.142  1.00 26.39 ?  435 HOH   C O   1 
HETATM 6892 O  O   . HOH   M 4 .   ? -59.907 -25.675 40.461  1.00 31.48 ?  436 HOH   C O   1 
HETATM 6893 O  O   . HOH   M 4 .   ? -43.512 26.816  30.214  1.00 28.40 ?  437 HOH   C O   1 
HETATM 6894 O  O   . HOH   M 4 .   ? -35.572 23.429  36.930  1.00 18.52 ?  438 HOH   C O   1 
HETATM 6895 O  O   . HOH   M 4 .   ? -39.600 15.378  22.090  1.00 33.53 ?  439 HOH   C O   1 
HETATM 6896 O  O   . HOH   M 4 .   ? -42.356 22.017  23.949  1.00 40.24 ?  440 HOH   C O   1 
HETATM 6897 O  O   . HOH   M 4 .   ? -40.498 3.029   55.664  1.00 25.48 ?  441 HOH   C O   1 
HETATM 6898 O  O   . HOH   M 4 .   ? -57.817 4.030   29.071  1.00 32.46 ?  442 HOH   C O   1 
HETATM 6899 O  O   . HOH   M 4 .   ? -37.855 7.710   34.725  1.00 18.65 ?  443 HOH   C O   1 
HETATM 6900 O  O   . HOH   M 4 .   ? -41.170 13.453  55.705  1.00 32.08 ?  444 HOH   C O   1 
HETATM 6901 O  O   . HOH   M 4 .   ? -28.867 26.287  40.636  1.00 36.72 ?  445 HOH   C O   1 
HETATM 6902 O  O   . HOH   M 4 .   ? -69.612 -3.393  33.990  1.00 37.06 ?  446 HOH   C O   1 
HETATM 6903 O  O   . HOH   M 4 .   ? -26.754 25.646  46.055  1.00 36.43 ?  447 HOH   C O   1 
HETATM 6904 O  O   . HOH   M 4 .   ? -47.138 24.108  30.278  1.00 23.37 ?  448 HOH   C O   1 
HETATM 6905 O  O   . HOH   M 4 .   ? -45.407 16.541  50.757  1.00 30.72 ?  449 HOH   C O   1 
HETATM 6906 O  O   . HOH   M 4 .   ? -44.532 13.675  20.324  1.00 42.50 ?  450 HOH   C O   1 
HETATM 6907 O  O   . HOH   M 4 .   ? -36.448 17.589  56.919  1.00 45.28 ?  451 HOH   C O   1 
HETATM 6908 O  O   . HOH   M 4 .   ? -60.607 -14.167 40.280  1.00 22.30 ?  452 HOH   C O   1 
HETATM 6909 O  O   . HOH   M 4 .   ? -64.674 -20.802 50.847  1.00 42.58 ?  453 HOH   C O   1 
HETATM 6910 O  O   . HOH   M 4 .   ? -61.493 -12.109 34.861  1.00 35.58 ?  454 HOH   C O   1 
HETATM 6911 O  O   . HOH   M 4 .   ? -52.739 -18.301 45.116  1.00 24.91 ?  455 HOH   C O   1 
HETATM 6912 O  O   . HOH   M 4 .   ? -36.986 17.503  26.330  1.00 24.34 ?  456 HOH   C O   1 
HETATM 6913 O  O   . HOH   M 4 .   ? -55.141 8.659   51.252  1.00 41.10 ?  457 HOH   C O   1 
HETATM 6914 O  O   . HOH   M 4 .   ? -47.393 29.404  42.144  1.00 46.63 ?  458 HOH   C O   1 
HETATM 6915 O  O   . HOH   M 4 .   ? -39.331 27.267  47.065  1.00 30.38 ?  459 HOH   C O   1 
HETATM 6916 O  O   . HOH   M 4 .   ? -53.237 -3.961  50.959  1.00 27.31 ?  460 HOH   C O   1 
HETATM 6917 O  O   . HOH   M 4 .   ? -51.860 4.403   50.799  1.00 35.72 ?  461 HOH   C O   1 
HETATM 6918 O  O   . HOH   M 4 .   ? -39.482 7.958   57.337  1.00 25.96 ?  462 HOH   C O   1 
HETATM 6919 O  O   . HOH   M 4 .   ? -48.174 9.850   45.702  1.00 19.67 ?  463 HOH   C O   1 
HETATM 6920 O  O   . HOH   M 4 .   ? -59.545 -1.842  31.119  1.00 30.59 ?  464 HOH   C O   1 
HETATM 6921 O  O   . HOH   M 4 .   ? -57.166 19.294  33.787  1.00 30.35 ?  465 HOH   C O   1 
HETATM 6922 O  O   . HOH   M 4 .   ? -48.464 3.245   30.762  1.00 20.47 ?  466 HOH   C O   1 
HETATM 6923 O  O   . HOH   M 4 .   ? -64.718 -19.498 38.082  1.00 28.67 ?  467 HOH   C O   1 
HETATM 6924 O  O   . HOH   M 4 .   ? -37.550 27.346  34.084  1.00 25.10 ?  468 HOH   C O   1 
HETATM 6925 O  O   . HOH   M 4 .   ? -56.330 11.040  51.515  1.00 51.44 ?  469 HOH   C O   1 
HETATM 6926 O  O   . HOH   M 4 .   ? -48.075 20.261  28.745  1.00 35.34 ?  470 HOH   C O   1 
HETATM 6927 O  O   . HOH   M 4 .   ? -42.244 14.924  42.144  1.00 17.74 ?  471 HOH   C O   1 
HETATM 6928 O  O   . HOH   M 4 .   ? -55.205 20.719  44.696  1.00 27.16 ?  472 HOH   C O   1 
HETATM 6929 O  O   . HOH   M 4 .   ? -49.900 5.706   31.766  1.00 21.22 ?  473 HOH   C O   1 
HETATM 6930 O  O   . HOH   M 4 .   ? -48.133 2.492   36.777  1.00 21.38 ?  474 HOH   C O   1 
HETATM 6931 O  O   . HOH   M 4 .   ? -47.013 -9.320  41.292  1.00 28.55 ?  475 HOH   C O   1 
HETATM 6932 O  O   . HOH   M 4 .   ? -46.614 10.517  52.981  1.00 40.98 ?  476 HOH   C O   1 
HETATM 6933 O  O   . HOH   M 4 .   ? -39.913 1.460   51.238  1.00 23.09 ?  477 HOH   C O   1 
HETATM 6934 O  O   . HOH   M 4 .   ? -59.815 3.784   52.496  1.00 51.22 ?  478 HOH   C O   1 
HETATM 6935 O  O   . HOH   M 4 .   ? -34.372 9.012   33.462  1.00 26.37 ?  479 HOH   C O   1 
HETATM 6936 O  O   . HOH   M 4 .   ? -39.826 24.305  29.422  1.00 33.95 ?  480 HOH   C O   1 
HETATM 6937 O  O   . HOH   M 4 .   ? -37.642 12.358  57.645  1.00 32.80 ?  481 HOH   C O   1 
HETATM 6938 O  O   . HOH   M 4 .   ? -60.684 16.125  47.134  1.00 32.17 ?  482 HOH   C O   1 
HETATM 6939 O  O   . HOH   M 4 .   ? -50.140 -15.451 42.833  1.00 23.33 ?  483 HOH   C O   1 
HETATM 6940 O  O   . HOH   M 4 .   ? -57.231 22.721  32.066  1.00 51.03 ?  484 HOH   C O   1 
HETATM 6941 O  O   . HOH   M 4 .   ? -64.451 15.894  42.889  1.00 41.07 ?  485 HOH   C O   1 
HETATM 6942 O  O   . HOH   M 4 .   ? -63.342 -10.326 46.462  1.00 32.41 ?  486 HOH   C O   1 
HETATM 6943 O  O   . HOH   M 4 .   ? -56.954 -7.995  56.284  1.00 44.34 ?  487 HOH   C O   1 
HETATM 6944 O  O   . HOH   M 4 .   ? -52.762 -17.879 42.425  1.00 18.62 ?  488 HOH   C O   1 
HETATM 6945 O  O   . HOH   M 4 .   ? -47.484 3.509   40.477  1.00 19.37 ?  489 HOH   C O   1 
HETATM 6946 O  O   . HOH   M 4 .   ? -49.586 11.767  47.298  1.00 23.05 ?  490 HOH   C O   1 
HETATM 6947 O  O   . HOH   M 4 .   ? -49.335 -16.563 47.278  1.00 33.00 ?  491 HOH   C O   1 
HETATM 6948 O  O   . HOH   M 4 .   ? -36.541 15.179  54.944  1.00 31.32 ?  492 HOH   C O   1 
HETATM 6949 O  O   . HOH   M 4 .   ? -57.295 -5.268  55.169  1.00 45.11 ?  493 HOH   C O   1 
HETATM 6950 O  O   . HOH   M 4 .   ? -66.971 7.422   47.643  1.00 32.91 ?  494 HOH   C O   1 
HETATM 6951 O  O   . HOH   M 4 .   ? -44.211 11.381  58.886  1.00 52.01 ?  495 HOH   C O   1 
HETATM 6952 O  O   . HOH   M 4 .   ? -52.089 16.734  50.691  1.00 38.60 ?  496 HOH   C O   1 
HETATM 6953 O  O   . HOH   M 4 .   ? -58.093 21.476  30.215  1.00 44.62 ?  497 HOH   C O   1 
HETATM 6954 O  O   . HOH   M 4 .   ? -60.793 -26.411 37.032  1.00 31.58 ?  498 HOH   C O   1 
HETATM 6955 O  O   . HOH   M 4 .   ? -67.286 -18.312 41.165  1.00 33.97 ?  499 HOH   C O   1 
HETATM 6956 O  O   . HOH   M 4 .   ? -43.585 -7.262  52.446  1.00 43.89 ?  500 HOH   C O   1 
HETATM 6957 O  O   . HOH   M 4 .   ? -31.036 17.445  32.964  1.00 26.54 ?  501 HOH   C O   1 
HETATM 6958 O  O   . HOH   M 4 .   ? -29.536 16.163  54.277  1.00 29.83 ?  502 HOH   C O   1 
HETATM 6959 O  O   . HOH   M 4 .   ? -61.881 15.315  49.178  1.00 35.08 ?  503 HOH   C O   1 
HETATM 6960 O  O   . HOH   M 4 .   ? -59.021 8.431   33.853  1.00 23.00 ?  504 HOH   C O   1 
HETATM 6961 O  O   . HOH   M 4 .   ? -39.572 22.992  36.598  1.00 17.49 ?  505 HOH   C O   1 
HETATM 6962 O  O   . HOH   M 4 .   ? -63.581 10.851  36.736  1.00 26.40 ?  506 HOH   C O   1 
HETATM 6963 O  O   . HOH   M 4 .   ? -60.683 -10.790 39.356  1.00 21.55 ?  507 HOH   C O   1 
HETATM 6964 O  O   . HOH   M 4 .   ? -32.804 11.204  34.292  1.00 25.68 ?  508 HOH   C O   1 
HETATM 6965 O  O   . HOH   M 4 .   ? -39.032 9.735   26.583  1.00 30.88 ?  509 HOH   C O   1 
HETATM 6966 O  O   . HOH   M 4 .   ? -27.684 13.127  53.932  1.00 31.81 ?  510 HOH   C O   1 
HETATM 6967 O  O   . HOH   M 4 .   ? -57.538 -21.419 49.546  1.00 26.56 ?  511 HOH   C O   1 
HETATM 6968 O  O   . HOH   M 4 .   ? -63.800 -12.603 50.517  1.00 47.01 ?  512 HOH   C O   1 
HETATM 6969 O  O   . HOH   M 4 .   ? -51.443 -3.474  39.821  1.00 19.50 ?  513 HOH   C O   1 
HETATM 6970 O  O   . HOH   M 4 .   ? -59.566 -12.774 32.985  1.00 32.59 ?  514 HOH   C O   1 
HETATM 6971 O  O   . HOH   M 4 .   ? -41.904 8.104   22.434  1.00 35.55 ?  515 HOH   C O   1 
HETATM 6972 O  O   . HOH   M 4 .   ? -46.481 25.380  43.770  1.00 40.40 ?  516 HOH   C O   1 
HETATM 6973 O  O   . HOH   M 4 .   ? -55.948 -13.726 53.642  1.00 40.79 ?  517 HOH   C O   1 
HETATM 6974 O  O   . HOH   M 4 .   ? -45.410 0.391   44.112  1.00 38.78 ?  518 HOH   C O   1 
HETATM 6975 O  O   . HOH   M 4 .   ? -44.923 1.828   46.283  1.00 27.91 ?  519 HOH   C O   1 
HETATM 6976 O  O   . HOH   M 4 .   ? -63.354 4.371   38.727  1.00 28.89 ?  520 HOH   C O   1 
HETATM 6977 O  O   . HOH   M 4 .   ? -44.375 4.583   17.189  1.00 28.75 ?  521 HOH   C O   1 
HETATM 6978 O  O   . HOH   M 4 .   ? -48.785 11.303  49.985  1.00 36.85 ?  522 HOH   C O   1 
HETATM 6979 O  O   . HOH   M 4 .   ? -51.335 -0.273  48.582  1.00 37.21 ?  523 HOH   C O   1 
HETATM 6980 O  O   . HOH   M 4 .   ? -42.631 22.131  49.423  1.00 25.99 ?  524 HOH   C O   1 
HETATM 6981 O  O   . HOH   M 4 .   ? -53.178 -9.849  54.154  1.00 36.86 ?  525 HOH   C O   1 
HETATM 6982 O  O   . HOH   M 4 .   ? -36.490 26.896  37.115  1.00 31.74 ?  526 HOH   C O   1 
HETATM 6983 O  O   . HOH   M 4 .   ? -29.930 17.167  57.378  1.00 35.49 ?  527 HOH   C O   1 
HETATM 6984 O  O   . HOH   M 4 .   ? -64.613 13.362  35.986  1.00 37.94 ?  528 HOH   C O   1 
HETATM 6985 O  O   . HOH   M 4 .   ? -49.788 -8.523  46.950  1.00 36.49 ?  529 HOH   C O   1 
HETATM 6986 O  O   . HOH   M 4 .   ? -39.116 6.256   32.657  1.00 20.81 ?  530 HOH   C O   1 
HETATM 6987 O  O   . HOH   M 4 .   ? -62.170 -14.207 35.916  1.00 30.62 ?  531 HOH   C O   1 
HETATM 6988 O  O   . HOH   M 4 .   ? -52.716 -19.717 52.555  1.00 41.88 ?  532 HOH   C O   1 
HETATM 6989 O  O   . HOH   M 4 .   ? -39.202 7.888   28.681  1.00 27.32 ?  533 HOH   C O   1 
HETATM 6990 O  O   . HOH   M 4 .   ? -31.109 12.456  58.399  1.00 28.83 ?  534 HOH   C O   1 
HETATM 6991 O  O   . HOH   M 4 .   ? -58.121 -11.556 57.477  1.00 47.83 ?  535 HOH   C O   1 
HETATM 6992 O  O   . HOH   M 4 .   ? -48.378 -13.258 40.753  1.00 22.35 ?  536 HOH   C O   1 
HETATM 6993 O  O   . HOH   M 4 .   ? -45.565 16.388  20.765  1.00 42.14 ?  537 HOH   C O   1 
HETATM 6994 O  O   . HOH   M 4 .   ? -37.859 1.528   53.988  1.00 29.94 ?  538 HOH   C O   1 
HETATM 6995 O  O   . HOH   M 4 .   ? -62.905 -18.817 35.870  1.00 20.40 ?  539 HOH   C O   1 
HETATM 6996 O  O   . HOH   M 4 .   ? -45.875 -6.350  40.694  1.00 36.69 ?  540 HOH   C O   1 
HETATM 6997 O  O   . HOH   M 4 .   ? -63.140 -10.399 48.940  1.00 38.05 ?  541 HOH   C O   1 
HETATM 6998 O  O   . HOH   M 4 .   ? -37.055 23.473  29.284  1.00 25.29 ?  542 HOH   C O   1 
HETATM 6999 O  O   . HOH   M 4 .   ? -29.714 14.221  32.056  1.00 40.43 ?  543 HOH   C O   1 
HETATM 7000 O  O   . HOH   M 4 .   ? -60.899 9.404   43.949  1.00 24.53 ?  544 HOH   C O   1 
HETATM 7001 O  O   . HOH   M 4 .   ? -47.280 -2.528  41.952  1.00 42.89 ?  545 HOH   C O   1 
HETATM 7002 O  O   . HOH   M 4 .   ? -26.461 20.780  50.678  1.00 27.24 ?  546 HOH   C O   1 
HETATM 7003 O  O   . HOH   M 4 .   ? -55.935 12.852  53.252  1.00 45.62 ?  547 HOH   C O   1 
HETATM 7004 O  O   . HOH   M 4 .   ? -49.843 14.252  15.655  1.00 42.69 ?  548 HOH   C O   1 
HETATM 7005 O  O   . HOH   M 4 .   ? -67.774 -22.817 35.661  1.00 48.26 ?  549 HOH   C O   1 
HETATM 7006 O  O   . HOH   M 4 .   ? -45.624 1.246   36.956  1.00 23.35 ?  550 HOH   C O   1 
HETATM 7007 O  O   . HOH   M 4 .   ? -56.476 1.448   47.647  1.00 25.23 ?  551 HOH   C O   1 
HETATM 7008 O  O   . HOH   M 4 .   ? -42.092 32.524  40.420  1.00 43.50 ?  552 HOH   C O   1 
HETATM 7009 O  O   . HOH   M 4 .   ? -70.912 -13.730 40.753  1.00 49.78 ?  553 HOH   C O   1 
HETATM 7010 O  O   . HOH   M 4 .   ? -48.284 -7.080  44.546  1.00 24.44 ?  554 HOH   C O   1 
HETATM 7011 O  O   . HOH   M 4 .   ? -47.134 18.770  21.705  1.00 52.06 ?  555 HOH   C O   1 
HETATM 7012 O  O   . HOH   M 4 .   ? -52.966 17.123  24.063  1.00 36.83 ?  556 HOH   C O   1 
HETATM 7013 O  O   . HOH   M 4 .   ? -44.562 3.566   43.368  1.00 21.03 ?  557 HOH   C O   1 
HETATM 7014 O  O   . HOH   M 4 .   ? -62.603 11.527  42.182  1.00 28.12 ?  558 HOH   C O   1 
HETATM 7015 O  O   . HOH   M 4 .   ? -42.291 1.787   54.029  1.00 31.67 ?  559 HOH   C O   1 
HETATM 7016 O  O   . HOH   M 4 .   ? -35.457 22.099  59.084  1.00 44.27 ?  560 HOH   C O   1 
HETATM 7017 O  O   . HOH   M 4 .   ? -51.263 23.082  43.469  1.00 31.75 ?  561 HOH   C O   1 
HETATM 7018 O  O   . HOH   M 4 .   ? -64.391 8.176   49.947  1.00 34.69 ?  562 HOH   C O   1 
HETATM 7019 O  O   . HOH   M 4 .   ? -56.303 14.059  29.705  1.00 36.98 ?  563 HOH   C O   1 
HETATM 7020 O  O   . HOH   M 4 .   ? -65.610 4.665   43.824  1.00 46.30 ?  564 HOH   C O   1 
HETATM 7021 O  O   . HOH   M 4 .   ? -70.645 -18.965 47.837  1.00 31.10 ?  565 HOH   C O   1 
HETATM 7022 O  O   . HOH   M 4 .   ? -43.773 -14.373 48.605  1.00 37.98 ?  566 HOH   C O   1 
HETATM 7023 O  O   . HOH   M 4 .   ? -28.313 22.757  52.950  1.00 33.78 ?  567 HOH   C O   1 
HETATM 7024 O  O   . HOH   M 4 .   ? -45.758 -10.337 54.236  1.00 36.04 ?  568 HOH   C O   1 
HETATM 7025 O  O   . HOH   M 4 .   ? -62.904 8.815   42.435  1.00 37.76 ?  569 HOH   C O   1 
HETATM 7026 O  O   . HOH   M 4 .   ? -57.910 18.776  31.473  1.00 44.49 ?  570 HOH   C O   1 
HETATM 7027 O  O   . HOH   M 4 .   ? -30.715 22.379  32.715  1.00 33.95 ?  571 HOH   C O   1 
HETATM 7028 O  O   . HOH   M 4 .   ? -62.840 -1.873  54.964  1.00 46.99 ?  572 HOH   C O   1 
HETATM 7029 O  O   . HOH   M 4 .   ? -39.936 21.025  52.791  1.00 38.95 ?  573 HOH   C O   1 
HETATM 7030 O  O   . HOH   M 4 .   ? -45.160 19.398  21.302  1.00 47.37 ?  574 HOH   C O   1 
HETATM 7031 O  O   . HOH   M 4 .   ? -68.196 -2.704  42.752  1.00 39.79 ?  575 HOH   C O   1 
HETATM 7032 O  O   . HOH   M 4 .   ? -53.138 26.511  29.110  1.00 47.64 ?  576 HOH   C O   1 
HETATM 7033 O  O   . HOH   M 4 .   ? -66.074 1.902   32.348  1.00 45.18 ?  577 HOH   C O   1 
HETATM 7034 O  O   . HOH   M 4 .   ? -47.733 -11.781 43.319  1.00 40.87 ?  578 HOH   C O   1 
HETATM 7035 O  O   . HOH   M 4 .   ? -23.169 19.377  43.323  1.00 46.48 ?  579 HOH   C O   1 
HETATM 7036 O  O   . HOH   M 4 .   ? -62.074 3.718   27.573  1.00 47.60 ?  580 HOH   C O   1 
HETATM 7037 O  O   . HOH   M 4 .   ? -59.489 -22.151 51.462  1.00 44.97 ?  581 HOH   C O   1 
HETATM 7038 O  O   . HOH   M 4 .   ? -39.079 25.294  49.121  1.00 36.45 ?  582 HOH   C O   1 
HETATM 7039 O  O   . HOH   M 4 .   ? -35.070 27.852  43.989  1.00 36.75 ?  583 HOH   C O   1 
HETATM 7040 O  O   . HOH   M 4 .   ? -23.921 21.314  50.333  1.00 37.41 ?  584 HOH   C O   1 
HETATM 7041 O  O   . HOH   M 4 .   ? -55.097 0.900   50.996  1.00 41.34 ?  585 HOH   C O   1 
HETATM 7042 O  O   . HOH   M 4 .   ? -41.980 20.311  51.588  1.00 29.81 ?  586 HOH   C O   1 
HETATM 7043 O  O   . HOH   M 4 .   ? -55.115 -21.786 49.859  1.00 38.91 ?  587 HOH   C O   1 
HETATM 7044 O  O   . HOH   M 4 .   ? -70.973 -12.504 37.849  1.00 41.37 ?  588 HOH   C O   1 
HETATM 7045 O  O   . HOH   M 4 .   ? -57.948 21.340  45.268  1.00 49.10 ?  589 HOH   C O   1 
HETATM 7046 O  O   . HOH   M 4 .   ? -67.355 -6.461  47.641  1.00 43.11 ?  590 HOH   C O   1 
HETATM 7047 O  O   . HOH   M 4 .   ? -35.715 25.309  38.540  1.00 35.36 ?  591 HOH   C O   1 
HETATM 7048 O  O   . HOH   M 4 .   ? -49.824 -4.176  37.803  1.00 29.64 ?  592 HOH   C O   1 
HETATM 7049 O  O   . HOH   M 4 .   ? -54.306 1.378   48.727  1.00 34.99 ?  593 HOH   C O   1 
HETATM 7050 O  O   . HOH   M 4 .   ? -65.967 -8.919  46.901  1.00 41.97 ?  594 HOH   C O   1 
HETATM 7051 O  O   . HOH   M 4 .   ? -38.456 22.035  26.229  1.00 35.88 ?  595 HOH   C O   1 
HETATM 7052 O  O   . HOH   M 4 .   ? -56.431 -24.938 47.229  1.00 49.27 ?  596 HOH   C O   1 
HETATM 7053 O  O   . HOH   M 4 .   ? -35.249 7.098   35.490  1.00 31.61 ?  597 HOH   C O   1 
HETATM 7054 O  O   . HOH   M 4 .   ? -39.934 21.107  21.215  1.00 52.64 ?  598 HOH   C O   1 
HETATM 7055 O  O   . HOH   M 4 .   ? -55.064 22.413  34.198  1.00 46.40 ?  599 HOH   C O   1 
HETATM 7056 O  O   . HOH   M 4 .   ? -27.053 27.050  43.708  1.00 39.05 ?  600 HOH   C O   1 
HETATM 7057 O  O   . HOH   M 4 .   ? -65.127 10.628  39.398  1.00 39.34 ?  601 HOH   C O   1 
HETATM 7058 O  O   . HOH   M 4 .   ? -24.024 12.327  45.098  1.00 41.78 ?  602 HOH   C O   1 
HETATM 7059 O  O   . HOH   M 4 .   ? -28.465 13.302  57.559  1.00 43.61 ?  603 HOH   C O   1 
HETATM 7060 O  O   . HOH   M 4 .   ? -35.170 24.211  56.482  1.00 45.05 ?  604 HOH   C O   1 
HETATM 7061 O  O   . HOH   M 4 .   ? -41.079 24.252  49.935  1.00 44.85 ?  605 HOH   C O   1 
HETATM 7062 O  O   . HOH   M 4 .   ? -38.122 14.738  58.784  1.00 46.09 ?  606 HOH   C O   1 
HETATM 7063 O  O   . HOH   M 4 .   ? -50.473 1.391   50.404  1.00 39.43 ?  607 HOH   C O   1 
HETATM 7064 O  O   . HOH   M 4 .   ? -42.093 28.059  48.080  1.00 39.83 ?  608 HOH   C O   1 
HETATM 7065 O  O   . HOH   M 4 .   ? -31.525 13.073  60.819  1.00 42.01 ?  609 HOH   C O   1 
HETATM 7066 O  O   . HOH   M 4 .   ? -58.452 -27.948 40.824  1.00 40.20 ?  610 HOH   C O   1 
HETATM 7067 O  O   . HOH   M 4 .   ? -25.545 16.796  56.327  1.00 44.07 ?  611 HOH   C O   1 
HETATM 7068 O  O   . HOH   M 4 .   ? -30.050 17.169  35.557  1.00 37.23 ?  612 HOH   C O   1 
HETATM 7069 O  O   . HOH   M 4 .   ? -45.596 -0.664  49.141  1.00 49.63 ?  613 HOH   C O   1 
HETATM 7070 O  O   . HOH   M 4 .   ? -30.726 9.677   57.909  1.00 28.69 ?  614 HOH   C O   1 
HETATM 7071 O  O   . HOH   M 4 .   ? -70.151 -7.064  42.088  1.00 43.64 ?  615 HOH   C O   1 
HETATM 7072 O  O   . HOH   M 4 .   ? -31.040 19.826  31.639  1.00 37.60 ?  616 HOH   C O   1 
HETATM 7073 O  O   . HOH   M 4 .   ? -41.597 0.045   52.384  1.00 26.61 ?  617 HOH   C O   1 
HETATM 7074 O  O   . HOH   M 4 .   ? -50.398 -17.210 45.096  1.00 33.37 ?  618 HOH   C O   1 
HETATM 7075 O  O   . HOH   M 4 .   ? -53.174 -1.679  48.995  1.00 39.41 ?  619 HOH   C O   1 
HETATM 7076 O  O   . HOH   M 4 .   ? -44.761 19.079  52.403  1.00 40.36 ?  620 HOH   C O   1 
HETATM 7077 O  O   . HOH   M 4 .   ? -28.918 16.917  31.420  1.00 40.14 ?  621 HOH   C O   1 
HETATM 7078 O  O   . HOH   M 4 .   ? -59.305 17.920  48.515  1.00 36.10 ?  622 HOH   C O   1 
HETATM 7079 O  O   . HOH   M 4 .   ? -40.525 19.629  54.625  1.00 48.94 ?  623 HOH   C O   1 
HETATM 7080 O  O   . HOH   M 4 .   ? -43.130 0.741   47.717  1.00 29.05 ?  624 HOH   C O   1 
HETATM 7081 O  O   . HOH   M 4 .   ? -32.399 11.563  24.328  1.00 38.89 ?  625 HOH   C O   1 
HETATM 7082 O  O   . HOH   M 4 .   ? -43.638 0.306   51.184  1.00 33.03 ?  626 HOH   C O   1 
HETATM 7083 O  O   . HOH   M 4 .   ? -49.308 26.107  44.681  1.00 39.99 ?  627 HOH   C O   1 
HETATM 7084 O  O   . HOH   M 4 .   ? -33.199 13.394  22.029  1.00 46.31 ?  628 HOH   C O   1 
HETATM 7085 O  O   . HOH   M 4 .   ? -43.133 26.432  49.412  1.00 46.44 ?  629 HOH   C O   1 
HETATM 7086 O  O   . HOH   M 4 .   ? -43.521 -2.542  51.483  1.00 41.82 ?  630 HOH   C O   1 
HETATM 7087 O  O   . HOH   M 4 .   ? -43.373 19.137  55.015  1.00 47.82 ?  631 HOH   C O   1 
HETATM 7088 O  O   . HOH   N 4 .   ? -47.955 3.753   67.356  1.00 34.62 ?  401 HOH   D O   1 
HETATM 7089 O  O   . HOH   N 4 .   ? -56.905 -22.648 81.722  1.00 34.41 ?  402 HOH   D O   1 
HETATM 7090 O  O   . HOH   N 4 .   ? -62.165 8.048   75.210  1.00 27.76 ?  403 HOH   D O   1 
HETATM 7091 O  O   . HOH   N 4 .   ? -43.582 -8.769  73.375  1.00 36.02 ?  404 HOH   D O   1 
HETATM 7092 O  O   . HOH   N 4 .   ? -47.876 2.583   61.949  1.00 33.22 ?  405 HOH   D O   1 
HETATM 7093 O  O   . HOH   N 4 .   ? -29.565 -25.051 73.329  1.00 31.00 ?  406 HOH   D O   1 
HETATM 7094 O  O   . HOH   N 4 .   ? -47.240 -30.134 80.659  1.00 31.13 ?  407 HOH   D O   1 
HETATM 7095 O  O   . HOH   N 4 .   ? -52.790 12.531  66.249  1.00 23.01 ?  408 HOH   D O   1 
HETATM 7096 O  O   . HOH   N 4 .   ? -58.331 17.492  64.057  1.00 22.36 ?  409 HOH   D O   1 
HETATM 7097 O  O   . HOH   N 4 .   ? -46.730 -20.055 86.868  1.00 30.87 ?  410 HOH   D O   1 
HETATM 7098 O  O   . HOH   N 4 .   ? -43.024 -12.624 90.097  1.00 27.17 ?  411 HOH   D O   1 
HETATM 7099 O  O   . HOH   N 4 .   ? -39.778 -32.979 63.910  1.00 37.03 ?  412 HOH   D O   1 
HETATM 7100 O  O   . HOH   N 4 .   ? -54.327 -29.603 64.103  1.00 38.40 ?  413 HOH   D O   1 
HETATM 7101 O  O   . HOH   N 4 .   ? -43.632 -32.648 80.919  1.00 30.63 ?  414 HOH   D O   1 
HETATM 7102 O  O   . HOH   N 4 .   ? -36.975 -33.101 73.896  1.00 43.16 ?  415 HOH   D O   1 
HETATM 7103 O  O   . HOH   N 4 .   ? -45.718 -32.713 78.952  1.00 33.37 ?  416 HOH   D O   1 
HETATM 7104 O  O   . HOH   N 4 .   ? -39.360 -21.436 88.683  1.00 29.59 ?  417 HOH   D O   1 
HETATM 7105 O  O   . HOH   N 4 .   ? -60.722 11.266  58.218  1.00 39.75 ?  418 HOH   D O   1 
HETATM 7106 O  O   . HOH   N 4 .   ? -32.892 -16.861 76.472  1.00 25.82 ?  419 HOH   D O   1 
HETATM 7107 O  O   . HOH   N 4 .   ? -63.612 -13.101 71.421  1.00 36.49 ?  420 HOH   D O   1 
HETATM 7108 O  O   . HOH   N 4 .   ? -61.147 20.347  74.860  1.00 34.05 ?  421 HOH   D O   1 
HETATM 7109 O  O   . HOH   N 4 .   ? -47.114 -14.862 62.746  1.00 22.38 ?  422 HOH   D O   1 
HETATM 7110 O  O   . HOH   N 4 .   ? -31.266 -23.332 77.752  1.00 27.98 ?  423 HOH   D O   1 
HETATM 7111 O  O   . HOH   N 4 .   ? -34.441 -15.044 77.356  1.00 30.79 ?  424 HOH   D O   1 
HETATM 7112 O  O   . HOH   N 4 .   ? -62.974 -8.307  70.293  1.00 28.85 ?  425 HOH   D O   1 
HETATM 7113 O  O   . HOH   N 4 .   ? -46.418 -6.597  69.995  1.00 27.37 ?  426 HOH   D O   1 
HETATM 7114 O  O   . HOH   N 4 .   ? -61.048 10.578  74.736  1.00 19.64 ?  427 HOH   D O   1 
HETATM 7115 O  O   . HOH   N 4 .   ? -64.414 -14.125 75.477  1.00 45.59 ?  428 HOH   D O   1 
HETATM 7116 O  O   . HOH   N 4 .   ? -61.035 -21.726 64.359  1.00 32.68 ?  429 HOH   D O   1 
HETATM 7117 O  O   . HOH   N 4 .   ? -27.385 -31.783 64.230  1.00 39.57 ?  430 HOH   D O   1 
HETATM 7118 O  O   . HOH   N 4 .   ? -64.481 13.607  73.280  1.00 36.53 ?  431 HOH   D O   1 
HETATM 7119 O  O   . HOH   N 4 .   ? -47.708 -6.912  61.791  1.00 27.23 ?  432 HOH   D O   1 
HETATM 7120 O  O   . HOH   N 4 .   ? -65.412 -2.213  66.988  1.00 32.53 ?  433 HOH   D O   1 
HETATM 7121 O  O   . HOH   N 4 .   ? -30.491 -23.124 53.444  1.00 32.91 ?  434 HOH   D O   1 
HETATM 7122 O  O   . HOH   N 4 .   ? -38.007 -18.288 53.169  1.00 33.00 ?  435 HOH   D O   1 
HETATM 7123 O  O   . HOH   N 4 .   ? -60.708 8.426   71.012  1.00 20.68 ?  436 HOH   D O   1 
HETATM 7124 O  O   . HOH   N 4 .   ? -55.489 -26.535 66.539  1.00 27.33 ?  437 HOH   D O   1 
HETATM 7125 O  O   . HOH   N 4 .   ? -35.861 -29.401 73.832  1.00 20.02 ?  438 HOH   D O   1 
HETATM 7126 O  O   . HOH   N 4 .   ? -49.337 -17.594 61.089  1.00 42.98 ?  439 HOH   D O   1 
HETATM 7127 O  O   . HOH   N 4 .   ? -28.623 -18.925 66.811  1.00 39.22 ?  440 HOH   D O   1 
HETATM 7128 O  O   . HOH   N 4 .   ? -51.650 -19.265 86.427  1.00 30.76 ?  441 HOH   D O   1 
HETATM 7129 O  O   . HOH   N 4 .   ? -32.530 -13.825 51.459  1.00 26.66 ?  442 HOH   D O   1 
HETATM 7130 O  O   . HOH   N 4 .   ? -49.329 10.715  63.989  1.00 27.42 ?  443 HOH   D O   1 
HETATM 7131 O  O   . HOH   N 4 .   ? -37.786 -33.336 76.941  1.00 26.98 ?  444 HOH   D O   1 
HETATM 7132 O  O   . HOH   N 4 .   ? -40.754 -8.744  55.236  1.00 28.44 ?  445 HOH   D O   1 
HETATM 7133 O  O   . HOH   N 4 .   ? -36.712 -23.465 84.350  1.00 23.53 ?  446 HOH   D O   1 
HETATM 7134 O  O   . HOH   N 4 .   ? -47.493 -9.324  70.609  1.00 20.09 ?  447 HOH   D O   1 
HETATM 7135 O  O   . HOH   N 4 .   ? -59.005 -12.849 84.332  1.00 35.11 ?  448 HOH   D O   1 
HETATM 7136 O  O   . HOH   N 4 .   ? -37.893 -13.621 76.026  1.00 17.89 ?  449 HOH   D O   1 
HETATM 7137 O  O   . HOH   N 4 .   ? -49.123 -20.760 61.647  1.00 35.66 ?  450 HOH   D O   1 
HETATM 7138 O  O   . HOH   N 4 .   ? -41.497 -19.114 55.190  1.00 30.49 ?  451 HOH   D O   1 
HETATM 7139 O  O   . HOH   N 4 .   ? -57.108 -0.444  56.203  1.00 44.96 ?  452 HOH   D O   1 
HETATM 7140 O  O   . HOH   N 4 .   ? -59.895 -9.620  58.619  1.00 40.73 ?  453 HOH   D O   1 
HETATM 7141 O  O   . HOH   N 4 .   ? -59.184 -4.078  80.239  1.00 26.11 ?  454 HOH   D O   1 
HETATM 7142 O  O   . HOH   N 4 .   ? -63.061 4.781   62.373  1.00 40.85 ?  455 HOH   D O   1 
HETATM 7143 O  O   . HOH   N 4 .   ? -42.403 -20.690 68.784  1.00 17.02 ?  456 HOH   D O   1 
HETATM 7144 O  O   . HOH   N 4 .   ? -63.975 -18.680 56.117  1.00 51.42 ?  457 HOH   D O   1 
HETATM 7145 O  O   . HOH   N 4 .   ? -52.767 12.111  69.076  1.00 19.01 ?  458 HOH   D O   1 
HETATM 7146 O  O   . HOH   N 4 .   ? -57.631 -9.774  82.212  1.00 29.09 ?  459 HOH   D O   1 
HETATM 7147 O  O   . HOH   N 4 .   ? -52.511 -22.733 60.323  1.00 40.81 ?  460 HOH   D O   1 
HETATM 7148 O  O   . HOH   N 4 .   ? -48.375 -15.577 65.325  1.00 19.55 ?  461 HOH   D O   1 
HETATM 7149 O  O   . HOH   N 4 .   ? -55.280 -14.337 59.955  1.00 43.09 ?  462 HOH   D O   1 
HETATM 7150 O  O   . HOH   N 4 .   ? -39.842 -28.933 74.256  1.00 20.30 ?  463 HOH   D O   1 
HETATM 7151 O  O   . HOH   N 4 .   ? -29.825 -22.046 56.460  1.00 29.18 ?  464 HOH   D O   1 
HETATM 7152 O  O   . HOH   N 4 .   ? -39.964 -7.215  59.879  1.00 19.25 ?  465 HOH   D O   1 
HETATM 7153 O  O   . HOH   N 4 .   ? -38.928 -15.756 84.404  1.00 35.03 ?  466 HOH   D O   1 
HETATM 7154 O  O   . HOH   N 4 .   ? -60.698 5.002   71.934  1.00 21.94 ?  467 HOH   D O   1 
HETATM 7155 O  O   . HOH   N 4 .   ? -39.781 -13.541 53.594  1.00 22.12 ?  468 HOH   D O   1 
HETATM 7156 O  O   . HOH   N 4 .   ? -60.231 19.854  71.232  1.00 29.70 ?  469 HOH   D O   1 
HETATM 7157 O  O   . HOH   N 4 .   ? -56.955 2.143   54.942  1.00 41.80 ?  470 HOH   D O   1 
HETATM 7158 O  O   . HOH   N 4 .   ? -41.931 -10.917 54.288  1.00 38.62 ?  471 HOH   D O   1 
HETATM 7159 O  O   . HOH   N 4 .   ? -63.078 -14.544 68.772  1.00 31.02 ?  472 HOH   D O   1 
HETATM 7160 O  O   . HOH   N 4 .   ? -36.971 -20.947 55.829  1.00 29.37 ?  473 HOH   D O   1 
HETATM 7161 O  O   . HOH   N 4 .   ? -56.045 8.118   57.805  1.00 37.57 ?  474 HOH   D O   1 
HETATM 7162 O  O   . HOH   N 4 .   ? -45.190 -7.522  64.839  1.00 25.76 ?  475 HOH   D O   1 
HETATM 7163 O  O   . HOH   N 4 .   ? -64.702 -21.638 68.501  1.00 44.47 ?  476 HOH   D O   1 
HETATM 7164 O  O   . HOH   N 4 .   ? -50.089 9.556   68.537  1.00 20.74 ?  477 HOH   D O   1 
HETATM 7165 O  O   . HOH   N 4 .   ? -67.427 12.511  70.504  1.00 31.25 ?  478 HOH   D O   1 
HETATM 7166 O  O   . HOH   N 4 .   ? -46.250 -8.736  57.757  1.00 42.55 ?  479 HOH   D O   1 
HETATM 7167 O  O   . HOH   N 4 .   ? -53.260 -1.720  60.233  1.00 29.87 ?  480 HOH   D O   1 
HETATM 7168 O  O   . HOH   N 4 .   ? -53.766 -29.064 72.054  1.00 41.25 ?  481 HOH   D O   1 
HETATM 7169 O  O   . HOH   N 4 .   ? -59.004 -14.287 77.479  1.00 21.93 ?  482 HOH   D O   1 
HETATM 7170 O  O   . HOH   N 4 .   ? -57.692 15.744  62.089  1.00 28.84 ?  483 HOH   D O   1 
HETATM 7171 O  O   . HOH   N 4 .   ? -43.034 -27.847 61.497  1.00 30.47 ?  484 HOH   D O   1 
HETATM 7172 O  O   . HOH   N 4 .   ? -43.467 1.637   58.476  1.00 40.09 ?  485 HOH   D O   1 
HETATM 7173 O  O   . HOH   N 4 .   ? -63.438 4.503   64.874  1.00 30.95 ?  486 HOH   D O   1 
HETATM 7174 O  O   . HOH   N 4 .   ? -45.250 -22.348 90.074  1.00 42.60 ?  487 HOH   D O   1 
HETATM 7175 O  O   . HOH   N 4 .   ? -64.661 -19.011 75.352  1.00 39.18 ?  488 HOH   D O   1 
HETATM 7176 O  O   . HOH   N 4 .   ? -49.872 -11.581 79.419  1.00 20.64 ?  489 HOH   D O   1 
HETATM 7177 O  O   . HOH   N 4 .   ? -70.006 -2.582  77.432  1.00 31.35 ?  490 HOH   D O   1 
HETATM 7178 O  O   . HOH   N 4 .   ? -51.467 -2.248  71.448  1.00 15.20 ?  491 HOH   D O   1 
HETATM 7179 O  O   . HOH   N 4 .   ? -45.928 -22.231 60.245  1.00 29.36 ?  492 HOH   D O   1 
HETATM 7180 O  O   . HOH   N 4 .   ? -67.066 -13.258 63.614  1.00 37.31 ?  493 HOH   D O   1 
HETATM 7181 O  O   . HOH   N 4 .   ? -53.162 4.212   57.156  1.00 38.38 ?  494 HOH   D O   1 
HETATM 7182 O  O   . HOH   N 4 .   ? -43.914 -10.580 93.703  1.00 34.97 ?  495 HOH   D O   1 
HETATM 7183 O  O   . HOH   N 4 .   ? -47.007 3.654   69.947  1.00 34.73 ?  496 HOH   D O   1 
HETATM 7184 O  O   . HOH   N 4 .   ? -35.994 -26.733 82.728  1.00 33.66 ?  497 HOH   D O   1 
HETATM 7185 O  O   . HOH   N 4 .   ? -57.323 -25.159 77.554  1.00 33.37 ?  498 HOH   D O   1 
HETATM 7186 O  O   . HOH   N 4 .   ? -68.533 22.616  75.697  1.00 38.94 ?  499 HOH   D O   1 
HETATM 7187 O  O   . HOH   N 4 .   ? -62.205 -21.086 62.033  1.00 39.03 ?  500 HOH   D O   1 
HETATM 7188 O  O   . HOH   N 4 .   ? -62.063 -23.203 66.323  1.00 46.10 ?  501 HOH   D O   1 
HETATM 7189 O  O   . HOH   N 4 .   ? -39.144 -13.814 82.243  1.00 28.25 ?  502 HOH   D O   1 
HETATM 7190 O  O   . HOH   N 4 .   ? -48.119 -8.241  74.275  1.00 21.80 ?  503 HOH   D O   1 
HETATM 7191 O  O   . HOH   N 4 .   ? -39.096 -12.128 78.267  1.00 20.13 ?  504 HOH   D O   1 
HETATM 7192 O  O   . HOH   N 4 .   ? -48.311 7.516   70.551  1.00 21.85 ?  505 HOH   D O   1 
HETATM 7193 O  O   . HOH   N 4 .   ? -45.667 -7.128  74.141  1.00 23.82 ?  506 HOH   D O   1 
HETATM 7194 O  O   . HOH   N 4 .   ? -46.408 -31.143 66.848  1.00 43.32 ?  507 HOH   D O   1 
HETATM 7195 O  O   . HOH   N 4 .   ? -61.028 -15.121 67.289  1.00 24.80 ?  508 HOH   D O   1 
HETATM 7196 O  O   . HOH   N 4 .   ? -63.430 -9.974  72.341  1.00 40.59 ?  509 HOH   D O   1 
HETATM 7197 O  O   . HOH   N 4 .   ? -45.618 4.807   56.833  1.00 35.92 ?  510 HOH   D O   1 
HETATM 7198 O  O   . HOH   N 4 .   ? -64.626 15.456  60.698  1.00 38.67 ?  511 HOH   D O   1 
HETATM 7199 O  O   . HOH   N 4 .   ? -52.155 -10.532 60.185  1.00 31.61 ?  512 HOH   D O   1 
HETATM 7200 O  O   . HOH   N 4 .   ? -49.790 -17.458 63.707  1.00 24.15 ?  513 HOH   D O   1 
HETATM 7201 O  O   . HOH   N 4 .   ? -37.977 -7.357  57.001  1.00 32.05 ?  514 HOH   D O   1 
HETATM 7202 O  O   . HOH   N 4 .   ? -28.600 -33.655 62.322  1.00 46.58 ?  515 HOH   D O   1 
HETATM 7203 O  O   . HOH   N 4 .   ? -56.629 -7.205  63.624  1.00 23.55 ?  516 HOH   D O   1 
HETATM 7204 O  O   . HOH   N 4 .   ? -43.535 9.218   59.097  1.00 45.99 ?  517 HOH   D O   1 
HETATM 7205 O  O   . HOH   N 4 .   ? -43.717 -15.619 51.931  1.00 37.24 ?  518 HOH   D O   1 
HETATM 7206 O  O   . HOH   N 4 .   ? -26.939 -26.812 59.979  1.00 29.41 ?  519 HOH   D O   1 
HETATM 7207 O  O   . HOH   N 4 .   ? -24.319 -27.242 60.427  1.00 37.10 ?  520 HOH   D O   1 
HETATM 7208 O  O   . HOH   N 4 .   ? -49.861 2.794   64.415  1.00 35.73 ?  521 HOH   D O   1 
HETATM 7209 O  O   . HOH   N 4 .   ? -63.790 -16.451 74.595  1.00 29.66 ?  522 HOH   D O   1 
HETATM 7210 O  O   . HOH   N 4 .   ? -52.486 14.026  59.201  1.00 38.67 ?  523 HOH   D O   1 
HETATM 7211 O  O   . HOH   N 4 .   ? -31.433 -18.319 52.466  1.00 28.04 ?  524 HOH   D O   1 
HETATM 7212 O  O   . HOH   N 4 .   ? -65.653 -7.491  79.404  1.00 38.76 ?  525 HOH   D O   1 
HETATM 7213 O  O   . HOH   N 4 .   ? -44.680 -9.408  67.669  1.00 21.79 ?  526 HOH   D O   1 
HETATM 7214 O  O   . HOH   N 4 .   ? -43.609 8.453   62.325  1.00 37.99 ?  527 HOH   D O   1 
HETATM 7215 O  O   . HOH   N 4 .   ? -64.370 17.993  60.713  1.00 41.63 ?  528 HOH   D O   1 
HETATM 7216 O  O   . HOH   N 4 .   ? -36.682 -29.300 81.468  1.00 24.42 ?  529 HOH   D O   1 
HETATM 7217 O  O   . HOH   N 4 .   ? -48.574 -9.671  58.850  1.00 50.95 ?  530 HOH   D O   1 
HETATM 7218 O  O   . HOH   N 4 .   ? -64.516 -13.788 61.336  1.00 31.57 ?  531 HOH   D O   1 
HETATM 7219 O  O   . HOH   N 4 .   ? -70.154 7.306   73.800  1.00 36.33 ?  532 HOH   D O   1 
HETATM 7220 O  O   . HOH   N 4 .   ? -58.122 -6.853  61.118  1.00 52.86 ?  533 HOH   D O   1 
HETATM 7221 O  O   . HOH   N 4 .   ? -43.630 -29.928 84.011  1.00 36.18 ?  534 HOH   D O   1 
HETATM 7222 O  O   . HOH   N 4 .   ? -42.549 -38.441 70.416  1.00 48.92 ?  535 HOH   D O   1 
HETATM 7223 O  O   . HOH   N 4 .   ? -70.673 13.183  64.036  1.00 38.63 ?  536 HOH   D O   1 
HETATM 7224 O  O   . HOH   N 4 .   ? -62.747 -17.111 69.274  1.00 27.61 ?  537 HOH   D O   1 
HETATM 7225 O  O   . HOH   N 4 .   ? -48.341 1.275   66.521  1.00 23.30 ?  538 HOH   D O   1 
HETATM 7226 O  O   . HOH   N 4 .   ? -62.870 13.017  75.357  1.00 23.26 ?  539 HOH   D O   1 
HETATM 7227 O  O   . HOH   N 4 .   ? -28.886 -28.720 57.609  1.00 33.62 ?  540 HOH   D O   1 
HETATM 7228 O  O   . HOH   N 4 .   ? -44.253 -17.631 52.120  1.00 43.19 ?  541 HOH   D O   1 
HETATM 7229 O  O   . HOH   N 4 .   ? -51.725 -28.769 67.592  1.00 30.61 ?  542 HOH   D O   1 
HETATM 7230 O  O   . HOH   N 4 .   ? -23.593 -26.099 67.491  1.00 49.33 ?  543 HOH   D O   1 
HETATM 7231 O  O   . HOH   N 4 .   ? -67.209 21.263  71.669  1.00 38.71 ?  544 HOH   D O   1 
HETATM 7232 O  O   . HOH   N 4 .   ? -42.397 -7.370  57.048  1.00 31.98 ?  545 HOH   D O   1 
HETATM 7233 O  O   . HOH   N 4 .   ? -39.723 -30.044 81.659  1.00 38.42 ?  546 HOH   D O   1 
HETATM 7234 O  O   . HOH   N 4 .   ? -54.539 -16.117 55.310  1.00 48.46 ?  547 HOH   D O   1 
HETATM 7235 O  O   . HOH   N 4 .   ? -45.612 0.543   70.769  1.00 37.94 ?  548 HOH   D O   1 
HETATM 7236 O  O   . HOH   N 4 .   ? -71.027 7.253   70.192  1.00 41.90 ?  549 HOH   D O   1 
HETATM 7237 O  O   . HOH   N 4 .   ? -59.487 -17.430 83.446  1.00 43.87 ?  550 HOH   D O   1 
HETATM 7238 O  O   . HOH   N 4 .   ? -42.849 -26.063 90.243  1.00 46.30 ?  551 HOH   D O   1 
HETATM 7239 O  O   . HOH   N 4 .   ? -46.039 -30.822 62.664  1.00 46.31 ?  552 HOH   D O   1 
HETATM 7240 O  O   . HOH   N 4 .   ? -26.608 -28.585 56.727  1.00 47.89 ?  553 HOH   D O   1 
HETATM 7241 O  O   . HOH   N 4 .   ? -71.437 -2.578  71.987  1.00 45.28 ?  554 HOH   D O   1 
HETATM 7242 O  O   . HOH   N 4 .   ? -39.415 -31.200 61.919  1.00 40.10 ?  555 HOH   D O   1 
HETATM 7243 O  O   . HOH   N 4 .   ? -42.756 -26.058 59.327  1.00 35.42 ?  556 HOH   D O   1 
HETATM 7244 O  O   . HOH   N 4 .   ? -66.129 3.434   64.281  1.00 37.89 ?  557 HOH   D O   1 
HETATM 7245 O  O   . HOH   N 4 .   ? -58.217 -27.048 66.065  1.00 42.44 ?  558 HOH   D O   1 
HETATM 7246 O  O   . HOH   N 4 .   ? -40.166 -17.096 53.794  1.00 37.18 ?  559 HOH   D O   1 
HETATM 7247 O  O   . HOH   N 4 .   ? -54.627 10.682  56.182  1.00 45.13 ?  560 HOH   D O   1 
HETATM 7248 O  O   . HOH   N 4 .   ? -49.705 -1.612  73.422  1.00 28.44 ?  561 HOH   D O   1 
HETATM 7249 O  O   . HOH   N 4 .   ? -69.882 18.688  74.773  1.00 38.90 ?  562 HOH   D O   1 
HETATM 7250 O  O   . HOH   N 4 .   ? -36.232 -31.669 72.296  1.00 41.07 ?  563 HOH   D O   1 
HETATM 7251 O  O   . HOH   N 4 .   ? -54.299 -7.139  62.768  1.00 35.59 ?  564 HOH   D O   1 
HETATM 7252 O  O   . HOH   N 4 .   ? -54.960 16.101  61.727  1.00 39.67 ?  565 HOH   D O   1 
HETATM 7253 O  O   . HOH   N 4 .   ? -33.053 -21.884 86.826  1.00 42.49 ?  566 HOH   D O   1 
HETATM 7254 O  O   . HOH   N 4 .   ? -58.569 -24.410 79.926  1.00 39.77 ?  567 HOH   D O   1 
HETATM 7255 O  O   . HOH   N 4 .   ? -40.763 -23.515 90.167  1.00 37.15 ?  568 HOH   D O   1 
HETATM 7256 O  O   . HOH   N 4 .   ? -62.518 -11.556 86.055  1.00 43.68 ?  569 HOH   D O   1 
HETATM 7257 O  O   . HOH   N 4 .   ? -59.632 16.427  60.048  1.00 39.76 ?  570 HOH   D O   1 
HETATM 7258 O  O   . HOH   N 4 .   ? -41.521 -30.131 61.004  1.00 42.87 ?  571 HOH   D O   1 
HETATM 7259 O  O   . HOH   N 4 .   ? -35.116 -13.055 75.363  1.00 31.77 ?  572 HOH   D O   1 
HETATM 7260 O  O   . HOH   N 4 .   ? -47.053 -37.681 69.808  1.00 52.68 ?  573 HOH   D O   1 
HETATM 7261 O  O   . HOH   N 4 .   ? -57.470 -27.742 77.467  1.00 48.59 ?  574 HOH   D O   1 
HETATM 7262 O  O   . HOH   N 4 .   ? -50.437 -7.063  60.893  1.00 41.02 ?  575 HOH   D O   1 
HETATM 7263 O  O   . HOH   N 4 .   ? -28.731 -19.126 53.275  1.00 45.41 ?  576 HOH   D O   1 
HETATM 7264 O  O   . HOH   N 4 .   ? -64.654 8.732   76.706  1.00 37.69 ?  577 HOH   D O   1 
HETATM 7265 O  O   . HOH   N 4 .   ? -47.322 -2.461  73.367  1.00 29.21 ?  578 HOH   D O   1 
HETATM 7266 O  O   . HOH   N 4 .   ? -69.982 0.213   77.416  1.00 38.87 ?  579 HOH   D O   1 
HETATM 7267 O  O   . HOH   N 4 .   ? -59.563 -21.036 85.064  1.00 42.24 ?  580 HOH   D O   1 
HETATM 7268 O  O   . HOH   N 4 .   ? -41.694 -5.879  58.740  1.00 30.80 ?  581 HOH   D O   1 
HETATM 7269 O  O   . HOH   N 4 .   ? -52.396 -3.852  61.644  1.00 45.15 ?  582 HOH   D O   1 
HETATM 7270 O  O   . HOH   N 4 .   ? -50.383 11.389  66.315  1.00 27.51 ?  583 HOH   D O   1 
HETATM 7271 O  O   . HOH   N 4 .   ? -32.461 -17.545 86.388  1.00 33.19 ?  584 HOH   D O   1 
HETATM 7272 O  O   . HOH   N 4 .   ? -29.195 -19.528 84.429  1.00 43.14 ?  585 HOH   D O   1 
HETATM 7273 O  O   . HOH   N 4 .   ? -42.681 -22.973 91.521  1.00 46.04 ?  586 HOH   D O   1 
HETATM 7274 O  O   . HOH   N 4 .   ? -43.187 -6.482  63.351  1.00 27.57 ?  587 HOH   D O   1 
HETATM 7275 O  O   . HOH   N 4 .   ? -59.792 -23.804 62.951  1.00 42.49 ?  588 HOH   D O   1 
HETATM 7276 O  O   . HOH   N 4 .   ? -43.711 -5.942  60.177  1.00 33.99 ?  589 HOH   D O   1 
HETATM 7277 O  O   . HOH   N 4 .   ? -43.341 -1.830  56.405  1.00 36.94 ?  590 HOH   D O   1 
HETATM 7278 O  O   . HOH   O 4 .   ? -44.180 18.132  95.562  1.00 41.96 ?  401 HOH   A O   1 
HETATM 7279 O  O   . HOH   O 4 .   ? -51.378 24.534  73.225  1.00 38.49 ?  402 HOH   A O   1 
HETATM 7280 O  O   . HOH   O 4 .   ? -45.562 -0.769  74.575  1.00 26.21 ?  403 HOH   A O   1 
HETATM 7281 O  O   . HOH   O 4 .   ? -33.098 9.927   79.555  1.00 42.16 ?  404 HOH   A O   1 
HETATM 7282 O  O   . HOH   O 4 .   ? -63.628 11.203  77.849  1.00 37.33 ?  405 HOH   A O   1 
HETATM 7283 O  O   . HOH   O 4 .   ? -46.615 0.312   96.705  1.00 40.31 ?  406 HOH   A O   1 
HETATM 7284 O  O   . HOH   O 4 .   ? -23.415 0.245   69.139  1.00 41.10 ?  407 HOH   A O   1 
HETATM 7285 O  O   . HOH   O 4 .   ? -52.611 13.398  95.315  1.00 33.71 ?  408 HOH   A O   1 
HETATM 7286 O  O   . HOH   O 4 .   ? -41.740 6.940   63.050  1.00 39.65 ?  409 HOH   A O   1 
HETATM 7287 O  O   . HOH   O 4 .   ? -29.882 -14.983 68.429  1.00 36.14 ?  410 HOH   A O   1 
HETATM 7288 O  O   . HOH   O 4 .   ? -37.962 7.765   77.021  1.00 32.98 ?  411 HOH   A O   1 
HETATM 7289 O  O   . HOH   O 4 .   ? -55.421 27.852  79.878  1.00 30.26 ?  412 HOH   A O   1 
HETATM 7290 O  O   . HOH   O 4 .   ? -50.231 -1.761  76.182  1.00 40.49 ?  413 HOH   A O   1 
HETATM 7291 O  O   . HOH   O 4 .   ? -22.532 -13.883 65.193  1.00 34.19 ?  414 HOH   A O   1 
HETATM 7292 O  O   . HOH   O 4 .   ? -43.340 16.391  87.234  1.00 34.72 ?  415 HOH   A O   1 
HETATM 7293 O  O   . HOH   O 4 .   ? -57.734 -15.024 84.174  1.00 28.03 ?  416 HOH   A O   1 
HETATM 7294 O  O   . HOH   O 4 .   ? -36.219 -9.342  90.103  1.00 44.02 ?  417 HOH   A O   1 
HETATM 7295 O  O   . HOH   O 4 .   ? -59.064 -0.039  98.853  1.00 39.89 ?  418 HOH   A O   1 
HETATM 7296 O  O   . HOH   O 4 .   ? -65.967 8.226   81.020  1.00 46.78 ?  419 HOH   A O   1 
HETATM 7297 O  O   . HOH   O 4 .   ? -55.260 -10.322 91.187  1.00 34.05 ?  420 HOH   A O   1 
HETATM 7298 O  O   . HOH   O 4 .   ? -34.366 4.295   69.757  1.00 27.36 ?  421 HOH   A O   1 
HETATM 7299 O  O   . HOH   O 4 .   ? -28.952 -11.669 52.636  1.00 39.39 ?  422 HOH   A O   1 
HETATM 7300 O  O   . HOH   O 4 .   ? -62.393 7.243   91.813  1.00 27.64 ?  423 HOH   A O   1 
HETATM 7301 O  O   . HOH   O 4 .   ? -56.150 6.666   99.113  1.00 48.73 ?  424 HOH   A O   1 
HETATM 7302 O  O   . HOH   O 4 .   ? -50.401 21.090  76.222  1.00 30.73 ?  425 HOH   A O   1 
HETATM 7303 O  O   . HOH   O 4 .   ? -26.490 -4.791  76.673  1.00 39.12 ?  426 HOH   A O   1 
HETATM 7304 O  O   . HOH   O 4 .   ? -36.499 -3.906  96.827  1.00 41.07 ?  427 HOH   A O   1 
HETATM 7305 O  O   . HOH   O 4 .   ? -66.724 7.722   85.456  1.00 28.17 ?  428 HOH   A O   1 
HETATM 7306 O  O   . HOH   O 4 .   ? -30.047 -15.313 65.672  1.00 24.38 ?  429 HOH   A O   1 
HETATM 7307 O  O   . HOH   O 4 .   ? -55.849 1.619   99.620  1.00 44.26 ?  430 HOH   A O   1 
HETATM 7308 O  O   . HOH   O 4 .   ? -50.494 -11.285 92.181  1.00 28.28 ?  431 HOH   A O   1 
HETATM 7309 O  O   . HOH   O 4 .   ? -58.904 5.902   92.870  1.00 24.51 ?  432 HOH   A O   1 
HETATM 7310 O  O   . HOH   O 4 .   ? -54.609 -1.169  98.343  1.00 37.04 ?  433 HOH   A O   1 
HETATM 7311 O  O   . HOH   O 4 .   ? -47.247 -7.741  82.683  1.00 20.75 ?  434 HOH   A O   1 
HETATM 7312 O  O   . HOH   O 4 .   ? -48.140 18.585  73.653  1.00 25.33 ?  435 HOH   A O   1 
HETATM 7313 O  O   . HOH   O 4 .   ? -34.554 6.863   91.369  1.00 36.92 ?  436 HOH   A O   1 
HETATM 7314 O  O   . HOH   O 4 .   ? -26.914 -4.870  56.773  1.00 22.01 ?  437 HOH   A O   1 
HETATM 7315 O  O   . HOH   O 4 .   ? -57.453 -1.148  79.151  1.00 16.66 ?  438 HOH   A O   1 
HETATM 7316 O  O   . HOH   O 4 .   ? -43.857 -2.295  96.657  1.00 30.61 ?  439 HOH   A O   1 
HETATM 7317 O  O   . HOH   O 4 .   ? -45.485 12.131  94.993  1.00 33.34 ?  440 HOH   A O   1 
HETATM 7318 O  O   . HOH   O 4 .   ? -60.028 -7.784  83.792  1.00 33.31 ?  441 HOH   A O   1 
HETATM 7319 O  O   . HOH   O 4 .   ? -44.523 8.939   79.842  1.00 25.22 ?  442 HOH   A O   1 
HETATM 7320 O  O   . HOH   O 4 .   ? -27.672 -15.598 55.991  1.00 28.84 ?  443 HOH   A O   1 
HETATM 7321 O  O   . HOH   O 4 .   ? -39.236 -7.328  87.949  1.00 24.73 ?  444 HOH   A O   1 
HETATM 7322 O  O   . HOH   O 4 .   ? -36.257 3.287   53.481  1.00 29.80 ?  445 HOH   A O   1 
HETATM 7323 O  O   . HOH   O 4 .   ? -63.959 -4.301  89.833  1.00 33.15 ?  446 HOH   A O   1 
HETATM 7324 O  O   . HOH   O 4 .   ? -38.412 3.997   72.623  1.00 36.93 ?  447 HOH   A O   1 
HETATM 7325 O  O   . HOH   O 4 .   ? -35.058 10.037  84.112  1.00 37.62 ?  448 HOH   A O   1 
HETATM 7326 O  O   . HOH   O 4 .   ? -43.980 11.789  85.352  1.00 31.05 ?  449 HOH   A O   1 
HETATM 7327 O  O   . HOH   O 4 .   ? -36.380 -16.798 89.949  1.00 43.12 ?  450 HOH   A O   1 
HETATM 7328 O  O   . HOH   O 4 .   ? -31.372 -4.338  81.990  1.00 33.41 ?  451 HOH   A O   1 
HETATM 7329 O  O   . HOH   O 4 .   ? -38.788 2.997   64.648  1.00 21.05 ?  452 HOH   A O   1 
HETATM 7330 O  O   . HOH   O 4 .   ? -63.062 -9.409  90.245  1.00 34.64 ?  453 HOH   A O   1 
HETATM 7331 O  O   . HOH   O 4 .   ? -41.343 8.332   94.031  1.00 29.72 ?  454 HOH   A O   1 
HETATM 7332 O  O   . HOH   O 4 .   ? -52.556 7.140   85.042  1.00 19.51 ?  455 HOH   A O   1 
HETATM 7333 O  O   . HOH   O 4 .   ? -31.071 5.483   59.755  1.00 26.72 ?  456 HOH   A O   1 
HETATM 7334 O  O   . HOH   O 4 .   ? -42.165 0.325   64.600  1.00 42.00 ?  457 HOH   A O   1 
HETATM 7335 O  O   . HOH   O 4 .   ? -42.235 -4.781  65.552  1.00 34.75 ?  458 HOH   A O   1 
HETATM 7336 O  O   . HOH   O 4 .   ? -40.152 -2.705  64.138  1.00 33.51 ?  459 HOH   A O   1 
HETATM 7337 O  O   . HOH   O 4 .   ? -50.850 11.250  95.449  1.00 38.92 ?  460 HOH   A O   1 
HETATM 7338 O  O   . HOH   O 4 .   ? -46.893 -10.872 99.808  1.00 43.69 ?  461 HOH   A O   1 
HETATM 7339 O  O   . HOH   O 4 .   ? -55.664 -5.819  76.973  1.00 40.23 ?  462 HOH   A O   1 
HETATM 7340 O  O   . HOH   O 4 .   ? -29.474 -11.077 66.717  1.00 26.04 ?  463 HOH   A O   1 
HETATM 7341 O  O   . HOH   O 4 .   ? -26.869 -7.567  55.616  1.00 23.78 ?  464 HOH   A O   1 
HETATM 7342 O  O   . HOH   O 4 .   ? -57.772 -11.792 93.605  1.00 44.18 ?  465 HOH   A O   1 
HETATM 7343 O  O   . HOH   O 4 .   ? -56.298 16.872  93.247  1.00 33.09 ?  466 HOH   A O   1 
HETATM 7344 O  O   . HOH   O 4 .   ? -20.327 -5.586  59.334  1.00 36.49 ?  467 HOH   A O   1 
HETATM 7345 O  O   . HOH   O 4 .   ? -32.355 -5.498  84.383  1.00 44.08 ?  468 HOH   A O   1 
HETATM 7346 O  O   . HOH   O 4 .   ? -47.044 15.013  85.473  1.00 27.81 ?  469 HOH   A O   1 
HETATM 7347 O  O   . HOH   O 4 .   ? -46.388 14.522  69.513  1.00 40.18 ?  470 HOH   A O   1 
HETATM 7348 O  O   . HOH   O 4 .   ? -40.575 -4.714  72.873  1.00 17.09 ?  471 HOH   A O   1 
HETATM 7349 O  O   . HOH   O 4 .   ? -61.406 8.427   94.091  1.00 45.81 ?  472 HOH   A O   1 
HETATM 7350 O  O   . HOH   O 4 .   ? -25.660 -5.051  69.273  1.00 33.05 ?  473 HOH   A O   1 
HETATM 7351 O  O   . HOH   O 4 .   ? -41.437 -13.987 88.652  1.00 37.47 ?  474 HOH   A O   1 
HETATM 7352 O  O   . HOH   O 4 .   ? -33.403 -7.062  89.376  1.00 45.49 ?  475 HOH   A O   1 
HETATM 7353 O  O   . HOH   O 4 .   ? -45.667 -0.343  77.392  1.00 17.15 ?  476 HOH   A O   1 
HETATM 7354 O  O   . HOH   O 4 .   ? -45.334 4.756   73.494  1.00 24.94 ?  477 HOH   A O   1 
HETATM 7355 O  O   . HOH   O 4 .   ? -32.235 8.106   90.445  1.00 41.23 ?  478 HOH   A O   1 
HETATM 7356 O  O   . HOH   O 4 .   ? -32.382 -0.562  87.125  1.00 36.60 ?  479 HOH   A O   1 
HETATM 7357 O  O   . HOH   O 4 .   ? -34.050 -6.591  58.200  1.00 23.54 ?  480 HOH   A O   1 
HETATM 7358 O  O   . HOH   O 4 .   ? -41.470 6.775   72.975  1.00 29.19 ?  481 HOH   A O   1 
HETATM 7359 O  O   . HOH   O 4 .   ? -36.054 9.118   81.512  1.00 39.83 ?  482 HOH   A O   1 
HETATM 7360 O  O   . HOH   O 4 .   ? -57.836 -19.185 83.627  1.00 36.14 ?  483 HOH   A O   1 
HETATM 7361 O  O   . HOH   O 4 .   ? -27.945 -19.043 56.887  1.00 33.59 ?  484 HOH   A O   1 
HETATM 7362 O  O   . HOH   O 4 .   ? -66.098 20.570  89.352  1.00 28.65 ?  485 HOH   A O   1 
HETATM 7363 O  O   . HOH   O 4 .   ? -28.705 1.967   57.118  1.00 27.04 ?  486 HOH   A O   1 
HETATM 7364 O  O   . HOH   O 4 .   ? -64.742 23.693  78.396  1.00 36.41 ?  487 HOH   A O   1 
HETATM 7365 O  O   . HOH   O 4 .   ? -76.173 15.437  88.082  1.00 32.43 ?  488 HOH   A O   1 
HETATM 7366 O  O   . HOH   O 4 .   ? -62.141 0.126   95.697  1.00 39.19 ?  489 HOH   A O   1 
HETATM 7367 O  O   . HOH   O 4 .   ? -58.545 -6.720  81.499  1.00 31.01 ?  490 HOH   A O   1 
HETATM 7368 O  O   . HOH   O 4 .   ? -28.199 4.986   84.851  1.00 33.93 ?  491 HOH   A O   1 
HETATM 7369 O  O   . HOH   O 4 .   ? -32.603 4.793   76.566  1.00 40.75 ?  492 HOH   A O   1 
HETATM 7370 O  O   . HOH   O 4 .   ? -61.373 -0.865  79.266  1.00 35.21 ?  493 HOH   A O   1 
HETATM 7371 O  O   . HOH   O 4 .   ? -37.495 -13.909 79.805  1.00 27.39 ?  494 HOH   A O   1 
HETATM 7372 O  O   . HOH   O 4 .   ? -37.851 -6.428  61.070  1.00 19.34 ?  495 HOH   A O   1 
HETATM 7373 O  O   . HOH   O 4 .   ? -41.674 11.930  95.954  1.00 38.09 ?  496 HOH   A O   1 
HETATM 7374 O  O   . HOH   O 4 .   ? -34.029 0.749   52.737  1.00 22.46 ?  497 HOH   A O   1 
HETATM 7375 O  O   . HOH   O 4 .   ? -47.942 10.288  69.791  1.00 27.60 ?  498 HOH   A O   1 
HETATM 7376 O  O   . HOH   O 4 .   ? -62.702 1.069   80.383  1.00 34.04 ?  499 HOH   A O   1 
HETATM 7377 O  O   . HOH   O 4 .   ? -48.425 -9.189  80.346  1.00 19.03 ?  500 HOH   A O   1 
HETATM 7378 O  O   . HOH   O 4 .   ? -44.508 6.658   81.730  1.00 18.53 ?  501 HOH   A O   1 
HETATM 7379 O  O   . HOH   O 4 .   ? -59.877 21.466  77.959  1.00 24.69 ?  502 HOH   A O   1 
HETATM 7380 O  O   . HOH   O 4 .   ? -30.713 -10.599 69.881  1.00 20.68 ?  503 HOH   A O   1 
HETATM 7381 O  O   . HOH   O 4 .   ? -32.275 -13.283 84.927  1.00 40.32 ?  504 HOH   A O   1 
HETATM 7382 O  O   . HOH   O 4 .   ? -43.209 8.473   83.362  1.00 24.16 ?  505 HOH   A O   1 
HETATM 7383 O  O   . HOH   O 4 .   ? -29.197 6.419   68.658  1.00 35.70 ?  506 HOH   A O   1 
HETATM 7384 O  O   . HOH   O 4 .   ? -34.648 5.313   93.715  1.00 43.04 ?  507 HOH   A O   1 
HETATM 7385 O  O   . HOH   O 4 .   ? -21.877 -7.612  72.457  1.00 45.28 ?  508 HOH   A O   1 
HETATM 7386 O  O   . HOH   O 4 .   ? -45.326 2.106   72.653  1.00 37.52 ?  509 HOH   A O   1 
HETATM 7387 O  O   . HOH   O 4 .   ? -52.820 19.902  79.175  1.00 33.87 ?  510 HOH   A O   1 
HETATM 7388 O  O   . HOH   O 4 .   ? -34.392 2.764   76.840  1.00 26.46 ?  511 HOH   A O   1 
HETATM 7389 O  O   . HOH   O 4 .   ? -46.123 -4.263  77.725  1.00 20.07 ?  512 HOH   A O   1 
HETATM 7390 O  O   . HOH   O 4 .   ? -25.710 -16.248 64.092  1.00 34.17 ?  513 HOH   A O   1 
HETATM 7391 O  O   . HOH   O 4 .   ? -48.300 8.818   96.145  1.00 39.17 ?  514 HOH   A O   1 
HETATM 7392 O  O   . HOH   O 4 .   ? -62.349 11.310  98.701  1.00 37.12 ?  515 HOH   A O   1 
HETATM 7393 O  O   . HOH   O 4 .   ? -57.212 18.812  94.834  1.00 37.20 ?  516 HOH   A O   1 
HETATM 7394 O  O   . HOH   O 4 .   ? -63.570 22.995  83.761  1.00 32.87 ?  517 HOH   A O   1 
HETATM 7395 O  O   . HOH   O 4 .   ? -64.614 14.705  91.984  1.00 37.91 ?  518 HOH   A O   1 
HETATM 7396 O  O   . HOH   O 4 .   ? -34.849 -8.703  59.800  1.00 21.29 ?  519 HOH   A O   1 
HETATM 7397 O  O   . HOH   O 4 .   ? -30.724 5.575   74.760  1.00 37.51 ?  520 HOH   A O   1 
HETATM 7398 O  O   . HOH   O 4 .   ? -28.643 2.186   61.694  1.00 29.93 ?  521 HOH   A O   1 
HETATM 7399 O  O   . HOH   O 4 .   ? -41.142 -12.822 84.697  1.00 25.69 ?  522 HOH   A O   1 
HETATM 7400 O  O   . HOH   O 4 .   ? -40.900 1.460   57.784  1.00 22.52 ?  523 HOH   A O   1 
HETATM 7401 O  O   . HOH   O 4 .   ? -52.696 -23.000 86.929  1.00 37.15 ?  524 HOH   A O   1 
HETATM 7402 O  O   . HOH   O 4 .   ? -33.847 1.552   86.527  1.00 26.07 ?  525 HOH   A O   1 
HETATM 7403 O  O   . HOH   O 4 .   ? -36.442 -2.853  58.364  1.00 23.82 ?  526 HOH   A O   1 
HETATM 7404 O  O   . HOH   O 4 .   ? -69.297 9.710   87.090  1.00 36.00 ?  527 HOH   A O   1 
HETATM 7405 O  O   . HOH   O 4 .   ? -40.395 -1.003  67.315  1.00 27.60 ?  528 HOH   A O   1 
HETATM 7406 O  O   . HOH   O 4 .   ? -56.233 23.086  73.849  1.00 27.13 ?  529 HOH   A O   1 
HETATM 7407 O  O   . HOH   O 4 .   ? -34.455 -4.955  90.877  1.00 27.66 ?  530 HOH   A O   1 
HETATM 7408 O  O   . HOH   O 4 .   ? -43.821 -7.143  69.361  1.00 38.12 ?  531 HOH   A O   1 
HETATM 7409 O  O   . HOH   O 4 .   ? -58.642 24.531  77.894  1.00 37.81 ?  532 HOH   A O   1 
HETATM 7410 O  O   . HOH   O 4 .   ? -66.705 3.083   84.954  1.00 31.19 ?  533 HOH   A O   1 
HETATM 7411 O  O   . HOH   O 4 .   ? -50.633 13.770  69.297  1.00 27.28 ?  534 HOH   A O   1 
HETATM 7412 O  O   . HOH   O 4 .   ? -56.802 -3.915  78.862  1.00 18.87 ?  535 HOH   A O   1 
HETATM 7413 O  O   . HOH   O 4 .   ? -27.395 2.868   59.530  1.00 38.18 ?  536 HOH   A O   1 
HETATM 7414 O  O   . HOH   O 4 .   ? -45.985 8.898   95.099  1.00 37.01 ?  537 HOH   A O   1 
HETATM 7415 O  O   . HOH   O 4 .   ? -47.153 3.000   75.444  1.00 27.30 ?  538 HOH   A O   1 
HETATM 7416 O  O   . HOH   O 4 .   ? -26.253 2.412   85.876  1.00 45.40 ?  539 HOH   A O   1 
HETATM 7417 O  O   . HOH   O 4 .   ? -27.338 3.159   63.641  1.00 40.72 ?  540 HOH   A O   1 
HETATM 7418 O  O   . HOH   O 4 .   ? -43.690 11.378  80.239  1.00 35.25 ?  541 HOH   A O   1 
HETATM 7419 O  O   . HOH   O 4 .   ? -47.981 -3.772  75.726  1.00 27.12 ?  542 HOH   A O   1 
HETATM 7420 O  O   . HOH   O 4 .   ? -64.744 0.577   93.580  1.00 37.71 ?  543 HOH   A O   1 
HETATM 7421 O  O   . HOH   O 4 .   ? -21.143 -18.120 57.142  1.00 37.34 ?  544 HOH   A O   1 
HETATM 7422 O  O   . HOH   O 4 .   ? -42.933 10.980  82.700  1.00 29.96 ?  545 HOH   A O   1 
HETATM 7423 O  O   . HOH   O 4 .   ? -44.728 -7.806  93.182  1.00 34.12 ?  546 HOH   A O   1 
HETATM 7424 O  O   . HOH   O 4 .   ? -38.039 0.256   65.883  1.00 26.45 ?  547 HOH   A O   1 
HETATM 7425 O  O   . HOH   O 4 .   ? -16.851 -9.502  63.911  1.00 38.09 ?  548 HOH   A O   1 
HETATM 7426 O  O   . HOH   O 4 .   ? -24.825 -4.648  79.769  1.00 46.91 ?  549 HOH   A O   1 
HETATM 7427 O  O   . HOH   O 4 .   ? -26.651 -15.341 80.877  1.00 43.61 ?  550 HOH   A O   1 
HETATM 7428 O  O   . HOH   O 4 .   ? -52.578 22.426  80.194  1.00 41.52 ?  551 HOH   A O   1 
HETATM 7429 O  O   . HOH   O 4 .   ? -40.782 -7.051  62.850  1.00 19.52 ?  552 HOH   A O   1 
HETATM 7430 O  O   . HOH   O 4 .   ? -41.530 14.492  73.002  1.00 45.23 ?  553 HOH   A O   1 
HETATM 7431 O  O   . HOH   O 4 .   ? -69.716 13.081  89.891  1.00 41.41 ?  554 HOH   A O   1 
HETATM 7432 O  O   . HOH   O 4 .   ? -33.466 0.208   89.473  1.00 33.24 ?  555 HOH   A O   1 
HETATM 7433 O  O   . HOH   O 4 .   ? -34.603 -1.935  55.800  1.00 34.16 ?  556 HOH   A O   1 
HETATM 7434 O  O   . HOH   O 4 .   ? -28.168 -17.299 64.644  1.00 22.98 ?  557 HOH   A O   1 
HETATM 7435 O  O   . HOH   O 4 .   ? -23.131 -2.344  65.908  1.00 36.76 ?  558 HOH   A O   1 
HETATM 7436 O  O   . HOH   O 4 .   ? -48.133 16.205  67.466  1.00 45.68 ?  559 HOH   A O   1 
HETATM 7437 O  O   . HOH   O 4 .   ? -28.562 -1.709  84.025  1.00 47.41 ?  560 HOH   A O   1 
HETATM 7438 O  O   . HOH   O 4 .   ? -62.444 16.177  92.750  1.00 36.06 ?  561 HOH   A O   1 
HETATM 7439 O  O   . HOH   O 4 .   ? -67.376 1.755   83.020  1.00 36.77 ?  562 HOH   A O   1 
HETATM 7440 O  O   . HOH   O 4 .   ? -61.351 7.476   95.995  1.00 46.83 ?  563 HOH   A O   1 
HETATM 7441 O  O   . HOH   O 4 .   ? -28.384 -2.946  55.479  1.00 25.48 ?  564 HOH   A O   1 
HETATM 7442 O  O   . HOH   O 4 .   ? -40.944 9.895   74.397  1.00 41.95 ?  565 HOH   A O   1 
HETATM 7443 O  O   . HOH   O 4 .   ? -38.273 5.807   64.801  1.00 33.58 ?  566 HOH   A O   1 
HETATM 7444 O  O   . HOH   O 4 .   ? -25.414 -16.794 67.780  1.00 45.86 ?  567 HOH   A O   1 
HETATM 7445 O  O   . HOH   O 4 .   ? -32.453 -7.616  84.363  1.00 51.11 ?  568 HOH   A O   1 
HETATM 7446 O  O   . HOH   O 4 .   ? -21.907 3.663   61.788  1.00 47.14 ?  569 HOH   A O   1 
HETATM 7447 O  O   . HOH   O 4 .   ? -58.117 19.921  84.582  1.00 41.44 ?  570 HOH   A O   1 
HETATM 7448 O  O   . HOH   O 4 .   ? -34.270 -17.124 89.716  1.00 41.09 ?  571 HOH   A O   1 
HETATM 7449 O  O   . HOH   O 4 .   ? -42.656 -6.503  72.073  1.00 29.55 ?  572 HOH   A O   1 
HETATM 7450 O  O   . HOH   O 4 .   ? -28.302 6.389   79.806  1.00 39.57 ?  573 HOH   A O   1 
HETATM 7451 O  O   . HOH   O 4 .   ? -56.919 21.378  85.892  1.00 40.30 ?  574 HOH   A O   1 
HETATM 7452 O  O   . HOH   O 4 .   ? -67.888 16.781  90.408  1.00 35.10 ?  575 HOH   A O   1 
HETATM 7453 O  O   . HOH   O 4 .   ? -23.494 -4.729  71.276  1.00 38.84 ?  576 HOH   A O   1 
HETATM 7454 O  O   . HOH   O 4 .   ? -41.892 -11.637 92.520  1.00 37.58 ?  577 HOH   A O   1 
HETATM 7455 O  O   . HOH   O 4 .   ? -27.877 -16.858 68.549  1.00 36.48 ?  578 HOH   A O   1 
HETATM 7456 O  O   . HOH   O 4 .   ? -62.484 -10.395 92.785  1.00 41.69 ?  579 HOH   A O   1 
HETATM 7457 O  O   . HOH   O 4 .   ? -36.201 3.856   75.504  1.00 43.92 ?  580 HOH   A O   1 
HETATM 7458 O  O   . HOH   O 4 .   ? -33.747 -15.342 86.314  1.00 35.72 ?  581 HOH   A O   1 
HETATM 7459 O  O   . HOH   O 4 .   ? -32.259 -3.767  90.321  1.00 43.03 ?  582 HOH   A O   1 
HETATM 7460 O  O   . HOH   O 4 .   ? -42.914 0.513   70.113  1.00 39.05 ?  583 HOH   A O   1 
HETATM 7461 O  O   . HOH   O 4 .   ? -59.328 0.147   77.420  1.00 29.84 ?  584 HOH   A O   1 
HETATM 7462 O  O   . HOH   O 4 .   ? -24.286 -3.891  56.480  1.00 38.93 ?  585 HOH   A O   1 
HETATM 7463 O  O   . HOH   O 4 .   ? -60.690 22.808  75.923  1.00 44.97 ?  586 HOH   A O   1 
HETATM 7464 O  O   . HOH   O 4 .   ? -47.162 2.973   97.151  1.00 47.35 ?  587 HOH   A O   1 
HETATM 7465 O  O   . HOH   O 4 .   ? -48.233 12.964  67.028  1.00 45.66 ?  588 HOH   A O   1 
HETATM 7466 O  O   . HOH   O 4 .   ? -36.345 -0.373  52.000  1.00 25.58 ?  589 HOH   A O   1 
HETATM 7467 O  O   . HOH   O 4 .   ? -45.592 -2.206  69.400  1.00 41.46 ?  590 HOH   A O   1 
HETATM 7468 O  O   . HOH   O 4 .   ? -40.878 2.617   66.263  1.00 40.68 ?  591 HOH   A O   1 
HETATM 7469 O  O   . HOH   O 4 .   ? -62.751 -11.658 88.642  1.00 41.94 ?  592 HOH   A O   1 
HETATM 7470 O  O   . HOH   O 4 .   ? -49.451 4.215   98.455  1.00 42.12 ?  593 HOH   A O   1 
HETATM 7471 O  O   . HOH   O 4 .   ? -68.074 8.666   80.603  1.00 40.18 ?  594 HOH   A O   1 
HETATM 7472 O  O   . HOH   O 4 .   ? -28.284 -15.468 53.564  1.00 35.55 ?  595 HOH   A O   1 
HETATM 7473 O  O   . HOH   O 4 .   ? -43.207 -11.376 96.176  1.00 45.53 ?  596 HOH   A O   1 
HETATM 7474 O  O   . HOH   O 4 .   ? -30.353 4.368   62.078  1.00 34.02 ?  597 HOH   A O   1 
HETATM 7475 O  O   . HOH   O 4 .   ? -65.445 -8.488  90.550  1.00 48.18 ?  598 HOH   A O   1 
HETATM 7476 O  O   . HOH   O 4 .   ? -30.910 -15.601 53.020  1.00 26.58 ?  599 HOH   A O   1 
HETATM 7477 O  O   . HOH   O 4 .   ? -45.343 -5.220  72.142  1.00 32.04 ?  600 HOH   A O   1 
HETATM 7478 O  O   . HOH   O 4 .   ? -22.951 -2.896  79.203  1.00 42.00 ?  601 HOH   A O   1 
HETATM 7479 O  O   . HOH   O 4 .   ? -56.056 21.993  71.428  1.00 36.45 ?  602 HOH   A O   1 
HETATM 7480 O  O   . HOH   O 4 .   ? -40.145 -4.463  62.184  1.00 37.79 ?  603 HOH   A O   1 
HETATM 7481 O  O   . HOH   O 4 .   ? -64.976 26.524  79.514  1.00 36.97 ?  604 HOH   A O   1 
HETATM 7482 O  O   . HOH   O 4 .   ? -39.309 -2.906  58.081  1.00 32.35 ?  605 HOH   A O   1 
HETATM 7483 O  O   . HOH   O 4 .   ? -43.495 14.963  82.683  1.00 45.51 ?  606 HOH   A O   1 
HETATM 7484 O  O   . HOH   O 4 .   ? -44.592 14.415  85.216  1.00 34.66 ?  607 HOH   A O   1 
HETATM 7485 O  O   . HOH   O 4 .   ? -41.034 9.645   72.134  1.00 38.18 ?  608 HOH   A O   1 
HETATM 7486 O  O   . HOH   O 4 .   ? -47.279 23.152  73.039  1.00 46.63 ?  609 HOH   A O   1 
HETATM 7487 O  O   . HOH   O 4 .   ? -46.010 6.258   71.166  1.00 27.25 ?  610 HOH   A O   1 
HETATM 7488 O  O   . HOH   O 4 .   ? -38.752 6.494   67.319  1.00 49.84 ?  611 HOH   A O   1 
HETATM 7489 O  O   . HOH   O 4 .   ? -40.913 -1.204  56.691  1.00 26.74 ?  612 HOH   A O   1 
HETATM 7490 O  O   . HOH   O 4 .   ? -61.644 27.411  77.192  1.00 44.92 ?  613 HOH   A O   1 
HETATM 7491 O  O   . HOH   O 4 .   ? -28.553 7.003   62.371  1.00 49.01 ?  614 HOH   A O   1 
HETATM 7492 O  O   . HOH   O 4 .   ? -40.807 -3.889  59.817  1.00 27.69 ?  615 HOH   A O   1 
HETATM 7493 O  O   . HOH   O 4 .   ? -56.293 26.166  70.193  1.00 49.71 ?  616 HOH   A O   1 
# 
