data_9NF3
# 
_entry.id   9NF3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9NF3         pdb_00009nf3 10.2210/pdb9nf3/pdb 
WWPDB D_1000293273 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-05-14 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Structure summary' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            struct 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    2 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_struct.title' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9NF3 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 geiger@chemistry.msu.edu James Geiger H 'principal investigator/group leader' 0000-0002-9443-4488 
3 draths@chemistry.msu.edu Karen Draths ? 'principal investigator/group leader' 0000-0001-7852-1090 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Silva, K.'    1 ? 
'Geiger, J.H.' 2 ? 
'Draths, K.'   3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'cis-CaaD E114D mutant with a covalent ethylene intermediate of the hydration and decarboxylation of acetylenecarboxylic acid' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Silva, K.'    1 ? 
primary 'Geiger, J.H.' 2 ? 
primary 'Draths, K.'   3 ? 
# 
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 'Cis-3-chloroacrylic acid dehalogenase' 18553.557 2   ? E114D ? ? 
2 polymer     man 'Cis-3-chloroacrylic acid dehalogenase' 18579.594 1   ? E114D ? ? 
3 non-polymer syn 'SULFATE ION'                           96.063    3   ? ?     ? ? 
4 water       nat water                                   18.015    406 ? ?     ? ? 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVDYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEHH
HHHH
;
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVDYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEHH
HHHH
;
B,A ? 
2 'polypeptide(L)' no yes 
;(N80)VYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSAD
LKGQLAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVDYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQG
LEHHHHHH
;
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVDYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRTENLYFQGLEHH
HHHH
;
C   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SULFATE ION' SO4 
4 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PRO n 
1 2   VAL n 
1 3   TYR n 
1 4   MET n 
1 5   VAL n 
1 6   TYR n 
1 7   VAL n 
1 8   SER n 
1 9   GLN n 
1 10  ASP n 
1 11  ARG n 
1 12  LEU n 
1 13  THR n 
1 14  PRO n 
1 15  SER n 
1 16  ALA n 
1 17  LYS n 
1 18  HIS n 
1 19  ALA n 
1 20  VAL n 
1 21  ALA n 
1 22  LYS n 
1 23  ALA n 
1 24  ILE n 
1 25  THR n 
1 26  ASP n 
1 27  ALA n 
1 28  HIS n 
1 29  ARG n 
1 30  GLY n 
1 31  LEU n 
1 32  THR n 
1 33  GLY n 
1 34  THR n 
1 35  GLN n 
1 36  HIS n 
1 37  PHE n 
1 38  LEU n 
1 39  ALA n 
1 40  GLN n 
1 41  VAL n 
1 42  ASN n 
1 43  PHE n 
1 44  GLN n 
1 45  GLU n 
1 46  GLN n 
1 47  PRO n 
1 48  ALA n 
1 49  GLY n 
1 50  ASN n 
1 51  VAL n 
1 52  PHE n 
1 53  LEU n 
1 54  GLY n 
1 55  GLY n 
1 56  VAL n 
1 57  GLN n 
1 58  GLN n 
1 59  GLY n 
1 60  GLY n 
1 61  ASP n 
1 62  THR n 
1 63  ILE n 
1 64  PHE n 
1 65  VAL n 
1 66  HIS n 
1 67  GLY n 
1 68  LEU n 
1 69  HIS n 
1 70  ARG n 
1 71  GLU n 
1 72  GLY n 
1 73  ARG n 
1 74  SER n 
1 75  ALA n 
1 76  ASP n 
1 77  LEU n 
1 78  LYS n 
1 79  GLY n 
1 80  GLN n 
1 81  LEU n 
1 82  ALA n 
1 83  GLN n 
1 84  ARG n 
1 85  ILE n 
1 86  VAL n 
1 87  ASP n 
1 88  ASP n 
1 89  VAL n 
1 90  SER n 
1 91  VAL n 
1 92  ALA n 
1 93  ALA n 
1 94  GLU n 
1 95  ILE n 
1 96  ASP n 
1 97  ARG n 
1 98  LYS n 
1 99  HIS n 
1 100 ILE n 
1 101 TRP n 
1 102 VAL n 
1 103 TYR n 
1 104 PHE n 
1 105 GLY n 
1 106 GLU n 
1 107 MET n 
1 108 PRO n 
1 109 ALA n 
1 110 GLN n 
1 111 GLN n 
1 112 MET n 
1 113 VAL n 
1 114 ASP n 
1 115 TYR n 
1 116 GLY n 
1 117 ARG n 
1 118 PHE n 
1 119 LEU n 
1 120 PRO n 
1 121 GLN n 
1 122 PRO n 
1 123 GLY n 
1 124 HIS n 
1 125 GLU n 
1 126 GLY n 
1 127 GLU n 
1 128 TRP n 
1 129 PHE n 
1 130 ASP n 
1 131 ASN n 
1 132 LEU n 
1 133 SER n 
1 134 SER n 
1 135 ASP n 
1 136 GLU n 
1 137 ARG n 
1 138 ALA n 
1 139 PHE n 
1 140 MET n 
1 141 GLU n 
1 142 THR n 
1 143 ASN n 
1 144 VAL n 
1 145 ASP n 
1 146 VAL n 
1 147 SER n 
1 148 ARG n 
1 149 THR n 
1 150 GLU n 
1 151 ASN n 
1 152 LEU n 
1 153 TYR n 
1 154 PHE n 
1 155 GLN n 
1 156 GLY n 
1 157 LEU n 
1 158 GLU n 
1 159 HIS n 
1 160 HIS n 
1 161 HIS n 
1 162 HIS n 
1 163 HIS n 
1 164 HIS n 
2 1   N80 n 
2 2   VAL n 
2 3   TYR n 
2 4   MET n 
2 5   VAL n 
2 6   TYR n 
2 7   VAL n 
2 8   SER n 
2 9   GLN n 
2 10  ASP n 
2 11  ARG n 
2 12  LEU n 
2 13  THR n 
2 14  PRO n 
2 15  SER n 
2 16  ALA n 
2 17  LYS n 
2 18  HIS n 
2 19  ALA n 
2 20  VAL n 
2 21  ALA n 
2 22  LYS n 
2 23  ALA n 
2 24  ILE n 
2 25  THR n 
2 26  ASP n 
2 27  ALA n 
2 28  HIS n 
2 29  ARG n 
2 30  GLY n 
2 31  LEU n 
2 32  THR n 
2 33  GLY n 
2 34  THR n 
2 35  GLN n 
2 36  HIS n 
2 37  PHE n 
2 38  LEU n 
2 39  ALA n 
2 40  GLN n 
2 41  VAL n 
2 42  ASN n 
2 43  PHE n 
2 44  GLN n 
2 45  GLU n 
2 46  GLN n 
2 47  PRO n 
2 48  ALA n 
2 49  GLY n 
2 50  ASN n 
2 51  VAL n 
2 52  PHE n 
2 53  LEU n 
2 54  GLY n 
2 55  GLY n 
2 56  VAL n 
2 57  GLN n 
2 58  GLN n 
2 59  GLY n 
2 60  GLY n 
2 61  ASP n 
2 62  THR n 
2 63  ILE n 
2 64  PHE n 
2 65  VAL n 
2 66  HIS n 
2 67  GLY n 
2 68  LEU n 
2 69  HIS n 
2 70  ARG n 
2 71  GLU n 
2 72  GLY n 
2 73  ARG n 
2 74  SER n 
2 75  ALA n 
2 76  ASP n 
2 77  LEU n 
2 78  LYS n 
2 79  GLY n 
2 80  GLN n 
2 81  LEU n 
2 82  ALA n 
2 83  GLN n 
2 84  ARG n 
2 85  ILE n 
2 86  VAL n 
2 87  ASP n 
2 88  ASP n 
2 89  VAL n 
2 90  SER n 
2 91  VAL n 
2 92  ALA n 
2 93  ALA n 
2 94  GLU n 
2 95  ILE n 
2 96  ASP n 
2 97  ARG n 
2 98  LYS n 
2 99  HIS n 
2 100 ILE n 
2 101 TRP n 
2 102 VAL n 
2 103 TYR n 
2 104 PHE n 
2 105 GLY n 
2 106 GLU n 
2 107 MET n 
2 108 PRO n 
2 109 ALA n 
2 110 GLN n 
2 111 GLN n 
2 112 MET n 
2 113 VAL n 
2 114 ASP n 
2 115 TYR n 
2 116 GLY n 
2 117 ARG n 
2 118 PHE n 
2 119 LEU n 
2 120 PRO n 
2 121 GLN n 
2 122 PRO n 
2 123 GLY n 
2 124 HIS n 
2 125 GLU n 
2 126 GLY n 
2 127 GLU n 
2 128 TRP n 
2 129 PHE n 
2 130 ASP n 
2 131 ASN n 
2 132 LEU n 
2 133 SER n 
2 134 SER n 
2 135 ASP n 
2 136 GLU n 
2 137 ARG n 
2 138 ALA n 
2 139 PHE n 
2 140 MET n 
2 141 GLU n 
2 142 THR n 
2 143 ASN n 
2 144 VAL n 
2 145 ASP n 
2 146 VAL n 
2 147 SER n 
2 148 ARG n 
2 149 THR n 
2 150 GLU n 
2 151 ASN n 
2 152 LEU n 
2 153 TYR n 
2 154 PHE n 
2 155 GLN n 
2 156 GLY n 
2 157 LEU n 
2 158 GLU n 
2 159 HIS n 
2 160 HIS n 
2 161 HIS n 
2 162 HIS n 
2 163 HIS n 
2 164 HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 164 ? ? cis-caaD ? ? ? ? ? ? 'coryneform bacterium' 1728 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 164 ? ? cis-caaD ? ? ? ? ? ? 'coryneform bacterium' 1728 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 
? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE             ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE            ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE          ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'     ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE           ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'     ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE             ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE           ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER               ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE          ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE             ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE              ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE          ? 'C5 H11 N O2 S'  149.211 
N80 'L-peptide linking' n 1-ethenyl-L-proline ? 'C7 H11 N O2'    141.168 
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 
SO4 non-polymer         . 'SULFATE ION'       ? 'O4 S -2'        96.063  
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   PRO 1   1   1   PRO PRO B . n 
A 1 2   VAL 2   2   2   VAL VAL B . n 
A 1 3   TYR 3   3   3   TYR TYR B . n 
A 1 4   MET 4   4   4   MET MET B . n 
A 1 5   VAL 5   5   5   VAL VAL B . n 
A 1 6   TYR 6   6   6   TYR TYR B . n 
A 1 7   VAL 7   7   7   VAL VAL B . n 
A 1 8   SER 8   8   8   SER SER B . n 
A 1 9   GLN 9   9   9   GLN GLN B . n 
A 1 10  ASP 10  10  10  ASP ASP B . n 
A 1 11  ARG 11  11  11  ARG ARG B . n 
A 1 12  LEU 12  12  12  LEU LEU B . n 
A 1 13  THR 13  13  13  THR THR B . n 
A 1 14  PRO 14  14  14  PRO PRO B . n 
A 1 15  SER 15  15  15  SER SER B . n 
A 1 16  ALA 16  16  16  ALA ALA B . n 
A 1 17  LYS 17  17  17  LYS LYS B . n 
A 1 18  HIS 18  18  18  HIS HIS B . n 
A 1 19  ALA 19  19  19  ALA ALA B . n 
A 1 20  VAL 20  20  20  VAL VAL B . n 
A 1 21  ALA 21  21  21  ALA ALA B . n 
A 1 22  LYS 22  22  22  LYS LYS B . n 
A 1 23  ALA 23  23  23  ALA ALA B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  THR 25  25  25  THR THR B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  ALA 27  27  27  ALA ALA B . n 
A 1 28  HIS 28  28  28  HIS HIS B . n 
A 1 29  ARG 29  29  29  ARG ARG B . n 
A 1 30  GLY 30  30  30  GLY GLY B . n 
A 1 31  LEU 31  31  31  LEU LEU B . n 
A 1 32  THR 32  32  32  THR THR B . n 
A 1 33  GLY 33  33  33  GLY GLY B . n 
A 1 34  THR 34  34  34  THR THR B . n 
A 1 35  GLN 35  35  35  GLN GLN B . n 
A 1 36  HIS 36  36  36  HIS HIS B . n 
A 1 37  PHE 37  37  37  PHE PHE B . n 
A 1 38  LEU 38  38  38  LEU LEU B . n 
A 1 39  ALA 39  39  39  ALA ALA B . n 
A 1 40  GLN 40  40  40  GLN GLN B . n 
A 1 41  VAL 41  41  41  VAL VAL B . n 
A 1 42  ASN 42  42  42  ASN ASN B . n 
A 1 43  PHE 43  43  43  PHE PHE B . n 
A 1 44  GLN 44  44  44  GLN GLN B . n 
A 1 45  GLU 45  45  45  GLU GLU B . n 
A 1 46  GLN 46  46  46  GLN GLN B . n 
A 1 47  PRO 47  47  47  PRO PRO B . n 
A 1 48  ALA 48  48  48  ALA ALA B . n 
A 1 49  GLY 49  49  49  GLY GLY B . n 
A 1 50  ASN 50  50  50  ASN ASN B . n 
A 1 51  VAL 51  51  51  VAL VAL B . n 
A 1 52  PHE 52  52  52  PHE PHE B . n 
A 1 53  LEU 53  53  53  LEU LEU B . n 
A 1 54  GLY 54  54  54  GLY GLY B . n 
A 1 55  GLY 55  55  55  GLY GLY B . n 
A 1 56  VAL 56  56  56  VAL VAL B . n 
A 1 57  GLN 57  57  57  GLN GLN B . n 
A 1 58  GLN 58  58  58  GLN GLN B . n 
A 1 59  GLY 59  59  59  GLY GLY B . n 
A 1 60  GLY 60  60  60  GLY GLY B . n 
A 1 61  ASP 61  61  61  ASP ASP B . n 
A 1 62  THR 62  62  62  THR THR B . n 
A 1 63  ILE 63  63  63  ILE ILE B . n 
A 1 64  PHE 64  64  64  PHE PHE B . n 
A 1 65  VAL 65  65  65  VAL VAL B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  GLY 67  67  67  GLY GLY B . n 
A 1 68  LEU 68  68  68  LEU LEU B . n 
A 1 69  HIS 69  69  69  HIS HIS B . n 
A 1 70  ARG 70  70  70  ARG ARG B . n 
A 1 71  GLU 71  71  71  GLU GLU B . n 
A 1 72  GLY 72  72  72  GLY GLY B . n 
A 1 73  ARG 73  73  73  ARG ARG B . n 
A 1 74  SER 74  74  74  SER SER B . n 
A 1 75  ALA 75  75  75  ALA ALA B . n 
A 1 76  ASP 76  76  76  ASP ASP B . n 
A 1 77  LEU 77  77  77  LEU LEU B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  GLY 79  79  79  GLY GLY B . n 
A 1 80  GLN 80  80  80  GLN GLN B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ALA 82  82  82  ALA ALA B . n 
A 1 83  GLN 83  83  83  GLN GLN B . n 
A 1 84  ARG 84  84  84  ARG ARG B . n 
A 1 85  ILE 85  85  85  ILE ILE B . n 
A 1 86  VAL 86  86  86  VAL VAL B . n 
A 1 87  ASP 87  87  87  ASP ASP B . n 
A 1 88  ASP 88  88  88  ASP ASP B . n 
A 1 89  VAL 89  89  89  VAL VAL B . n 
A 1 90  SER 90  90  90  SER SER B . n 
A 1 91  VAL 91  91  91  VAL VAL B . n 
A 1 92  ALA 92  92  92  ALA ALA B . n 
A 1 93  ALA 93  93  93  ALA ALA B . n 
A 1 94  GLU 94  94  94  GLU GLU B . n 
A 1 95  ILE 95  95  95  ILE ILE B . n 
A 1 96  ASP 96  96  96  ASP ASP B . n 
A 1 97  ARG 97  97  97  ARG ARG B . n 
A 1 98  LYS 98  98  98  LYS LYS B . n 
A 1 99  HIS 99  99  99  HIS HIS B . n 
A 1 100 ILE 100 100 100 ILE ILE B . n 
A 1 101 TRP 101 101 101 TRP TRP B . n 
A 1 102 VAL 102 102 102 VAL VAL B . n 
A 1 103 TYR 103 103 103 TYR TYR B . n 
A 1 104 PHE 104 104 104 PHE PHE B . n 
A 1 105 GLY 105 105 105 GLY GLY B . n 
A 1 106 GLU 106 106 106 GLU GLU B . n 
A 1 107 MET 107 107 107 MET MET B . n 
A 1 108 PRO 108 108 108 PRO PRO B . n 
A 1 109 ALA 109 109 109 ALA ALA B . n 
A 1 110 GLN 110 110 110 GLN GLN B . n 
A 1 111 GLN 111 111 111 GLN GLN B . n 
A 1 112 MET 112 112 112 MET MET B . n 
A 1 113 VAL 113 113 113 VAL VAL B . n 
A 1 114 ASP 114 114 114 ASP ASP B . n 
A 1 115 TYR 115 115 115 TYR TYR B . n 
A 1 116 GLY 116 116 116 GLY GLY B . n 
A 1 117 ARG 117 117 117 ARG ARG B . n 
A 1 118 PHE 118 118 118 PHE PHE B . n 
A 1 119 LEU 119 119 119 LEU LEU B . n 
A 1 120 PRO 120 120 120 PRO PRO B . n 
A 1 121 GLN 121 121 121 GLN GLN B . n 
A 1 122 PRO 122 122 122 PRO PRO B . n 
A 1 123 GLY 123 123 123 GLY GLY B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 GLU 125 125 125 GLU GLU B . n 
A 1 126 GLY 126 126 126 GLY GLY B . n 
A 1 127 GLU 127 127 127 GLU GLU B . n 
A 1 128 TRP 128 128 128 TRP TRP B . n 
A 1 129 PHE 129 129 129 PHE PHE B . n 
A 1 130 ASP 130 130 130 ASP ASP B . n 
A 1 131 ASN 131 131 131 ASN ASN B . n 
A 1 132 LEU 132 132 132 LEU LEU B . n 
A 1 133 SER 133 133 133 SER SER B . n 
A 1 134 SER 134 134 134 SER SER B . n 
A 1 135 ASP 135 135 135 ASP ASP B . n 
A 1 136 GLU 136 136 136 GLU GLU B . n 
A 1 137 ARG 137 137 137 ARG ARG B . n 
A 1 138 ALA 138 138 138 ALA ALA B . n 
A 1 139 PHE 139 139 139 PHE PHE B . n 
A 1 140 MET 140 140 140 MET MET B . n 
A 1 141 GLU 141 141 141 GLU GLU B . n 
A 1 142 THR 142 142 142 THR THR B . n 
A 1 143 ASN 143 143 143 ASN ASN B . n 
A 1 144 VAL 144 144 144 VAL VAL B . n 
A 1 145 ASP 145 145 145 ASP ASP B . n 
A 1 146 VAL 146 146 ?   ?   ?   B . n 
A 1 147 SER 147 147 ?   ?   ?   B . n 
A 1 148 ARG 148 148 ?   ?   ?   B . n 
A 1 149 THR 149 149 ?   ?   ?   B . n 
A 1 150 GLU 150 150 ?   ?   ?   B . n 
A 1 151 ASN 151 151 ?   ?   ?   B . n 
A 1 152 LEU 152 152 ?   ?   ?   B . n 
A 1 153 TYR 153 153 ?   ?   ?   B . n 
A 1 154 PHE 154 154 ?   ?   ?   B . n 
A 1 155 GLN 155 155 ?   ?   ?   B . n 
A 1 156 GLY 156 156 ?   ?   ?   B . n 
A 1 157 LEU 157 157 ?   ?   ?   B . n 
A 1 158 GLU 158 158 ?   ?   ?   B . n 
A 1 159 HIS 159 159 ?   ?   ?   B . n 
A 1 160 HIS 160 160 ?   ?   ?   B . n 
A 1 161 HIS 161 161 ?   ?   ?   B . n 
A 1 162 HIS 162 162 ?   ?   ?   B . n 
A 1 163 HIS 163 163 ?   ?   ?   B . n 
A 1 164 HIS 164 164 ?   ?   ?   B . n 
B 2 1   N80 1   1   1   N80 PRO C . n 
B 2 2   VAL 2   2   2   VAL VAL C . n 
B 2 3   TYR 3   3   3   TYR TYR C . n 
B 2 4   MET 4   4   4   MET MET C . n 
B 2 5   VAL 5   5   5   VAL VAL C . n 
B 2 6   TYR 6   6   6   TYR TYR C . n 
B 2 7   VAL 7   7   7   VAL VAL C . n 
B 2 8   SER 8   8   8   SER SER C . n 
B 2 9   GLN 9   9   9   GLN GLN C . n 
B 2 10  ASP 10  10  10  ASP ASP C . n 
B 2 11  ARG 11  11  11  ARG ARG C . n 
B 2 12  LEU 12  12  12  LEU LEU C . n 
B 2 13  THR 13  13  13  THR THR C . n 
B 2 14  PRO 14  14  14  PRO PRO C . n 
B 2 15  SER 15  15  15  SER SER C . n 
B 2 16  ALA 16  16  16  ALA ALA C . n 
B 2 17  LYS 17  17  17  LYS LYS C . n 
B 2 18  HIS 18  18  18  HIS HIS C . n 
B 2 19  ALA 19  19  19  ALA ALA C . n 
B 2 20  VAL 20  20  20  VAL VAL C . n 
B 2 21  ALA 21  21  21  ALA ALA C . n 
B 2 22  LYS 22  22  22  LYS LYS C . n 
B 2 23  ALA 23  23  23  ALA ALA C . n 
B 2 24  ILE 24  24  24  ILE ILE C . n 
B 2 25  THR 25  25  25  THR THR C . n 
B 2 26  ASP 26  26  26  ASP ASP C . n 
B 2 27  ALA 27  27  27  ALA ALA C . n 
B 2 28  HIS 28  28  28  HIS HIS C . n 
B 2 29  ARG 29  29  29  ARG ARG C . n 
B 2 30  GLY 30  30  30  GLY GLY C . n 
B 2 31  LEU 31  31  31  LEU LEU C . n 
B 2 32  THR 32  32  32  THR THR C . n 
B 2 33  GLY 33  33  33  GLY GLY C . n 
B 2 34  THR 34  34  34  THR THR C . n 
B 2 35  GLN 35  35  35  GLN GLN C . n 
B 2 36  HIS 36  36  36  HIS HIS C . n 
B 2 37  PHE 37  37  37  PHE PHE C . n 
B 2 38  LEU 38  38  38  LEU LEU C . n 
B 2 39  ALA 39  39  39  ALA ALA C . n 
B 2 40  GLN 40  40  40  GLN GLN C . n 
B 2 41  VAL 41  41  41  VAL VAL C . n 
B 2 42  ASN 42  42  42  ASN ASN C . n 
B 2 43  PHE 43  43  43  PHE PHE C . n 
B 2 44  GLN 44  44  44  GLN GLN C . n 
B 2 45  GLU 45  45  45  GLU GLU C . n 
B 2 46  GLN 46  46  46  GLN GLN C . n 
B 2 47  PRO 47  47  47  PRO PRO C . n 
B 2 48  ALA 48  48  48  ALA ALA C . n 
B 2 49  GLY 49  49  49  GLY GLY C . n 
B 2 50  ASN 50  50  50  ASN ASN C . n 
B 2 51  VAL 51  51  51  VAL VAL C . n 
B 2 52  PHE 52  52  52  PHE PHE C . n 
B 2 53  LEU 53  53  53  LEU LEU C . n 
B 2 54  GLY 54  54  54  GLY GLY C . n 
B 2 55  GLY 55  55  55  GLY GLY C . n 
B 2 56  VAL 56  56  56  VAL VAL C . n 
B 2 57  GLN 57  57  57  GLN GLN C . n 
B 2 58  GLN 58  58  58  GLN GLN C . n 
B 2 59  GLY 59  59  59  GLY GLY C . n 
B 2 60  GLY 60  60  60  GLY GLY C . n 
B 2 61  ASP 61  61  61  ASP ASP C . n 
B 2 62  THR 62  62  62  THR THR C . n 
B 2 63  ILE 63  63  63  ILE ILE C . n 
B 2 64  PHE 64  64  64  PHE PHE C . n 
B 2 65  VAL 65  65  65  VAL VAL C . n 
B 2 66  HIS 66  66  66  HIS HIS C . n 
B 2 67  GLY 67  67  67  GLY GLY C . n 
B 2 68  LEU 68  68  68  LEU LEU C . n 
B 2 69  HIS 69  69  69  HIS HIS C . n 
B 2 70  ARG 70  70  70  ARG ARG C . n 
B 2 71  GLU 71  71  71  GLU GLU C . n 
B 2 72  GLY 72  72  72  GLY GLY C . n 
B 2 73  ARG 73  73  73  ARG ARG C . n 
B 2 74  SER 74  74  74  SER SER C . n 
B 2 75  ALA 75  75  75  ALA ALA C . n 
B 2 76  ASP 76  76  76  ASP ASP C . n 
B 2 77  LEU 77  77  77  LEU LEU C . n 
B 2 78  LYS 78  78  78  LYS LYS C . n 
B 2 79  GLY 79  79  79  GLY GLY C . n 
B 2 80  GLN 80  80  80  GLN GLN C . n 
B 2 81  LEU 81  81  81  LEU LEU C . n 
B 2 82  ALA 82  82  82  ALA ALA C . n 
B 2 83  GLN 83  83  83  GLN GLN C . n 
B 2 84  ARG 84  84  84  ARG ARG C . n 
B 2 85  ILE 85  85  85  ILE ILE C . n 
B 2 86  VAL 86  86  86  VAL VAL C . n 
B 2 87  ASP 87  87  87  ASP ASP C . n 
B 2 88  ASP 88  88  88  ASP ASP C . n 
B 2 89  VAL 89  89  89  VAL VAL C . n 
B 2 90  SER 90  90  90  SER SER C . n 
B 2 91  VAL 91  91  91  VAL VAL C . n 
B 2 92  ALA 92  92  92  ALA ALA C . n 
B 2 93  ALA 93  93  93  ALA ALA C . n 
B 2 94  GLU 94  94  94  GLU GLU C . n 
B 2 95  ILE 95  95  95  ILE ILE C . n 
B 2 96  ASP 96  96  96  ASP ASP C . n 
B 2 97  ARG 97  97  97  ARG ARG C . n 
B 2 98  LYS 98  98  98  LYS LYS C . n 
B 2 99  HIS 99  99  99  HIS HIS C . n 
B 2 100 ILE 100 100 100 ILE ILE C . n 
B 2 101 TRP 101 101 101 TRP TRP C . n 
B 2 102 VAL 102 102 102 VAL VAL C . n 
B 2 103 TYR 103 103 103 TYR TYR C . n 
B 2 104 PHE 104 104 104 PHE PHE C . n 
B 2 105 GLY 105 105 105 GLY GLY C . n 
B 2 106 GLU 106 106 106 GLU GLU C . n 
B 2 107 MET 107 107 107 MET MET C . n 
B 2 108 PRO 108 108 108 PRO PRO C . n 
B 2 109 ALA 109 109 109 ALA ALA C . n 
B 2 110 GLN 110 110 110 GLN GLN C . n 
B 2 111 GLN 111 111 111 GLN GLN C . n 
B 2 112 MET 112 112 112 MET MET C . n 
B 2 113 VAL 113 113 113 VAL VAL C . n 
B 2 114 ASP 114 114 114 ASP ASP C . n 
B 2 115 TYR 115 115 115 TYR TYR C . n 
B 2 116 GLY 116 116 116 GLY GLY C . n 
B 2 117 ARG 117 117 117 ARG ARG C . n 
B 2 118 PHE 118 118 118 PHE PHE C . n 
B 2 119 LEU 119 119 119 LEU LEU C . n 
B 2 120 PRO 120 120 120 PRO PRO C . n 
B 2 121 GLN 121 121 121 GLN GLN C . n 
B 2 122 PRO 122 122 122 PRO PRO C . n 
B 2 123 GLY 123 123 123 GLY GLY C . n 
B 2 124 HIS 124 124 124 HIS HIS C . n 
B 2 125 GLU 125 125 125 GLU GLU C . n 
B 2 126 GLY 126 126 126 GLY GLY C . n 
B 2 127 GLU 127 127 127 GLU GLU C . n 
B 2 128 TRP 128 128 128 TRP TRP C . n 
B 2 129 PHE 129 129 129 PHE PHE C . n 
B 2 130 ASP 130 130 130 ASP ASP C . n 
B 2 131 ASN 131 131 131 ASN ASN C . n 
B 2 132 LEU 132 132 132 LEU LEU C . n 
B 2 133 SER 133 133 133 SER SER C . n 
B 2 134 SER 134 134 134 SER SER C . n 
B 2 135 ASP 135 135 135 ASP ASP C . n 
B 2 136 GLU 136 136 136 GLU GLU C . n 
B 2 137 ARG 137 137 137 ARG ARG C . n 
B 2 138 ALA 138 138 138 ALA ALA C . n 
B 2 139 PHE 139 139 139 PHE PHE C . n 
B 2 140 MET 140 140 140 MET MET C . n 
B 2 141 GLU 141 141 141 GLU GLU C . n 
B 2 142 THR 142 142 142 THR THR C . n 
B 2 143 ASN 143 143 143 ASN ASN C . n 
B 2 144 VAL 144 144 144 VAL VAL C . n 
B 2 145 ASP 145 145 145 ASP ASP C . n 
B 2 146 VAL 146 146 146 VAL VAL C . n 
B 2 147 SER 147 147 ?   ?   ?   C . n 
B 2 148 ARG 148 148 ?   ?   ?   C . n 
B 2 149 THR 149 149 ?   ?   ?   C . n 
B 2 150 GLU 150 150 ?   ?   ?   C . n 
B 2 151 ASN 151 151 ?   ?   ?   C . n 
B 2 152 LEU 152 152 ?   ?   ?   C . n 
B 2 153 TYR 153 153 ?   ?   ?   C . n 
B 2 154 PHE 154 154 ?   ?   ?   C . n 
B 2 155 GLN 155 155 ?   ?   ?   C . n 
B 2 156 GLY 156 156 ?   ?   ?   C . n 
B 2 157 LEU 157 157 ?   ?   ?   C . n 
B 2 158 GLU 158 158 ?   ?   ?   C . n 
B 2 159 HIS 159 159 ?   ?   ?   C . n 
B 2 160 HIS 160 160 ?   ?   ?   C . n 
B 2 161 HIS 161 161 ?   ?   ?   C . n 
B 2 162 HIS 162 162 ?   ?   ?   C . n 
B 2 163 HIS 163 163 ?   ?   ?   C . n 
B 2 164 HIS 164 164 ?   ?   ?   C . n 
C 1 1   PRO 1   1   1   PRO PRO A . n 
C 1 2   VAL 2   2   2   VAL VAL A . n 
C 1 3   TYR 3   3   3   TYR TYR A . n 
C 1 4   MET 4   4   4   MET MET A . n 
C 1 5   VAL 5   5   5   VAL VAL A . n 
C 1 6   TYR 6   6   6   TYR TYR A . n 
C 1 7   VAL 7   7   7   VAL VAL A . n 
C 1 8   SER 8   8   8   SER SER A . n 
C 1 9   GLN 9   9   9   GLN GLN A . n 
C 1 10  ASP 10  10  10  ASP ASP A . n 
C 1 11  ARG 11  11  11  ARG ARG A . n 
C 1 12  LEU 12  12  12  LEU LEU A . n 
C 1 13  THR 13  13  13  THR THR A . n 
C 1 14  PRO 14  14  14  PRO PRO A . n 
C 1 15  SER 15  15  15  SER SER A . n 
C 1 16  ALA 16  16  16  ALA ALA A . n 
C 1 17  LYS 17  17  17  LYS LYS A . n 
C 1 18  HIS 18  18  18  HIS HIS A . n 
C 1 19  ALA 19  19  19  ALA ALA A . n 
C 1 20  VAL 20  20  20  VAL VAL A . n 
C 1 21  ALA 21  21  21  ALA ALA A . n 
C 1 22  LYS 22  22  22  LYS LYS A . n 
C 1 23  ALA 23  23  23  ALA ALA A . n 
C 1 24  ILE 24  24  24  ILE ILE A . n 
C 1 25  THR 25  25  25  THR THR A . n 
C 1 26  ASP 26  26  26  ASP ASP A . n 
C 1 27  ALA 27  27  27  ALA ALA A . n 
C 1 28  HIS 28  28  28  HIS HIS A . n 
C 1 29  ARG 29  29  29  ARG ARG A . n 
C 1 30  GLY 30  30  30  GLY GLY A . n 
C 1 31  LEU 31  31  31  LEU LEU A . n 
C 1 32  THR 32  32  32  THR THR A . n 
C 1 33  GLY 33  33  33  GLY GLY A . n 
C 1 34  THR 34  34  34  THR THR A . n 
C 1 35  GLN 35  35  35  GLN GLN A . n 
C 1 36  HIS 36  36  36  HIS HIS A . n 
C 1 37  PHE 37  37  37  PHE PHE A . n 
C 1 38  LEU 38  38  38  LEU LEU A . n 
C 1 39  ALA 39  39  39  ALA ALA A . n 
C 1 40  GLN 40  40  40  GLN GLN A . n 
C 1 41  VAL 41  41  41  VAL VAL A . n 
C 1 42  ASN 42  42  42  ASN ASN A . n 
C 1 43  PHE 43  43  43  PHE PHE A . n 
C 1 44  GLN 44  44  44  GLN GLN A . n 
C 1 45  GLU 45  45  45  GLU GLU A . n 
C 1 46  GLN 46  46  46  GLN GLN A . n 
C 1 47  PRO 47  47  47  PRO PRO A . n 
C 1 48  ALA 48  48  48  ALA ALA A . n 
C 1 49  GLY 49  49  49  GLY GLY A . n 
C 1 50  ASN 50  50  50  ASN ASN A . n 
C 1 51  VAL 51  51  51  VAL VAL A . n 
C 1 52  PHE 52  52  52  PHE PHE A . n 
C 1 53  LEU 53  53  53  LEU LEU A . n 
C 1 54  GLY 54  54  54  GLY GLY A . n 
C 1 55  GLY 55  55  55  GLY GLY A . n 
C 1 56  VAL 56  56  56  VAL VAL A . n 
C 1 57  GLN 57  57  57  GLN GLN A . n 
C 1 58  GLN 58  58  58  GLN GLN A . n 
C 1 59  GLY 59  59  59  GLY GLY A . n 
C 1 60  GLY 60  60  60  GLY GLY A . n 
C 1 61  ASP 61  61  61  ASP ASP A . n 
C 1 62  THR 62  62  62  THR THR A . n 
C 1 63  ILE 63  63  63  ILE ILE A . n 
C 1 64  PHE 64  64  64  PHE PHE A . n 
C 1 65  VAL 65  65  65  VAL VAL A . n 
C 1 66  HIS 66  66  66  HIS HIS A . n 
C 1 67  GLY 67  67  67  GLY GLY A . n 
C 1 68  LEU 68  68  68  LEU LEU A . n 
C 1 69  HIS 69  69  69  HIS HIS A . n 
C 1 70  ARG 70  70  70  ARG ARG A . n 
C 1 71  GLU 71  71  71  GLU GLU A . n 
C 1 72  GLY 72  72  72  GLY GLY A . n 
C 1 73  ARG 73  73  73  ARG ARG A . n 
C 1 74  SER 74  74  74  SER SER A . n 
C 1 75  ALA 75  75  75  ALA ALA A . n 
C 1 76  ASP 76  76  76  ASP ASP A . n 
C 1 77  LEU 77  77  77  LEU LEU A . n 
C 1 78  LYS 78  78  78  LYS LYS A . n 
C 1 79  GLY 79  79  79  GLY GLY A . n 
C 1 80  GLN 80  80  80  GLN GLN A . n 
C 1 81  LEU 81  81  81  LEU LEU A . n 
C 1 82  ALA 82  82  82  ALA ALA A . n 
C 1 83  GLN 83  83  83  GLN GLN A . n 
C 1 84  ARG 84  84  84  ARG ARG A . n 
C 1 85  ILE 85  85  85  ILE ILE A . n 
C 1 86  VAL 86  86  86  VAL VAL A . n 
C 1 87  ASP 87  87  87  ASP ASP A . n 
C 1 88  ASP 88  88  88  ASP ASP A . n 
C 1 89  VAL 89  89  89  VAL VAL A . n 
C 1 90  SER 90  90  90  SER SER A . n 
C 1 91  VAL 91  91  91  VAL VAL A . n 
C 1 92  ALA 92  92  92  ALA ALA A . n 
C 1 93  ALA 93  93  93  ALA ALA A . n 
C 1 94  GLU 94  94  94  GLU GLU A . n 
C 1 95  ILE 95  95  95  ILE ILE A . n 
C 1 96  ASP 96  96  96  ASP ASP A . n 
C 1 97  ARG 97  97  97  ARG ARG A . n 
C 1 98  LYS 98  98  98  LYS LYS A . n 
C 1 99  HIS 99  99  99  HIS HIS A . n 
C 1 100 ILE 100 100 100 ILE ILE A . n 
C 1 101 TRP 101 101 101 TRP TRP A . n 
C 1 102 VAL 102 102 102 VAL VAL A . n 
C 1 103 TYR 103 103 103 TYR TYR A . n 
C 1 104 PHE 104 104 104 PHE PHE A . n 
C 1 105 GLY 105 105 105 GLY GLY A . n 
C 1 106 GLU 106 106 106 GLU GLU A . n 
C 1 107 MET 107 107 107 MET MET A . n 
C 1 108 PRO 108 108 108 PRO PRO A . n 
C 1 109 ALA 109 109 109 ALA ALA A . n 
C 1 110 GLN 110 110 110 GLN GLN A . n 
C 1 111 GLN 111 111 111 GLN GLN A . n 
C 1 112 MET 112 112 112 MET MET A . n 
C 1 113 VAL 113 113 113 VAL VAL A . n 
C 1 114 ASP 114 114 114 ASP ASP A . n 
C 1 115 TYR 115 115 115 TYR TYR A . n 
C 1 116 GLY 116 116 116 GLY GLY A . n 
C 1 117 ARG 117 117 117 ARG ARG A . n 
C 1 118 PHE 118 118 118 PHE PHE A . n 
C 1 119 LEU 119 119 119 LEU LEU A . n 
C 1 120 PRO 120 120 120 PRO PRO A . n 
C 1 121 GLN 121 121 121 GLN GLN A . n 
C 1 122 PRO 122 122 122 PRO PRO A . n 
C 1 123 GLY 123 123 123 GLY GLY A . n 
C 1 124 HIS 124 124 124 HIS HIS A . n 
C 1 125 GLU 125 125 125 GLU GLU A . n 
C 1 126 GLY 126 126 126 GLY GLY A . n 
C 1 127 GLU 127 127 127 GLU GLU A . n 
C 1 128 TRP 128 128 128 TRP TRP A . n 
C 1 129 PHE 129 129 129 PHE PHE A . n 
C 1 130 ASP 130 130 130 ASP ASP A . n 
C 1 131 ASN 131 131 131 ASN ASN A . n 
C 1 132 LEU 132 132 132 LEU LEU A . n 
C 1 133 SER 133 133 133 SER SER A . n 
C 1 134 SER 134 134 134 SER SER A . n 
C 1 135 ASP 135 135 135 ASP ASP A . n 
C 1 136 GLU 136 136 136 GLU GLU A . n 
C 1 137 ARG 137 137 137 ARG ARG A . n 
C 1 138 ALA 138 138 138 ALA ALA A . n 
C 1 139 PHE 139 139 139 PHE PHE A . n 
C 1 140 MET 140 140 140 MET MET A . n 
C 1 141 GLU 141 141 141 GLU GLU A . n 
C 1 142 THR 142 142 142 THR THR A . n 
C 1 143 ASN 143 143 143 ASN ASN A . n 
C 1 144 VAL 144 144 144 VAL VAL A . n 
C 1 145 ASP 145 145 145 ASP ASP A . n 
C 1 146 VAL 146 146 ?   ?   ?   A . n 
C 1 147 SER 147 147 ?   ?   ?   A . n 
C 1 148 ARG 148 148 ?   ?   ?   A . n 
C 1 149 THR 149 149 ?   ?   ?   A . n 
C 1 150 GLU 150 150 ?   ?   ?   A . n 
C 1 151 ASN 151 151 ?   ?   ?   A . n 
C 1 152 LEU 152 152 ?   ?   ?   A . n 
C 1 153 TYR 153 153 ?   ?   ?   A . n 
C 1 154 PHE 154 154 ?   ?   ?   A . n 
C 1 155 GLN 155 155 ?   ?   ?   A . n 
C 1 156 GLY 156 156 ?   ?   ?   A . n 
C 1 157 LEU 157 157 ?   ?   ?   A . n 
C 1 158 GLU 158 158 ?   ?   ?   A . n 
C 1 159 HIS 159 159 ?   ?   ?   A . n 
C 1 160 HIS 160 160 ?   ?   ?   A . n 
C 1 161 HIS 161 161 ?   ?   ?   A . n 
C 1 162 HIS 162 162 ?   ?   ?   A . n 
C 1 163 HIS 163 163 ?   ?   ?   A . n 
C 1 164 HIS 164 164 ?   ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 3 SO4 1   201 4   SO4 SO4 B . 
E 3 SO4 1   201 2   SO4 SO4 C . 
F 3 SO4 1   201 3   SO4 SO4 A . 
G 4 HOH 1   301 373 HOH HOH B . 
G 4 HOH 2   302 339 HOH HOH B . 
G 4 HOH 3   303 64  HOH HOH B . 
G 4 HOH 4   304 293 HOH HOH B . 
G 4 HOH 5   305 101 HOH HOH B . 
G 4 HOH 6   306 113 HOH HOH B . 
G 4 HOH 7   307 260 HOH HOH B . 
G 4 HOH 8   308 127 HOH HOH B . 
G 4 HOH 9   309 190 HOH HOH B . 
G 4 HOH 10  310 298 HOH HOH B . 
G 4 HOH 11  311 283 HOH HOH B . 
G 4 HOH 12  312 217 HOH HOH B . 
G 4 HOH 13  313 128 HOH HOH B . 
G 4 HOH 14  314 124 HOH HOH B . 
G 4 HOH 15  315 183 HOH HOH B . 
G 4 HOH 16  316 123 HOH HOH B . 
G 4 HOH 17  317 228 HOH HOH B . 
G 4 HOH 18  318 176 HOH HOH B . 
G 4 HOH 19  319 340 HOH HOH B . 
G 4 HOH 20  320 310 HOH HOH B . 
G 4 HOH 21  321 207 HOH HOH B . 
G 4 HOH 22  322 52  HOH HOH B . 
G 4 HOH 23  323 29  HOH HOH B . 
G 4 HOH 24  324 28  HOH HOH B . 
G 4 HOH 25  325 9   HOH HOH B . 
G 4 HOH 26  326 51  HOH HOH B . 
G 4 HOH 27  327 273 HOH HOH B . 
G 4 HOH 28  328 281 HOH HOH B . 
G 4 HOH 29  329 42  HOH HOH B . 
G 4 HOH 30  330 182 HOH HOH B . 
G 4 HOH 31  331 195 HOH HOH B . 
G 4 HOH 32  332 105 HOH HOH B . 
G 4 HOH 33  333 63  HOH HOH B . 
G 4 HOH 34  334 30  HOH HOH B . 
G 4 HOH 35  335 40  HOH HOH B . 
G 4 HOH 36  336 396 HOH HOH B . 
G 4 HOH 37  337 177 HOH HOH B . 
G 4 HOH 38  338 200 HOH HOH B . 
G 4 HOH 39  339 2   HOH HOH B . 
G 4 HOH 40  340 256 HOH HOH B . 
G 4 HOH 41  341 38  HOH HOH B . 
G 4 HOH 42  342 388 HOH HOH B . 
G 4 HOH 43  343 276 HOH HOH B . 
G 4 HOH 44  344 306 HOH HOH B . 
G 4 HOH 45  345 166 HOH HOH B . 
G 4 HOH 46  346 153 HOH HOH B . 
G 4 HOH 47  347 13  HOH HOH B . 
G 4 HOH 48  348 268 HOH HOH B . 
G 4 HOH 49  349 53  HOH HOH B . 
G 4 HOH 50  350 192 HOH HOH B . 
G 4 HOH 51  351 389 HOH HOH B . 
G 4 HOH 52  352 170 HOH HOH B . 
G 4 HOH 53  353 186 HOH HOH B . 
G 4 HOH 54  354 224 HOH HOH B . 
G 4 HOH 55  355 316 HOH HOH B . 
G 4 HOH 56  356 6   HOH HOH B . 
G 4 HOH 57  357 353 HOH HOH B . 
G 4 HOH 58  358 98  HOH HOH B . 
G 4 HOH 59  359 68  HOH HOH B . 
G 4 HOH 60  360 32  HOH HOH B . 
G 4 HOH 61  361 96  HOH HOH B . 
G 4 HOH 62  362 44  HOH HOH B . 
G 4 HOH 63  363 22  HOH HOH B . 
G 4 HOH 64  364 344 HOH HOH B . 
G 4 HOH 65  365 197 HOH HOH B . 
G 4 HOH 66  366 393 HOH HOH B . 
G 4 HOH 67  367 312 HOH HOH B . 
G 4 HOH 68  368 102 HOH HOH B . 
G 4 HOH 69  369 56  HOH HOH B . 
G 4 HOH 70  370 173 HOH HOH B . 
G 4 HOH 71  371 1   HOH HOH B . 
G 4 HOH 72  372 60  HOH HOH B . 
G 4 HOH 73  373 178 HOH HOH B . 
G 4 HOH 74  374 110 HOH HOH B . 
G 4 HOH 75  375 107 HOH HOH B . 
G 4 HOH 76  376 202 HOH HOH B . 
G 4 HOH 77  377 26  HOH HOH B . 
G 4 HOH 78  378 93  HOH HOH B . 
G 4 HOH 79  379 157 HOH HOH B . 
G 4 HOH 80  380 218 HOH HOH B . 
G 4 HOH 81  381 235 HOH HOH B . 
G 4 HOH 82  382 351 HOH HOH B . 
G 4 HOH 83  383 297 HOH HOH B . 
G 4 HOH 84  384 169 HOH HOH B . 
G 4 HOH 85  385 327 HOH HOH B . 
G 4 HOH 86  386 49  HOH HOH B . 
G 4 HOH 87  387 204 HOH HOH B . 
G 4 HOH 88  388 383 HOH HOH B . 
G 4 HOH 89  389 326 HOH HOH B . 
G 4 HOH 90  390 307 HOH HOH B . 
G 4 HOH 91  391 65  HOH HOH B . 
G 4 HOH 92  392 291 HOH HOH B . 
G 4 HOH 93  393 164 HOH HOH B . 
G 4 HOH 94  394 257 HOH HOH B . 
G 4 HOH 95  395 405 HOH HOH B . 
G 4 HOH 96  396 382 HOH HOH B . 
G 4 HOH 97  397 201 HOH HOH B . 
G 4 HOH 98  398 57  HOH HOH B . 
G 4 HOH 99  399 71  HOH HOH B . 
G 4 HOH 100 400 399 HOH HOH B . 
G 4 HOH 101 401 271 HOH HOH B . 
G 4 HOH 102 402 203 HOH HOH B . 
G 4 HOH 103 403 299 HOH HOH B . 
G 4 HOH 104 404 76  HOH HOH B . 
G 4 HOH 105 405 246 HOH HOH B . 
G 4 HOH 106 406 392 HOH HOH B . 
G 4 HOH 107 407 126 HOH HOH B . 
G 4 HOH 108 408 92  HOH HOH B . 
G 4 HOH 109 409 342 HOH HOH B . 
G 4 HOH 110 410 324 HOH HOH B . 
G 4 HOH 111 411 289 HOH HOH B . 
G 4 HOH 112 412 302 HOH HOH B . 
G 4 HOH 113 413 250 HOH HOH B . 
G 4 HOH 114 414 295 HOH HOH B . 
G 4 HOH 115 415 320 HOH HOH B . 
G 4 HOH 116 416 400 HOH HOH B . 
G 4 HOH 117 417 366 HOH HOH B . 
G 4 HOH 118 418 41  HOH HOH B . 
G 4 HOH 119 419 387 HOH HOH B . 
G 4 HOH 120 420 277 HOH HOH B . 
G 4 HOH 121 421 181 HOH HOH B . 
G 4 HOH 122 422 264 HOH HOH B . 
G 4 HOH 123 423 300 HOH HOH B . 
G 4 HOH 124 424 337 HOH HOH B . 
G 4 HOH 125 425 251 HOH HOH B . 
G 4 HOH 126 426 129 HOH HOH B . 
G 4 HOH 127 427 220 HOH HOH B . 
G 4 HOH 128 428 401 HOH HOH B . 
G 4 HOH 129 429 292 HOH HOH B . 
G 4 HOH 130 430 240 HOH HOH B . 
G 4 HOH 131 431 350 HOH HOH B . 
G 4 HOH 132 432 62  HOH HOH B . 
G 4 HOH 133 433 335 HOH HOH B . 
G 4 HOH 134 434 206 HOH HOH B . 
G 4 HOH 135 435 97  HOH HOH B . 
G 4 HOH 136 436 262 HOH HOH B . 
G 4 HOH 137 437 377 HOH HOH B . 
G 4 HOH 138 438 229 HOH HOH B . 
G 4 HOH 139 439 193 HOH HOH B . 
G 4 HOH 140 440 305 HOH HOH B . 
G 4 HOH 141 441 333 HOH HOH B . 
G 4 HOH 142 442 261 HOH HOH B . 
G 4 HOH 143 443 114 HOH HOH B . 
G 4 HOH 144 444 187 HOH HOH B . 
G 4 HOH 145 445 121 HOH HOH B . 
G 4 HOH 146 446 332 HOH HOH B . 
H 4 HOH 1   301 347 HOH HOH C . 
H 4 HOH 2   302 345 HOH HOH C . 
H 4 HOH 3   303 375 HOH HOH C . 
H 4 HOH 4   304 23  HOH HOH C . 
H 4 HOH 5   305 150 HOH HOH C . 
H 4 HOH 6   306 27  HOH HOH C . 
H 4 HOH 7   307 162 HOH HOH C . 
H 4 HOH 8   308 386 HOH HOH C . 
H 4 HOH 9   309 158 HOH HOH C . 
H 4 HOH 10  310 286 HOH HOH C . 
H 4 HOH 11  311 371 HOH HOH C . 
H 4 HOH 12  312 372 HOH HOH C . 
H 4 HOH 13  313 227 HOH HOH C . 
H 4 HOH 14  314 58  HOH HOH C . 
H 4 HOH 15  315 194 HOH HOH C . 
H 4 HOH 16  316 239 HOH HOH C . 
H 4 HOH 17  317 5   HOH HOH C . 
H 4 HOH 18  318 34  HOH HOH C . 
H 4 HOH 19  319 145 HOH HOH C . 
H 4 HOH 20  320 304 HOH HOH C . 
H 4 HOH 21  321 142 HOH HOH C . 
H 4 HOH 22  322 360 HOH HOH C . 
H 4 HOH 23  323 336 HOH HOH C . 
H 4 HOH 24  324 88  HOH HOH C . 
H 4 HOH 25  325 394 HOH HOH C . 
H 4 HOH 26  326 321 HOH HOH C . 
H 4 HOH 27  327 161 HOH HOH C . 
H 4 HOH 28  328 163 HOH HOH C . 
H 4 HOH 29  329 147 HOH HOH C . 
H 4 HOH 30  330 89  HOH HOH C . 
H 4 HOH 31  331 130 HOH HOH C . 
H 4 HOH 32  332 385 HOH HOH C . 
H 4 HOH 33  333 149 HOH HOH C . 
H 4 HOH 34  334 243 HOH HOH C . 
H 4 HOH 35  335 376 HOH HOH C . 
H 4 HOH 36  336 132 HOH HOH C . 
H 4 HOH 37  337 83  HOH HOH C . 
H 4 HOH 38  338 349 HOH HOH C . 
H 4 HOH 39  339 25  HOH HOH C . 
H 4 HOH 40  340 20  HOH HOH C . 
H 4 HOH 41  341 232 HOH HOH C . 
H 4 HOH 42  342 12  HOH HOH C . 
H 4 HOH 43  343 45  HOH HOH C . 
H 4 HOH 44  344 125 HOH HOH C . 
H 4 HOH 45  345 285 HOH HOH C . 
H 4 HOH 46  346 152 HOH HOH C . 
H 4 HOH 47  347 4   HOH HOH C . 
H 4 HOH 48  348 139 HOH HOH C . 
H 4 HOH 49  349 172 HOH HOH C . 
H 4 HOH 50  350 39  HOH HOH C . 
H 4 HOH 51  351 216 HOH HOH C . 
H 4 HOH 52  352 122 HOH HOH C . 
H 4 HOH 53  353 111 HOH HOH C . 
H 4 HOH 54  354 19  HOH HOH C . 
H 4 HOH 55  355 7   HOH HOH C . 
H 4 HOH 56  356 185 HOH HOH C . 
H 4 HOH 57  357 109 HOH HOH C . 
H 4 HOH 58  358 136 HOH HOH C . 
H 4 HOH 59  359 61  HOH HOH C . 
H 4 HOH 60  360 223 HOH HOH C . 
H 4 HOH 61  361 270 HOH HOH C . 
H 4 HOH 62  362 24  HOH HOH C . 
H 4 HOH 63  363 17  HOH HOH C . 
H 4 HOH 64  364 248 HOH HOH C . 
H 4 HOH 65  365 214 HOH HOH C . 
H 4 HOH 66  366 174 HOH HOH C . 
H 4 HOH 67  367 104 HOH HOH C . 
H 4 HOH 68  368 95  HOH HOH C . 
H 4 HOH 69  369 379 HOH HOH C . 
H 4 HOH 70  370 241 HOH HOH C . 
H 4 HOH 71  371 346 HOH HOH C . 
H 4 HOH 72  372 143 HOH HOH C . 
H 4 HOH 73  373 43  HOH HOH C . 
H 4 HOH 74  374 69  HOH HOH C . 
H 4 HOH 75  375 180 HOH HOH C . 
H 4 HOH 76  376 222 HOH HOH C . 
H 4 HOH 77  377 407 HOH HOH C . 
H 4 HOH 78  378 315 HOH HOH C . 
H 4 HOH 79  379 225 HOH HOH C . 
H 4 HOH 80  380 3   HOH HOH C . 
H 4 HOH 81  381 36  HOH HOH C . 
H 4 HOH 82  382 77  HOH HOH C . 
H 4 HOH 83  383 99  HOH HOH C . 
H 4 HOH 84  384 191 HOH HOH C . 
H 4 HOH 85  385 287 HOH HOH C . 
H 4 HOH 86  386 47  HOH HOH C . 
H 4 HOH 87  387 269 HOH HOH C . 
H 4 HOH 88  388 252 HOH HOH C . 
H 4 HOH 89  389 50  HOH HOH C . 
H 4 HOH 90  390 10  HOH HOH C . 
H 4 HOH 91  391 331 HOH HOH C . 
H 4 HOH 92  392 91  HOH HOH C . 
H 4 HOH 93  393 133 HOH HOH C . 
H 4 HOH 94  394 18  HOH HOH C . 
H 4 HOH 95  395 352 HOH HOH C . 
H 4 HOH 96  396 245 HOH HOH C . 
H 4 HOH 97  397 317 HOH HOH C . 
H 4 HOH 98  398 357 HOH HOH C . 
H 4 HOH 99  399 37  HOH HOH C . 
H 4 HOH 100 400 378 HOH HOH C . 
H 4 HOH 101 401 374 HOH HOH C . 
H 4 HOH 102 402 120 HOH HOH C . 
H 4 HOH 103 403 82  HOH HOH C . 
H 4 HOH 104 404 234 HOH HOH C . 
H 4 HOH 105 405 233 HOH HOH C . 
H 4 HOH 106 406 355 HOH HOH C . 
H 4 HOH 107 407 272 HOH HOH C . 
H 4 HOH 108 408 313 HOH HOH C . 
H 4 HOH 109 409 84  HOH HOH C . 
H 4 HOH 110 410 259 HOH HOH C . 
H 4 HOH 111 411 364 HOH HOH C . 
H 4 HOH 112 412 325 HOH HOH C . 
H 4 HOH 113 413 116 HOH HOH C . 
H 4 HOH 114 414 255 HOH HOH C . 
H 4 HOH 115 415 356 HOH HOH C . 
H 4 HOH 116 416 231 HOH HOH C . 
H 4 HOH 117 417 238 HOH HOH C . 
H 4 HOH 118 418 290 HOH HOH C . 
H 4 HOH 119 419 8   HOH HOH C . 
H 4 HOH 120 420 196 HOH HOH C . 
H 4 HOH 121 421 141 HOH HOH C . 
H 4 HOH 122 422 155 HOH HOH C . 
H 4 HOH 123 423 338 HOH HOH C . 
H 4 HOH 124 424 328 HOH HOH C . 
H 4 HOH 125 425 112 HOH HOH C . 
H 4 HOH 126 426 117 HOH HOH C . 
H 4 HOH 127 427 115 HOH HOH C . 
H 4 HOH 128 428 226 HOH HOH C . 
H 4 HOH 129 429 79  HOH HOH C . 
H 4 HOH 130 430 309 HOH HOH C . 
H 4 HOH 131 431 258 HOH HOH C . 
H 4 HOH 132 432 168 HOH HOH C . 
H 4 HOH 133 433 249 HOH HOH C . 
H 4 HOH 134 434 329 HOH HOH C . 
H 4 HOH 135 435 274 HOH HOH C . 
H 4 HOH 136 436 369 HOH HOH C . 
H 4 HOH 137 437 275 HOH HOH C . 
H 4 HOH 138 438 118 HOH HOH C . 
H 4 HOH 139 439 284 HOH HOH C . 
H 4 HOH 140 440 397 HOH HOH C . 
H 4 HOH 141 441 86  HOH HOH C . 
H 4 HOH 142 442 361 HOH HOH C . 
H 4 HOH 143 443 219 HOH HOH C . 
H 4 HOH 144 444 78  HOH HOH C . 
H 4 HOH 145 445 156 HOH HOH C . 
H 4 HOH 146 446 212 HOH HOH C . 
H 4 HOH 147 447 370 HOH HOH C . 
H 4 HOH 148 448 390 HOH HOH C . 
H 4 HOH 149 449 402 HOH HOH C . 
H 4 HOH 150 450 159 HOH HOH C . 
H 4 HOH 151 451 363 HOH HOH C . 
H 4 HOH 152 452 406 HOH HOH C . 
I 4 HOH 1   301 380 HOH HOH A . 
I 4 HOH 2   302 294 HOH HOH A . 
I 4 HOH 3   303 348 HOH HOH A . 
I 4 HOH 4   304 213 HOH HOH A . 
I 4 HOH 5   305 119 HOH HOH A . 
I 4 HOH 6   306 171 HOH HOH A . 
I 4 HOH 7   307 144 HOH HOH A . 
I 4 HOH 8   308 254 HOH HOH A . 
I 4 HOH 9   309 184 HOH HOH A . 
I 4 HOH 10  310 175 HOH HOH A . 
I 4 HOH 11  311 247 HOH HOH A . 
I 4 HOH 12  312 94  HOH HOH A . 
I 4 HOH 13  313 90  HOH HOH A . 
I 4 HOH 14  314 14  HOH HOH A . 
I 4 HOH 15  315 75  HOH HOH A . 
I 4 HOH 16  316 100 HOH HOH A . 
I 4 HOH 17  317 131 HOH HOH A . 
I 4 HOH 18  318 215 HOH HOH A . 
I 4 HOH 19  319 311 HOH HOH A . 
I 4 HOH 20  320 266 HOH HOH A . 
I 4 HOH 21  321 87  HOH HOH A . 
I 4 HOH 22  322 66  HOH HOH A . 
I 4 HOH 23  323 237 HOH HOH A . 
I 4 HOH 24  324 282 HOH HOH A . 
I 4 HOH 25  325 74  HOH HOH A . 
I 4 HOH 26  326 73  HOH HOH A . 
I 4 HOH 27  327 140 HOH HOH A . 
I 4 HOH 28  328 278 HOH HOH A . 
I 4 HOH 29  329 67  HOH HOH A . 
I 4 HOH 30  330 209 HOH HOH A . 
I 4 HOH 31  331 31  HOH HOH A . 
I 4 HOH 32  332 165 HOH HOH A . 
I 4 HOH 33  333 21  HOH HOH A . 
I 4 HOH 34  334 308 HOH HOH A . 
I 4 HOH 35  335 72  HOH HOH A . 
I 4 HOH 36  336 80  HOH HOH A . 
I 4 HOH 37  337 33  HOH HOH A . 
I 4 HOH 38  338 365 HOH HOH A . 
I 4 HOH 39  339 106 HOH HOH A . 
I 4 HOH 40  340 15  HOH HOH A . 
I 4 HOH 41  341 46  HOH HOH A . 
I 4 HOH 42  342 303 HOH HOH A . 
I 4 HOH 43  343 314 HOH HOH A . 
I 4 HOH 44  344 70  HOH HOH A . 
I 4 HOH 45  345 368 HOH HOH A . 
I 4 HOH 46  346 103 HOH HOH A . 
I 4 HOH 47  347 404 HOH HOH A . 
I 4 HOH 48  348 55  HOH HOH A . 
I 4 HOH 49  349 205 HOH HOH A . 
I 4 HOH 50  350 146 HOH HOH A . 
I 4 HOH 51  351 11  HOH HOH A . 
I 4 HOH 52  352 160 HOH HOH A . 
I 4 HOH 53  353 35  HOH HOH A . 
I 4 HOH 54  354 108 HOH HOH A . 
I 4 HOH 55  355 208 HOH HOH A . 
I 4 HOH 56  356 134 HOH HOH A . 
I 4 HOH 57  357 319 HOH HOH A . 
I 4 HOH 58  358 211 HOH HOH A . 
I 4 HOH 59  359 242 HOH HOH A . 
I 4 HOH 60  360 151 HOH HOH A . 
I 4 HOH 61  361 384 HOH HOH A . 
I 4 HOH 62  362 16  HOH HOH A . 
I 4 HOH 63  363 54  HOH HOH A . 
I 4 HOH 64  364 48  HOH HOH A . 
I 4 HOH 65  365 59  HOH HOH A . 
I 4 HOH 66  366 398 HOH HOH A . 
I 4 HOH 67  367 137 HOH HOH A . 
I 4 HOH 68  368 267 HOH HOH A . 
I 4 HOH 69  369 179 HOH HOH A . 
I 4 HOH 70  370 265 HOH HOH A . 
I 4 HOH 71  371 288 HOH HOH A . 
I 4 HOH 72  372 221 HOH HOH A . 
I 4 HOH 73  373 138 HOH HOH A . 
I 4 HOH 74  374 301 HOH HOH A . 
I 4 HOH 75  375 198 HOH HOH A . 
I 4 HOH 76  376 362 HOH HOH A . 
I 4 HOH 77  377 253 HOH HOH A . 
I 4 HOH 78  378 154 HOH HOH A . 
I 4 HOH 79  379 81  HOH HOH A . 
I 4 HOH 80  380 381 HOH HOH A . 
I 4 HOH 81  381 341 HOH HOH A . 
I 4 HOH 82  382 279 HOH HOH A . 
I 4 HOH 83  383 343 HOH HOH A . 
I 4 HOH 84  384 318 HOH HOH A . 
I 4 HOH 85  385 322 HOH HOH A . 
I 4 HOH 86  386 167 HOH HOH A . 
I 4 HOH 87  387 244 HOH HOH A . 
I 4 HOH 88  388 330 HOH HOH A . 
I 4 HOH 89  389 189 HOH HOH A . 
I 4 HOH 90  390 403 HOH HOH A . 
I 4 HOH 91  391 135 HOH HOH A . 
I 4 HOH 92  392 296 HOH HOH A . 
I 4 HOH 93  393 354 HOH HOH A . 
I 4 HOH 94  394 358 HOH HOH A . 
I 4 HOH 95  395 263 HOH HOH A . 
I 4 HOH 96  396 367 HOH HOH A . 
I 4 HOH 97  397 395 HOH HOH A . 
I 4 HOH 98  398 334 HOH HOH A . 
I 4 HOH 99  399 210 HOH HOH A . 
I 4 HOH 100 400 188 HOH HOH A . 
I 4 HOH 101 401 85  HOH HOH A . 
I 4 HOH 102 402 199 HOH HOH A . 
I 4 HOH 103 403 391 HOH HOH A . 
I 4 HOH 104 404 323 HOH HOH A . 
I 4 HOH 105 405 230 HOH HOH A . 
I 4 HOH 106 406 148 HOH HOH A . 
I 4 HOH 107 407 280 HOH HOH A . 
I 4 HOH 108 408 236 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.21.2_5419 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NF3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     59.534 
_cell.length_a_esd                 ? 
_cell.length_b                     99.939 
_cell.length_b_esd                 ? 
_cell.length_c                     142.794 
_cell.length_c_esd                 ? 
_cell.volume                       849591.233 
_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                         9NF3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            'C 2c 2' 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9NF3 
_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             1.91 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          35.50 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M ammonium sulfate 20% w/v PEG 3,353' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_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 EIGER2 S 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         2021-07-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.13 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 21-ID-D' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.13 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-D 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          23.74 
_reflns.entry_id                                       9NF3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.00 
_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                                     36388 
_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                           90.69 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          13.3 
_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                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1251 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.375 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               27.39 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NF3 
_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                            1.80 
_refine.ls_d_res_low                             29.77 
_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                     36018 
_refine.ls_number_reflns_R_free                  1973 
_refine.ls_number_reflns_R_work                  34045 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    90.69 
_refine.ls_percent_reflns_R_free                 5.48 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1828 
_refine.ls_R_factor_R_free                       0.2238 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1804 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.7431 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2114 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        29.77 
_refine_hist.number_atoms_solvent             406 
_refine_hist.number_atoms_total               3853 
_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        3430 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         17 
_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' ? 0.0080  ? 3539 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0057  ? 4794 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0624  ? 498  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0086  ? 643  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 16.9484 ? 1269 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.85  . . 104 1703 64.70 . . . . 0.2872 . . . . . . . . . . . . . . . 0.3699 
'X-RAY DIFFRACTION' 1.85 1.90  . . 103 2018 75.83 . . . . 0.2499 . . . . . . . . . . . . . . . 0.2763 
'X-RAY DIFFRACTION' 1.90 1.95  . . 142 2224 84.47 . . . . 0.2326 . . . . . . . . . . . . . . . 0.2809 
'X-RAY DIFFRACTION' 1.95 2.02  . . 142 2429 91.66 . . . . 0.2227 . . . . . . . . . . . . . . . 0.2645 
'X-RAY DIFFRACTION' 2.02 2.09  . . 142 2588 96.60 . . . . 0.1905 . . . . . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 2.09 2.17  . . 159 2613 98.96 . . . . 0.1873 . . . . . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 2.17 2.27  . . 154 2632 98.90 . . . . 0.1788 . . . . . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 2.27 2.39  . . 150 2619 98.44 . . . . 0.1815 . . . . . . . . . . . . . . . 0.2348 
'X-RAY DIFFRACTION' 2.39 2.54  . . 151 2625 98.34 . . . . 0.1854 . . . . . . . . . . . . . . . 0.2146 
'X-RAY DIFFRACTION' 2.54 2.74  . . 147 2594 96.72 . . . . 0.1848 . . . . . . . . . . . . . . . 0.2506 
'X-RAY DIFFRACTION' 2.74 3.01  . . 143 2567 95.19 . . . . 0.1842 . . . . . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 3.01 3.45  . . 150 2488 92.17 . . . . 0.1704 . . . . . . . . . . . . . . . 0.2209 
'X-RAY DIFFRACTION' 3.45 4.34  . . 136 2398 87.89 . . . . 0.1501 . . . . . . . . . . . . . . . 0.1812 
'X-RAY DIFFRACTION' 4.34 29.77 . . 150 2547 89.60 . . . . 0.1729 . . . . . . . . . . . . . . . 0.2106 
# 
_struct.entry_id                     9NF3 
_struct.title                        
'cis-CaaD E114D mutant with a covalent ethylene intermediate of the hydration and decarboxylation of cis-3-chloroacrylic acid' 
_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        9NF3 
_struct_keywords.text            'cis-CaaD, tautomerase, acetylenecarboxylic acid, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Q6VPE5_9CORY Q6VPE5 ? 1 
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRT
;
2 
2 UNP Q6VPE5_9CORY Q6VPE5 ? 2 
;PVYMVYVSQDRLTPSAKHAVAKAITDAHRGLTGTQHFLAQVNFQEQPAGNVFLGGVQQGGDTIFVHGLHREGRSADLKGQ
LAQRIVDDVSVAAEIDRKHIWVYFGEMPAQQMVEYGRFLPQPGHEGEWFDNLSSDERAFMETNVDVSRT
;
2 
# 
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 9NF3 B 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
2 2 9NF3 C 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
3 1 9NF3 A 1 ? 149 ? Q6VPE5 2 ? 150 ? 1 149 
# 
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 9NF3 ASP B 114 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 1  
1 9NF3 GLU B 150 ? UNP Q6VPE5 ?   ?   'expression tag'      150 2  
1 9NF3 ASN B 151 ? UNP Q6VPE5 ?   ?   'expression tag'      151 3  
1 9NF3 LEU B 152 ? UNP Q6VPE5 ?   ?   'expression tag'      152 4  
1 9NF3 TYR B 153 ? UNP Q6VPE5 ?   ?   'expression tag'      153 5  
1 9NF3 PHE B 154 ? UNP Q6VPE5 ?   ?   'expression tag'      154 6  
1 9NF3 GLN B 155 ? UNP Q6VPE5 ?   ?   'expression tag'      155 7  
1 9NF3 GLY B 156 ? UNP Q6VPE5 ?   ?   'expression tag'      156 8  
1 9NF3 LEU B 157 ? UNP Q6VPE5 ?   ?   'expression tag'      157 9  
1 9NF3 GLU B 158 ? UNP Q6VPE5 ?   ?   'expression tag'      158 10 
1 9NF3 HIS B 159 ? UNP Q6VPE5 ?   ?   'expression tag'      159 11 
1 9NF3 HIS B 160 ? UNP Q6VPE5 ?   ?   'expression tag'      160 12 
1 9NF3 HIS B 161 ? UNP Q6VPE5 ?   ?   'expression tag'      161 13 
1 9NF3 HIS B 162 ? UNP Q6VPE5 ?   ?   'expression tag'      162 14 
1 9NF3 HIS B 163 ? UNP Q6VPE5 ?   ?   'expression tag'      163 15 
1 9NF3 HIS B 164 ? UNP Q6VPE5 ?   ?   'expression tag'      164 16 
2 9NF3 ASP C 114 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 17 
2 9NF3 GLU C 150 ? UNP Q6VPE5 ?   ?   'expression tag'      150 18 
2 9NF3 ASN C 151 ? UNP Q6VPE5 ?   ?   'expression tag'      151 19 
2 9NF3 LEU C 152 ? UNP Q6VPE5 ?   ?   'expression tag'      152 20 
2 9NF3 TYR C 153 ? UNP Q6VPE5 ?   ?   'expression tag'      153 21 
2 9NF3 PHE C 154 ? UNP Q6VPE5 ?   ?   'expression tag'      154 22 
2 9NF3 GLN C 155 ? UNP Q6VPE5 ?   ?   'expression tag'      155 23 
2 9NF3 GLY C 156 ? UNP Q6VPE5 ?   ?   'expression tag'      156 24 
2 9NF3 LEU C 157 ? UNP Q6VPE5 ?   ?   'expression tag'      157 25 
2 9NF3 GLU C 158 ? UNP Q6VPE5 ?   ?   'expression tag'      158 26 
2 9NF3 HIS C 159 ? UNP Q6VPE5 ?   ?   'expression tag'      159 27 
2 9NF3 HIS C 160 ? UNP Q6VPE5 ?   ?   'expression tag'      160 28 
2 9NF3 HIS C 161 ? UNP Q6VPE5 ?   ?   'expression tag'      161 29 
2 9NF3 HIS C 162 ? UNP Q6VPE5 ?   ?   'expression tag'      162 30 
2 9NF3 HIS C 163 ? UNP Q6VPE5 ?   ?   'expression tag'      163 31 
2 9NF3 HIS C 164 ? UNP Q6VPE5 ?   ?   'expression tag'      164 32 
3 9NF3 ASP A 114 ? UNP Q6VPE5 GLU 115 'engineered mutation' 114 33 
3 9NF3 GLU A 150 ? UNP Q6VPE5 ?   ?   'expression tag'      150 34 
3 9NF3 ASN A 151 ? UNP Q6VPE5 ?   ?   'expression tag'      151 35 
3 9NF3 LEU A 152 ? UNP Q6VPE5 ?   ?   'expression tag'      152 36 
3 9NF3 TYR A 153 ? UNP Q6VPE5 ?   ?   'expression tag'      153 37 
3 9NF3 PHE A 154 ? UNP Q6VPE5 ?   ?   'expression tag'      154 38 
3 9NF3 GLN A 155 ? UNP Q6VPE5 ?   ?   'expression tag'      155 39 
3 9NF3 GLY A 156 ? UNP Q6VPE5 ?   ?   'expression tag'      156 40 
3 9NF3 LEU A 157 ? UNP Q6VPE5 ?   ?   'expression tag'      157 41 
3 9NF3 GLU A 158 ? UNP Q6VPE5 ?   ?   'expression tag'      158 42 
3 9NF3 HIS A 159 ? UNP Q6VPE5 ?   ?   'expression tag'      159 43 
3 9NF3 HIS A 160 ? UNP Q6VPE5 ?   ?   'expression tag'      160 44 
3 9NF3 HIS A 161 ? UNP Q6VPE5 ?   ?   'expression tag'      161 45 
3 9NF3 HIS A 162 ? UNP Q6VPE5 ?   ?   'expression tag'      162 46 
3 9NF3 HIS A 163 ? UNP Q6VPE5 ?   ?   'expression tag'      163 47 
3 9NF3 HIS A 164 ? UNP Q6VPE5 ?   ?   'expression tag'      164 48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
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)' 9050  ? 
1 MORE         -107  ? 
1 'SSA (A^2)'  15360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 THR A 13  ? GLY A 33  ? THR B 13  GLY B 33  1 ? 21 
HELX_P HELX_P2  AA2 GLN A 35  ? LEU A 38  ? GLN B 35  LEU B 38  5 ? 4  
HELX_P HELX_P3  AA3 SER A 74  ? ALA A 93  ? SER B 74  ALA B 93  1 ? 20 
HELX_P HELX_P4  AA4 ASP A 96  ? LYS A 98  ? ASP B 96  LYS B 98  5 ? 3  
HELX_P HELX_P5  AA5 PRO A 108 ? GLN A 110 ? PRO B 108 GLN B 110 5 ? 3  
HELX_P HELX_P6  AA6 GLN A 121 ? GLY A 123 ? GLN B 121 GLY B 123 5 ? 3  
HELX_P HELX_P7  AA7 HIS A 124 ? ASN A 131 ? HIS B 124 ASN B 131 1 ? 8  
HELX_P HELX_P8  AA8 SER A 133 ? ASN A 143 ? SER B 133 ASN B 143 1 ? 11 
HELX_P HELX_P9  AA9 THR B 13  ? GLY B 33  ? THR C 13  GLY C 33  1 ? 21 
HELX_P HELX_P10 AB1 GLN B 35  ? LEU B 38  ? GLN C 35  LEU C 38  5 ? 4  
HELX_P HELX_P11 AB2 SER B 74  ? GLU B 94  ? SER C 74  GLU C 94  1 ? 21 
HELX_P HELX_P12 AB3 ASP B 96  ? LYS B 98  ? ASP C 96  LYS C 98  5 ? 3  
HELX_P HELX_P13 AB4 PRO B 108 ? GLN B 110 ? PRO C 108 GLN C 110 5 ? 3  
HELX_P HELX_P14 AB5 HIS B 124 ? ASN B 131 ? HIS C 124 ASN C 131 1 ? 8  
HELX_P HELX_P15 AB6 SER B 133 ? ASN B 143 ? SER C 133 ASN C 143 1 ? 11 
HELX_P HELX_P16 AB7 THR C 13  ? GLY C 33  ? THR A 13  GLY A 33  1 ? 21 
HELX_P HELX_P17 AB8 GLN C 35  ? LEU C 38  ? GLN A 35  LEU A 38  5 ? 4  
HELX_P HELX_P18 AB9 SER C 74  ? GLU C 94  ? SER A 74  GLU A 94  1 ? 21 
HELX_P HELX_P19 AC1 ASP C 96  ? LYS C 98  ? ASP A 96  LYS A 98  5 ? 3  
HELX_P HELX_P20 AC2 PRO C 108 ? GLN C 110 ? PRO A 108 GLN A 110 5 ? 3  
HELX_P HELX_P21 AC3 HIS C 124 ? LEU C 132 ? HIS A 124 LEU A 132 1 ? 9  
HELX_P HELX_P22 AC4 SER C 133 ? THR C 142 ? SER A 133 THR A 142 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        both 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           B 
_struct_conn.ptnr1_label_comp_id           N80 
_struct_conn.ptnr1_label_seq_id            1 
_struct_conn.ptnr1_label_atom_id           C 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           VAL 
_struct_conn.ptnr2_label_seq_id            2 
_struct_conn.ptnr2_label_atom_id           N 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            C 
_struct_conn.ptnr1_auth_comp_id            N80 
_struct_conn.ptnr1_auth_seq_id             1 
_struct_conn.ptnr2_auth_asym_id            C 
_struct_conn.ptnr2_auth_comp_id            VAL 
_struct_conn.ptnr2_auth_seq_id             2 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.328 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      N80 
_pdbx_modification_feature.label_asym_id                      B 
_pdbx_modification_feature.label_seq_id                       1 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     . 
_pdbx_modification_feature.modified_residue_label_asym_id     . 
_pdbx_modification_feature.modified_residue_label_seq_id      . 
_pdbx_modification_feature.modified_residue_label_alt_id      . 
_pdbx_modification_feature.auth_comp_id                       N80 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        1 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      . 
_pdbx_modification_feature.modified_residue_auth_asym_id      . 
_pdbx_modification_feature.modified_residue_auth_seq_id       . 
_pdbx_modification_feature.modified_residue_PDB_ins_code      . 
_pdbx_modification_feature.modified_residue_symmetry          . 
_pdbx_modification_feature.comp_id_linking_atom               . 
_pdbx_modification_feature.modified_residue_id_linking_atom   . 
_pdbx_modification_feature.modified_residue_id                PRO 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        N80 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Non-standard residue' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
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 ? parallel      
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? parallel      
AA2 6 7 ? anti-parallel 
AA2 7 8 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? parallel      
AA3 4 5 ? anti-parallel 
AA3 5 6 ? parallel      
AA3 6 7 ? anti-parallel 
AA3 7 8 ? 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 VAL B 56  ? GLN B 57  ? VAL C 56  GLN C 57  
AA1 2 VAL B 51  ? LEU B 53  ? VAL C 51  LEU C 53  
AA1 3 GLN A 40  ? GLN A 46  ? GLN B 40  GLN B 46  
AA1 4 VAL A 2   ? SER A 8   ? VAL B 2   SER B 8   
AA1 5 ILE A 63  ? ARG A 70  ? ILE B 63  ARG B 70  
AA1 6 ILE A 100 ? MET A 107 ? ILE B 100 MET B 107 
AA1 7 MET C 112 ? ASP C 114 ? MET A 112 ASP A 114 
AA1 8 ARG C 117 ? PHE C 118 ? ARG A 117 PHE A 118 
AA2 1 VAL A 56  ? GLN A 57  ? VAL B 56  GLN B 57  
AA2 2 VAL A 51  ? LEU A 53  ? VAL B 51  LEU B 53  
AA2 3 GLN C 40  ? GLN C 46  ? GLN A 40  GLN A 46  
AA2 4 VAL C 2   ? SER C 8   ? VAL A 2   SER A 8   
AA2 5 ILE C 63  ? ARG C 70  ? ILE A 63  ARG A 70  
AA2 6 ILE C 100 ? MET C 107 ? ILE A 100 MET A 107 
AA2 7 MET B 112 ? ASP B 114 ? MET C 112 ASP C 114 
AA2 8 ARG B 117 ? PHE B 118 ? ARG C 117 PHE C 118 
AA3 1 ARG A 117 ? PHE A 118 ? ARG B 117 PHE B 118 
AA3 2 MET A 112 ? ASP A 114 ? MET B 112 ASP B 114 
AA3 3 ILE B 100 ? MET B 107 ? ILE C 100 MET C 107 
AA3 4 ILE B 63  ? ARG B 70  ? ILE C 63  ARG C 70  
AA3 5 VAL B 2   ? SER B 8   ? VAL C 2   SER C 8   
AA3 6 GLN B 40  ? GLN B 46  ? GLN C 40  GLN C 46  
AA3 7 VAL C 51  ? LEU C 53  ? VAL A 51  LEU A 53  
AA3 8 VAL C 56  ? GLN C 57  ? VAL A 56  GLN A 57  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL B 56  ? O VAL C 56  N LEU B 53  ? N LEU C 53  
AA1 2 3 O PHE B 52  ? O PHE C 52  N VAL A 41  ? N VAL B 41  
AA1 3 4 O GLN A 44  ? O GLN B 44  N VAL A 5   ? N VAL B 5   
AA1 4 5 N MET A 4   ? N MET B 4   O HIS A 66  ? O HIS B 66  
AA1 5 6 N GLY A 67  ? N GLY B 67  O GLY A 105 ? O GLY B 105 
AA1 6 7 N VAL A 102 ? N VAL B 102 O VAL C 113 ? O VAL A 113 
AA1 7 8 N ASP C 114 ? N ASP A 114 O ARG C 117 ? O ARG A 117 
AA2 1 2 O VAL A 56  ? O VAL B 56  N LEU A 53  ? N LEU B 53  
AA2 2 3 N PHE A 52  ? N PHE B 52  O VAL C 41  ? O VAL A 41  
AA2 3 4 O GLN C 40  ? O GLN A 40  N TYR C 3   ? N TYR A 3   
AA2 4 5 N TYR C 6   ? N TYR A 6   O PHE C 64  ? O PHE A 64  
AA2 5 6 N HIS C 69  ? N HIS A 69  O GLY C 105 ? O GLY A 105 
AA2 6 7 O VAL C 102 ? O VAL A 102 N VAL B 113 ? N VAL C 113 
AA2 7 8 N ASP B 114 ? N ASP C 114 O ARG B 117 ? O ARG C 117 
AA3 1 2 O ARG A 117 ? O ARG B 117 N ASP A 114 ? N ASP B 114 
AA3 2 3 N VAL A 113 ? N VAL B 113 O VAL B 102 ? O VAL C 102 
AA3 3 4 O GLY B 105 ? O GLY C 105 N GLY B 67  ? N GLY C 67  
AA3 4 5 O HIS B 66  ? O HIS C 66  N MET B 4   ? N MET C 4   
AA3 5 6 N TYR B 3   ? N TYR C 3   O ASN B 42  ? O ASN C 42  
AA3 6 7 N VAL B 41  ? N VAL C 41  O PHE C 52  ? O PHE A 52  
AA3 7 8 N LEU C 53  ? N LEU A 53  O VAL C 56  ? O VAL A 56  
# 
_pdbx_entry_details.entry_id                   9NF3 
_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   Y 
# 
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 O   B HOH 404 ? ? O  B HOH 437 ? ? 1.81 
2  1 O   B HOH 376 ? ? O  B HOH 437 ? ? 1.89 
3  1 O   B HOH 376 ? ? O  B HOH 404 ? ? 1.91 
4  1 NH1 B ARG 29  ? B O  B HOH 301 ? ? 1.94 
5  1 NH1 C ARG 73  ? ? O1 C SO4 201 ? ? 1.95 
6  1 O   B HOH 400 ? ? O  B HOH 406 ? ? 1.99 
7  1 NH1 A ARG 29  ? ? O  A HOH 301 ? ? 2.00 
8  1 O   B HOH 385 ? ? O  B HOH 390 ? ? 2.00 
9  1 ND2 C ASN 131 ? ? O  C HOH 301 ? ? 2.01 
10 1 OD2 A ASP 135 ? ? O  A HOH 302 ? ? 2.05 
11 1 OE1 B GLN 80  ? ? O  B HOH 302 ? ? 2.08 
12 1 O   B HOH 357 ? ? O  B HOH 417 ? ? 2.09 
13 1 OD2 C ASP 61  ? ? O  C HOH 302 ? ? 2.09 
14 1 O   C HOH 352 ? ? O  C HOH 384 ? ? 2.11 
15 1 O   C HOH 313 ? ? O  C HOH 332 ? ? 2.12 
16 1 O   C HOH 415 ? ? O  C HOH 436 ? ? 2.13 
17 1 O   B HOH 336 ? ? O  B HOH 416 ? ? 2.13 
18 1 OE1 A GLU 141 ? ? O  A HOH 303 ? ? 2.14 
19 1 O   B HOH 301 ? ? O  B HOH 309 ? ? 2.14 
20 1 O   C HOH 378 ? ? O  C HOH 413 ? ? 2.15 
21 1 O   A HOH 355 ? ? O  A HOH 405 ? ? 2.16 
22 1 O   B PRO 122 ? ? N  B HIS 124 ? ? 2.16 
23 1 O   A HOH 377 ? ? O  A HOH 399 ? ? 2.17 
24 1 OE1 B GLN 9   ? ? O  B HOH 303 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 437 ? ? 1_555 O C HOH 413 ? ? 3_554 1.93 
2 1 O B HOH 343 ? ? 1_555 O B HOH 429 ? ? 3_554 2.03 
3 1 O B HOH 404 ? ? 1_555 O C HOH 413 ? ? 3_554 2.19 
# 
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 10  ? ? 78.39  -5.53   
2 1 GLU B 94  ? ? 38.31  62.63   
3 1 PRO B 122 ? ? -38.23 -100.64 
4 1 ASN B 143 ? ? -95.27 57.11   
5 1 ASN C 143 ? ? -91.41 57.57   
6 1 ASN A 143 ? ? -96.19 55.48   
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    B 
_pdbx_struct_mod_residue.label_comp_id    N80 
_pdbx_struct_mod_residue.label_seq_id     1 
_pdbx_struct_mod_residue.auth_asym_id     C 
_pdbx_struct_mod_residue.auth_comp_id     N80 
_pdbx_struct_mod_residue.auth_seq_id      1 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   PRO 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     408 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   I 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z+1/2         
4 -x,-y,z+1/2         
5 x+1/2,y+1/2,z       
6 x+1/2,-y+1/2,-z     
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       452 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.01 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 VAL 146 ? A VAL 146 
2  1 Y 1 B SER 147 ? A SER 147 
3  1 Y 1 B ARG 148 ? A ARG 148 
4  1 Y 1 B THR 149 ? A THR 149 
5  1 Y 1 B GLU 150 ? A GLU 150 
6  1 Y 1 B ASN 151 ? A ASN 151 
7  1 Y 1 B LEU 152 ? A LEU 152 
8  1 Y 1 B TYR 153 ? A TYR 153 
9  1 Y 1 B PHE 154 ? A PHE 154 
10 1 Y 1 B GLN 155 ? A GLN 155 
11 1 Y 1 B GLY 156 ? A GLY 156 
12 1 Y 1 B LEU 157 ? A LEU 157 
13 1 Y 1 B GLU 158 ? A GLU 158 
14 1 Y 1 B HIS 159 ? A HIS 159 
15 1 Y 1 B HIS 160 ? A HIS 160 
16 1 Y 1 B HIS 161 ? A HIS 161 
17 1 Y 1 B HIS 162 ? A HIS 162 
18 1 Y 1 B HIS 163 ? A HIS 163 
19 1 Y 1 B HIS 164 ? A HIS 164 
20 1 Y 1 C SER 147 ? B SER 147 
21 1 Y 1 C ARG 148 ? B ARG 148 
22 1 Y 1 C THR 149 ? B THR 149 
23 1 Y 1 C GLU 150 ? B GLU 150 
24 1 Y 1 C ASN 151 ? B ASN 151 
25 1 Y 1 C LEU 152 ? B LEU 152 
26 1 Y 1 C TYR 153 ? B TYR 153 
27 1 Y 1 C PHE 154 ? B PHE 154 
28 1 Y 1 C GLN 155 ? B GLN 155 
29 1 Y 1 C GLY 156 ? B GLY 156 
30 1 Y 1 C LEU 157 ? B LEU 157 
31 1 Y 1 C GLU 158 ? B GLU 158 
32 1 Y 1 C HIS 159 ? B HIS 159 
33 1 Y 1 C HIS 160 ? B HIS 160 
34 1 Y 1 C HIS 161 ? B HIS 161 
35 1 Y 1 C HIS 162 ? B HIS 162 
36 1 Y 1 C HIS 163 ? B HIS 163 
37 1 Y 1 C HIS 164 ? B HIS 164 
38 1 Y 1 A VAL 146 ? C VAL 146 
39 1 Y 1 A SER 147 ? C SER 147 
40 1 Y 1 A ARG 148 ? C ARG 148 
41 1 Y 1 A THR 149 ? C THR 149 
42 1 Y 1 A GLU 150 ? C GLU 150 
43 1 Y 1 A ASN 151 ? C ASN 151 
44 1 Y 1 A LEU 152 ? C LEU 152 
45 1 Y 1 A TYR 153 ? C TYR 153 
46 1 Y 1 A PHE 154 ? C PHE 154 
47 1 Y 1 A GLN 155 ? C GLN 155 
48 1 Y 1 A GLY 156 ? C GLY 156 
49 1 Y 1 A LEU 157 ? C LEU 157 
50 1 Y 1 A GLU 158 ? C GLU 158 
51 1 Y 1 A HIS 159 ? C HIS 159 
52 1 Y 1 A HIS 160 ? C HIS 160 
53 1 Y 1 A HIS 161 ? C HIS 161 
54 1 Y 1 A HIS 162 ? C HIS 162 
55 1 Y 1 A HIS 163 ? C HIS 163 
56 1 Y 1 A HIS 164 ? C HIS 164 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
N80 O    O N N 236 
N80 C    C N N 237 
N80 CA   C N S 238 
N80 CB   C N N 239 
N80 CG   C N N 240 
N80 CD   C N N 241 
N80 N    N N N 242 
N80 CAD  C N N 243 
N80 CAA  C N N 244 
N80 OXT  O N N 245 
N80 HA   H N N 246 
N80 H1   H N N 247 
N80 H3   H N N 248 
N80 H4   H N N 249 
N80 H5   H N N 250 
N80 H6   H N N 251 
N80 H7   H N N 252 
N80 H8   H N N 253 
N80 H9   H N N 254 
N80 H10  H N N 255 
N80 HXT  H N N 256 
PHE N    N N N 257 
PHE CA   C N S 258 
PHE C    C N N 259 
PHE O    O N N 260 
PHE CB   C N N 261 
PHE CG   C Y N 262 
PHE CD1  C Y N 263 
PHE CD2  C Y N 264 
PHE CE1  C Y N 265 
PHE CE2  C Y N 266 
PHE CZ   C Y N 267 
PHE OXT  O N N 268 
PHE H    H N N 269 
PHE H2   H N N 270 
PHE HA   H N N 271 
PHE HB2  H N N 272 
PHE HB3  H N N 273 
PHE HD1  H N N 274 
PHE HD2  H N N 275 
PHE HE1  H N N 276 
PHE HE2  H N N 277 
PHE HZ   H N N 278 
PHE HXT  H N N 279 
PRO N    N N N 280 
PRO CA   C N S 281 
PRO C    C N N 282 
PRO O    O N N 283 
PRO CB   C N N 284 
PRO CG   C N N 285 
PRO CD   C N N 286 
PRO OXT  O N N 287 
PRO H    H N N 288 
PRO HA   H N N 289 
PRO HB2  H N N 290 
PRO HB3  H N N 291 
PRO HG2  H N N 292 
PRO HG3  H N N 293 
PRO HD2  H N N 294 
PRO HD3  H N N 295 
PRO HXT  H N N 296 
SER N    N N N 297 
SER CA   C N S 298 
SER C    C N N 299 
SER O    O N N 300 
SER CB   C N N 301 
SER OG   O N N 302 
SER OXT  O N N 303 
SER H    H N N 304 
SER H2   H N N 305 
SER HA   H N N 306 
SER HB2  H N N 307 
SER HB3  H N N 308 
SER HG   H N N 309 
SER HXT  H N N 310 
SO4 S    S N N 311 
SO4 O1   O N N 312 
SO4 O2   O N N 313 
SO4 O3   O N N 314 
SO4 O4   O N N 315 
THR N    N N N 316 
THR CA   C N S 317 
THR C    C N N 318 
THR O    O N N 319 
THR CB   C N R 320 
THR OG1  O N N 321 
THR CG2  C N N 322 
THR OXT  O N N 323 
THR H    H N N 324 
THR H2   H N N 325 
THR HA   H N N 326 
THR HB   H N N 327 
THR HG1  H N N 328 
THR HG21 H N N 329 
THR HG22 H N N 330 
THR HG23 H N N 331 
THR HXT  H N N 332 
TRP N    N N N 333 
TRP CA   C N S 334 
TRP C    C N N 335 
TRP O    O N N 336 
TRP CB   C N N 337 
TRP CG   C Y N 338 
TRP CD1  C Y N 339 
TRP CD2  C Y N 340 
TRP NE1  N Y N 341 
TRP CE2  C Y N 342 
TRP CE3  C Y N 343 
TRP CZ2  C Y N 344 
TRP CZ3  C Y N 345 
TRP CH2  C Y N 346 
TRP OXT  O N N 347 
TRP H    H N N 348 
TRP H2   H N N 349 
TRP HA   H N N 350 
TRP HB2  H N N 351 
TRP HB3  H N N 352 
TRP HD1  H N N 353 
TRP HE1  H N N 354 
TRP HE3  H N N 355 
TRP HZ2  H N N 356 
TRP HZ3  H N N 357 
TRP HH2  H N N 358 
TRP HXT  H N N 359 
TYR N    N N N 360 
TYR CA   C N S 361 
TYR C    C N N 362 
TYR O    O N N 363 
TYR CB   C N N 364 
TYR CG   C Y N 365 
TYR CD1  C Y N 366 
TYR CD2  C Y N 367 
TYR CE1  C Y N 368 
TYR CE2  C Y N 369 
TYR CZ   C Y N 370 
TYR OH   O N N 371 
TYR OXT  O N N 372 
TYR H    H N N 373 
TYR H2   H N N 374 
TYR HA   H N N 375 
TYR HB2  H N N 376 
TYR HB3  H N N 377 
TYR HD1  H N N 378 
TYR HD2  H N N 379 
TYR HE1  H N N 380 
TYR HE2  H N N 381 
TYR HH   H N N 382 
TYR HXT  H N N 383 
VAL N    N N N 384 
VAL CA   C N S 385 
VAL C    C N N 386 
VAL O    O N N 387 
VAL CB   C N N 388 
VAL CG1  C N N 389 
VAL CG2  C N N 390 
VAL OXT  O N N 391 
VAL H    H N N 392 
VAL H2   H N N 393 
VAL HA   H N N 394 
VAL HB   H N N 395 
VAL HG11 H N N 396 
VAL HG12 H N N 397 
VAL HG13 H N N 398 
VAL HG21 H N N 399 
VAL HG22 H N N 400 
VAL HG23 H N N 401 
VAL HXT  H N N 402 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
N80 O   C    doub N N 224 
N80 C   CA   sing N N 225 
N80 CB  CG   sing N N 226 
N80 CB  CA   sing N N 227 
N80 CG  CD   sing N N 228 
N80 CA  N    sing N N 229 
N80 N   CD   sing N N 230 
N80 N   CAD  sing N N 231 
N80 CAD CAA  doub N N 232 
N80 C   OXT  sing N N 233 
N80 CA  HA   sing N N 234 
N80 CB  H1   sing N N 235 
N80 CB  H3   sing N N 236 
N80 CG  H4   sing N N 237 
N80 CG  H5   sing N N 238 
N80 CD  H6   sing N N 239 
N80 CD  H7   sing N N 240 
N80 CAD H8   sing N N 241 
N80 CAA H9   sing N N 242 
N80 CAA H10  sing N N 243 
N80 OXT HXT  sing N N 244 
PHE N   CA   sing N N 245 
PHE N   H    sing N N 246 
PHE N   H2   sing N N 247 
PHE CA  C    sing N N 248 
PHE CA  CB   sing N N 249 
PHE CA  HA   sing N N 250 
PHE C   O    doub N N 251 
PHE C   OXT  sing N N 252 
PHE CB  CG   sing N N 253 
PHE CB  HB2  sing N N 254 
PHE CB  HB3  sing N N 255 
PHE CG  CD1  doub Y N 256 
PHE CG  CD2  sing Y N 257 
PHE CD1 CE1  sing Y N 258 
PHE CD1 HD1  sing N N 259 
PHE CD2 CE2  doub Y N 260 
PHE CD2 HD2  sing N N 261 
PHE CE1 CZ   doub Y N 262 
PHE CE1 HE1  sing N N 263 
PHE CE2 CZ   sing Y N 264 
PHE CE2 HE2  sing N N 265 
PHE CZ  HZ   sing N N 266 
PHE OXT HXT  sing N N 267 
PRO N   CA   sing N N 268 
PRO N   CD   sing N N 269 
PRO N   H    sing N N 270 
PRO CA  C    sing N N 271 
PRO CA  CB   sing N N 272 
PRO CA  HA   sing N N 273 
PRO C   O    doub N N 274 
PRO C   OXT  sing N N 275 
PRO CB  CG   sing N N 276 
PRO CB  HB2  sing N N 277 
PRO CB  HB3  sing N N 278 
PRO CG  CD   sing N N 279 
PRO CG  HG2  sing N N 280 
PRO CG  HG3  sing N N 281 
PRO CD  HD2  sing N N 282 
PRO CD  HD3  sing N N 283 
PRO OXT HXT  sing N N 284 
SER N   CA   sing N N 285 
SER N   H    sing N N 286 
SER N   H2   sing N N 287 
SER CA  C    sing N N 288 
SER CA  CB   sing N N 289 
SER CA  HA   sing N N 290 
SER C   O    doub N N 291 
SER C   OXT  sing N N 292 
SER CB  OG   sing N N 293 
SER CB  HB2  sing N N 294 
SER CB  HB3  sing N N 295 
SER OG  HG   sing N N 296 
SER OXT HXT  sing N N 297 
SO4 S   O1   doub N N 298 
SO4 S   O2   doub N N 299 
SO4 S   O3   sing N N 300 
SO4 S   O4   sing N N 301 
THR N   CA   sing N N 302 
THR N   H    sing N N 303 
THR N   H2   sing N N 304 
THR CA  C    sing N N 305 
THR CA  CB   sing N N 306 
THR CA  HA   sing N N 307 
THR C   O    doub N N 308 
THR C   OXT  sing N N 309 
THR CB  OG1  sing N N 310 
THR CB  CG2  sing N N 311 
THR CB  HB   sing N N 312 
THR OG1 HG1  sing N N 313 
THR CG2 HG21 sing N N 314 
THR CG2 HG22 sing N N 315 
THR CG2 HG23 sing N N 316 
THR OXT HXT  sing N N 317 
TRP N   CA   sing N N 318 
TRP N   H    sing N N 319 
TRP N   H2   sing N N 320 
TRP CA  C    sing N N 321 
TRP CA  CB   sing N N 322 
TRP CA  HA   sing N N 323 
TRP C   O    doub N N 324 
TRP C   OXT  sing N N 325 
TRP CB  CG   sing N N 326 
TRP CB  HB2  sing N N 327 
TRP CB  HB3  sing N N 328 
TRP CG  CD1  doub Y N 329 
TRP CG  CD2  sing Y N 330 
TRP CD1 NE1  sing Y N 331 
TRP CD1 HD1  sing N N 332 
TRP CD2 CE2  doub Y N 333 
TRP CD2 CE3  sing Y N 334 
TRP NE1 CE2  sing Y N 335 
TRP NE1 HE1  sing N N 336 
TRP CE2 CZ2  sing Y N 337 
TRP CE3 CZ3  doub Y N 338 
TRP CE3 HE3  sing N N 339 
TRP CZ2 CH2  doub Y N 340 
TRP CZ2 HZ2  sing N N 341 
TRP CZ3 CH2  sing Y N 342 
TRP CZ3 HZ3  sing N N 343 
TRP CH2 HH2  sing N N 344 
TRP OXT HXT  sing N N 345 
TYR N   CA   sing N N 346 
TYR N   H    sing N N 347 
TYR N   H2   sing N N 348 
TYR CA  C    sing N N 349 
TYR CA  CB   sing N N 350 
TYR CA  HA   sing N N 351 
TYR C   O    doub N N 352 
TYR C   OXT  sing N N 353 
TYR CB  CG   sing N N 354 
TYR CB  HB2  sing N N 355 
TYR CB  HB3  sing N N 356 
TYR CG  CD1  doub Y N 357 
TYR CG  CD2  sing Y N 358 
TYR CD1 CE1  sing Y N 359 
TYR CD1 HD1  sing N N 360 
TYR CD2 CE2  doub Y N 361 
TYR CD2 HD2  sing N N 362 
TYR CE1 CZ   doub Y N 363 
TYR CE1 HE1  sing N N 364 
TYR CE2 CZ   sing Y N 365 
TYR CE2 HE2  sing N N 366 
TYR CZ  OH   sing N N 367 
TYR OH  HH   sing N N 368 
TYR OXT HXT  sing N N 369 
VAL N   CA   sing N N 370 
VAL N   H    sing N N 371 
VAL N   H2   sing N N 372 
VAL CA  C    sing N N 373 
VAL CA  CB   sing N N 374 
VAL CA  HA   sing N N 375 
VAL C   O    doub N N 376 
VAL C   OXT  sing N N 377 
VAL CB  CG1  sing N N 378 
VAL CB  CG2  sing N N 379 
VAL CB  HB   sing N N 380 
VAL CG1 HG11 sing N N 381 
VAL CG1 HG12 sing N N 382 
VAL CG1 HG13 sing N N 383 
VAL CG2 HG21 sing N N 384 
VAL CG2 HG22 sing N N 385 
VAL CG2 HG23 sing N N 386 
VAL OXT HXT  sing N N 387 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3MF8 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 2 2 21' 
_space_group.name_Hall        'C 2c 2' 
_space_group.IT_number        20 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9NF3 
_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]   0.016797 
_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]   0.010006 
_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]   0.007003 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . PRO A 1 1   ? 10.27700  34.90000 -22.93500 1.000 30.72234 ? 1   PRO B N   1 
ATOM   2    C CA  . PRO A 1 1   ? 10.06600  33.46300 -22.74300 1.000 25.68609 ? 1   PRO B CA  1 
ATOM   3    C C   . PRO A 1 1   ? 9.65800   33.16300 -21.31700 1.000 21.93338 ? 1   PRO B C   1 
ATOM   4    O O   . PRO A 1 1   ? 9.91500   33.99400 -20.44300 1.000 21.99091 ? 1   PRO B O   1 
ATOM   5    C CB  . PRO A 1 1   ? 11.44000  32.83900 -23.00700 1.000 27.30493 ? 1   PRO B CB  1 
ATOM   6    C CG  . PRO A 1 1   ? 12.39300  33.94600 -23.15800 1.000 28.74899 ? 1   PRO B CG  1 
ATOM   7    C CD  . PRO A 1 1   ? 11.67600  35.25500 -23.19800 1.000 29.52229 ? 1   PRO B CD  1 
ATOM   8    N N   . VAL A 1 2   ? 9.07600   31.99400 -21.06900 1.000 19.85378 ? 2   VAL B N   1 
ATOM   9    C CA  . VAL A 1 2   ? 9.08200   31.41100 -19.73000 1.000 16.07667 ? 2   VAL B CA  1 
ATOM   10   C C   . VAL A 1 2   ? 9.84000   30.09500 -19.78900 1.000 21.26710 ? 2   VAL B C   1 
ATOM   11   O O   . VAL A 1 2   ? 9.43200   29.17000 -20.50200 1.000 18.06372 ? 2   VAL B O   1 
ATOM   12   C CB  . VAL A 1 2   ? 7.67600   31.18400 -19.17500 1.000 19.17245 ? 2   VAL B CB  1 
ATOM   13   C CG1 . VAL A 1 2   ? 7.80400   30.52300 -17.82600 1.000 21.25894 ? 2   VAL B CG1 1 
ATOM   14   C CG2 . VAL A 1 2   ? 6.92400   32.50900 -19.05000 1.000 17.05423 ? 2   VAL B CG2 1 
ATOM   15   N N   . TYR A 1 3   ? 10.91700  29.99900 -19.01100 1.000 18.70177 ? 3   TYR B N   1 
ATOM   16   C CA  . TYR A 1 3   ? 11.68600  28.76900 -18.85500 1.000 17.97841 ? 3   TYR B CA  1 
ATOM   17   C C   . TYR A 1 3   ? 11.38400  28.20100 -17.47200 1.000 17.55415 ? 3   TYR B C   1 
ATOM   18   O O   . TYR A 1 3   ? 11.85800  28.73100 -16.46200 1.000 17.38421 ? 3   TYR B O   1 
ATOM   19   C CB  . TYR A 1 3   ? 13.18600  29.03100 -19.02500 1.000 17.47468 ? 3   TYR B CB  1 
ATOM   20   C CG  . TYR A 1 3   ? 13.59200  29.28800 -20.47200 1.000 18.74342 ? 3   TYR B CG  1 
ATOM   21   C CD1 . TYR A 1 3   ? 13.81200  28.23200 -21.35300 1.000 19.16442 ? 3   TYR B CD1 1 
ATOM   22   C CD2 . TYR A 1 3   ? 13.77300  30.58200 -20.94300 1.000 15.53954 ? 3   TYR B CD2 1 
ATOM   23   C CE1 . TYR A 1 3   ? 14.18000  28.46500 -22.66600 1.000 20.12546 ? 3   TYR B CE1 1 
ATOM   24   C CE2 . TYR A 1 3   ? 14.16400  30.82100 -22.25300 1.000 16.29426 ? 3   TYR B CE2 1 
ATOM   25   C CZ  . TYR A 1 3   ? 14.35700  29.75800 -23.10700 1.000 20.04425 ? 3   TYR B CZ  1 
ATOM   26   O OH  . TYR A 1 3   ? 14.73000  29.97500 -24.41700 1.000 21.69521 ? 3   TYR B OH  1 
ATOM   27   N N   . MET A 1 4   ? 10.58000  27.14000 -17.42100 1.000 18.00047 ? 4   MET B N   1 
ATOM   28   C CA  . MET A 1 4   ? 10.44400  26.38400 -16.17800 1.000 16.59232 ? 4   MET B CA  1 
ATOM   29   C C   . MET A 1 4   ? 11.64200  25.44700 -16.01100 1.000 18.50578 ? 4   MET B C   1 
ATOM   30   O O   . MET A 1 4   ? 11.92900  24.62400 -16.88600 1.000 16.32496 ? 4   MET B O   1 
ATOM   31   C CB  . MET A 1 4   ? 9.11100   25.63000 -16.12100 1.000 20.05400 ? 4   MET B CB  1 
ATOM   32   C CG  . MET A 1 4   ? 7.90800   26.43000 -16.67000 1.000 20.73063 ? 4   MET B CG  1 
ATOM   33   S SD  . MET A 1 4   ? 7.53000   27.82600 -15.54400 1.000 19.66245 ? 4   MET B SD  1 
ATOM   34   C CE  . MET A 1 4   ? 7.51800   26.98700 -13.96900 1.000 20.59282 ? 4   MET B CE  1 
ATOM   35   N N   . VAL A 1 5   ? 12.35200  25.60000 -14.89900 1.000 19.63485 ? 5   VAL B N   1 
ATOM   36   C CA  . VAL A 1 5   ? 13.57600  24.85800 -14.62300 1.000 16.30296 ? 5   VAL B CA  1 
ATOM   37   C C   . VAL A 1 5   ? 13.32600  23.98300 -13.40800 1.000 18.57452 ? 5   VAL B C   1 
ATOM   38   O O   . VAL A 1 5   ? 13.18300  24.48000 -12.28000 1.000 20.06475 ? 5   VAL B O   1 
ATOM   39   C CB  . VAL A 1 5   ? 14.77500  25.79300 -14.41000 1.000 16.24266 ? 5   VAL B CB  1 
ATOM   40   C CG1 . VAL A 1 5   ? 16.04800  24.97800 -14.14300 1.000 17.61541 ? 5   VAL B CG1 1 
ATOM   41   C CG2 . VAL A 1 5   ? 14.94500  26.67700 -15.64000 1.000 16.77935 ? 5   VAL B CG2 1 
ATOM   42   N N   . TYR A 1 6   ? 13.28100  22.67600 -13.64400 1.000 17.59221 ? 6   TYR B N   1 
ATOM   43   C CA  . TYR A 1 6   ? 12.94600  21.69300 -12.63100 1.000 17.75892 ? 6   TYR B CA  1 
ATOM   44   C C   . TYR A 1 6   ? 14.23600  21.09200 -12.09200 1.000 17.69934 ? 6   TYR B C   1 
ATOM   45   O O   . TYR A 1 6   ? 14.94400  20.38300 -12.80800 1.000 19.56983 ? 6   TYR B O   1 
ATOM   46   C CB  . TYR A 1 6   ? 12.02800  20.63400 -13.22500 1.000 17.77346 ? 6   TYR B CB  1 
ATOM   47   C CG  . TYR A 1 6   ? 10.73600  21.24800 -13.72500 1.000 17.85992 ? 6   TYR B CG  1 
ATOM   48   C CD1 . TYR A 1 6   ? 9.66300   21.45100 -12.86000 1.000 18.98673 ? 6   TYR B CD1 1 
ATOM   49   C CD2 . TYR A 1 6   ? 10.59100  21.61700 -15.05300 1.000 15.60026 ? 6   TYR B CD2 1 
ATOM   50   C CE1 . TYR A 1 6   ? 8.46100   22.01900 -13.31700 1.000 17.85697 ? 6   TYR B CE1 1 
ATOM   51   C CE2 . TYR A 1 6   ? 9.40600   22.17900 -15.52100 1.000 16.26457 ? 6   TYR B CE2 1 
ATOM   52   C CZ  . TYR A 1 6   ? 8.34800   22.37500 -14.65200 1.000 16.03109 ? 6   TYR B CZ  1 
ATOM   53   O OH  . TYR A 1 6   ? 7.18400   22.93800 -15.12000 1.000 15.95281 ? 6   TYR B OH  1 
ATOM   54   N N   . VAL A 1 7   ? 14.53700  21.37900 -10.82500 1.000 18.53387 ? 7   VAL B N   1 
ATOM   55   C CA  . VAL A 1 7   ? 15.77500  20.94200 -10.20000 1.000 18.98095 ? 7   VAL B CA  1 
ATOM   56   C C   . VAL A 1 7   ? 15.47400  20.37300 -8.82200  1.000 21.03077 ? 7   VAL B C   1 
ATOM   57   O O   . VAL A 1 7   ? 14.40900  20.60200 -8.23900  1.000 19.55291 ? 7   VAL B O   1 
ATOM   58   C CB  . VAL A 1 7   ? 16.81800  22.08600 -10.08900 1.000 23.81128 ? 7   VAL B CB  1 
ATOM   59   C CG1 . VAL A 1 7   ? 17.37400  22.44300 -11.44200 1.000 21.46216 ? 7   VAL B CG1 1 
ATOM   60   C CG2 . VAL A 1 7   ? 16.21500  23.32900 -9.43300  1.000 20.60846 ? 7   VAL B CG2 1 
ATOM   61   N N   . SER A 1 8   ? 16.43100  19.61700 -8.30000  1.000 19.75960 ? 8   SER B N   1 
ATOM   62   C CA  . SER A 1 8   ? 16.31000  19.16700 -6.92300  1.000 20.19926 ? 8   SER B CA  1 
ATOM   63   C C   . SER A 1 8   ? 16.63800  20.30900 -5.97600  1.000 21.18736 ? 8   SER B C   1 
ATOM   64   O O   . SER A 1 8   ? 17.46700  21.17400 -6.26900  1.000 20.65209 ? 8   SER B O   1 
ATOM   65   C CB  . SER A 1 8   ? 17.22500  17.97700 -6.65500  1.000 25.63888 ? 8   SER B CB  1 
ATOM   66   O OG  . SER A 1 8   ? 16.89000  16.89900 -7.51700  1.000 24.44100 ? 8   SER B OG  1 
ATOM   67   N N   . GLN A 1 9   ? 15.97200  20.30200 -4.82400  1.000 22.07930 ? 9   GLN B N   1 
ATOM   68   C CA  . GLN A 1 9   ? 16.07000  21.42800 -3.91800  1.000 21.85775 ? 9   GLN B CA  1 
ATOM   69   C C   . GLN A 1 9   ? 17.50500  21.54200 -3.40000  1.000 22.10268 ? 9   GLN B C   1 
ATOM   70   O O   . GLN A 1 9   ? 18.11800  20.54200 -3.01000  1.000 22.20877 ? 9   GLN B O   1 
ATOM   71   C CB  . GLN A 1 9   ? 15.04700  21.25600 -2.79700  1.000 26.52348 ? 9   GLN B CB  1 
ATOM   72   C CG  . GLN A 1 9   ? 15.14800  22.22600 -1.65700  1.000 24.96721 ? 9   GLN B CG  1 
ATOM   73   C CD  . GLN A 1 9   ? 14.35100  21.75700 -0.48500  1.000 31.66240 ? 9   GLN B CD  1 
ATOM   74   O OE1 . GLN A 1 9   ? 13.99300  20.58200 -0.39600  1.000 34.62223 ? 9   GLN B OE1 1 
ATOM   75   N NE2 . GLN A 1 9   ? 14.00500  22.68100 0.40100   1.000 39.92917 ? 9   GLN B NE2 1 
ATOM   76   N N   . ASP A 1 10  ? 18.06200  22.74600 -3.48700  1.000 20.78033 ? 10  ASP B N   1 
ATOM   77   C CA  . ASP A 1 10  ? 19.40600  23.15600 -3.07800  1.000 23.70772 ? 10  ASP B CA  1 
ATOM   78   C C   . ASP A 1 10  ? 20.49300  22.75000 -4.07800  1.000 23.39666 ? 10  ASP B C   1 
ATOM   79   O O   . ASP A 1 10  ? 21.65200  23.12600 -3.87700  1.000 23.91657 ? 10  ASP B O   1 
ATOM   80   C CB  . ASP A 1 10  ? 19.82200  22.62400 -1.68900  1.000 24.82862 ? 10  ASP B CB  1 
ATOM   81   C CG  . ASP A 1 10  ? 18.93700  23.12800 -0.57900  1.000 26.83583 ? 10  ASP B CG  1 
ATOM   82   O OD1 . ASP A 1 10  ? 17.98700  23.89100 -0.85300  1.000 26.05951 ? 10  ASP B OD1 1 
ATOM   83   O OD2 . ASP A 1 10  ? 19.21100  22.76200 0.58700   1.000 26.66515 ? 10  ASP B OD2 1 
ATOM   84   N N   . ARG A 1 11  ? 20.18600  21.99300 -5.13700  1.000 21.86962 ? 11  ARG B N   1 
ATOM   85   C CA  . ARG A 1 11  ? 21.21800  21.72100 -6.13700  1.000 25.43573 ? 11  ARG B CA  1 
ATOM   86   C C   . ARG A 1 11  ? 21.80400  23.02300 -6.68500  1.000 27.53050 ? 11  ARG B C   1 
ATOM   87   O O   . ARG A 1 11  ? 23.00500  23.10800 -6.99300  1.000 25.86013 ? 11  ARG B O   1 
ATOM   88   C CB  . ARG A 1 11  ? 20.64900  20.86400 -7.27300  1.000 22.82843 ? 11  ARG B CB  1 
ATOM   89   C CG  . ARG A 1 11  ? 21.65200  20.52900 -8.36100  1.000 24.28510 ? 11  ARG B CG  1 
ATOM   90   C CD  . ARG A 1 11  ? 22.94200  19.93400 -7.80700  1.000 28.07777 ? 11  ARG B CD  1 
ATOM   91   N NE  . ARG A 1 11  ? 23.88700  19.65800 -8.88400  1.000 26.89370 ? 11  ARG B NE  1 
ATOM   92   C CZ  . ARG A 1 11  ? 24.71100  20.56300 -9.39300  1.000 29.63129 ? 11  ARG B CZ  1 
ATOM   93   N NH1 . ARG A 1 11  ? 24.69700  21.82000 -8.97700  1.000 27.76615 ? 11  ARG B NH1 1 
ATOM   94   N NH2 . ARG A 1 11  ? 25.54400  20.21000 -10.37200 1.000 33.29249 ? 11  ARG B NH2 1 
ATOM   95   N N   . LEU A 1 12  ? 20.97100  24.04500 -6.81900  1.000 21.66318 ? 12  LEU B N   1 
ATOM   96   C CA  . LEU A 1 12  ? 21.41400  25.38100 -7.18800  1.000 21.91130 ? 12  LEU B CA  1 
ATOM   97   C C   . LEU A 1 12  ? 21.24600  26.28100 -5.96900  1.000 23.70275 ? 12  LEU B C   1 
ATOM   98   O O   . LEU A 1 12  ? 20.11900  26.55800 -5.54300  1.000 23.54054 ? 12  LEU B O   1 
ATOM   99   C CB  . LEU A 1 12  ? 20.61700  25.92000 -8.37700  1.000 21.50806 ? 12  LEU B CB  1 
ATOM   100  C CG  . LEU A 1 12  ? 20.64500  25.08100 -9.66800  1.000 25.92039 ? 12  LEU B CG  1 
ATOM   101  C CD1 . LEU A 1 12  ? 19.77900  25.71700 -10.73500 1.000 24.68702 ? 12  LEU B CD1 1 
ATOM   102  C CD2 . LEU A 1 12  ? 22.05900  24.91100 -10.20800 1.000 23.64443 ? 12  LEU B CD2 1 
ATOM   103  N N   . THR A 1 13  ? 22.35800  26.75000 -5.42400  1.000 24.15507 ? 13  THR B N   1 
ATOM   104  C CA  . THR A 1 13  ? 22.32800  27.78500 -4.39800  1.000 27.37230 ? 13  THR B CA  1 
ATOM   105  C C   . THR A 1 13  ? 21.70200  29.04200 -4.97500  1.000 29.14514 ? 13  THR B C   1 
ATOM   106  O O   . THR A 1 13  ? 21.54600  29.15100 -6.20300  1.000 24.83440 ? 13  THR B O   1 
ATOM   107  C CB  . THR A 1 13  ? 23.73700  28.10200 -3.90900  1.000 26.83091 ? 13  THR B CB  1 
ATOM   108  O OG1 . THR A 1 13  ? 24.46700  28.70000 -4.99500  1.000 24.49574 ? 13  THR B OG1 1 
ATOM   109  C CG2 . THR A 1 13  ? 24.43400  26.83500 -3.44600  1.000 26.30649 ? 13  THR B CG2 1 
ATOM   110  N N   . PRO A 1 14  ? 21.32700  30.01000 -4.13600  1.000 26.56788 ? 14  PRO B N   1 
ATOM   111  C CA  . PRO A 1 14  ? 20.83700  31.28400 -4.68500  1.000 28.02148 ? 14  PRO B CA  1 
ATOM   112  C C   . PRO A 1 14  ? 21.73900  31.87800 -5.75900  1.000 29.21458 ? 14  PRO B C   1 
ATOM   113  O O   . PRO A 1 14  ? 21.23000  32.32100 -6.79600  1.000 27.08609 ? 14  PRO B O   1 
ATOM   114  C CB  . PRO A 1 14  ? 20.74400  32.17300 -3.44100  1.000 28.37691 ? 14  PRO B CB  1 
ATOM   115  C CG  . PRO A 1 14  ? 20.40600  31.21400 -2.36100  1.000 27.20867 ? 14  PRO B CG  1 
ATOM   116  C CD  . PRO A 1 14  ? 21.16000  29.94800 -2.66400  1.000 25.92886 ? 14  PRO B CD  1 
ATOM   117  N N   . SER A 1 15  ? 23.06700  31.87500 -5.56900  1.000 30.83680 ? 15  SER B N   1 
ATOM   118  C CA  . SER A 1 15  ? 23.92900  32.47400 -6.58900  1.000 29.07922 ? 15  SER B CA  1 
ATOM   119  C C   . SER A 1 15  ? 23.99300  31.61100 -7.84000  1.000 25.26579 ? 15  SER B C   1 
ATOM   120  O O   . SER A 1 15  ? 24.14300  32.14000 -8.94700  1.000 26.14346 ? 15  SER B O   1 
ATOM   121  C CB  . SER A 1 15  ? 25.34500  32.69300 -6.06200  1.000 31.61109 ? 15  SER B CB  1 
ATOM   122  O OG  . SER A 1 15  ? 25.77700  31.57800 -5.31300  1.000 37.99169 ? 15  SER B OG  1 
ATOM   123  N N   . ALA A 1 16  ? 23.89900  30.28700 -7.68600  1.000 25.81372 ? 16  ALA B N   1 
ATOM   124  C CA  . ALA A 1 16  ? 23.91000  29.41700 -8.85400  1.000 25.64784 ? 16  ALA B CA  1 
ATOM   125  C C   . ALA A 1 16  ? 22.60300  29.53700 -9.62200  1.000 25.84205 ? 16  ALA B C   1 
ATOM   126  O O   . ALA A 1 16  ? 22.59100  29.45400 -10.85500 1.000 23.40953 ? 16  ALA B O   1 
ATOM   127  C CB  . ALA A 1 16  ? 24.15800  27.97200 -8.43500  1.000 25.23833 ? 16  ALA B CB  1 
ATOM   128  N N   . LYS A 1 17  ? 21.49100  29.72000 -8.90800  1.000 25.01196 ? 17  LYS B N   1 
ATOM   129  C CA  . LYS A 1 17  ? 20.24100  30.05900 -9.58300  1.000 22.03922 ? 17  LYS B CA  1 
ATOM   130  C C   . LYS A 1 17  ? 20.40600  31.31700 -10.42500 1.000 24.47521 ? 17  LYS B C   1 
ATOM   131  O O   . LYS A 1 17  ? 19.97000  31.36500 -11.58400 1.000 23.49509 ? 17  LYS B O   1 
ATOM   132  C CB  . LYS A 1 17  ? 19.12300  30.24400 -8.55700  1.000 22.02236 ? 17  LYS B CB  1 
ATOM   133  C CG  . LYS A 1 17  ? 18.51500  28.94000 -8.09100  1.000 21.08633 ? 17  LYS B CG  1 
ATOM   134  C CD  . LYS A 1 17  ? 17.47800  29.13200 -6.98100  1.000 23.55606 ? 17  LYS B CD  1 
ATOM   135  C CE  . LYS A 1 17  ? 17.30100  27.78200 -6.30100  1.000 29.19825 ? 17  LYS B CE  1 
ATOM   136  N NZ  . LYS A 1 17  ? 16.90800  27.86100 -4.89200  1.000 34.24269 ? 17  LYS B NZ  1 
ATOM   137  N N   . HIS A 1 18  ? 21.06100  32.34000 -9.87000  1.000 20.16527 ? 18  HIS B N   1 
ATOM   138  C CA  . HIS A 1 18  ? 21.28700  33.56800 -10.61900 1.000 24.47716 ? 18  HIS B CA  1 
ATOM   139  C C   . HIS A 1 18  ? 22.15700  33.31500 -11.83900 1.000 24.19543 ? 18  HIS B C   1 
ATOM   140  O O   . HIS A 1 18  ? 21.90900  33.87800 -12.90800 1.000 22.75541 ? 18  HIS B O   1 
ATOM   141  C CB  . HIS A 1 18  ? 21.92500  34.63900 -9.73300  1.000 24.97146 ? 18  HIS B CB  1 
ATOM   142  C CG  . HIS A 1 18  ? 22.16900  35.93300 -10.45200 1.000 34.18255 ? 18  HIS B CG  1 
ATOM   143  N ND1 . HIS A 1 18  ? 23.27400  36.14400 -11.24800 1.000 33.19015 ? 18  HIS B ND1 1 
ATOM   144  C CD2 . HIS A 1 18  ? 21.43100  37.06800 -10.52600 1.000 35.42147 ? 18  HIS B CD2 1 
ATOM   145  C CE1 . HIS A 1 18  ? 23.21000  37.35500 -11.77500 1.000 35.69104 ? 18  HIS B CE1 1 
ATOM   146  N NE2 . HIS A 1 18  ? 22.10600  37.94000 -11.34700 1.000 32.83124 ? 18  HIS B NE2 1 
ATOM   147  N N   . ALA A 1 19  ? 23.20400  32.49100 -11.69200 1.000 25.80262 ? 19  ALA B N   1 
ATOM   148  C CA  . ALA A 1 19  ? 24.07300  32.18400 -12.83100 1.000 24.25703 ? 19  ALA B CA  1 
ATOM   149  C C   . ALA A 1 19  ? 23.33600  31.39500 -13.90600 1.000 22.04613 ? 19  ALA B C   1 
ATOM   150  O O   . ALA A 1 19  ? 23.53000  31.63400 -15.10400 1.000 21.61583 ? 19  ALA B O   1 
ATOM   151  C CB  . ALA A 1 19  ? 25.29300  31.39400 -12.36900 1.000 24.34278 ? 19  ALA B CB  1 
ATOM   152  N N   . VAL A 1 20  ? 22.52900  30.41900 -13.49900 1.000 19.08893 ? 20  VAL B N   1 
ATOM   153  C CA  . VAL A 1 20  ? 21.76400  29.64400 -14.47300 1.000 21.24835 ? 20  VAL B CA  1 
ATOM   154  C C   . VAL A 1 20  ? 20.74400  30.53500 -15.16600 1.000 21.17227 ? 20  VAL B C   1 
ATOM   155  O O   . VAL A 1 20  ? 20.57900  30.48800 -16.39400 1.000 21.72083 ? 20  VAL B O   1 
ATOM   156  C CB  . VAL A 1 20  ? 21.09700  28.43500 -13.78900 1.000 24.15992 ? 20  VAL B CB  1 
ATOM   157  C CG1 . VAL A 1 20  ? 20.04700  27.78400 -14.71900 1.000 20.83897 ? 20  VAL B CG1 1 
ATOM   158  C CG2 . VAL A 1 20  ? 22.15800  27.40600 -13.36000 1.000 23.52896 ? 20  VAL B CG2 1 
ATOM   159  N N   . ALA A 1 21  ? 20.03800  31.35800 -14.39700 1.000 21.26957 ? 21  ALA B N   1 
ATOM   160  C CA  . ALA A 1 21  ? 19.04500  32.22400 -15.01200 1.000 21.87127 ? 21  ALA B CA  1 
ATOM   161  C C   . ALA A 1 21  ? 19.70300  33.25100 -15.92000 1.000 23.37894 ? 21  ALA B C   1 
ATOM   162  O O   . ALA A 1 21  ? 19.12900  33.61600 -16.95000 1.000 21.21015 ? 21  ALA B O   1 
ATOM   163  C CB  . ALA A 1 21  ? 18.18400  32.90100 -13.93600 1.000 24.73640 ? 21  ALA B CB  1 
ATOM   164  N N   . LYS A 1 22  ? 20.92100  33.70100 -15.59600 1.000 22.97746 ? 22  LYS B N   1 
ATOM   165  C CA  . LYS A 1 22  ? 21.54200  34.67300 -16.48900 1.000 21.88253 ? 22  LYS B CA  1 
ATOM   166  C C   . LYS A 1 22  ? 22.04300  34.00800 -17.76000 1.000 21.66299 ? 22  LYS B C   1 
ATOM   167  O O   . LYS A 1 22  ? 21.99900  34.61500 -18.84000 1.000 26.74103 ? 22  LYS B O   1 
ATOM   168  C CB  . LYS A 1 22  ? 22.68800  35.41200 -15.78300 1.000 29.02033 ? 22  LYS B CB  1 
ATOM   169  C CG  . LYS A 1 22  ? 23.90200  35.68800 -16.65300 1.000 31.82623 ? 22  LYS B CG  1 
ATOM   170  C CD  . LYS A 1 22  ? 25.00200  36.37500 -15.84000 1.000 32.20405 ? 22  LYS B CD  1 
ATOM   171  C CE  . LYS A 1 22  ? 24.83200  37.88600 -15.88500 1.000 42.11133 ? 22  LYS B CE  1 
ATOM   172  N NZ  . LYS A 1 22  ? 25.58800  38.60100 -14.81600 1.000 45.46815 ? 22  LYS B NZ  1 
ATOM   173  N N   . ALA A 1 23  ? 22.47700  32.75200 -17.66700 1.000 22.68177 ? 23  ALA B N   1 
ATOM   174  C CA  . ALA A 1 23  ? 22.93300  32.04300 -18.85600 1.000 22.81108 ? 23  ALA B CA  1 
ATOM   175  C C   . ALA A 1 23  ? 21.78000  31.79200 -19.81900 1.000 21.75397 ? 23  ALA B C   1 
ATOM   176  O O   . ALA A 1 23  ? 21.91100  31.99700 -21.02900 1.000 23.14753 ? 23  ALA B O   1 
ATOM   177  C CB  . ALA A 1 23  ? 23.59400  30.73000 -18.45700 1.000 25.78603 ? 23  ALA B CB  1 
ATOM   178  N N   . ILE A 1 24  ? 20.64100  31.33600 -19.30000 1.000 23.48012 ? 24  ILE B N   1 
ATOM   179  C CA  . ILE A 1 24  ? 19.46400  31.11200 -20.15000 1.000 20.38201 ? 24  ILE B CA  1 
ATOM   180  C C   . ILE A 1 24  ? 19.00900  32.42000 -20.78200 1.000 18.84697 ? 24  ILE B C   1 
ATOM   181  O O   . ILE A 1 24  ? 18.71800  32.49200 -21.98500 1.000 19.96894 ? 24  ILE B O   1 
ATOM   182  C CB  . ILE A 1 24  ? 18.33400  30.47600 -19.32200 1.000 22.15112 ? 24  ILE B CB  1 
ATOM   183  C CG1 . ILE A 1 24  ? 18.76400  29.10300 -18.80300 1.000 21.84830 ? 24  ILE B CG1 1 
ATOM   184  C CG2 . ILE A 1 24  ? 17.04000  30.43200 -20.14200 1.000 18.61245 ? 24  ILE B CG2 1 
ATOM   185  C CD1 . ILE A 1 24  ? 17.65900  28.29400 -18.16900 1.000 23.16776 ? 24  ILE B CD1 1 
ATOM   186  N N   . THR A 1 25  ? 18.94100  33.47100 -19.96900 1.000 17.74462 ? 25  THR B N   1 
ATOM   187  C CA  . THR A 1 25  ? 18.51100  34.78700 -20.43300 1.000 23.70414 ? 25  THR B CA  1 
ATOM   188  C C   . THR A 1 25  ? 19.41900  35.31500 -21.53600 1.000 22.09810 ? 25  THR B C   1 
ATOM   189  O O   . THR A 1 25  ? 18.94900  35.79200 -22.58500 1.000 20.16202 ? 25  THR B O   1 
ATOM   190  C CB  . THR A 1 25  ? 18.49200  35.74400 -19.24000 1.000 21.79374 ? 25  THR B CB  1 
ATOM   191  O OG1 . THR A 1 25  ? 17.56400  35.26000 -18.25500 1.000 22.19645 ? 25  THR B OG1 1 
ATOM   192  C CG2 . THR A 1 25  ? 18.12600  37.16200 -19.67300 1.000 26.68138 ? 25  THR B CG2 1 
ATOM   193  N N   . ASP A 1 26  ? 20.73200  35.23800 -21.31700 1.000 24.06122 ? 26  ASP B N   1 
ATOM   194  C CA  . ASP A 1 26  ? 21.67300  35.72300 -22.32000 1.000 21.26939 ? 26  ASP B CA  1 
ATOM   195  C C   . ASP A 1 26  ? 21.58100  34.89600 -23.59400 1.000 23.00293 ? 26  ASP B C   1 
ATOM   196  O O   . ASP A 1 26  ? 21.68200  35.43900 -24.70000 1.000 24.41341 ? 26  ASP B O   1 
ATOM   197  C CB  . ASP A 1 26  ? 23.10800  35.69400 -21.77300 1.000 22.36466 ? 26  ASP B CB  1 
ATOM   198  C CG  . ASP A 1 26  ? 23.37200  36.77000 -20.72100 1.000 28.91030 ? 26  ASP B CG  1 
ATOM   199  O OD1 . ASP A 1 26  ? 22.48500  37.61300 -20.47000 1.000 28.19552 ? 26  ASP B OD1 1 
ATOM   200  O OD2 . ASP A 1 26  ? 24.48800  36.77600 -20.14700 1.000 30.60669 ? 26  ASP B OD2 1 
ATOM   201  N N   . ALA A 1 27  ? 21.40600  33.57900 -23.46800 1.000 22.75008 ? 27  ALA B N   1 
ATOM   202  C CA  . ALA A 1 27  ? 21.28800  32.75800 -24.67200 1.000 21.14280 ? 27  ALA B CA  1 
ATOM   203  C C   . ALA A 1 27  ? 20.04500  33.13900 -25.46400 1.000 23.27967 ? 27  ALA B C   1 
ATOM   204  O O   . ALA A 1 27  ? 20.09500  33.26900 -26.69400 1.000 21.40878 ? 27  ALA B O   1 
ATOM   205  C CB  . ALA A 1 27  ? 21.26700  31.27300 -24.30900 1.000 20.67221 ? 27  ALA B CB  1 
ATOM   206  N N   . HIS A 1 28  ? 18.92700  33.36300 -24.77000 1.000 19.30733 ? 28  HIS B N   1 
ATOM   207  C CA  . HIS A 1 28  ? 17.69400  33.72400 -25.46700 1.000 22.49517 ? 28  HIS B CA  1 
ATOM   208  C C   . HIS A 1 28  ? 17.80300  35.08000 -26.15900 1.000 22.17199 ? 28  HIS B C   1 
ATOM   209  O O   . HIS A 1 28  ? 17.39700  35.22400 -27.31900 1.000 23.00407 ? 28  HIS B O   1 
ATOM   210  C CB  . HIS A 1 28  ? 16.51400  33.71000 -24.50100 1.000 19.82883 ? 28  HIS B CB  1 
ATOM   211  C CG  . HIS A 1 28  ? 15.19400  33.60500 -25.20000 1.000 20.27938 ? 28  HIS B CG  1 
ATOM   212  N ND1 . HIS A 1 28  ? 14.56900  32.39800 -25.42700 1.000 23.15585 ? 28  HIS B ND1 1 
ATOM   213  C CD2 . HIS A 1 28  ? 14.39300  34.55300 -25.74100 1.000 22.98056 ? 28  HIS B CD2 1 
ATOM   214  C CE1 . HIS A 1 28  ? 13.42900  32.60700 -26.06500 1.000 24.42908 ? 28  HIS B CE1 1 
ATOM   215  N NE2 . HIS A 1 28  ? 13.29300  33.90800 -26.26000 1.000 25.44839 ? 28  HIS B NE2 1 
ATOM   216  N N   A ARG A 1 29  ? 18.35300  36.08300 -25.46700 0.488 23.19199 ? 29  ARG B N   1 
ATOM   217  N N   B ARG A 1 29  ? 18.33100  36.09600 -25.46300 0.512 23.17488 ? 29  ARG B N   1 
ATOM   218  C CA  A ARG A 1 29  ? 18.52900  37.39800 -26.07600 0.488 25.33760 ? 29  ARG B CA  1 
ATOM   219  C CA  B ARG A 1 29  ? 18.51800  37.38700 -26.11900 0.512 25.33358 ? 29  ARG B CA  1 
ATOM   220  C C   A ARG A 1 29  ? 19.54800  37.34600 -27.20700 0.488 24.99204 ? 29  ARG B C   1 
ATOM   221  C C   B ARG A 1 29  ? 19.51600  37.28100 -27.25600 0.512 25.03031 ? 29  ARG B C   1 
ATOM   222  O O   A ARG A 1 29  ? 19.37200  38.00800 -28.23700 0.488 26.60648 ? 29  ARG B O   1 
ATOM   223  O O   B ARG A 1 29  ? 19.28700  37.82700 -28.34300 0.512 26.62077 ? 29  ARG B O   1 
ATOM   224  C CB  A ARG A 1 29  ? 18.95100  38.41500 -25.01100 0.488 26.84288 ? 29  ARG B CB  1 
ATOM   225  C CB  B ARG A 1 29  ? 18.97200  38.46900 -25.13600 0.512 26.88299 ? 29  ARG B CB  1 
ATOM   226  C CG  A ARG A 1 29  ? 19.20100  39.84500 -25.52000 0.488 30.80689 ? 29  ARG B CG  1 
ATOM   227  C CG  B ARG A 1 29  ? 19.64300  39.65000 -25.87200 0.512 30.07003 ? 29  ARG B CG  1 
ATOM   228  C CD  A ARG A 1 29  ? 20.66300  40.05900 -25.88900 0.488 29.55000 ? 29  ARG B CD  1 
ATOM   229  C CD  B ARG A 1 29  ? 19.57200  40.97800 -25.12200 0.512 31.71957 ? 29  ARG B CD  1 
ATOM   230  N NE  A ARG A 1 29  ? 21.50500  39.09500 -25.18800 0.488 32.17234 ? 29  ARG B NE  1 
ATOM   231  N NE  B ARG A 1 29  ? 18.97200  41.99800 -25.97700 0.512 33.30643 ? 29  ARG B NE  1 
ATOM   232  C CZ  A ARG A 1 29  ? 22.77100  38.83200 -25.48300 0.488 28.34630 ? 29  ARG B CZ  1 
ATOM   233  C CZ  B ARG A 1 29  ? 18.18000  42.97600 -25.55000 0.512 35.47075 ? 29  ARG B CZ  1 
ATOM   234  N NH1 A ARG A 1 29  ? 23.39700  39.44700 -26.47800 0.488 26.73751 ? 29  ARG B NH1 1 
ATOM   235  N NH1 B ARG A 1 29  ? 17.91600  43.14200 -24.26500 0.512 35.47715 ? 29  ARG B NH1 1 
ATOM   236  N NH2 A ARG A 1 29  ? 23.41300  37.90100 -24.78700 0.488 25.62451 ? 29  ARG B NH2 1 
ATOM   237  N NH2 B ARG A 1 29  ? 17.63400  43.80800 -26.43600 0.512 34.30937 ? 29  ARG B NH2 1 
ATOM   238  N N   . GLY A 1 30  ? 20.62200  36.57100 -27.02800 1.000 23.95564 ? 30  GLY B N   1 
ATOM   239  C CA  . GLY A 1 30  ? 21.65700  36.49700 -28.04900 1.000 26.60184 ? 30  GLY B CA  1 
ATOM   240  C C   . GLY A 1 30  ? 21.17500  35.87700 -29.34700 1.000 25.19825 ? 30  GLY B C   1 
ATOM   241  O O   . GLY A 1 30  ? 21.52100  36.34900 -30.43700 1.000 29.69225 ? 30  GLY B O   1 
ATOM   242  N N   . LEU A 1 31  ? 20.36100  34.82400 -29.26000 1.000 21.63204 ? 31  LEU B N   1 
ATOM   243  C CA  . LEU A 1 31  ? 19.91400  34.13700 -30.46700 1.000 25.34009 ? 31  LEU B CA  1 
ATOM   244  C C   . LEU A 1 31  ? 18.58700  34.64400 -31.03500 1.000 28.46188 ? 31  LEU B C   1 
ATOM   245  O O   . LEU A 1 31  ? 18.34500  34.45000 -32.23600 1.000 25.78440 ? 31  LEU B O   1 
ATOM   246  C CB  . LEU A 1 31  ? 19.83400  32.63600 -30.19500 1.000 24.71903 ? 31  LEU B CB  1 
ATOM   247  C CG  . LEU A 1 31  ? 21.24000  32.11500 -29.88700 1.000 27.92744 ? 31  LEU B CG  1 
ATOM   248  C CD1 . LEU A 1 31  ? 21.23200  30.67600 -29.44000 1.000 24.08947 ? 31  LEU B CD1 1 
ATOM   249  C CD2 . LEU A 1 31  ? 22.07700  32.24900 -31.15000 1.000 32.12281 ? 31  LEU B CD2 1 
ATOM   250  N N   . THR A 1 32  ? 17.72700  35.29700 -30.23400 1.000 23.11667 ? 32  THR B N   1 
ATOM   251  C CA  . THR A 1 32  ? 16.44500  35.78700 -30.73900 1.000 25.41167 ? 32  THR B CA  1 
ATOM   252  C C   . THR A 1 32  ? 16.31400  37.30300 -30.80300 1.000 28.97936 ? 32  THR B C   1 
ATOM   253  O O   . THR A 1 32  ? 15.40800  37.79100 -31.48100 1.000 28.04126 ? 32  THR B O   1 
ATOM   254  C CB  . THR A 1 32  ? 15.26500  35.28000 -29.89100 1.000 24.00035 ? 32  THR B CB  1 
ATOM   255  O OG1 . THR A 1 32  ? 15.26500  35.94800 -28.62000 1.000 25.29235 ? 32  THR B OG1 1 
ATOM   256  C CG2 . THR A 1 32  ? 15.32100  33.77400 -29.68700 1.000 25.48846 ? 32  THR B CG2 1 
ATOM   257  N N   . GLY A 1 33  ? 17.13700  38.05700 -30.08000 1.000 28.55977 ? 33  GLY B N   1 
ATOM   258  C CA  . GLY A 1 33  ? 16.97500  39.49500 -30.02300 1.000 27.94320 ? 33  GLY B CA  1 
ATOM   259  C C   . GLY A 1 33  ? 15.93900  39.99000 -29.03000 1.000 30.02659 ? 33  GLY B C   1 
ATOM   260  O O   . GLY A 1 33  ? 15.81700  41.21200 -28.84500 1.000 28.83579 ? 33  GLY B O   1 
ATOM   261  N N   . THR A 1 34  ? 15.19800  39.08900 -28.38700 1.000 27.44822 ? 34  THR B N   1 
ATOM   262  C CA  . THR A 1 34  ? 14.21300  39.46800 -27.37800 1.000 27.79840 ? 34  THR B CA  1 
ATOM   263  C C   . THR A 1 34  ? 14.90600  40.06000 -26.15900 1.000 30.96956 ? 34  THR B C   1 
ATOM   264  O O   . THR A 1 34  ? 15.89200  39.50200 -25.66800 1.000 35.66405 ? 34  THR B O   1 
ATOM   265  C CB  . THR A 1 34  ? 13.38200  38.24600 -26.98000 1.000 29.80648 ? 34  THR B CB  1 
ATOM   266  O OG1 . THR A 1 34  ? 12.81400  37.64800 -28.15800 1.000 31.68058 ? 34  THR B OG1 1 
ATOM   267  C CG2 . THR A 1 34  ? 12.26900  38.62100 -26.04000 1.000 30.30522 ? 34  THR B CG2 1 
ATOM   268  N N   . GLN A 1 35  ? 14.38400  41.18600 -25.66400 1.000 29.38768 ? 35  GLN B N   1 
ATOM   269  C CA  . GLN A 1 35  ? 15.03400  41.92000 -24.58200 1.000 30.77858 ? 35  GLN B CA  1 
ATOM   270  C C   . GLN A 1 35  ? 15.28000  41.02500 -23.37500 1.000 28.54350 ? 35  GLN B C   1 
ATOM   271  O O   . GLN A 1 35  ? 14.55200  40.05800 -23.12500 1.000 28.71728 ? 35  GLN B O   1 
ATOM   272  C CB  . GLN A 1 35  ? 14.18500  43.12600 -24.16300 1.000 29.28192 ? 35  GLN B CB  1 
ATOM   273  C CG  . GLN A 1 35  ? 13.99700  44.13600 -25.27400 1.000 30.01117 ? 35  GLN B CG  1 
ATOM   274  C CD  . GLN A 1 35  ? 12.65100  43.93700 -25.95500 1.000 29.93700 ? 35  GLN B CD  1 
ATOM   275  O OE1 . GLN A 1 35  ? 12.19200  42.80300 -26.08900 1.000 28.91150 ? 35  GLN B OE1 1 
ATOM   276  N NE2 . GLN A 1 35  ? 12.02300  45.02400 -26.39300 1.000 27.90205 ? 35  GLN B NE2 1 
ATOM   277  N N   . HIS A 1 36  ? 16.31900  41.37200 -22.61600 1.000 27.36507 ? 36  HIS B N   1 
ATOM   278  C CA  . HIS A 1 36  ? 16.63400  40.64000 -21.39500 1.000 29.23854 ? 36  HIS B CA  1 
ATOM   279  C C   . HIS A 1 36  ? 15.40400  40.48100 -20.51500 1.000 26.03751 ? 36  HIS B C   1 
ATOM   280  O O   . HIS A 1 36  ? 15.13400  39.39100 -19.99800 1.000 24.88678 ? 36  HIS B O   1 
ATOM   281  C CB  . HIS A 1 36  ? 17.73400  41.36800 -20.61900 1.000 31.01494 ? 36  HIS B CB  1 
ATOM   282  C CG  . HIS A 1 36  ? 19.09200  41.24900 -21.23400 1.000 34.69966 ? 36  HIS B CG  1 
ATOM   283  N ND1 . HIS A 1 36  ? 19.79800  42.34700 -21.67800 1.000 39.97446 ? 36  HIS B ND1 1 
ATOM   284  C CD2 . HIS A 1 36  ? 19.88300  40.17300 -21.46400 1.000 36.09630 ? 36  HIS B CD2 1 
ATOM   285  C CE1 . HIS A 1 36  ? 20.96100  41.95100 -22.16700 1.000 38.92985 ? 36  HIS B CE1 1 
ATOM   286  N NE2 . HIS A 1 36  ? 21.03800  40.63700 -22.04700 1.000 39.43071 ? 36  HIS B NE2 1 
ATOM   287  N N   . PHE A 1 37  ? 14.64600  41.56900 -20.32600 1.000 23.70701 ? 37  PHE B N   1 
ATOM   288  C CA  . PHE A 1 37  ? 13.60300  41.56200 -19.30200 1.000 26.74334 ? 37  PHE B CA  1 
ATOM   289  C C   . PHE A 1 37  ? 12.41500  40.68600 -19.67300 1.000 25.25556 ? 37  PHE B C   1 
ATOM   290  O O   . PHE A 1 37  ? 11.55800  40.43000 -18.81700 1.000 23.00903 ? 37  PHE B O   1 
ATOM   291  C CB  . PHE A 1 37  ? 13.11900  42.98500 -19.00300 1.000 25.48260 ? 37  PHE B CB  1 
ATOM   292  C CG  . PHE A 1 37  ? 12.77100  43.79900 -20.22700 1.000 28.63057 ? 37  PHE B CG  1 
ATOM   293  C CD1 . PHE A 1 37  ? 11.61200  43.53900 -20.94600 1.000 26.91163 ? 37  PHE B CD1 1 
ATOM   294  C CD2 . PHE A 1 37  ? 13.55200  44.88400 -20.59800 1.000 24.91955 ? 37  PHE B CD2 1 
ATOM   295  C CE1 . PHE A 1 37  ? 11.27000  44.30600 -22.05100 1.000 25.85478 ? 37  PHE B CE1 1 
ATOM   296  C CE2 . PHE A 1 37  ? 13.21700  45.66100 -21.68800 1.000 26.56997 ? 37  PHE B CE2 1 
ATOM   297  C CZ  . PHE A 1 37  ? 12.07400  45.37100 -22.42000 1.000 30.54826 ? 37  PHE B CZ  1 
ATOM   298  N N   . LEU A 1 38  ? 12.33100  40.22200 -20.91700 1.000 25.04296 ? 38  LEU B N   1 
ATOM   299  C CA  . LEU A 1 38  ? 11.24000  39.32500 -21.27300 1.000 24.96482 ? 38  LEU B CA  1 
ATOM   300  C C   . LEU A 1 38  ? 11.53500  37.88100 -20.89800 1.000 22.76202 ? 38  LEU B C   1 
ATOM   301  O O   . LEU A 1 38  ? 10.61700  37.05100 -20.91600 1.000 23.01858 ? 38  LEU B O   1 
ATOM   302  C CB  . LEU A 1 38  ? 10.93000  39.44100 -22.77300 1.000 23.76448 ? 38  LEU B CB  1 
ATOM   303  C CG  . LEU A 1 38  ? 10.27300  40.76600 -23.17600 1.000 25.80209 ? 38  LEU B CG  1 
ATOM   304  C CD1 . LEU A 1 38  ? 9.95700   40.81500 -24.67600 1.000 25.57065 ? 38  LEU B CD1 1 
ATOM   305  C CD2 . LEU A 1 38  ? 9.00900   41.00600 -22.36500 1.000 25.82615 ? 38  LEU B CD2 1 
ATOM   306  N N   . ALA A 1 39  ? 12.78100  37.56400 -20.53800 1.000 24.71269 ? 39  ALA B N   1 
ATOM   307  C CA  . ALA A 1 39  ? 13.14900  36.20200 -20.15700 1.000 23.99826 ? 39  ALA B CA  1 
ATOM   308  C C   . ALA A 1 39  ? 12.78200  35.96600 -18.69900 1.000 24.55409 ? 39  ALA B C   1 
ATOM   309  O O   . ALA A 1 39  ? 13.39800  36.53900 -17.79200 1.000 22.37085 ? 39  ALA B O   1 
ATOM   310  C CB  . ALA A 1 39  ? 14.63900  35.94700 -20.37700 1.000 26.26192 ? 39  ALA B CB  1 
ATOM   311  N N   . GLN A 1 40  ? 11.78700  35.11900 -18.47100 1.000 20.02719 ? 40  GLN B N   1 
ATOM   312  C CA  . GLN A 1 40  ? 11.48100  34.63600 -17.14000 1.000 19.79878 ? 40  GLN B CA  1 
ATOM   313  C C   . GLN A 1 40  ? 12.09900  33.25600 -16.98000 1.000 21.55782 ? 40  GLN B C   1 
ATOM   314  O O   . GLN A 1 40  ? 11.94800  32.38800 -17.84600 1.000 20.64259 ? 40  GLN B O   1 
ATOM   315  C CB  . GLN A 1 40  ? 9.97400   34.59700 -16.87300 1.000 17.22621 ? 40  GLN B CB  1 
ATOM   316  C CG  . GLN A 1 40  ? 9.64900   34.03200 -15.50100 1.000 20.19638 ? 40  GLN B CG  1 
ATOM   317  C CD  . GLN A 1 40  ? 8.17300   34.05400 -15.15200 1.000 22.53739 ? 40  GLN B CD  1 
ATOM   318  O OE1 . GLN A 1 40  ? 7.72800   33.26900 -14.32200 1.000 21.91798 ? 40  GLN B OE1 1 
ATOM   319  N NE2 . GLN A 1 40  ? 7.41100   34.96200 -15.76800 1.000 21.65668 ? 40  GLN B NE2 1 
ATOM   320  N N   . VAL A 1 41  ? 12.82300  33.07100 -15.88800 1.000 18.48537 ? 41  VAL B N   1 
ATOM   321  C CA  . VAL A 1 41  ? 13.35300  31.77400 -15.49800 1.000 19.20376 ? 41  VAL B CA  1 
ATOM   322  C C   . VAL A 1 41  ? 12.74300  31.46300 -14.13600 1.000 21.46878 ? 41  VAL B C   1 
ATOM   323  O O   . VAL A 1 41  ? 12.92100  32.22900 -13.17900 1.000 20.56313 ? 41  VAL B O   1 
ATOM   324  C CB  . VAL A 1 41  ? 14.89100  31.76900 -15.44800 1.000 20.60449 ? 41  VAL B CB  1 
ATOM   325  C CG1 . VAL A 1 41  ? 15.41000  30.44500 -14.89000 1.000 19.26646 ? 41  VAL B CG1 1 
ATOM   326  C CG2 . VAL A 1 41  ? 15.47300  32.01500 -16.84300 1.000 19.16751 ? 41  VAL B CG2 1 
ATOM   327  N N   . ASN A 1 42  ? 11.99100  30.37400 -14.06400 1.000 17.88197 ? 42  ASN B N   1 
ATOM   328  C CA  . ASN A 1 42  ? 11.12300  30.07300 -12.93000 1.000 19.04911 ? 42  ASN B CA  1 
ATOM   329  C C   . ASN A 1 42  ? 11.57100  28.73200 -12.37100 1.000 19.71494 ? 42  ASN B C   1 
ATOM   330  O O   . ASN A 1 42  ? 11.26700  27.68000 -12.95200 1.000 17.97645 ? 42  ASN B O   1 
ATOM   331  C CB  . ASN A 1 42  ? 9.65400   30.05400 -13.37900 1.000 19.64176 ? 42  ASN B CB  1 
ATOM   332  C CG  . ASN A 1 42  ? 8.70000   30.17600 -12.23200 1.000 19.19334 ? 42  ASN B CG  1 
ATOM   333  O OD1 . ASN A 1 42  ? 8.84500   29.47700 -11.22400 1.000 20.70673 ? 42  ASN B OD1 1 
ATOM   334  N ND2 . ASN A 1 42  ? 7.68700   31.04800 -12.37700 1.000 15.67937 ? 42  ASN B ND2 1 
ATOM   335  N N   . PHE A 1 43  ? 12.31600  28.77300 -11.25800 1.000 16.26402 ? 43  PHE B N   1 
ATOM   336  C CA  . PHE A 1 43  ? 12.91400  27.56300 -10.71300 1.000 20.59540 ? 43  PHE B CA  1 
ATOM   337  C C   . PHE A 1 43  ? 11.88100  26.80300 -9.89200  1.000 20.79193 ? 43  PHE B C   1 
ATOM   338  O O   . PHE A 1 43  ? 11.24900  27.36200 -8.99100  1.000 19.00138 ? 43  PHE B O   1 
ATOM   339  C CB  . PHE A 1 43  ? 14.14200  27.89900 -9.85400  1.000 16.31767 ? 43  PHE B CB  1 
ATOM   340  C CG  . PHE A 1 43  ? 15.35100  28.30800 -10.65200 1.000 19.44812 ? 43  PHE B CG  1 
ATOM   341  C CD1 . PHE A 1 43  ? 16.15800  27.35600 -11.26600 1.000 20.29396 ? 43  PHE B CD1 1 
ATOM   342  C CD2 . PHE A 1 43  ? 15.66300  29.64400 -10.81800 1.000 17.05810 ? 43  PHE B CD2 1 
ATOM   343  C CE1 . PHE A 1 43  ? 17.26100  27.73500 -12.01200 1.000 19.90476 ? 43  PHE B CE1 1 
ATOM   344  C CE2 . PHE A 1 43  ? 16.77600  30.03600 -11.54900 1.000 18.33834 ? 43  PHE B CE2 1 
ATOM   345  C CZ  . PHE A 1 43  ? 17.57500  29.07300 -12.15600 1.000 20.98961 ? 43  PHE B CZ  1 
ATOM   346  N N   . GLN A 1 44  ? 11.71800  25.52300 -10.19500 1.000 17.56343 ? 44  GLN B N   1 
ATOM   347  C CA  . GLN A 1 44  ? 10.78200  24.67000 -9.47900  1.000 18.09885 ? 44  GLN B CA  1 
ATOM   348  C C   . GLN A 1 44  ? 11.59700  23.60300 -8.77100  1.000 20.40533 ? 44  GLN B C   1 
ATOM   349  O O   . GLN A 1 44  ? 12.16100  22.71600 -9.41900  1.000 19.15664 ? 44  GLN B O   1 
ATOM   350  C CB  . GLN A 1 44  ? 9.75600   24.05400 -10.42900 1.000 18.68079 ? 44  GLN B CB  1 
ATOM   351  C CG  . GLN A 1 44  ? 8.93800   25.09800 -11.17300 1.000 18.85192 ? 44  GLN B CG  1 
ATOM   352  C CD  . GLN A 1 44  ? 7.87700   25.67900 -10.29000 1.000 21.83101 ? 44  GLN B CD  1 
ATOM   353  O OE1 . GLN A 1 44  ? 7.11600   24.93900 -9.68000  1.000 25.82015 ? 44  GLN B OE1 1 
ATOM   354  N NE2 . GLN A 1 44  ? 7.83700   27.00300 -10.18300 1.000 20.91716 ? 44  GLN B NE2 1 
ATOM   355  N N   . GLU A 1 45  ? 11.67400  23.68900 -7.44500  1.000 20.21796 ? 45  GLU B N   1 
ATOM   356  C CA  . GLU A 1 45  ? 12.47700  22.75900 -6.67300  1.000 20.52832 ? 45  GLU B CA  1 
ATOM   357  C C   . GLU A 1 45  ? 11.61400  21.65300 -6.06100  1.000 22.24007 ? 45  GLU B C   1 
ATOM   358  O O   . GLU A 1 45  ? 10.48700  21.88900 -5.61200  1.000 22.05008 ? 45  GLU B O   1 
ATOM   359  C CB  . GLU A 1 45  ? 13.24000  23.50700 -5.57200  1.000 21.08154 ? 45  GLU B CB  1 
ATOM   360  C CG  . GLU A 1 45  ? 14.41600  24.34300 -6.09800  1.000 25.11080 ? 45  GLU B CG  1 
ATOM   361  C CD  . GLU A 1 45  ? 15.07100  25.18400 -5.00400  1.000 24.80809 ? 45  GLU B CD  1 
ATOM   362  O OE1 . GLU A 1 45  ? 14.39200  26.05100 -4.42200  1.000 25.20121 ? 45  GLU B OE1 1 
ATOM   363  O OE2 . GLU A 1 45  ? 16.26700  24.96100 -4.72300  1.000 29.41746 ? 45  GLU B OE2 1 
ATOM   364  N N   . GLN A 1 46  ? 12.16000  20.44500 -6.03400  1.000 20.48252 ? 46  GLN B N   1 
ATOM   365  C CA  . GLN A 1 46  ? 11.52800  19.30600 -5.39500  1.000 19.57781 ? 46  GLN B CA  1 
ATOM   366  C C   . GLN A 1 46  ? 12.59100  18.54600 -4.61200  1.000 19.91426 ? 46  GLN B C   1 
ATOM   367  O O   . GLN A 1 46  ? 13.78100  18.64500 -4.91900  1.000 23.25333 ? 46  GLN B O   1 
ATOM   368  C CB  . GLN A 1 46  ? 10.86300  18.37700 -6.42300  1.000 21.48912 ? 46  GLN B CB  1 
ATOM   369  C CG  . GLN A 1 46  ? 9.62800   19.01400 -7.06800  1.000 21.85012 ? 46  GLN B CG  1 
ATOM   370  C CD  . GLN A 1 46  ? 8.47100   19.08200 -6.09800  1.000 18.89121 ? 46  GLN B CD  1 
ATOM   371  O OE1 . GLN A 1 46  ? 8.17200   18.11000 -5.41400  1.000 24.47427 ? 46  GLN B OE1 1 
ATOM   372  N NE2 . GLN A 1 46  ? 7.82300   20.23300 -6.02000  1.000 20.42134 ? 46  GLN B NE2 1 
ATOM   373  N N   . PRO A 1 47  ? 12.18300  17.78200 -3.60800  1.000 21.84246 ? 47  PRO B N   1 
ATOM   374  C CA  . PRO A 1 47  ? 13.15800  16.97500 -2.86900  1.000 24.47688 ? 47  PRO B CA  1 
ATOM   375  C C   . PRO A 1 47  ? 13.83200  15.95200 -3.77200  1.000 26.67711 ? 47  PRO B C   1 
ATOM   376  O O   . PRO A 1 47  ? 13.24200  15.44800 -4.73000  1.000 26.93891 ? 47  PRO B O   1 
ATOM   377  C CB  . PRO A 1 47  ? 12.30900  16.30000 -1.78800  1.000 23.16798 ? 47  PRO B CB  1 
ATOM   378  C CG  . PRO A 1 47  ? 10.89700  16.44000 -2.23600  1.000 28.64556 ? 47  PRO B CG  1 
ATOM   379  C CD  . PRO A 1 47  ? 10.84600  17.71500 -2.99700  1.000 23.34250 ? 47  PRO B CD  1 
ATOM   380  N N   . ALA A 1 48  ? 15.09200  15.66100 -3.46800  1.000 28.81575 ? 48  ALA B N   1 
ATOM   381  C CA  . ALA A 1 48  ? 15.79700  14.62700 -4.20800  1.000 25.91780 ? 48  ALA B CA  1 
ATOM   382  C C   . ALA A 1 48  ? 15.08800  13.29300 -4.02600  1.000 25.73553 ? 48  ALA B C   1 
ATOM   383  O O   . ALA A 1 48  ? 14.59800  12.97000 -2.94100  1.000 26.06660 ? 48  ALA B O   1 
ATOM   384  C CB  . ALA A 1 48  ? 17.25000  14.52500 -3.74400  1.000 27.73797 ? 48  ALA B CB  1 
ATOM   385  N N   . GLY A 1 49  ? 15.03000  12.52000 -5.10400  1.000 22.82986 ? 49  GLY B N   1 
ATOM   386  C CA  . GLY A 1 49  ? 14.29000  11.28300 -5.13900  1.000 22.27556 ? 49  GLY B CA  1 
ATOM   387  C C   . GLY A 1 49  ? 12.95800  11.38900 -5.85000  1.000 25.55799 ? 49  GLY B C   1 
ATOM   388  O O   . GLY A 1 49  ? 12.26600  10.37200 -6.00200  1.000 24.42702 ? 49  GLY B O   1 
ATOM   389  N N   . ASN A 1 50  ? 12.56200  12.58400 -6.27200  1.000 22.37303 ? 50  ASN B N   1 
ATOM   390  C CA  . ASN A 1 50  ? 11.29100  12.68700 -6.97200  1.000 25.45738 ? 50  ASN B CA  1 
ATOM   391  C C   . ASN A 1 50  ? 11.43500  12.48700 -8.47000  1.000 23.85300 ? 50  ASN B C   1 
ATOM   392  O O   . ASN A 1 50  ? 10.41900  12.42900 -9.16600  1.000 21.49601 ? 50  ASN B O   1 
ATOM   393  C CB  . ASN A 1 50  ? 10.62000  14.03200 -6.68300  1.000 19.60508 ? 50  ASN B CB  1 
ATOM   394  C CG  . ASN A 1 50  ? 9.78700   14.00200 -5.41200  1.000 25.65418 ? 50  ASN B CG  1 
ATOM   395  O OD1 . ASN A 1 50  ? 9.91800   13.08900 -4.58900  1.000 23.76721 ? 50  ASN B OD1 1 
ATOM   396  N ND2 . ASN A 1 50  ? 8.94400   15.00800 -5.23300  1.000 23.34253 ? 50  ASN B ND2 1 
ATOM   397  N N   . VAL A 1 51  ? 12.65900  12.38800 -8.98500  1.000 22.21170 ? 51  VAL B N   1 
ATOM   398  C CA  . VAL A 1 51  ? 12.89000  12.15500 -10.41100 1.000 21.72702 ? 51  VAL B CA  1 
ATOM   399  C C   . VAL A 1 51  ? 13.19600  10.68200 -10.63300 1.000 26.89457 ? 51  VAL B C   1 
ATOM   400  O O   . VAL A 1 51  ? 14.03600  10.10100 -9.92900  1.000 25.81337 ? 51  VAL B O   1 
ATOM   401  C CB  . VAL A 1 51  ? 14.02800  13.03800 -10.94100 1.000 21.77509 ? 51  VAL B CB  1 
ATOM   402  C CG1 . VAL A 1 51  ? 14.33500  12.69000 -12.40900 1.000 24.41245 ? 51  VAL B CG1 1 
ATOM   403  C CG2 . VAL A 1 51  ? 13.64100  14.50600 -10.80500 1.000 20.81784 ? 51  VAL B CG2 1 
ATOM   404  N N   . PHE A 1 52  ? 12.52200  10.07700 -11.61900 1.000 21.93981 ? 52  PHE B N   1 
ATOM   405  C CA  . PHE A 1 52  ? 12.77000  8.70300  -12.02000 1.000 22.73661 ? 52  PHE B CA  1 
ATOM   406  C C   . PHE A 1 52  ? 13.10600  8.68900  -13.49900 1.000 24.45217 ? 52  PHE B C   1 
ATOM   407  O O   . PHE A 1 52  ? 12.46200  9.38200  -14.29300 1.000 24.20955 ? 52  PHE B O   1 
ATOM   408  C CB  . PHE A 1 52  ? 11.56800  7.80400  -11.74400 1.000 23.54025 ? 52  PHE B CB  1 
ATOM   409  C CG  . PHE A 1 52  ? 11.28300  7.62600  -10.28400 1.000 26.50474 ? 52  PHE B CG  1 
ATOM   410  C CD1 . PHE A 1 52  ? 10.65300  8.63100  -9.56400  1.000 25.85237 ? 52  PHE B CD1 1 
ATOM   411  C CD2 . PHE A 1 52  ? 11.66700  6.46800  -9.62500  1.000 28.67290 ? 52  PHE B CD2 1 
ATOM   412  C CE1 . PHE A 1 52  ? 10.40600  8.48300  -8.20600  1.000 27.17468 ? 52  PHE B CE1 1 
ATOM   413  C CE2 . PHE A 1 52  ? 11.41000  6.30900  -8.25900  1.000 27.55034 ? 52  PHE B CE2 1 
ATOM   414  C CZ  . PHE A 1 52  ? 10.78500  7.31600  -7.55800  1.000 31.71232 ? 52  PHE B CZ  1 
ATOM   415  N N   . LEU A 1 53  ? 14.14000  7.92600  -13.84800 1.000 24.40196 ? 53  LEU B N   1 
ATOM   416  C CA  . LEU A 1 53  ? 14.58700  7.73400  -15.22100 1.000 23.84945 ? 53  LEU B CA  1 
ATOM   417  C C   . LEU A 1 53  ? 14.58100  6.23900  -15.49500 1.000 28.48501 ? 53  LEU B C   1 
ATOM   418  O O   . LEU A 1 53  ? 15.30500  5.48800  -14.83500 1.000 26.94555 ? 53  LEU B O   1 
ATOM   419  C CB  . LEU A 1 53  ? 15.98500  8.32800  -15.42400 1.000 27.62271 ? 53  LEU B CB  1 
ATOM   420  C CG  . LEU A 1 53  ? 16.12100  9.84300  -15.24200 1.000 28.70206 ? 53  LEU B CG  1 
ATOM   421  C CD1 . LEU A 1 53  ? 17.57900  10.28000 -15.28700 1.000 26.95538 ? 53  LEU B CD1 1 
ATOM   422  C CD2 . LEU A 1 53  ? 15.32100  10.55500 -16.34300 1.000 24.11344 ? 53  LEU B CD2 1 
ATOM   423  N N   . GLY A 1 54  ? 13.75300  5.80700  -16.44900 1.000 27.85297 ? 54  GLY B N   1 
ATOM   424  C CA  . GLY A 1 54  ? 13.56300  4.38700  -16.68100 1.000 27.80546 ? 54  GLY B CA  1 
ATOM   425  C C   . GLY A 1 54  ? 13.13300  3.60500  -15.45900 1.000 31.66096 ? 54  GLY B C   1 
ATOM   426  O O   . GLY A 1 54  ? 13.52000  2.44200  -15.31700 1.000 32.50480 ? 54  GLY B O   1 
ATOM   427  N N   . GLY A 1 55  ? 12.33800  4.21300  -14.56700 1.000 24.73256 ? 55  GLY B N   1 
ATOM   428  C CA  . GLY A 1 55  ? 11.86000  3.56000  -13.36600 1.000 27.45555 ? 55  GLY B CA  1 
ATOM   429  C C   . GLY A 1 55  ? 12.80500  3.60600  -12.18400 1.000 30.67239 ? 55  GLY B C   1 
ATOM   430  O O   . GLY A 1 55  ? 12.42100  3.17400  -11.08500 1.000 30.99321 ? 55  GLY B O   1 
ATOM   431  N N   . VAL A 1 56  ? 14.01400  4.12800  -12.36600 1.000 27.70299 ? 56  VAL B N   1 
ATOM   432  C CA  . VAL A 1 56  ? 15.05400  4.15100  -11.34200 1.000 32.30939 ? 56  VAL B CA  1 
ATOM   433  C C   . VAL A 1 56  ? 15.03200  5.50600  -10.65700 1.000 27.32067 ? 56  VAL B C   1 
ATOM   434  O O   . VAL A 1 56  ? 15.07600  6.54500  -11.32600 1.000 29.31138 ? 56  VAL B O   1 
ATOM   435  C CB  . VAL A 1 56  ? 16.44000  3.88100  -11.95600 1.000 32.92478 ? 56  VAL B CB  1 
ATOM   436  C CG1 . VAL A 1 56  ? 17.53300  4.06000  -10.90500 1.000 30.62392 ? 56  VAL B CG1 1 
ATOM   437  C CG2 . VAL A 1 56  ? 16.49200  2.48200  -12.56700 1.000 35.75335 ? 56  VAL B CG2 1 
ATOM   438  N N   . GLN A 1 57  ? 14.99000  5.50000  -9.33000  1.000 31.98003 ? 57  GLN B N   1 
ATOM   439  C CA  . GLN A 1 57  ? 14.98400  6.74900  -8.57900  1.000 29.76904 ? 57  GLN B CA  1 
ATOM   440  C C   . GLN A 1 57  ? 16.33400  7.45700  -8.71000  1.000 31.46772 ? 57  GLN B C   1 
ATOM   441  O O   . GLN A 1 57  ? 17.39900  6.82900  -8.69500  1.000 28.73709 ? 57  GLN B O   1 
ATOM   442  C CB  . GLN A 1 57  ? 14.63500  6.47400  -7.10700  1.000 28.91551 ? 57  GLN B CB  1 
ATOM   443  C CG  . GLN A 1 57  ? 14.32400  7.72900  -6.28000  1.000 31.95285 ? 57  GLN B CG  1 
ATOM   444  C CD  . GLN A 1 57  ? 13.92400  7.43100  -4.84000  1.000 36.00803 ? 57  GLN B CD  1 
ATOM   445  O OE1 . GLN A 1 57  ? 14.66600  6.79700  -4.09500  1.000 37.90791 ? 57  GLN B OE1 1 
ATOM   446  N NE2 . GLN A 1 57  ? 12.74600  7.90600  -4.44200  1.000 37.11161 ? 57  GLN B NE2 1 
ATOM   447  N N   . GLN A 1 58  ? 16.28800  8.77300  -8.88100  1.000 29.48686 ? 58  GLN B N   1 
ATOM   448  C CA  . GLN A 1 58  ? 17.49400  9.55800  -9.08400  1.000 29.65202 ? 58  GLN B CA  1 
ATOM   449  C C   . GLN A 1 58  ? 17.87300  10.31800 -7.82100  1.000 25.62343 ? 58  GLN B C   1 
ATOM   450  O O   . GLN A 1 58  ? 17.05300  10.54000 -6.92300  1.000 27.84057 ? 58  GLN B O   1 
ATOM   451  C CB  . GLN A 1 58  ? 17.32300  10.55400 -10.23500 1.000 25.38086 ? 58  GLN B CB  1 
ATOM   452  C CG  . GLN A 1 58  ? 17.03400  9.92200  -11.58400 1.000 26.52149 ? 58  GLN B CG  1 
ATOM   453  C CD  . GLN A 1 58  ? 18.14700  9.01000  -12.03400 1.000 30.95652 ? 58  GLN B CD  1 
ATOM   454  O OE1 . GLN A 1 58  ? 19.26100  9.45900  -12.32100 1.000 31.18061 ? 58  GLN B OE1 1 
ATOM   455  N NE2 . GLN A 1 58  ? 17.85300  7.71900  -12.11000 1.000 30.56559 ? 58  GLN B NE2 1 
ATOM   456  N N   . GLY A 1 59  ? 19.14000  10.72400 -7.77400  1.000 28.87385 ? 59  GLY B N   1 
ATOM   457  C CA  . GLY A 1 59  ? 19.61300  11.70000 -6.81400  1.000 28.46240 ? 59  GLY B CA  1 
ATOM   458  C C   . GLY A 1 59  ? 19.23500  13.10000 -7.24000  1.000 30.43205 ? 59  GLY B C   1 
ATOM   459  O O   . GLY A 1 59  ? 18.21100  13.32400 -7.89700  1.000 28.84237 ? 59  GLY B O   1 
ATOM   460  N N   . GLY A 1 60  ? 20.07600  14.05800 -6.88700  1.000 27.09026 ? 60  GLY B N   1 
ATOM   461  C CA  . GLY A 1 60  ? 19.67800  15.44300 -7.03100  1.000 28.90759 ? 60  GLY B CA  1 
ATOM   462  C C   . GLY A 1 60  ? 20.25400  16.20900 -8.20300  1.000 28.69332 ? 60  GLY B C   1 
ATOM   463  O O   . GLY A 1 60  ? 20.25900  17.44300 -8.17000  1.000 27.34572 ? 60  GLY B O   1 
ATOM   464  N N   . ASP A 1 61  ? 20.73100  15.52400 -9.24900  1.000 25.36494 ? 61  ASP B N   1 
ATOM   465  C CA  . ASP A 1 61  ? 21.43700  16.21700 -10.32400 1.000 30.78602 ? 61  ASP B CA  1 
ATOM   466  C C   . ASP A 1 61  ? 20.62200  16.46100 -11.59400 1.000 25.33089 ? 61  ASP B C   1 
ATOM   467  O O   . ASP A 1 61  ? 21.07200  17.23100 -12.44500 1.000 30.68316 ? 61  ASP B O   1 
ATOM   468  C CB  . ASP A 1 61  ? 22.71000  15.45500 -10.71600 1.000 30.32525 ? 61  ASP B CB  1 
ATOM   469  C CG  . ASP A 1 61  ? 23.82700  15.64400 -9.72100  1.000 36.69305 ? 61  ASP B CG  1 
ATOM   470  O OD1 . ASP A 1 61  ? 23.91600  16.74700 -9.14200  1.000 33.95410 ? 61  ASP B OD1 1 
ATOM   471  O OD2 . ASP A 1 61  ? 24.62100  14.69200 -9.53200  1.000 42.26368 ? 61  ASP B OD2 1 
ATOM   472  N N   . THR A 1 62  ? 19.48000  15.82600 -11.79700 1.000 26.94567 ? 62  THR B N   1 
ATOM   473  C CA  . THR A 1 62  ? 18.79600  16.05100 -13.06700 1.000 23.23912 ? 62  THR B CA  1 
ATOM   474  C C   . THR A 1 62  ? 18.27200  17.48100 -13.15200 1.000 24.53965 ? 62  THR B C   1 
ATOM   475  O O   . THR A 1 62  ? 17.78600  18.03900 -12.16900 1.000 22.36915 ? 62  THR B O   1 
ATOM   476  C CB  . THR A 1 62  ? 17.64600  15.07000 -13.26000 1.000 26.50939 ? 62  THR B CB  1 
ATOM   477  O OG1 . THR A 1 62  ? 18.07500  13.75500 -12.91200 1.000 32.65243 ? 62  THR B OG1 1 
ATOM   478  C CG2 . THR A 1 62  ? 17.19300  15.06100 -14.72900 1.000 29.02516 ? 62  THR B CG2 1 
ATOM   479  N N   . ILE A 1 63  ? 18.39700  18.08500 -14.33200 1.000 22.92392 ? 63  ILE B N   1 
ATOM   480  C CA  . ILE A 1 63  ? 17.80300  19.38500 -14.62800 1.000 19.87536 ? 63  ILE B CA  1 
ATOM   481  C C   . ILE A 1 63  ? 16.91900  19.21500 -15.85400 1.000 19.62779 ? 63  ILE B C   1 
ATOM   482  O O   . ILE A 1 63  ? 17.38000  18.71100 -16.87700 1.000 20.29589 ? 63  ILE B O   1 
ATOM   483  C CB  . ILE A 1 63  ? 18.86500  20.46500 -14.89200 1.000 22.29962 ? 63  ILE B CB  1 
ATOM   484  C CG1 . ILE A 1 63  ? 19.83100  20.61400 -13.70800 1.000 23.91779 ? 63  ILE B CG1 1 
ATOM   485  C CG2 . ILE A 1 63  ? 18.19500  21.80600 -15.21100 1.000 23.12345 ? 63  ILE B CG2 1 
ATOM   486  C CD1 . ILE A 1 63  ? 20.87800  21.66600 -13.93300 1.000 25.38311 ? 63  ILE B CD1 1 
ATOM   487  N N   . PHE A 1 64  ? 15.65400  19.61200 -15.74700 1.000 19.40732 ? 64  PHE B N   1 
ATOM   488  C CA  . PHE A 1 64  ? 14.77200  19.66700 -16.90600 1.000 18.31621 ? 64  PHE B CA  1 
ATOM   489  C C   . PHE A 1 64  ? 14.36700  21.11300 -17.13800 1.000 19.75035 ? 64  PHE B C   1 
ATOM   490  O O   . PHE A 1 64  ? 13.77300  21.73700 -16.25800 1.000 20.87078 ? 64  PHE B O   1 
ATOM   491  C CB  . PHE A 1 64  ? 13.53500  18.78700 -16.70900 1.000 16.85501 ? 64  PHE B CB  1 
ATOM   492  C CG  . PHE A 1 64  ? 12.51200  18.94200 -17.79500 1.000 16.68949 ? 64  PHE B CG  1 
ATOM   493  C CD1 . PHE A 1 64  ? 12.89000  19.00900 -19.10500 1.000 16.29505 ? 64  PHE B CD1 1 
ATOM   494  C CD2 . PHE A 1 64  ? 11.15600  19.02300 -17.48200 1.000 18.60248 ? 64  PHE B CD2 1 
ATOM   495  C CE1 . PHE A 1 64  ? 11.92700  19.15900 -20.11800 1.000 19.51663 ? 64  PHE B CE1 1 
ATOM   496  C CE2 . PHE A 1 64  ? 10.20600  19.17400 -18.48100 1.000 18.43148 ? 64  PHE B CE2 1 
ATOM   497  C CZ  . PHE A 1 64  ? 10.59300  19.24000 -19.79200 1.000 15.85610 ? 64  PHE B CZ  1 
ATOM   498  N N   . VAL A 1 65  ? 14.66500  21.63100 -18.32600 1.000 18.17976 ? 65  VAL B N   1 
ATOM   499  C CA  . VAL A 1 65  ? 14.27300  22.97100 -18.74700 1.000 15.96177 ? 65  VAL B CA  1 
ATOM   500  C C   . VAL A 1 65  ? 13.11300  22.82900 -19.72700 1.000 20.17809 ? 65  VAL B C   1 
ATOM   501  O O   . VAL A 1 65  ? 13.28800  22.28700 -20.82800 1.000 16.53961 ? 65  VAL B O   1 
ATOM   502  C CB  . VAL A 1 65  ? 15.44000  23.72800 -19.39200 1.000 20.15421 ? 65  VAL B CB  1 
ATOM   503  C CG1 . VAL A 1 65  ? 14.98000  25.10800 -19.87000 1.000 18.33164 ? 65  VAL B CG1 1 
ATOM   504  C CG2 . VAL A 1 65  ? 16.64700  23.82700 -18.40400 1.000 19.87375 ? 65  VAL B CG2 1 
ATOM   505  N N   . HIS A 1 66  ? 11.93400  23.32000 -19.33500 1.000 16.33386 ? 66  HIS B N   1 
ATOM   506  C CA  . HIS A 1 66  ? 10.77300  23.40400 -20.22400 1.000 17.21767 ? 66  HIS B CA  1 
ATOM   507  C C   . HIS A 1 66  ? 10.61400  24.85600 -20.67600 1.000 17.61484 ? 66  HIS B C   1 
ATOM   508  O O   . HIS A 1 66  ? 10.16200  25.71300 -19.90800 1.000 16.53393 ? 66  HIS B O   1 
ATOM   509  C CB  . HIS A 1 66  ? 9.51600   22.92000 -19.51200 1.000 17.49819 ? 66  HIS B CB  1 
ATOM   510  C CG  . HIS A 1 66  ? 8.34700   22.69700 -20.42600 1.000 17.80109 ? 66  HIS B CG  1 
ATOM   511  N ND1 . HIS A 1 66  ? 7.06700   22.47500 -19.95500 1.000 17.51490 ? 66  HIS B ND1 1 
ATOM   512  C CD2 . HIS A 1 66  ? 8.25900   22.66700 -21.77800 1.000 17.26216 ? 66  HIS B CD2 1 
ATOM   513  C CE1 . HIS A 1 66  ? 6.24700   22.30200 -20.97900 1.000 17.75930 ? 66  HIS B CE1 1 
ATOM   514  N NE2 . HIS A 1 66  ? 6.94300   22.41300 -22.09500 1.000 16.56597 ? 66  HIS B NE2 1 
ATOM   515  N N   . GLY A 1 67  ? 10.98000  25.13000 -21.93300 1.000 18.14970 ? 67  GLY B N   1 
ATOM   516  C CA  . GLY A 1 67  ? 10.87600  26.47000 -22.48400 1.000 19.18736 ? 67  GLY B CA  1 
ATOM   517  C C   . GLY A 1 67  ? 9.56100   26.65600 -23.21300 1.000 17.71164 ? 67  GLY B C   1 
ATOM   518  O O   . GLY A 1 67  ? 9.18100   25.83000 -24.05200 1.000 17.24419 ? 67  GLY B O   1 
ATOM   519  N N   . LEU A 1 68  ? 8.85100   27.73600 -22.87200 1.000 14.85826 ? 68  LEU B N   1 
ATOM   520  C CA  . LEU A 1 68  ? 7.59100   28.09900 -23.51900 1.000 15.10753 ? 68  LEU B CA  1 
ATOM   521  C C   . LEU A 1 68  ? 7.84500   29.34200 -24.36200 1.000 17.38976 ? 68  LEU B C   1 
ATOM   522  O O   . LEU A 1 68  ? 8.12500   30.41900 -23.81400 1.000 17.49113 ? 68  LEU B O   1 
ATOM   523  C CB  . LEU A 1 68  ? 6.49900   28.35100 -22.47000 1.000 15.57232 ? 68  LEU B CB  1 
ATOM   524  C CG  . LEU A 1 68  ? 6.40400   27.19500 -21.48600 1.000 14.85795 ? 68  LEU B CG  1 
ATOM   525  C CD1 . LEU A 1 68  ? 5.44000   27.46600 -20.29600 1.000 19.35065 ? 68  LEU B CD1 1 
ATOM   526  C CD2 . LEU A 1 68  ? 6.00000   25.91900 -22.22500 1.000 16.71991 ? 68  LEU B CD2 1 
ATOM   527  N N   . HIS A 1 69  ? 7.75000   29.19100 -25.69000 1.000 17.24402 ? 69  HIS B N   1 
ATOM   528  C CA  . HIS A 1 69  ? 8.07900   30.22200 -26.66600 1.000 18.03695 ? 69  HIS B CA  1 
ATOM   529  C C   . HIS A 1 69  ? 6.86400   30.60300 -27.50900 1.000 19.26119 ? 69  HIS B C   1 
ATOM   530  O O   . HIS A 1 69  ? 5.87800   29.86700 -27.59200 1.000 15.84154 ? 69  HIS B O   1 
ATOM   531  C CB  . HIS A 1 69  ? 9.15800   29.77000 -27.67000 1.000 17.21562 ? 69  HIS B CB  1 
ATOM   532  C CG  . HIS A 1 69  ? 10.48300  29.45600 -27.06400 1.000 22.09692 ? 69  HIS B CG  1 
ATOM   533  N ND1 . HIS A 1 69  ? 11.54400  29.00200 -27.81700 1.000 25.92394 ? 69  HIS B ND1 1 
ATOM   534  C CD2 . HIS A 1 69  ? 10.92000  29.50900 -25.78700 1.000 24.28244 ? 69  HIS B CD2 1 
ATOM   535  C CE1 . HIS A 1 69  ? 12.58300  28.80200 -27.02800 1.000 26.32717 ? 69  HIS B CE1 1 
ATOM   536  N NE2 . HIS A 1 69  ? 12.22800  29.09700 -25.79200 1.000 22.91633 ? 69  HIS B NE2 1 
ATOM   537  N N   . ARG A 1 70  ? 6.99200   31.73900 -28.19100 1.000 20.50992 ? 70  ARG B N   1 
ATOM   538  C CA  . ARG A 1 70  ? 6.10000   32.05600 -29.29400 1.000 18.13986 ? 70  ARG B CA  1 
ATOM   539  C C   . ARG A 1 70  ? 6.43400   31.21700 -30.52300 1.000 18.49394 ? 70  ARG B C   1 
ATOM   540  O O   . ARG A 1 70  ? 7.60200   30.92700 -30.80300 1.000 18.44460 ? 70  ARG B O   1 
ATOM   541  C CB  . ARG A 1 70  ? 6.19000   33.53500 -29.66200 1.000 20.31904 ? 70  ARG B CB  1 
ATOM   542  C CG  . ARG A 1 70  ? 5.82400   34.49700 -28.54100 1.000 21.11246 ? 70  ARG B CG  1 
ATOM   543  C CD  . ARG A 1 70  ? 6.23600   35.90700 -28.89900 1.000 19.86033 ? 70  ARG B CD  1 
ATOM   544  N NE  . ARG A 1 70  ? 7.61000   36.11600 -28.46000 1.000 23.60972 ? 70  ARG B NE  1 
ATOM   545  C CZ  . ARG A 1 70  ? 8.39600   37.10500 -28.85100 1.000 25.20149 ? 70  ARG B CZ  1 
ATOM   546  N NH1 . ARG A 1 70  ? 7.97500   38.02600 -29.70000 1.000 23.53840 ? 70  ARG B NH1 1 
ATOM   547  N NH2 . ARG A 1 70  ? 9.63500   37.17500 -28.37000 1.000 21.37214 ? 70  ARG B NH2 1 
ATOM   548  N N   . GLU A 1 71  ? 5.39800   30.82700 -31.26000 1.000 18.24945 ? 71  GLU B N   1 
ATOM   549  C CA  . GLU A 1 71  ? 5.59300   30.31300 -32.61000 1.000 17.43358 ? 71  GLU B CA  1 
ATOM   550  C C   . GLU A 1 71  ? 6.25500   31.35400 -33.50500 1.000 21.40342 ? 71  GLU B C   1 
ATOM   551  O O   . GLU A 1 71  ? 6.07100   32.56100 -33.33600 1.000 19.94162 ? 71  GLU B O   1 
ATOM   552  C CB  . GLU A 1 71  ? 4.25500   29.92600 -33.23500 1.000 19.37812 ? 71  GLU B CB  1 
ATOM   553  C CG  . GLU A 1 71  ? 3.58900   28.75000 -32.61400 1.000 20.44319 ? 71  GLU B CG  1 
ATOM   554  C CD  . GLU A 1 71  ? 2.16500   28.57700 -33.11100 1.000 24.51791 ? 71  GLU B CD  1 
ATOM   555  O OE1 . GLU A 1 71  ? 1.67500   29.44800 -33.85700 1.000 23.25363 ? 71  GLU B OE1 1 
ATOM   556  O OE2 . GLU A 1 71  ? 1.53700   27.57200 -32.74100 1.000 26.57924 ? 71  GLU B OE2 1 
ATOM   557  N N   . GLY A 1 72  ? 7.01300   30.87500 -34.49200 1.000 17.51665 ? 72  GLY B N   1 
ATOM   558  C CA  . GLY A 1 72  ? 7.48900   31.77200 -35.53000 1.000 20.37467 ? 72  GLY B CA  1 
ATOM   559  C C   . GLY A 1 72  ? 8.97100   31.66700 -35.85400 1.000 19.64532 ? 72  GLY B C   1 
ATOM   560  O O   . GLY A 1 72  ? 9.41500   32.23500 -36.85700 1.000 17.51706 ? 72  GLY B O   1 
ATOM   561  N N   . ARG A 1 73  ? 9.74200   30.94100 -35.03900 1.000 18.92623 ? 73  ARG B N   1 
ATOM   562  C CA  . ARG A 1 73  ? 11.17400  30.78000 -35.26300 1.000 16.93084 ? 73  ARG B CA  1 
ATOM   563  C C   . ARG A 1 73  ? 11.47400  29.48200 -36.01100 1.000 20.38670 ? 73  ARG B C   1 
ATOM   564  O O   . ARG A 1 73  ? 10.67800  28.53300 -36.02400 1.000 17.94836 ? 73  ARG B O   1 
ATOM   565  C CB  . ARG A 1 73  ? 11.94100  30.80800 -33.92700 1.000 16.19217 ? 73  ARG B CB  1 
ATOM   566  C CG  . ARG A 1 73  ? 11.65900  32.08600 -33.16000 1.000 19.35227 ? 73  ARG B CG  1 
ATOM   567  C CD  . ARG A 1 73  ? 12.80600  32.50000 -32.23700 1.000 21.12716 ? 73  ARG B CD  1 
ATOM   568  N NE  . ARG A 1 73  ? 12.48500  33.77000 -31.60200 1.000 21.34390 ? 73  ARG B NE  1 
ATOM   569  C CZ  . ARG A 1 73  ? 11.81400  33.88100 -30.46600 1.000 26.14943 ? 73  ARG B CZ  1 
ATOM   570  N NH1 . ARG A 1 73  ? 11.41400  32.81400 -29.79100 1.000 27.00793 ? 73  ARG B NH1 1 
ATOM   571  N NH2 . ARG A 1 73  ? 11.53600  35.09300 -29.99400 1.000 29.20569 ? 73  ARG B NH2 1 
ATOM   572  N N   . SER A 1 74  ? 12.64600  29.45500 -36.63800 1.000 15.85643 ? 74  SER B N   1 
ATOM   573  C CA  . SER A 1 74  ? 13.04000  28.31700 -37.45700 1.000 18.72989 ? 74  SER B CA  1 
ATOM   574  C C   . SER A 1 74  ? 13.51300  27.15400 -36.59200 1.000 22.53330 ? 74  SER B C   1 
ATOM   575  O O   . SER A 1 74  ? 13.98400  27.33400 -35.46300 1.000 19.59944 ? 74  SER B O   1 
ATOM   576  C CB  . SER A 1 74  ? 14.15500  28.71200 -38.42600 1.000 19.43513 ? 74  SER B CB  1 
ATOM   577  O OG  . SER A 1 74  ? 15.37500  28.89900 -37.72000 1.000 20.25876 ? 74  SER B OG  1 
ATOM   578  N N   . ALA A 1 75  ? 13.41200  25.94500 -37.15900 1.000 19.04688 ? 75  ALA B N   1 
ATOM   579  C CA  . ALA A 1 75  ? 13.96700  24.76900 -36.49700 1.000 18.18311 ? 75  ALA B CA  1 
ATOM   580  C C   . ALA A 1 75  ? 15.46000  24.93600 -36.23900 1.000 19.37336 ? 75  ALA B C   1 
ATOM   581  O O   . ALA A 1 75  ? 15.96700  24.54000 -35.18100 1.000 19.90861 ? 75  ALA B O   1 
ATOM   582  C CB  . ALA A 1 75  ? 13.69800  23.51800 -37.33900 1.000 20.21441 ? 75  ALA B CB  1 
ATOM   583  N N   . ASP A 1 76  ? 16.17300  25.52800 -37.20300 1.000 22.89427 ? 76  ASP B N   1 
ATOM   584  C CA  . ASP A 1 76  ? 17.61000  25.77700 -37.07500 1.000 23.08775 ? 76  ASP B CA  1 
ATOM   585  C C   . ASP A 1 76  ? 17.90600  26.62900 -35.84300 1.000 23.28857 ? 76  ASP B C   1 
ATOM   586  O O   . ASP A 1 76  ? 18.74900  26.27800 -35.00200 1.000 21.22609 ? 76  ASP B O   1 
ATOM   587  C CB  . ASP A 1 76  ? 18.08800  26.46800 -38.35700 1.000 21.06502 ? 76  ASP B CB  1 
ATOM   588  C CG  . ASP A 1 76  ? 19.59000  26.77200 -38.37700 1.000 33.11073 ? 76  ASP B CG  1 
ATOM   589  O OD1 . ASP A 1 76  ? 20.27500  26.65700 -37.34800 1.000 33.21314 ? 76  ASP B OD1 1 
ATOM   590  O OD2 . ASP A 1 76  ? 20.08900  27.12600 -39.46600 1.000 42.10152 ? 76  ASP B OD2 1 
ATOM   591  N N   . LEU A 1 77  ? 17.19600  27.74500 -35.71100 1.000 18.28612 ? 77  LEU B N   1 
ATOM   592  C CA  . LEU A 1 77  ? 17.42200  28.65900 -34.60000 1.000 22.12836 ? 77  LEU B CA  1 
ATOM   593  C C   . LEU A 1 77  ? 17.05100  28.01300 -33.26700 1.000 20.05781 ? 77  LEU B C   1 
ATOM   594  O O   . LEU A 1 77  ? 17.77400  28.16400 -32.27800 1.000 18.20335 ? 77  LEU B O   1 
ATOM   595  C CB  . LEU A 1 77  ? 16.64000  29.95300 -34.85000 1.000 20.61517 ? 77  LEU B CB  1 
ATOM   596  C CG  . LEU A 1 77  ? 16.91300  31.23100 -34.03900 1.000 24.67862 ? 77  LEU B CG  1 
ATOM   597  C CD1 . LEU A 1 77  ? 16.31000  31.13500 -32.65300 1.000 26.03159 ? 77  LEU B CD1 1 
ATOM   598  C CD2 . LEU A 1 77  ? 18.41300  31.48500 -33.93700 1.000 28.08015 ? 77  LEU B CD2 1 
ATOM   599  N N   . LYS A 1 78  ? 15.93800  27.28300 -33.21700 1.000 20.30919 ? 78  LYS B N   1 
ATOM   600  C CA  . LYS A 1 78  ? 15.55300  26.62300 -31.97100 1.000 19.03827 ? 78  LYS B CA  1 
ATOM   601  C C   . LYS A 1 78  ? 16.55200  25.54000 -31.58300 1.000 18.38210 ? 78  LYS B C   1 
ATOM   602  O O   . LYS A 1 78  ? 16.80600  25.32600 -30.38900 1.000 18.78492 ? 78  LYS B O   1 
ATOM   603  C CB  . LYS A 1 78  ? 14.15700  26.03000 -32.11000 1.000 19.80206 ? 78  LYS B CB  1 
ATOM   604  C CG  . LYS A 1 78  ? 13.06000  27.08300 -32.08700 1.000 19.06798 ? 78  LYS B CG  1 
ATOM   605  C CD  . LYS A 1 78  ? 11.67800  26.42500 -32.23900 1.000 22.79693 ? 78  LYS B CD  1 
ATOM   606  C CE  . LYS A 1 78  ? 11.45700  25.95700 -33.66200 1.000 19.81066 ? 78  LYS B CE  1 
ATOM   607  N NZ  . LYS A 1 78  ? 10.10500  25.36100 -33.82700 1.000 18.75120 ? 78  LYS B NZ  1 
ATOM   608  N N   . GLY A 1 79  ? 17.12000  24.84600 -32.56600 1.000 19.80088 ? 79  GLY B N   1 
ATOM   609  C CA  . GLY A 1 79  ? 18.17700  23.89100 -32.26800 1.000 18.88190 ? 79  GLY B CA  1 
ATOM   610  C C   . GLY A 1 79  ? 19.40600  24.56100 -31.68800 1.000 17.67759 ? 79  GLY B C   1 
ATOM   611  O O   . GLY A 1 79  ? 19.98100  24.09100 -30.70100 1.000 19.90392 ? 79  GLY B O   1 
ATOM   612  N N   . GLN A 1 80  ? 19.82500  25.67300 -32.29100 1.000 18.60661 ? 80  GLN B N   1 
ATOM   613  C CA  . GLN A 1 80  ? 20.97800  26.39800 -31.76300 1.000 23.13912 ? 80  GLN B CA  1 
ATOM   614  C C   . GLN A 1 80  ? 20.71500  26.87100 -30.34500 1.000 22.36146 ? 80  GLN B C   1 
ATOM   615  O O   . GLN A 1 80  ? 21.59700  26.79500 -29.47700 1.000 18.26420 ? 80  GLN B O   1 
ATOM   616  C CB  . GLN A 1 80  ? 21.31000  27.59600 -32.64100 1.000 22.22396 ? 80  GLN B CB  1 
ATOM   617  C CG  . GLN A 1 80  ? 21.76400  27.26500 -34.04600 1.000 28.67902 ? 80  GLN B CG  1 
ATOM   618  C CD  . GLN A 1 80  ? 21.95900  28.51700 -34.86100 1.000 34.23742 ? 80  GLN B CD  1 
ATOM   619  O OE1 . GLN A 1 80  ? 22.48500  29.50900 -34.35900 1.000 37.47041 ? 80  GLN B OE1 1 
ATOM   620  N NE2 . GLN A 1 80  ? 21.50500  28.49900 -36.11600 1.000 31.80981 ? 80  GLN B NE2 1 
ATOM   621  N N   . LEU A 1 81  ? 19.50900  27.38300 -30.09500 1.000 18.12950 ? 81  LEU B N   1 
ATOM   622  C CA  . LEU A 1 81  ? 19.18800  27.87300 -28.75700 1.000 17.42735 ? 81  LEU B CA  1 
ATOM   623  C C   . LEU A 1 81  ? 19.17700  26.73800 -27.74300 1.000 18.54503 ? 81  LEU B C   1 
ATOM   624  O O   . LEU A 1 81  ? 19.67300  26.89600 -26.61800 1.000 22.37480 ? 81  LEU B O   1 
ATOM   625  C CB  . LEU A 1 81  ? 17.84400  28.61400 -28.79000 1.000 18.74923 ? 81  LEU B CB  1 
ATOM   626  C CG  . LEU A 1 81  ? 17.30800  29.24700 -27.50200 1.000 19.97217 ? 81  LEU B CG  1 
ATOM   627  C CD1 . LEU A 1 81  ? 18.31800  30.18400 -26.83800 1.000 20.43200 ? 81  LEU B CD1 1 
ATOM   628  C CD2 . LEU A 1 81  ? 15.97700  29.96600 -27.76100 1.000 18.38863 ? 81  LEU B CD2 1 
ATOM   629  N N   . ALA A 1 82  ? 18.60800  25.58800 -28.11000 1.000 18.54345 ? 82  ALA B N   1 
ATOM   630  C CA  . ALA A 1 82  ? 18.52600  24.48600 -27.15900 1.000 20.03842 ? 82  ALA B CA  1 
ATOM   631  C C   . ALA A 1 82  ? 19.90900  23.94800 -26.83900 1.000 20.57313 ? 82  ALA B C   1 
ATOM   632  O O   . ALA A 1 82  ? 20.20100  23.62100 -25.68100 1.000 21.89168 ? 82  ALA B O   1 
ATOM   633  C CB  . ALA A 1 82  ? 17.63000  23.37300 -27.69500 1.000 17.86977 ? 82  ALA B CB  1 
ATOM   634  N N   . GLN A 1 83  ? 20.78200  23.89400 -27.84700 1.000 21.89090 ? 83  GLN B N   1 
ATOM   635  C CA  . GLN A 1 83  ? 22.15900  23.46800 -27.61600 1.000 21.61415 ? 83  GLN B CA  1 
ATOM   636  C C   . GLN A 1 83  ? 22.89300  24.45600 -26.72800 1.000 23.02075 ? 83  GLN B C   1 
ATOM   637  O O   . GLN A 1 83  ? 23.61700  24.05500 -25.80400 1.000 26.65697 ? 83  GLN B O   1 
ATOM   638  C CB  . GLN A 1 83  ? 22.88400  23.30300 -28.95200 1.000 23.16581 ? 83  GLN B CB  1 
ATOM   639  C CG  . GLN A 1 83  ? 24.30400  22.73400 -28.80700 1.000 27.16832 ? 83  GLN B CG  1 
ATOM   640  C CD  . GLN A 1 83  ? 24.30000  21.37400 -28.14400 1.000 29.27157 ? 83  GLN B CD  1 
ATOM   641  O OE1 . GLN A 1 83  ? 24.77100  21.21800 -27.01500 1.000 31.86041 ? 83  GLN B OE1 1 
ATOM   642  N NE2 . GLN A 1 83  ? 23.76000  20.38500 -28.83300 1.000 25.39183 ? 83  GLN B NE2 1 
ATOM   643  N N   . ARG A 1 84  ? 22.70600  25.75500 -26.96900 1.000 21.10966 ? 84  ARG B N   1 
ATOM   644  C CA  . ARG A 1 84  ? 23.39500  26.73000 -26.13500 1.000 23.49897 ? 84  ARG B CA  1 
ATOM   645  C C   . ARG A 1 84  ? 22.91200  26.67400 -24.69900 1.000 23.74475 ? 84  ARG B C   1 
ATOM   646  O O   . ARG A 1 84  ? 23.69800  26.89500 -23.77200 1.000 23.70230 ? 84  ARG B O   1 
ATOM   647  C CB  . ARG A 1 84  ? 23.22300  28.14700 -26.68200 1.000 23.62081 ? 84  ARG B CB  1 
ATOM   648  C CG  . ARG A 1 84  ? 24.23200  29.10700 -26.04900 1.000 27.52497 ? 84  ARG B CG  1 
ATOM   649  C CD  . ARG A 1 84  ? 24.14900  30.50200 -26.60600 1.000 30.90942 ? 84  ARG B CD  1 
ATOM   650  N NE  . ARG A 1 84  ? 24.56200  31.47600 -25.60100 1.000 30.95580 ? 84  ARG B NE  1 
ATOM   651  C CZ  . ARG A 1 84  ? 24.70600  32.77200 -25.83200 1.000 25.60421 ? 84  ARG B CZ  1 
ATOM   652  N NH1 . ARG A 1 84  ? 24.53500  33.28100 -27.04400 1.000 29.65956 ? 84  ARG B NH1 1 
ATOM   653  N NH2 . ARG A 1 84  ? 25.03400  33.57700 -24.82500 1.000 27.16143 ? 84  ARG B NH2 1 
ATOM   654  N N   . ILE A 1 85  ? 21.62500  26.38600 -24.48800 1.000 20.54773 ? 85  ILE B N   1 
ATOM   655  C CA  . ILE A 1 85  ? 21.13400  26.27100 -23.12400 1.000 19.36493 ? 85  ILE B CA  1 
ATOM   656  C C   . ILE A 1 85  ? 21.77300  25.07200 -22.43900 1.000 25.45337 ? 85  ILE B C   1 
ATOM   657  O O   . ILE A 1 85  ? 22.19400  25.15600 -21.27800 1.000 17.91202 ? 85  ILE B O   1 
ATOM   658  C CB  . ILE A 1 85  ? 19.59800  26.18500 -23.11700 1.000 19.24495 ? 85  ILE B CB  1 
ATOM   659  C CG1 . ILE A 1 85  ? 19.00300  27.58200 -23.30300 1.000 20.77781 ? 85  ILE B CG1 1 
ATOM   660  C CG2 . ILE A 1 85  ? 19.13100  25.61500 -21.78900 1.000 21.17874 ? 85  ILE B CG2 1 
ATOM   661  C CD1 . ILE A 1 85  ? 17.54300  27.57900 -23.75500 1.000 23.17139 ? 85  ILE B CD1 1 
ATOM   662  N N   . VAL A 1 86  ? 21.85300  23.94000 -23.14400 1.000 19.97372 ? 86  VAL B N   1 
ATOM   663  C CA  . VAL A 1 86  ? 22.57600  22.78200 -22.62300 1.000 20.96622 ? 86  VAL B CA  1 
ATOM   664  C C   . VAL A 1 86  ? 24.01000  23.17100 -22.27400 1.000 23.97554 ? 86  VAL B C   1 
ATOM   665  O O   . VAL A 1 86  ? 24.48100  22.93600 -21.15800 1.000 23.02574 ? 86  VAL B O   1 
ATOM   666  C CB  . VAL A 1 86  ? 22.55000  21.62500 -23.63900 1.000 25.64188 ? 86  VAL B CB  1 
ATOM   667  C CG1 . VAL A 1 86  ? 23.47000  20.49400 -23.16600 1.000 25.35237 ? 86  VAL B CG1 1 
ATOM   668  C CG2 . VAL A 1 86  ? 21.11300  21.12500 -23.86600 1.000 22.85815 ? 86  VAL B CG2 1 
ATOM   669  N N   . ASP A 1 87  ? 24.70100  23.81800 -23.21100 1.000 19.16899 ? 87  ASP B N   1 
ATOM   670  C CA  . ASP A 1 87  ? 26.11300  24.14800 -23.01100 1.000 25.07127 ? 87  ASP B CA  1 
ATOM   671  C C   . ASP A 1 87  ? 26.29900  25.15700 -21.88300 1.000 24.89402 ? 87  ASP B C   1 
ATOM   672  O O   . ASP A 1 87  ? 27.14700  24.97100 -21.00100 1.000 25.82411 ? 87  ASP B O   1 
ATOM   673  C CB  . ASP A 1 87  ? 26.72000  24.69100 -24.30300 1.000 29.03552 ? 87  ASP B CB  1 
ATOM   674  C CG  . ASP A 1 87  ? 26.80600  23.64600 -25.39200 1.000 25.90871 ? 87  ASP B CG  1 
ATOM   675  O OD1 . ASP A 1 87  ? 26.77100  22.44500 -25.05400 1.000 29.90593 ? 87  ASP B OD1 1 
ATOM   676  O OD2 . ASP A 1 87  ? 26.95300  24.02400 -26.57400 1.000 30.19450 ? 87  ASP B OD2 1 
ATOM   677  N N   . ASP A 1 88  ? 25.52500  26.24300 -21.90000 1.000 23.05412 ? 88  ASP B N   1 
ATOM   678  C CA  . ASP A 1 88  ? 25.72500  27.30700 -20.93200 1.000 25.28583 ? 88  ASP B CA  1 
ATOM   679  C C   . ASP A 1 88  ? 25.12000  27.00500 -19.56800 1.000 24.43920 ? 88  ASP B C   1 
ATOM   680  O O   . ASP A 1 88  ? 25.57700  27.57100 -18.57300 1.000 23.79160 ? 88  ASP B O   1 
ATOM   681  C CB  . ASP A 1 88  ? 25.16600  28.61900 -21.46200 1.000 25.77744 ? 88  ASP B CB  1 
ATOM   682  C CG  . ASP A 1 88  ? 25.92700  29.12900 -22.67100 1.000 32.53664 ? 88  ASP B CG  1 
ATOM   683  O OD1 . ASP A 1 88  ? 26.91000  28.47000 -23.08900 1.000 29.83797 ? 88  ASP B OD1 1 
ATOM   684  O OD2 . ASP A 1 88  ? 25.55900  30.20300 -23.18100 1.000 29.07334 ? 88  ASP B OD2 1 
ATOM   685  N N   . VAL A 1 89  ? 24.10400  26.15000 -19.48100 1.000 25.77834 ? 89  VAL B N   1 
ATOM   686  C CA  . VAL A 1 89  ? 23.64700  25.75000 -18.15200 1.000 25.05849 ? 89  VAL B CA  1 
ATOM   687  C C   . VAL A 1 89  ? 24.61300  24.74000 -17.53900 1.000 25.08643 ? 89  VAL B C   1 
ATOM   688  O O   . VAL A 1 89  ? 24.87000  24.76500 -16.32800 1.000 21.92885 ? 89  VAL B O   1 
ATOM   689  C CB  . VAL A 1 89  ? 22.20700  25.21300 -18.20100 1.000 24.49968 ? 89  VAL B CB  1 
ATOM   690  C CG1 . VAL A 1 89  ? 21.85200  24.51200 -16.88900 1.000 22.12611 ? 89  VAL B CG1 1 
ATOM   691  C CG2 . VAL A 1 89  ? 21.22700  26.36900 -18.45200 1.000 18.29727 ? 89  VAL B CG2 1 
ATOM   692  N N   . SER A 1 90  ? 25.18200  23.85400 -18.36300 1.000 22.85645 ? 90  SER B N   1 
ATOM   693  C CA  . SER A 1 90  ? 26.25200  22.98300 -17.88300 1.000 26.58027 ? 90  SER B CA  1 
ATOM   694  C C   . SER A 1 90  ? 27.38900  23.77500 -17.22200 1.000 24.08762 ? 90  SER B C   1 
ATOM   695  O O   . SER A 1 90  ? 27.93400  23.34500 -16.19800 1.000 27.53167 ? 90  SER B O   1 
ATOM   696  C CB  . SER A 1 90  ? 26.79300  22.13700 -19.03700 1.000 26.83742 ? 90  SER B CB  1 
ATOM   697  O OG  . SER A 1 90  ? 27.95300  21.42700 -18.63300 1.000 32.50893 ? 90  SER B OG  1 
ATOM   698  N N   . VAL A 1 91  ? 27.74800  24.94500 -17.76500 1.000 26.57813 ? 91  VAL B N   1 
ATOM   699  C CA  . VAL A 1 91  ? 28.86100  25.70000 -17.17300 1.000 25.28995 ? 91  VAL B CA  1 
ATOM   700  C C   . VAL A 1 91  ? 28.38800  26.45000 -15.92700 1.000 30.51746 ? 91  VAL B C   1 
ATOM   701  O O   . VAL A 1 91  ? 29.07600  26.46700 -14.89600 1.000 27.58028 ? 91  VAL B O   1 
ATOM   702  C CB  . VAL A 1 91  ? 29.49500  26.67700 -18.18900 1.000 27.57390 ? 91  VAL B CB  1 
ATOM   703  C CG1 . VAL A 1 91  ? 30.42600  25.94800 -19.18900 1.000 31.92724 ? 91  VAL B CG1 1 
ATOM   704  C CG2 . VAL A 1 91  ? 28.48900  27.54000 -18.87400 1.000 33.66417 ? 91  VAL B CG2 1 
ATOM   705  N N   . ALA A 1 92  ? 27.21300  27.08600 -15.99800 1.000 21.42640 ? 92  ALA B N   1 
ATOM   706  C CA  . ALA A 1 92  ? 26.73300  27.89900 -14.88200 1.000 23.82231 ? 92  ALA B CA  1 
ATOM   707  C C   . ALA A 1 92  ? 26.42400  27.04200 -13.66300 1.000 27.66477 ? 92  ALA B C   1 
ATOM   708  O O   . ALA A 1 92  ? 26.71700  27.43600 -12.52900 1.000 25.72549 ? 92  ALA B O   1 
ATOM   709  C CB  . ALA A 1 92  ? 25.49400  28.69200 -15.30100 1.000 21.75306 ? 92  ALA B CB  1 
ATOM   710  N N   . ALA A 1 93  ? 25.84800  25.86800 -13.87700 1.000 25.13025 ? 93  ALA B N   1 
ATOM   711  C CA  . ALA A 1 93  ? 25.49600  24.95000 -12.80600 1.000 28.22816 ? 93  ALA B CA  1 
ATOM   712  C C   . ALA A 1 93  ? 26.61300  23.96600 -12.47700 1.000 26.20123 ? 93  ALA B C   1 
ATOM   713  O O   . ALA A 1 93  ? 26.43400  23.14500 -11.57700 1.000 27.52265 ? 93  ALA B O   1 
ATOM   714  C CB  . ALA A 1 93  ? 24.22700  24.17600 -13.18700 1.000 23.41070 ? 93  ALA B CB  1 
ATOM   715  N N   . GLU A 1 94  ? 27.74500  24.03800 -13.17600 1.000 26.74402 ? 94  GLU B N   1 
ATOM   716  C CA  . GLU A 1 94  ? 28.82900  23.04800 -13.09700 1.000 28.54476 ? 94  GLU B CA  1 
ATOM   717  C C   . GLU A 1 94  ? 28.27200  21.63000 -12.97100 1.000 27.50085 ? 94  GLU B C   1 
ATOM   718  O O   . GLU A 1 94  ? 28.48400  20.90700 -11.99700 1.000 26.38705 ? 94  GLU B O   1 
ATOM   719  C CB  . GLU A 1 94  ? 29.82200  23.40200 -11.98000 1.000 30.93654 ? 94  GLU B CB  1 
ATOM   720  C CG  . GLU A 1 94  ? 29.81500  24.89700 -11.65500 1.000 34.42433 ? 94  GLU B CG  1 
ATOM   721  C CD  . GLU A 1 94  ? 30.64500  25.27200 -10.43500 1.000 40.12055 ? 94  GLU B CD  1 
ATOM   722  O OE1 . GLU A 1 94  ? 31.39200  24.40500 -9.93200  1.000 36.57072 ? 94  GLU B OE1 1 
ATOM   723  O OE2 . GLU A 1 94  ? 30.53900  26.43600 -9.98600  1.000 42.95640 ? 94  GLU B OE2 1 
ATOM   724  N N   . ILE A 1 95  ? 27.55000  21.24300 -14.01600 1.000 29.97251 ? 95  ILE B N   1 
ATOM   725  C CA  . ILE A 1 95  ? 26.85500  19.96700 -14.07700 1.000 29.65331 ? 95  ILE B CA  1 
ATOM   726  C C   . ILE A 1 95  ? 27.12000  19.31900 -15.42800 1.000 26.68410 ? 95  ILE B C   1 
ATOM   727  O O   . ILE A 1 95  ? 27.26300  20.01000 -16.44200 1.000 28.79380 ? 95  ILE B O   1 
ATOM   728  C CB  . ILE A 1 95  ? 25.34800  20.16700 -13.82800 1.000 26.67710 ? 95  ILE B CB  1 
ATOM   729  C CG1 . ILE A 1 95  ? 24.70400  18.83900 -13.46400 1.000 29.80754 ? 95  ILE B CG1 1 
ATOM   730  C CG2 . ILE A 1 95  ? 24.67100  20.84400 -15.04900 1.000 26.89580 ? 95  ILE B CG2 1 
ATOM   731  C CD1 . ILE A 1 95  ? 23.25600  18.93000 -13.39700 1.000 30.88161 ? 95  ILE B CD1 1 
ATOM   732  N N   . ASP A 1 96  ? 27.21000  17.98900 -15.43700 1.000 27.36678 ? 96  ASP B N   1 
ATOM   733  C CA  . ASP A 1 96  ? 27.44900  17.25700 -16.67900 1.000 30.41669 ? 96  ASP B CA  1 
ATOM   734  C C   . ASP A 1 96  ? 26.27200  17.44900 -17.62400 1.000 24.01798 ? 96  ASP B C   1 
ATOM   735  O O   . ASP A 1 96  ? 25.11900  17.32400 -17.21300 1.000 25.53184 ? 96  ASP B O   1 
ATOM   736  C CB  . ASP A 1 96  ? 27.63900  15.76800 -16.38300 1.000 31.31232 ? 96  ASP B CB  1 
ATOM   737  C CG  . ASP A 1 96  ? 28.30900  15.01000 -17.52900 1.000 36.72242 ? 96  ASP B CG  1 
ATOM   738  O OD1 . ASP A 1 96  ? 27.63500  14.73600 -18.54900 1.000 34.34954 ? 96  ASP B OD1 1 
ATOM   739  O OD2 . ASP A 1 96  ? 29.51100  14.67500 -17.41300 1.000 41.70306 ? 96  ASP B OD2 1 
ATOM   740  N N   . ARG A 1 97  ? 26.56700  17.75800 -18.89400 1.000 26.45403 ? 97  ARG B N   1 
ATOM   741  C CA  . ARG A 1 97  ? 25.51700  17.92100 -19.90500 1.000 25.68782 ? 97  ARG B CA  1 
ATOM   742  C C   . ARG A 1 97  ? 24.57600  16.72900 -19.96300 1.000 25.60472 ? 97  ARG B C   1 
ATOM   743  O O   . ARG A 1 97  ? 23.41000  16.87200 -20.36000 1.000 27.50310 ? 97  ARG B O   1 
ATOM   744  C CB  . ARG A 1 97  ? 26.15100  18.11400 -21.28300 1.000 25.98207 ? 97  ARG B CB  1 
ATOM   745  C CG  . ARG A 1 97  ? 26.88900  19.42500 -21.50500 1.000 31.06485 ? 97  ARG B CG  1 
ATOM   746  C CD  . ARG A 1 97  ? 27.34800  19.48200 -22.95600 1.000 34.61230 ? 97  ARG B CD  1 
ATOM   747  N NE  . ARG A 1 97  ? 27.49500  18.12200 -23.47100 1.000 42.42265 ? 97  ARG B NE  1 
ATOM   748  C CZ  . ARG A 1 97  ? 26.71500  17.55100 -24.38600 1.000 43.77956 ? 97  ARG B CZ  1 
ATOM   749  N NH1 . ARG A 1 97  ? 25.68500  18.19700 -24.93000 1.000 39.26444 ? 97  ARG B NH1 1 
ATOM   750  N NH2 . ARG A 1 97  ? 26.96000  16.29500 -24.74900 1.000 40.14366 ? 97  ARG B NH2 1 
ATOM   751  N N   . LYS A 1 98  ? 25.06100  15.54100 -19.61000 1.000 22.66204 ? 98  LYS B N   1 
ATOM   752  C CA  . LYS A 1 98  ? 24.20000  14.37600 -19.67400 1.000 25.17435 ? 98  LYS B CA  1 
ATOM   753  C C   . LYS A 1 98  ? 23.08400  14.41600 -18.63700 1.000 26.21738 ? 98  LYS B C   1 
ATOM   754  O O   . LYS A 1 98  ? 22.15400  13.60500 -18.72200 1.000 23.61413 ? 98  LYS B O   1 
ATOM   755  C CB  . LYS A 1 98  ? 25.05500  13.10400 -19.57900 1.000 26.16665 ? 98  LYS B CB  1 
ATOM   756  C CG  . LYS A 1 98  ? 25.18700  12.40800 -18.23200 1.000 36.14057 ? 98  LYS B CG  1 
ATOM   757  C CD  . LYS A 1 98  ? 26.60900  11.80500 -18.15900 1.000 42.19577 ? 98  LYS B CD  1 
ATOM   758  C CE  . LYS A 1 98  ? 26.97200  11.15800 -16.82000 1.000 43.26035 ? 98  LYS B CE  1 
ATOM   759  N NZ  . LYS A 1 98  ? 27.10700  12.05400 -15.63700 1.000 41.57054 ? 98  LYS B NZ  1 
ATOM   760  N N   . HIS A 1 99  ? 23.11800  15.36500 -17.70100 1.000 25.93656 ? 99  HIS B N   1 
ATOM   761  C CA  . HIS A 1 99  ? 22.02800  15.54500 -16.75200 1.000 24.62525 ? 99  HIS B CA  1 
ATOM   762  C C   . HIS A 1 99  ? 20.97400  16.54800 -17.22300 1.000 24.41084 ? 99  HIS B C   1 
ATOM   763  O O   . HIS A 1 99  ? 20.03400  16.81900 -16.47600 1.000 23.10283 ? 99  HIS B O   1 
ATOM   764  C CB  . HIS A 1 99  ? 22.57000  16.02100 -15.40400 1.000 22.18138 ? 99  HIS B CB  1 
ATOM   765  C CG  . HIS A 1 99  ? 23.35400  14.98900 -14.66100 1.000 28.98013 ? 99  HIS B CG  1 
ATOM   766  N ND1 . HIS A 1 99  ? 22.80000  13.80800 -14.21700 1.000 30.72986 ? 99  HIS B ND1 1 
ATOM   767  C CD2 . HIS A 1 99  ? 24.63400  14.99600 -14.21900 1.000 31.51357 ? 99  HIS B CD2 1 
ATOM   768  C CE1 . HIS A 1 99  ? 23.71800  13.11200 -13.56800 1.000 33.62030 ? 99  HIS B CE1 1 
ATOM   769  N NE2 . HIS A 1 99  ? 24.83700  13.81400 -13.54800 1.000 33.82635 ? 99  HIS B NE2 1 
ATOM   770  N N   . ILE A 1 100 ? 21.11200  17.13000 -18.41400 1.000 22.23370 ? 100 ILE B N   1 
ATOM   771  C CA  . ILE A 1 100 ? 20.31100  18.28700 -18.80700 1.000 21.24849 ? 100 ILE B CA  1 
ATOM   772  C C   . ILE A 1 100 ? 19.33100  17.87700 -19.90100 1.000 21.54313 ? 100 ILE B C   1 
ATOM   773  O O   . ILE A 1 100 ? 19.74000  17.39200 -20.96400 1.000 18.75735 ? 100 ILE B O   1 
ATOM   774  C CB  . ILE A 1 100 ? 21.18000  19.45900 -19.27900 1.000 20.94211 ? 100 ILE B CB  1 
ATOM   775  C CG1 . ILE A 1 100 ? 22.19200  19.85300 -18.20000 1.000 23.53634 ? 100 ILE B CG1 1 
ATOM   776  C CG2 . ILE A 1 100 ? 20.30600  20.65000 -19.62500 1.000 18.94287 ? 100 ILE B CG2 1 
ATOM   777  C CD1 . ILE A 1 100 ? 23.07600  20.99800 -18.61700 1.000 23.44403 ? 100 ILE B CD1 1 
ATOM   778  N N   . TRP A 1 101 ? 18.04400  18.09700 -19.63500 1.000 21.35684 ? 101 TRP B N   1 
ATOM   779  C CA  . TRP A 1 101 ? 16.95100  17.89500 -20.58100 1.000 17.44927 ? 101 TRP B CA  1 
ATOM   780  C C   . TRP A 1 101 ? 16.33200  19.24600 -20.90600 1.000 18.01044 ? 101 TRP B C   1 
ATOM   781  O O   . TRP A 1 101 ? 16.14800  20.07700 -20.01300 1.000 18.94233 ? 101 TRP B O   1 
ATOM   782  C CB  . TRP A 1 101 ? 15.88100  16.95900 -20.00000 1.000 20.18192 ? 101 TRP B CB  1 
ATOM   783  C CG  . TRP A 1 101 ? 16.37200  15.57400 -19.67100 1.000 20.33490 ? 101 TRP B CG  1 
ATOM   784  C CD1 . TRP A 1 101 ? 17.54100  15.23500 -19.02800 1.000 24.46581 ? 101 TRP B CD1 1 
ATOM   785  C CD2 . TRP A 1 101 ? 15.71000  14.34300 -19.96800 1.000 18.82553 ? 101 TRP B CD2 1 
ATOM   786  N NE1 . TRP A 1 101 ? 17.63400  13.86500 -18.91100 1.000 24.35529 ? 101 TRP B NE1 1 
ATOM   787  C CE2 . TRP A 1 101 ? 16.52500  13.29800 -19.48100 1.000 22.59302 ? 101 TRP B CE2 1 
ATOM   788  C CE3 . TRP A 1 101 ? 14.49000  14.02100 -20.58200 1.000 21.33424 ? 101 TRP B CE3 1 
ATOM   789  C CZ2 . TRP A 1 101 ? 16.16400  11.96100 -19.59300 1.000 22.65530 ? 101 TRP B CZ2 1 
ATOM   790  C CZ3 . TRP A 1 101 ? 14.13800  12.70500 -20.69200 1.000 20.90866 ? 101 TRP B CZ3 1 
ATOM   791  C CH2 . TRP A 1 101 ? 14.97300  11.68300 -20.20500 1.000 24.06405 ? 101 TRP B CH2 1 
ATOM   792  N N   . VAL A 1 102 ? 16.03200  19.48600 -22.18500 1.000 19.31100 ? 102 VAL B N   1 
ATOM   793  C CA  . VAL A 1 102 ? 15.52500  20.77900 -22.62900 1.000 16.37548 ? 102 VAL B CA  1 
ATOM   794  C C   . VAL A 1 102 ? 14.47000  20.52100 -23.69400 1.000 22.74185 ? 102 VAL B C   1 
ATOM   795  O O   . VAL A 1 102 ? 14.78800  19.94700 -24.73700 1.000 18.54054 ? 102 VAL B O   1 
ATOM   796  C CB  . VAL A 1 102 ? 16.62600  21.68900 -23.20700 1.000 17.61703 ? 102 VAL B CB  1 
ATOM   797  C CG1 . VAL A 1 102 ? 16.02000  23.00200 -23.67000 1.000 18.28560 ? 102 VAL B CG1 1 
ATOM   798  C CG2 . VAL A 1 102 ? 17.73200  21.94400 -22.18100 1.000 21.95455 ? 102 VAL B CG2 1 
ATOM   799  N N   . TYR A 1 103 ? 13.22100  20.91100 -23.42500 1.000 19.28509 ? 103 TYR B N   1 
ATOM   800  C CA  . TYR A 1 103 ? 12.12200  20.81700 -24.39000 1.000 17.97529 ? 103 TYR B CA  1 
ATOM   801  C C   . TYR A 1 103 ? 11.55100  22.20300 -24.63600 1.000 18.71745 ? 103 TYR B C   1 
ATOM   802  O O   . TYR A 1 103 ? 11.25600  22.92400 -23.68000 1.000 16.71498 ? 103 TYR B O   1 
ATOM   803  C CB  . TYR A 1 103 ? 10.99200  19.93400 -23.88700 1.000 15.10042 ? 103 TYR B CB  1 
ATOM   804  C CG  . TYR A 1 103 ? 11.24000  18.45600 -23.77800 1.000 18.03582 ? 103 TYR B CG  1 
ATOM   805  C CD1 . TYR A 1 103 ? 12.45400  17.88500 -24.13900 1.000 20.97630 ? 103 TYR B CD1 1 
ATOM   806  C CD2 . TYR A 1 103 ? 10.23100  17.62300 -23.32500 1.000 19.34844 ? 103 TYR B CD2 1 
ATOM   807  C CE1 . TYR A 1 103 ? 12.65500  16.51600 -24.02700 1.000 20.99249 ? 103 TYR B CE1 1 
ATOM   808  C CE2 . TYR A 1 103 ? 10.41800  16.27400 -23.21600 1.000 21.60317 ? 103 TYR B CE2 1 
ATOM   809  C CZ  . TYR A 1 103 ? 11.62400  15.71800 -23.57300 1.000 18.97670 ? 103 TYR B CZ  1 
ATOM   810  O OH  . TYR A 1 103 ? 11.77100  14.35000 -23.44200 1.000 19.13051 ? 103 TYR B OH  1 
ATOM   811  N N   . PHE A 1 104 ? 11.33600  22.55800 -25.90100 1.000 17.28074 ? 104 PHE B N   1 
ATOM   812  C CA  . PHE A 1 104 ? 10.70800  23.82400 -26.24700 1.000 20.44310 ? 104 PHE B CA  1 
ATOM   813  C C   . PHE A 1 104 ? 9.28600   23.55900 -26.71100 1.000 20.59995 ? 104 PHE B C   1 
ATOM   814  O O   . PHE A 1 104 ? 9.07600   22.75000 -27.62000 1.000 19.51896 ? 104 PHE B O   1 
ATOM   815  C CB  . PHE A 1 104 ? 11.46200  24.55900 -27.36300 1.000 19.54208 ? 104 PHE B CB  1 
ATOM   816  C CG  . PHE A 1 104 ? 12.81300  25.09900 -26.96100 1.000 19.64594 ? 104 PHE B CG  1 
ATOM   817  C CD1 . PHE A 1 104 ? 13.17200  25.24100 -25.62700 1.000 17.79134 ? 104 PHE B CD1 1 
ATOM   818  C CD2 . PHE A 1 104 ? 13.71000  25.49900 -27.93400 1.000 20.36761 ? 104 PHE B CD2 1 
ATOM   819  C CE1 . PHE A 1 104 ? 14.41300  25.74700 -25.26700 1.000 21.38328 ? 104 PHE B CE1 1 
ATOM   820  C CE2 . PHE A 1 104 ? 14.96800  25.99500 -27.58700 1.000 20.49822 ? 104 PHE B CE2 1 
ATOM   821  C CZ  . PHE A 1 104 ? 15.31200  26.13400 -26.24300 1.000 20.78879 ? 104 PHE B CZ  1 
ATOM   822  N N   . GLY A 1 105 ? 8.32200   24.24400 -26.10300 1.000 17.17132 ? 105 GLY B N   1 
ATOM   823  C CA  . GLY A 1 105 ? 6.95800   24.29200 -26.60700 1.000 19.21119 ? 105 GLY B CA  1 
ATOM   824  C C   . GLY A 1 105 ? 6.65400   25.67200 -27.16200 1.000 21.46389 ? 105 GLY B C   1 
ATOM   825  O O   . GLY A 1 105 ? 7.17700   26.67600 -26.66900 1.000 20.47103 ? 105 GLY B O   1 
ATOM   826  N N   . GLU A 1 106 ? 5.78200   25.72500 -28.18800 1.000 16.29459 ? 106 GLU B N   1 
ATOM   827  C CA  . GLU A 1 106 ? 5.46600   26.96600 -28.88100 1.000 16.74929 ? 106 GLU B CA  1 
ATOM   828  C C   . GLU A 1 106 ? 3.95900   27.17500 -28.92800 1.000 17.70721 ? 106 GLU B C   1 
ATOM   829  O O   . GLU A 1 106 ? 3.19300   26.22000 -29.11000 1.000 17.55011 ? 106 GLU B O   1 
ATOM   830  C CB  . GLU A 1 106 ? 5.97800   26.96800 -30.32000 1.000 17.33663 ? 106 GLU B CB  1 
ATOM   831  C CG  . GLU A 1 106 ? 7.48400   26.83400 -30.50100 1.000 17.99827 ? 106 GLU B CG  1 
ATOM   832  C CD  . GLU A 1 106 ? 7.79500   26.28700 -31.87700 1.000 22.71504 ? 106 GLU B CD  1 
ATOM   833  O OE1 . GLU A 1 106 ? 7.54200   25.08900 -32.08400 1.000 17.75228 ? 106 GLU B OE1 1 
ATOM   834  O OE2 . GLU A 1 106 ? 8.26700   27.04900 -32.74500 1.000 23.97073 ? 106 GLU B OE2 1 
ATOM   835  N N   . MET A 1 107 ? 3.55200   28.43800 -28.82500 1.000 17.25842 ? 107 MET B N   1 
ATOM   836  C CA  . MET A 1 107 ? 2.16200   28.88500 -28.84200 1.000 16.22940 ? 107 MET B CA  1 
ATOM   837  C C   . MET A 1 107 ? 2.04800   30.12200 -29.71500 1.000 17.03242 ? 107 MET B C   1 
ATOM   838  O O   . MET A 1 107 ? 3.01800   30.87700 -29.85000 1.000 17.21523 ? 107 MET B O   1 
ATOM   839  C CB  . MET A 1 107 ? 1.75400   29.19300 -27.39400 1.000 17.58545 ? 107 MET B CB  1 
ATOM   840  C CG  . MET A 1 107 ? 1.70700   27.93900 -26.57100 1.000 18.70259 ? 107 MET B CG  1 
ATOM   841  S SD  . MET A 1 107 ? 1.80600   28.33900 -24.83300 1.000 23.19427 ? 107 MET B SD  1 
ATOM   842  C CE  . MET A 1 107 ? 3.14900   29.48200 -24.85300 1.000 27.43851 ? 107 MET B CE  1 
ATOM   843  N N   . PRO A 1 108 ? 0.88000   30.37100 -30.30600 1.000 17.72276 ? 108 PRO B N   1 
ATOM   844  C CA  . PRO A 1 108 ? 0.68700   31.65000 -30.99900 1.000 20.02382 ? 108 PRO B CA  1 
ATOM   845  C C   . PRO A 1 108 ? 0.89700   32.81200 -30.03800 1.000 20.43002 ? 108 PRO B C   1 
ATOM   846  O O   . PRO A 1 108 ? 0.42400   32.79300 -28.89800 1.000 17.49132 ? 108 PRO B O   1 
ATOM   847  C CB  . PRO A 1 108 ? -0.76300  31.57500 -31.49800 1.000 22.98517 ? 108 PRO B CB  1 
ATOM   848  C CG  . PRO A 1 108 ? -1.07300  30.12000 -31.56200 1.000 24.94322 ? 108 PRO B CG  1 
ATOM   849  C CD  . PRO A 1 108 ? -0.29300  29.48700 -30.42900 1.000 23.61090 ? 108 PRO B CD  1 
ATOM   850  N N   . ALA A 1 109 ? 1.64100   33.82400 -30.49900 1.000 20.68366 ? 109 ALA B N   1 
ATOM   851  C CA  . ALA A 1 109 ? 1.87500   34.99800 -29.66300 1.000 21.62941 ? 109 ALA B CA  1 
ATOM   852  C C   . ALA A 1 109 ? 0.57000   35.61200 -29.16300 1.000 21.54698 ? 109 ALA B C   1 
ATOM   853  O O   . ALA A 1 109 ? 0.54500   36.22400 -28.08900 1.000 20.87527 ? 109 ALA B O   1 
ATOM   854  C CB  . ALA A 1 109 ? 2.68100   36.04800 -30.43500 1.000 23.26098 ? 109 ALA B CB  1 
ATOM   855  N N   . GLN A 1 110 ? -0.53000  35.43900 -29.91300 1.000 21.49770 ? 110 GLN B N   1 
ATOM   856  C CA  . GLN A 1 110 ? -1.77300  36.09700 -29.54000 1.000 20.00966 ? 110 GLN B CA  1 
ATOM   857  C C   . GLN A 1 110 ? -2.44700  35.48100 -28.31500 1.000 21.58323 ? 110 GLN B C   1 
ATOM   858  O O   . GLN A 1 110 ? -3.38400  36.08700 -27.77300 1.000 20.17567 ? 110 GLN B O   1 
ATOM   859  C CB  . GLN A 1 110 ? -2.77600  36.09100 -30.70900 1.000 28.17048 ? 110 GLN B CB  1 
ATOM   860  C CG  . GLN A 1 110 ? -2.27700  36.59800 -32.07200 1.000 24.82740 ? 110 GLN B CG  1 
ATOM   861  C CD  . GLN A 1 110 ? -1.55400  35.53900 -32.92600 1.000 28.75127 ? 110 GLN B CD  1 
ATOM   862  O OE1 . GLN A 1 110 ? -0.46000  35.09200 -32.62600 1.000 31.54179 ? 110 GLN B OE1 1 
ATOM   863  N NE2 . GLN A 1 110 ? -2.19100  35.16400 -34.03100 1.000 39.11420 ? 110 GLN B NE2 1 
ATOM   864  N N   . GLN A 1 111 ? -2.03900  34.28900 -27.87900 1.000 19.45378 ? 111 GLN B N   1 
ATOM   865  C CA  . GLN A 1 111 ? -2.50400  33.73500 -26.60900 1.000 21.96099 ? 111 GLN B CA  1 
ATOM   866  C C   . GLN A 1 111 ? -1.38700  33.68500 -25.56700 1.000 17.82387 ? 111 GLN B C   1 
ATOM   867  O O   . GLN A 1 111 ? -1.31700  32.75400 -24.75800 1.000 18.22632 ? 111 GLN B O   1 
ATOM   868  C CB  . GLN A 1 111 ? -3.11800  32.34600 -26.80700 1.000 20.86469 ? 111 GLN B CB  1 
ATOM   869  C CG  . GLN A 1 111 ? -2.18100  31.30200 -27.40400 1.000 20.65335 ? 111 GLN B CG  1 
ATOM   870  C CD  . GLN A 1 111 ? -2.93800  30.20400 -28.13600 1.000 21.38122 ? 111 GLN B CD  1 
ATOM   871  O OE1 . GLN A 1 111 ? -3.68200  30.48300 -29.07500 1.000 22.20431 ? 111 GLN B OE1 1 
ATOM   872  N NE2 . GLN A 1 111 ? -2.73700  28.95300 -27.72200 1.000 19.07102 ? 111 GLN B NE2 1 
ATOM   873  N N   . MET A 1 112 ? -0.49700  34.67800 -25.58100 1.000 17.55890 ? 112 MET B N   1 
ATOM   874  C CA  . MET A 1 112 ? 0.63500   34.72400 -24.65900 1.000 18.97534 ? 112 MET B CA  1 
ATOM   875  C C   . MET A 1 112 ? 0.80700   36.12800 -24.10700 1.000 17.30792 ? 112 MET B C   1 
ATOM   876  O O   . MET A 1 112 ? 0.98900   37.07800 -24.86700 1.000 22.03984 ? 112 MET B O   1 
ATOM   877  C CB  . MET A 1 112 ? 1.92800   34.26200 -25.34200 1.000 20.61339 ? 112 MET B CB  1 
ATOM   878  C CG  . MET A 1 112 ? 1.96500   32.80100 -25.72200 1.000 19.46600 ? 112 MET B CG  1 
ATOM   879  S SD  . MET A 1 112 ? 3.42300   32.46100 -26.73800 1.000 21.32366 ? 112 MET B SD  1 
ATOM   880  C CE  . MET A 1 112 ? 4.65300   32.44600 -25.47200 1.000 18.18564 ? 112 MET B CE  1 
ATOM   881  N N   . VAL A 1 113 ? 0.81100   36.24300 -22.78500 1.000 18.60699 ? 113 VAL B N   1 
ATOM   882  C CA  . VAL A 1 113 ? 0.83100   37.52000 -22.08400 1.000 17.32433 ? 113 VAL B CA  1 
ATOM   883  C C   . VAL A 1 113 ? 2.05300   37.54900 -21.16600 1.000 18.12526 ? 113 VAL B C   1 
ATOM   884  O O   . VAL A 1 113 ? 2.19800   36.67100 -20.30600 1.000 19.15238 ? 113 VAL B O   1 
ATOM   885  C CB  . VAL A 1 113 ? -0.45400  37.71100 -21.26200 1.000 16.78621 ? 113 VAL B CB  1 
ATOM   886  C CG1 . VAL A 1 113 ? -0.31300  38.87200 -20.28500 1.000 18.27278 ? 113 VAL B CG1 1 
ATOM   887  C CG2 . VAL A 1 113 ? -1.65800  37.87600 -22.17700 1.000 19.19492 ? 113 VAL B CG2 1 
ATOM   888  N N   . ASP A 1 114 ? 2.93300   38.54100 -21.35400 1.000 18.69009 ? 114 ASP B N   1 
ATOM   889  C CA  . ASP A 1 114 ? 4.02400   38.85800 -20.42300 1.000 18.85793 ? 114 ASP B CA  1 
ATOM   890  C C   . ASP A 1 114 ? 3.74600   40.21400 -19.80100 1.000 19.87656 ? 114 ASP B C   1 
ATOM   891  O O   . ASP A 1 114 ? 3.32700   41.13400 -20.50300 1.000 17.03502 ? 114 ASP B O   1 
ATOM   892  C CB  . ASP A 1 114 ? 5.41700   38.94700 -21.07900 1.000 19.74625 ? 114 ASP B CB  1 
ATOM   893  C CG  . ASP A 1 114 ? 5.88300   37.65600 -21.73100 1.000 20.43178 ? 114 ASP B CG  1 
ATOM   894  O OD1 . ASP A 1 114 ? 5.18000   36.63000 -21.67000 1.000 21.50821 ? 114 ASP B OD1 1 
ATOM   895  O OD2 . ASP A 1 114 ? 7.03900   37.65400 -22.22300 1.000 22.19189 ? 114 ASP B OD2 1 
ATOM   896  N N   . TYR A 1 115 ? 3.98000   40.35000 -18.49200 1.000 19.54291 ? 115 TYR B N   1 
ATOM   897  C CA  . TYR A 1 115 ? 3.80000   41.64300 -17.82700 1.000 20.46394 ? 115 TYR B CA  1 
ATOM   898  C C   . TYR A 1 115 ? 2.40500   42.20500 -18.07600 1.000 19.26976 ? 115 TYR B C   1 
ATOM   899  O O   . TYR A 1 115 ? 2.21800   43.41700 -18.20900 1.000 19.37711 ? 115 TYR B O   1 
ATOM   900  C CB  . TYR A 1 115 ? 4.85300   42.66700 -18.27900 1.000 21.05192 ? 115 TYR B CB  1 
ATOM   901  C CG  . TYR A 1 115 ? 6.29400   42.35400 -17.90000 1.000 21.31167 ? 115 TYR B CG  1 
ATOM   902  C CD1 . TYR A 1 115 ? 6.81800   42.78000 -16.68200 1.000 25.24859 ? 115 TYR B CD1 1 
ATOM   903  C CD2 . TYR A 1 115 ? 7.15000   41.71700 -18.79300 1.000 24.08087 ? 115 TYR B CD2 1 
ATOM   904  C CE1 . TYR A 1 115 ? 8.14800   42.52600 -16.33500 1.000 24.68642 ? 115 TYR B CE1 1 
ATOM   905  C CE2 . TYR A 1 115 ? 8.48700   41.45900 -18.45100 1.000 22.77267 ? 115 TYR B CE2 1 
ATOM   906  C CZ  . TYR A 1 115 ? 8.97100   41.86900 -17.22400 1.000 22.51984 ? 115 TYR B CZ  1 
ATOM   907  O OH  . TYR A 1 115 ? 10.29100  41.62000 -16.88000 1.000 23.48671 ? 115 TYR B OH  1 
ATOM   908  N N   . GLY A 1 116 ? 1.41100   41.32800 -18.18600 1.000 19.80082 ? 116 GLY B N   1 
ATOM   909  C CA  . GLY A 1 116 ? 0.05900   41.78700 -18.40700 1.000 22.08515 ? 116 GLY B CA  1 
ATOM   910  C C   . GLY A 1 116 ? -0.25200  42.23000 -19.82300 1.000 20.68729 ? 116 GLY B C   1 
ATOM   911  O O   . GLY A 1 116 ? -1.36800  42.69600 -20.06900 1.000 23.22492 ? 116 GLY B O   1 
ATOM   912  N N   . ARG A 1 117 ? 0.67900   42.09500 -20.76400 1.000 20.10738 ? 117 ARG B N   1 
ATOM   913  C CA  . ARG A 1 117 ? 0.45500   42.52500 -22.14700 1.000 20.69360 ? 117 ARG B CA  1 
ATOM   914  C C   . ARG A 1 117 ? 0.62900   41.36100 -23.11100 1.000 21.23951 ? 117 ARG B C   1 
ATOM   915  O O   . ARG A 1 117 ? 1.46300   40.48300 -22.89900 1.000 18.85017 ? 117 ARG B O   1 
ATOM   916  C CB  . ARG A 1 117 ? 1.42300   43.65900 -22.55300 1.000 20.47901 ? 117 ARG B CB  1 
ATOM   917  C CG  . ARG A 1 117 ? 1.29600   44.89400 -21.67500 1.000 23.96244 ? 117 ARG B CG  1 
ATOM   918  C CD  . ARG A 1 117 ? -0.14100  45.43200 -21.72600 1.000 27.62924 ? 117 ARG B CD  1 
ATOM   919  N NE  . ARG A 1 117 ? -0.45500  45.91800 -23.06300 1.000 29.34403 ? 117 ARG B NE  1 
ATOM   920  C CZ  . ARG A 1 117 ? -0.11800  47.12200 -23.50300 1.000 33.24450 ? 117 ARG B CZ  1 
ATOM   921  N NH1 . ARG A 1 117 ? 0.47900   48.00200 -22.71100 1.000 34.07700 ? 117 ARG B NH1 1 
ATOM   922  N NH2 . ARG A 1 117 ? -0.38600  47.45300 -24.76400 1.000 36.48779 ? 117 ARG B NH2 1 
ATOM   923  N N   . PHE A 1 118 ? -0.14800  41.37100 -24.19100 1.000 20.19681 ? 118 PHE B N   1 
ATOM   924  C CA  . PHE A 1 118 ? 0.01400   40.36500 -25.22900 1.000 21.30197 ? 118 PHE B CA  1 
ATOM   925  C C   . PHE A 1 118 ? 1.31500   40.57800 -25.98900 1.000 22.00750 ? 118 PHE B C   1 
ATOM   926  O O   . PHE A 1 118 ? 1.69500   41.70900 -26.29900 1.000 21.79810 ? 118 PHE B O   1 
ATOM   927  C CB  . PHE A 1 118 ? -1.17300  40.40500 -26.19200 1.000 20.33082 ? 118 PHE B CB  1 
ATOM   928  C CG  . PHE A 1 118 ? -2.40600  39.79300 -25.61500 1.000 19.29722 ? 118 PHE B CG  1 
ATOM   929  C CD1 . PHE A 1 118 ? -3.26400  40.54300 -24.82700 1.000 23.58826 ? 118 PHE B CD1 1 
ATOM   930  C CD2 . PHE A 1 118 ? -2.68300  38.45700 -25.80800 1.000 21.31109 ? 118 PHE B CD2 1 
ATOM   931  C CE1 . PHE A 1 118 ? -4.39900  39.97000 -24.27200 1.000 21.87535 ? 118 PHE B CE1 1 
ATOM   932  C CE2 . PHE A 1 118 ? -3.80100  37.88900 -25.26200 1.000 19.54504 ? 118 PHE B CE2 1 
ATOM   933  C CZ  . PHE A 1 118 ? -4.66100  38.65000 -24.48400 1.000 21.22728 ? 118 PHE B CZ  1 
ATOM   934  N N   . LEU A 1 119 ? 2.00100   39.48500 -26.27900 1.000 19.89118 ? 119 LEU B N   1 
ATOM   935  C CA  . LEU A 1 119 ? 3.28200   39.54700 -26.95000 1.000 19.80622 ? 119 LEU B CA  1 
ATOM   936  C C   . LEU A 1 119 ? 3.10300   39.88200 -28.42700 1.000 22.07261 ? 119 LEU B C   1 
ATOM   937  O O   . LEU A 1 119 ? 2.06900   39.56700 -29.01600 1.000 21.26292 ? 119 LEU B O   1 
ATOM   938  C CB  . LEU A 1 119 ? 4.01200   38.21700 -26.82100 1.000 18.85782 ? 119 LEU B CB  1 
ATOM   939  C CG  . LEU A 1 119 ? 4.58400   37.94400 -25.43300 1.000 20.41150 ? 119 LEU B CG  1 
ATOM   940  C CD1 . LEU A 1 119 ? 5.17000   36.53900 -25.35500 1.000 20.04417 ? 119 LEU B CD1 1 
ATOM   941  C CD2 . LEU A 1 119 ? 5.65500   38.98100 -25.13400 1.000 23.20355 ? 119 LEU B CD2 1 
ATOM   942  N N   . PRO A 1 120 ? 4.10700   40.52700 -29.04600 1.000 19.79700 ? 120 PRO B N   1 
ATOM   943  C CA  . PRO A 1 120 ? 4.08800   40.71100 -30.49800 1.000 19.75514 ? 120 PRO B CA  1 
ATOM   944  C C   . PRO A 1 120 ? 4.65200   39.50000 -31.21000 1.000 23.51796 ? 120 PRO B C   1 
ATOM   945  O O   . PRO A 1 120 ? 5.08600   38.54200 -30.56100 1.000 22.17201 ? 120 PRO B O   1 
ATOM   946  C CB  . PRO A 1 120 ? 4.99400   41.92800 -30.69700 1.000 24.20871 ? 120 PRO B CB  1 
ATOM   947  C CG  . PRO A 1 120 ? 6.04800   41.71800 -29.66900 1.000 22.39887 ? 120 PRO B CG  1 
ATOM   948  C CD  . PRO A 1 120 ? 5.33300   41.09700 -28.45500 1.000 23.99855 ? 120 PRO B CD  1 
ATOM   949  N N   . GLN A 1 121 ? 4.70900   39.55500 -32.54100 1.000 22.82578 ? 121 GLN B N   1 
ATOM   950  C CA  . GLN A 1 121 ? 5.39200   38.51100 -33.29000 1.000 25.52978 ? 121 GLN B CA  1 
ATOM   951  C C   . GLN A 1 121 ? 6.89300   38.66200 -33.03700 1.000 26.95485 ? 121 GLN B C   1 
ATOM   952  O O   . GLN A 1 121 ? 7.35400   39.76300 -32.73300 1.000 25.08685 ? 121 GLN B O   1 
ATOM   953  C CB  . GLN A 1 121 ? 5.09500   38.66400 -34.77600 1.000 26.77141 ? 121 GLN B CB  1 
ATOM   954  C CG  . GLN A 1 121 ? 3.73100   38.09200 -35.26300 1.000 34.01131 ? 121 GLN B CG  1 
ATOM   955  C CD  . GLN A 1 121 ? 3.19700   36.84800 -34.53600 1.000 29.91316 ? 121 GLN B CD  1 
ATOM   956  O OE1 . GLN A 1 121 ? 3.91600   35.87900 -34.29100 1.000 33.27934 ? 121 GLN B OE1 1 
ATOM   957  N NE2 . GLN A 1 121 ? 1.92200   36.89100 -34.18000 1.000 31.06588 ? 121 GLN B NE2 1 
ATOM   958  N N   . PRO A 1 122 ? 7.68000   37.56700 -33.14900 1.000 27.42632 ? 122 PRO B N   1 
ATOM   959  C CA  . PRO A 1 122 ? 9.10400   37.61800 -32.76900 1.000 31.26877 ? 122 PRO B CA  1 
ATOM   960  C C   . PRO A 1 122 ? 9.86200   38.90300 -33.11300 1.000 34.90903 ? 122 PRO B C   1 
ATOM   961  O O   . PRO A 1 122 ? 9.69200   39.87700 -32.38700 1.000 43.16031 ? 122 PRO B O   1 
ATOM   962  C CB  . PRO A 1 122 ? 9.65700   36.39100 -33.48700 1.000 31.34925 ? 122 PRO B CB  1 
ATOM   963  C CG  . PRO A 1 122 ? 8.57500   35.38800 -33.17100 1.000 31.32903 ? 122 PRO B CG  1 
ATOM   964  C CD  . PRO A 1 122 ? 7.26300   36.17200 -33.37500 1.000 31.04710 ? 122 PRO B CD  1 
ATOM   965  N N   . GLY A 1 123 ? 10.65600  38.98800 -34.16300 1.000 36.95655 ? 123 GLY B N   1 
ATOM   966  C CA  . GLY A 1 123 ? 11.47800  40.18600 -34.35600 1.000 33.60892 ? 123 GLY B CA  1 
ATOM   967  C C   . GLY A 1 123 ? 10.87400  41.57800 -34.16600 1.000 33.59273 ? 123 GLY B C   1 
ATOM   968  O O   . GLY A 1 123 ? 11.51600  42.57800 -34.50600 1.000 33.28795 ? 123 GLY B O   1 
ATOM   969  N N   . HIS A 1 124 ? 9.66500   41.66700 -33.60200 1.000 25.89834 ? 124 HIS B N   1 
ATOM   970  C CA  . HIS A 1 124 ? 8.94200   42.92300 -33.41300 1.000 30.23516 ? 124 HIS B CA  1 
ATOM   971  C C   . HIS A 1 124 ? 8.99200   43.43000 -31.97700 1.000 30.24232 ? 124 HIS B C   1 
ATOM   972  O O   . HIS A 1 124 ? 8.16600   44.26300 -31.59400 1.000 29.26469 ? 124 HIS B O   1 
ATOM   973  C CB  . HIS A 1 124 ? 7.48200   42.77100 -33.85000 1.000 32.76697 ? 124 HIS B CB  1 
ATOM   974  C CG  . HIS A 1 124 ? 7.31100   42.55200 -35.32100 1.000 37.26971 ? 124 HIS B CG  1 
ATOM   975  N ND1 . HIS A 1 124 ? 8.14000   41.73100 -36.05500 1.000 37.74399 ? 124 HIS B ND1 1 
ATOM   976  C CD2 . HIS A 1 124 ? 6.39200   43.03500 -36.19200 1.000 44.45527 ? 124 HIS B CD2 1 
ATOM   977  C CE1 . HIS A 1 124 ? 7.75200   41.73100 -37.31800 1.000 38.06286 ? 124 HIS B CE1 1 
ATOM   978  N NE2 . HIS A 1 124 ? 6.69100   42.51000 -37.42700 1.000 43.48717 ? 124 HIS B NE2 1 
ATOM   979  N N   . GLU A 1 125 ? 9.94800   42.95700 -31.17700 1.000 26.97987 ? 125 GLU B N   1 
ATOM   980  C CA  . GLU A 1 125 ? 9.95300   43.31400 -29.76200 1.000 30.85480 ? 125 GLU B CA  1 
ATOM   981  C C   . GLU A 1 125 ? 10.22100  44.79500 -29.55200 1.000 31.53162 ? 125 GLU B C   1 
ATOM   982  O O   . GLU A 1 125 ? 9.76800   45.36500 -28.55300 1.000 29.05569 ? 125 GLU B O   1 
ATOM   983  C CB  . GLU A 1 125 ? 10.99600  42.48800 -29.00400 1.000 30.17908 ? 125 GLU B CB  1 
ATOM   984  C CG  . GLU A 1 125 ? 10.65000  41.02000 -28.84900 1.000 27.64629 ? 125 GLU B CG  1 
ATOM   985  C CD  . GLU A 1 125 ? 11.00800  40.22800 -30.09300 1.000 29.10058 ? 125 GLU B CD  1 
ATOM   986  O OE1 . GLU A 1 125 ? 11.67900  40.79800 -30.97600 1.000 29.36446 ? 125 GLU B OE1 1 
ATOM   987  O OE2 . GLU A 1 125 ? 10.60800  39.04600 -30.20600 1.000 26.35548 ? 125 GLU B OE2 1 
ATOM   988  N N   . GLY A 1 126 ? 10.95300  45.43100 -30.46900 1.000 34.53719 ? 126 GLY B N   1 
ATOM   989  C CA  . GLY A 1 126 ? 11.35300  46.81100 -30.24300 1.000 32.13930 ? 126 GLY B CA  1 
ATOM   990  C C   . GLY A 1 126 ? 10.19000  47.78200 -30.32500 1.000 31.45888 ? 126 GLY B C   1 
ATOM   991  O O   . GLY A 1 126 ? 9.96900   48.58300 -29.41200 1.000 37.26155 ? 126 GLY B O   1 
ATOM   992  N N   . GLU A 1 127 ? 9.44100   47.73800 -31.42400 1.000 34.09879 ? 127 GLU B N   1 
ATOM   993  C CA  . GLU A 1 127 ? 8.30400   48.64100 -31.56900 1.000 39.03177 ? 127 GLU B CA  1 
ATOM   994  C C   . GLU A 1 127 ? 7.24200   48.34800 -30.51700 1.000 34.23529 ? 127 GLU B C   1 
ATOM   995  O O   . GLU A 1 127 ? 6.61400   49.26800 -29.98300 1.000 32.57044 ? 127 GLU B O   1 
ATOM   996  C CB  . GLU A 1 127 ? 7.71900   48.52100 -32.97500 1.000 35.97203 ? 127 GLU B CB  1 
ATOM   997  C CG  . GLU A 1 127 ? 7.58700   47.09100 -33.47600 1.000 42.03759 ? 127 GLU B CG  1 
ATOM   998  C CD  . GLU A 1 127 ? 7.54000   46.99000 -34.99600 1.000 50.96565 ? 127 GLU B CD  1 
ATOM   999  O OE1 . GLU A 1 127 ? 8.37100   47.64500 -35.66800 1.000 58.82942 ? 127 GLU B OE1 1 
ATOM   1000 O OE2 . GLU A 1 127 ? 6.69400   46.22200 -35.51300 1.000 50.33069 ? 127 GLU B OE2 1 
ATOM   1001 N N   . TRP A 1 128 ? 7.03500   47.06900 -30.20800 1.000 31.08923 ? 128 TRP B N   1 
ATOM   1002 C CA  . TRP A 1 128 ? 6.09300   46.68100 -29.16100 1.000 30.32106 ? 128 TRP B CA  1 
ATOM   1003 C C   . TRP A 1 128 ? 6.44900   47.33200 -27.83000 1.000 30.16377 ? 128 TRP B C   1 
ATOM   1004 O O   . TRP A 1 128 ? 5.59500   47.93600 -27.16800 1.000 30.47204 ? 128 TRP B O   1 
ATOM   1005 C CB  . TRP A 1 128 ? 6.10000   45.16400 -29.02800 1.000 26.91325 ? 128 TRP B CB  1 
ATOM   1006 C CG  . TRP A 1 128 ? 5.30400   44.60700 -27.89100 1.000 28.04310 ? 128 TRP B CG  1 
ATOM   1007 C CD1 . TRP A 1 128 ? 3.95700   44.35300 -27.88100 1.000 26.81871 ? 128 TRP B CD1 1 
ATOM   1008 C CD2 . TRP A 1 128 ? 5.80300   44.18400 -26.61500 1.000 27.61371 ? 128 TRP B CD2 1 
ATOM   1009 N NE1 . TRP A 1 128 ? 3.59500   43.80600 -26.66900 1.000 26.43536 ? 128 TRP B NE1 1 
ATOM   1010 C CE2 . TRP A 1 128 ? 4.70600   43.70000 -25.87500 1.000 22.64811 ? 128 TRP B CE2 1 
ATOM   1011 C CE3 . TRP A 1 128 ? 7.07100   44.16500 -26.02600 1.000 25.58209 ? 128 TRP B CE3 1 
ATOM   1012 C CZ2 . TRP A 1 128 ? 4.84000   43.19900 -24.58200 1.000 22.05772 ? 128 TRP B CZ2 1 
ATOM   1013 C CZ3 . TRP A 1 128 ? 7.19900   43.67600 -24.73000 1.000 28.39837 ? 128 TRP B CZ3 1 
ATOM   1014 C CH2 . TRP A 1 128 ? 6.08700   43.20400 -24.02200 1.000 26.24826 ? 128 TRP B CH2 1 
ATOM   1015 N N   . PHE A 1 129 ? 7.71400   47.21000 -27.41700 1.000 27.87549 ? 129 PHE B N   1 
ATOM   1016 C CA  . PHE A 1 129 ? 8.13800   47.79500 -26.14900 1.000 30.35877 ? 129 PHE B CA  1 
ATOM   1017 C C   . PHE A 1 129 ? 8.01100   49.31200 -26.18100 1.000 31.15871 ? 129 PHE B C   1 
ATOM   1018 O O   . PHE A 1 129 ? 7.56600   49.93000 -25.20500 1.000 29.56137 ? 129 PHE B O   1 
ATOM   1019 C CB  . PHE A 1 129 ? 9.58100   47.38300 -25.82800 1.000 30.41793 ? 129 PHE B CB  1 
ATOM   1020 C CG  . PHE A 1 129 ? 10.17300  48.12300 -24.65400 1.000 32.56237 ? 129 PHE B CG  1 
ATOM   1021 C CD1 . PHE A 1 129 ? 9.89900   47.70800 -23.36100 1.000 33.38168 ? 129 PHE B CD1 1 
ATOM   1022 C CD2 . PHE A 1 129 ? 11.00900  49.21500 -24.83600 1.000 33.59931 ? 129 PHE B CD2 1 
ATOM   1023 C CE1 . PHE A 1 129 ? 10.44500  48.37200 -22.26100 1.000 26.82115 ? 129 PHE B CE1 1 
ATOM   1024 C CE2 . PHE A 1 129 ? 11.55500  49.88200 -23.74100 1.000 31.58000 ? 129 PHE B CE2 1 
ATOM   1025 C CZ  . PHE A 1 129 ? 11.26600  49.45600 -22.45500 1.000 30.85053 ? 129 PHE B CZ  1 
ATOM   1026 N N   . ASP A 1 130 ? 8.39000   49.93000 -27.30100 1.000 32.08000 ? 130 ASP B N   1 
ATOM   1027 C CA  . ASP A 1 130 ? 8.30700   51.38000 -27.40300 1.000 34.89135 ? 130 ASP B CA  1 
ATOM   1028 C C   . ASP A 1 130 ? 6.87600   51.86600 -27.22600 1.000 32.99203 ? 130 ASP B C   1 
ATOM   1029 O O   . ASP A 1 130 ? 6.65200   52.94200 -26.66600 1.000 34.76455 ? 130 ASP B O   1 
ATOM   1030 C CB  . ASP A 1 130 ? 8.89300   51.84300 -28.74200 1.000 33.28286 ? 130 ASP B CB  1 
ATOM   1031 C CG  . ASP A 1 130 ? 10.41300  51.66000 -28.81000 1.000 36.10119 ? 130 ASP B CG  1 
ATOM   1032 O OD1 . ASP A 1 130 ? 11.06100  51.66400 -27.74700 1.000 38.56054 ? 130 ASP B OD1 1 
ATOM   1033 O OD2 . ASP A 1 130 ? 10.96100  51.49900 -29.92100 1.000 39.87959 ? 130 ASP B OD2 1 
ATOM   1034 N N   . ASN A 1 131 ? 5.89900   51.06500 -27.62500 1.000 30.87458 ? 131 ASN B N   1 
ATOM   1035 C CA  . ASN A 1 131 ? 4.50900   51.48800 -27.56200 1.000 34.91215 ? 131 ASN B CA  1 
ATOM   1036 C C   . ASN A 1 131 ? 3.82000   51.10300 -26.26000 1.000 31.71291 ? 131 ASN B C   1 
ATOM   1037 O O   . ASN A 1 131 ? 2.62500   51.36700 -26.11200 1.000 30.91310 ? 131 ASN B O   1 
ATOM   1038 C CB  . ASN A 1 131 ? 3.75000   50.92100 -28.76100 1.000 38.47968 ? 131 ASN B CB  1 
ATOM   1039 C CG  . ASN A 1 131 ? 3.84100   51.83000 -29.97600 1.000 46.34137 ? 131 ASN B CG  1 
ATOM   1040 O OD1 . ASN A 1 131 ? 4.72700   51.67100 -30.82200 1.000 48.64847 ? 131 ASN B OD1 1 
ATOM   1041 N ND2 . ASN A 1 131 ? 2.92200   52.78300 -30.07200 1.000 47.06932 ? 131 ASN B ND2 1 
ATOM   1042 N N   . LEU A 1 132 ? 4.52800   50.48600 -25.32100 1.000 29.04804 ? 132 LEU B N   1 
ATOM   1043 C CA  . LEU A 1 132 ? 3.98400   50.30700 -23.98400 1.000 27.79996 ? 132 LEU B CA  1 
ATOM   1044 C C   . LEU A 1 132 ? 3.95200   51.64900 -23.25500 1.000 30.62074 ? 132 LEU B C   1 
ATOM   1045 O O   . LEU A 1 132 ? 4.63900   52.60400 -23.63000 1.000 29.56981 ? 132 LEU B O   1 
ATOM   1046 C CB  . LEU A 1 132 ? 4.82000   49.29700 -23.19600 1.000 29.24359 ? 132 LEU B CB  1 
ATOM   1047 C CG  . LEU A 1 132 ? 4.94300   47.90100 -23.80000 1.000 28.71768 ? 132 LEU B CG  1 
ATOM   1048 C CD1 . LEU A 1 132 ? 6.01100   47.13500 -23.06500 1.000 28.12688 ? 132 LEU B CD1 1 
ATOM   1049 C CD2 . LEU A 1 132 ? 3.60500   47.16500 -23.75000 1.000 32.67750 ? 132 LEU B CD2 1 
ATOM   1050 N N   . SER A 1 133 ? 3.13100   51.72400 -22.20900 1.000 26.73788 ? 133 SER B N   1 
ATOM   1051 C CA  . SER A 1 133 ? 3.06200   52.94300 -21.42000 1.000 28.96363 ? 133 SER B CA  1 
ATOM   1052 C C   . SER A 1 133 ? 4.38300   53.16800 -20.69700 1.000 29.86644 ? 133 SER B C   1 
ATOM   1053 O O   . SER A 1 133 ? 5.18300   52.25000 -20.51800 1.000 24.22361 ? 133 SER B O   1 
ATOM   1054 C CB  . SER A 1 133 ? 1.92600   52.88500 -20.40100 1.000 23.82065 ? 133 SER B CB  1 
ATOM   1055 O OG  . SER A 1 133 ? 2.24000   52.01400 -19.32500 1.000 25.43689 ? 133 SER B OG  1 
ATOM   1056 N N   . SER A 1 134 ? 4.59200   54.41200 -20.26200 1.000 30.54346 ? 134 SER B N   1 
ATOM   1057 C CA  . SER A 1 134 ? 5.86100   54.77400 -19.64000 1.000 31.60047 ? 134 SER B CA  1 
ATOM   1058 C C   . SER A 1 134 ? 6.08200   54.01500 -18.33300 1.000 27.57749 ? 134 SER B C   1 
ATOM   1059 O O   . SER A 1 134 ? 7.21000   53.60300 -18.03200 1.000 25.20035 ? 134 SER B O   1 
ATOM   1060 C CB  . SER A 1 134 ? 5.91800   56.28900 -19.42400 1.000 33.12995 ? 134 SER B CB  1 
ATOM   1061 O OG  . SER A 1 134 ? 5.23100   56.65800 -18.24000 1.000 35.10001 ? 134 SER B OG  1 
ATOM   1062 N N   . ASP A 1 135 ? 5.02900   53.79700 -17.54000 1.000 24.37036 ? 135 ASP B N   1 
ATOM   1063 C CA  . ASP A 1 135 ? 5.24400   53.03800 -16.31000 1.000 25.87930 ? 135 ASP B CA  1 
ATOM   1064 C C   . ASP A 1 135 ? 5.56900   51.57700 -16.60200 1.000 26.26664 ? 135 ASP B C   1 
ATOM   1065 O O   . ASP A 1 135 ? 6.36300   50.96400 -15.88200 1.000 29.06680 ? 135 ASP B O   1 
ATOM   1066 C CB  . ASP A 1 135 ? 4.03900   53.13400 -15.37400 1.000 31.48036 ? 135 ASP B CB  1 
ATOM   1067 C CG  . ASP A 1 135 ? 3.89100   54.51300 -14.74800 1.000 34.47989 ? 135 ASP B CG  1 
ATOM   1068 O OD1 . ASP A 1 135 ? 4.87800   55.27700 -14.73600 1.000 30.99657 ? 135 ASP B OD1 1 
ATOM   1069 O OD2 . ASP A 1 135 ? 2.80300   54.81100 -14.21500 1.000 34.27257 ? 135 ASP B OD2 1 
ATOM   1070 N N   . GLU A 1 136 ? 4.96100   50.99900 -17.64200 1.000 27.12489 ? 136 GLU B N   1 
ATOM   1071 C CA  . GLU A 1 136 ? 5.27400   49.62000 -17.99800 1.000 25.56589 ? 136 GLU B CA  1 
ATOM   1072 C C   . GLU A 1 136 ? 6.72400   49.49300 -18.44500 1.000 26.93285 ? 136 GLU B C   1 
ATOM   1073 O O   . GLU A 1 136 ? 7.42800   48.56400 -18.03100 1.000 22.58074 ? 136 GLU B O   1 
ATOM   1074 C CB  . GLU A 1 136 ? 4.33900   49.13500 -19.10500 1.000 22.87797 ? 136 GLU B CB  1 
ATOM   1075 C CG  . GLU A 1 136 ? 2.92000   48.91000 -18.64600 1.000 26.94013 ? 136 GLU B CG  1 
ATOM   1076 C CD  . GLU A 1 136 ? 1.97300   48.68100 -19.80100 1.000 30.08507 ? 136 GLU B CD  1 
ATOM   1077 O OE1 . GLU A 1 136 ? 1.55400   49.66800 -20.45300 1.000 30.00826 ? 136 GLU B OE1 1 
ATOM   1078 O OE2 . GLU A 1 136 ? 1.65100   47.50900 -20.06100 1.000 27.81068 ? 136 GLU B OE2 1 
ATOM   1079 N N   . ARG A 1 137 ? 7.17400   50.41400 -19.30600 1.000 22.03238 ? 137 ARG B N   1 
ATOM   1080 C CA  . ARG A 1 137 ? 8.55500   50.40300 -19.77900 1.000 25.43390 ? 137 ARG B CA  1 
ATOM   1081 C C   . ARG A 1 137 ? 9.51900   50.49300 -18.60500 1.000 28.80308 ? 137 ARG B C   1 
ATOM   1082 O O   . ARG A 1 137 ? 10.46700  49.70500 -18.50400 1.000 25.83743 ? 137 ARG B O   1 
ATOM   1083 C CB  . ARG A 1 137 ? 8.77900   51.56400 -20.75400 1.000 29.20548 ? 137 ARG B CB  1 
ATOM   1084 C CG  . ARG A 1 137 ? 8.04100   51.42200 -22.08100 1.000 28.73476 ? 137 ARG B CG  1 
ATOM   1085 C CD  . ARG A 1 137 ? 8.71700   52.21000 -23.19400 1.000 31.50525 ? 137 ARG B CD  1 
ATOM   1086 N NE  . ARG A 1 137 ? 8.93400   53.61500 -22.85500 1.000 34.24406 ? 137 ARG B NE  1 
ATOM   1087 C CZ  . ARG A 1 137 ? 7.97100   54.50700 -22.64700 1.000 37.46393 ? 137 ARG B CZ  1 
ATOM   1088 N NH1 . ARG A 1 137 ? 6.69300   54.19700 -22.79700 1.000 32.86576 ? 137 ARG B NH1 1 
ATOM   1089 N NH2 . ARG A 1 137 ? 8.30100   55.74900 -22.30200 1.000 33.87263 ? 137 ARG B NH2 1 
ATOM   1090 N N   . ALA A 1 138 ? 9.25800   51.43000 -17.68600 1.000 25.66111 ? 138 ALA B N   1 
ATOM   1091 C CA  . ALA A 1 138 ? 10.11800  51.60700 -16.52200 1.000 27.83390 ? 138 ALA B CA  1 
ATOM   1092 C C   . ALA A 1 138 ? 10.17700  50.34100 -15.67600 1.000 27.33241 ? 138 ALA B C   1 
ATOM   1093 O O   . ALA A 1 138 ? 11.24700  49.95800 -15.19100 1.000 26.14365 ? 138 ALA B O   1 
ATOM   1094 C CB  . ALA A 1 138 ? 9.62400   52.78300 -15.68300 1.000 25.43664 ? 138 ALA B CB  1 
ATOM   1095 N N   . PHE A 1 139 ? 9.03700   49.67200 -15.49000 1.000 25.24866 ? 139 PHE B N   1 
ATOM   1096 C CA  . PHE A 1 139 ? 9.02900   48.45500 -14.69100 1.000 24.77508 ? 139 PHE B CA  1 
ATOM   1097 C C   . PHE A 1 139 ? 9.85300   47.34700 -15.33700 1.000 24.64939 ? 139 PHE B C   1 
ATOM   1098 O O   . PHE A 1 139 ? 10.64500  46.68800 -14.65200 1.000 25.65786 ? 139 PHE B O   1 
ATOM   1099 C CB  . PHE A 1 139 ? 7.59900   47.98400 -14.42900 1.000 27.08761 ? 139 PHE B CB  1 
ATOM   1100 C CG  . PHE A 1 139 ? 7.52700   46.74400 -13.56700 1.000 29.60680 ? 139 PHE B CG  1 
ATOM   1101 C CD1 . PHE A 1 139 ? 7.79200   46.81500 -12.21500 1.000 33.85076 ? 139 PHE B CD1 1 
ATOM   1102 C CD2 . PHE A 1 139 ? 7.22600   45.50800 -14.11800 1.000 28.59457 ? 139 PHE B CD2 1 
ATOM   1103 C CE1 . PHE A 1 139 ? 7.74200   45.67600 -11.41600 1.000 37.88200 ? 139 PHE B CE1 1 
ATOM   1104 C CE2 . PHE A 1 139 ? 7.16200   44.36200 -13.32400 1.000 30.14464 ? 139 PHE B CE2 1 
ATOM   1105 C CZ  . PHE A 1 139 ? 7.42200   44.44700 -11.97000 1.000 35.31059 ? 139 PHE B CZ  1 
ATOM   1106 N N   . MET A 1 140 ? 9.69200   47.10500 -16.65400 1.000 21.24212 ? 140 MET B N   1 
ATOM   1107 C CA  . MET A 1 140 ? 10.51600  46.04100 -17.23200 1.000 26.04661 ? 140 MET B CA  1 
ATOM   1108 C C   . MET A 1 140 ? 11.99700  46.37900 -17.26300 1.000 27.52418 ? 140 MET B C   1 
ATOM   1109 O O   . MET A 1 140 ? 12.82100  45.47000 -17.13800 1.000 26.97733 ? 140 MET B O   1 
ATOM   1110 C CB  . MET A 1 140 ? 10.12000  45.57700 -18.64800 1.000 26.83634 ? 140 MET B CB  1 
ATOM   1111 C CG  . MET A 1 140 ? 8.70600   45.11500 -18.94900 1.000 25.01719 ? 140 MET B CG  1 
ATOM   1112 S SD  . MET A 1 140 ? 8.01000   45.66800 -20.52500 1.000 30.17957 ? 140 MET B SD  1 
ATOM   1113 C CE  . MET A 1 140 ? 6.29700   45.37300 -20.11800 1.000 29.63783 ? 140 MET B CE  1 
ATOM   1114 N N   . GLU A 1 141 ? 12.36500  47.65600 -17.43600 1.000 27.93756 ? 141 GLU B N   1 
ATOM   1115 C CA  . GLU A 1 141 ? 13.78900  48.00100 -17.47100 1.000 29.10975 ? 141 GLU B CA  1 
ATOM   1116 C C   . GLU A 1 141 ? 14.48300  47.82400 -16.12600 1.000 30.32999 ? 141 GLU B C   1 
ATOM   1117 O O   . GLU A 1 141 ? 15.71200  47.70600 -16.08700 1.000 30.96675 ? 141 GLU B O   1 
ATOM   1118 C CB  . GLU A 1 141 ? 13.99000  49.42500 -17.98600 1.000 29.99548 ? 141 GLU B CB  1 
ATOM   1119 C CG  . GLU A 1 141 ? 13.27600  49.68900 -19.30400 1.000 30.09224 ? 141 GLU B CG  1 
ATOM   1120 C CD  . GLU A 1 141 ? 13.85600  50.84300 -20.09400 1.000 39.09900 ? 141 GLU B CD  1 
ATOM   1121 O OE1 . GLU A 1 141 ? 13.80800  51.99000 -19.59700 1.000 35.81186 ? 141 GLU B OE1 1 
ATOM   1122 O OE2 . GLU A 1 141 ? 14.29800  50.61100 -21.23900 1.000 44.33677 ? 141 GLU B OE2 1 
ATOM   1123 N N   . THR A 1 142 ? 13.74800  47.80600 -15.02100 1.000 32.58683 ? 142 THR B N   1 
ATOM   1124 C CA  . THR A 1 142 ? 14.38000  47.38700 -13.77700 1.000 31.31753 ? 142 THR B CA  1 
ATOM   1125 C C   . THR A 1 142 ? 14.80900  45.92300 -13.82000 1.000 32.96307 ? 142 THR B C   1 
ATOM   1126 O O   . THR A 1 142 ? 15.73600  45.54100 -13.10000 1.000 32.98467 ? 142 THR B O   1 
ATOM   1127 C CB  . THR A 1 142 ? 13.44400  47.62700 -12.59300 1.000 32.24621 ? 142 THR B CB  1 
ATOM   1128 O OG1 . THR A 1 142 ? 12.34700  46.70100 -12.65400 1.000 35.36877 ? 142 THR B OG1 1 
ATOM   1129 C CG2 . THR A 1 142 ? 12.91500  49.04900 -12.61800 1.000 30.48957 ? 142 THR B CG2 1 
ATOM   1130 N N   . ASN A 1 143 ? 14.18200  45.10100 -14.66100 1.000 31.64461 ? 143 ASN B N   1 
ATOM   1131 C CA  . ASN A 1 143 ? 14.45800  43.66500 -14.68100 1.000 29.86079 ? 143 ASN B CA  1 
ATOM   1132 C C   . ASN A 1 143 ? 15.49700  43.32900 -15.75500 1.000 31.88140 ? 143 ASN B C   1 
ATOM   1133 O O   . ASN A 1 143 ? 15.27200  42.52900 -16.67000 1.000 30.67891 ? 143 ASN B O   1 
ATOM   1134 C CB  . ASN A 1 143 ? 13.16600  42.88800 -14.89700 1.000 26.64438 ? 143 ASN B CB  1 
ATOM   1135 C CG  . ASN A 1 143 ? 12.26100  42.90800 -13.68700 1.000 30.63885 ? 143 ASN B CG  1 
ATOM   1136 O OD1 . ASN A 1 143 ? 12.72100  42.85300 -12.54100 1.000 29.31698 ? 143 ASN B OD1 1 
ATOM   1137 N ND2 . ASN A 1 143 ? 10.95600  43.01200 -13.93300 1.000 30.02278 ? 143 ASN B ND2 1 
ATOM   1138 N N   . VAL A 1 144 ? 16.65700  43.97300 -15.63600 1.000 30.34558 ? 144 VAL B N   1 
ATOM   1139 C CA  . VAL A 1 144 ? 17.78200  43.73600 -16.53000 1.000 29.05898 ? 144 VAL B CA  1 
ATOM   1140 C C   . VAL A 1 144 ? 19.02600  43.60600 -15.66300 1.000 34.50943 ? 144 VAL B C   1 
ATOM   1141 O O   . VAL A 1 144 ? 19.33000  44.51000 -14.87700 1.000 32.11452 ? 144 VAL B O   1 
ATOM   1142 C CB  . VAL A 1 144 ? 17.96000  44.86500 -17.55800 1.000 34.14012 ? 144 VAL B CB  1 
ATOM   1143 C CG1 . VAL A 1 144 ? 19.27600  44.68300 -18.32400 1.000 35.34087 ? 144 VAL B CG1 1 
ATOM   1144 C CG2 . VAL A 1 144 ? 16.77000  44.92400 -18.51600 1.000 30.64669 ? 144 VAL B CG2 1 
ATOM   1145 N N   . ASP A 1 145 ? 19.73200  42.48800 -15.79100 1.000 32.80721 ? 145 ASP B N   1 
ATOM   1146 C CA  . ASP A 1 145 ? 20.97200  42.30000 -15.04300 1.000 39.83996 ? 145 ASP B CA  1 
ATOM   1147 C C   . ASP A 1 145 ? 22.17400  42.66600 -15.90900 1.000 41.68111 ? 145 ASP B C   1 
ATOM   1148 O O   . ASP A 1 145 ? 22.88400  43.63200 -15.60700 1.000 49.07951 ? 145 ASP B O   1 
ATOM   1149 C CB  . ASP A 1 145 ? 21.09000  40.86600 -14.53000 1.000 30.96011 ? 145 ASP B CB  1 
ATOM   1150 C CG  . ASP A 1 145 ? 22.24200  40.68900 -13.54500 1.000 40.61298 ? 145 ASP B CG  1 
ATOM   1151 O OD1 . ASP A 1 145 ? 23.36300  41.16800 -13.82200 1.000 47.15698 ? 145 ASP B OD1 1 
ATOM   1152 O OD2 . ASP A 1 145 ? 22.01600  40.09300 -12.47500 1.000 42.72692 ? 145 ASP B OD2 1 
HETATM 1153 O O   . N80 B 2 1   ? -8.72400  22.25800 -16.11200 1.000 19.27753 ? 1   N80 C O   1 
HETATM 1154 C C   . N80 B 2 1   ? -8.15000  22.51800 -17.17500 1.000 23.33882 ? 1   N80 C C   1 
HETATM 1155 C CA  . N80 B 2 1   ? -8.96700  22.81500 -18.40800 1.000 27.25348 ? 1   N80 C CA  1 
HETATM 1156 C CB  . N80 B 2 1   ? -9.06800  24.32900 -18.61500 1.000 27.52792 ? 1   N80 C CB  1 
HETATM 1157 C CG  . N80 B 2 1   ? -10.32800 24.69500 -17.90100 1.000 26.96381 ? 1   N80 C CG  1 
HETATM 1158 C CD  . N80 B 2 1   ? -11.27100 23.56100 -18.22800 1.000 26.25593 ? 1   N80 C CD  1 
HETATM 1159 N N   . N80 B 2 1   ? -10.36600 22.40000 -18.27100 1.000 29.18539 ? 1   N80 C N   1 
HETATM 1160 C CAD . N80 B 2 1   ? -10.66300 21.06600 -18.69500 1.000 28.52351 ? 1   N80 C CAD 1 
HETATM 1161 C CAA . N80 B 2 1   ? -11.57100 20.69300 -19.56800 1.000 23.71561 ? 1   N80 C CAA 1 
ATOM   1162 N N   . VAL B 2 2   ? -6.82900  22.53100 -17.31400 1.000 18.27293 ? 2   VAL C N   1 
ATOM   1163 C CA  . VAL B 2 2   ? -5.93900  22.58900 -16.16000 1.000 17.21517 ? 2   VAL C CA  1 
ATOM   1164 C C   . VAL B 2 2   ? -5.20200  23.91300 -16.22900 1.000 20.27997 ? 2   VAL C C   1 
ATOM   1165 O O   . VAL B 2 2   ? -4.50200  24.19100 -17.20900 1.000 18.09705 ? 2   VAL C O   1 
ATOM   1166 C CB  . VAL B 2 2   ? -4.95900  21.41300 -16.11400 1.000 17.90068 ? 2   VAL C CB  1 
ATOM   1167 C CG1 . VAL B 2 2   ? -3.93100  21.62500 -14.97900 1.000 17.93113 ? 2   VAL C CG1 1 
ATOM   1168 C CG2 . VAL B 2 2   ? -5.70900  20.10500 -15.91800 1.000 18.12918 ? 2   VAL C CG2 1 
ATOM   1169 N N   . TYR B 2 3   ? -5.35600  24.72800 -15.19300 1.000 17.61270 ? 3   TYR C N   1 
ATOM   1170 C CA  . TYR B 2 3   ? -4.61700  25.97600 -15.06700 1.000 18.70795 ? 3   TYR C CA  1 
ATOM   1171 C C   . TYR B 2 3   ? -3.55700  25.76400 -14.00300 1.000 16.99202 ? 3   TYR C C   1 
ATOM   1172 O O   . TYR B 2 3   ? -3.89000  25.66500 -12.82100 1.000 17.53524 ? 3   TYR C O   1 
ATOM   1173 C CB  . TYR B 2 3   ? -5.54900  27.12700 -14.69200 1.000 19.77842 ? 3   TYR C CB  1 
ATOM   1174 C CG  . TYR B 2 3   ? -6.40800  27.63000 -15.82500 1.000 18.96378 ? 3   TYR C CG  1 
ATOM   1175 C CD1 . TYR B 2 3   ? -5.90900  28.56000 -16.74000 1.000 17.75494 ? 3   TYR C CD1 1 
ATOM   1176 C CD2 . TYR B 2 3   ? -7.72100  27.20800 -15.96600 1.000 18.90668 ? 3   TYR C CD2 1 
ATOM   1177 C CE1 . TYR B 2 3   ? -6.69300  29.03900 -17.76400 1.000 19.71967 ? 3   TYR C CE1 1 
ATOM   1178 C CE2 . TYR B 2 3   ? -8.51400  27.68000 -16.99200 1.000 19.47988 ? 3   TYR C CE2 1 
ATOM   1179 C CZ  . TYR B 2 3   ? -7.99100  28.59200 -17.88700 1.000 19.34062 ? 3   TYR C CZ  1 
ATOM   1180 O OH  . TYR B 2 3   ? -8.77700  29.06800 -18.90800 1.000 19.81728 ? 3   TYR C OH  1 
ATOM   1181 N N   . MET B 2 4   ? -2.29300  25.63400 -14.43700 1.000 18.89642 ? 4   MET C N   1 
ATOM   1182 C CA  . MET B 2 4   ? -1.13900  25.65800 -13.54000 1.000 17.24348 ? 4   MET C CA  1 
ATOM   1183 C C   . MET B 2 4   ? -0.84000  27.10200 -13.14200 1.000 18.38325 ? 4   MET C C   1 
ATOM   1184 O O   . MET B 2 4   ? -0.56100  27.93900 -14.00100 1.000 18.41903 ? 4   MET C O   1 
ATOM   1185 C CB  . MET B 2 4   ? 0.06900   25.02900 -14.25400 1.000 19.47909 ? 4   MET C CB  1 
ATOM   1186 C CG  . MET B 2 4   ? -0.05200  23.55200 -14.72200 1.000 16.52301 ? 4   MET C CG  1 
ATOM   1187 S SD  . MET B 2 4   ? -0.84100  22.33200 -13.61900 1.000 19.91687 ? 4   MET C SD  1 
ATOM   1188 C CE  . MET B 2 4   ? 0.54800   22.06400 -12.52200 1.000 19.60762 ? 4   MET C CE  1 
ATOM   1189 N N   . VAL B 2 5   ? -0.86700  27.40200 -11.84500 1.000 18.59175 ? 5   VAL C N   1 
ATOM   1190 C CA  . VAL B 2 5   ? -0.64800  28.76000 -11.35900 1.000 17.08669 ? 5   VAL C CA  1 
ATOM   1191 C C   . VAL B 2 5   ? 0.59800   28.77400 -10.47500 1.000 16.91550 ? 5   VAL C C   1 
ATOM   1192 O O   . VAL B 2 5   ? 0.59000   28.23600 -9.35800  1.000 16.78914 ? 5   VAL C O   1 
ATOM   1193 C CB  . VAL B 2 5   ? -1.86200  29.29900 -10.59200 1.000 16.58255 ? 5   VAL C CB  1 
ATOM   1194 C CG1 . VAL B 2 5   ? -1.62200  30.76100 -10.21300 1.000 17.04040 ? 5   VAL C CG1 1 
ATOM   1195 C CG2 . VAL B 2 5   ? -3.10500  29.14500 -11.44500 1.000 15.82573 ? 5   VAL C CG2 1 
ATOM   1196 N N   . TYR B 2 6   ? 1.65400   29.40800 -10.96200 1.000 17.11740 ? 6   TYR C N   1 
ATOM   1197 C CA  . TYR B 2 6   ? 2.93800   29.44900 -10.27300 1.000 17.73269 ? 6   TYR C CA  1 
ATOM   1198 C C   . TYR B 2 6   ? 3.02400   30.73300 -9.47500  1.000 16.11222 ? 6   TYR C C   1 
ATOM   1199 O O   . TYR B 2 6   ? 3.00200   31.83400 -10.03800 1.000 16.68324 ? 6   TYR C O   1 
ATOM   1200 C CB  . TYR B 2 6   ? 4.09000   29.34300 -11.27900 1.000 17.61217 ? 6   TYR C CB  1 
ATOM   1201 C CG  . TYR B 2 6   ? 3.97100   28.08200 -12.07800 1.000 19.08266 ? 6   TYR C CG  1 
ATOM   1202 C CD1 . TYR B 2 6   ? 4.53000   26.89600 -11.62500 1.000 16.46600 ? 6   TYR C CD1 1 
ATOM   1203 C CD2 . TYR B 2 6   ? 3.24900   28.06100 -13.27300 1.000 17.30245 ? 6   TYR C CD2 1 
ATOM   1204 C CE1 . TYR B 2 6   ? 4.40100   25.71900 -12.35000 1.000 16.60908 ? 6   TYR C CE1 1 
ATOM   1205 C CE2 . TYR B 2 6   ? 3.10000   26.87900 -14.00200 1.000 17.19469 ? 6   TYR C CE2 1 
ATOM   1206 C CZ  . TYR B 2 6   ? 3.67900   25.71600 -13.53000 1.000 19.14732 ? 6   TYR C CZ  1 
ATOM   1207 O OH  . TYR B 2 6   ? 3.55300   24.54400 -14.23400 1.000 17.05760 ? 6   TYR C OH  1 
ATOM   1208 N N   . VAL B 2 7   ? 3.15000   30.58500 -8.16000  1.000 18.63303 ? 7   VAL C N   1 
ATOM   1209 C CA  . VAL B 2 7   ? 3.14200   31.70000 -7.23400  1.000 17.21529 ? 7   VAL C CA  1 
ATOM   1210 C C   . VAL B 2 7   ? 4.22800   31.43600 -6.20200  1.000 21.10012 ? 7   VAL C C   1 
ATOM   1211 O O   . VAL B 2 7   ? 4.71900   30.31200 -6.05500  1.000 19.34156 ? 7   VAL C O   1 
ATOM   1212 C CB  . VAL B 2 7   ? 1.76500   31.86300 -6.53900  1.000 15.91517 ? 7   VAL C CB  1 
ATOM   1213 C CG1 . VAL B 2 7   ? 0.68100   32.25000 -7.56500  1.000 21.80143 ? 7   VAL C CG1 1 
ATOM   1214 C CG2 . VAL B 2 7   ? 1.38300   30.59000 -5.82100  1.000 18.45276 ? 7   VAL C CG2 1 
ATOM   1215 N N   . SER B 2 8   ? 4.60400   32.49200 -5.49200  1.000 20.05357 ? 8   SER C N   1 
ATOM   1216 C CA  . SER B 2 8   ? 5.53900   32.36300 -4.38700  1.000 19.72201 ? 8   SER C CA  1 
ATOM   1217 C C   . SER B 2 8   ? 4.81800   31.90700 -3.12200  1.000 21.84090 ? 8   SER C C   1 
ATOM   1218 O O   . SER B 2 8   ? 3.68000   32.29600 -2.85500  1.000 23.04935 ? 8   SER C O   1 
ATOM   1219 C CB  . SER B 2 8   ? 6.24000   33.69000 -4.12700  1.000 21.45662 ? 8   SER C CB  1 
ATOM   1220 O OG  . SER B 2 8   ? 7.09300   34.01200 -5.21000  1.000 23.91746 ? 8   SER C OG  1 
ATOM   1221 N N   . GLN B 2 9   ? 5.51800   31.09500 -2.33500  1.000 23.10798 ? 9   GLN C N   1 
ATOM   1222 C CA  . GLN B 2 9   ? 4.97400   30.52500 -1.10600  1.000 27.08569 ? 9   GLN C CA  1 
ATOM   1223 C C   . GLN B 2 9   ? 4.48600   31.64400 -0.19200  1.000 27.65365 ? 9   GLN C C   1 
ATOM   1224 O O   . GLN B 2 9   ? 5.16100   32.66700 -0.02200  1.000 24.68884 ? 9   GLN C O   1 
ATOM   1225 C CB  . GLN B 2 9   ? 6.06700   29.69300 -0.42200  1.000 29.11646 ? 9   GLN C CB  1 
ATOM   1226 C CG  . GLN B 2 9   ? 5.92700   28.19000 -0.69900  1.000 35.04982 ? 9   GLN C CG  1 
ATOM   1227 C CD  . GLN B 2 9   ? 7.21500   27.39800 -0.43900  1.000 39.79102 ? 9   GLN C CD  1 
ATOM   1228 O OE1 . GLN B 2 9   ? 7.39900   26.31100 -1.00200  1.000 40.71684 ? 9   GLN C OE1 1 
ATOM   1229 N NE2 . GLN B 2 9   ? 8.08600   27.91100 0.44200   1.000 37.15955 ? 9   GLN C NE2 1 
ATOM   1230 N N   . ASP B 2 10  ? 3.28900   31.46000 0.36400   1.000 28.76712 ? 10  ASP C N   1 
ATOM   1231 C CA  . ASP B 2 10  ? 2.66300   32.39700 1.29100   1.000 30.55533 ? 10  ASP C CA  1 
ATOM   1232 C C   . ASP B 2 10  ? 2.36000   33.77600 0.69600   1.000 29.68196 ? 10  ASP C C   1 
ATOM   1233 O O   . ASP B 2 10  ? 1.91000   34.66700 1.42500   1.000 25.96212 ? 10  ASP C O   1 
ATOM   1234 C CB  . ASP B 2 10  ? 3.52200   32.56500 2.55200   1.000 37.24716 ? 10  ASP C CB  1 
ATOM   1235 C CG  . ASP B 2 10  ? 3.95700   31.23700 3.15400   1.000 39.74122 ? 10  ASP C CG  1 
ATOM   1236 O OD1 . ASP B 2 10  ? 3.07500   30.41000 3.46500   1.000 42.03659 ? 10  ASP C OD1 1 
ATOM   1237 O OD2 . ASP B 2 10  ? 5.18000   31.03800 3.35200   1.000 50.67216 ? 10  ASP C OD2 1 
ATOM   1238 N N   . ARG B 2 11  ? 2.59100   33.98800 -0.60900  1.000 21.85773 ? 11  ARG C N   1 
ATOM   1239 C CA  . ARG B 2 11  ? 2.11900   35.22300 -1.22100  1.000 20.51266 ? 11  ARG C CA  1 
ATOM   1240 C C   . ARG B 2 11  ? 0.59800   35.31800 -1.13900  1.000 26.92436 ? 11  ARG C C   1 
ATOM   1241 O O   . ARG B 2 11  ? 0.03900   36.40500 -0.95200  1.000 25.78047 ? 11  ARG C O   1 
ATOM   1242 C CB  . ARG B 2 11  ? 2.58300   35.31500 -2.67800  1.000 25.30334 ? 11  ARG C CB  1 
ATOM   1243 C CG  . ARG B 2 11  ? 1.97800   36.49100 -3.44300  1.000 27.62252 ? 11  ARG C CG  1 
ATOM   1244 C CD  . ARG B 2 11  ? 2.51300   37.82900 -2.91200  1.000 31.62221 ? 11  ARG C CD  1 
ATOM   1245 N NE  . ARG B 2 11  ? 1.77400   38.97100 -3.44300  1.000 36.37350 ? 11  ARG C NE  1 
ATOM   1246 C CZ  . ARG B 2 11  ? 0.83200   39.62900 -2.77900  1.000 41.57380 ? 11  ARG C CZ  1 
ATOM   1247 N NH1 . ARG B 2 11  ? 0.51500   39.31400 -1.53200  1.000 38.79563 ? 11  ARG C NH1 1 
ATOM   1248 N NH2 . ARG B 2 11  ? 0.17200   40.61200 -3.38800  1.000 41.48662 ? 11  ARG C NH2 1 
ATOM   1249 N N   . LEU B 2 12  ? -0.08300  34.18400 -1.27700  1.000 23.69532 ? 12  LEU C N   1 
ATOM   1250 C CA  . LEU B 2 12  ? -1.53600  34.10100 -1.26000  1.000 21.54865 ? 12  LEU C CA  1 
ATOM   1251 C C   . LEU B 2 12  ? -1.96800  33.32700 -0.02800  1.000 21.35260 ? 12  LEU C C   1 
ATOM   1252 O O   . LEU B 2 12  ? -1.59200  32.15900 0.12900   1.000 19.80440 ? 12  LEU C O   1 
ATOM   1253 C CB  . LEU B 2 12  ? -2.06300  33.39600 -2.50700  1.000 20.70203 ? 12  LEU C CB  1 
ATOM   1254 C CG  . LEU B 2 12  ? -1.74900  34.03200 -3.85800  1.000 22.71482 ? 12  LEU C CG  1 
ATOM   1255 C CD1 . LEU B 2 12  ? -2.35900  33.17300 -4.93700  1.000 23.32044 ? 12  LEU C CD1 1 
ATOM   1256 C CD2 . LEU B 2 12  ? -2.29600  35.44900 -3.91600  1.000 23.37196 ? 12  LEU C CD2 1 
ATOM   1257 N N   . THR B 2 13  ? -2.77000  33.97400 0.83000   1.000 23.26948 ? 13  THR C N   1 
ATOM   1258 C CA  . THR B 2 13  ? -3.45000  33.32400 1.94700   1.000 23.38868 ? 13  THR C CA  1 
ATOM   1259 C C   . THR B 2 13  ? -4.36400  32.21500 1.43500   1.000 20.27372 ? 13  THR C C   1 
ATOM   1260 O O   . THR B 2 13  ? -4.66500  32.17600 0.24400   1.000 18.51198 ? 13  THR C O   1 
ATOM   1261 C CB  . THR B 2 13  ? -4.29100  34.33800 2.72800   1.000 22.82073 ? 13  THR C CB  1 
ATOM   1262 O OG1 . THR B 2 13  ? -5.25000  34.93900 1.84800   1.000 22.07473 ? 13  THR C OG1 1 
ATOM   1263 C CG2 . THR B 2 13  ? -3.41700  35.42700 3.35100   1.000 25.74427 ? 13  THR C CG2 1 
ATOM   1264 N N   . PRO B 2 14  ? -4.85300  31.32000 2.29300   1.000 22.09455 ? 14  PRO C N   1 
ATOM   1265 C CA  . PRO B 2 14  ? -5.93900  30.42700 1.86200   1.000 22.18171 ? 14  PRO C CA  1 
ATOM   1266 C C   . PRO B 2 14  ? -7.11800  31.16000 1.22800   1.000 21.46935 ? 14  PRO C C   1 
ATOM   1267 O O   . PRO B 2 14  ? -7.64400  30.70600 0.20100   1.000 20.64728 ? 14  PRO C O   1 
ATOM   1268 C CB  . PRO B 2 14  ? -6.33000  29.72400 3.16800   1.000 28.09372 ? 14  PRO C CB  1 
ATOM   1269 C CG  . PRO B 2 14  ? -5.05200  29.67300 3.94000   1.000 28.76533 ? 14  PRO C CG  1 
ATOM   1270 C CD  . PRO B 2 14  ? -4.33200  30.95700 3.62500   1.000 26.20391 ? 14  PRO C CD  1 
ATOM   1271 N N   . SER B 2 15  ? -7.52800  32.30300 1.78100   1.000 22.60841 ? 15  SER C N   1 
ATOM   1272 C CA  . SER B 2 15  ? -8.66100  33.03200 1.21000   1.000 21.74073 ? 15  SER C CA  1 
ATOM   1273 C C   . SER B 2 15  ? -8.31700  33.63200 -0.14700  1.000 21.13472 ? 15  SER C C   1 
ATOM   1274 O O   . SER B 2 15  ? -9.14400  33.60800 -1.06900  1.000 19.80891 ? 15  SER C O   1 
ATOM   1275 C CB  . SER B 2 15  ? -9.12900  34.12900 2.16300   1.000 23.81126 ? 15  SER C CB  1 
ATOM   1276 O OG  . SER B 2 15  ? -9.58100  33.56200 3.37300   1.000 30.79124 ? 15  SER C OG  1 
ATOM   1277 N N   . ALA B 2 16  ? -7.11500  34.19700 -0.28000  1.000 23.46614 ? 16  ALA C N   1 
ATOM   1278 C CA  . ALA B 2 16  ? -6.68200  34.72400 -1.57400  1.000 21.93856 ? 16  ALA C CA  1 
ATOM   1279 C C   . ALA B 2 16  ? -6.60300  33.61800 -2.62500  1.000 19.56034 ? 16  ALA C C   1 
ATOM   1280 O O   . ALA B 2 16  ? -7.00900  33.81600 -3.78300  1.000 20.89772 ? 16  ALA C O   1 
ATOM   1281 C CB  . ALA B 2 16  ? -5.33100  35.42600 -1.41600  1.000 19.43031 ? 16  ALA C CB  1 
ATOM   1282 N N   . LYS B 2 17  ? -6.09800  32.44200 -2.23700  1.000 18.99974 ? 17  LYS C N   1 
ATOM   1283 C CA  . LYS B 2 17  ? -6.02700  31.31400 -3.16400  1.000 20.75087 ? 17  LYS C CA  1 
ATOM   1284 C C   . LYS B 2 17  ? -7.41000  30.92600 -3.64900  1.000 20.71331 ? 17  LYS C C   1 
ATOM   1285 O O   . LYS B 2 17  ? -7.61600  30.70800 -4.84400  1.000 16.99440 ? 17  LYS C O   1 
ATOM   1286 C CB  . LYS B 2 17  ? -5.34200  30.11200 -2.50200  1.000 19.85980 ? 17  LYS C CB  1 
ATOM   1287 C CG  . LYS B 2 17  ? -3.82400  30.22900 -2.46200  1.000 21.26560 ? 17  LYS C CG  1 
ATOM   1288 C CD  . LYS B 2 17  ? -3.12000  28.88400 -2.41600  1.000 25.86265 ? 17  LYS C CD  1 
ATOM   1289 C CE  . LYS B 2 17  ? -2.02000  28.88700 -1.37300  1.000 31.14277 ? 17  LYS C CE  1 
ATOM   1290 N NZ  . LYS B 2 17  ? -1.57200  27.52000 -0.99400  1.000 36.50703 ? 17  LYS C NZ  1 
ATOM   1291 N N   . HIS B 2 18  ? -8.37500  30.82700 -2.72700  1.000 17.30865 ? 18  HIS C N   1 
ATOM   1292 C CA  . HIS B 2 18  ? -9.74400  30.52400 -3.14200  1.000 20.04099 ? 18  HIS C CA  1 
ATOM   1293 C C   . HIS B 2 18  ? -10.26100 31.58200 -4.10300  1.000 19.87125 ? 18  HIS C C   1 
ATOM   1294 O O   . HIS B 2 18  ? -10.90700 31.25900 -5.11100  1.000 20.38833 ? 18  HIS C O   1 
ATOM   1295 C CB  . HIS B 2 18  ? -10.65700 30.41200 -1.91200  1.000 20.12779 ? 18  HIS C CB  1 
ATOM   1296 C CG  . HIS B 2 18  ? -12.05300 29.96600 -2.23400  1.000 22.76356 ? 18  HIS C CG  1 
ATOM   1297 N ND1 . HIS B 2 18  ? -12.47900 28.66400 -2.07300  1.000 21.06327 ? 18  HIS C ND1 1 
ATOM   1298 C CD2 . HIS B 2 18  ? -13.12000 30.65300 -2.70200  1.000 25.73098 ? 18  HIS C CD2 1 
ATOM   1299 C CE1 . HIS B 2 18  ? -13.74500 28.56700 -2.43900  1.000 22.64178 ? 18  HIS C CE1 1 
ATOM   1300 N NE2 . HIS B 2 18  ? -14.16000 29.76100 -2.81800  1.000 25.76599 ? 18  HIS C NE2 1 
ATOM   1301 N N   . ALA B 2 19  ? -9.96200  32.85700 -3.82500  1.000 20.20073 ? 19  ALA C N   1 
ATOM   1302 C CA  . ALA B 2 19  ? -10.43400 33.92400 -4.70300  1.000 20.22497 ? 19  ALA C CA  1 
ATOM   1303 C C   . ALA B 2 19  ? -9.80500  33.82700 -6.08600  1.000 17.45594 ? 19  ALA C C   1 
ATOM   1304 O O   . ALA B 2 19  ? -10.49400 33.98500 -7.09500  1.000 19.39663 ? 19  ALA C O   1 
ATOM   1305 C CB  . ALA B 2 19  ? -10.14700 35.29600 -4.09200  1.000 20.40655 ? 19  ALA C CB  1 
ATOM   1306 N N   . VAL B 2 20  ? -8.50200  33.57400 -6.15300  1.000 17.15424 ? 20  VAL C N   1 
ATOM   1307 C CA  . VAL B 2 20  ? -7.84000  33.48200 -7.45200  1.000 16.60534 ? 20  VAL C CA  1 
ATOM   1308 C C   . VAL B 2 20  ? -8.36400  32.28100 -8.23200  1.000 18.42057 ? 20  VAL C C   1 
ATOM   1309 O O   . VAL B 2 20  ? -8.64300  32.38000 -9.43400  1.000 21.16427 ? 20  VAL C O   1 
ATOM   1310 C CB  . VAL B 2 20  ? -6.31600  33.43500 -7.25800  1.000 22.03976 ? 20  VAL C CB  1 
ATOM   1311 C CG1 . VAL B 2 20  ? -5.60100  33.06400 -8.55600  1.000 17.47024 ? 20  VAL C CG1 1 
ATOM   1312 C CG2 . VAL B 2 20  ? -5.83400  34.79200 -6.75700  1.000 20.36110 ? 20  VAL C CG2 1 
ATOM   1313 N N   . ALA B 2 21  ? -8.51100  31.13100 -7.56900  1.000 17.17981 ? 21  ALA C N   1 
ATOM   1314 C CA  . ALA B 2 21  ? -9.07200  29.97500 -8.25100  1.000 20.92480 ? 21  ALA C CA  1 
ATOM   1315 C C   . ALA B 2 21  ? -10.48500 30.26800 -8.74000  1.000 20.51333 ? 21  ALA C C   1 
ATOM   1316 O O   . ALA B 2 21  ? -10.86600 29.84400 -9.83700  1.000 17.98057 ? 21  ALA C O   1 
ATOM   1317 C CB  . ALA B 2 21  ? -9.05600  28.75300 -7.33100  1.000 18.98768 ? 21  ALA C CB  1 
ATOM   1318 N N   . LYS B 2 22  ? -11.26200 31.04100 -7.97000  1.000 19.72104 ? 22  LYS C N   1 
ATOM   1319 C CA  . LYS B 2 22  ? -12.62800 31.30500 -8.40800  1.000 20.89538 ? 22  LYS C CA  1 
ATOM   1320 C C   . LYS B 2 22  ? -12.63700 32.28700 -9.56900  1.000 20.21819 ? 22  LYS C C   1 
ATOM   1321 O O   . LYS B 2 22  ? -13.46000 32.15900 -10.48400 1.000 21.95336 ? 22  LYS C O   1 
ATOM   1322 C CB  . LYS B 2 22  ? -13.48400 31.83500 -7.24000  1.000 24.71642 ? 22  LYS C CB  1 
ATOM   1323 C CG  . LYS B 2 22  ? -14.63000 32.82700 -7.61000  1.000 26.11068 ? 22  LYS C CG  1 
ATOM   1324 C CD  . LYS B 2 22  ? -15.40200 33.24500 -6.31500  1.000 27.60653 ? 22  LYS C CD  1 
ATOM   1325 C CE  . LYS B 2 22  ? -16.61600 34.16300 -6.56600  1.000 34.52751 ? 22  LYS C CE  1 
ATOM   1326 N NZ  . LYS B 2 22  ? -17.23300 34.04600 -7.92400  1.000 34.02733 ? 22  LYS C NZ  1 
ATOM   1327 N N   . ALA B 2 23  ? -11.71200 33.25400 -9.57300  1.000 19.30722 ? 23  ALA C N   1 
ATOM   1328 C CA  . ALA B 2 23  ? -11.62500 34.19200 -10.69600 1.000 21.27489 ? 23  ALA C CA  1 
ATOM   1329 C C   . ALA B 2 23  ? -11.30900 33.47000 -12.00700 1.000 21.77020 ? 23  ALA C C   1 
ATOM   1330 O O   . ALA B 2 23  ? -11.91200 33.75400 -13.05200 1.000 18.97342 ? 23  ALA C O   1 
ATOM   1331 C CB  . ALA B 2 23  ? -10.56500 35.25700 -10.40700 1.000 21.81465 ? 23  ALA C CB  1 
ATOM   1332 N N   . ILE B 2 24  ? -10.34800 32.55000 -11.97400 1.000 21.72533 ? 24  ILE C N   1 
ATOM   1333 C CA  . ILE B 2 24  ? -9.98100  31.79000 -13.17400 1.000 20.13085 ? 24  ILE C CA  1 
ATOM   1334 C C   . ILE B 2 24  ? -11.12000 30.87000 -13.59300 1.000 20.36590 ? 24  ILE C C   1 
ATOM   1335 O O   . ILE B 2 24  ? -11.49100 30.80300 -14.77500 1.000 19.87097 ? 24  ILE C O   1 
ATOM   1336 C CB  . ILE B 2 24  ? -8.69500  30.98400 -12.91300 1.000 17.37500 ? 24  ILE C CB  1 
ATOM   1337 C CG1 . ILE B 2 24  ? -7.50900  31.91300 -12.63000 1.000 18.25090 ? 24  ILE C CG1 1 
ATOM   1338 C CG2 . ILE B 2 24  ? -8.41000  30.05100 -14.09200 1.000 20.52545 ? 24  ILE C CG2 1 
ATOM   1339 C CD1 . ILE B 2 24  ? -6.17000  31.16200 -12.46700 1.000 23.18975 ? 24  ILE C CD1 1 
ATOM   1340 N N   . THR B 2 25  ? -11.66300 30.11600 -12.62900 1.000 18.17766 ? 25  THR C N   1 
ATOM   1341 C CA  . THR B 2 25  ? -12.74600 29.18200 -12.92200 1.000 20.43865 ? 25  THR C CA  1 
ATOM   1342 C C   . THR B 2 25  ? -13.94600 29.90300 -13.52200 1.000 22.55820 ? 25  THR C C   1 
ATOM   1343 O O   . THR B 2 25  ? -14.51900 29.45300 -14.52700 1.000 23.77609 ? 25  THR C O   1 
ATOM   1344 C CB  . THR B 2 25  ? -13.14600 28.42000 -11.65300 1.000 18.33560 ? 25  THR C CB  1 
ATOM   1345 O OG1 . THR B 2 25  ? -11.99800 27.74700 -11.12900 1.000 20.89297 ? 25  THR C OG1 1 
ATOM   1346 C CG2 . THR B 2 25  ? -14.20500 27.38100 -11.96000 1.000 21.97079 ? 25  THR C CG2 1 
ATOM   1347 N N   . ASP B 2 26  ? -14.33700 31.03300 -12.92400 1.000 22.99536 ? 26  ASP C N   1 
ATOM   1348 C CA  . ASP B 2 26  ? -15.47000 31.79500 -13.44300 1.000 26.28759 ? 26  ASP C CA  1 
ATOM   1349 C C   . ASP B 2 26  ? -15.17000 32.36800 -14.82200 1.000 23.14504 ? 26  ASP C C   1 
ATOM   1350 O O   . ASP B 2 26  ? -16.05900 32.44300 -15.68000 1.000 24.88665 ? 26  ASP C O   1 
ATOM   1351 C CB  . ASP B 2 26  ? -15.84900 32.93400 -12.49300 1.000 23.65838 ? 26  ASP C CB  1 
ATOM   1352 C CG  . ASP B 2 26  ? -16.51300 32.45600 -11.21900 1.000 29.40878 ? 26  ASP C CG  1 
ATOM   1353 O OD1 . ASP B 2 26  ? -16.78700 31.24500 -11.07100 1.000 28.40104 ? 26  ASP C OD1 1 
ATOM   1354 O OD2 . ASP B 2 26  ? -16.75100 33.31300 -10.34900 1.000 27.19607 ? 26  ASP C OD2 1 
ATOM   1355 N N   . ALA B 2 27  ? -13.93700 32.81500 -15.04700 1.000 23.44934 ? 27  ALA C N   1 
ATOM   1356 C CA  . ALA B 2 27  ? -13.60700 33.35600 -16.36100 1.000 22.73704 ? 27  ALA C CA  1 
ATOM   1357 C C   . ALA B 2 27  ? -13.70200 32.27300 -17.41600 1.000 19.87504 ? 27  ALA C C   1 
ATOM   1358 O O   . ALA B 2 27  ? -14.23500 32.50000 -18.51100 1.000 23.02440 ? 27  ALA C O   1 
ATOM   1359 C CB  . ALA B 2 27  ? -12.20300 33.96600 -16.35700 1.000 22.16787 ? 27  ALA C CB  1 
ATOM   1360 N N   . HIS B 2 28  ? -13.19800 31.08200 -17.10000 1.000 20.37796 ? 28  HIS C N   1 
ATOM   1361 C CA  . HIS B 2 28  ? -13.28200 29.99000 -18.05700 1.000 22.24494 ? 28  HIS C CA  1 
ATOM   1362 C C   . HIS B 2 28  ? -14.73300 29.63000 -18.34200 1.000 25.29892 ? 28  HIS C C   1 
ATOM   1363 O O   . HIS B 2 28  ? -15.15200 29.57100 -19.50200 1.000 22.20167 ? 28  HIS C O   1 
ATOM   1364 C CB  . HIS B 2 28  ? -12.51700 28.76400 -17.56300 1.000 19.92036 ? 28  HIS C CB  1 
ATOM   1365 C CG  . HIS B 2 28  ? -12.28200 27.76500 -18.65300 1.000 22.70790 ? 28  HIS C CG  1 
ATOM   1366 N ND1 . HIS B 2 28  ? -11.17200 27.80800 -19.46700 1.000 23.51926 ? 28  HIS C ND1 1 
ATOM   1367 C CD2 . HIS B 2 28  ? -13.04800 26.74500 -19.11300 1.000 26.48392 ? 28  HIS C CD2 1 
ATOM   1368 C CE1 . HIS B 2 28  ? -11.25000 26.84200 -20.36600 1.000 25.79839 ? 28  HIS C CE1 1 
ATOM   1369 N NE2 . HIS B 2 28  ? -12.37600 26.18000 -20.17200 1.000 25.54455 ? 28  HIS C NE2 1 
ATOM   1370 N N   . ARG B 2 29  ? -15.51400 29.38300 -17.29300 1.000 22.99930 ? 29  ARG C N   1 
ATOM   1371 C CA  . ARG B 2 29  ? -16.92100 29.06100 -17.48600 1.000 26.40633 ? 29  ARG C CA  1 
ATOM   1372 C C   . ARG B 2 29  ? -17.61900 30.15400 -18.28600 1.000 26.03369 ? 29  ARG C C   1 
ATOM   1373 O O   . ARG B 2 29  ? -18.34200 29.87800 -19.25200 1.000 27.45726 ? 29  ARG C O   1 
ATOM   1374 C CB  . ARG B 2 29  ? -17.59700 28.85600 -16.12000 1.000 28.13286 ? 29  ARG C CB  1 
ATOM   1375 C CG  . ARG B 2 29  ? -19.14500 28.72400 -16.18000 1.000 34.10159 ? 29  ARG C CG  1 
ATOM   1376 C CD  . ARG B 2 29  ? -19.83100 30.08500 -15.98000 1.000 37.77071 ? 29  ARG C CD  1 
ATOM   1377 N NE  . ARG B 2 29  ? -20.02200 30.43300 -14.57400 1.000 42.65509 ? 29  ARG C NE  1 
ATOM   1378 C CZ  . ARG B 2 29  ? -19.53100 31.52100 -13.98800 1.000 42.79815 ? 29  ARG C CZ  1 
ATOM   1379 N NH1 . ARG B 2 29  ? -18.79200 32.39700 -14.65600 1.000 33.66722 ? 29  ARG C NH1 1 
ATOM   1380 N NH2 . ARG B 2 29  ? -19.77400 31.72700 -12.69300 1.000 41.79324 ? 29  ARG C NH2 1 
ATOM   1381 N N   . GLY B 2 30  ? -17.40800 31.40800 -17.89900 1.000 25.35366 ? 30  GLY C N   1 
ATOM   1382 C CA  . GLY B 2 30  ? -18.20800 32.47800 -18.45900 1.000 29.15213 ? 30  GLY C CA  1 
ATOM   1383 C C   . GLY B 2 30  ? -17.98600 32.65400 -19.94200 1.000 29.60864 ? 30  GLY C C   1 
ATOM   1384 O O   . GLY B 2 30  ? -18.92000 32.98300 -20.67700 1.000 26.78900 ? 30  GLY C O   1 
ATOM   1385 N N   . LEU B 2 31  ? -16.76000 32.42600 -20.40700 1.000 23.17111 ? 31  LEU C N   1 
ATOM   1386 C CA  . LEU B 2 31  ? -16.42500 32.69100 -21.79800 1.000 25.06822 ? 31  LEU C CA  1 
ATOM   1387 C C   . LEU B 2 31  ? -16.48900 31.46100 -22.69500 1.000 28.23306 ? 31  LEU C C   1 
ATOM   1388 O O   . LEU B 2 31  ? -16.72100 31.61400 -23.89700 1.000 30.70422 ? 31  LEU C O   1 
ATOM   1389 C CB  . LEU B 2 31  ? -15.03100 33.31900 -21.89800 1.000 21.75814 ? 31  LEU C CB  1 
ATOM   1390 C CG  . LEU B 2 31  ? -14.95000 34.75500 -21.37800 1.000 24.72325 ? 31  LEU C CG  1 
ATOM   1391 C CD1 . LEU B 2 31  ? -13.52000 35.09900 -21.02500 1.000 24.70005 ? 31  LEU C CD1 1 
ATOM   1392 C CD2 . LEU B 2 31  ? -15.53000 35.74900 -22.41100 1.000 29.69557 ? 31  LEU C CD2 1 
ATOM   1393 N N   . THR B 2 32  ? -16.30900 30.25200 -22.15300 1.000 26.32627 ? 32  THR C N   1 
ATOM   1394 C CA  . THR B 2 32  ? -16.35600 29.02800 -22.95100 1.000 25.47905 ? 32  THR C CA  1 
ATOM   1395 C C   . THR B 2 32  ? -17.63100 28.21400 -22.76200 1.000 31.88043 ? 32  THR C C   1 
ATOM   1396 O O   . THR B 2 32  ? -17.94600 27.38900 -23.62300 1.000 31.92290 ? 32  THR C O   1 
ATOM   1397 C CB  . THR B 2 32  ? -15.16800 28.10600 -22.62800 1.000 30.27641 ? 32  THR C CB  1 
ATOM   1398 O OG1 . THR B 2 32  ? -15.34900 27.53500 -21.32500 1.000 26.79258 ? 32  THR C OG1 1 
ATOM   1399 C CG2 . THR B 2 32  ? -13.83300 28.85600 -22.69300 1.000 24.27941 ? 32  THR C CG2 1 
ATOM   1400 N N   . GLY B 2 33  ? -18.35500 28.39700 -21.65900 1.000 30.67650 ? 33  GLY C N   1 
ATOM   1401 C CA  . GLY B 2 33  ? -19.51200 27.57100 -21.37300 1.000 34.40257 ? 33  GLY C CA  1 
ATOM   1402 C C   . GLY B 2 33  ? -19.20200 26.18200 -20.85300 1.000 33.79572 ? 33  GLY C C   1 
ATOM   1403 O O   . GLY B 2 33  ? -20.13900 25.44300 -20.51800 1.000 32.65902 ? 33  GLY C O   1 
ATOM   1404 N N   . THR B 2 34  ? -17.92800 25.79300 -20.79900 1.000 28.68098 ? 34  THR C N   1 
ATOM   1405 C CA  . THR B 2 34  ? -17.52300 24.56200 -20.13000 1.000 32.04484 ? 34  THR C CA  1 
ATOM   1406 C C   . THR B 2 34  ? -17.98600 24.57900 -18.67500 1.000 31.04401 ? 34  THR C C   1 
ATOM   1407 O O   . THR B 2 34  ? -17.96300 25.62300 -18.02000 1.000 34.62526 ? 34  THR C O   1 
ATOM   1408 C CB  . THR B 2 34  ? -15.99600 24.42200 -20.20700 1.000 31.48922 ? 34  THR C CB  1 
ATOM   1409 O OG1 . THR B 2 34  ? -15.57600 24.42900 -21.58200 1.000 37.01589 ? 34  THR C OG1 1 
ATOM   1410 C CG2 . THR B 2 34  ? -15.51600 23.14800 -19.53500 1.000 35.10549 ? 34  THR C CG2 1 
ATOM   1411 N N   . GLN B 2 35  ? -18.40200 23.41800 -18.16300 1.000 28.93662 ? 35  GLN C N   1 
ATOM   1412 C CA  . GLN B 2 35  ? -18.94100 23.35600 -16.80400 1.000 31.77969 ? 35  GLN C CA  1 
ATOM   1413 C C   . GLN B 2 35  ? -17.88500 23.72800 -15.77100 1.000 30.56513 ? 35  GLN C C   1 
ATOM   1414 O O   . GLN B 2 35  ? -16.69100 23.46000 -15.95300 1.000 30.49811 ? 35  GLN C O   1 
ATOM   1415 C CB  . GLN B 2 35  ? -19.48000 21.95800 -16.49200 1.000 31.35268 ? 35  GLN C CB  1 
ATOM   1416 C CG  . GLN B 2 35  ? -20.65600 21.51700 -17.34100 1.000 32.10638 ? 35  GLN C CG  1 
ATOM   1417 C CD  . GLN B 2 35  ? -20.22100 20.58000 -18.42800 1.000 34.48058 ? 35  GLN C CD  1 
ATOM   1418 O OE1 . GLN B 2 35  ? -19.19500 20.80200 -19.07000 1.000 37.95638 ? 35  GLN C OE1 1 
ATOM   1419 N NE2 . GLN B 2 35  ? -20.99000 19.52200 -18.64800 1.000 36.10575 ? 35  GLN C NE2 1 
ATOM   1420 N N   . HIS B 2 36  ? -18.33900 24.35300 -14.67700 1.000 27.31485 ? 36  HIS C N   1 
ATOM   1421 C CA  . HIS B 2 36  ? -17.52100 24.66500 -13.50800 1.000 31.36627 ? 36  HIS C CA  1 
ATOM   1422 C C   . HIS B 2 36  ? -16.56200 23.55200 -13.11900 1.000 26.12335 ? 36  HIS C C   1 
ATOM   1423 O O   . HIS B 2 36  ? -15.36500 23.79600 -12.95900 1.000 25.23650 ? 36  HIS C O   1 
ATOM   1424 C CB  . HIS B 2 36  ? -18.41400 24.96800 -12.29900 1.000 33.84040 ? 36  HIS C CB  1 
ATOM   1425 C CG  . HIS B 2 36  ? -19.01100 26.33400 -12.31000 1.000 39.26806 ? 36  HIS C CG  1 
ATOM   1426 N ND1 . HIS B 2 36  ? -18.26000 27.46900 -12.51800 1.000 39.63369 ? 36  HIS C ND1 1 
ATOM   1427 C CD2 . HIS B 2 36  ? -20.29200 26.74800 -12.17100 1.000 43.29861 ? 36  HIS C CD2 1 
ATOM   1428 C CE1 . HIS B 2 36  ? -19.04900 28.52800 -12.47700 1.000 40.98571 ? 36  HIS C CE1 1 
ATOM   1429 N NE2 . HIS B 2 36  ? -20.28900 28.11600 -12.28200 1.000 44.61316 ? 36  HIS C NE2 1 
ATOM   1430 N N   . PHE B 2 37  ? -17.08500 22.33400 -12.95700 1.000 24.38609 ? 37  PHE C N   1 
ATOM   1431 C CA  . PHE B 2 37  ? -16.31800 21.25500 -12.35200 1.000 24.70178 ? 37  PHE C CA  1 
ATOM   1432 C C   . PHE B 2 37  ? -15.20300 20.74100 -13.24600 1.000 23.39939 ? 37  PHE C C   1 
ATOM   1433 O O   . PHE B 2 37  ? -14.35800 19.98000 -12.76600 1.000 22.11078 ? 37  PHE C O   1 
ATOM   1434 C CB  . PHE B 2 37  ? -17.23100 20.09000 -11.95300 1.000 25.38911 ? 37  PHE C CB  1 
ATOM   1435 C CG  . PHE B 2 37  ? -18.12500 19.60500 -13.06100 1.000 30.53518 ? 37  PHE C CG  1 
ATOM   1436 C CD1 . PHE B 2 37  ? -17.65800 18.70100 -14.00700 1.000 29.46287 ? 37  PHE C CD1 1 
ATOM   1437 C CD2 . PHE B 2 37  ? -19.45400 19.99800 -13.11700 1.000 31.86028 ? 37  PHE C CD2 1 
ATOM   1438 C CE1 . PHE B 2 37  ? -18.49100 18.24500 -15.01300 1.000 27.95764 ? 37  PHE C CE1 1 
ATOM   1439 C CE2 . PHE B 2 37  ? -20.29400 19.53900 -14.12900 1.000 31.71067 ? 37  PHE C CE2 1 
ATOM   1440 C CZ  . PHE B 2 37  ? -19.80600 18.66600 -15.07200 1.000 33.41624 ? 37  PHE C CZ  1 
ATOM   1441 N N   . LEU B 2 38  ? -15.18600 21.11900 -14.52100 1.000 23.95186 ? 38  LEU C N   1 
ATOM   1442 C CA  . LEU B 2 38  ? -14.07600 20.75000 -15.38300 1.000 28.14129 ? 38  LEU C CA  1 
ATOM   1443 C C   . LEU B 2 38  ? -12.88300 21.69000 -15.25000 1.000 27.03221 ? 38  LEU C C   1 
ATOM   1444 O O   . LEU B 2 38  ? -11.79700 21.35900 -15.74500 1.000 26.63201 ? 38  LEU C O   1 
ATOM   1445 C CB  . LEU B 2 38  ? -14.53400 20.72000 -16.84500 1.000 23.99692 ? 38  LEU C CB  1 
ATOM   1446 C CG  . LEU B 2 38  ? -15.45100 19.59000 -17.31200 1.000 25.79033 ? 38  LEU C CG  1 
ATOM   1447 C CD1 . LEU B 2 38  ? -15.67900 19.67900 -18.82100 1.000 28.69928 ? 38  LEU C CD1 1 
ATOM   1448 C CD2 . LEU B 2 38  ? -14.86300 18.23700 -16.93900 1.000 30.66611 ? 38  LEU C CD2 1 
ATOM   1449 N N   . ALA B 2 39  ? -13.04500 22.86200 -14.63300 1.000 22.14810 ? 39  ALA C N   1 
ATOM   1450 C CA  . ALA B 2 39  ? -11.91100 23.77200 -14.50200 1.000 23.13063 ? 39  ALA C CA  1 
ATOM   1451 C C   . ALA B 2 39  ? -11.06800 23.33300 -13.31100 1.000 25.03349 ? 39  ALA C C   1 
ATOM   1452 O O   . ALA B 2 39  ? -11.53200 23.36100 -12.16500 1.000 20.22656 ? 39  ALA C O   1 
ATOM   1453 C CB  . ALA B 2 39  ? -12.37900 25.21800 -14.35600 1.000 21.52795 ? 39  ALA C CB  1 
ATOM   1454 N N   . GLN B 2 40  ? -9.83300  22.90400 -13.57400 1.000 17.55601 ? 40  GLN C N   1 
ATOM   1455 C CA  . GLN B 2 40  ? -8.87700  22.61700 -12.50900 1.000 18.52520 ? 40  GLN C CA  1 
ATOM   1456 C C   . GLN B 2 40  ? -7.92900  23.79700 -12.38100 1.000 19.70729 ? 40  GLN C C   1 
ATOM   1457 O O   . GLN B 2 40  ? -7.37800  24.26900 -13.37900 1.000 17.82349 ? 40  GLN C O   1 
ATOM   1458 C CB  . GLN B 2 40  ? -8.07400  21.33900 -12.77500 1.000 17.94037 ? 40  GLN C CB  1 
ATOM   1459 C CG  . GLN B 2 40  ? -6.95300  21.13900 -11.74200 1.000 17.16841 ? 40  GLN C CG  1 
ATOM   1460 C CD  . GLN B 2 40  ? -6.27500  19.77500 -11.78700 1.000 17.08561 ? 40  GLN C CD  1 
ATOM   1461 O OE1 . GLN B 2 40  ? -5.16400  19.64100 -11.30700 1.000 20.31332 ? 40  GLN C OE1 1 
ATOM   1462 N NE2 . GLN B 2 40  ? -6.95900  18.75900 -12.31500 1.000 16.94744 ? 40  GLN C NE2 1 
ATOM   1463 N N   . VAL B 2 41  ? -7.75400  24.28700 -11.16200 1.000 17.14812 ? 41  VAL C N   1 
ATOM   1464 C CA  . VAL B 2 41  ? -6.74400  25.29800 -10.87400 1.000 18.67026 ? 41  VAL C CA  1 
ATOM   1465 C C   . VAL B 2 41  ? -5.74400  24.64900 -9.93300  1.000 20.71926 ? 41  VAL C C   1 
ATOM   1466 O O   . VAL B 2 41  ? -6.11500  24.19200 -8.84700  1.000 18.98834 ? 41  VAL C O   1 
ATOM   1467 C CB  . VAL B 2 41  ? -7.34600  26.56600 -10.25200 1.000 18.63395 ? 41  VAL C CB  1 
ATOM   1468 C CG1 . VAL B 2 41  ? -6.24300  27.52600 -9.84400  1.000 17.65398 ? 41  VAL C CG1 1 
ATOM   1469 C CG2 . VAL B 2 41  ? -8.33600  27.22200 -11.22200 1.000 17.14083 ? 41  VAL C CG2 1 
ATOM   1470 N N   . ASN B 2 42  ? -4.49500  24.56500 -10.36300 1.000 16.89636 ? 42  ASN C N   1 
ATOM   1471 C CA  . ASN B 2 42  ? -3.48400  23.80000 -9.64600  1.000 19.12487 ? 42  ASN C CA  1 
ATOM   1472 C C   . ASN B 2 42  ? -2.38700  24.76200 -9.20200  1.000 18.77288 ? 42  ASN C C   1 
ATOM   1473 O O   . ASN B 2 42  ? -1.58800  25.22000 -10.02900 1.000 18.11768 ? 42  ASN C O   1 
ATOM   1474 C CB  . ASN B 2 42  ? -2.94500  22.68200 -10.54500 1.000 19.88542 ? 42  ASN C CB  1 
ATOM   1475 C CG  . ASN B 2 42  ? -2.16200  21.64500 -9.78000  1.000 21.05121 ? 42  ASN C CG  1 
ATOM   1476 O OD1 . ASN B 2 42  ? -1.26200  21.97900 -9.00600  1.000 23.30171 ? 42  ASN C OD1 1 
ATOM   1477 N ND2 . ASN B 2 42  ? -2.50500  20.37400 -9.97900  1.000 22.35073 ? 42  ASN C ND2 1 
ATOM   1478 N N   . PHE B 2 43  ? -2.33600  25.07600 -7.89900  1.000 19.72606 ? 43  PHE C N   1 
ATOM   1479 C CA  . PHE B 2 43  ? -1.37100  26.06900 -7.42500  1.000 18.22416 ? 43  PHE C CA  1 
ATOM   1480 C C   . PHE B 2 43  ? -0.01400  25.42400 -7.18700  1.000 19.55861 ? 43  PHE C C   1 
ATOM   1481 O O   . PHE B 2 43  ? 0.08800   24.42800 -6.46400  1.000 20.19156 ? 43  PHE C O   1 
ATOM   1482 C CB  . PHE B 2 43  ? -1.84900  26.74200 -6.13200  1.000 19.60673 ? 43  PHE C CB  1 
ATOM   1483 C CG  . PHE B 2 43  ? -2.86800  27.83200 -6.35400  1.000 16.54861 ? 43  PHE C CG  1 
ATOM   1484 C CD1 . PHE B 2 43  ? -2.47900  29.09700 -6.74000  1.000 16.43558 ? 43  PHE C CD1 1 
ATOM   1485 C CD2 . PHE B 2 43  ? -4.22000  27.57100 -6.20400  1.000 16.36028 ? 43  PHE C CD2 1 
ATOM   1486 C CE1 . PHE B 2 43  ? -3.42000  30.10600 -6.95200  1.000 16.51783 ? 43  PHE C CE1 1 
ATOM   1487 C CE2 . PHE B 2 43  ? -5.16000  28.56900 -6.40500  1.000 18.04603 ? 43  PHE C CE2 1 
ATOM   1488 C CZ  . PHE B 2 43  ? -4.75800  29.83800 -6.77900  1.000 17.67431 ? 43  PHE C CZ  1 
ATOM   1489 N N   . GLN B 2 44  ? 1.03200   26.02400 -7.75800  1.000 15.91613 ? 44  GLN C N   1 
ATOM   1490 C CA  . GLN B 2 44  ? 2.40300   25.53800 -7.63200  1.000 17.11061 ? 44  GLN C CA  1 
ATOM   1491 C C   . GLN B 2 44  ? 3.19000   26.60600 -6.89200  1.000 18.49220 ? 44  GLN C C   1 
ATOM   1492 O O   . GLN B 2 44  ? 3.58000   27.61700 -7.48800  1.000 18.55917 ? 44  GLN C O   1 
ATOM   1493 C CB  . GLN B 2 44  ? 3.02700   25.24000 -9.00000  1.000 16.83929 ? 44  GLN C CB  1 
ATOM   1494 C CG  . GLN B 2 44  ? 2.28700   24.13800 -9.76500  1.000 19.93164 ? 44  GLN C CG  1 
ATOM   1495 C CD  . GLN B 2 44  ? 2.53700   22.77000 -9.17400  1.000 20.78188 ? 44  GLN C CD  1 
ATOM   1496 O OE1 . GLN B 2 44  ? 3.68900   22.35600 -9.01800  1.000 25.74345 ? 44  GLN C OE1 1 
ATOM   1497 N NE2 . GLN B 2 44  ? 1.46700   22.05900 -8.83200  1.000 18.53150 ? 44  GLN C NE2 1 
ATOM   1498 N N   . GLU B 2 45  ? 3.44000   26.37300 -5.60500  1.000 20.57709 ? 45  GLU C N   1 
ATOM   1499 C CA  . GLU B 2 45  ? 4.17700   27.32300 -4.78200  1.000 19.86558 ? 45  GLU C CA  1 
ATOM   1500 C C   . GLU B 2 45  ? 5.66700   27.00900 -4.73600  1.000 21.25776 ? 45  GLU C C   1 
ATOM   1501 O O   . GLU B 2 45  ? 6.07500   25.84800 -4.62600  1.000 21.76941 ? 45  GLU C O   1 
ATOM   1502 C CB  . GLU B 2 45  ? 3.63500   27.33900 -3.35300  1.000 20.74270 ? 45  GLU C CB  1 
ATOM   1503 C CG  . GLU B 2 45  ? 2.27900   27.99300 -3.24500  1.000 22.45127 ? 45  GLU C CG  1 
ATOM   1504 C CD  . GLU B 2 45  ? 1.71100   27.86800 -1.83000  1.000 29.42248 ? 45  GLU C CD  1 
ATOM   1505 O OE1 . GLU B 2 45  ? 1.62500   26.73400 -1.33100  1.000 26.77528 ? 45  GLU C OE1 1 
ATOM   1506 O OE2 . GLU B 2 45  ? 1.35700   28.90400 -1.24100  1.000 30.77684 ? 45  GLU C OE2 1 
ATOM   1507 N N   . GLN B 2 46  ? 6.47500   28.06100 -4.76300  1.000 18.56800 ? 46  GLN C N   1 
ATOM   1508 C CA  . GLN B 2 46  ? 7.91200   27.96300 -4.55000  1.000 21.82280 ? 46  GLN C CA  1 
ATOM   1509 C C   . GLN B 2 46  ? 8.37000   29.14800 -3.71600  1.000 22.17457 ? 46  GLN C C   1 
ATOM   1510 O O   . GLN B 2 46  ? 7.75800   30.21700 -3.76800  1.000 21.05774 ? 46  GLN C O   1 
ATOM   1511 C CB  . GLN B 2 46  ? 8.67800   27.94800 -5.88200  1.000 24.12167 ? 46  GLN C CB  1 
ATOM   1512 C CG  . GLN B 2 46  ? 8.48500   26.67200 -6.70600  1.000 21.69335 ? 46  GLN C CG  1 
ATOM   1513 C CD  . GLN B 2 46  ? 9.24600   25.49700 -6.12800  1.000 21.87107 ? 46  GLN C CD  1 
ATOM   1514 O OE1 . GLN B 2 46  ? 10.41200  25.62500 -5.73500  1.000 24.58436 ? 46  GLN C OE1 1 
ATOM   1515 N NE2 . GLN B 2 46  ? 8.60100   24.34200 -6.08100  1.000 21.56385 ? 46  GLN C NE2 1 
ATOM   1516 N N   . PRO B 2 47  ? 9.46700   29.01100 -2.98400  1.000 24.47218 ? 47  PRO C N   1 
ATOM   1517 C CA  . PRO B 2 47  ? 9.93600   30.14300 -2.17500  1.000 24.55236 ? 47  PRO C CA  1 
ATOM   1518 C C   . PRO B 2 47  ? 10.15100  31.39200 -3.02700  1.000 23.99363 ? 47  PRO C C   1 
ATOM   1519 O O   . PRO B 2 47  ? 10.53900  31.31600 -4.19600  1.000 21.23246 ? 47  PRO C O   1 
ATOM   1520 C CB  . PRO B 2 47  ? 11.25100  29.63100 -1.56900  1.000 25.16424 ? 47  PRO C CB  1 
ATOM   1521 C CG  . PRO B 2 47  ? 11.64900  28.45500 -2.38300  1.000 30.84801 ? 47  PRO C CG  1 
ATOM   1522 C CD  . PRO B 2 47  ? 10.36300  27.84500 -2.89700  1.000 23.42573 ? 47  PRO C CD  1 
ATOM   1523 N N   . ALA B 2 48  ? 9.85100   32.55100 -2.44200  1.000 22.09420 ? 48  ALA C N   1 
ATOM   1524 C CA  . ALA B 2 48  ? 10.23500  33.81200 -3.06500  1.000 22.99295 ? 48  ALA C CA  1 
ATOM   1525 C C   . ALA B 2 48  ? 11.73000  33.81300 -3.32300  1.000 23.43102 ? 48  ALA C C   1 
ATOM   1526 O O   . ALA B 2 48  ? 12.51500  33.30300 -2.51800  1.000 24.73797 ? 48  ALA C O   1 
ATOM   1527 C CB  . ALA B 2 48  ? 9.85600   35.00000 -2.17100  1.000 25.64137 ? 48  ALA C CB  1 
ATOM   1528 N N   . GLY B 2 49  ? 12.12100  34.37800 -4.46100  1.000 22.53057 ? 49  GLY C N   1 
ATOM   1529 C CA  . GLY B 2 49  ? 13.48700  34.31100 -4.92900  1.000 24.18770 ? 49  GLY C CA  1 
ATOM   1530 C C   . GLY B 2 49  ? 13.73300  33.25200 -5.98500  1.000 21.32808 ? 49  GLY C C   1 
ATOM   1531 O O   . GLY B 2 49  ? 14.83300  33.21200 -6.54700  1.000 25.04790 ? 49  GLY C O   1 
ATOM   1532 N N   . ASN B 2 50  ? 12.75700  32.38300 -6.26800  1.000 18.09806 ? 50  ASN C N   1 
ATOM   1533 C CA  . ASN B 2 50  ? 12.94400  31.38200 -7.31200  1.000 22.58158 ? 50  ASN C CA  1 
ATOM   1534 C C   . ASN B 2 50  ? 12.54900  31.88400 -8.70000  1.000 21.52372 ? 50  ASN C C   1 
ATOM   1535 O O   . ASN B 2 50  ? 12.73600  31.14900 -9.67900  1.000 20.12220 ? 50  ASN C O   1 
ATOM   1536 C CB  . ASN B 2 50  ? 12.18100  30.09000 -6.97100  1.000 20.04659 ? 50  ASN C CB  1 
ATOM   1537 C CG  . ASN B 2 50  ? 12.98800  29.15400 -6.05400  1.000 26.27086 ? 50  ASN C CG  1 
ATOM   1538 O OD1 . ASN B 2 50  ? 13.88400  29.59900 -5.34300  1.000 26.43396 ? 50  ASN C OD1 1 
ATOM   1539 N ND2 . ASN B 2 50  ? 12.65000  27.86500 -6.05200  1.000 24.28913 ? 50  ASN C ND2 1 
ATOM   1540 N N   . VAL B 2 51  ? 12.03500  33.10900 -8.82500  1.000 18.08850 ? 51  VAL C N   1 
ATOM   1541 C CA  . VAL B 2 51  ? 11.71100  33.69200 -10.12900 1.000 20.61996 ? 51  VAL C CA  1 
ATOM   1542 C C   . VAL B 2 51  ? 12.75300  34.74400 -10.48600 1.000 22.22254 ? 51  VAL C C   1 
ATOM   1543 O O   . VAL B 2 51  ? 13.07600  35.61600 -9.67200  1.000 20.18777 ? 51  VAL C O   1 
ATOM   1544 C CB  . VAL B 2 51  ? 10.29600  34.29600 -10.15100 1.000 21.78613 ? 51  VAL C CB  1 
ATOM   1545 C CG1 . VAL B 2 51  ? 10.05600  35.06000 -11.45000 1.000 23.35728 ? 51  VAL C CG1 1 
ATOM   1546 C CG2 . VAL B 2 51  ? 9.25200   33.18300 -9.99500  1.000 21.68102 ? 51  VAL C CG2 1 
ATOM   1547 N N   . PHE B 2 52  ? 13.26100  34.67400 -11.71700 1.000 19.24342 ? 52  PHE C N   1 
ATOM   1548 C CA  . PHE B 2 52  ? 14.19400  35.64900 -12.25500 1.000 21.31429 ? 52  PHE C CA  1 
ATOM   1549 C C   . PHE B 2 52  ? 13.61000  36.26600 -13.51900 1.000 23.11198 ? 52  PHE C C   1 
ATOM   1550 O O   . PHE B 2 52  ? 13.12000  35.54800 -14.39500 1.000 24.42615 ? 52  PHE C O   1 
ATOM   1551 C CB  . PHE B 2 52  ? 15.54400  34.99800 -12.56000 1.000 19.30254 ? 52  PHE C CB  1 
ATOM   1552 C CG  . PHE B 2 52  ? 16.32800  34.66300 -11.34300 1.000 23.63414 ? 52  PHE C CG  1 
ATOM   1553 C CD1 . PHE B 2 52  ? 15.99100  33.56200 -10.56700 1.000 19.30259 ? 52  PHE C CD1 1 
ATOM   1554 C CD2 . PHE B 2 52  ? 17.39000  35.47200 -10.95000 1.000 23.62189 ? 52  PHE C CD2 1 
ATOM   1555 C CE1 . PHE B 2 52  ? 16.71000  33.25800 -9.41400  1.000 23.32090 ? 52  PHE C CE1 1 
ATOM   1556 C CE2 . PHE B 2 52  ? 18.11700  35.18300 -9.81100  1.000 24.24671 ? 52  PHE C CE2 1 
ATOM   1557 C CZ  . PHE B 2 52  ? 17.77500  34.06200 -9.03700  1.000 24.92218 ? 52  PHE C CZ  1 
ATOM   1558 N N   . LEU B 2 53  ? 13.68000  37.59000 -13.61800 1.000 21.99752 ? 53  LEU C N   1 
ATOM   1559 C CA  . LEU B 2 53  ? 13.23300  38.32000 -14.79800 1.000 21.37021 ? 53  LEU C CA  1 
ATOM   1560 C C   . LEU B 2 53  ? 14.42300  39.09700 -15.33600 1.000 21.97246 ? 53  LEU C C   1 
ATOM   1561 O O   . LEU B 2 53  ? 14.93000  39.99300 -14.65800 1.000 23.23836 ? 53  LEU C O   1 
ATOM   1562 C CB  . LEU B 2 53  ? 12.07800  39.27300 -14.46500 1.000 21.99604 ? 53  LEU C CB  1 
ATOM   1563 C CG  . LEU B 2 53  ? 10.76700  38.61700 -14.03700 1.000 23.92967 ? 53  LEU C CG  1 
ATOM   1564 C CD1 . LEU B 2 53  ? 9.67900   39.65400 -13.80700 1.000 23.24140 ? 53  LEU C CD1 1 
ATOM   1565 C CD2 . LEU B 2 53  ? 10.31700  37.63100 -15.11400 1.000 23.31344 ? 53  LEU C CD2 1 
ATOM   1566 N N   . GLY B 2 54  ? 14.84800  38.77500 -16.55700 1.000 22.72766 ? 54  GLY C N   1 
ATOM   1567 C CA  . GLY B 2 54  ? 16.04000  39.40100 -17.10400 1.000 24.32117 ? 54  GLY C CA  1 
ATOM   1568 C C   . GLY B 2 54  ? 17.27400  39.14300 -16.27300 1.000 23.87403 ? 54  GLY C C   1 
ATOM   1569 O O   . GLY B 2 54  ? 18.19300  39.97100 -16.25600 1.000 29.12357 ? 54  GLY C O   1 
ATOM   1570 N N   . GLY B 2 55  ? 17.31400  38.01600 -15.56400 1.000 21.25022 ? 55  GLY C N   1 
ATOM   1571 C CA  . GLY B 2 55  ? 18.41500  37.71500 -14.67100 1.000 23.89935 ? 55  GLY C CA  1 
ATOM   1572 C C   . GLY B 2 55  ? 18.34100  38.38900 -13.31800 1.000 25.19403 ? 55  GLY C C   1 
ATOM   1573 O O   . GLY B 2 55  ? 19.26800  38.22600 -12.51600 1.000 30.12605 ? 55  GLY C O   1 
ATOM   1574 N N   . VAL B 2 56  ? 17.28000  39.14300 -13.03800 1.000 25.78003 ? 56  VAL C N   1 
ATOM   1575 C CA  . VAL B 2 56  ? 17.10300  39.83100 -11.75600 1.000 25.06326 ? 56  VAL C CA  1 
ATOM   1576 C C   . VAL B 2 56  ? 16.19800  38.98600 -10.87200 1.000 24.95874 ? 56  VAL C C   1 
ATOM   1577 O O   . VAL B 2 56  ? 15.03800  38.74200 -11.22300 1.000 22.81136 ? 56  VAL C O   1 
ATOM   1578 C CB  . VAL B 2 56  ? 16.51100  41.23700 -11.95900 1.000 25.85824 ? 56  VAL C CB  1 
ATOM   1579 C CG1 . VAL B 2 56  ? 16.15700  41.90000 -10.61700 1.000 26.82040 ? 56  VAL C CG1 1 
ATOM   1580 C CG2 . VAL B 2 56  ? 17.46100  42.11500 -12.77200 1.000 27.73051 ? 56  VAL C CG2 1 
ATOM   1581 N N   . GLN B 2 57  ? 16.70700  38.57800 -9.70200  1.000 25.10738 ? 57  GLN C N   1 
ATOM   1582 C CA  . GLN B 2 57  ? 15.89200  37.83900 -8.74000  1.000 26.73971 ? 57  GLN C CA  1 
ATOM   1583 C C   . GLN B 2 57  ? 14.67700  38.67200 -8.34700  1.000 26.38737 ? 57  GLN C C   1 
ATOM   1584 O O   . GLN B 2 57  ? 14.80600  39.86200 -8.05000  1.000 25.80460 ? 57  GLN C O   1 
ATOM   1585 C CB  . GLN B 2 57  ? 16.69900  37.51200 -7.48100  1.000 24.87950 ? 57  GLN C CB  1 
ATOM   1586 C CG  . GLN B 2 57  ? 15.88800  36.78500 -6.42700  1.000 25.27189 ? 57  GLN C CG  1 
ATOM   1587 C CD  . GLN B 2 57  ? 16.70600  36.35900 -5.22000  1.000 35.04621 ? 57  GLN C CD  1 
ATOM   1588 O OE1 . GLN B 2 57  ? 16.63700  36.99200 -4.16800  1.000 37.49708 ? 57  GLN C OE1 1 
ATOM   1589 N NE2 . GLN B 2 57  ? 17.49300  35.31000 -5.36800  1.000 35.39761 ? 57  GLN C NE2 1 
ATOM   1590 N N   . GLN B 2 58  ? 13.49800  38.04900 -8.32700  1.000 24.46055 ? 58  GLN C N   1 
ATOM   1591 C CA  . GLN B 2 58  ? 12.26100  38.72700 -7.95700  1.000 23.11129 ? 58  GLN C CA  1 
ATOM   1592 C C   . GLN B 2 58  ? 11.86000  38.43200 -6.51200  1.000 25.19884 ? 58  GLN C C   1 
ATOM   1593 O O   . GLN B 2 58  ? 12.27700  37.43900 -5.91600  1.000 26.98087 ? 58  GLN C O   1 
ATOM   1594 C CB  . GLN B 2 58  ? 11.11500  38.29900 -8.88200  1.000 25.51222 ? 58  GLN C CB  1 
ATOM   1595 C CG  . GLN B 2 58  ? 11.36900  38.56400 -10.35200 1.000 24.62045 ? 58  GLN C CG  1 
ATOM   1596 C CD  . GLN B 2 58  ? 11.56200  40.04400 -10.64200 1.000 24.55228 ? 58  GLN C CD  1 
ATOM   1597 O OE1 . GLN B 2 58  ? 10.64800  40.83900 -10.45200 1.000 29.49836 ? 58  GLN C OE1 1 
ATOM   1598 N NE2 . GLN B 2 58  ? 12.75000  40.41800 -11.08300 1.000 24.31452 ? 58  GLN C NE2 1 
ATOM   1599 N N   . GLY B 2 59  ? 11.01300  39.30500 -5.96500  1.000 22.28897 ? 59  GLY C N   1 
ATOM   1600 C CA  . GLY B 2 59  ? 10.32900  39.03800 -4.71400  1.000 23.81573 ? 59  GLY C CA  1 
ATOM   1601 C C   . GLY B 2 59  ? 9.18300   38.07200 -4.95500  1.000 29.29927 ? 59  GLY C C   1 
ATOM   1602 O O   . GLY B 2 59  ? 9.24300   37.20500 -5.83700  1.000 28.25349 ? 59  GLY C O   1 
ATOM   1603 N N   . GLY B 2 60  ? 8.10600   38.23200 -4.19200  1.000 23.95944 ? 60  GLY C N   1 
ATOM   1604 C CA  . GLY B 2 60  ? 7.06800   37.22500 -4.21800  1.000 26.72674 ? 60  GLY C CA  1 
ATOM   1605 C C   . GLY B 2 60  ? 5.83500   37.54500 -5.04100  1.000 26.50950 ? 60  GLY C C   1 
ATOM   1606 O O   . GLY B 2 60  ? 4.79900   36.88600 -4.89900  1.000 23.31717 ? 60  GLY C O   1 
ATOM   1607 N N   . ASP B 2 61  ? 5.92000   38.54000 -5.91500  1.000 24.57849 ? 61  ASP C N   1 
ATOM   1608 C CA  . ASP B 2 61  ? 4.71700   39.05600 -6.54600  1.000 26.24895 ? 61  ASP C CA  1 
ATOM   1609 C C   . ASP B 2 61  ? 4.45400   38.49800 -7.94500  1.000 26.39661 ? 61  ASP C C   1 
ATOM   1610 O O   . ASP B 2 61  ? 3.39600   38.77100 -8.50600  1.000 30.40083 ? 61  ASP C O   1 
ATOM   1611 C CB  . ASP B 2 61  ? 4.78500   40.58000 -6.61700  1.000 31.89322 ? 61  ASP C CB  1 
ATOM   1612 C CG  . ASP B 2 61  ? 4.14000   41.24500 -5.42700  1.000 39.08116 ? 61  ASP C CG  1 
ATOM   1613 O OD1 . ASP B 2 61  ? 3.88400   40.54200 -4.41800  1.000 34.69971 ? 61  ASP C OD1 1 
ATOM   1614 O OD2 . ASP B 2 61  ? 3.90400   42.47500 -5.49700  1.000 42.44695 ? 61  ASP C OD2 1 
ATOM   1615 N N   . THR B 2 62  ? 5.35600   37.73500 -8.53600  1.000 22.51278 ? 62  THR C N   1 
ATOM   1616 C CA  . THR B 2 62  ? 5.07700   37.25600 -9.88300  1.000 21.24172 ? 62  THR C CA  1 
ATOM   1617 C C   . THR B 2 62  ? 4.04000   36.13400 -9.86000  1.000 19.98784 ? 62  THR C C   1 
ATOM   1618 O O   . THR B 2 62  ? 4.02400   35.29000 -8.96400  1.000 19.50376 ? 62  THR C O   1 
ATOM   1619 C CB  . THR B 2 62  ? 6.36400   36.79600 -10.56500 1.000 23.55653 ? 62  THR C CB  1 
ATOM   1620 O OG1 . THR B 2 62  ? 7.38400   37.78500 -10.36900 1.000 28.40842 ? 62  THR C OG1 1 
ATOM   1621 C CG2 . THR B 2 62  ? 6.14600   36.62200 -12.06000 1.000 23.97695 ? 62  THR C CG2 1 
ATOM   1622 N N   . ILE B 2 63  ? 3.14500   36.15000 -10.84500 1.000 18.94587 ? 63  ILE C N   1 
ATOM   1623 C CA  . ILE B 2 63  ? 2.15000   35.10100 -11.03400 1.000 17.89124 ? 63  ILE C CA  1 
ATOM   1624 C C   . ILE B 2 63  ? 2.20300   34.66300 -12.48700 1.000 18.88563 ? 63  ILE C C   1 
ATOM   1625 O O   . ILE B 2 63  ? 1.96900   35.47900 -13.38400 1.000 20.31695 ? 63  ILE C O   1 
ATOM   1626 C CB  . ILE B 2 63  ? 0.72700   35.57100 -10.70100 1.000 19.53753 ? 63  ILE C CB  1 
ATOM   1627 C CG1 . ILE B 2 63  ? 0.60400   35.92200 -9.21700  1.000 21.11964 ? 63  ILE C CG1 1 
ATOM   1628 C CG2 . ILE B 2 63  ? -0.28600  34.47700 -11.06500 1.000 19.17826 ? 63  ILE C CG2 1 
ATOM   1629 C CD1 . ILE B 2 63  ? -0.80600  36.26500 -8.82600  1.000 25.08840 ? 63  ILE C CD1 1 
ATOM   1630 N N   . PHE B 2 64  ? 2.46900   33.38000 -12.71600 1.000 18.93698 ? 64  PHE C N   1 
ATOM   1631 C CA  . PHE B 2 64  ? 2.42900   32.79400 -14.05500 1.000 19.45755 ? 64  PHE C CA  1 
ATOM   1632 C C   . PHE B 2 64  ? 1.31000   31.76500 -14.12700 1.000 18.19354 ? 64  PHE C C   1 
ATOM   1633 O O   . PHE B 2 64  ? 1.32400   30.77500 -13.38800 1.000 16.71631 ? 64  PHE C O   1 
ATOM   1634 C CB  . PHE B 2 64  ? 3.76000   32.13400 -14.40500 1.000 16.32744 ? 64  PHE C CB  1 
ATOM   1635 C CG  . PHE B 2 64  ? 3.75500   31.42000 -15.73100 1.000 18.80179 ? 64  PHE C CG  1 
ATOM   1636 C CD1 . PHE B 2 64  ? 3.17300   32.00900 -16.85000 1.000 19.26157 ? 64  PHE C CD1 1 
ATOM   1637 C CD2 . PHE B 2 64  ? 4.31600   30.15400 -15.85100 1.000 15.85060 ? 64  PHE C CD2 1 
ATOM   1638 C CE1 . PHE B 2 64  ? 3.17700   31.34200 -18.08100 1.000 19.98301 ? 64  PHE C CE1 1 
ATOM   1639 C CE2 . PHE B 2 64  ? 4.32400   29.48700 -17.07100 1.000 17.50718 ? 64  PHE C CE2 1 
ATOM   1640 C CZ  . PHE B 2 64  ? 3.75100   30.07500 -18.17700 1.000 18.01571 ? 64  PHE C CZ  1 
ATOM   1641 N N   . VAL B 2 65  ? 0.36300   31.98000 -15.03700 1.000 15.95175 ? 65  VAL C N   1 
ATOM   1642 C CA  . VAL B 2 65  ? -0.72700  31.04100 -15.28400 1.000 16.47288 ? 65  VAL C CA  1 
ATOM   1643 C C   . VAL B 2 65  ? -0.42700  30.31200 -16.58700 1.000 19.53579 ? 65  VAL C C   1 
ATOM   1644 O O   . VAL B 2 65  ? -0.28900  30.95100 -17.63600 1.000 19.57520 ? 65  VAL C O   1 
ATOM   1645 C CB  . VAL B 2 65  ? -2.08200  31.76400 -15.35200 1.000 17.75449 ? 65  VAL C CB  1 
ATOM   1646 C CG1 . VAL B 2 65  ? -3.20500  30.77200 -15.63800 1.000 18.49143 ? 65  VAL C CG1 1 
ATOM   1647 C CG2 . VAL B 2 65  ? -2.35300  32.52400 -14.03700 1.000 16.72477 ? 65  VAL C CG2 1 
ATOM   1648 N N   . HIS B 2 66  ? -0.27300  28.98900 -16.52000 1.000 17.29690 ? 66  HIS C N   1 
ATOM   1649 C CA  . HIS B 2 66  ? -0.08600  28.15100 -17.70800 1.000 15.78425 ? 66  HIS C CA  1 
ATOM   1650 C C   . HIS B 2 66  ? -1.39200  27.38700 -17.88100 1.000 17.38526 ? 66  HIS C C   1 
ATOM   1651 O O   . HIS B 2 66  ? -1.68900  26.46200 -17.12500 1.000 15.86286 ? 66  HIS C O   1 
ATOM   1652 C CB  . HIS B 2 66  ? 1.12000   27.21200 -17.56600 1.000 17.06108 ? 66  HIS C CB  1 
ATOM   1653 C CG  . HIS B 2 66  ? 1.53500   26.55400 -18.85700 1.000 18.86019 ? 66  HIS C CG  1 
ATOM   1654 N ND1 . HIS B 2 66  ? 2.40600   25.48700 -18.90700 1.000 15.65404 ? 66  HIS C ND1 1 
ATOM   1655 C CD2 . HIS B 2 66  ? 1.17700   26.80400 -20.14200 1.000 18.76059 ? 66  HIS C CD2 1 
ATOM   1656 C CE1 . HIS B 2 66  ? 2.58000   25.11600 -20.16400 1.000 19.76140 ? 66  HIS C CE1 1 
ATOM   1657 N NE2 . HIS B 2 66  ? 1.83800   25.89400 -20.93400 1.000 19.05018 ? 66  HIS C NE2 1 
ATOM   1658 N N   . GLY B 2 67  ? -2.19600  27.80800 -18.86700 1.000 18.64145 ? 67  GLY C N   1 
ATOM   1659 C CA  . GLY B 2 67  ? -3.49500  27.19600 -19.10100 1.000 20.47238 ? 67  GLY C CA  1 
ATOM   1660 C C   . GLY B 2 67  ? -3.38600  26.14500 -20.18800 1.000 21.09677 ? 67  GLY C C   1 
ATOM   1661 O O   . GLY B 2 67  ? -2.81800  26.40000 -21.25400 1.000 20.05741 ? 67  GLY C O   1 
ATOM   1662 N N   . LEU B 2 68  ? -3.89900  24.94400 -19.89300 1.000 16.74283 ? 68  LEU C N   1 
ATOM   1663 C CA  . LEU B 2 68  ? -3.83700  23.79500 -20.79400 1.000 17.07965 ? 68  LEU C CA  1 
ATOM   1664 C C   . LEU B 2 68  ? -5.25200  23.50100 -21.27700 1.000 20.01339 ? 68  LEU C C   1 
ATOM   1665 O O   . LEU B 2 68  ? -6.10100  23.04400 -20.49700 1.000 16.36384 ? 68  LEU C O   1 
ATOM   1666 C CB  . LEU B 2 68  ? -3.20000  22.60000 -20.08800 1.000 17.23606 ? 68  LEU C CB  1 
ATOM   1667 C CG  . LEU B 2 68  ? -1.82800  22.98400 -19.50900 1.000 17.23656 ? 68  LEU C CG  1 
ATOM   1668 C CD1 . LEU B 2 68  ? -1.23200  21.89700 -18.64400 1.000 17.46963 ? 68  LEU C CD1 1 
ATOM   1669 C CD2 . LEU B 2 68  ? -0.88400  23.30400 -20.70500 1.000 20.35116 ? 68  LEU C CD2 1 
ATOM   1670 N N   . HIS B 2 69  ? -5.49600  23.78700 -22.56300 1.000 19.51651 ? 69  HIS C N   1 
ATOM   1671 C CA  . HIS B 2 69  ? -6.81100  23.77200 -23.18700 1.000 21.21121 ? 69  HIS C CA  1 
ATOM   1672 C C   . HIS B 2 69  ? -6.87900  22.71900 -24.28000 1.000 20.54746 ? 69  HIS C C   1 
ATOM   1673 O O   . HIS B 2 69  ? -5.85500  22.28500 -24.81900 1.000 17.18950 ? 69  HIS C O   1 
ATOM   1674 C CB  . HIS B 2 69  ? -7.15500  25.11400 -23.85800 1.000 21.70479 ? 69  HIS C CB  1 
ATOM   1675 C CG  . HIS B 2 69  ? -7.26700  26.27300 -22.91900 1.000 26.89991 ? 69  HIS C CG  1 
ATOM   1676 N ND1 . HIS B 2 69  ? -7.28400  27.58100 -23.36300 1.000 27.18735 ? 69  HIS C ND1 1 
ATOM   1677 C CD2 . HIS B 2 69  ? -7.40100  26.32800 -21.57100 1.000 22.49244 ? 69  HIS C CD2 1 
ATOM   1678 C CE1 . HIS B 2 69  ? -7.40900  28.39100 -22.32400 1.000 24.94510 ? 69  HIS C CE1 1 
ATOM   1679 N NE2 . HIS B 2 69  ? -7.46700  27.65700 -21.22700 1.000 22.68967 ? 69  HIS C NE2 1 
ATOM   1680 N N   . ARG B 2 70  ? -8.10500  22.34700 -24.63500 1.000 20.09498 ? 70  ARG C N   1 
ATOM   1681 C CA  . ARG B 2 70  ? -8.32100  21.66600 -25.90300 1.000 19.50814 ? 70  ARG C CA  1 
ATOM   1682 C C   . ARG B 2 70  ? -8.21400  22.63200 -27.07300 1.000 19.88674 ? 70  ARG C C   1 
ATOM   1683 O O   . ARG B 2 70  ? -8.58900  23.80500 -26.97400 1.000 19.91382 ? 70  ARG C O   1 
ATOM   1684 C CB  . ARG B 2 70  ? -9.69800  20.98600 -25.97200 1.000 20.66661 ? 70  ARG C CB  1 
ATOM   1685 C CG  . ARG B 2 70  ? -9.96000  19.86100 -25.01600 1.000 23.30208 ? 70  ARG C CG  1 
ATOM   1686 C CD  . ARG B 2 70  ? -11.04700 20.25600 -24.08700 1.000 32.31434 ? 70  ARG C CD  1 
ATOM   1687 N NE  . ARG B 2 70  ? -12.34500 20.27200 -24.72700 1.000 31.08074 ? 70  ARG C NE  1 
ATOM   1688 C CZ  . ARG B 2 70  ? -13.43400 20.81400 -24.19700 1.000 35.05111 ? 70  ARG C CZ  1 
ATOM   1689 N NH1 . ARG B 2 70  ? -13.38100 21.54800 -23.09500 1.000 39.32062 ? 70  ARG C NH1 1 
ATOM   1690 N NH2 . ARG B 2 70  ? -14.60600 20.61700 -24.78500 1.000 33.17183 ? 70  ARG C NH2 1 
ATOM   1691 N N   . GLU B 2 71  ? -7.69900  22.10900 -28.19100 1.000 18.52734 ? 71  GLU C N   1 
ATOM   1692 C CA  . GLU B 2 71  ? -7.77200  22.79000 -29.47700 1.000 19.83088 ? 71  GLU C CA  1 
ATOM   1693 C C   . GLU B 2 71  ? -9.21900  23.03200 -29.87600 1.000 22.57574 ? 71  GLU C C   1 
ATOM   1694 O O   . GLU B 2 71  ? -10.12100 22.28400 -29.48800 1.000 21.70748 ? 71  GLU C O   1 
ATOM   1695 C CB  . GLU B 2 71  ? -7.10300  21.95700 -30.57000 1.000 20.33128 ? 71  GLU C CB  1 
ATOM   1696 C CG  . GLU B 2 71  ? -5.59300  21.92800 -30.50600 1.000 23.41325 ? 71  GLU C CG  1 
ATOM   1697 C CD  . GLU B 2 71  ? -4.95900  20.91700 -31.45900 1.000 28.13028 ? 71  GLU C CD  1 
ATOM   1698 O OE1 . GLU B 2 71  ? -5.69000  20.15600 -32.14000 1.000 27.14456 ? 71  GLU C OE1 1 
ATOM   1699 O OE2 . GLU B 2 71  ? -3.71500  20.91700 -31.53100 1.000 28.60295 ? 71  GLU C OE2 1 
ATOM   1700 N N   . GLY B 2 72  ? -9.42800  24.07900 -30.67400 1.000 19.04119 ? 72  GLY C N   1 
ATOM   1701 C CA  . GLY B 2 72  ? -10.73200 24.30500 -31.28400 1.000 22.06792 ? 72  GLY C CA  1 
ATOM   1702 C C   . GLY B 2 72  ? -11.38500 25.66100 -31.06800 1.000 20.61219 ? 72  GLY C C   1 
ATOM   1703 O O   . GLY B 2 72  ? -12.38500 25.97300 -31.72900 1.000 19.76414 ? 72  GLY C O   1 
ATOM   1704 N N   . ARG B 2 73  ? -10.84700 26.47900 -30.16400 1.000 21.11798 ? 73  ARG C N   1 
ATOM   1705 C CA  . ARG B 2 73  ? -11.39400 27.81200 -29.93500 1.000 19.23169 ? 73  ARG C CA  1 
ATOM   1706 C C   . ARG B 2 73  ? -10.69200 28.87700 -30.78100 1.000 22.78101 ? 73  ARG C C   1 
ATOM   1707 O O   . ARG B 2 73  ? -9.56800  28.69900 -31.25400 1.000 17.50614 ? 73  ARG C O   1 
ATOM   1708 C CB  . ARG B 2 73  ? -11.30600 28.18900 -28.46000 1.000 22.36858 ? 73  ARG C CB  1 
ATOM   1709 C CG  . ARG B 2 73  ? -12.09200 27.26600 -27.59900 1.000 25.45258 ? 73  ARG C CG  1 
ATOM   1710 C CD  . ARG B 2 73  ? -12.56600 27.97300 -26.34000 1.000 28.20546 ? 73  ARG C CD  1 
ATOM   1711 N NE  . ARG B 2 73  ? -13.26000 27.00900 -25.49900 1.000 28.13486 ? 73  ARG C NE  1 
ATOM   1712 C CZ  . ARG B 2 73  ? -12.62700 26.15300 -24.72300 1.000 29.65951 ? 73  ARG C CZ  1 
ATOM   1713 N NH1 . ARG B 2 73  ? -11.30700 26.17200 -24.61900 1.000 28.19649 ? 73  ARG C NH1 1 
ATOM   1714 N NH2 . ARG B 2 73  ? -13.32800 25.25500 -24.03000 1.000 35.27204 ? 73  ARG C NH2 1 
ATOM   1715 N N   . SER B 2 74  ? -11.38400 30.00200 -30.96100 1.000 19.57093 ? 74  SER C N   1 
ATOM   1716 C CA  . SER B 2 74  ? -10.87700 31.08000 -31.79800 1.000 18.14813 ? 74  SER C CA  1 
ATOM   1717 C C   . SER B 2 74  ? -9.82000  31.89400 -31.06700 1.000 22.24209 ? 74  SER C C   1 
ATOM   1718 O O   . SER B 2 74  ? -9.80000  31.97200 -29.83500 1.000 17.24142 ? 74  SER C O   1 
ATOM   1719 C CB  . SER B 2 74  ? -12.01700 31.99400 -32.24500 1.000 20.77447 ? 74  SER C CB  1 
ATOM   1720 O OG  . SER B 2 74  ? -12.47600 32.82600 -31.18600 1.000 20.71142 ? 74  SER C OG  1 
ATOM   1721 N N   . ALA B 2 75  ? -8.93300  32.50700 -31.85500 1.000 22.02680 ? 75  ALA C N   1 
ATOM   1722 C CA  . ALA B 2 75  ? -7.95000  33.43900 -31.30900 1.000 19.25390 ? 75  ALA C CA  1 
ATOM   1723 C C   . ALA B 2 75  ? -8.63100  34.58600 -30.57900 1.000 22.58703 ? 75  ALA C C   1 
ATOM   1724 O O   . ALA B 2 75  ? -8.12700  35.07700 -29.56300 1.000 18.84597 ? 75  ALA C O   1 
ATOM   1725 C CB  . ALA B 2 75  ? -7.06500  33.98200 -32.43400 1.000 16.84216 ? 75  ALA C CB  1 
ATOM   1726 N N   . ASP B 2 76  ? -9.78200  35.02200 -31.08600 1.000 18.85946 ? 76  ASP C N   1 
ATOM   1727 C CA  . ASP B 2 76  ? -10.52400 36.10300 -30.44700 1.000 24.31223 ? 76  ASP C CA  1 
ATOM   1728 C C   . ASP B 2 76  ? -10.94000 35.71600 -29.03200 1.000 22.45722 ? 76  ASP C C   1 
ATOM   1729 O O   . ASP B 2 76  ? -10.71400 36.47000 -28.07900 1.000 21.30949 ? 76  ASP C O   1 
ATOM   1730 C CB  . ASP B 2 76  ? -11.74400 36.44400 -31.30300 1.000 27.41389 ? 76  ASP C CB  1 
ATOM   1731 C CG  . ASP B 2 76  ? -12.24900 37.85300 -31.06400 1.000 40.45014 ? 76  ASP C CG  1 
ATOM   1732 O OD1 . ASP B 2 76  ? -12.54400 38.21000 -29.90900 1.000 35.64880 ? 76  ASP C OD1 1 
ATOM   1733 O OD2 . ASP B 2 76  ? -12.29800 38.62400 -32.05100 1.000 52.73133 ? 76  ASP C OD2 1 
ATOM   1734 N N   . LEU B 2 77  ? -11.54600 34.53000 -28.87800 1.000 19.23386 ? 77  LEU C N   1 
ATOM   1735 C CA  . LEU B 2 77  ? -12.00300 34.08600 -27.56300 1.000 22.42572 ? 77  LEU C CA  1 
ATOM   1736 C C   . LEU B 2 77  ? -10.83300 33.83800 -26.61900 1.000 18.16348 ? 77  LEU C C   1 
ATOM   1737 O O   . LEU B 2 77  ? -10.88900 34.18700 -25.43500 1.000 18.38427 ? 77  LEU C O   1 
ATOM   1738 C CB  . LEU B 2 77  ? -12.83400 32.81400 -27.69500 1.000 20.68186 ? 77  LEU C CB  1 
ATOM   1739 C CG  . LEU B 2 77  ? -13.66200 32.48100 -26.44900 1.000 27.42860 ? 77  LEU C CG  1 
ATOM   1740 C CD1 . LEU B 2 77  ? -14.57500 33.64800 -26.07100 1.000 28.80328 ? 77  LEU C CD1 1 
ATOM   1741 C CD2 . LEU B 2 77  ? -14.45900 31.19100 -26.62400 1.000 29.96204 ? 77  LEU C CD2 1 
ATOM   1742 N N   . LYS B 2 78  ? -9.77700  33.21300 -27.12200 1.000 18.90479 ? 78  LYS C N   1 
ATOM   1743 C CA  . LYS B 2 78  ? -8.60100  32.96300 -26.29800 1.000 19.16459 ? 78  LYS C CA  1 
ATOM   1744 C C   . LYS B 2 78  ? -8.01900  34.26900 -25.77700 1.000 18.01538 ? 78  LYS C C   1 
ATOM   1745 O O   . LYS B 2 78  ? -7.63900  34.37000 -24.60600 1.000 18.43425 ? 78  LYS C O   1 
ATOM   1746 C CB  . LYS B 2 78  ? -7.57100  32.17200 -27.10800 1.000 19.58434 ? 78  LYS C CB  1 
ATOM   1747 C CG  . LYS B 2 78  ? -7.91500  30.66200 -27.17400 1.000 22.28068 ? 78  LYS C CG  1 
ATOM   1748 C CD  . LYS B 2 78  ? -6.85500  29.83000 -27.91600 1.000 21.51414 ? 78  LYS C CD  1 
ATOM   1749 C CE  . LYS B 2 78  ? -6.90600  30.06400 -29.42300 1.000 22.34767 ? 78  LYS C CE  1 
ATOM   1750 N NZ  . LYS B 2 78  ? -5.97800  29.17200 -30.20700 1.000 23.13745 ? 78  LYS C NZ  1 
ATOM   1751 N N   . GLY B 2 79  ? -7.97600  35.29000 -26.63000 1.000 17.81922 ? 79  GLY C N   1 
ATOM   1752 C CA  . GLY B 2 79  ? -7.50300  36.58400 -26.19200 1.000 19.12838 ? 79  GLY C CA  1 
ATOM   1753 C C   . GLY B 2 79  ? -8.40500  37.21700 -25.15200 1.000 21.15481 ? 79  GLY C C   1 
ATOM   1754 O O   . GLY B 2 79  ? -7.92000  37.83400 -24.20300 1.000 19.74322 ? 79  GLY C O   1 
ATOM   1755 N N   . GLN B 2 80  ? -9.72800  37.10900 -25.33100 1.000 19.31718 ? 80  GLN C N   1 
ATOM   1756 C CA  . GLN B 2 80  ? -10.63900 37.61800 -24.30500 1.000 21.72335 ? 80  GLN C CA  1 
ATOM   1757 C C   . GLN B 2 80  ? -10.41900 36.90000 -22.98600 1.000 19.35717 ? 80  GLN C C   1 
ATOM   1758 O O   . GLN B 2 80  ? -10.48100 37.51500 -21.91400 1.000 20.30148 ? 80  GLN C O   1 
ATOM   1759 C CB  . GLN B 2 80  ? -12.09900 37.43700 -24.72200 1.000 20.64044 ? 80  GLN C CB  1 
ATOM   1760 C CG  . GLN B 2 80  ? -12.53400 38.19000 -25.96100 1.000 25.11618 ? 80  GLN C CG  1 
ATOM   1761 C CD  . GLN B 2 80  ? -14.00600 37.92800 -26.26700 1.000 29.11618 ? 80  GLN C CD  1 
ATOM   1762 O OE1 . GLN B 2 80  ? -14.81600 37.77600 -25.34800 1.000 34.32421 ? 80  GLN C OE1 1 
ATOM   1763 N NE2 . GLN B 2 80  ? -14.35100 37.84700 -27.54900 1.000 29.05049 ? 80  GLN C NE2 1 
ATOM   1764 N N   . LEU B 2 81  ? -10.17900 35.58800 -23.05100 1.000 20.45474 ? 81  LEU C N   1 
ATOM   1765 C CA  . LEU B 2 81  ? -10.05500 34.79200 -21.84000 1.000 19.52875 ? 81  LEU C CA  1 
ATOM   1766 C C   . LEU B 2 81  ? -8.76000  35.12100 -21.10900 1.000 19.93003 ? 81  LEU C C   1 
ATOM   1767 O O   . LEU B 2 81  ? -8.75600  35.27100 -19.88500 1.000 21.64338 ? 81  LEU C O   1 
ATOM   1768 C CB  . LEU B 2 81  ? -10.13400 33.30000 -22.19200 1.000 18.03668 ? 81  LEU C CB  1 
ATOM   1769 C CG  . LEU B 2 81  ? -9.97100  32.29500 -21.05600 1.000 21.26420 ? 81  LEU C CG  1 
ATOM   1770 C CD1 . LEU B 2 81  ? -10.92800 32.63200 -19.92300 1.000 17.92969 ? 81  LEU C CD1 1 
ATOM   1771 C CD2 . LEU B 2 81  ? -10.20500 30.87100 -21.55000 1.000 19.06540 ? 81  LEU C CD2 1 
ATOM   1772 N N   . ALA B 2 82  ? -7.65200  35.26200 -21.84200 1.000 19.42007 ? 82  ALA C N   1 
ATOM   1773 C CA  . ALA B 2 82  ? -6.40200  35.63200 -21.18200 1.000 18.90851 ? 82  ALA C CA  1 
ATOM   1774 C C   . ALA B 2 82  ? -6.51900  37.00500 -20.51600 1.000 21.86154 ? 82  ALA C C   1 
ATOM   1775 O O   . ALA B 2 82  ? -6.09600  37.18600 -19.36300 1.000 17.74088 ? 82  ALA C O   1 
ATOM   1776 C CB  . ALA B 2 82  ? -5.24900  35.60700 -22.18700 1.000 16.42264 ? 82  ALA C CB  1 
ATOM   1777 N N   . GLN B 2 83  ? -7.11600  37.97800 -21.21400 1.000 19.42952 ? 83  GLN C N   1 
ATOM   1778 C CA  . GLN B 2 83  ? -7.25500  39.31400 -20.63900 1.000 22.23886 ? 83  GLN C CA  1 
ATOM   1779 C C   . GLN B 2 83  ? -8.13600  39.28600 -19.39200 1.000 21.77666 ? 83  GLN C C   1 
ATOM   1780 O O   . GLN B 2 83  ? -7.83500  39.94700 -18.38700 1.000 20.89703 ? 83  GLN C O   1 
ATOM   1781 C CB  . GLN B 2 83  ? -7.81400  40.27900 -21.69400 1.000 20.59847 ? 83  GLN C CB  1 
ATOM   1782 C CG  . GLN B 2 83  ? -7.98200  41.72700 -21.20400 1.000 23.53939 ? 83  GLN C CG  1 
ATOM   1783 C CD  . GLN B 2 83  ? -6.65500  42.38200 -20.87900 1.000 27.76974 ? 83  GLN C CD  1 
ATOM   1784 O OE1 . GLN B 2 83  ? -6.38800  42.76000 -19.73400 1.000 30.70388 ? 83  GLN C OE1 1 
ATOM   1785 N NE2 . GLN B 2 83  ? -5.80100  42.48700 -21.87300 1.000 21.46658 ? 83  GLN C NE2 1 
ATOM   1786 N N   . ARG B 2 84  ? -9.20800  38.48500 -19.41200 1.000 21.79858 ? 84  ARG C N   1 
ATOM   1787 C CA  . ARG B 2 84  ? -10.06700 38.42100 -18.23400 1.000 21.24318 ? 84  ARG C CA  1 
ATOM   1788 C C   . ARG B 2 84  ? -9.36100  37.73100 -17.07500 1.000 20.74784 ? 84  ARG C C   1 
ATOM   1789 O O   . ARG B 2 84  ? -9.58100  38.10700 -15.91900 1.000 22.60195 ? 84  ARG C O   1 
ATOM   1790 C CB  . ARG B 2 84  ? -11.38200 37.72600 -18.58700 1.000 23.46772 ? 84  ARG C CB  1 
ATOM   1791 C CG  . ARG B 2 84  ? -12.56000 38.00700 -17.64300 1.000 29.66712 ? 84  ARG C CG  1 
ATOM   1792 C CD  . ARG B 2 84  ? -13.51300 36.84600 -17.63900 1.000 27.52957 ? 84  ARG C CD  1 
ATOM   1793 N NE  . ARG B 2 84  ? -14.17500 36.59600 -16.36300 1.000 31.78659 ? 84  ARG C NE  1 
ATOM   1794 C CZ  . ARG B 2 84  ? -15.48600 36.42300 -16.25000 1.000 31.83322 ? 84  ARG C CZ  1 
ATOM   1795 N NH1 . ARG B 2 84  ? -16.28100 36.48200 -17.31100 1.000 32.51185 ? 84  ARG C NH1 1 
ATOM   1796 N NH2 . ARG B 2 84  ? -16.00900 36.16200 -15.05400 1.000 26.81568 ? 84  ARG C NH2 1 
ATOM   1797 N N   . ILE B 2 85  ? -8.48000  36.76200 -17.34900 1.000 18.85101 ? 85  ILE C N   1 
ATOM   1798 C CA  . ILE B 2 85  ? -7.69300  36.17500 -16.26300 1.000 19.30903 ? 85  ILE C CA  1 
ATOM   1799 C C   . ILE B 2 85  ? -6.74200  37.21200 -15.67800 1.000 17.96556 ? 85  ILE C C   1 
ATOM   1800 O O   . ILE B 2 85  ? -6.63800  37.35900 -14.45800 1.000 19.10703 ? 85  ILE C O   1 
ATOM   1801 C CB  . ILE B 2 85  ? -6.94100  34.92100 -16.75200 1.000 20.18684 ? 85  ILE C CB  1 
ATOM   1802 C CG1 . ILE B 2 85  ? -7.91200  33.76800 -16.98500 1.000 23.13792 ? 85  ILE C CG1 1 
ATOM   1803 C CG2 . ILE B 2 85  ? -5.89200  34.47400 -15.71800 1.000 19.41989 ? 85  ILE C CG2 1 
ATOM   1804 C CD1 . ILE B 2 85  ? -7.25600  32.56000 -17.65000 1.000 20.69881 ? 85  ILE C CD1 1 
ATOM   1805 N N   . VAL B 2 86  ? -6.03500  37.94900 -16.53800 1.000 18.44703 ? 86  VAL C N   1 
ATOM   1806 C CA  . VAL B 2 86  ? -5.17200  39.03500 -16.06500 1.000 20.90131 ? 86  VAL C CA  1 
ATOM   1807 C C   . VAL B 2 86  ? -5.94600  39.99700 -15.16200 1.000 21.81940 ? 86  VAL C C   1 
ATOM   1808 O O   . VAL B 2 86  ? -5.51700  40.31400 -14.04500 1.000 20.93999 ? 86  VAL C O   1 
ATOM   1809 C CB  . VAL B 2 86  ? -4.54800  39.78000 -17.25700 1.000 21.69259 ? 86  VAL C CB  1 
ATOM   1810 C CG1 . VAL B 2 86  ? -3.83300  41.03300 -16.75900 1.000 28.11559 ? 86  VAL C CG1 1 
ATOM   1811 C CG2 . VAL B 2 86  ? -3.58900  38.85200 -18.04600 1.000 16.91156 ? 86  VAL C CG2 1 
ATOM   1812 N N   . ASP B 2 87  ? -7.08700  40.49300 -15.64200 1.000 20.66380 ? 87  ASP C N   1 
ATOM   1813 C CA  . ASP B 2 87  ? -7.84400  41.49100 -14.89300 1.000 20.65538 ? 87  ASP C CA  1 
ATOM   1814 C C   . ASP B 2 87  ? -8.39300  40.91400 -13.59100 1.000 19.76698 ? 87  ASP C C   1 
ATOM   1815 O O   . ASP B 2 87  ? -8.32800  41.55500 -12.53800 1.000 23.01765 ? 87  ASP C O   1 
ATOM   1816 C CB  . ASP B 2 87  ? -9.01000  42.02500 -15.73000 1.000 22.60381 ? 87  ASP C CB  1 
ATOM   1817 C CG  . ASP B 2 87  ? -8.57900  42.75600 -16.97900 1.000 26.52173 ? 87  ASP C CG  1 
ATOM   1818 O OD1 . ASP B 2 87  ? -7.40500  43.15700 -17.10100 1.000 26.76551 ? 87  ASP C OD1 1 
ATOM   1819 O OD2 . ASP B 2 87  ? -9.45700  42.95900 -17.84400 1.000 26.02284 ? 87  ASP C OD2 1 
ATOM   1820 N N   . ASP B 2 88  ? -9.00600  39.73300 -13.65400 1.000 21.04451 ? 88  ASP C N   1 
ATOM   1821 C CA  . ASP B 2 88  ? -9.70000  39.23100 -12.46700 1.000 22.02321 ? 88  ASP C CA  1 
ATOM   1822 C C   . ASP B 2 88  ? -8.74800  38.61600 -11.45800 1.000 20.98421 ? 88  ASP C C   1 
ATOM   1823 O O   . ASP B 2 88  ? -9.03700  38.64500 -10.25600 1.000 21.60505 ? 88  ASP C O   1 
ATOM   1824 C CB  . ASP B 2 88  ? -10.76900 38.20900 -12.85400 1.000 23.68196 ? 88  ASP C CB  1 
ATOM   1825 C CG  . ASP B 2 88  ? -11.87600 38.81400 -13.69700 1.000 25.26713 ? 88  ASP C CG  1 
ATOM   1826 O OD1 . ASP B 2 88  ? -11.81700 40.03200 -13.95200 1.000 24.42502 ? 88  ASP C OD1 1 
ATOM   1827 O OD2 . ASP B 2 88  ? -12.78300 38.06500 -14.13100 1.000 24.56087 ? 88  ASP C OD2 1 
ATOM   1828 N N   . VAL B 2 89  ? -7.61800  38.05400 -11.91300 1.000 20.56839 ? 89  VAL C N   1 
ATOM   1829 C CA  . VAL B 2 89  ? -6.59500  37.60400 -10.96800 1.000 20.92038 ? 89  VAL C CA  1 
ATOM   1830 C C   . VAL B 2 89  ? -5.91600  38.79200 -10.30000 1.000 21.95768 ? 89  VAL C C   1 
ATOM   1831 O O   . VAL B 2 89  ? -5.54300  38.72300 -9.11900  1.000 20.58857 ? 89  VAL C O   1 
ATOM   1832 C CB  . VAL B 2 89  ? -5.56900  36.69000 -11.66200 1.000 19.05274 ? 89  VAL C CB  1 
ATOM   1833 C CG1 . VAL B 2 89  ? -4.37400  36.42900 -10.74700 1.000 17.83197 ? 89  VAL C CG1 1 
ATOM   1834 C CG2 . VAL B 2 89  ? -6.20000  35.38200 -12.02600 1.000 15.82750 ? 89  VAL C CG2 1 
ATOM   1835 N N   . SER B 2 90  ? -5.74900  39.90100 -11.02100 1.000 20.70503 ? 90  SER C N   1 
ATOM   1836 C CA  . SER B 2 90  ? -5.18600  41.09600 -10.39600 1.000 22.08845 ? 90  SER C CA  1 
ATOM   1837 C C   . SER B 2 90  ? -6.04400  41.55300 -9.22800  1.000 26.34970 ? 90  SER C C   1 
ATOM   1838 O O   . SER B 2 90  ? -5.52700  41.88400 -8.15500  1.000 27.52697 ? 90  SER C O   1 
ATOM   1839 C CB  . SER B 2 90  ? -5.05800  42.23000 -11.41100 1.000 26.17786 ? 90  SER C CB  1 
ATOM   1840 O OG  . SER B 2 90  ? -4.51300  43.37200 -10.75800 1.000 28.02132 ? 90  SER C OG  1 
ATOM   1841 N N   . VAL B 2 91  ? -7.36300  41.58200 -9.42800  1.000 23.73435 ? 91  VAL C N   1 
ATOM   1842 C CA  . VAL B 2 91  ? -8.28100  41.97400 -8.36200  1.000 22.83621 ? 91  VAL C CA  1 
ATOM   1843 C C   . VAL B 2 91  ? -8.26600  40.94200 -7.24400  1.000 23.71305 ? 91  VAL C C   1 
ATOM   1844 O O   . VAL B 2 91  ? -8.15800  41.28600 -6.06200  1.000 24.09301 ? 91  VAL C O   1 
ATOM   1845 C CB  . VAL B 2 91  ? -9.70000  42.18300 -8.92900  1.000 25.05490 ? 91  VAL C CB  1 
ATOM   1846 C CG1 . VAL B 2 91  ? -10.76300 42.26600 -7.80200  1.000 26.81899 ? 91  VAL C CG1 1 
ATOM   1847 C CG2 . VAL B 2 91  ? -9.74400  43.43800 -9.78100  1.000 29.40874 ? 91  VAL C CG2 1 
ATOM   1848 N N   . ALA B 2 92  ? -8.35400  39.66000 -7.59600  1.000 22.14046 ? 92  ALA C N   1 
ATOM   1849 C CA  . ALA B 2 92  ? -8.45800  38.63000 -6.56600  1.000 23.02137 ? 92  ALA C CA  1 
ATOM   1850 C C   . ALA B 2 92  ? -7.19000  38.53600 -5.71600  1.000 25.63654 ? 92  ALA C C   1 
ATOM   1851 O O   . ALA B 2 92  ? -7.26400  38.35700 -4.49200  1.000 25.04533 ? 92  ALA C O   1 
ATOM   1852 C CB  . ALA B 2 92  ? -8.77500  37.28600 -7.21100  1.000 22.60043 ? 92  ALA C CB  1 
ATOM   1853 N N   . ALA B 2 93  ? -6.02000  38.63300 -6.33600  1.000 21.97250 ? 93  ALA C N   1 
ATOM   1854 C CA  . ALA B 2 93  ? -4.78000  38.52900 -5.57100  1.000 25.04758 ? 93  ALA C CA  1 
ATOM   1855 C C   . ALA B 2 93  ? -4.27000  39.87100 -5.06300  1.000 23.65278 ? 93  ALA C C   1 
ATOM   1856 O O   . ALA B 2 93  ? -3.26100  39.89900 -4.34800  1.000 28.31041 ? 93  ALA C O   1 
ATOM   1857 C CB  . ALA B 2 93  ? -3.69100  37.85100 -6.40300  1.000 23.60449 ? 93  ALA C CB  1 
ATOM   1858 N N   . GLU B 2 94  ? -4.93700  40.96900 -5.40300  1.000 19.59262 ? 94  GLU C N   1 
ATOM   1859 C CA  . GLU B 2 94  ? -4.50400  42.32200 -5.04100  1.000 27.58352 ? 94  GLU C CA  1 
ATOM   1860 C C   . GLU B 2 94  ? -3.07000  42.56100 -5.51800  1.000 26.40917 ? 94  GLU C C   1 
ATOM   1861 O O   . GLU B 2 94  ? -2.16000  42.90700 -4.76100  1.000 24.50504 ? 94  GLU C O   1 
ATOM   1862 C CB  . GLU B 2 94  ? -4.64900  42.57700 -3.53400  1.000 28.13590 ? 94  GLU C CB  1 
ATOM   1863 C CG  . GLU B 2 94  ? -6.10000  42.63600 -3.06100  1.000 31.19912 ? 94  GLU C CG  1 
ATOM   1864 C CD  . GLU B 2 94  ? -6.23200  42.58600 -1.54500  1.000 34.27156 ? 94  GLU C CD  1 
ATOM   1865 O OE1 . GLU B 2 94  ? -5.58000  43.40400 -0.87100  1.000 41.18203 ? 94  GLU C OE1 1 
ATOM   1866 O OE2 . GLU B 2 94  ? -6.98500  41.73700 -1.02500  1.000 39.43388 ? 94  GLU C OE2 1 
ATOM   1867 N N   . ILE B 2 95  ? -2.88900  42.36600 -6.81700  1.000 26.41542 ? 95  ILE C N   1 
ATOM   1868 C CA  . ILE B 2 95  ? -1.57000  42.34200 -7.43000  1.000 26.56388 ? 95  ILE C CA  1 
ATOM   1869 C C   . ILE B 2 95  ? -1.64200  43.13600 -8.73300  1.000 28.90540 ? 95  ILE C C   1 
ATOM   1870 O O   . ILE B 2 95  ? -2.60800  42.99800 -9.49000  1.000 26.01742 ? 95  ILE C O   1 
ATOM   1871 C CB  . ILE B 2 95  ? -1.15900  40.88100 -7.66700  1.000 27.20356 ? 95  ILE C CB  1 
ATOM   1872 C CG1 . ILE B 2 95  ? 0.12400   40.78800 -8.43800  1.000 28.27185 ? 95  ILE C CG1 1 
ATOM   1873 C CG2 . ILE B 2 95  ? -2.21000  40.16500 -8.51200  1.000 29.52648 ? 95  ILE C CG2 1 
ATOM   1874 C CD1 . ILE B 2 95  ? 0.84100   39.63200 -7.98600  1.000 36.75347 ? 95  ILE C CD1 1 
ATOM   1875 N N   . ASP B 2 96  ? -0.64200  43.98900 -8.98600  1.000 26.59497 ? 96  ASP C N   1 
ATOM   1876 C CA  . ASP B 2 96  ? -0.61700  44.76900 -10.22500 1.000 25.44827 ? 96  ASP C CA  1 
ATOM   1877 C C   . ASP B 2 96  ? -0.56900  43.84100 -11.43000 1.000 23.77965 ? 96  ASP C C   1 
ATOM   1878 O O   . ASP B 2 96  ? 0.08000   42.79400 -11.39500 1.000 21.64269 ? 96  ASP C O   1 
ATOM   1879 C CB  . ASP B 2 96  ? 0.59400   45.71100 -10.24800 1.000 27.88357 ? 96  ASP C CB  1 
ATOM   1880 C CG  . ASP B 2 96  ? 0.47000   46.81900 -11.29500 1.000 35.65129 ? 96  ASP C CG  1 
ATOM   1881 O OD1 . ASP B 2 96  ? 0.54100   46.54200 -12.51600 1.000 35.06415 ? 96  ASP C OD1 1 
ATOM   1882 O OD2 . ASP B 2 96  ? 0.30100   47.99400 -10.89600 1.000 42.30823 ? 96  ASP C OD2 1 
ATOM   1883 N N   . ARG B 2 97  ? -1.26400  44.23000 -12.51000 1.000 24.28424 ? 97  ARG C N   1 
ATOM   1884 C CA  . ARG B 2 97  ? -1.30700  43.37800 -13.69500 1.000 21.57583 ? 97  ARG C CA  1 
ATOM   1885 C C   . ARG B 2 97  ? 0.07800   43.15700 -14.30100 1.000 23.47795 ? 97  ARG C C   1 
ATOM   1886 O O   . ARG B 2 97  ? 0.31200   42.13700 -14.96000 1.000 20.35565 ? 97  ARG C O   1 
ATOM   1887 C CB  . ARG B 2 97  ? -2.22500  43.97100 -14.76300 1.000 25.98200 ? 97  ARG C CB  1 
ATOM   1888 C CG  . ARG B 2 97  ? -3.70900  43.97700 -14.45400 1.000 29.10546 ? 97  ARG C CG  1 
ATOM   1889 C CD  . ARG B 2 97  ? -4.37100  45.12000 -15.23500 1.000 33.47050 ? 97  ARG C CD  1 
ATOM   1890 N NE  . ARG B 2 97  ? -5.80800  45.27600 -15.01900 1.000 38.46888 ? 97  ARG C NE  1 
ATOM   1891 C CZ  . ARG B 2 97  ? -6.41300  45.36100 -13.83800 1.000 38.87185 ? 97  ARG C CZ  1 
ATOM   1892 N NH1 . ARG B 2 97  ? -5.72900  45.49300 -12.71000 1.000 41.32503 ? 97  ARG C NH1 1 
ATOM   1893 N NH2 . ARG B 2 97  ? -7.74300  45.33300 -13.78700 1.000 39.70241 ? 97  ARG C NH2 1 
ATOM   1894 N N   . LYS B 2 98  ? 0.99700   44.10900 -14.11300 1.000 22.33714 ? 98  LYS C N   1 
ATOM   1895 C CA  . LYS B 2 98  ? 2.35000   43.97800 -14.64600 1.000 22.52128 ? 98  LYS C CA  1 
ATOM   1896 C C   . LYS B 2 98  ? 3.07200   42.75100 -14.08500 1.000 20.63280 ? 98  LYS C C   1 
ATOM   1897 O O   . LYS B 2 98  ? 4.08800   42.32800 -14.64100 1.000 18.94439 ? 98  LYS C O   1 
ATOM   1898 C CB  . LYS B 2 98  ? 3.13100   45.26200 -14.33600 1.000 24.75937 ? 98  LYS C CB  1 
ATOM   1899 C CG  . LYS B 2 98  ? 3.54500   45.34700 -12.84800 1.000 29.30222 ? 98  LYS C CG  1 
ATOM   1900 C CD  . LYS B 2 98  ? 3.96800   46.75400 -12.40600 1.000 33.99925 ? 98  LYS C CD  1 
ATOM   1901 C CE  . LYS B 2 98  ? 4.01800   46.86900 -10.88000 1.000 40.54904 ? 98  LYS C CE  1 
ATOM   1902 N NZ  . LYS B 2 98  ? 4.92600   47.97300 -10.45300 1.000 38.42310 ? 98  LYS C NZ  1 
ATOM   1903 N N   . HIS B 2 99  ? 2.57200   42.17300 -12.99600 1.000 18.10834 ? 99  HIS C N   1 
ATOM   1904 C CA  . HIS B 2 99  ? 3.15000   40.97600 -12.40800 1.000 19.20569 ? 99  HIS C CA  1 
ATOM   1905 C C   . HIS B 2 99  ? 2.57800   39.68300 -12.97700 1.000 21.27316 ? 99  HIS C C   1 
ATOM   1906 O O   . HIS B 2 99  ? 3.00800   38.60200 -12.56900 1.000 19.50821 ? 99  HIS C O   1 
ATOM   1907 C CB  . HIS B 2 99  ? 2.93500   40.97000 -10.89000 1.000 22.35534 ? 99  HIS C CB  1 
ATOM   1908 C CG  . HIS B 2 99  ? 3.72200   42.00700 -10.15800 1.000 25.21658 ? 99  HIS C CG  1 
ATOM   1909 N ND1 . HIS B 2 99  ? 5.09800   41.98400 -10.08200 1.000 28.46701 ? 99  HIS C ND1 1 
ATOM   1910 C CD2 . HIS B 2 99  ? 3.32300   43.08500 -9.44100  1.000 29.95164 ? 99  HIS C CD2 1 
ATOM   1911 C CE1 . HIS B 2 99  ? 5.51400   43.00900 -9.35800  1.000 30.74439 ? 99  HIS C CE1 1 
ATOM   1912 N NE2 . HIS B 2 99  ? 4.45700   43.69100 -8.95500  1.000 29.38564 ? 99  HIS C NE2 1 
ATOM   1913 N N   . ILE B 2 100 ? 1.64100   39.74800 -13.91600 1.000 18.32235 ? 100 ILE C N   1 
ATOM   1914 C CA  . ILE B 2 100 ? 0.85700   38.58000 -14.29300 1.000 18.09550 ? 100 ILE C CA  1 
ATOM   1915 C C   . ILE B 2 100 ? 1.21400   38.18000 -15.72200 1.000 18.67672 ? 100 ILE C C   1 
ATOM   1916 O O   . ILE B 2 100 ? 1.07900   38.97700 -16.66300 1.000 20.48636 ? 100 ILE C O   1 
ATOM   1917 C CB  . ILE B 2 100 ? -0.65000  38.83600 -14.13400 1.000 20.01438 ? 100 ILE C CB  1 
ATOM   1918 C CG1 . ILE B 2 100 ? -0.95800  39.19800 -12.68100 1.000 19.40083 ? 100 ILE C CG1 1 
ATOM   1919 C CG2 . ILE B 2 100 ? -1.45600  37.61300 -14.55700 1.000 16.80139 ? 100 ILE C CG2 1 
ATOM   1920 C CD1 . ILE B 2 100 ? -2.37700  39.71200 -12.46200 1.000 22.97461 ? 100 ILE C CD1 1 
ATOM   1921 N N   . TRP B 2 101 ? 1.65900   36.94500 -15.87300 1.000 17.96320 ? 101 TRP C N   1 
ATOM   1922 C CA  . TRP B 2 101 ? 1.90900   36.32300 -17.16200 1.000 17.78403 ? 101 TRP C CA  1 
ATOM   1923 C C   . TRP B 2 101 ? 0.91900   35.18100 -17.37400 1.000 18.44850 ? 101 TRP C C   1 
ATOM   1924 O O   . TRP B 2 101 ? 0.60500   34.43400 -16.43500 1.000 18.53434 ? 101 TRP C O   1 
ATOM   1925 C CB  . TRP B 2 101 ? 3.33900   35.78000 -17.23900 1.000 17.89678 ? 101 TRP C CB  1 
ATOM   1926 C CG  . TRP B 2 101 ? 4.43700   36.78400 -16.97500 1.000 18.25266 ? 101 TRP C CG  1 
ATOM   1927 C CD1 . TRP B 2 101 ? 4.46900   37.77300 -16.00300 1.000 19.18511 ? 101 TRP C CD1 1 
ATOM   1928 C CD2 . TRP B 2 101 ? 5.67700   36.87100 -17.67200 1.000 19.77670 ? 101 TRP C CD2 1 
ATOM   1929 N NE1 . TRP B 2 101 ? 5.65400   38.47400 -16.08800 1.000 22.33235 ? 101 TRP C NE1 1 
ATOM   1930 C CE2 . TRP B 2 101 ? 6.41300   37.93600 -17.09700 1.000 20.62523 ? 101 TRP C CE2 1 
ATOM   1931 C CE3 . TRP B 2 101 ? 6.24500   36.14600 -18.72500 1.000 20.64204 ? 101 TRP C CE3 1 
ATOM   1932 C CZ2 . TRP B 2 101 ? 7.67800   38.29000 -17.54300 1.000 20.68865 ? 101 TRP C CZ2 1 
ATOM   1933 C CZ3 . TRP B 2 101 ? 7.51400   36.50700 -19.17600 1.000 21.39501 ? 101 TRP C CZ3 1 
ATOM   1934 C CH2 . TRP B 2 101 ? 8.21300   37.56500 -18.58500 1.000 21.91967 ? 101 TRP C CH2 1 
ATOM   1935 N N   . VAL B 2 102 ? 0.42900   35.03400 -18.60600 1.000 17.30759 ? 102 VAL C N   1 
ATOM   1936 C CA  . VAL B 2 102 ? -0.62300  34.06500 -18.91600 1.000 16.96473 ? 102 VAL C CA  1 
ATOM   1937 C C   . VAL B 2 102 ? -0.34300  33.45200 -20.28000 1.000 16.71654 ? 102 VAL C C   1 
ATOM   1938 O O   . VAL B 2 102 ? -0.37900  34.16100 -21.29200 1.000 17.59561 ? 102 VAL C O   1 
ATOM   1939 C CB  . VAL B 2 102 ? -2.02500  34.69900 -18.92200 1.000 14.99022 ? 102 VAL C CB  1 
ATOM   1940 C CG1 . VAL B 2 102 ? -3.05300  33.63000 -19.18300 1.000 19.24846 ? 102 VAL C CG1 1 
ATOM   1941 C CG2 . VAL B 2 102 ? -2.32000  35.36900 -17.59400 1.000 17.34812 ? 102 VAL C CG2 1 
ATOM   1942 N N   . TYR B 2 103 ? -0.11900  32.13700 -20.31500 1.000 17.15042 ? 103 TYR C N   1 
ATOM   1943 C CA  . TYR B 2 103 ? 0.13000   31.39200 -21.55100 1.000 18.42733 ? 103 TYR C CA  1 
ATOM   1944 C C   . TYR B 2 103 ? -0.88500  30.27400 -21.72000 1.000 19.16119 ? 103 TYR C C   1 
ATOM   1945 O O   . TYR B 2 103 ? -1.06600  29.46000 -20.80500 1.000 18.73243 ? 103 TYR C O   1 
ATOM   1946 C CB  . TYR B 2 103 ? 1.52500   30.74500 -21.54600 1.000 15.34692 ? 103 TYR C CB  1 
ATOM   1947 C CG  . TYR B 2 103 ? 2.70300   31.65900 -21.71600 1.000 16.99974 ? 103 TYR C CG  1 
ATOM   1948 C CD1 . TYR B 2 103 ? 2.56400   33.03700 -21.74700 1.000 17.41674 ? 103 TYR C CD1 1 
ATOM   1949 C CD2 . TYR B 2 103 ? 3.97900   31.13000 -21.82400 1.000 16.47809 ? 103 TYR C CD2 1 
ATOM   1950 C CE1 . TYR B 2 103 ? 3.67700   33.85800 -21.88900 1.000 19.62273 ? 103 TYR C CE1 1 
ATOM   1951 C CE2 . TYR B 2 103 ? 5.08200   31.93700 -21.99700 1.000 16.77747 ? 103 TYR C CE2 1 
ATOM   1952 C CZ  . TYR B 2 103 ? 4.92900   33.29500 -22.01300 1.000 19.20478 ? 103 TYR C CZ  1 
ATOM   1953 O OH  . TYR B 2 103 ? 6.05400   34.08200 -22.15000 1.000 20.82191 ? 103 TYR C OH  1 
ATOM   1954 N N   . PHE B 2 104 ? -1.49700  30.18800 -22.90300 1.000 15.79273 ? 104 PHE C N   1 
ATOM   1955 C CA  . PHE B 2 104 ? -2.42000  29.10300 -23.21600 1.000 19.48858 ? 104 PHE C CA  1 
ATOM   1956 C C   . PHE B 2 104 ? -1.75800  28.09800 -24.15600 1.000 18.67388 ? 104 PHE C C   1 
ATOM   1957 O O   . PHE B 2 104 ? -1.25800  28.47100 -25.22200 1.000 18.66636 ? 104 PHE C O   1 
ATOM   1958 C CB  . PHE B 2 104 ? -3.71300  29.62600 -23.85100 1.000 19.61101 ? 104 PHE C CB  1 
ATOM   1959 C CG  . PHE B 2 104 ? -4.57100  30.46000 -22.93100 1.000 20.51856 ? 104 PHE C CG  1 
ATOM   1960 C CD1 . PHE B 2 104 ? -4.37400  30.46000 -21.56100 1.000 22.84615 ? 104 PHE C CD1 1 
ATOM   1961 C CD2 . PHE B 2 104 ? -5.60900  31.22400 -23.45200 1.000 20.12833 ? 104 PHE C CD2 1 
ATOM   1962 C CE1 . PHE B 2 104 ? -5.18100  31.23400 -20.72600 1.000 19.46431 ? 104 PHE C CE1 1 
ATOM   1963 C CE2 . PHE B 2 104 ? -6.40900  31.99600 -22.62600 1.000 21.74553 ? 104 PHE C CE2 1 
ATOM   1964 C CZ  . PHE B 2 104 ? -6.18200  32.00300 -21.25900 1.000 19.83888 ? 104 PHE C CZ  1 
ATOM   1965 N N   . GLY B 2 105 ? -1.75300  26.83100 -23.74800 1.000 18.53926 ? 105 GLY C N   1 
ATOM   1966 C CA  . GLY B 2 105 ? -1.32300  25.72600 -24.58700 1.000 20.99121 ? 105 GLY C CA  1 
ATOM   1967 C C   . GLY B 2 105 ? -2.53800  24.90700 -24.98100 1.000 21.02950 ? 105 GLY C C   1 
ATOM   1968 O O   . GLY B 2 105 ? -3.50900  24.82100 -24.22800 1.000 21.82269 ? 105 GLY C O   1 
ATOM   1969 N N   . GLU B 2 106 ? -2.50400  24.33800 -26.18600 1.000 17.08548 ? 106 GLU C N   1 
ATOM   1970 C CA  . GLU B 2 106 ? -3.64800  23.62300 -26.74400 1.000 18.64613 ? 106 GLU C CA  1 
ATOM   1971 C C   . GLU B 2 106 ? -3.23000  22.25400 -27.25200 1.000 20.07108 ? 106 GLU C C   1 
ATOM   1972 O O   . GLU B 2 106 ? -2.17700  22.11900 -27.88000 1.000 20.16849 ? 106 GLU C O   1 
ATOM   1973 C CB  . GLU B 2 106 ? -4.26400  24.38100 -27.92200 1.000 18.29833 ? 106 GLU C CB  1 
ATOM   1974 C CG  . GLU B 2 106 ? -4.78800  25.74500 -27.59500 1.000 22.68111 ? 106 GLU C CG  1 
ATOM   1975 C CD  . GLU B 2 106 ? -4.96700  26.56800 -28.85700 1.000 23.83829 ? 106 GLU C CD  1 
ATOM   1976 O OE1 . GLU B 2 106 ? -3.93800  27.02400 -29.40500 1.000 23.57422 ? 106 GLU C OE1 1 
ATOM   1977 O OE2 . GLU B 2 106 ? -6.13300  26.74600 -29.30600 1.000 23.64424 ? 106 GLU C OE2 1 
ATOM   1978 N N   . MET B 2 107 ? -4.05500  21.24900 -27.00000 1.000 17.65932 ? 107 MET C N   1 
ATOM   1979 C CA  . MET B 2 107 ? -3.84200  19.90500 -27.51800 1.000 18.60370 ? 107 MET C CA  1 
ATOM   1980 C C   . MET B 2 107 ? -5.16100  19.32100 -28.01100 1.000 20.51975 ? 107 MET C C   1 
ATOM   1981 O O   . MET B 2 107 ? -6.23400  19.78600 -27.62500 1.000 19.42766 ? 107 MET C O   1 
ATOM   1982 C CB  . MET B 2 107 ? -3.20700  18.98400 -26.46200 1.000 20.78444 ? 107 MET C CB  1 
ATOM   1983 C CG  . MET B 2 107 ? -2.14600  19.66800 -25.62200 1.000 19.22489 ? 107 MET C CG  1 
ATOM   1984 S SD  . MET B 2 107 ? -2.11100  19.08800 -23.92400 1.000 24.79658 ? 107 MET C SD  1 
ATOM   1985 C CE  . MET B 2 107 ? -3.03900  20.43000 -23.19400 1.000 21.27072 ? 107 MET C CE  1 
ATOM   1986 N N   . PRO B 2 108 ? -5.10400  18.33200 -28.90700 1.000 23.30469 ? 108 PRO C N   1 
ATOM   1987 C CA  . PRO B 2 108 ? -6.33300  17.65000 -29.33600 1.000 20.82304 ? 108 PRO C CA  1 
ATOM   1988 C C   . PRO B 2 108 ? -7.07300  17.05900 -28.14900 1.000 24.36333 ? 108 PRO C C   1 
ATOM   1989 O O   . PRO B 2 108 ? -6.46900  16.44300 -27.27600 1.000 20.93790 ? 108 PRO C O   1 
ATOM   1990 C CB  . PRO B 2 108 ? -5.81400  16.54700 -30.26400 1.000 21.91018 ? 108 PRO C CB  1 
ATOM   1991 C CG  . PRO B 2 108 ? -4.50300  17.04900 -30.75100 1.000 25.60096 ? 108 PRO C CG  1 
ATOM   1992 C CD  . PRO B 2 108 ? -3.91600  17.79800 -29.58600 1.000 22.62848 ? 108 PRO C CD  1 
ATOM   1993 N N   . ALA B 2 109 ? -8.39900  17.21800 -28.14000 1.000 20.20211 ? 109 ALA C N   1 
ATOM   1994 C CA  . ALA B 2 109 ? -9.18900  16.66200 -27.04500 1.000 21.96846 ? 109 ALA C CA  1 
ATOM   1995 C C   . ALA B 2 109 ? -8.99300  15.15600 -26.91600 1.000 23.28373 ? 109 ALA C C   1 
ATOM   1996 O O   . ALA B 2 109 ? -9.15700  14.60600 -25.81600 1.000 23.07561 ? 109 ALA C O   1 
ATOM   1997 C CB  . ALA B 2 109 ? -10.66800 16.98700 -27.24600 1.000 20.28521 ? 109 ALA C CB  1 
ATOM   1998 N N   . GLN B 2 110 ? -8.61800  14.49000 -28.01100 1.000 22.04717 ? 110 GLN C N   1 
ATOM   1999 C CA  . GLN B 2 110 ? -8.43100  13.04900 -28.04700 1.000 22.13274 ? 110 GLN C CA  1 
ATOM   2000 C C   . GLN B 2 110 ? -7.23000  12.57000 -27.23600 1.000 22.89148 ? 110 GLN C C   1 
ATOM   2001 O O   . GLN B 2 110 ? -7.12800  11.36500 -26.97500 1.000 20.29736 ? 110 GLN C O   1 
ATOM   2002 C CB  . GLN B 2 110 ? -8.29300  12.61500 -29.50200 1.000 25.38601 ? 110 GLN C CB  1 
ATOM   2003 C CG  . GLN B 2 110 ? -9.56400  12.01500 -30.03800 1.000 30.13009 ? 110 GLN C CG  1 
ATOM   2004 C CD  . GLN B 2 110 ? -9.53300  11.94700 -31.54600 1.000 38.56379 ? 110 GLN C CD  1 
ATOM   2005 O OE1 . GLN B 2 110 ? -9.69200  10.88100 -32.13800 1.000 45.62461 ? 110 GLN C OE1 1 
ATOM   2006 N NE2 . GLN B 2 110 ? -9.30000  13.10100 -32.18400 1.000 40.09791 ? 110 GLN C NE2 1 
ATOM   2007 N N   . GLN B 2 111 ? -6.32900  13.46000 -26.81500 1.000 22.24329 ? 111 GLN C N   1 
ATOM   2008 C CA  . GLN B 2 111 ? -5.22000  13.06600 -25.95000 1.000 19.80263 ? 111 GLN C CA  1 
ATOM   2009 C C   . GLN B 2 111 ? -5.28400  13.79800 -24.61500 1.000 21.18394 ? 111 GLN C C   1 
ATOM   2010 O O   . GLN B 2 111 ? -4.25100  14.21200 -24.05900 1.000 18.87733 ? 111 GLN C O   1 
ATOM   2011 C CB  . GLN B 2 111 ? -3.87400  13.31000 -26.63000 1.000 20.06149 ? 111 GLN C CB  1 
ATOM   2012 C CG  . GLN B 2 111 ? -3.57900  14.77800 -26.99300 1.000 22.63624 ? 111 GLN C CG  1 
ATOM   2013 C CD  . GLN B 2 111 ? -2.59900  14.90000 -28.15300 1.000 24.04967 ? 111 GLN C CD  1 
ATOM   2014 O OE1 . GLN B 2 111 ? -2.86400  14.39900 -29.24500 1.000 23.95084 ? 111 GLN C OE1 1 
ATOM   2015 N NE2 . GLN B 2 111 ? -1.45100  15.53300 -27.91300 1.000 23.76044 ? 111 GLN C NE2 1 
ATOM   2016 N N   . MET B 2 112 ? -6.49800  13.95000 -24.07700 1.000 19.37970 ? 112 MET C N   1 
ATOM   2017 C CA  . MET B 2 112 ? -6.76900  14.83900 -22.93800 1.000 20.09237 ? 112 MET C CA  1 
ATOM   2018 C C   . MET B 2 112 ? -7.81700  14.13800 -22.08100 1.000 18.91718 ? 112 MET C C   1 
ATOM   2019 O O   . MET B 2 112 ? -8.90900  13.82900 -22.57300 1.000 20.11326 ? 112 MET C O   1 
ATOM   2020 C CB  . MET B 2 112 ? -7.32500  16.14900 -23.49700 1.000 20.21937 ? 112 MET C CB  1 
ATOM   2021 C CG  . MET B 2 112 ? -6.25100  17.06800 -24.08500 1.000 22.17865 ? 112 MET C CG  1 
ATOM   2022 S SD  . MET B 2 112 ? -6.65100  18.81500 -24.24100 1.000 21.78889 ? 112 MET C SD  1 
ATOM   2023 C CE  . MET B 2 112 ? -6.69500  19.51300 -22.56700 1.000 19.93053 ? 112 MET C CE  1 
ATOM   2024 N N   . VAL B 2 113 ? -7.50200  13.87800 -20.81000 1.000 18.26556 ? 113 VAL C N   1 
ATOM   2025 C CA  . VAL B 2 113 ? -8.34500  13.07700 -19.92800 1.000 18.13105 ? 113 VAL C CA  1 
ATOM   2026 C C   . VAL B 2 113 ? -8.59800  13.89100 -18.65500 1.000 17.51472 ? 113 VAL C C   1 
ATOM   2027 O O   . VAL B 2 113 ? -7.64200  14.29500 -17.98500 1.000 17.83975 ? 113 VAL C O   1 
ATOM   2028 C CB  . VAL B 2 113 ? -7.68400  11.72100 -19.59600 1.000 19.69368 ? 113 VAL C CB  1 
ATOM   2029 C CG1 . VAL B 2 113 ? -8.37500  11.03200 -18.42600 1.000 23.27863 ? 113 VAL C CG1 1 
ATOM   2030 C CG2 . VAL B 2 113 ? -7.67500  10.78800 -20.80400 1.000 21.44763 ? 113 VAL C CG2 1 
ATOM   2031 N N   . ASP B 2 114 ? -9.87200  14.15800 -18.34800 1.000 19.70812 ? 114 ASP C N   1 
ATOM   2032 C CA  . ASP B 2 114 ? -10.30700 14.72100 -17.06400 1.000 19.91205 ? 114 ASP C CA  1 
ATOM   2033 C C   . ASP B 2 114 ? -11.14500 13.69200 -16.31300 1.000 20.97811 ? 114 ASP C C   1 
ATOM   2034 O O   . ASP B 2 114 ? -11.99600 13.03400 -16.91300 1.000 20.59969 ? 114 ASP C O   1 
ATOM   2035 C CB  . ASP B 2 114 ? -11.20200 15.96000 -17.22100 1.000 20.17001 ? 114 ASP C CB  1 
ATOM   2036 C CG  . ASP B 2 114 ? -10.52700 17.13300 -17.87900 1.000 21.03382 ? 114 ASP C CG  1 
ATOM   2037 O OD1 . ASP B 2 114 ? -9.34600  17.05200 -18.27500 1.000 19.41330 ? 114 ASP C OD1 1 
ATOM   2038 O OD2 . ASP B 2 114 ? -11.19900 18.18100 -17.95400 1.000 21.56997 ? 114 ASP C OD2 1 
ATOM   2039 N N   . TYR B 2 115 ? -10.94400 13.58400 -15.00000 1.000 21.24858 ? 115 TYR C N   1 
ATOM   2040 C CA  . TYR B 2 115 ? -11.73300 12.65900 -14.17700 1.000 23.99963 ? 115 TYR C CA  1 
ATOM   2041 C C   . TYR B 2 115 ? -11.69100 11.24200 -14.75300 1.000 22.13871 ? 115 TYR C C   1 
ATOM   2042 O O   . TYR B 2 115 ? -12.68300 10.50900 -14.73200 1.000 23.89458 ? 115 TYR C O   1 
ATOM   2043 C CB  . TYR B 2 115 ? -13.18700 13.13000 -14.04100 1.000 21.82296 ? 115 TYR C CB  1 
ATOM   2044 C CG  . TYR B 2 115 ? -13.41700 14.43600 -13.31600 1.000 21.34797 ? 115 TYR C CG  1 
ATOM   2045 C CD1 . TYR B 2 115 ? -13.55600 14.45900 -11.93200 1.000 26.43856 ? 115 TYR C CD1 1 
ATOM   2046 C CD2 . TYR B 2 115 ? -13.55100 15.63300 -14.01000 1.000 20.32625 ? 115 TYR C CD2 1 
ATOM   2047 C CE1 . TYR B 2 115 ? -13.78200 15.64700 -11.24800 1.000 26.84900 ? 115 TYR C CE1 1 
ATOM   2048 C CE2 . TYR B 2 115 ? -13.78300 16.83600 -13.33800 1.000 22.65155 ? 115 TYR C CE2 1 
ATOM   2049 C CZ  . TYR B 2 115 ? -13.89600 16.83100 -11.95000 1.000 24.57445 ? 115 TYR C CZ  1 
ATOM   2050 O OH  . TYR B 2 115 ? -14.12700 17.99600 -11.26000 1.000 21.18000 ? 115 TYR C OH  1 
ATOM   2051 N N   . GLY B 2 116 ? -10.54000 10.86800 -15.31000 1.000 21.90945 ? 116 GLY C N   1 
ATOM   2052 C CA  . GLY B 2 116 ? -10.38800 9.56500  -15.92800 1.000 20.02219 ? 116 GLY C CA  1 
ATOM   2053 C C   . GLY B 2 116 ? -11.12100 9.36000  -17.24100 1.000 23.19986 ? 116 GLY C C   1 
ATOM   2054 O O   . GLY B 2 116 ? -11.12900 8.23900  -17.76000 1.000 22.49208 ? 116 GLY C O   1 
ATOM   2055 N N   . ARG B 2 117 ? -11.71700 10.39500 -17.82100 1.000 22.23833 ? 117 ARG C N   1 
ATOM   2056 C CA  . ARG B 2 117 ? -12.42700 10.24000 -19.08400 1.000 22.61247 ? 117 ARG C CA  1 
ATOM   2057 C C   . ARG B 2 117 ? -11.86400 11.15600 -20.15900 1.000 20.84192 ? 117 ARG C C   1 
ATOM   2058 O O   . ARG B 2 117 ? -11.43100 12.26900 -19.87700 1.000 19.44326 ? 117 ARG C O   1 
ATOM   2059 C CB  . ARG B 2 117 ? -13.91700 10.53500 -18.94100 1.000 24.92730 ? 117 ARG C CB  1 
ATOM   2060 C CG  . ARG B 2 117 ? -14.61600 9.72800  -17.87600 1.000 26.57403 ? 117 ARG C CG  1 
ATOM   2061 C CD  . ARG B 2 117 ? -14.71100 8.29900  -18.32200 1.000 32.47939 ? 117 ARG C CD  1 
ATOM   2062 N NE  . ARG B 2 117 ? -15.29400 8.22000  -19.64900 1.000 37.00063 ? 117 ARG C NE  1 
ATOM   2063 C CZ  . ARG B 2 117 ? -16.56300 7.93300  -19.88800 1.000 42.59429 ? 117 ARG C CZ  1 
ATOM   2064 N NH1 . ARG B 2 117 ? -17.42100 7.73400  -18.90100 1.000 38.44461 ? 117 ARG C NH1 1 
ATOM   2065 N NH2 . ARG B 2 117 ? -16.98500 7.85700  -21.14900 1.000 43.45111 ? 117 ARG C NH2 1 
ATOM   2066 N N   . PHE B 2 118 ? -11.94400 10.70600 -21.41300 1.000 20.53219 ? 118 PHE C N   1 
ATOM   2067 C CA  . PHE B 2 118 ? -11.46400 11.52500 -22.51600 1.000 18.95862 ? 118 PHE C CA  1 
ATOM   2068 C C   . PHE B 2 118 ? -12.41900 12.69000 -22.76100 1.000 20.06432 ? 118 PHE C C   1 
ATOM   2069 O O   . PHE B 2 118 ? -13.63700 12.53600 -22.70100 1.000 19.62606 ? 118 PHE C O   1 
ATOM   2070 C CB  . PHE B 2 118 ? -11.30300 10.67600 -23.78600 1.000 20.66802 ? 118 PHE C CB  1 
ATOM   2071 C CG  . PHE B 2 118 ? -10.07100 9.82500  -23.78900 1.000 22.98580 ? 118 PHE C CG  1 
ATOM   2072 C CD1 . PHE B 2 118 ? -8.85800  10.33100 -24.23900 1.000 23.31014 ? 118 PHE C CD1 1 
ATOM   2073 C CD2 . PHE B 2 118 ? -10.11200 8.51800  -23.32100 1.000 27.94751 ? 118 PHE C CD2 1 
ATOM   2074 C CE1 . PHE B 2 118 ? -7.71500  9.55700  -24.22700 1.000 22.66518 ? 118 PHE C CE1 1 
ATOM   2075 C CE2 . PHE B 2 118 ? -8.97300  7.73400  -23.31600 1.000 29.29279 ? 118 PHE C CE2 1 
ATOM   2076 C CZ  . PHE B 2 118 ? -7.76500  8.25900  -23.77500 1.000 26.82589 ? 118 PHE C CZ  1 
ATOM   2077 N N   . LEU B 2 119 ? -11.86100 13.86600 -23.03300 1.000 19.10750 ? 119 LEU C N   1 
ATOM   2078 C CA  . LEU B 2 119 ? -12.67300 15.05800 -23.17100 1.000 21.06238 ? 119 LEU C CA  1 
ATOM   2079 C C   . LEU B 2 119 ? -13.38000 15.07900 -24.52400 1.000 25.46716 ? 119 LEU C C   1 
ATOM   2080 O O   . LEU B 2 119 ? -12.94000 14.43100 -25.47700 1.000 21.95050 ? 119 LEU C O   1 
ATOM   2081 C CB  . LEU B 2 119 ? -11.81300 16.30500 -23.01200 1.000 23.50663 ? 119 LEU C CB  1 
ATOM   2082 C CG  . LEU B 2 119 ? -11.51700 16.76700 -21.58100 1.000 24.49528 ? 119 LEU C CG  1 
ATOM   2083 C CD1 . LEU B 2 119 ? -10.60800 17.98100 -21.64100 1.000 21.74940 ? 119 LEU C CD1 1 
ATOM   2084 C CD2 . LEU B 2 119 ? -12.80000 17.09500 -20.83300 1.000 22.54826 ? 119 LEU C CD2 1 
ATOM   2085 N N   . PRO B 2 120 ? -14.49800 15.81600 -24.63100 1.000 24.46693 ? 120 PRO C N   1 
ATOM   2086 C CA  . PRO B 2 120 ? -15.13900 16.00000 -25.94300 1.000 27.02867 ? 120 PRO C CA  1 
ATOM   2087 C C   . PRO B 2 120 ? -14.53600 17.17500 -26.70700 1.000 27.86493 ? 120 PRO C C   1 
ATOM   2088 O O   . PRO B 2 120 ? -13.60300 17.82600 -26.23100 1.000 26.41605 ? 120 PRO C O   1 
ATOM   2089 C CB  . PRO B 2 120 ? -16.59700 16.27200 -25.56400 1.000 27.08386 ? 120 PRO C CB  1 
ATOM   2090 C CG  . PRO B 2 120 ? -16.44800 17.10800 -24.31900 1.000 27.14847 ? 120 PRO C CG  1 
ATOM   2091 C CD  . PRO B 2 120 ? -15.21700 16.55200 -23.57700 1.000 25.52410 ? 120 PRO C CD  1 
ATOM   2092 N N   . GLN B 2 121 ? -15.08100 17.49300 -27.87600 1.000 32.42077 ? 121 GLN C N   1 
ATOM   2093 C CA  . GLN B 2 121 ? -14.66200 18.70900 -28.55600 1.000 32.74552 ? 121 GLN C CA  1 
ATOM   2094 C C   . GLN B 2 121 ? -15.26000 19.94800 -27.87700 1.000 37.55750 ? 121 GLN C C   1 
ATOM   2095 O O   . GLN B 2 121 ? -16.31800 19.86900 -27.24200 1.000 34.24173 ? 121 GLN C O   1 
ATOM   2096 C CB  . GLN B 2 121 ? -15.06700 18.64500 -30.02200 1.000 38.34550 ? 121 GLN C CB  1 
ATOM   2097 C CG  . GLN B 2 121 ? -14.48000 17.41600 -30.70400 1.000 36.92123 ? 121 GLN C CG  1 
ATOM   2098 C CD  . GLN B 2 121 ? -12.97600 17.56100 -30.91100 1.000 37.13386 ? 121 GLN C CD  1 
ATOM   2099 O OE1 . GLN B 2 121 ? -12.42600 18.65400 -30.76000 1.000 37.51372 ? 121 GLN C OE1 1 
ATOM   2100 N NE2 . GLN B 2 121 ? -12.30100 16.45400 -31.20700 1.000 32.37103 ? 121 GLN C NE2 1 
ATOM   2101 N N   . PRO B 2 122 ? -14.58800 21.09900 -27.98000 1.000 34.14931 ? 122 PRO C N   1 
ATOM   2102 C CA  . PRO B 2 122 ? -15.09400 22.31600 -27.32600 1.000 34.73546 ? 122 PRO C CA  1 
ATOM   2103 C C   . PRO B 2 122 ? -16.50500 22.65500 -27.77900 1.000 39.28575 ? 122 PRO C C   1 
ATOM   2104 O O   . PRO B 2 122 ? -16.81400 22.65700 -28.97200 1.000 35.06955 ? 122 PRO C O   1 
ATOM   2105 C CB  . PRO B 2 122 ? -14.09000 23.39800 -27.74500 1.000 35.57439 ? 122 PRO C CB  1 
ATOM   2106 C CG  . PRO B 2 122 ? -12.86800 22.68000 -28.11300 1.000 33.17050 ? 122 PRO C CG  1 
ATOM   2107 C CD  . PRO B 2 122 ? -13.24200 21.29000 -28.54800 1.000 36.88374 ? 122 PRO C CD  1 
ATOM   2108 N N   . GLY B 2 123 ? -17.36400 22.93600 -26.80500 1.000 36.84147 ? 123 GLY C N   1 
ATOM   2109 C CA  . GLY B 2 123 ? -18.73500 23.26800 -27.07200 1.000 37.42874 ? 123 GLY C CA  1 
ATOM   2110 C C   . GLY B 2 123 ? -19.69500 22.10500 -26.97800 1.000 38.72604 ? 123 GLY C C   1 
ATOM   2111 O O   . GLY B 2 123 ? -20.90800 22.32900 -26.90400 1.000 36.69789 ? 123 GLY C O   1 
ATOM   2112 N N   . HIS B 2 124 ? -19.19100 20.86900 -26.99200 1.000 35.80793 ? 124 HIS C N   1 
ATOM   2113 C CA  . HIS B 2 124 ? -20.02200 19.67200 -26.89000 1.000 36.74191 ? 124 HIS C CA  1 
ATOM   2114 C C   . HIS B 2 124 ? -19.90600 19.01400 -25.52900 1.000 29.63652 ? 124 HIS C C   1 
ATOM   2115 O O   . HIS B 2 124 ? -19.97000 17.79100 -25.41400 1.000 33.56935 ? 124 HIS C O   1 
ATOM   2116 C CB  . HIS B 2 124 ? -19.71000 18.64300 -27.97700 1.000 33.98497 ? 124 HIS C CB  1 
ATOM   2117 C CG  . HIS B 2 124 ? -19.64000 19.20200 -29.36000 1.000 40.55570 ? 124 HIS C CG  1 
ATOM   2118 N ND1 . HIS B 2 124 ? -20.01200 20.49100 -29.66600 1.000 42.84106 ? 124 HIS C ND1 1 
ATOM   2119 C CD2 . HIS B 2 124 ? -19.32600 18.61200 -30.53800 1.000 46.83212 ? 124 HIS C CD2 1 
ATOM   2120 C CE1 . HIS B 2 124 ? -19.88700 20.68900 -30.96600 1.000 42.85477 ? 124 HIS C CE1 1 
ATOM   2121 N NE2 . HIS B 2 124 ? -19.47200 19.56400 -31.51800 1.000 46.83387 ? 124 HIS C NE2 1 
ATOM   2122 N N   . GLU B 2 125 ? -19.74200 19.83500 -24.49300 1.000 31.30006 ? 125 GLU C N   1 
ATOM   2123 C CA  . GLU B 2 125 ? -19.71800 19.33300 -23.13200 1.000 36.04727 ? 125 GLU C CA  1 
ATOM   2124 C C   . GLU B 2 125 ? -21.07100 18.78000 -22.70500 1.000 36.04662 ? 125 GLU C C   1 
ATOM   2125 O O   . GLU B 2 125 ? -21.12100 17.91500 -21.82300 1.000 36.51838 ? 125 GLU C O   1 
ATOM   2126 C CB  . GLU B 2 125 ? -19.26200 20.44800 -22.18500 1.000 36.73675 ? 125 GLU C CB  1 
ATOM   2127 C CG  . GLU B 2 125 ? -17.80700 20.90200 -22.41400 1.000 36.94929 ? 125 GLU C CG  1 
ATOM   2128 C CD  . GLU B 2 125 ? -17.66800 21.90900 -23.55200 1.000 36.56755 ? 125 GLU C CD  1 
ATOM   2129 O OE1 . GLU B 2 125 ? -18.70600 22.41700 -24.02700 1.000 37.09562 ? 125 GLU C OE1 1 
ATOM   2130 O OE2 . GLU B 2 125 ? -16.52100 22.18400 -23.97600 1.000 35.27672 ? 125 GLU C OE2 1 
ATOM   2131 N N   . GLY B 2 126 ? -22.16300 19.24100 -23.32100 1.000 39.98711 ? 126 GLY C N   1 
ATOM   2132 C CA  . GLY B 2 126 ? -23.47800 18.76900 -22.91300 1.000 35.45957 ? 126 GLY C CA  1 
ATOM   2133 C C   . GLY B 2 126 ? -23.74700 17.34300 -23.35700 1.000 34.18654 ? 126 GLY C C   1 
ATOM   2134 O O   . GLY B 2 126 ? -24.18100 16.50700 -22.56100 1.000 40.85600 ? 126 GLY C O   1 
ATOM   2135 N N   . GLU B 2 127 ? -23.52000 17.06000 -24.64300 1.000 32.78982 ? 127 GLU C N   1 
ATOM   2136 C CA  . GLU B 2 127 ? -23.52500 15.69300 -25.15400 1.000 35.44252 ? 127 GLU C CA  1 
ATOM   2137 C C   . GLU B 2 127 ? -22.66300 14.79700 -24.27000 1.000 37.13139 ? 127 GLU C C   1 
ATOM   2138 O O   . GLU B 2 127 ? -23.10000 13.74100 -23.79600 1.000 31.76877 ? 127 GLU C O   1 
ATOM   2139 C CB  . GLU B 2 127 ? -22.98800 15.70300 -26.58900 1.000 43.35027 ? 127 GLU C CB  1 
ATOM   2140 C CG  . GLU B 2 127 ? -22.64400 14.34900 -27.19500 1.000 43.20072 ? 127 GLU C CG  1 
ATOM   2141 C CD  . GLU B 2 127 ? -23.85800 13.58900 -27.68200 1.000 53.57536 ? 127 GLU C CD  1 
ATOM   2142 O OE1 . GLU B 2 127 ? -24.26100 13.83100 -28.84000 1.000 66.11599 ? 127 GLU C OE1 1 
ATOM   2143 O OE2 . GLU B 2 127 ? -24.39100 12.74000 -26.93800 1.000 59.89971 ? 127 GLU C OE2 1 
ATOM   2144 N N   . TRP B 2 128 ? -21.43500 15.24700 -24.00000 1.000 33.39656 ? 128 TRP C N   1 
ATOM   2145 C CA  . TRP B 2 128 ? -20.47900 14.46800 -23.21400 1.000 30.91828 ? 128 TRP C CA  1 
ATOM   2146 C C   . TRP B 2 128 ? -21.00900 14.17200 -21.81100 1.000 32.32998 ? 128 TRP C C   1 
ATOM   2147 O O   . TRP B 2 128 ? -20.99600 13.02100 -21.35700 1.000 30.43246 ? 128 TRP C O   1 
ATOM   2148 C CB  . TRP B 2 128 ? -19.16600 15.24100 -23.15900 1.000 28.64700 ? 128 TRP C CB  1 
ATOM   2149 C CG  . TRP B 2 128 ? -18.04600 14.61100 -22.37700 1.000 29.11078 ? 128 TRP C CG  1 
ATOM   2150 C CD1 . TRP B 2 128 ? -17.17600 13.64300 -22.81000 1.000 26.82378 ? 128 TRP C CD1 1 
ATOM   2151 C CD2 . TRP B 2 128 ? -17.63400 14.95400 -21.05200 1.000 26.24715 ? 128 TRP C CD2 1 
ATOM   2152 N NE1 . TRP B 2 128 ? -16.26800 13.34800 -21.81700 1.000 28.32157 ? 128 TRP C NE1 1 
ATOM   2153 C CE2 . TRP B 2 128 ? -16.52700 14.13900 -20.72900 1.000 27.24555 ? 128 TRP C CE2 1 
ATOM   2154 C CE3 . TRP B 2 128 ? -18.09800 15.86600 -20.10200 1.000 26.74824 ? 128 TRP C CE3 1 
ATOM   2155 C CZ2 . TRP B 2 128 ? -15.87400 14.21800 -19.49600 1.000 25.57691 ? 128 TRP C CZ2 1 
ATOM   2156 C CZ3 . TRP B 2 128 ? -17.45300 15.93700 -18.87400 1.000 28.26525 ? 128 TRP C CZ3 1 
ATOM   2157 C CH2 . TRP B 2 128 ? -16.35800 15.11900 -18.58100 1.000 27.74440 ? 128 TRP C CH2 1 
ATOM   2158 N N   . PHE B 2 129 ? -21.48500 15.20000 -21.10900 1.000 28.66074 ? 129 PHE C N   1 
ATOM   2159 C CA  . PHE B 2 129 ? -21.91100 15.00200 -19.72800 1.000 32.14831 ? 129 PHE C CA  1 
ATOM   2160 C C   . PHE B 2 129 ? -23.15100 14.12000 -19.64000 1.000 31.89803 ? 129 PHE C C   1 
ATOM   2161 O O   . PHE B 2 129 ? -23.28800 13.35100 -18.68600 1.000 32.25578 ? 129 PHE C O   1 
ATOM   2162 C CB  . PHE B 2 129 ? -22.13900 16.35500 -19.05500 1.000 33.63984 ? 129 PHE C CB  1 
ATOM   2163 C CG  . PHE B 2 129 ? -22.43200 16.26500 -17.57100 1.000 32.59775 ? 129 PHE C CG  1 
ATOM   2164 C CD1 . PHE B 2 129 ? -21.41200 16.00600 -16.66700 1.000 34.23650 ? 129 PHE C CD1 1 
ATOM   2165 C CD2 . PHE B 2 129 ? -23.71300 16.51200 -17.08300 1.000 35.60185 ? 129 PHE C CD2 1 
ATOM   2166 C CE1 . PHE B 2 129 ? -21.66800 15.93500 -15.30600 1.000 33.29164 ? 129 PHE C CE1 1 
ATOM   2167 C CE2 . PHE B 2 129 ? -23.98200 16.46100 -15.71700 1.000 31.91734 ? 129 PHE C CE2 1 
ATOM   2168 C CZ  . PHE B 2 129 ? -22.95700 16.17500 -14.82900 1.000 34.33517 ? 129 PHE C CZ  1 
ATOM   2169 N N   . ASP B 2 130 ? -24.04700 14.20200 -20.62800 1.000 32.89890 ? 130 ASP C N   1 
ATOM   2170 C CA  . ASP B 2 130 ? -25.21100 13.32200 -20.66100 1.000 37.21161 ? 130 ASP C CA  1 
ATOM   2171 C C   . ASP B 2 130 ? -24.82600 11.86500 -20.88400 1.000 36.56452 ? 130 ASP C C   1 
ATOM   2172 O O   . ASP B 2 130 ? -25.64400 10.97100 -20.64600 1.000 34.89518 ? 130 ASP C O   1 
ATOM   2173 C CB  . ASP B 2 130 ? -26.18200 13.75200 -21.77000 1.000 34.20938 ? 130 ASP C CB  1 
ATOM   2174 C CG  . ASP B 2 130 ? -26.80900 15.11700 -21.52600 1.000 35.93853 ? 130 ASP C CG  1 
ATOM   2175 O OD1 . ASP B 2 130 ? -26.84900 15.57100 -20.36700 1.000 39.36918 ? 130 ASP C OD1 1 
ATOM   2176 O OD2 . ASP B 2 130 ? -27.27800 15.73300 -22.50800 1.000 43.25154 ? 130 ASP C OD2 1 
ATOM   2177 N N   . ASN B 2 131 ? -23.61200 11.60800 -21.35000 1.000 30.90284 ? 131 ASN C N   1 
ATOM   2178 C CA  . ASN B 2 131 ? -23.16100 10.26600 -21.66000 1.000 33.53797 ? 131 ASN C CA  1 
ATOM   2179 C C   . ASN B 2 131 ? -22.35900 9.66900  -20.50900 1.000 34.28862 ? 131 ASN C C   1 
ATOM   2180 O O   . ASN B 2 131 ? -21.86800 8.54300  -20.61400 1.000 36.44610 ? 131 ASN C O   1 
ATOM   2181 C CB  . ASN B 2 131 ? -22.35000 10.30700 -22.96700 1.000 38.99323 ? 131 ASN C CB  1 
ATOM   2182 C CG  . ASN B 2 131 ? -21.72300 8.98600  -23.32400 1.000 44.58186 ? 131 ASN C CG  1 
ATOM   2183 O OD1 . ASN B 2 131 ? -20.52800 8.77000  -23.11000 1.000 48.74699 ? 131 ASN C OD1 1 
ATOM   2184 N ND2 . ASN B 2 131 ? -22.53200 8.08100  -23.86600 1.000 44.44906 ? 131 ASN C ND2 1 
ATOM   2185 N N   . LEU B 2 132 ? -22.24500 10.38900 -19.39900 1.000 33.64142 ? 132 LEU C N   1 
ATOM   2186 C CA  . LEU B 2 132 ? -21.47500 9.95800  -18.24300 1.000 31.28010 ? 132 LEU C CA  1 
ATOM   2187 C C   . LEU B 2 132 ? -22.36900 9.13100  -17.32400 1.000 32.15942 ? 132 LEU C C   1 
ATOM   2188 O O   . LEU B 2 132 ? -23.58700 9.32400  -17.28200 1.000 31.29010 ? 132 LEU C O   1 
ATOM   2189 C CB  . LEU B 2 132 ? -20.93500 11.18600 -17.51500 1.000 30.87638 ? 132 LEU C CB  1 
ATOM   2190 C CG  . LEU B 2 132 ? -19.82400 11.88300 -18.31900 1.000 34.78223 ? 132 LEU C CG  1 
ATOM   2191 C CD1 . LEU B 2 132 ? -19.23400 13.00000 -17.53400 1.000 29.16417 ? 132 LEU C CD1 1 
ATOM   2192 C CD2 . LEU B 2 132 ? -18.73200 10.91200 -18.75500 1.000 33.63704 ? 132 LEU C CD2 1 
ATOM   2193 N N   . SER B 2 133 ? -21.76300 8.20100  -16.59000 1.000 29.98629 ? 133 SER C N   1 
ATOM   2194 C CA  . SER B 2 133 ? -22.54800 7.38500  -15.67000 1.000 27.54630 ? 133 SER C CA  1 
ATOM   2195 C C   . SER B 2 133 ? -23.06100 8.23700  -14.51200 1.000 29.66316 ? 133 SER C C   1 
ATOM   2196 O O   . SER B 2 133 ? -22.57100 9.34200  -14.25600 1.000 27.33275 ? 133 SER C O   1 
ATOM   2197 C CB  . SER B 2 133 ? -21.71400 6.22700  -15.12500 1.000 30.54857 ? 133 SER C CB  1 
ATOM   2198 O OG  . SER B 2 133 ? -20.63300 6.70000  -14.33000 1.000 29.21305 ? 133 SER C OG  1 
ATOM   2199 N N   . SER B 2 134 ? -24.06300 7.70000  -13.80300 1.000 30.57404 ? 134 SER C N   1 
ATOM   2200 C CA  . SER B 2 134 ? -24.65800 8.42400  -12.67800 1.000 30.69757 ? 134 SER C CA  1 
ATOM   2201 C C   . SER B 2 134 ? -23.61400 8.77300  -11.62300 1.000 30.84567 ? 134 SER C C   1 
ATOM   2202 O O   . SER B 2 134 ? -23.59700 9.89500  -11.09700 1.000 31.81856 ? 134 SER C O   1 
ATOM   2203 C CB  . SER B 2 134 ? -25.78900 7.60000  -12.05000 1.000 27.46553 ? 134 SER C CB  1 
ATOM   2204 O OG  . SER B 2 134 ? -26.83700 7.35700  -12.97800 1.000 37.39705 ? 134 SER C OG  1 
ATOM   2205 N N   . ASP B 2 135 ? -22.74500 7.82100  -11.28600 1.000 32.04165 ? 135 ASP C N   1 
ATOM   2206 C CA  . ASP B 2 135 ? -21.74500 8.07400  -10.25400 1.000 33.47002 ? 135 ASP C CA  1 
ATOM   2207 C C   . ASP B 2 135 ? -20.74700 9.13200  -10.70300 1.000 33.19734 ? 135 ASP C C   1 
ATOM   2208 O O   . ASP B 2 135 ? -20.30200 9.96100  -9.89700  1.000 30.18852 ? 135 ASP C O   1 
ATOM   2209 C CB  . ASP B 2 135 ? -21.02800 6.77400  -9.89600  1.000 35.26879 ? 135 ASP C CB  1 
ATOM   2210 C CG  . ASP B 2 135 ? -21.90700 5.83100  -9.09500  1.000 38.74826 ? 135 ASP C CG  1 
ATOM   2211 O OD1 . ASP B 2 135 ? -23.00900 6.24800  -8.66500  1.000 37.69004 ? 135 ASP C OD1 1 
ATOM   2212 O OD2 . ASP B 2 135 ? -21.50700 4.66000  -8.92400  1.000 44.41325 ? 135 ASP C OD2 1 
ATOM   2213 N N   . GLU B 2 136 ? -20.38700 9.12700  -11.98600 1.000 27.67237 ? 136 GLU C N   1 
ATOM   2214 C CA  . GLU B 2 136 ? -19.45300 10.13800 -12.46300 1.000 27.43244 ? 136 GLU C CA  1 
ATOM   2215 C C   . GLU B 2 136 ? -20.09100 11.51400 -12.45000 1.000 28.56132 ? 136 GLU C C   1 
ATOM   2216 O O   . GLU B 2 136 ? -19.44700 12.48400 -12.04500 1.000 25.90895 ? 136 GLU C O   1 
ATOM   2217 C CB  . GLU B 2 136 ? -18.93200 9.79200  -13.85400 1.000 26.94001 ? 136 GLU C CB  1 
ATOM   2218 C CG  . GLU B 2 136 ? -18.04900 8.55300  -13.87300 1.000 29.79915 ? 136 GLU C CG  1 
ATOM   2219 C CD  . GLU B 2 136 ? -17.77000 8.07800  -15.28200 1.000 37.78081 ? 136 GLU C CD  1 
ATOM   2220 O OE1 . GLU B 2 136 ? -18.70200 7.53500  -15.92800 1.000 34.73860 ? 136 GLU C OE1 1 
ATOM   2221 O OE2 . GLU B 2 136 ? -16.61400 8.23000  -15.73700 1.000 37.84428 ? 136 GLU C OE2 1 
ATOM   2222 N N   . ARG B 2 137 ? -21.35400 11.62100 -12.88000 1.000 26.34636 ? 137 ARG C N   1 
ATOM   2223 C CA  . ARG B 2 137 ? -22.01800 12.92000 -12.82600 1.000 27.80984 ? 137 ARG C CA  1 
ATOM   2224 C C   . ARG B 2 137 ? -22.11300 13.41800 -11.39300 1.000 29.38108 ? 137 ARG C C   1 
ATOM   2225 O O   . ARG B 2 137 ? -21.88300 14.60200 -11.12700 1.000 29.63727 ? 137 ARG C O   1 
ATOM   2226 C CB  . ARG B 2 137 ? -23.41000 12.86800 -13.46600 1.000 29.27584 ? 137 ARG C CB  1 
ATOM   2227 C CG  . ARG B 2 137 ? -23.42500 12.67900 -14.97500 1.000 29.36313 ? 137 ARG C CG  1 
ATOM   2228 C CD  . ARG B 2 137 ? -24.85700 12.38700 -15.48900 1.000 33.24093 ? 137 ARG C CD  1 
ATOM   2229 N NE  . ARG B 2 137 ? -25.07100 11.00100 -15.88100 1.000 39.20293 ? 137 ARG C NE  1 
ATOM   2230 C CZ  . ARG B 2 137 ? -26.09600 10.25600 -15.48700 1.000 40.75198 ? 137 ARG C CZ  1 
ATOM   2231 N NH1 . ARG B 2 137 ? -27.00500 10.71800 -14.63700 1.000 39.67767 ? 137 ARG C NH1 1 
ATOM   2232 N NH2 . ARG B 2 137 ? -26.21700 9.01600  -15.96200 1.000 44.01812 ? 137 ARG C NH2 1 
ATOM   2233 N N   . ALA B 2 138 ? -22.39900 12.51900 -10.44900 1.000 31.84417 ? 138 ALA C N   1 
ATOM   2234 C CA  . ALA B 2 138 ? -22.53400 12.92700 -9.05200  1.000 32.10397 ? 138 ALA C CA  1 
ATOM   2235 C C   . ALA B 2 138 ? -21.20700 13.42100 -8.48300  1.000 34.73215 ? 138 ALA C C   1 
ATOM   2236 O O   . ALA B 2 138 ? -21.15400 14.46800 -7.82600  1.000 34.49672 ? 138 ALA C O   1 
ATOM   2237 C CB  . ALA B 2 138 ? -23.07900 11.77100 -8.21300  1.000 34.95390 ? 138 ALA C CB  1 
ATOM   2238 N N   . PHE B 2 139 ? -20.12600 12.66400 -8.70400  1.000 26.40721 ? 139 PHE C N   1 
ATOM   2239 C CA  . PHE B 2 139 ? -18.81100 13.09600 -8.24200  1.000 28.41631 ? 139 PHE C CA  1 
ATOM   2240 C C   . PHE B 2 139 ? -18.44200 14.44600 -8.82600  1.000 28.81812 ? 139 PHE C C   1 
ATOM   2241 O O   . PHE B 2 139 ? -18.00200 15.35100 -8.10900  1.000 28.87523 ? 139 PHE C O   1 
ATOM   2242 C CB  . PHE B 2 139 ? -17.76400 12.05000 -8.59700  1.000 28.24931 ? 139 PHE C CB  1 
ATOM   2243 C CG  . PHE B 2 139 ? -16.39800 12.38100 -8.09700  1.000 31.27937 ? 139 PHE C CG  1 
ATOM   2244 C CD1 . PHE B 2 139 ? -16.04500 12.13200 -6.78600  1.000 33.78260 ? 139 PHE C CD1 1 
ATOM   2245 C CD2 . PHE B 2 139 ? -15.44400 12.89000 -8.96700  1.000 27.90143 ? 139 PHE C CD2 1 
ATOM   2246 C CE1 . PHE B 2 139 ? -14.78300 12.42100 -6.33000  1.000 35.68551 ? 139 PHE C CE1 1 
ATOM   2247 C CE2 . PHE B 2 139 ? -14.17300 13.16400 -8.52700  1.000 29.42469 ? 139 PHE C CE2 1 
ATOM   2248 C CZ  . PHE B 2 139 ? -13.83800 12.93300 -7.20200  1.000 33.35459 ? 139 PHE C CZ  1 
ATOM   2249 N N   . MET B 2 140 ? -18.59200 14.58100 -10.13800 1.000 26.51465 ? 140 MET C N   1 
ATOM   2250 C CA  . MET B 2 140 ? -18.37600 15.85000 -10.81900 1.000 27.67522 ? 140 MET C CA  1 
ATOM   2251 C C   . MET B 2 140 ? -19.15100 16.98000 -10.16200 1.000 31.86372 ? 140 MET C C   1 
ATOM   2252 O O   . MET B 2 140 ? -18.59000 18.03900 -9.86100  1.000 29.72092 ? 140 MET C O   1 
ATOM   2253 C CB  . MET B 2 140 ? -18.78900 15.64500 -12.26300 1.000 28.11883 ? 140 MET C CB  1 
ATOM   2254 C CG  . MET B 2 140 ? -17.76400 14.80600 -12.95900 1.000 28.17431 ? 140 MET C CG  1 
ATOM   2255 S SD  . MET B 2 140 ? -17.69000 14.91100 -14.74100 1.000 33.10560 ? 140 MET C SD  1 
ATOM   2256 C CE  . MET B 2 140 ? -17.16400 13.21200 -14.98700 1.000 35.56914 ? 140 MET C CE  1 
ATOM   2257 N N   . GLU B 2 141 ? -20.44400 16.76100 -9.90700  1.000 31.32597 ? 141 GLU C N   1 
ATOM   2258 C CA  . GLU B 2 141 ? -21.31300 17.83900 -9.45300  1.000 30.22331 ? 141 GLU C CA  1 
ATOM   2259 C C   . GLU B 2 141 ? -20.98900 18.31200 -8.04200  1.000 31.39661 ? 141 GLU C C   1 
ATOM   2260 O O   . GLU B 2 141 ? -21.39400 19.41900 -7.67800  1.000 33.13286 ? 141 GLU C O   1 
ATOM   2261 C CB  . GLU B 2 141 ? -22.76800 17.39000 -9.55900  1.000 34.15601 ? 141 GLU C CB  1 
ATOM   2262 C CG  . GLU B 2 141 ? -23.23500 17.29200 -11.00800 1.000 34.66489 ? 141 GLU C CG  1 
ATOM   2263 C CD  . GLU B 2 141 ? -24.65000 16.77600 -11.14500 1.000 39.88300 ? 141 GLU C CD  1 
ATOM   2264 O OE1 . GLU B 2 141 ? -25.04500 15.93000 -10.31600 1.000 40.50942 ? 141 GLU C OE1 1 
ATOM   2265 O OE2 . GLU B 2 141 ? -25.34800 17.17300 -12.10200 1.000 44.78398 ? 141 GLU C OE2 1 
ATOM   2266 N N   . THR B 2 142 ? -20.27300 17.51800 -7.24100  1.000 30.34477 ? 142 THR C N   1 
ATOM   2267 C CA  . THR B 2 142 ? -19.83800 18.02300 -5.94100  1.000 34.15560 ? 142 THR C CA  1 
ATOM   2268 C C   . THR B 2 142 ? -18.68900 19.01600 -6.06300  1.000 31.88768 ? 142 THR C C   1 
ATOM   2269 O O   . THR B 2 142 ? -18.46300 19.80100 -5.14000  1.000 32.57583 ? 142 THR C O   1 
ATOM   2270 C CB  . THR B 2 142 ? -19.40300 16.88900 -5.00100  1.000 32.77464 ? 142 THR C CB  1 
ATOM   2271 O OG1 . THR B 2 142 ? -18.06600 16.48600 -5.31100  1.000 37.97074 ? 142 THR C OG1 1 
ATOM   2272 C CG2 . THR B 2 142 ? -20.31600 15.70300 -5.12200  1.000 32.79241 ? 142 THR C CG2 1 
ATOM   2273 N N   . ASN B 2 143 ? -17.96300 19.00900 -7.17500  1.000 32.28781 ? 143 ASN C N   1 
ATOM   2274 C CA  . ASN B 2 143 ? -16.83800 19.92500 -7.34200  1.000 29.78522 ? 143 ASN C CA  1 
ATOM   2275 C C   . ASN B 2 143 ? -17.30800 21.21600 -8.01500  1.000 28.72055 ? 143 ASN C C   1 
ATOM   2276 O O   . ASN B 2 143 ? -16.82500 21.61700 -9.06200  1.000 25.67956 ? 143 ASN C O   1 
ATOM   2277 C CB  . ASN B 2 143 ? -15.72100 19.25400 -8.13300  1.000 29.24592 ? 143 ASN C CB  1 
ATOM   2278 C CG  . ASN B 2 143 ? -14.95900 18.23200 -7.30500  1.000 32.47673 ? 143 ASN C CG  1 
ATOM   2279 O OD1 . ASN B 2 143 ? -14.70700 18.43300 -6.10900  1.000 29.66995 ? 143 ASN C OD1 1 
ATOM   2280 N ND2 . ASN B 2 143 ? -14.57800 17.12700 -7.94200  1.000 31.64572 ? 143 ASN C ND2 1 
ATOM   2281 N N   . VAL B 2 144 ? -18.27800 21.86600 -7.37700  1.000 27.97230 ? 144 VAL C N   1 
ATOM   2282 C CA  . VAL B 2 144 ? -18.75900 23.18100 -7.78700  1.000 30.86107 ? 144 VAL C CA  1 
ATOM   2283 C C   . VAL B 2 144 ? -18.95800 24.01300 -6.52600  1.000 35.38280 ? 144 VAL C C   1 
ATOM   2284 O O   . VAL B 2 144 ? -19.64600 23.58100 -5.59400  1.000 32.02421 ? 144 VAL C O   1 
ATOM   2285 C CB  . VAL B 2 144 ? -20.07600 23.10600 -8.58600  1.000 34.90489 ? 144 VAL C CB  1 
ATOM   2286 C CG1 . VAL B 2 144 ? -20.71300 24.48800 -8.69100  1.000 36.98306 ? 144 VAL C CG1 1 
ATOM   2287 C CG2 . VAL B 2 144 ? -19.84400 22.50200 -9.95800  1.000 34.29357 ? 144 VAL C CG2 1 
ATOM   2288 N N   . ASP B 2 145 ? -18.34600 25.19500 -6.48700  1.000 30.95214 ? 145 ASP C N   1 
ATOM   2289 C CA  . ASP B 2 145 ? -18.43800 26.05100 -5.30800  1.000 38.89462 ? 145 ASP C CA  1 
ATOM   2290 C C   . ASP B 2 145 ? -19.82400 26.69000 -5.20100  1.000 42.54752 ? 145 ASP C C   1 
ATOM   2291 O O   . ASP B 2 145 ? -20.50300 26.92800 -6.20500  1.000 45.24394 ? 145 ASP C O   1 
ATOM   2292 C CB  . ASP B 2 145 ? -17.36800 27.13900 -5.37600  1.000 35.52112 ? 145 ASP C CB  1 
ATOM   2293 C CG  . ASP B 2 145 ? -17.04400 27.74500 -4.02000  1.000 33.98520 ? 145 ASP C CG  1 
ATOM   2294 O OD1 . ASP B 2 145 ? -17.42600 27.18200 -2.96300  1.000 39.84108 ? 145 ASP C OD1 1 
ATOM   2295 O OD2 . ASP B 2 145 ? -16.40100 28.81600 -4.02300  1.000 35.67911 ? 145 ASP C OD2 1 
ATOM   2296 N N   . VAL B 2 146 ? -20.24300 26.97700 -3.96900  1.000 49.19822 ? 146 VAL C N   1 
ATOM   2297 C CA  . VAL B 2 146 ? -21.51600 27.67000 -3.74700  1.000 42.98774 ? 146 VAL C CA  1 
ATOM   2298 C C   . VAL B 2 146 ? -21.42000 29.11700 -4.21300  1.000 49.06810 ? 146 VAL C C   1 
ATOM   2299 O O   . VAL B 2 146 ? -21.94400 29.47500 -5.27300  1.000 51.11677 ? 146 VAL C O   1 
ATOM   2300 C CB  . VAL B 2 146 ? -21.95800 27.60600 -2.26400  1.000 53.69074 ? 146 VAL C CB  1 
ATOM   2301 C CG1 . VAL B 2 146 ? -21.97400 26.15600 -1.75900  1.000 46.62759 ? 146 VAL C CG1 1 
ATOM   2302 C CG2 . VAL B 2 146 ? -21.06500 28.48800 -1.39100  1.000 46.44404 ? 146 VAL C CG2 1 
ATOM   2303 N N   . PRO C 1 1   ? 10.34000  10.46200 -23.02900 1.000 28.94469 ? 1   PRO A N   1 
ATOM   2304 C CA  . PRO C 1 1   ? 9.30100   11.44400 -22.69300 1.000 25.83501 ? 1   PRO A CA  1 
ATOM   2305 C C   . PRO C 1 1   ? 9.66100   12.09100 -21.37800 1.000 24.23208 ? 1   PRO A C   1 
ATOM   2306 O O   . PRO C 1 1   ? 10.48400  11.52200 -20.65500 1.000 23.70724 ? 1   PRO A O   1 
ATOM   2307 C CB  . PRO C 1 1   ? 8.03300   10.60900 -22.49500 1.000 26.33360 ? 1   PRO A CB  1 
ATOM   2308 C CG  . PRO C 1 1   ? 8.44500   9.19400  -22.57300 1.000 28.66419 ? 1   PRO A CG  1 
ATOM   2309 C CD  . PRO C 1 1   ? 9.83500   9.08100  -23.09200 1.000 28.59918 ? 1   PRO A CD  1 
ATOM   2310 N N   . VAL C 1 2   ? 9.05900   13.23200 -21.06000 1.000 18.38790 ? 2   VAL A N   1 
ATOM   2311 C CA  . VAL C 1 2   ? 9.04200   13.74000 -19.69100 1.000 18.95586 ? 2   VAL A CA  1 
ATOM   2312 C C   . VAL C 1 2   ? 7.60000   13.72700 -19.21400 1.000 18.87870 ? 2   VAL A C   1 
ATOM   2313 O O   . VAL C 1 2   ? 6.73500   14.37200 -19.82000 1.000 20.23961 ? 2   VAL A O   1 
ATOM   2314 C CB  . VAL C 1 2   ? 9.63700   15.15000 -19.57000 1.000 18.52850 ? 2   VAL A CB  1 
ATOM   2315 C CG1 . VAL C 1 2   ? 9.50200   15.64200 -18.13700 1.000 18.55752 ? 2   VAL A CG1 1 
ATOM   2316 C CG2 . VAL C 1 2   ? 11.11600  15.14300 -20.00000 1.000 17.18897 ? 2   VAL A CG2 1 
ATOM   2317 N N   . TYR C 1 3   ? 7.33800   12.99900 -18.14000 1.000 18.65383 ? 3   TYR A N   1 
ATOM   2318 C CA  . TYR C 1 3   ? 6.01400   12.96200 -17.53100 1.000 16.94101 ? 3   TYR A CA  1 
ATOM   2319 C C   . TYR C 1 3   ? 6.08400   13.77000 -16.24100 1.000 19.38034 ? 3   TYR A C   1 
ATOM   2320 O O   . TYR C 1 3   ? 6.69700   13.32900 -15.25900 1.000 20.12716 ? 3   TYR A O   1 
ATOM   2321 C CB  . TYR C 1 3   ? 5.56400   11.52600 -17.25400 1.000 19.28966 ? 3   TYR A CB  1 
ATOM   2322 C CG  . TYR C 1 3   ? 5.11100   10.77500 -18.49100 1.000 19.77940 ? 3   TYR A CG  1 
ATOM   2323 C CD1 . TYR C 1 3   ? 3.81100   10.89100 -18.93900 1.000 22.57153 ? 3   TYR A CD1 1 
ATOM   2324 C CD2 . TYR C 1 3   ? 5.97900   9.92900  -19.19000 1.000 17.38031 ? 3   TYR A CD2 1 
ATOM   2325 C CE1 . TYR C 1 3   ? 3.37300   10.21600 -20.06400 1.000 21.43771 ? 3   TYR A CE1 1 
ATOM   2326 C CE2 . TYR C 1 3   ? 5.54300   9.23200  -20.32000 1.000 20.81294 ? 3   TYR A CE2 1 
ATOM   2327 C CZ  . TYR C 1 3   ? 4.23900   9.39500  -20.75400 1.000 21.26739 ? 3   TYR A CZ  1 
ATOM   2328 O OH  . TYR C 1 3   ? 3.76900   8.72800  -21.87100 1.000 22.24406 ? 3   TYR A OH  1 
ATOM   2329 N N   . MET C 1 4   ? 5.46600   14.94700 -16.24200 1.000 18.23579 ? 4   MET A N   1 
ATOM   2330 C CA  . MET C 1 4   ? 5.34900   15.72300 -15.01300 1.000 18.15773 ? 4   MET A CA  1 
ATOM   2331 C C   . MET C 1 4   ? 4.13300   15.20500 -14.25900 1.000 19.05570 ? 4   MET A C   1 
ATOM   2332 O O   . MET C 1 4   ? 3.03000   15.14500 -14.81300 1.000 18.92050 ? 4   MET A O   1 
ATOM   2333 C CB  . MET C 1 4   ? 5.21600   17.21200 -15.31800 1.000 19.40496 ? 4   MET A CB  1 
ATOM   2334 C CG  . MET C 1 4   ? 6.26900   17.73600 -16.29500 1.000 17.14469 ? 4   MET A CG  1 
ATOM   2335 S SD  . MET C 1 4   ? 7.93700   17.70000 -15.64400 1.000 20.69480 ? 4   MET A SD  1 
ATOM   2336 C CE  . MET C 1 4   ? 7.81800   18.61300 -14.10700 1.000 15.68343 ? 4   MET A CE  1 
ATOM   2337 N N   . VAL C 1 5   ? 4.31500   14.80400 -13.00200 1.000 18.98766 ? 5   VAL A N   1 
ATOM   2338 C CA  . VAL C 1 5   ? 3.23100   14.18600 -12.24900 1.000 19.29567 ? 5   VAL A CA  1 
ATOM   2339 C C   . VAL C 1 5   ? 2.97500   15.04300 -11.02200 1.000 17.68923 ? 5   VAL A C   1 
ATOM   2340 O O   . VAL C 1 5   ? 3.80200   15.08300 -10.10600 1.000 18.80512 ? 5   VAL A O   1 
ATOM   2341 C CB  . VAL C 1 5   ? 3.55900   12.74200 -11.85800 1.000 22.55538 ? 5   VAL A CB  1 
ATOM   2342 C CG1 . VAL C 1 5   ? 2.36400   12.12400 -11.18500 1.000 17.60896 ? 5   VAL A CG1 1 
ATOM   2343 C CG2 . VAL C 1 5   ? 4.00200   11.93700 -13.09900 1.000 19.54396 ? 5   VAL A CG2 1 
ATOM   2344 N N   . TYR C 1 6   ? 1.82700   15.70700 -10.99400 1.000 19.50814 ? 6   TYR A N   1 
ATOM   2345 C CA  . TYR C 1 6   ? 1.48900   16.66600 -9.94800  1.000 18.29496 ? 6   TYR A CA  1 
ATOM   2346 C C   . TYR C 1 6   ? 0.63500   15.97100 -8.90400  1.000 18.67122 ? 6   TYR A C   1 
ATOM   2347 O O   . TYR C 1 6   ? -0.49400  15.55800 -9.18600  1.000 19.55530 ? 6   TYR A O   1 
ATOM   2348 C CB  . TYR C 1 6   ? 0.77800   17.87200 -10.54700 1.000 17.58367 ? 6   TYR A CB  1 
ATOM   2349 C CG  . TYR C 1 6   ? 1.65100   18.55800 -11.57100 1.000 21.06657 ? 6   TYR A CG  1 
ATOM   2350 C CD1 . TYR C 1 6   ? 2.59200   19.49900 -11.18100 1.000 16.84102 ? 6   TYR A CD1 1 
ATOM   2351 C CD2 . TYR C 1 6   ? 1.56700   18.22900 -12.91900 1.000 19.62809 ? 6   TYR A CD2 1 
ATOM   2352 C CE1 . TYR C 1 6   ? 3.40900   20.11100 -12.11100 1.000 17.79499 ? 6   TYR A CE1 1 
ATOM   2353 C CE2 . TYR C 1 6   ? 2.38500   18.84800 -13.86300 1.000 17.74058 ? 6   TYR A CE2 1 
ATOM   2354 C CZ  . TYR C 1 6   ? 3.29600   19.78300 -13.44600 1.000 16.92526 ? 6   TYR A CZ  1 
ATOM   2355 O OH  . TYR C 1 6   ? 4.11400   20.39300 -14.35900 1.000 17.37012 ? 6   TYR A OH  1 
ATOM   2356 N N   . VAL C 1 7   ? 1.18800   15.82700 -7.70200  1.000 20.77408 ? 7   VAL A N   1 
ATOM   2357 C CA  . VAL C 1 7   ? 0.54300   15.10300 -6.62100  1.000 21.35028 ? 7   VAL A CA  1 
ATOM   2358 C C   . VAL C 1 7   ? 0.66800   15.93700 -5.35300  1.000 21.01169 ? 7   VAL A C   1 
ATOM   2359 O O   . VAL C 1 7   ? 1.49500   16.85000 -5.25300  1.000 21.95009 ? 7   VAL A O   1 
ATOM   2360 C CB  . VAL C 1 7   ? 1.14500   13.68700 -6.40700  1.000 23.53661 ? 7   VAL A CB  1 
ATOM   2361 C CG1 . VAL C 1 7   ? 0.83000   12.78500 -7.60800  1.000 25.80563 ? 7   VAL A CG1 1 
ATOM   2362 C CG2 . VAL C 1 7   ? 2.65000   13.75700 -6.17100  1.000 20.35233 ? 7   VAL A CG2 1 
ATOM   2363 N N   . SER C 1 8   ? -0.15200  15.59500 -4.37200  1.000 22.27473 ? 8   SER A N   1 
ATOM   2364 C CA  . SER C 1 8   ? -0.06300  16.24200 -3.07600  1.000 21.86909 ? 8   SER A CA  1 
ATOM   2365 C C   . SER C 1 8   ? 1.06800   15.63800 -2.25900  1.000 25.07182 ? 8   SER A C   1 
ATOM   2366 O O   . SER C 1 8   ? 1.28200   14.42000 -2.26600  1.000 25.95708 ? 8   SER A O   1 
ATOM   2367 C CB  . SER C 1 8   ? -1.38000  16.11700 -2.31600  1.000 19.15676 ? 8   SER A CB  1 
ATOM   2368 O OG  . SER C 1 8   ? -2.42700  16.82000 -2.97000  1.000 25.05565 ? 8   SER A OG  1 
ATOM   2369 N N   . GLN C 1 9   ? 1.78500   16.51200 -1.55900  1.000 23.52238 ? 9   GLN A N   1 
ATOM   2370 C CA  . GLN C 1 9   ? 2.84100   16.11900 -0.63800  1.000 29.26337 ? 9   GLN A CA  1 
ATOM   2371 C C   . GLN C 1 9   ? 2.37400   15.00500 0.28400   1.000 29.28348 ? 9   GLN A C   1 
ATOM   2372 O O   . GLN C 1 9   ? 1.29600   15.08400 0.87100   1.000 26.06384 ? 9   GLN A O   1 
ATOM   2373 C CB  . GLN C 1 9   ? 3.27200   17.34700 0.17200   1.000 26.65168 ? 9   GLN A CB  1 
ATOM   2374 C CG  . GLN C 1 9   ? 4.25600   17.05400 1.26200   1.000 35.26379 ? 9   GLN A CG  1 
ATOM   2375 C CD  . GLN C 1 9   ? 5.66700   17.01500 0.74400   1.000 42.23258 ? 9   GLN A CD  1 
ATOM   2376 O OE1 . GLN C 1 9   ? 6.27300   15.94700 0.64900   1.000 42.47303 ? 9   GLN A OE1 1 
ATOM   2377 N NE2 . GLN C 1 9   ? 6.19900   18.17700 0.38700   1.000 46.52880 ? 9   GLN A NE2 1 
ATOM   2378 N N   . ASP C 1 10  ? 3.17500   13.94500 0.36900   1.000 34.98623 ? 10  ASP A N   1 
ATOM   2379 C CA  . ASP C 1 10  ? 2.96400   12.79800 1.24700   1.000 37.32106 ? 10  ASP A CA  1 
ATOM   2380 C C   . ASP C 1 10  ? 1.80300   11.90200 0.81100   1.000 34.40376 ? 10  ASP A C   1 
ATOM   2381 O O   . ASP C 1 10  ? 1.47200   10.94800 1.52500   1.000 35.06801 ? 10  ASP A O   1 
ATOM   2382 C CB  . ASP C 1 10  ? 2.74100   13.23300 2.70200   1.000 40.27129 ? 10  ASP A CB  1 
ATOM   2383 C CG  . ASP C 1 10  ? 4.03800   13.58900 3.40900   1.000 42.12530 ? 10  ASP A CG  1 
ATOM   2384 O OD1 . ASP C 1 10  ? 5.07500   13.76100 2.72500   1.000 43.07850 ? 10  ASP A OD1 1 
ATOM   2385 O OD2 . ASP C 1 10  ? 4.01200   13.71500 4.65400   1.000 49.69542 ? 10  ASP A OD2 1 
ATOM   2386 N N   . ARG C 1 11  ? 1.16500   12.16900 -0.32600  1.000 28.60672 ? 11  ARG A N   1 
ATOM   2387 C CA  . ARG C 1 11  ? 0.14700   11.24200 -0.80500  1.000 29.21956 ? 11  ARG A CA  1 
ATOM   2388 C C   . ARG C 1 11  ? 0.76500   9.92100  -1.24600  1.000 30.13140 ? 11  ARG A C   1 
ATOM   2389 O O   . ARG C 1 11  ? 0.14800   8.86100  -1.08600  1.000 31.30780 ? 11  ARG A O   1 
ATOM   2390 C CB  . ARG C 1 11  ? -0.62900  11.86400 -1.96600  1.000 27.46501 ? 11  ARG A CB  1 
ATOM   2391 C CG  . ARG C 1 11  ? -1.63900  10.94000 -2.62000  1.000 30.92506 ? 11  ARG A CG  1 
ATOM   2392 C CD  . ARG C 1 11  ? -2.69300  10.51400 -1.61100  1.000 35.48823 ? 11  ARG A CD  1 
ATOM   2393 N NE  . ARG C 1 11  ? -3.62000  9.52800  -2.15300  1.000 36.85599 ? 11  ARG A NE  1 
ATOM   2394 C CZ  . ARG C 1 11  ? -3.92400  8.38400  -1.55600  1.000 43.48010 ? 11  ARG A CZ  1 
ATOM   2395 N NH1 . ARG C 1 11  ? -3.34200  8.01700  -0.42500  1.000 46.07865 ? 11  ARG A NH1 1 
ATOM   2396 N NH2 . ARG C 1 11  ? -4.82800  7.58200  -2.11000  1.000 44.74322 ? 11  ARG A NH2 1 
ATOM   2397 N N   . LEU C 1 12  ? 1.96800   9.96700  -1.80600  1.000 29.92805 ? 12  LEU A N   1 
ATOM   2398 C CA  . LEU C 1 12  ? 2.68200   8.78600  -2.28200  1.000 30.50709 ? 12  LEU A CA  1 
ATOM   2399 C C   . LEU C 1 12  ? 3.94100   8.60000  -1.45300  1.000 31.80513 ? 12  LEU A C   1 
ATOM   2400 O O   . LEU C 1 12  ? 4.80600   9.48500  -1.42500  1.000 31.78223 ? 12  LEU A O   1 
ATOM   2401 C CB  . LEU C 1 12  ? 3.06100   8.91900  -3.75800  1.000 24.45728 ? 12  LEU A CB  1 
ATOM   2402 C CG  . LEU C 1 12  ? 1.88300   9.12000  -4.72000  1.000 28.00761 ? 12  LEU A CG  1 
ATOM   2403 C CD1 . LEU C 1 12  ? 2.39100   9.26500  -6.16600  1.000 28.03753 ? 12  LEU A CD1 1 
ATOM   2404 C CD2 . LEU C 1 12  ? 0.88700   7.98100  -4.59300  1.000 27.73937 ? 12  LEU A CD2 1 
ATOM   2405 N N   . THR C 1 13  ? 4.06100   7.43400  -0.82000  1.000 32.34016 ? 13  THR A N   1 
ATOM   2406 C CA  . THR C 1 13  ? 5.29100   7.03500  -0.16600  1.000 33.85534 ? 13  THR A CA  1 
ATOM   2407 C C   . THR C 1 13  ? 6.37300   6.82100  -1.22000  1.000 36.90743 ? 13  THR A C   1 
ATOM   2408 O O   . THR C 1 13  ? 6.08800   6.82500  -2.42200  1.000 31.50158 ? 13  THR A O   1 
ATOM   2409 C CB  . THR C 1 13  ? 5.07100   5.75600  0.63600   1.000 32.78573 ? 13  THR A CB  1 
ATOM   2410 O OG1 . THR C 1 13  ? 4.76700   4.68500  -0.26400  1.000 32.15712 ? 13  THR A OG1 1 
ATOM   2411 C CG2 . THR C 1 13  ? 3.93200   5.93600  1.61400   1.000 28.54834 ? 13  THR A CG2 1 
ATOM   2412 N N   . PRO C 1 14  ? 7.63700   6.65000  -0.80400  1.000 30.90574 ? 14  PRO A N   1 
ATOM   2413 C CA  . PRO C 1 14  ? 8.67100   6.31400  -1.79600  1.000 32.10873 ? 14  PRO A CA  1 
ATOM   2414 C C   . PRO C 1 14  ? 8.36400   5.04400  -2.56600  1.000 34.50388 ? 14  PRO A C   1 
ATOM   2415 O O   . PRO C 1 14  ? 8.65300   4.96700  -3.76800  1.000 34.40964 ? 14  PRO A O   1 
ATOM   2416 C CB  . PRO C 1 14  ? 9.93700   6.18600  -0.93900  1.000 37.63535 ? 14  PRO A CB  1 
ATOM   2417 C CG  . PRO C 1 14  ? 9.69500   7.14300  0.19400   1.000 33.14112 ? 14  PRO A CG  1 
ATOM   2418 C CD  . PRO C 1 14  ? 8.22500   7.05700  0.48900   1.000 33.17109 ? 14  PRO A CD  1 
ATOM   2419 N N   . SER C 1 15  ? 7.77400   4.04800  -1.90300  1.000 34.68462 ? 15  SER A N   1 
ATOM   2420 C CA  . SER C 1 15  ? 7.33300   2.83700  -2.58900  1.000 35.78159 ? 15  SER A CA  1 
ATOM   2421 C C   . SER C 1 15  ? 6.29300   3.14900  -3.65900  1.000 31.36528 ? 15  SER A C   1 
ATOM   2422 O O   . SER C 1 15  ? 6.34200   2.60300  -4.77000  1.000 32.11410 ? 15  SER A O   1 
ATOM   2423 C CB  . SER C 1 15  ? 6.76500   1.84800  -1.57100  1.000 35.81853 ? 15  SER A CB  1 
ATOM   2424 O OG  . SER C 1 15  ? 6.18700   0.72500  -2.20900  1.000 42.34836 ? 15  SER A OG  1 
ATOM   2425 N N   . ALA C 1 16  ? 5.32000   4.00500  -3.32900  1.000 30.63927 ? 16  ALA A N   1 
ATOM   2426 C CA  . ALA C 1 16  ? 4.22400   4.26500  -4.26000  1.000 29.96560 ? 16  ALA A CA  1 
ATOM   2427 C C   . ALA C 1 16  ? 4.66900   5.15600  -5.41500  1.000 30.98413 ? 16  ALA A C   1 
ATOM   2428 O O   . ALA C 1 16  ? 4.19500   4.99400  -6.54600  1.000 29.74517 ? 16  ALA A O   1 
ATOM   2429 C CB  . ALA C 1 16  ? 3.04000   4.88900  -3.51600  1.000 29.28994 ? 16  ALA A CB  1 
ATOM   2430 N N   . LYS C 1 17  ? 5.57100   6.10500  -5.15400  1.000 29.07775 ? 17  LYS A N   1 
ATOM   2431 C CA  . LYS C 1 17  ? 6.18800   6.85500  -6.24900  1.000 27.95724 ? 17  LYS A CA  1 
ATOM   2432 C C   . LYS C 1 17  ? 6.89500   5.91700  -7.21900  1.000 30.52372 ? 17  LYS A C   1 
ATOM   2433 O O   . LYS C 1 17  ? 6.77200   6.05800  -8.44200  1.000 28.40105 ? 17  LYS A O   1 
ATOM   2434 C CB  . LYS C 1 17  ? 7.17800   7.87900  -5.69200  1.000 28.90329 ? 17  LYS A CB  1 
ATOM   2435 C CG  . LYS C 1 17  ? 6.52400   9.16100  -5.18700  1.000 30.91906 ? 17  LYS A CG  1 
ATOM   2436 C CD  . LYS C 1 17  ? 7.55700   10.09900 -4.59500  1.000 30.95740 ? 17  LYS A CD  1 
ATOM   2437 C CE  . LYS C 1 17  ? 6.87700   11.23300 -3.85000  1.000 27.50097 ? 17  LYS A CE  1 
ATOM   2438 N NZ  . LYS C 1 17  ? 7.78700   11.82100 -2.84300  1.000 33.92447 ? 17  LYS A NZ  1 
ATOM   2439 N N   . HIS C 1 18  ? 7.67000   4.96400  -6.68700  1.000 28.50669 ? 18  HIS A N   1 
ATOM   2440 C CA  . HIS C 1 18  ? 8.33800   4.00200  -7.55000  1.000 30.58987 ? 18  HIS A CA  1 
ATOM   2441 C C   . HIS C 1 18  ? 7.33600   3.20700  -8.37400  1.000 29.75624 ? 18  HIS A C   1 
ATOM   2442 O O   . HIS C 1 18  ? 7.56800   2.95400  -9.56100  1.000 26.90449 ? 18  HIS A O   1 
ATOM   2443 C CB  . HIS C 1 18  ? 9.22000   3.06400  -6.72900  1.000 31.76920 ? 18  HIS A CB  1 
ATOM   2444 C CG  . HIS C 1 18  ? 10.09500  2.19000  -7.56700  1.000 32.31048 ? 18  HIS A CG  1 
ATOM   2445 N ND1 . HIS C 1 18  ? 9.64200   1.02500  -8.14700  1.000 39.73127 ? 18  HIS A ND1 1 
ATOM   2446 C CD2 . HIS C 1 18  ? 11.38300  2.32800  -7.95900  1.000 37.46637 ? 18  HIS A CD2 1 
ATOM   2447 C CE1 . HIS C 1 18  ? 10.61700  0.47500  -8.84800  1.000 35.80730 ? 18  HIS A CE1 1 
ATOM   2448 N NE2 . HIS C 1 18  ? 11.68700  1.24100  -8.74300  1.000 39.75077 ? 18  HIS A NE2 1 
ATOM   2449 N N   . ALA C 1 19  ? 6.21700   2.80700  -7.76300  1.000 26.86272 ? 19  ALA A N   1 
ATOM   2450 C CA  . ALA C 1 19  ? 5.21800   2.02300  -8.48600  1.000 31.93113 ? 19  ALA A CA  1 
ATOM   2451 C C   . ALA C 1 19  ? 4.52300   2.85500  -9.56000  1.000 28.09866 ? 19  ALA A C   1 
ATOM   2452 O O   . ALA C 1 19  ? 4.23100   2.35000  -10.65200 1.000 26.81164 ? 19  ALA A O   1 
ATOM   2453 C CB  . ALA C 1 19  ? 4.18300   1.45000  -7.51800  1.000 25.76711 ? 19  ALA A CB  1 
ATOM   2454 N N   . VAL C 1 20  ? 4.22500   4.11900  -9.25400  1.000 26.51790 ? 20  VAL A N   1 
ATOM   2455 C CA  . VAL C 1 20  ? 3.61800   5.01400  -10.23600 1.000 23.69615 ? 20  VAL A CA  1 
ATOM   2456 C C   . VAL C 1 20  ? 4.58700   5.27500  -11.38600 1.000 25.71431 ? 20  VAL A C   1 
ATOM   2457 O O   . VAL C 1 20  ? 4.21100   5.21100  -12.56300 1.000 25.59930 ? 20  VAL A O   1 
ATOM   2458 C CB  . VAL C 1 20  ? 3.17800   6.32300  -9.55000  1.000 26.62704 ? 20  VAL A CB  1 
ATOM   2459 C CG1 . VAL C 1 20  ? 2.77200   7.38300  -10.56800 1.000 20.92769 ? 20  VAL A CG1 1 
ATOM   2460 C CG2 . VAL C 1 20  ? 2.05900   6.05200  -8.58100  1.000 24.48857 ? 20  VAL A CG2 1 
ATOM   2461 N N   . ALA C 1 21  ? 5.85300   5.56300  -11.06000 1.000 23.75934 ? 21  ALA A N   1 
ATOM   2462 C CA  . ALA C 1 21  ? 6.85600   5.83200  -12.08800 1.000 26.17824 ? 21  ALA A CA  1 
ATOM   2463 C C   . ALA C 1 21  ? 7.09000   4.61400  -12.96300 1.000 26.95581 ? 21  ALA A C   1 
ATOM   2464 O O   . ALA C 1 21  ? 7.33200   4.74500  -14.16800 1.000 23.83394 ? 21  ALA A O   1 
ATOM   2465 C CB  . ALA C 1 21  ? 8.17100   6.27200  -11.44600 1.000 27.20774 ? 21  ALA A CB  1 
ATOM   2466 N N   . LYS C 1 22  ? 7.04000   3.42000  -12.36700 1.000 28.08301 ? 22  LYS A N   1 
ATOM   2467 C CA  . LYS C 1 22  ? 7.14600   2.19000  -13.14600 1.000 31.80777 ? 22  LYS A CA  1 
ATOM   2468 C C   . LYS C 1 22  ? 5.92800   1.97800  -14.03700 1.000 30.38639 ? 22  LYS A C   1 
ATOM   2469 O O   . LYS C 1 22  ? 6.06400   1.51600  -15.17600 1.000 30.75883 ? 22  LYS A O   1 
ATOM   2470 C CB  . LYS C 1 22  ? 7.31900   0.98800  -12.22000 1.000 33.78344 ? 22  LYS A CB  1 
ATOM   2471 C CG  . LYS C 1 22  ? 7.72200   -0.27400 -12.95700 1.000 40.16964 ? 22  LYS A CG  1 
ATOM   2472 C CD  . LYS C 1 22  ? 8.20000   -1.36600 -12.00000 1.000 47.34372 ? 22  LYS A CD  1 
ATOM   2473 C CE  . LYS C 1 22  ? 8.35600   -2.70500 -12.72500 1.000 50.85393 ? 22  LYS A CE  1 
ATOM   2474 N NZ  . LYS C 1 22  ? 7.09300   -3.16700 -13.37600 1.000 45.09694 ? 22  LYS A NZ  1 
ATOM   2475 N N   . ALA C 1 23  ? 4.73100   2.28300  -13.53600 1.000 27.26512 ? 23  ALA A N   1 
ATOM   2476 C CA  . ALA C 1 23  ? 3.52600   2.05900  -14.33300 1.000 30.66981 ? 23  ALA A CA  1 
ATOM   2477 C C   . ALA C 1 23  ? 3.53100   2.92700  -15.58400 1.000 28.00309 ? 23  ALA A C   1 
ATOM   2478 O O   . ALA C 1 23  ? 3.25900   2.44700  -16.69000 1.000 32.00835 ? 23  ALA A O   1 
ATOM   2479 C CB  . ALA C 1 23  ? 2.27300   2.33200  -13.49900 1.000 28.05212 ? 23  ALA A CB  1 
ATOM   2480 N N   . ILE C 1 24  ? 3.82600   4.21800  -15.42100 1.000 26.87557 ? 24  ILE A N   1 
ATOM   2481 C CA  . ILE C 1 24  ? 3.92200   5.12600  -16.56100 1.000 24.37179 ? 24  ILE A CA  1 
ATOM   2482 C C   . ILE C 1 24  ? 5.03600   4.68400  -17.50600 1.000 25.69350 ? 24  ILE A C   1 
ATOM   2483 O O   . ILE C 1 24  ? 4.85600   4.63600  -18.72900 1.000 22.47796 ? 24  ILE A O   1 
ATOM   2484 C CB  . ILE C 1 24  ? 4.15200   6.56400  -16.06300 1.000 26.93810 ? 24  ILE A CB  1 
ATOM   2485 C CG1 . ILE C 1 24  ? 2.90800   7.09200  -15.34800 1.000 24.42062 ? 24  ILE A CG1 1 
ATOM   2486 C CG2 . ILE C 1 24  ? 4.60600   7.46600  -17.22700 1.000 23.45842 ? 24  ILE A CG2 1 
ATOM   2487 C CD1 . ILE C 1 24  ? 3.17200   8.32300  -14.47500 1.000 22.52129 ? 24  ILE A CD1 1 
ATOM   2488 N N   . THR C 1 25  ? 6.20900   4.35800  -16.95000 1.000 26.95513 ? 25  THR A N   1 
ATOM   2489 C CA  . THR C 1 25  ? 7.36900   4.01300  -17.77800 1.000 23.26688 ? 25  THR A CA  1 
ATOM   2490 C C   . THR C 1 25  ? 7.11100   2.75100  -18.59900 1.000 27.14435 ? 25  THR A C   1 
ATOM   2491 O O   . THR C 1 25  ? 7.35700   2.72200  -19.81500 1.000 26.86177 ? 25  THR A O   1 
ATOM   2492 C CB  . THR C 1 25  ? 8.60100   3.82900  -16.89000 1.000 29.83605 ? 25  THR A CB  1 
ATOM   2493 O OG1 . THR C 1 25  ? 8.84000   5.03300  -16.15600 1.000 30.97819 ? 25  THR A OG1 1 
ATOM   2494 C CG2 . THR C 1 25  ? 9.81200   3.55600  -17.72600 1.000 31.12393 ? 25  THR A CG2 1 
ATOM   2495 N N   . ASP C 1 26  ? 6.61700   1.69300  -17.94400 1.000 28.62769 ? 26  ASP A N   1 
ATOM   2496 C CA  . ASP C 1 26  ? 6.22200   0.47500  -18.65000 1.000 28.23314 ? 26  ASP A CA  1 
ATOM   2497 C C   . ASP C 1 26  ? 5.15800   0.76300  -19.70500 1.000 29.29658 ? 26  ASP A C   1 
ATOM   2498 O O   . ASP C 1 26  ? 5.19600   0.20400  -20.80800 1.000 27.54825 ? 26  ASP A O   1 
ATOM   2499 C CB  . ASP C 1 26  ? 5.69600   -0.57000 -17.65800 1.000 31.23937 ? 26  ASP A CB  1 
ATOM   2500 C CG  . ASP C 1 26  ? 6.78600   -1.17000 -16.77200 1.000 37.54356 ? 26  ASP A CG  1 
ATOM   2501 O OD1 . ASP C 1 26  ? 7.99200   -0.90700 -17.00100 1.000 34.18614 ? 26  ASP A OD1 1 
ATOM   2502 O OD2 . ASP C 1 26  ? 6.41400   -1.91100 -15.82700 1.000 36.86874 ? 26  ASP A OD2 1 
ATOM   2503 N N   . ALA C 1 27  ? 4.17900   1.60900  -19.38100 1.000 24.89153 ? 27  ALA A N   1 
ATOM   2504 C CA  . ALA C 1 27  ? 3.15000   1.91700  -20.36800 1.000 26.37284 ? 27  ALA A CA  1 
ATOM   2505 C C   . ALA C 1 27  ? 3.77300   2.54600  -21.60100 1.000 25.10952 ? 27  ALA A C   1 
ATOM   2506 O O   . ALA C 1 27  ? 3.47400   2.14000  -22.73000 1.000 27.26984 ? 27  ALA A O   1 
ATOM   2507 C CB  . ALA C 1 27  ? 2.08300   2.83900  -19.77800 1.000 25.36227 ? 27  ALA A CB  1 
ATOM   2508 N N   . HIS C 1 28  ? 4.68300   3.51000  -21.39900 1.000 22.69266 ? 28  HIS A N   1 
ATOM   2509 C CA  . HIS C 1 28  ? 5.27000   4.22300  -22.53200 1.000 26.00900 ? 28  HIS A CA  1 
ATOM   2510 C C   . HIS C 1 28  ? 6.17300   3.31100  -23.35300 1.000 28.29154 ? 28  HIS A C   1 
ATOM   2511 O O   . HIS C 1 28  ? 6.06600   3.27700  -24.58400 1.000 32.12569 ? 28  HIS A O   1 
ATOM   2512 C CB  . HIS C 1 28  ? 6.04600   5.45700  -22.06100 1.000 26.94816 ? 28  HIS A CB  1 
ATOM   2513 C CG  . HIS C 1 28  ? 6.35000   6.41800  -23.16800 1.000 26.11706 ? 28  HIS A CG  1 
ATOM   2514 N ND1 . HIS C 1 28  ? 5.55200   7.50800  -23.44800 1.000 24.95602 ? 28  HIS A ND1 1 
ATOM   2515 C CD2 . HIS C 1 28  ? 7.34000   6.43000  -24.09600 1.000 30.37614 ? 28  HIS A CD2 1 
ATOM   2516 C CE1 . HIS C 1 28  ? 6.04600   8.16000  -24.48800 1.000 28.80455 ? 28  HIS A CE1 1 
ATOM   2517 N NE2 . HIS C 1 28  ? 7.13000   7.52500  -24.90100 1.000 27.14988 ? 28  HIS A NE2 1 
ATOM   2518 N N   . ARG C 1 29  ? 7.08500   2.57500  -22.70000 1.000 27.93473 ? 29  ARG A N   1 
ATOM   2519 C CA  . ARG C 1 29  ? 7.95000   1.67700  -23.46600 1.000 31.79552 ? 29  ARG A CA  1 
ATOM   2520 C C   . ARG C 1 29  ? 7.11800   0.62400  -24.18300 1.000 32.18771 ? 29  ARG A C   1 
ATOM   2521 O O   . ARG C 1 29  ? 7.39200   0.28200  -25.33900 1.000 31.07968 ? 29  ARG A O   1 
ATOM   2522 C CB  . ARG C 1 29  ? 9.02400   0.98300  -22.59400 1.000 36.26412 ? 29  ARG A CB  1 
ATOM   2523 C CG  . ARG C 1 29  ? 9.37500   -0.39700 -23.22700 1.000 34.80364 ? 29  ARG A CG  1 
ATOM   2524 C CD  . ARG C 1 29  ? 10.63500  -1.21400 -22.89300 1.000 43.25328 ? 29  ARG A CD  1 
ATOM   2525 N NE  . ARG C 1 29  ? 11.15300  -1.25300 -21.53200 1.000 48.57799 ? 29  ARG A NE  1 
ATOM   2526 C CZ  . ARG C 1 29  ? 12.44300  -1.18400 -21.22600 1.000 52.51606 ? 29  ARG A CZ  1 
ATOM   2527 N NH1 . ARG C 1 29  ? 13.36400  -0.91200 -22.14300 1.000 51.04834 ? 29  ARG A NH1 1 
ATOM   2528 N NH2 . ARG C 1 29  ? 12.82500  -1.44600 -19.98200 1.000 49.24588 ? 29  ARG A NH2 1 
ATOM   2529 N N   . GLY C 1 30  ? 6.06500   0.13300  -23.52500 1.000 30.77523 ? 30  GLY A N   1 
ATOM   2530 C CA  . GLY C 1 30  ? 5.30800   -0.97900 -24.07900 1.000 33.13248 ? 30  GLY A CA  1 
ATOM   2531 C C   . GLY C 1 30  ? 4.51700   -0.60200 -25.31700 1.000 35.11993 ? 30  GLY A C   1 
ATOM   2532 O O   . GLY C 1 30  ? 4.37600   -1.40700 -26.24200 1.000 35.50791 ? 30  GLY A O   1 
ATOM   2533 N N   . LEU C 1 31  ? 3.99600   0.62200  -25.36200 1.000 30.10543 ? 31  LEU A N   1 
ATOM   2534 C CA  . LEU C 1 31  ? 3.22500   1.02800  -26.52700 1.000 31.98182 ? 31  LEU A CA  1 
ATOM   2535 C C   . LEU C 1 31  ? 4.02100   1.81200  -27.55900 1.000 33.62670 ? 31  LEU A C   1 
ATOM   2536 O O   . LEU C 1 31  ? 3.57100   1.90500  -28.70800 1.000 31.26229 ? 31  LEU A O   1 
ATOM   2537 C CB  . LEU C 1 31  ? 1.99500   1.84100  -26.09600 1.000 30.16675 ? 31  LEU A CB  1 
ATOM   2538 C CG  . LEU C 1 31  ? 1.04500   1.11700  -25.14300 1.000 31.26466 ? 31  LEU A CG  1 
ATOM   2539 C CD1 . LEU C 1 31  ? 0.03800   2.06000  -24.54500 1.000 28.53421 ? 31  LEU A CD1 1 
ATOM   2540 C CD2 . LEU C 1 31  ? 0.31700   0.02600  -25.90400 1.000 36.11612 ? 31  LEU A CD2 1 
ATOM   2541 N N   . THR C 1 32  ? 5.19600   2.35400  -27.20800 1.000 28.66147 ? 32  THR A N   1 
ATOM   2542 C CA  . THR C 1 32  ? 5.94700   3.14900  -28.16700 1.000 32.47772 ? 32  THR A CA  1 
ATOM   2543 C C   . THR C 1 32  ? 7.22200   2.47600  -28.64200 1.000 34.13583 ? 32  THR A C   1 
ATOM   2544 O O   . THR C 1 32  ? 7.75300   2.87400  -29.67800 1.000 29.93464 ? 32  THR A O   1 
ATOM   2545 C CB  . THR C 1 32  ? 6.33900   4.51200  -27.57700 1.000 32.47214 ? 32  THR A CB  1 
ATOM   2546 O OG1 . THR C 1 32  ? 7.08000   4.31900  -26.36800 1.000 34.54975 ? 32  THR A OG1 1 
ATOM   2547 C CG2 . THR C 1 32  ? 5.08500   5.29800  -27.22500 1.000 28.25451 ? 32  THR A CG2 1 
ATOM   2548 N N   . GLY C 1 33  ? 7.73800   1.49700  -27.90200 1.000 36.37114 ? 33  GLY A N   1 
ATOM   2549 C CA  . GLY C 1 33  ? 9.02900   0.91700  -28.20200 1.000 38.52696 ? 33  GLY A CA  1 
ATOM   2550 C C   . GLY C 1 33  ? 10.21700  1.74100  -27.76300 1.000 38.99215 ? 33  GLY A C   1 
ATOM   2551 O O   . GLY C 1 33  ? 11.35600  1.27700  -27.90900 1.000 41.10826 ? 33  GLY A O   1 
ATOM   2552 N N   . THR C 1 34  ? 9.99800   2.95100  -27.25200 1.000 36.99256 ? 34  THR A N   1 
ATOM   2553 C CA  . THR C 1 34  ? 11.08700  3.76700  -26.73000 1.000 41.01293 ? 34  THR A CA  1 
ATOM   2554 C C   . THR C 1 34  ? 11.74000  3.05900  -25.54800 1.000 36.03372 ? 34  THR A C   1 
ATOM   2555 O O   . THR C 1 34  ? 11.06700  2.39500  -24.76100 1.000 39.79377 ? 34  THR A O   1 
ATOM   2556 C CB  . THR C 1 34  ? 10.54700  5.14300  -26.31700 1.000 40.59987 ? 34  THR A CB  1 
ATOM   2557 O OG1 . THR C 1 34  ? 9.98300   5.79700  -27.46700 1.000 43.59876 ? 34  THR A OG1 1 
ATOM   2558 C CG2 . THR C 1 34  ? 11.63900  6.02200  -25.70700 1.000 37.37323 ? 34  THR A CG2 1 
ATOM   2559 N N   . GLN C 1 35  ? 13.06300  3.16800  -25.44500 1.000 40.02122 ? 35  GLN A N   1 
ATOM   2560 C CA  . GLN C 1 35  ? 13.76800  2.45900  -24.38700 1.000 40.51644 ? 35  GLN A CA  1 
ATOM   2561 C C   . GLN C 1 35  ? 13.38500  3.01100  -23.02100 1.000 39.52745 ? 35  GLN A C   1 
ATOM   2562 O O   . GLN C 1 35  ? 12.98400  4.16800  -22.87400 1.000 38.65746 ? 35  GLN A O   1 
ATOM   2563 C CB  . GLN C 1 35  ? 15.27800  2.56400  -24.56500 1.000 41.40551 ? 35  GLN A CB  1 
ATOM   2564 C CG  . GLN C 1 35  ? 15.77200  2.06300  -25.89800 1.000 42.36424 ? 35  GLN A CG  1 
ATOM   2565 C CD  . GLN C 1 35  ? 16.00500  3.20900  -26.85800 1.000 43.74963 ? 35  GLN A CD  1 
ATOM   2566 O OE1 . GLN C 1 35  ? 15.17300  4.11300  -26.96200 1.000 44.65888 ? 35  GLN A OE1 1 
ATOM   2567 N NE2 . GLN C 1 35  ? 17.14900  3.19700  -27.54600 1.000 41.31920 ? 35  GLN A NE2 1 
ATOM   2568 N N   . HIS C 1 36  ? 13.53700  2.15000  -22.01400 1.000 39.91195 ? 36  HIS A N   1 
ATOM   2569 C CA  . HIS C 1 36  ? 13.19800  2.47800  -20.63400 1.000 38.25915 ? 36  HIS A CA  1 
ATOM   2570 C C   . HIS C 1 36  ? 13.80200  3.80900  -20.22200 1.000 32.70348 ? 36  HIS A C   1 
ATOM   2571 O O   . HIS C 1 36  ? 13.10500  4.71000  -19.74200 1.000 33.52548 ? 36  HIS A O   1 
ATOM   2572 C CB  . HIS C 1 36  ? 13.74700  1.39200  -19.71000 1.000 41.84468 ? 36  HIS A CB  1 
ATOM   2573 C CG  . HIS C 1 36  ? 12.83600  1.01900  -18.58600 1.000 44.38086 ? 36  HIS A CG  1 
ATOM   2574 N ND1 . HIS C 1 36  ? 13.28500  0.37600  -17.45200 1.000 43.88741 ? 36  HIS A ND1 1 
ATOM   2575 C CD2 . HIS C 1 36  ? 11.48700  1.02100  -18.50000 1.000 42.85318 ? 36  HIS A CD2 1 
ATOM   2576 C CE1 . HIS C 1 36  ? 12.26000  0.12100  -16.65800 1.000 41.76174 ? 36  HIS A CE1 1 
ATOM   2577 N NE2 . HIS C 1 36  ? 11.15500  0.50300  -17.27100 1.000 44.64813 ? 36  HIS A NE2 1 
ATOM   2578 N N   . PHE C 1 37  ? 15.11800  3.93800  -20.38900 1.000 31.38399 ? 37  PHE A N   1 
ATOM   2579 C CA  . PHE C 1 37  ? 15.88800  5.02700  -19.79800 1.000 31.83886 ? 37  PHE A CA  1 
ATOM   2580 C C   . PHE C 1 37  ? 15.52000  6.39200  -20.35000 1.000 32.11612 ? 37  PHE A C   1 
ATOM   2581 O O   . PHE C 1 37  ? 15.94100  7.39600  -19.77400 1.000 28.51372 ? 37  PHE A O   1 
ATOM   2582 C CB  . PHE C 1 37  ? 17.38900  4.78200  -19.99700 1.000 35.77513 ? 37  PHE A CB  1 
ATOM   2583 C CG  . PHE C 1 37  ? 17.76300  4.32200  -21.38400 1.000 35.00180 ? 37  PHE A CG  1 
ATOM   2584 C CD1 . PHE C 1 37  ? 17.64900  5.17100  -22.47600 1.000 34.26470 ? 37  PHE A CD1 1 
ATOM   2585 C CD2 . PHE C 1 37  ? 18.27000  3.04600  -21.58500 1.000 37.86417 ? 37  PHE A CD2 1 
ATOM   2586 C CE1 . PHE C 1 37  ? 18.00800  4.74100  -23.73900 1.000 39.62551 ? 37  PHE A CE1 1 
ATOM   2587 C CE2 . PHE C 1 37  ? 18.63400  2.61700  -22.85000 1.000 38.22911 ? 37  PHE A CE2 1 
ATOM   2588 C CZ  . PHE C 1 37  ? 18.51000  3.46600  -23.92400 1.000 37.37875 ? 37  PHE A CZ  1 
ATOM   2589 N N   . LEU C 1 38  ? 14.76300  6.45500  -21.44700 1.000 30.08428 ? 38  LEU A N   1 
ATOM   2590 C CA  . LEU C 1 38  ? 14.33700  7.73500  -21.99000 1.000 30.16834 ? 38  LEU A CA  1 
ATOM   2591 C C   . LEU C 1 38  ? 13.07300  8.27200  -21.32100 1.000 28.20928 ? 38  LEU A C   1 
ATOM   2592 O O   . LEU C 1 38  ? 12.74900  9.44600  -21.51400 1.000 28.87131 ? 38  LEU A O   1 
ATOM   2593 C CB  . LEU C 1 38  ? 14.10700  7.60800  -23.50100 1.000 32.26032 ? 38  LEU A CB  1 
ATOM   2594 C CG  . LEU C 1 38  ? 15.35800  7.62500  -24.39000 1.000 34.19701 ? 38  LEU A CG  1 
ATOM   2595 C CD1 . LEU C 1 38  ? 14.99700  7.46700  -25.87000 1.000 36.59237 ? 38  LEU A CD1 1 
ATOM   2596 C CD2 . LEU C 1 38  ? 16.18000  8.88000  -24.18300 1.000 29.12528 ? 38  LEU A CD2 1 
ATOM   2597 N N   . ALA C 1 39  ? 12.35700  7.46600  -20.53800 1.000 28.43967 ? 39  ALA A N   1 
ATOM   2598 C CA  . ALA C 1 39  ? 11.15300  7.93800  -19.85100 1.000 26.75540 ? 39  ALA A CA  1 
ATOM   2599 C C   . ALA C 1 39  ? 11.55100  8.56800  -18.52000 1.000 26.86229 ? 39  ALA A C   1 
ATOM   2600 O O   . ALA C 1 39  ? 12.01800  7.87500  -17.60600 1.000 27.50886 ? 39  ALA A O   1 
ATOM   2601 C CB  . ALA C 1 39  ? 10.15800  6.80300  -19.63400 1.000 28.07420 ? 39  ALA A CB  1 
ATOM   2602 N N   . GLN C 1 40  ? 11.38300  9.88100  -18.41200 1.000 23.55292 ? 40  GLN A N   1 
ATOM   2603 C CA  . GLN C 1 40  ? 11.53900  10.58500 -17.14400 1.000 21.53141 ? 40  GLN A CA  1 
ATOM   2604 C C   . GLN C 1 40  ? 10.16600  10.76500 -16.50500 1.000 25.54769 ? 40  GLN A C   1 
ATOM   2605 O O   . GLN C 1 40  ? 9.22200   11.22100 -17.16000 1.000 23.29215 ? 40  GLN A O   1 
ATOM   2606 C CB  . GLN C 1 40  ? 12.21400  11.94200 -17.34600 1.000 21.86225 ? 40  GLN A CB  1 
ATOM   2607 C CG  . GLN C 1 40  ? 12.26400  12.77800 -16.07800 1.000 21.20628 ? 40  GLN A CG  1 
ATOM   2608 C CD  . GLN C 1 40  ? 13.06400  14.05800 -16.21500 1.000 25.42795 ? 40  GLN A CD  1 
ATOM   2609 O OE1 . GLN C 1 40  ? 12.90400  14.98000 -15.40100 1.000 22.96391 ? 40  GLN A OE1 1 
ATOM   2610 N NE2 . GLN C 1 40  ? 13.94100  14.13000 -17.23600 1.000 20.20747 ? 40  GLN A NE2 1 
ATOM   2611 N N   . VAL C 1 41  ? 10.04800  10.37900 -15.23800 1.000 23.49056 ? 41  VAL A N   1 
ATOM   2612 C CA  . VAL C 1 41  ? 8.86400   10.66200 -14.44800 1.000 20.36738 ? 41  VAL A CA  1 
ATOM   2613 C C   . VAL C 1 41  ? 9.29300   11.61200 -13.34400 1.000 22.73219 ? 41  VAL A C   1 
ATOM   2614 O O   . VAL C 1 41  ? 10.14700  11.26900 -12.51400 1.000 22.84839 ? 41  VAL A O   1 
ATOM   2615 C CB  . VAL C 1 41  ? 8.22600   9.38500  -13.88200 1.000 24.90439 ? 41  VAL A CB  1 
ATOM   2616 C CG1 . VAL C 1 41  ? 6.99600   9.74800  -13.03600 1.000 20.08923 ? 41  VAL A CG1 1 
ATOM   2617 C CG2 . VAL C 1 41  ? 7.83700   8.45700  -15.00000 1.000 22.32409 ? 41  VAL A CG2 1 
ATOM   2618 N N   . ASN C 1 42  ? 8.72900   12.81700 -13.36100 1.000 18.30936 ? 42  ASN A N   1 
ATOM   2619 C CA  . ASN C 1 42  ? 9.19300   13.93600 -12.54700 1.000 20.47797 ? 42  ASN A CA  1 
ATOM   2620 C C   . ASN C 1 42  ? 8.04100   14.32500 -11.62900 1.000 22.88200 ? 42  ASN A C   1 
ATOM   2621 O O   . ASN C 1 42  ? 7.09900   14.99300 -12.07000 1.000 19.69070 ? 42  ASN A O   1 
ATOM   2622 C CB  . ASN C 1 42  ? 9.62900   15.10000 -13.44100 1.000 21.65103 ? 42  ASN A CB  1 
ATOM   2623 C CG  . ASN C 1 42  ? 10.57000  16.05800 -12.74600 1.000 24.01643 ? 42  ASN A CG  1 
ATOM   2624 O OD1 . ASN C 1 42  ? 10.30300  16.52000 -11.63600 1.000 24.86316 ? 42  ASN A OD1 1 
ATOM   2625 N ND2 . ASN C 1 42  ? 11.68000  16.36800 -13.40100 1.000 20.97457 ? 42  ASN A ND2 1 
ATOM   2626 N N   . PHE C 1 43  ? 8.09800   13.88100 -10.36500 1.000 19.08020 ? 43  PHE A N   1 
ATOM   2627 C CA  . PHE C 1 43  ? 7.02100   14.12000 -9.41300  1.000 19.92921 ? 43  PHE A CA  1 
ATOM   2628 C C   . PHE C 1 43  ? 7.12900   15.52700 -8.85600  1.000 20.75720 ? 43  PHE A C   1 
ATOM   2629 O O   . PHE C 1 43  ? 8.14700   15.88900 -8.26100  1.000 21.21857 ? 43  PHE A O   1 
ATOM   2630 C CB  . PHE C 1 43  ? 7.06800   13.12000 -8.26100  1.000 21.38660 ? 43  PHE A CB  1 
ATOM   2631 C CG  . PHE C 1 43  ? 6.56400   11.75300 -8.61400  1.000 23.13126 ? 43  PHE A CG  1 
ATOM   2632 C CD1 . PHE C 1 43  ? 5.19900   11.49900 -8.72600  1.000 20.19881 ? 43  PHE A CD1 1 
ATOM   2633 C CD2 . PHE C 1 43  ? 7.45700   10.72500 -8.85500  1.000 21.18088 ? 43  PHE A CD2 1 
ATOM   2634 C CE1 . PHE C 1 43  ? 4.74300   10.23300 -9.03400  1.000 22.95142 ? 43  PHE A CE1 1 
ATOM   2635 C CE2 . PHE C 1 43  ? 7.00900   9.46100  -9.17300  1.000 23.49126 ? 43  PHE A CE2 1 
ATOM   2636 C CZ  . PHE C 1 43  ? 5.64400   9.21200  -9.26300  1.000 20.89475 ? 43  PHE A CZ  1 
ATOM   2637 N N   . GLN C 1 44  ? 6.06300   16.29500 -8.99800  1.000 20.34742 ? 44  GLN A N   1 
ATOM   2638 C CA  . GLN C 1 44  ? 5.97200   17.65900 -8.49000  1.000 20.87488 ? 44  GLN A CA  1 
ATOM   2639 C C   . GLN C 1 44  ? 4.94700   17.65500 -7.35700  1.000 18.79496 ? 44  GLN A C   1 
ATOM   2640 O O   . GLN C 1 44  ? 3.74200   17.58500 -7.60600  1.000 18.30617 ? 44  GLN A O   1 
ATOM   2641 C CB  . GLN C 1 44  ? 5.56600   18.61400 -9.60400  1.000 20.36619 ? 44  GLN A CB  1 
ATOM   2642 C CG  . GLN C 1 44  ? 6.57400   18.68500 -10.74200 1.000 19.21781 ? 44  GLN A CG  1 
ATOM   2643 C CD  . GLN C 1 44  ? 7.80600   19.42000 -10.34300 1.000 19.92885 ? 44  GLN A CD  1 
ATOM   2644 O OE1 . GLN C 1 44  ? 7.73200   20.51500 -9.78900  1.000 27.13178 ? 44  GLN A OE1 1 
ATOM   2645 N NE2 . GLN C 1 44  ? 8.96200   18.82100 -10.59500 1.000 19.19306 ? 44  GLN A NE2 1 
ATOM   2646 N N   . GLU C 1 45  ? 5.43000   17.71500 -6.11900  1.000 20.62732 ? 45  GLU A N   1 
ATOM   2647 C CA  . GLU C 1 45  ? 4.57700   17.67100 -4.93600  1.000 21.39332 ? 45  GLU A CA  1 
ATOM   2648 C C   . GLU C 1 45  ? 4.28100   19.07200 -4.42700  1.000 19.98600 ? 45  GLU A C   1 
ATOM   2649 O O   . GLU C 1 45  ? 5.15900   19.94200 -4.40600  1.000 18.83107 ? 45  GLU A O   1 
ATOM   2650 C CB  . GLU C 1 45  ? 5.22800   16.86900 -3.80400  1.000 22.30994 ? 45  GLU A CB  1 
ATOM   2651 C CG  . GLU C 1 45  ? 5.31200   15.37100 -4.03900  1.000 22.04958 ? 45  GLU A CG  1 
ATOM   2652 C CD  . GLU C 1 45  ? 6.17100   14.67400 -2.98100  1.000 27.03166 ? 45  GLU A CD  1 
ATOM   2653 O OE1 . GLU C 1 45  ? 7.34000   15.05700 -2.83600  1.000 28.70218 ? 45  GLU A OE1 1 
ATOM   2654 O OE2 . GLU C 1 45  ? 5.68000   13.74000 -2.31700  1.000 32.42418 ? 45  GLU A OE2 1 
ATOM   2655 N N   . GLN C 1 46  ? 3.04100   19.27100 -3.99600  1.000 21.93587 ? 46  GLN A N   1 
ATOM   2656 C CA  . GLN C 1 46  ? 2.56700   20.49400 -3.36800  1.000 22.13175 ? 46  GLN A CA  1 
ATOM   2657 C C   . GLN C 1 46  ? 1.72500   20.13100 -2.15500  1.000 21.82017 ? 46  GLN A C   1 
ATOM   2658 O O   . GLN C 1 46  ? 1.11800   19.05100 -2.11400  1.000 23.88399 ? 46  GLN A O   1 
ATOM   2659 C CB  . GLN C 1 46  ? 1.71500   21.33000 -4.33300  1.000 21.82951 ? 46  GLN A CB  1 
ATOM   2660 C CG  . GLN C 1 46  ? 2.52400   21.93600 -5.46000  1.000 21.53274 ? 46  GLN A CG  1 
ATOM   2661 C CD  . GLN C 1 46  ? 3.34800   23.10800 -4.98700  1.000 21.37467 ? 46  GLN A CD  1 
ATOM   2662 O OE1 . GLN C 1 46  ? 2.85000   23.97500 -4.26200  1.000 22.45199 ? 46  GLN A OE1 1 
ATOM   2663 N NE2 . GLN C 1 46  ? 4.60400   23.15900 -5.40400  1.000 22.01251 ? 46  GLN A NE2 1 
ATOM   2664 N N   . PRO C 1 47  ? 1.63700   21.02300 -1.17400  1.000 25.54616 ? 47  PRO A N   1 
ATOM   2665 C CA  . PRO C 1 47  ? 0.74200   20.77000 -0.03800  1.000 26.07599 ? 47  PRO A CA  1 
ATOM   2666 C C   . PRO C 1 47  ? -0.67300  20.47800 -0.50900  1.000 25.22675 ? 47  PRO A C   1 
ATOM   2667 O O   . PRO C 1 47  ? -1.18000  21.11400 -1.43800  1.000 22.51004 ? 47  PRO A O   1 
ATOM   2668 C CB  . PRO C 1 47  ? 0.81100   22.07300 0.76900   1.000 30.32853 ? 47  PRO A CB  1 
ATOM   2669 C CG  . PRO C 1 47  ? 1.45900   23.09200 -0.15100  1.000 30.90043 ? 47  PRO A CG  1 
ATOM   2670 C CD  . PRO C 1 47  ? 2.37500   22.29000 -1.02500  1.000 26.46333 ? 47  PRO A CD  1 
ATOM   2671 N N   . ALA C 1 48  ? -1.30000  19.48100 0.11900   1.000 21.95384 ? 48  ALA A N   1 
ATOM   2672 C CA  . ALA C 1 48  ? -2.71600  19.22600 -0.11900  1.000 25.58771 ? 48  ALA A CA  1 
ATOM   2673 C C   . ALA C 1 48  ? -3.49500  20.50800 0.12800   1.000 27.71007 ? 48  ALA A C   1 
ATOM   2674 O O   . ALA C 1 48  ? -3.17000  21.27400 1.03500   1.000 28.70382 ? 48  ALA A O   1 
ATOM   2675 C CB  . ALA C 1 48  ? -3.22800  18.10800 0.79900   1.000 29.24760 ? 48  ALA A CB  1 
ATOM   2676 N N   . GLY C 1 49  ? -4.49800  20.76300 -0.70900  1.000 22.62365 ? 49  GLY A N   1 
ATOM   2677 C CA  . GLY C 1 49  ? -5.24600  22.00700 -0.66200  1.000 21.92870 ? 49  GLY A CA  1 
ATOM   2678 C C   . GLY C 1 49  ? -4.87800  23.00600 -1.73900  1.000 26.33693 ? 49  GLY A C   1 
ATOM   2679 O O   . GLY C 1 49  ? -5.53700  24.04400 -1.85600  1.000 26.82495 ? 49  GLY A O   1 
ATOM   2680 N N   . ASN C 1 50  ? -3.86300  22.72300 -2.54000  1.000 24.81442 ? 50  ASN A N   1 
ATOM   2681 C CA  . ASN C 1 50  ? -3.50700  23.62400 -3.62400  1.000 21.79963 ? 50  ASN A CA  1 
ATOM   2682 C C   . ASN C 1 50  ? -4.21700  23.28900 -4.93000  1.000 22.01823 ? 50  ASN A C   1 
ATOM   2683 O O   . ASN C 1 50  ? -4.02400  24.00700 -5.91100  1.000 19.98671 ? 50  ASN A O   1 
ATOM   2684 C CB  . ASN C 1 50  ? -1.98900  23.63000 -3.82900  1.000 18.20147 ? 50  ASN A CB  1 
ATOM   2685 C CG  . ASN C 1 50  ? -1.26500  24.53000 -2.82300  1.000 27.25777 ? 50  ASN A CG  1 
ATOM   2686 O OD1 . ASN C 1 50  ? -1.84100  24.93400 -1.81600  1.000 25.92781 ? 50  ASN A OD1 1 
ATOM   2687 N ND2 . ASN C 1 50  ? 0.00600   24.84100 -3.09800  1.000 24.53824 ? 50  ASN A ND2 1 
ATOM   2688 N N   . VAL C 1 51  ? -5.04000  22.23700 -4.97500  1.000 19.47916 ? 51  VAL A N   1 
ATOM   2689 C CA  . VAL C 1 51  ? -5.77000  21.86700 -6.18400  1.000 20.40134 ? 51  VAL A CA  1 
ATOM   2690 C C   . VAL C 1 51  ? -7.23300  22.23000 -5.98800  1.000 24.13089 ? 51  VAL A C   1 
ATOM   2691 O O   . VAL C 1 51  ? -7.83500  21.86300 -4.97200  1.000 21.60822 ? 51  VAL A O   1 
ATOM   2692 C CB  . VAL C 1 51  ? -5.60700  20.37300 -6.51900  1.000 22.13458 ? 51  VAL A CB  1 
ATOM   2693 C CG1 . VAL C 1 51  ? -6.49900  19.98600 -7.71100  1.000 18.93524 ? 51  VAL A CG1 1 
ATOM   2694 C CG2 . VAL C 1 51  ? -4.16700  20.08500 -6.87300  1.000 18.90003 ? 51  VAL A CG2 1 
ATOM   2695 N N   . PHE C 1 52  ? -7.79800  22.96100 -6.94700  1.000 18.99636 ? 52  PHE A N   1 
ATOM   2696 C CA  . PHE C 1 52  ? -9.21000  23.33600 -6.92700  1.000 20.96130 ? 52  PHE A CA  1 
ATOM   2697 C C   . PHE C 1 52  ? -9.88100  22.77300 -8.16800  1.000 22.50649 ? 52  PHE A C   1 
ATOM   2698 O O   . PHE C 1 52  ? -9.33700  22.87700 -9.26700  1.000 19.47554 ? 52  PHE A O   1 
ATOM   2699 C CB  . PHE C 1 52  ? -9.38300  24.85500 -6.89600  1.000 19.24029 ? 52  PHE A CB  1 
ATOM   2700 C CG  . PHE C 1 52  ? -8.83300  25.49300 -5.66300  1.000 18.85548 ? 52  PHE A CG  1 
ATOM   2701 C CD1 . PHE C 1 52  ? -7.46400  25.66700 -5.49900  1.000 20.84091 ? 52  PHE A CD1 1 
ATOM   2702 C CD2 . PHE C 1 52  ? -9.68100  25.89600 -4.64200  1.000 22.87865 ? 52  PHE A CD2 1 
ATOM   2703 C CE1 . PHE C 1 52  ? -6.95700  26.23600 -4.34900  1.000 24.59603 ? 52  PHE A CE1 1 
ATOM   2704 C CE2 . PHE C 1 52  ? -9.16800  26.47800 -3.48700  1.000 20.70877 ? 52  PHE A CE2 1 
ATOM   2705 C CZ  . PHE C 1 52  ? -7.81600  26.65800 -3.34700  1.000 20.85764 ? 52  PHE A CZ  1 
ATOM   2706 N N   . LEU C 1 53  ? -11.05800 22.17900 -7.99000  1.000 21.49409 ? 53  LEU A N   1 
ATOM   2707 C CA  . LEU C 1 53  ? -11.88000 21.68900 -9.08500  1.000 21.26236 ? 53  LEU A CA  1 
ATOM   2708 C C   . LEU C 1 53  ? -13.21200 22.41300 -9.00100  1.000 25.91891 ? 53  LEU A C   1 
ATOM   2709 O O   . LEU C 1 53  ? -13.89700 22.33100 -7.97300  1.000 23.03142 ? 53  LEU A O   1 
ATOM   2710 C CB  . LEU C 1 53  ? -12.06600 20.17200 -9.00600  1.000 22.02816 ? 53  LEU A CB  1 
ATOM   2711 C CG  . LEU C 1 53  ? -10.78400 19.33000 -8.97000  1.000 25.63895 ? 53  LEU A CG  1 
ATOM   2712 C CD1 . LEU C 1 53  ? -11.08700 17.84900 -8.77100  1.000 23.77510 ? 53  LEU A CD1 1 
ATOM   2713 C CD2 . LEU C 1 53  ? -10.02700 19.51200 -10.27000 1.000 21.19954 ? 53  LEU A CD2 1 
ATOM   2714 N N   . GLY C 1 54  ? -13.57300 23.12700 -10.06600 1.000 22.52684 ? 54  GLY A N   1 
ATOM   2715 C CA  . GLY C 1 54  ? -14.77300 23.95000 -9.99000  1.000 25.31533 ? 54  GLY A CA  1 
ATOM   2716 C C   . GLY C 1 54  ? -14.76400 24.94000 -8.84300  1.000 24.64666 ? 54  GLY A C   1 
ATOM   2717 O O   . GLY C 1 54  ? -15.82800 25.29900 -8.33200  1.000 22.60229 ? 54  GLY A O   1 
ATOM   2718 N N   . GLY C 1 55  ? -13.58600 25.41100 -8.43200  1.000 23.43406 ? 55  GLY A N   1 
ATOM   2719 C CA  . GLY C 1 55  ? -13.49400 26.33200 -7.31100  1.000 23.60442 ? 55  GLY A CA  1 
ATOM   2720 C C   . GLY C 1 55  ? -13.45500 25.68900 -5.93800  1.000 22.84658 ? 55  GLY A C   1 
ATOM   2721 O O   . GLY C 1 55  ? -13.31500 26.41200 -4.93700  1.000 21.81868 ? 55  GLY A O   1 
ATOM   2722 N N   . VAL C 1 56  ? -13.56100 24.36500 -5.84800  1.000 18.44106 ? 56  VAL A N   1 
ATOM   2723 C CA  . VAL C 1 56  ? -13.63500 23.67200 -4.56400  1.000 21.66570 ? 56  VAL A CA  1 
ATOM   2724 C C   . VAL C 1 56  ? -12.26900 23.12600 -4.20000  1.000 23.03841 ? 56  VAL A C   1 
ATOM   2725 O O   . VAL C 1 56  ? -11.68500 22.34700 -4.96400  1.000 22.21436 ? 56  VAL A O   1 
ATOM   2726 C CB  . VAL C 1 56  ? -14.66100 22.53100 -4.60200  1.000 23.83330 ? 56  VAL A CB  1 
ATOM   2727 C CG1 . VAL C 1 56  ? -14.65000 21.77900 -3.25900  1.000 23.80963 ? 56  VAL A CG1 1 
ATOM   2728 C CG2 . VAL C 1 56  ? -16.02000 23.07800 -4.94900  1.000 25.77220 ? 56  VAL A CG2 1 
ATOM   2729 N N   . GLN C 1 57  ? -11.78700 23.47800 -3.00600  1.000 21.48595 ? 57  GLN A N   1 
ATOM   2730 C CA  . GLN C 1 57  ? -10.48700 22.99400 -2.56000  1.000 23.87538 ? 57  GLN A CA  1 
ATOM   2731 C C   . GLN C 1 57  ? -10.51200 21.48200 -2.41500  1.000 27.70566 ? 57  GLN A C   1 
ATOM   2732 O O   . GLN C 1 57  ? -11.42700 20.91900 -1.80400  1.000 25.75080 ? 57  GLN A O   1 
ATOM   2733 C CB  . GLN C 1 57  ? -10.10000 23.63500 -1.23500  1.000 22.14843 ? 57  GLN A CB  1 
ATOM   2734 C CG  . GLN C 1 57  ? -8.67300  23.28500 -0.78700  1.000 23.61831 ? 57  GLN A CG  1 
ATOM   2735 C CD  . GLN C 1 57  ? -8.31300  23.91200 0.53500   1.000 28.27587 ? 57  GLN A CD  1 
ATOM   2736 O OE1 . GLN C 1 57  ? -8.99200  23.69200 1.53100   1.000 27.20254 ? 57  GLN A OE1 1 
ATOM   2737 N NE2 . GLN C 1 57  ? -7.25400  24.70900 0.54800   1.000 30.43476 ? 57  GLN A NE2 1 
ATOM   2738 N N   . GLN C 1 58  ? -9.50000  20.82700 -2.97100  1.000 21.98578 ? 58  GLN A N   1 
ATOM   2739 C CA  . GLN C 1 58  ? -9.40400  19.37800 -2.93900  1.000 26.31469 ? 58  GLN A CA  1 
ATOM   2740 C C   . GLN C 1 58  ? -8.54100  18.88900 -1.78200  1.000 23.34565 ? 58  GLN A C   1 
ATOM   2741 O O   . GLN C 1 58  ? -7.73400  19.62500 -1.22200  1.000 24.08445 ? 58  GLN A O   1 
ATOM   2742 C CB  . GLN C 1 58  ? -8.82800  18.85700 -4.25600  1.000 25.68951 ? 58  GLN A CB  1 
ATOM   2743 C CG  . GLN C 1 58  ? -9.72200  19.16900 -5.45300  1.000 25.14109 ? 58  GLN A CG  1 
ATOM   2744 C CD  . GLN C 1 58  ? -11.13200 18.62800 -5.25800  1.000 25.71592 ? 58  GLN A CD  1 
ATOM   2745 O OE1 . GLN C 1 58  ? -11.32900 17.43000 -5.09100  1.000 27.53338 ? 58  GLN A OE1 1 
ATOM   2746 N NE2 . GLN C 1 58  ? -12.10900 19.51400 -5.25300  1.000 26.74063 ? 58  GLN A NE2 1 
ATOM   2747 N N   . GLY C 1 59  ? -8.71000  17.61200 -1.45000  1.000 27.30489 ? 59  GLY A N   1 
ATOM   2748 C CA  . GLY C 1 59  ? -7.80200  16.91300 -0.55900  1.000 24.58929 ? 59  GLY A CA  1 
ATOM   2749 C C   . GLY C 1 59  ? -6.54600  16.51300 -1.30700  1.000 33.69700 ? 59  GLY A C   1 
ATOM   2750 O O   . GLY C 1 59  ? -6.11400  17.17900 -2.25600  1.000 29.47444 ? 59  GLY A O   1 
ATOM   2751 N N   . GLY C 1 60  ? -5.97100  15.38700 -0.91300  1.000 30.26554 ? 60  GLY A N   1 
ATOM   2752 C CA  . GLY C 1 60  ? -4.72500  14.93100 -1.48700  1.000 26.07882 ? 60  GLY A CA  1 
ATOM   2753 C C   . GLY C 1 60  ? -4.81900  13.90600 -2.59700  1.000 29.69291 ? 60  GLY A C   1 
ATOM   2754 O O   . GLY C 1 60  ? -3.78300  13.34700 -2.96800  1.000 27.30371 ? 60  GLY A O   1 
ATOM   2755 N N   . ASP C 1 61  ? -6.01000  13.65600 -3.16200  1.000 23.67817 ? 61  ASP A N   1 
ATOM   2756 C CA  . ASP C 1 61  ? -6.20500  12.52400 -4.06300  1.000 27.00716 ? 61  ASP A CA  1 
ATOM   2757 C C   . ASP C 1 61  ? -6.02900  12.85400 -5.54400  1.000 28.70369 ? 61  ASP A C   1 
ATOM   2758 O O   . ASP C 1 61  ? -5.78300  11.93400 -6.33200  1.000 30.12869 ? 61  ASP A O   1 
ATOM   2759 C CB  . ASP C 1 61  ? -7.60100  11.92200 -3.86600  1.000 28.44975 ? 61  ASP A CB  1 
ATOM   2760 C CG  . ASP C 1 61  ? -7.57500  10.65300 -3.04400  1.000 37.28045 ? 61  ASP A CG  1 
ATOM   2761 O OD1 . ASP C 1 61  ? -6.65700  10.50800 -2.20800  1.000 36.11855 ? 61  ASP A OD1 1 
ATOM   2762 O OD2 . ASP C 1 61  ? -8.47200  9.80100  -3.22400  1.000 42.46230 ? 61  ASP A OD2 1 
ATOM   2763 N N   . THR C 1 62  ? -6.13600  14.11400 -5.95300  1.000 24.87242 ? 62  THR A N   1 
ATOM   2764 C CA  . THR C 1 62  ? -5.97100  14.42400 -7.37300  1.000 23.74861 ? 62  THR A CA  1 
ATOM   2765 C C   . THR C 1 62  ? -4.56700  14.11000 -7.87500  1.000 20.46784 ? 62  THR A C   1 
ATOM   2766 O O   . THR C 1 62  ? -3.56900  14.37200 -7.20500  1.000 19.55137 ? 62  THR A O   1 
ATOM   2767 C CB  . THR C 1 62  ? -6.27700  15.89200 -7.66000  1.000 27.68894 ? 62  THR A CB  1 
ATOM   2768 O OG1 . THR C 1 62  ? -7.34200  16.34400 -6.81700  1.000 34.30123 ? 62  THR A OG1 1 
ATOM   2769 C CG2 . THR C 1 62  ? -6.63900  16.08900 -9.14100  1.000 25.53072 ? 62  THR A CG2 1 
ATOM   2770 N N   . ILE C 1 63  ? -4.49500  13.55500 -9.08200  1.000 21.02358 ? 63  ILE A N   1 
ATOM   2771 C CA  . ILE C 1 63  ? -3.23500  13.36000 -9.77800  1.000 17.85804 ? 63  ILE A CA  1 
ATOM   2772 C C   . ILE C 1 63  ? -3.38700  13.94900 -11.17900 1.000 14.50340 ? 63  ILE A C   1 
ATOM   2773 O O   . ILE C 1 63  ? -4.33100  13.61000 -11.89700 1.000 18.25182 ? 63  ILE A O   1 
ATOM   2774 C CB  . ILE C 1 63  ? -2.83400  11.87500 -9.85700  1.000 19.09835 ? 63  ILE A CB  1 
ATOM   2775 C CG1 . ILE C 1 63  ? -2.69800  11.23600 -8.46700  1.000 23.11295 ? 63  ILE A CG1 1 
ATOM   2776 C CG2 . ILE C 1 63  ? -1.53000  11.71700 -10.65200 1.000 20.88882 ? 63  ILE A CG2 1 
ATOM   2777 C CD1 . ILE C 1 63  ? -2.31000  9.75300  -8.54000  1.000 26.03014 ? 63  ILE A CD1 1 
ATOM   2778 N N   . PHE C 1 64  ? -2.46500  14.82800 -11.56600 1.000 19.61545 ? 64  PHE A N   1 
ATOM   2779 C CA  . PHE C 1 64  ? -2.41400  15.33400 -12.93800 1.000 16.80057 ? 64  PHE A CA  1 
ATOM   2780 C C   . PHE C 1 64  ? -1.10100  14.90500 -13.56600 1.000 17.88143 ? 64  PHE A C   1 
ATOM   2781 O O   . PHE C 1 64  ? -0.02400  15.23600 -13.05300 1.000 18.89819 ? 64  PHE A O   1 
ATOM   2782 C CB  . PHE C 1 64  ? -2.55800  16.86300 -12.97700 1.000 20.19659 ? 64  PHE A CB  1 
ATOM   2783 C CG  . PHE C 1 64  ? -2.37200  17.46000 -14.36000 1.000 18.59498 ? 64  PHE A CG  1 
ATOM   2784 C CD1 . PHE C 1 64  ? -2.95200  16.87300 -15.47000 1.000 18.07718 ? 64  PHE A CD1 1 
ATOM   2785 C CD2 . PHE C 1 64  ? -1.60100  18.60000 -14.54000 1.000 19.97518 ? 64  PHE A CD2 1 
ATOM   2786 C CE1 . PHE C 1 64  ? -2.76800  17.41400 -16.74000 1.000 18.81027 ? 64  PHE A CE1 1 
ATOM   2787 C CE2 . PHE C 1 64  ? -1.43100  19.14700 -15.80100 1.000 18.23162 ? 64  PHE A CE2 1 
ATOM   2788 C CZ  . PHE C 1 64  ? -2.00600  18.54400 -16.89800 1.000 16.16271 ? 64  PHE A CZ  1 
ATOM   2789 N N   . VAL C 1 65  ? -1.18600  14.20300 -14.69300 1.000 17.69896 ? 65  VAL A N   1 
ATOM   2790 C CA  . VAL C 1 65  ? -0.01900  13.73500 -15.42700 1.000 17.90611 ? 65  VAL A CA  1 
ATOM   2791 C C   . VAL C 1 65  ? 0.05400   14.55500 -16.71100 1.000 18.01370 ? 65  VAL A C   1 
ATOM   2792 O O   . VAL C 1 65  ? -0.90000  14.56800 -17.49900 1.000 19.27130 ? 65  VAL A O   1 
ATOM   2793 C CB  . VAL C 1 65  ? -0.10100  12.22400 -15.70600 1.000 16.81053 ? 65  VAL A CB  1 
ATOM   2794 C CG1 . VAL C 1 65  ? 1.03900   11.76800 -16.62500 1.000 18.50183 ? 65  VAL A CG1 1 
ATOM   2795 C CG2 . VAL C 1 65  ? -0.04700  11.46500 -14.40400 1.000 19.36458 ? 65  VAL A CG2 1 
ATOM   2796 N N   . HIS C 1 66  ? 1.14100   15.29600 -16.87400 1.000 16.96215 ? 66  HIS A N   1 
ATOM   2797 C CA  . HIS C 1 66  ? 1.39100   16.10500 -18.06500 1.000 19.55380 ? 66  HIS A CA  1 
ATOM   2798 C C   . HIS C 1 66  ? 2.54300   15.43500 -18.80300 1.000 18.76820 ? 66  HIS A C   1 
ATOM   2799 O O   . HIS C 1 66  ? 3.70800   15.59100 -18.42100 1.000 17.91892 ? 66  HIS A O   1 
ATOM   2800 C CB  . HIS C 1 66  ? 1.72900   17.54900 -17.70400 1.000 19.01626 ? 66  HIS A CB  1 
ATOM   2801 C CG  . HIS C 1 66  ? 1.71600   18.48400 -18.87400 1.000 20.03507 ? 66  HIS A CG  1 
ATOM   2802 N ND1 . HIS C 1 66  ? 2.14300   19.79300 -18.78300 1.000 18.67734 ? 66  HIS A ND1 1 
ATOM   2803 C CD2 . HIS C 1 66  ? 1.32700   18.30200 -20.16000 1.000 17.65858 ? 66  HIS A CD2 1 
ATOM   2804 C CE1 . HIS C 1 66  ? 2.00200   20.38200 -19.95800 1.000 18.27294 ? 66  HIS A CE1 1 
ATOM   2805 N NE2 . HIS C 1 66  ? 1.50700   19.50000 -20.81100 1.000 19.17636 ? 66  HIS A NE2 1 
ATOM   2806 N N   . GLY C 1 67  ? 2.21700   14.68700 -19.85400 1.000 19.72086 ? 67  GLY A N   1 
ATOM   2807 C CA  . GLY C 1 67  ? 3.23200   14.01000 -20.64200 1.000 17.29933 ? 67  GLY A CA  1 
ATOM   2808 C C   . GLY C 1 67  ? 3.67600   14.86500 -21.81200 1.000 20.62161 ? 67  GLY A C   1 
ATOM   2809 O O   . GLY C 1 67  ? 2.84900   15.40000 -22.54700 1.000 18.14851 ? 67  GLY A O   1 
ATOM   2810 N N   . LEU C 1 68  ? 4.98900   14.97300 -21.99400 1.000 19.10675 ? 68  LEU A N   1 
ATOM   2811 C CA  . LEU C 1 68  ? 5.57300   15.81400 -23.03400 1.000 17.85826 ? 68  LEU A CA  1 
ATOM   2812 C C   . LEU C 1 68  ? 6.29000   14.88200 -23.99800 1.000 19.15337 ? 68  LEU A C   1 
ATOM   2813 O O   . LEU C 1 68  ? 7.26500   14.21900 -23.61400 1.000 17.92123 ? 68  LEU A O   1 
ATOM   2814 C CB  . LEU C 1 68  ? 6.50600   16.85700 -22.41700 1.000 17.41984 ? 68  LEU A CB  1 
ATOM   2815 C CG  . LEU C 1 68  ? 5.81600   17.78800 -21.40900 1.000 18.80227 ? 68  LEU A CG  1 
ATOM   2816 C CD1 . LEU C 1 68  ? 6.80900   18.53500 -20.56200 1.000 18.47021 ? 68  LEU A CD1 1 
ATOM   2817 C CD2 . LEU C 1 68  ? 4.89700   18.78600 -22.13100 1.000 20.04676 ? 68  LEU A CD2 1 
ATOM   2818 N N   . HIS C 1 69  ? 5.79000   14.82400 -25.24000 1.000 20.49202 ? 69  HIS A N   1 
ATOM   2819 C CA  . HIS C 1 69  ? 6.16500   13.82700 -26.23300 1.000 19.48526 ? 69  HIS A CA  1 
ATOM   2820 C C   . HIS C 1 69  ? 6.70200   14.49400 -27.49100 1.000 19.35316 ? 69  HIS A C   1 
ATOM   2821 O O   . HIS C 1 69  ? 6.42700   15.65900 -27.76500 1.000 18.19594 ? 69  HIS A O   1 
ATOM   2822 C CB  . HIS C 1 69  ? 4.97400   12.96700 -26.67300 1.000 21.15088 ? 69  HIS A CB  1 
ATOM   2823 C CG  . HIS C 1 69  ? 4.41000   12.09000 -25.60700 1.000 24.53369 ? 69  HIS A CG  1 
ATOM   2824 N ND1 . HIS C 1 69  ? 3.23700   11.39000 -25.77700 1.000 27.27740 ? 69  HIS A ND1 1 
ATOM   2825 C CD2 . HIS C 1 69  ? 4.84600   11.80000 -24.35800 1.000 25.36556 ? 69  HIS A CD2 1 
ATOM   2826 C CE1 . HIS C 1 69  ? 2.97100   10.70600 -24.67600 1.000 27.41206 ? 69  HIS A CE1 1 
ATOM   2827 N NE2 . HIS C 1 69  ? 3.93400   10.93500 -23.80200 1.000 25.84608 ? 69  HIS A NE2 1 
ATOM   2828 N N   . ARG C 1 70  ? 7.44700   13.71600 -28.27200 1.000 21.59210 ? 70  ARG A N   1 
ATOM   2829 C CA  . ARG C 1 70  ? 7.72800   14.07200 -29.65700 1.000 19.97346 ? 70  ARG A CA  1 
ATOM   2830 C C   . ARG C 1 70  ? 6.46000   13.97000 -30.49800 1.000 20.53121 ? 70  ARG A C   1 
ATOM   2831 O O   . ARG C 1 70  ? 5.61500   13.10600 -30.27300 1.000 19.74760 ? 70  ARG A O   1 
ATOM   2832 C CB  . ARG C 1 70  ? 8.77700   13.13600 -30.26200 1.000 22.42753 ? 70  ARG A CB  1 
ATOM   2833 C CG  . ARG C 1 70  ? 10.20200  13.39200 -29.83700 1.000 22.17471 ? 70  ARG A CG  1 
ATOM   2834 C CD  . ARG C 1 70  ? 11.07500  12.15400 -30.11900 1.000 26.37922 ? 70  ARG A CD  1 
ATOM   2835 N NE  . ARG C 1 70  ? 10.61800  10.99400 -29.35900 1.000 35.31376 ? 70  ARG A NE  1 
ATOM   2836 C CZ  . ARG C 1 70  ? 11.03800  9.74800  -29.53900 1.000 38.17291 ? 70  ARG A CZ  1 
ATOM   2837 N NH1 . ARG C 1 70  ? 11.90500  9.43800  -30.49100 1.000 35.87971 ? 70  ARG A NH1 1 
ATOM   2838 N NH2 . ARG C 1 70  ? 10.57600  8.78700  -28.73900 1.000 37.47948 ? 70  ARG A NH2 1 
ATOM   2839 N N   . GLU C 1 71  ? 6.35300   14.84900 -31.49100 1.000 17.70138 ? 71  GLU A N   1 
ATOM   2840 C CA  . GLU C 1 71  ? 5.32300   14.71400 -32.50600 1.000 22.00349 ? 71  GLU A CA  1 
ATOM   2841 C C   . GLU C 1 71  ? 5.52700   13.42700 -33.30900 1.000 22.49839 ? 71  GLU A C   1 
ATOM   2842 O O   . GLU C 1 71  ? 6.62900   12.88600 -33.39000 1.000 19.25838 ? 71  GLU A O   1 
ATOM   2843 C CB  . GLU C 1 71  ? 5.34700   15.91600 -33.45100 1.000 23.28529 ? 71  GLU A CB  1 
ATOM   2844 C CG  . GLU C 1 71  ? 4.89100   17.21700 -32.82500 1.000 23.55009 ? 71  GLU A CG  1 
ATOM   2845 C CD  . GLU C 1 71  ? 5.08300   18.41300 -33.73400 1.000 29.21171 ? 71  GLU A CD  1 
ATOM   2846 O OE1 . GLU C 1 71  ? 5.72000   18.25500 -34.80700 1.000 29.67054 ? 71  GLU A OE1 1 
ATOM   2847 O OE2 . GLU C 1 71  ? 4.60600   19.51300 -33.36500 1.000 25.33478 ? 71  GLU A OE2 1 
ATOM   2848 N N   . GLY C 1 72  ? 4.43800   12.92800 -33.89200 1.000 21.27278 ? 72  GLY A N   1 
ATOM   2849 C CA  . GLY C 1 72  ? 4.51700   11.85900 -34.87500 1.000 20.95720 ? 72  GLY A CA  1 
ATOM   2850 C C   . GLY C 1 72  ? 3.74000   10.59600 -34.55200 1.000 20.82330 ? 72  GLY A C   1 
ATOM   2851 O O   . GLY C 1 72  ? 3.72400   9.69000  -35.39100 1.000 20.70767 ? 72  GLY A O   1 
ATOM   2852 N N   . ARG C 1 73  ? 3.09600   10.45000 -33.39400 1.000 18.82486 ? 73  ARG A N   1 
ATOM   2853 C CA  . ARG C 1 73  ? 2.31100   9.25200  -33.11700 1.000 19.88431 ? 73  ARG A CA  1 
ATOM   2854 C C   . ARG C 1 73  ? 0.83900   9.45800  -33.46900 1.000 19.56847 ? 73  ARG A C   1 
ATOM   2855 O O   . ARG C 1 73  ? 0.33700   10.58500 -33.55500 1.000 18.70693 ? 73  ARG A O   1 
ATOM   2856 C CB  . ARG C 1 73  ? 2.45400   8.83700  -31.64600 1.000 24.22665 ? 73  ARG A CB  1 
ATOM   2857 C CG  . ARG C 1 73  ? 3.91800   8.58100  -31.28800 1.000 28.07430 ? 73  ARG A CG  1 
ATOM   2858 C CD  . ARG C 1 73  ? 4.12200   7.59400  -30.15200 1.000 25.64104 ? 73  ARG A CD  1 
ATOM   2859 N NE  . ARG C 1 73  ? 5.55600   7.42400  -29.92800 1.000 26.24247 ? 73  ARG A NE  1 
ATOM   2860 C CZ  . ARG C 1 73  ? 6.25900   8.16200  -29.08100 1.000 35.34429 ? 73  ARG A CZ  1 
ATOM   2861 N NH1 . ARG C 1 73  ? 5.68200   9.09700  -28.34400 1.000 30.83558 ? 73  ARG A NH1 1 
ATOM   2862 N NH2 . ARG C 1 73  ? 7.57400   7.95300  -28.96700 1.000 30.21038 ? 73  ARG A NH2 1 
ATOM   2863 N N   . SER C 1 74  ? 0.14800   8.34400  -33.68900 1.000 21.05531 ? 74  SER A N   1 
ATOM   2864 C CA  . SER C 1 74  ? -1.25800  8.42200  -34.07400 1.000 19.44025 ? 74  SER A CA  1 
ATOM   2865 C C   . SER C 1 74  ? -2.12300  8.79500  -32.87300 1.000 21.39032 ? 74  SER A C   1 
ATOM   2866 O O   . SER C 1 74  ? -1.77300  8.52900  -31.71800 1.000 19.92554 ? 74  SER A O   1 
ATOM   2867 C CB  . SER C 1 74  ? -1.73000  7.08800  -34.67600 1.000 22.62823 ? 74  SER A CB  1 
ATOM   2868 O OG  . SER C 1 74  ? -1.90300  6.08900  -33.67600 1.000 21.79309 ? 74  SER A OG  1 
ATOM   2869 N N   . ALA C 1 75  ? -3.26300  9.43100  -33.15100 1.000 21.38261 ? 75  ALA A N   1 
ATOM   2870 C CA  . ALA C 1 75  ? -4.22700  9.66900  -32.07900 1.000 22.17242 ? 75  ALA A CA  1 
ATOM   2871 C C   . ALA C 1 75  ? -4.67000  8.35900  -31.44800 1.000 21.77100 ? 75  ALA A C   1 
ATOM   2872 O O   . ALA C 1 75  ? -4.94300  8.30500  -30.23800 1.000 18.51803 ? 75  ALA A O   1 
ATOM   2873 C CB  . ALA C 1 75  ? -5.44300  10.43800 -32.60600 1.000 25.31446 ? 75  ALA A CB  1 
ATOM   2874 N N   . ASP C 1 76  ? -4.74200  7.29300  -32.25100 1.000 20.00944 ? 76  ASP A N   1 
ATOM   2875 C CA  . ASP C 1 76  ? -5.12700  5.98300  -31.73600 1.000 24.03879 ? 76  ASP A CA  1 
ATOM   2876 C C   . ASP C 1 76  ? -4.14000  5.52500  -30.66500 1.000 21.61145 ? 76  ASP A C   1 
ATOM   2877 O O   . ASP C 1 76  ? -4.53000  5.18500  -29.54000 1.000 21.98299 ? 76  ASP A O   1 
ATOM   2878 C CB  . ASP C 1 76  ? -5.17900  4.97500  -32.89300 1.000 24.31818 ? 76  ASP A CB  1 
ATOM   2879 C CG  . ASP C 1 76  ? -5.47700  3.54700  -32.43500 1.000 33.68549 ? 76  ASP A CG  1 
ATOM   2880 O OD1 . ASP C 1 76  ? -5.81300  3.32500  -31.25100 1.000 38.41018 ? 76  ASP A OD1 1 
ATOM   2881 O OD2 . ASP C 1 76  ? -5.34000  2.62700  -33.27200 1.000 41.50022 ? 76  ASP A OD2 1 
ATOM   2882 N N   . LEU C 1 77  ? -2.84800  5.50800  -31.00900 1.000 21.76747 ? 77  LEU A N   1 
ATOM   2883 C CA  . LEU C 1 77  ? -1.81000  5.12200  -30.04900 1.000 23.87600 ? 77  LEU A CA  1 
ATOM   2884 C C   . LEU C 1 77  ? -1.82700  6.01500  -28.81700 1.000 22.59586 ? 77  LEU A C   1 
ATOM   2885 O O   . LEU C 1 77  ? -1.74600  5.52600  -27.68600 1.000 23.46315 ? 77  LEU A O   1 
ATOM   2886 C CB  . LEU C 1 77  ? -0.42900  5.18200  -30.69700 1.000 22.69547 ? 77  LEU A CB  1 
ATOM   2887 C CG  . LEU C 1 77  ? 0.68100   4.32000  -30.05500 1.000 24.93329 ? 77  LEU A CG  1 
ATOM   2888 C CD1 . LEU C 1 77  ? 0.15100   3.03400  -29.42600 1.000 29.33165 ? 77  LEU A CD1 1 
ATOM   2889 C CD2 . LEU C 1 77  ? 1.82500   4.02700  -31.00000 1.000 29.54344 ? 77  LEU A CD2 1 
ATOM   2890 N N   . LYS C 1 78  ? -1.89800  7.33400  -29.01700 1.000 22.74657 ? 78  LYS A N   1 
ATOM   2891 C CA  . LYS C 1 78  ? -1.88900  8.24600  -27.87900 1.000 20.33780 ? 78  LYS A CA  1 
ATOM   2892 C C   . LYS C 1 78  ? -3.08500  7.99600  -26.96600 1.000 22.70192 ? 78  LYS A C   1 
ATOM   2893 O O   . LYS C 1 78  ? -2.96400  8.06300  -25.73900 1.000 19.90080 ? 78  LYS A O   1 
ATOM   2894 C CB  . LYS C 1 78  ? -1.87200  9.69300  -28.36300 1.000 20.09898 ? 78  LYS A CB  1 
ATOM   2895 C CG  . LYS C 1 78  ? -0.48400  10.17400 -28.80300 1.000 19.87279 ? 78  LYS A CG  1 
ATOM   2896 C CD  . LYS C 1 78  ? -0.52600  11.61500 -29.30600 1.000 20.78220 ? 78  LYS A CD  1 
ATOM   2897 C CE  . LYS C 1 78  ? -1.21900  11.70400 -30.67700 1.000 21.62433 ? 78  LYS A CE  1 
ATOM   2898 N NZ  . LYS C 1 78  ? -1.20200  13.06400 -31.28600 1.000 20.20551 ? 78  LYS A NZ  1 
ATOM   2899 N N   . GLY C 1 79  ? -4.24700  7.70000  -27.54500 1.000 21.51807 ? 79  GLY A N   1 
ATOM   2900 C CA  . GLY C 1 79  ? -5.39900  7.36500  -26.72200 1.000 20.93783 ? 79  GLY A CA  1 
ATOM   2901 C C   . GLY C 1 79  ? -5.20500  6.07900  -25.94000 1.000 22.39978 ? 79  GLY A C   1 
ATOM   2902 O O   . GLY C 1 79  ? -5.54900  6.00100  -24.75800 1.000 23.96066 ? 79  GLY A O   1 
ATOM   2903 N N   . GLN C 1 80  ? -4.65300  5.05300  -26.58700 1.000 19.09583 ? 80  GLN A N   1 
ATOM   2904 C CA  . GLN C 1 80  ? -4.31700  3.82900  -25.86600 1.000 25.67336 ? 80  GLN A CA  1 
ATOM   2905 C C   . GLN C 1 80  ? -3.36000  4.10900  -24.71900 1.000 24.25204 ? 80  GLN A C   1 
ATOM   2906 O O   . GLN C 1 80  ? -3.51600  3.55000  -23.62800 1.000 22.62710 ? 80  GLN A O   1 
ATOM   2907 C CB  . GLN C 1 80  ? -3.69100  2.78800  -26.80300 1.000 25.49693 ? 80  GLN A CB  1 
ATOM   2908 C CG  . GLN C 1 80  ? -4.65000  2.06100  -27.73500 1.000 26.74531 ? 80  GLN A CG  1 
ATOM   2909 C CD  . GLN C 1 80  ? -3.89400  1.13000  -28.67100 1.000 38.08404 ? 80  GLN A CD  1 
ATOM   2910 O OE1 . GLN C 1 80  ? -2.99100  0.39600  -28.24300 1.000 35.37894 ? 80  GLN A OE1 1 
ATOM   2911 N NE2 . GLN C 1 80  ? -4.24900  1.16100  -29.95300 1.000 39.99790 ? 80  GLN A NE2 1 
ATOM   2912 N N   . LEU C 1 81  ? -2.35000  4.95500  -24.95400 1.000 21.98215 ? 81  LEU A N   1 
ATOM   2913 C CA  . LEU C 1 81  ? -1.34100  5.22400  -23.92900 1.000 24.04244 ? 81  LEU A CA  1 
ATOM   2914 C C   . LEU C 1 81  ? -1.93000  6.01200  -22.76300 1.000 20.98923 ? 81  LEU A C   1 
ATOM   2915 O O   . LEU C 1 81  ? -1.65600  5.71100  -21.59300 1.000 23.77842 ? 81  LEU A O   1 
ATOM   2916 C CB  . LEU C 1 81  ? -0.16400  5.98100  -24.54200 1.000 20.18812 ? 81  LEU A CB  1 
ATOM   2917 C CG  . LEU C 1 81  ? 0.99800   6.41300  -23.63900 1.000 23.61788 ? 81  LEU A CG  1 
ATOM   2918 C CD1 . LEU C 1 81  ? 1.65900   5.23900  -22.90500 1.000 21.35270 ? 81  LEU A CD1 1 
ATOM   2919 C CD2 . LEU C 1 81  ? 2.04100   7.20500  -24.41500 1.000 21.29961 ? 81  LEU A CD2 1 
ATOM   2920 N N   . ALA C 1 82  ? -2.70800  7.05600  -23.06200 1.000 18.86861 ? 82  ALA A N   1 
ATOM   2921 C CA  . ALA C 1 82  ? -3.35100  7.81400  -21.99200 1.000 20.44123 ? 82  ALA A CA  1 
ATOM   2922 C C   . ALA C 1 82  ? -4.24800  6.92000  -21.14600 1.000 24.31340 ? 82  ALA A C   1 
ATOM   2923 O O   . ALA C 1 82  ? -4.27400  7.04300  -19.91500 1.000 21.81432 ? 82  ALA A O   1 
ATOM   2924 C CB  . ALA C 1 82  ? -4.15300  8.97600  -22.56600 1.000 22.42363 ? 82  ALA A CB  1 
ATOM   2925 N N   . GLN C 1 83  ? -4.99200  6.01600  -21.78700 1.000 21.80155 ? 83  GLN A N   1 
ATOM   2926 C CA  . GLN C 1 83  ? -5.87400  5.12900  -21.03400 1.000 26.88077 ? 83  GLN A CA  1 
ATOM   2927 C C   . GLN C 1 83  ? -5.07300  4.16600  -20.16800 1.000 25.85875 ? 83  GLN A C   1 
ATOM   2928 O O   . GLN C 1 83  ? -5.42500  3.92800  -19.00700 1.000 25.91879 ? 83  GLN A O   1 
ATOM   2929 C CB  . GLN C 1 83  ? -6.79200  4.36500  -21.98800 1.000 25.37308 ? 83  GLN A CB  1 
ATOM   2930 C CG  . GLN C 1 83  ? -7.85100  3.50700  -21.29800 1.000 29.25364 ? 83  GLN A CG  1 
ATOM   2931 C CD  . GLN C 1 83  ? -8.84900  4.33800  -20.50300 1.000 28.33088 ? 83  GLN A CD  1 
ATOM   2932 O OE1 . GLN C 1 83  ? -9.56000  5.17200  -21.06000 1.000 30.13217 ? 83  GLN A OE1 1 
ATOM   2933 N NE2 . GLN C 1 83  ? -8.90200  4.11100  -19.19200 1.000 32.86533 ? 83  GLN A NE2 1 
ATOM   2934 N N   . ARG C 1 84  ? -3.99200  3.60200  -20.71100 1.000 20.96197 ? 84  ARG A N   1 
ATOM   2935 C CA  . ARG C 1 84  ? -3.18100  2.69400  -19.91000 1.000 24.39358 ? 84  ARG A CA  1 
ATOM   2936 C C   . ARG C 1 84  ? -2.55700  3.41000  -18.72300 1.000 23.77581 ? 84  ARG A C   1 
ATOM   2937 O O   . ARG C 1 84  ? -2.41800  2.81800  -17.64200 1.000 27.02842 ? 84  ARG A O   1 
ATOM   2938 C CB  . ARG C 1 84  ? -2.09900  2.04900  -20.77400 1.000 24.48986 ? 84  ARG A CB  1 
ATOM   2939 C CG  . ARG C 1 84  ? -1.07900  1.31900  -19.96100 1.000 29.59600 ? 84  ARG A CG  1 
ATOM   2940 C CD  . ARG C 1 84  ? -0.42500  0.14900  -20.68500 1.000 32.25487 ? 84  ARG A CD  1 
ATOM   2941 N NE  . ARG C 1 84  ? 0.59300   -0.42200 -19.80900 1.000 33.80029 ? 84  ARG A NE  1 
ATOM   2942 C CZ  . ARG C 1 84  ? 1.48800   -1.33200 -20.16700 1.000 33.45614 ? 84  ARG A CZ  1 
ATOM   2943 N NH1 . ARG C 1 84  ? 1.50500   -1.84100 -21.39100 1.000 31.52820 ? 84  ARG A NH1 1 
ATOM   2944 N NH2 . ARG C 1 84  ? 2.39900   -1.72600 -19.27900 1.000 29.95754 ? 84  ARG A NH2 1 
ATOM   2945 N N   . ILE C 1 85  ? -2.21300  4.69100  -18.88600 1.000 23.84790 ? 85  ILE A N   1 
ATOM   2946 C CA  . ILE C 1 85  ? -1.68500  5.46600  -17.76400 1.000 26.45346 ? 85  ILE A CA  1 
ATOM   2947 C C   . ILE C 1 85  ? -2.76000  5.67800  -16.70600 1.000 23.86254 ? 85  ILE A C   1 
ATOM   2948 O O   . ILE C 1 85  ? -2.50600  5.49700  -15.51000 1.000 25.44994 ? 85  ILE A O   1 
ATOM   2949 C CB  . ILE C 1 85  ? -1.09700  6.79600  -18.26100 1.000 21.50110 ? 85  ILE A CB  1 
ATOM   2950 C CG1 . ILE C 1 85  ? 0.21900   6.54200  -18.99500 1.000 22.69886 ? 85  ILE A CG1 1 
ATOM   2951 C CG2 . ILE C 1 85  ? -0.89100  7.76400  -17.09400 1.000 22.26274 ? 85  ILE A CG2 1 
ATOM   2952 C CD1 . ILE C 1 85  ? 0.70700   7.75600  -19.75400 1.000 22.41665 ? 85  ILE A CD1 1 
ATOM   2953 N N   . VAL C 1 86  ? -3.98300  6.03100  -17.11400 1.000 24.29493 ? 86  VAL A N   1 
ATOM   2954 C CA  . VAL C 1 86  ? -5.08100  6.08100  -16.14300 1.000 24.88014 ? 86  VAL A CA  1 
ATOM   2955 C C   . VAL C 1 86  ? -5.22200  4.75500  -15.41000 1.000 27.45707 ? 86  VAL A C   1 
ATOM   2956 O O   . VAL C 1 86  ? -5.30100  4.71500  -14.17200 1.000 24.71028 ? 86  VAL A O   1 
ATOM   2957 C CB  . VAL C 1 86  ? -6.40400  6.48700  -16.81400 1.000 23.94041 ? 86  VAL A CB  1 
ATOM   2958 C CG1 . VAL C 1 86  ? -7.48500  6.59100  -15.75500 1.000 28.17169 ? 86  VAL A CG1 1 
ATOM   2959 C CG2 . VAL C 1 86  ? -6.27700  7.85000  -17.42000 1.000 24.68728 ? 86  VAL A CG2 1 
ATOM   2960 N N   . ASP C 1 87  ? -5.26200  3.64900  -16.15400 1.000 26.36817 ? 87  ASP A N   1 
ATOM   2961 C CA  . ASP C 1 87  ? -5.53800  2.36600  -15.51300 1.000 29.34578 ? 87  ASP A CA  1 
ATOM   2962 C C   . ASP C 1 87  ? -4.39300  1.96200  -14.59900 1.000 27.24407 ? 87  ASP A C   1 
ATOM   2963 O O   . ASP C 1 87  ? -4.60800  1.53000  -13.45900 1.000 27.99408 ? 87  ASP A O   1 
ATOM   2964 C CB  . ASP C 1 87  ? -5.77600  1.27900  -16.55900 1.000 27.47543 ? 87  ASP A CB  1 
ATOM   2965 C CG  . ASP C 1 87  ? -6.99000  1.54800  -17.42200 1.000 33.72551 ? 87  ASP A CG  1 
ATOM   2966 O OD1 . ASP C 1 87  ? -7.84100  2.37500  -17.02800 1.000 35.39871 ? 87  ASP A OD1 1 
ATOM   2967 O OD2 . ASP C 1 87  ? -7.10300  0.90100  -18.48700 1.000 30.65698 ? 87  ASP A OD2 1 
ATOM   2968 N N   . ASP C 1 88  ? -3.16400  2.09800  -15.08000 1.000 27.93603 ? 88  ASP A N   1 
ATOM   2969 C CA  . ASP C 1 88  ? -2.05000  1.54200  -14.34000 1.000 28.73094 ? 88  ASP A CA  1 
ATOM   2970 C C   . ASP C 1 88  ? -1.59000  2.46300  -13.21900 1.000 29.60168 ? 88  ASP A C   1 
ATOM   2971 O O   . ASP C 1 88  ? -1.04300  1.97500  -12.22200 1.000 29.98803 ? 88  ASP A O   1 
ATOM   2972 C CB  . ASP C 1 88  ? -0.91500  1.22300  -15.30400 1.000 30.32841 ? 88  ASP A CB  1 
ATOM   2973 C CG  . ASP C 1 88  ? -1.27000  0.09500  -16.24700 1.000 32.10681 ? 88  ASP A CG  1 
ATOM   2974 O OD1 . ASP C 1 88  ? -2.38100  -0.45100 -16.10500 1.000 32.76162 ? 88  ASP A OD1 1 
ATOM   2975 O OD2 . ASP C 1 88  ? -0.44300  -0.24100 -17.12200 1.000 33.36860 ? 88  ASP A OD2 1 
ATOM   2976 N N   . VAL C 1 89  ? -1.79100  3.78000  -13.34600 1.000 25.89079 ? 89  VAL A N   1 
ATOM   2977 C CA  . VAL C 1 89  ? -1.53000  4.65400  -12.20100 1.000 28.72406 ? 89  VAL A CA  1 
ATOM   2978 C C   . VAL C 1 89  ? -2.58400  4.43900  -11.12100 1.000 28.51368 ? 89  VAL A C   1 
ATOM   2979 O O   . VAL C 1 89  ? -2.27600  4.44400  -9.91800  1.000 26.34881 ? 89  VAL A O   1 
ATOM   2980 C CB  . VAL C 1 89  ? -1.45600  6.13100  -12.63500 1.000 27.39343 ? 89  VAL A CB  1 
ATOM   2981 C CG1 . VAL C 1 89  ? -1.43400  7.04600  -11.41600 1.000 22.28421 ? 89  VAL A CG1 1 
ATOM   2982 C CG2 . VAL C 1 89  ? -0.21500  6.37100  -13.48000 1.000 22.55558 ? 89  VAL A CG2 1 
ATOM   2983 N N   . SER C 1 90  ? -3.83500  4.20900  -11.53000 1.000 25.96569 ? 90  SER A N   1 
ATOM   2984 C CA  . SER C 1 90  ? -4.90400  3.98800  -10.55800 1.000 29.25418 ? 90  SER A CA  1 
ATOM   2985 C C   . SER C 1 90  ? -4.59600  2.78200  -9.67500  1.000 31.17543 ? 90  SER A C   1 
ATOM   2986 O O   . SER C 1 90  ? -4.78700  2.83000  -8.45200  1.000 30.15329 ? 90  SER A O   1 
ATOM   2987 C CB  . SER C 1 90  ? -6.23900  3.81900  -11.28900 1.000 28.38881 ? 90  SER A CB  1 
ATOM   2988 O OG  . SER C 1 90  ? -7.23600  3.25600  -10.45100 1.000 34.48877 ? 90  SER A OG  1 
ATOM   2989 N N   . VAL C 1 91  ? -4.09000  1.70000  -10.27000 1.000 29.87633 ? 91  VAL A N   1 
ATOM   2990 C CA  . VAL C 1 91  ? -3.67400  0.54200  -9.47900  1.000 31.35181 ? 91  VAL A CA  1 
ATOM   2991 C C   . VAL C 1 91  ? -2.44300  0.87900  -8.64600  1.000 31.77852 ? 91  VAL A C   1 
ATOM   2992 O O   . VAL C 1 91  ? -2.42000  0.66500  -7.42600  1.000 28.79465 ? 91  VAL A O   1 
ATOM   2993 C CB  . VAL C 1 91  ? -3.41700  -0.67500 -10.38900 1.000 32.56236 ? 91  VAL A CB  1 
ATOM   2994 C CG1 . VAL C 1 91  ? -2.93200  -1.84400 -9.55400  1.000 33.46721 ? 91  VAL A CG1 1 
ATOM   2995 C CG2 . VAL C 1 91  ? -4.67000  -1.05800 -11.13200 1.000 34.26452 ? 91  VAL A CG2 1 
ATOM   2996 N N   . ALA C 1 92  ? -1.40600  1.42700  -9.29100  1.000 30.12261 ? 92  ALA A N   1 
ATOM   2997 C CA  . ALA C 1 92  ? -0.13200  1.65400  -8.60800  1.000 29.34216 ? 92  ALA A CA  1 
ATOM   2998 C C   . ALA C 1 92  ? -0.27800  2.58900  -7.41200  1.000 27.87402 ? 92  ALA A C   1 
ATOM   2999 O O   . ALA C 1 92  ? 0.31200   2.34900  -6.35200  1.000 31.51371 ? 92  ALA A O   1 
ATOM   3000 C CB  . ALA C 1 92  ? 0.89800   2.21800  -9.58700  1.000 28.85298 ? 92  ALA A CB  1 
ATOM   3001 N N   . ALA C 1 93  ? -1.04000  3.66600  -7.56300  1.000 27.81754 ? 93  ALA A N   1 
ATOM   3002 C CA  . ALA C 1 93  ? -1.24300  4.62200  -6.48700  1.000 28.19317 ? 93  ALA A CA  1 
ATOM   3003 C C   . ALA C 1 93  ? -2.43700  4.29100  -5.59800  1.000 30.16095 ? 93  ALA A C   1 
ATOM   3004 O O   . ALA C 1 93  ? -2.67100  5.00800  -4.61900  1.000 30.94835 ? 93  ALA A O   1 
ATOM   3005 C CB  . ALA C 1 93  ? -1.41200  6.02600  -7.06700  1.000 27.53705 ? 93  ALA A CB  1 
ATOM   3006 N N   . GLU C 1 94  ? -3.18800  3.23300  -5.90800  1.000 29.31488 ? 94  GLU A N   1 
ATOM   3007 C CA  . GLU C 1 94  ? -4.41200  2.87500  -5.18800  1.000 28.96194 ? 94  GLU A CA  1 
ATOM   3008 C C   . GLU C 1 94  ? -5.33000  4.08700  -5.05100  1.000 32.84113 ? 94  GLU A C   1 
ATOM   3009 O O   . GLU C 1 94  ? -5.73900  4.47600  -3.95600  1.000 35.13684 ? 94  GLU A O   1 
ATOM   3010 C CB  . GLU C 1 94  ? -4.08800  2.27300  -3.81300  1.000 32.24220 ? 94  GLU A CB  1 
ATOM   3011 C CG  . GLU C 1 94  ? -2.90700  1.31500  -3.82900  1.000 33.95150 ? 94  GLU A CG  1 
ATOM   3012 C CD  . GLU C 1 94  ? -2.74400  0.54800  -2.52900  1.000 42.70056 ? 94  GLU A CD  1 
ATOM   3013 O OE1 . GLU C 1 94  ? -3.49700  -0.41100 -2.26800  1.000 44.77294 ? 94  GLU A OE1 1 
ATOM   3014 O OE2 . GLU C 1 94  ? -1.83400  0.92500  -1.76200  1.000 45.07374 ? 94  GLU A OE2 1 
ATOM   3015 N N   . ILE C 1 95  ? -5.64500  4.68400  -6.19600  1.000 30.25006 ? 95  ILE A N   1 
ATOM   3016 C CA  . ILE C 1 95  ? -6.46000  5.89200  -6.27900  1.000 33.70408 ? 95  ILE A CA  1 
ATOM   3017 C C   . ILE C 1 95  ? -7.50500  5.67100  -7.36600  1.000 31.65109 ? 95  ILE A C   1 
ATOM   3018 O O   . ILE C 1 95  ? -7.18400  5.11100  -8.41600  1.000 29.65716 ? 95  ILE A O   1 
ATOM   3019 C CB  . ILE C 1 95  ? -5.57500  7.11700  -6.59900  1.000 30.06124 ? 95  ILE A CB  1 
ATOM   3020 C CG1 . ILE C 1 95  ? -4.74100  7.50700  -5.38100  1.000 36.04329 ? 95  ILE A CG1 1 
ATOM   3021 C CG2 . ILE C 1 95  ? -6.41900  8.31100  -6.97300  1.000 31.34618 ? 95  ILE A CG2 1 
ATOM   3022 C CD1 . ILE C 1 95  ? -4.27900  8.96200  -5.38400  1.000 36.29904 ? 95  ILE A CD1 1 
ATOM   3023 N N   . ASP C 1 96  ? -8.75200  6.09700  -7.12000  1.000 28.30903 ? 96  ASP A N   1 
ATOM   3024 C CA  . ASP C 1 96  ? -9.81900  5.93200  -8.11100  1.000 31.74347 ? 96  ASP A CA  1 
ATOM   3025 C C   . ASP C 1 96  ? -9.49600  6.67900  -9.39800  1.000 27.73188 ? 96  ASP A C   1 
ATOM   3026 O O   . ASP C 1 96  ? -8.94400  7.78100  -9.36900  1.000 25.65486 ? 96  ASP A O   1 
ATOM   3027 C CB  . ASP C 1 96  ? -11.15600 6.47600  -7.61200  1.000 31.93674 ? 96  ASP A CB  1 
ATOM   3028 C CG  . ASP C 1 96  ? -12.34300 5.88100  -8.37200  1.000 41.87065 ? 96  ASP A CG  1 
ATOM   3029 O OD1 . ASP C 1 96  ? -12.78300 4.76400  -8.01800  1.000 50.87869 ? 96  ASP A OD1 1 
ATOM   3030 O OD2 . ASP C 1 96  ? -12.75100 6.46200  -9.41000  1.000 39.29192 ? 96  ASP A OD2 1 
ATOM   3031 N N   . ARG C 1 97  ? -9.91400  6.09300  -10.53400 1.000 26.40037 ? 97  ARG A N   1 
ATOM   3032 C CA  . ARG C 1 97  ? -9.64800  6.69900  -11.84200 1.000 27.24827 ? 97  ARG A CA  1 
ATOM   3033 C C   . ARG C 1 97  ? -10.26600 8.08100  -11.97000 1.000 25.81691 ? 97  ARG A C   1 
ATOM   3034 O O   . ARG C 1 97  ? -9.79300  8.89700  -12.76600 1.000 23.13604 ? 97  ARG A O   1 
ATOM   3035 C CB  . ARG C 1 97  ? -10.19000 5.82100  -12.97600 1.000 26.84583 ? 97  ARG A CB  1 
ATOM   3036 C CG  . ARG C 1 97  ? -9.37000  4.58600  -13.29300 1.000 33.21630 ? 97  ARG A CG  1 
ATOM   3037 C CD  . ARG C 1 97  ? -10.15900 3.68100  -14.23800 1.000 38.87341 ? 97  ARG A CD  1 
ATOM   3038 N NE  . ARG C 1 97  ? -10.48800 2.41100  -13.60400 1.000 47.84940 ? 97  ARG A NE  1 
ATOM   3039 C CZ  . ARG C 1 97  ? -11.31600 1.50800  -14.11600 1.000 54.17070 ? 97  ARG A CZ  1 
ATOM   3040 N NH1 . ARG C 1 97  ? -11.96200 1.72500  -15.25400 1.000 45.94790 ? 97  ARG A NH1 1 
ATOM   3041 N NH2 . ARG C 1 97  ? -11.52900 0.37300  -13.45200 1.000 50.77585 ? 97  ARG A NH2 1 
ATOM   3042 N N   . LYS C 1 98  ? -11.34700 8.34800  -11.23700 1.000 24.38419 ? 98  LYS A N   1 
ATOM   3043 C CA  . LYS C 1 98  ? -11.99800 9.64800  -11.32300 1.000 26.23287 ? 98  LYS A CA  1 
ATOM   3044 C C   . LYS C 1 98  ? -11.09400 10.77000 -10.84700 1.000 24.03298 ? 98  LYS A C   1 
ATOM   3045 O O   . LYS C 1 98  ? -11.38200 11.93400 -11.13200 1.000 24.27432 ? 98  LYS A O   1 
ATOM   3046 C CB  . LYS C 1 98  ? -13.29300 9.67300  -10.51400 1.000 27.02663 ? 98  LYS A CB  1 
ATOM   3047 C CG  . LYS C 1 98  ? -13.07300 9.50200  -9.01000  1.000 34.77653 ? 98  LYS A CG  1 
ATOM   3048 C CD  . LYS C 1 98  ? -14.33200 8.96700  -8.31400  1.000 31.89391 ? 98  LYS A CD  1 
ATOM   3049 C CE  . LYS C 1 98  ? -14.23400 9.07800  -6.79700  1.000 36.65246 ? 98  LYS A CE  1 
ATOM   3050 N NZ  . LYS C 1 98  ? -14.85900 7.90900  -6.10400  1.000 42.58162 ? 98  LYS A NZ  1 
ATOM   3051 N N   . HIS C 1 99  ? -10.02900 10.45000 -10.11300 1.000 22.39719 ? 99  HIS A N   1 
ATOM   3052 C CA  . HIS C 1 99  ? -9.11500  11.45900 -9.60800  1.000 25.36677 ? 99  HIS A CA  1 
ATOM   3053 C C   . HIS C 1 99  ? -7.97800  11.78100 -10.56800 1.000 22.41101 ? 99  HIS A C   1 
ATOM   3054 O O   . HIS C 1 99  ? -7.13600  12.62800 -10.24500 1.000 20.55522 ? 99  HIS A O   1 
ATOM   3055 C CB  . HIS C 1 99  ? -8.52200  11.02300 -8.26500  1.000 24.33226 ? 99  HIS A CB  1 
ATOM   3056 C CG  . HIS C 1 99  ? -9.53900  10.87700 -7.17800  1.000 26.74662 ? 99  HIS A CG  1 
ATOM   3057 N ND1 . HIS C 1 99  ? -10.28700 11.93600 -6.71500  1.000 30.36945 ? 99  HIS A ND1 1 
ATOM   3058 C CD2 . HIS C 1 99  ? -9.88800  9.81100  -6.41800  1.000 34.32043 ? 99  HIS A CD2 1 
ATOM   3059 C CE1 . HIS C 1 99  ? -11.08100 11.52300 -5.74200  1.000 34.17674 ? 99  HIS A CE1 1 
ATOM   3060 N NE2 . HIS C 1 99  ? -10.85700 10.23600 -5.54100  1.000 31.00272 ? 99  HIS A NE2 1 
ATOM   3061 N N   . ILE C 1 100 ? -7.91100  11.13400 -11.72500 1.000 21.12128 ? 100 ILE A N   1 
ATOM   3062 C CA  . ILE C 1 100 ? -6.69900  11.14100 -12.53600 1.000 19.11446 ? 100 ILE A CA  1 
ATOM   3063 C C   . ILE C 1 100 ? -6.95600  11.93100 -13.81100 1.000 20.84274 ? 100 ILE A C   1 
ATOM   3064 O O   . ILE C 1 100 ? -7.91000  11.65200 -14.54800 1.000 21.68003 ? 100 ILE A O   1 
ATOM   3065 C CB  . ILE C 1 100 ? -6.23200  9.71300  -12.85800 1.000 23.54153 ? 100 ILE A CB  1 
ATOM   3066 C CG1 . ILE C 1 100 ? -6.05800  8.92000  -11.55800 1.000 21.95696 ? 100 ILE A CG1 1 
ATOM   3067 C CG2 . ILE C 1 100 ? -4.91900  9.76100  -13.70200 1.000 19.19073 ? 100 ILE A CG2 1 
ATOM   3068 C CD1 . ILE C 1 100 ? -5.52800  7.51100  -11.76700 1.000 27.13258 ? 100 ILE A CD1 1 
ATOM   3069 N N   . TRP C 1 101 ? -6.10900  12.92100 -14.05900 1.000 22.52934 ? 101 TRP A N   1 
ATOM   3070 C CA  . TRP C 1 101 ? -6.13800  13.71500 -15.27500 1.000 22.16984 ? 101 TRP A CA  1 
ATOM   3071 C C   . TRP C 1 101 ? -4.83700  13.49200 -16.04300 1.000 19.71000 ? 101 TRP A C   1 
ATOM   3072 O O   . TRP C 1 101 ? -3.75500  13.45500 -15.44800 1.000 16.85229 ? 101 TRP A O   1 
ATOM   3073 C CB  . TRP C 1 101 ? -6.31800  15.19500 -14.92700 1.000 21.05893 ? 101 TRP A CB  1 
ATOM   3074 C CG  . TRP C 1 101 ? -7.58300  15.56200 -14.14000 1.000 19.30465 ? 101 TRP A CG  1 
ATOM   3075 C CD1 . TRP C 1 101 ? -8.11400  14.91500 -13.04800 1.000 22.35518 ? 101 TRP A CD1 1 
ATOM   3076 C CD2 . TRP C 1 101 ? -8.41500  16.69600 -14.37100 1.000 19.09126 ? 101 TRP A CD2 1 
ATOM   3077 N NE1 . TRP C 1 101 ? -9.24300  15.57400 -12.60600 1.000 21.05660 ? 101 TRP A NE1 1 
ATOM   3078 C CE2 . TRP C 1 101 ? -9.44500  16.67100 -13.40400 1.000 21.45860 ? 101 TRP A CE2 1 
ATOM   3079 C CE3 . TRP C 1 101 ? -8.39300  17.73600 -15.31200 1.000 20.26463 ? 101 TRP A CE3 1 
ATOM   3080 C CZ2 . TRP C 1 101 ? -10.44000 17.64200 -13.35100 1.000 22.59977 ? 101 TRP A CZ2 1 
ATOM   3081 C CZ3 . TRP C 1 101 ? -9.38400  18.70700 -15.25500 1.000 22.31734 ? 101 TRP A CZ3 1 
ATOM   3082 C CH2 . TRP C 1 101 ? -10.40200 18.64400 -14.29300 1.000 23.78558 ? 101 TRP A CH2 1 
ATOM   3083 N N   . VAL C 1 102 ? -4.92400  13.34400 -17.36600 1.000 19.41041 ? 102 VAL A N   1 
ATOM   3084 C CA  . VAL C 1 102 ? -3.75800  13.01900 -18.19100 1.000 17.96284 ? 102 VAL A CA  1 
ATOM   3085 C C   . VAL C 1 102 ? -3.85500  13.83300 -19.47200 1.000 17.68580 ? 102 VAL A C   1 
ATOM   3086 O O   . VAL C 1 102 ? -4.78700  13.63100 -20.25500 1.000 17.33037 ? 102 VAL A O   1 
ATOM   3087 C CB  . VAL C 1 102 ? -3.68200  11.52100 -18.54500 1.000 21.30665 ? 102 VAL A CB  1 
ATOM   3088 C CG1 . VAL C 1 102 ? -2.48400  11.25200 -19.45500 1.000 23.10463 ? 102 VAL A CG1 1 
ATOM   3089 C CG2 . VAL C 1 102 ? -3.60700  10.65700 -17.29400 1.000 23.22653 ? 102 VAL A CG2 1 
ATOM   3090 N N   . TYR C 1 103 ? -2.91600  14.75800 -19.68000 1.000 15.99335 ? 103 TYR A N   1 
ATOM   3091 C CA  . TYR C 1 103 ? -2.80100  15.51300 -20.92800 1.000 18.83098 ? 103 TYR A CA  1 
ATOM   3092 C C   . TYR C 1 103 ? -1.45900  15.21700 -21.59300 1.000 18.29470 ? 103 TYR A C   1 
ATOM   3093 O O   . TYR C 1 103 ? -0.41700  15.23800 -20.93000 1.000 16.89445 ? 103 TYR A O   1 
ATOM   3094 C CB  . TYR C 1 103 ? -2.87300  17.03400 -20.69700 1.000 16.63266 ? 103 TYR A CB  1 
ATOM   3095 C CG  . TYR C 1 103 ? -4.18300  17.59700 -20.19200 1.000 17.91706 ? 103 TYR A CG  1 
ATOM   3096 C CD1 . TYR C 1 103 ? -5.30600  16.78900 -20.02300 1.000 18.84724 ? 103 TYR A CD1 1 
ATOM   3097 C CD2 . TYR C 1 103 ? -4.29800  18.95800 -19.89300 1.000 18.98483 ? 103 TYR A CD2 1 
ATOM   3098 C CE1 . TYR C 1 103 ? -6.50700  17.31300 -19.55500 1.000 16.36632 ? 103 TYR A CE1 1 
ATOM   3099 C CE2 . TYR C 1 103 ? -5.50600  19.49600 -19.43900 1.000 18.54639 ? 103 TYR A CE2 1 
ATOM   3100 C CZ  . TYR C 1 103 ? -6.61100  18.66000 -19.27700 1.000 21.20669 ? 103 TYR A CZ  1 
ATOM   3101 O OH  . TYR C 1 103 ? -7.80900  19.16700 -18.80100 1.000 19.17036 ? 103 TYR A OH  1 
ATOM   3102 N N   . PHE C 1 104 ? -1.46900  15.01000 -22.90800 1.000 18.29068 ? 104 PHE A N   1 
ATOM   3103 C CA  . PHE C 1 104 ? -0.23400  14.88400 -23.68500 1.000 18.99531 ? 104 PHE A CA  1 
ATOM   3104 C C   . PHE C 1 104 ? 0.00300   16.13400 -24.52400 1.000 18.44344 ? 104 PHE A C   1 
ATOM   3105 O O   . PHE C 1 104 ? -0.86800  16.54300 -25.29900 1.000 19.15546 ? 104 PHE A O   1 
ATOM   3106 C CB  . PHE C 1 104 ? -0.26400  13.66400 -24.60900 1.000 19.37928 ? 104 PHE A CB  1 
ATOM   3107 C CG  . PHE C 1 104 ? -0.30400  12.34600 -23.88800 1.000 21.88951 ? 104 PHE A CG  1 
ATOM   3108 C CD1 . PHE C 1 104 ? 0.13400   12.22900 -22.57600 1.000 20.17641 ? 104 PHE A CD1 1 
ATOM   3109 C CD2 . PHE C 1 104 ? -0.81600  11.22400 -24.51500 1.000 23.54500 ? 104 PHE A CD2 1 
ATOM   3110 C CE1 . PHE C 1 104 ? 0.08000   11.02000 -21.92400 1.000 20.08560 ? 104 PHE A CE1 1 
ATOM   3111 C CE2 . PHE C 1 104 ? -0.87200  10.00900 -23.85600 1.000 21.98917 ? 104 PHE A CE2 1 
ATOM   3112 C CZ  . PHE C 1 104 ? -0.41700  9.90800  -22.56400 1.000 18.81719 ? 104 PHE A CZ  1 
ATOM   3113 N N   . GLY C 1 105 ? 1.19500   16.71600 -24.39600 1.000 20.91936 ? 105 GLY A N   1 
ATOM   3114 C CA  . GLY C 1 105 ? 1.68000   17.71200 -25.33800 1.000 19.14182 ? 105 GLY A CA  1 
ATOM   3115 C C   . GLY C 1 105 ? 2.74500   17.12400 -26.24500 1.000 21.80039 ? 105 GLY A C   1 
ATOM   3116 O O   . GLY C 1 105 ? 3.46800   16.20600 -25.85400 1.000 20.40874 ? 105 GLY A O   1 
ATOM   3117 N N   . GLU C 1 106 ? 2.83300   17.64700 -27.47500 1.000 19.45683 ? 106 GLU A N   1 
ATOM   3118 C CA  . GLU C 1 106 ? 3.77600   17.14100 -28.46300 1.000 18.93000 ? 106 GLU A CA  1 
ATOM   3119 C C   . GLU C 1 106 ? 4.60700   18.27700 -29.04100 1.000 21.33048 ? 106 GLU A C   1 
ATOM   3120 O O   . GLU C 1 106 ? 4.13900   19.41100 -29.15800 1.000 19.51114 ? 106 GLU A O   1 
ATOM   3121 C CB  . GLU C 1 106 ? 3.08100   16.42300 -29.64100 1.000 22.47372 ? 106 GLU A CB  1 
ATOM   3122 C CG  . GLU C 1 106 ? 2.20900   15.26000 -29.26000 1.000 19.74820 ? 106 GLU A CG  1 
ATOM   3123 C CD  . GLU C 1 106 ? 1.23000   14.92500 -30.35900 1.000 22.12111 ? 106 GLU A CD  1 
ATOM   3124 O OE1 . GLU C 1 106 ? 0.14200   15.53200 -30.39600 1.000 21.76010 ? 106 GLU A OE1 1 
ATOM   3125 O OE2 . GLU C 1 106 ? 1.56600   14.05200 -31.19600 1.000 21.30265 ? 106 GLU A OE2 1 
ATOM   3126 N N   . MET C 1 107 ? 5.81800   17.93900 -29.48800 1.000 18.78589 ? 107 MET A N   1 
ATOM   3127 C CA  . MET C 1 107 ? 6.76700   18.95300 -29.90100 1.000 16.54501 ? 107 MET A CA  1 
ATOM   3128 C C   . MET C 1 107 ? 7.61300   18.32400 -31.00700 1.000 18.41461 ? 107 MET A C   1 
ATOM   3129 O O   . MET C 1 107 ? 7.80000   17.10100 -31.00900 1.000 19.93350 ? 107 MET A O   1 
ATOM   3130 C CB  . MET C 1 107 ? 7.60800   19.28200 -28.66800 1.000 24.89256 ? 107 MET A CB  1 
ATOM   3131 C CG  . MET C 1 107 ? 7.11500   20.46700 -27.89100 1.000 21.84932 ? 107 MET A CG  1 
ATOM   3132 S SD  . MET C 1 107 ? 7.90200   20.23000 -26.27700 1.000 22.33557 ? 107 MET A SD  1 
ATOM   3133 C CE  . MET C 1 107 ? 7.05800   18.78300 -25.68800 1.000 21.81716 ? 107 MET A CE  1 
ATOM   3134 N N   . PRO C 1 108 ? 8.12900   19.10600 -31.95400 1.000 21.13964 ? 108 PRO A N   1 
ATOM   3135 C CA  . PRO C 1 108 ? 9.06000   18.52500 -32.93400 1.000 23.21105 ? 108 PRO A CA  1 
ATOM   3136 C C   . PRO C 1 108 ? 10.29600  17.96300 -32.24300 1.000 21.36827 ? 108 PRO A C   1 
ATOM   3137 O O   . PRO C 1 108 ? 10.85600  18.58500 -31.34000 1.000 20.86576 ? 108 PRO A O   1 
ATOM   3138 C CB  . PRO C 1 108 ? 9.40300   19.71100 -33.84300 1.000 21.83209 ? 108 PRO A CB  1 
ATOM   3139 C CG  . PRO C 1 108 ? 8.21600   20.62900 -33.72200 1.000 23.60683 ? 108 PRO A CG  1 
ATOM   3140 C CD  . PRO C 1 108 ? 7.78200   20.49800 -32.28700 1.000 21.97261 ? 108 PRO A CD  1 
ATOM   3141 N N   . ALA C 1 109 ? 10.69900  16.75400 -32.65200 1.000 21.21064 ? 109 ALA A N   1 
ATOM   3142 C CA  . ALA C 1 109 ? 11.87300  16.12900 -32.04500 1.000 23.39472 ? 109 ALA A CA  1 
ATOM   3143 C C   . ALA C 1 109 ? 13.09500  17.04300 -32.09600 1.000 22.84097 ? 109 ALA A C   1 
ATOM   3144 O O   . ALA C 1 109 ? 13.95700  16.98100 -31.21000 1.000 21.63425 ? 109 ALA A O   1 
ATOM   3145 C CB  . ALA C 1 109 ? 12.18100  14.79700 -32.73600 1.000 27.95690 ? 109 ALA A CB  1 
ATOM   3146 N N   . GLN C 1 110 ? 13.16200  17.93100 -33.09100 1.000 23.26317 ? 110 GLN A N   1 
ATOM   3147 C CA  . GLN C 1 110 ? 14.34100  18.76700 -33.28200 1.000 21.90104 ? 110 GLN A CA  1 
ATOM   3148 C C   . GLN C 1 110 ? 14.48500  19.87700 -32.23800 1.000 23.54843 ? 110 GLN A C   1 
ATOM   3149 O O   . GLN C 1 110 ? 15.53500  20.52100 -32.19600 1.000 21.37362 ? 110 GLN A O   1 
ATOM   3150 C CB  . GLN C 1 110 ? 14.33300  19.34900 -34.70300 1.000 19.39156 ? 110 GLN A CB  1 
ATOM   3151 C CG  . GLN C 1 110 ? 14.56800  18.24900 -35.74900 1.000 26.16534 ? 110 GLN A CG  1 
ATOM   3152 C CD  . GLN C 1 110 ? 13.30500  17.47400 -36.15500 1.000 31.67487 ? 110 GLN A CD  1 
ATOM   3153 O OE1 . GLN C 1 110 ? 12.16700  17.80500 -35.76800 1.000 28.70434 ? 110 GLN A OE1 1 
ATOM   3154 N NE2 . GLN C 1 110 ? 13.51900  16.38200 -36.87700 1.000 37.83254 ? 110 GLN A NE2 1 
ATOM   3155 N N   . GLN C 1 111 ? 13.48300  20.12200 -31.39300 1.000 24.25207 ? 111 GLN A N   1 
ATOM   3156 C CA  . GLN C 1 111 ? 13.61700  21.07700 -30.29600 1.000 21.41751 ? 111 GLN A CA  1 
ATOM   3157 C C   . GLN C 1 111 ? 13.47100  20.37400 -28.95200 1.000 21.90658 ? 111 GLN A C   1 
ATOM   3158 O O   . GLN C 1 111 ? 12.91600  20.92700 -27.99000 1.000 20.74976 ? 111 GLN A O   1 
ATOM   3159 C CB  . GLN C 1 111 ? 12.60400  22.21500 -30.42900 1.000 19.48296 ? 111 GLN A CB  1 
ATOM   3160 C CG  . GLN C 1 111 ? 11.15800  21.78000 -30.41200 1.000 18.46329 ? 111 GLN A CG  1 
ATOM   3161 C CD  . GLN C 1 111 ? 10.26700  22.78800 -31.11100 1.000 21.13324 ? 111 GLN A CD  1 
ATOM   3162 O OE1 . GLN C 1 111 ? 10.49700  23.12100 -32.27000 1.000 18.97593 ? 111 GLN A OE1 1 
ATOM   3163 N NE2 . GLN C 1 111 ? 9.27400   23.31200 -30.39000 1.000 19.98521 ? 111 GLN A NE2 1 
ATOM   3164 N N   . MET C 1 112 ? 13.97300  19.13600 -28.88000 1.000 19.83937 ? 112 MET A N   1 
ATOM   3165 C CA  . MET C 1 112 ? 13.74900  18.26200 -27.73300 1.000 22.74255 ? 112 MET A CA  1 
ATOM   3166 C C   . MET C 1 112 ? 15.07600  17.56100 -27.44000 1.000 23.77902 ? 112 MET A C   1 
ATOM   3167 O O   . MET C 1 112 ? 15.64500  16.92200 -28.33800 1.000 21.61434 ? 112 MET A O   1 
ATOM   3168 C CB  . MET C 1 112 ? 12.66100  17.24100 -28.06300 1.000 20.37181 ? 112 MET A CB  1 
ATOM   3169 C CG  . MET C 1 112 ? 11.25600  17.80000 -27.86300 1.000 22.69519 ? 112 MET A CG  1 
ATOM   3170 S SD  . MET C 1 112 ? 9.99800   16.55900 -28.16700 1.000 21.82152 ? 112 MET A SD  1 
ATOM   3171 C CE  . MET C 1 112 ? 10.04300  15.60900 -26.64700 1.000 20.83358 ? 112 MET A CE  1 
ATOM   3172 N N   . VAL C 1 113 ? 15.55800  17.68600 -26.20000 1.000 19.83460 ? 113 VAL A N   1 
ATOM   3173 C CA  . VAL C 1 113 ? 16.88200  17.22500 -25.76900 1.000 22.56680 ? 113 VAL A CA  1 
ATOM   3174 C C   . VAL C 1 113 ? 16.70900  16.34900 -24.52500 1.000 22.78906 ? 113 VAL A C   1 
ATOM   3175 O O   . VAL C 1 113 ? 16.17900  16.82200 -23.51300 1.000 19.75559 ? 113 VAL A O   1 
ATOM   3176 C CB  . VAL C 1 113 ? 17.81000  18.41400 -25.44700 1.000 23.36924 ? 113 VAL A CB  1 
ATOM   3177 C CG1 . VAL C 1 113 ? 19.11000  17.93300 -24.81900 1.000 21.12385 ? 113 VAL A CG1 1 
ATOM   3178 C CG2 . VAL C 1 113 ? 18.09800  19.26900 -26.69500 1.000 22.19371 ? 113 VAL A CG2 1 
ATOM   3179 N N   . ASP C 1 114 ? 17.13200  15.07800 -24.60300 1.000 22.62918 ? 114 ASP A N   1 
ATOM   3180 C CA  . ASP C 1 114 ? 17.26600  14.19400 -23.44000 1.000 21.51696 ? 114 ASP A CA  1 
ATOM   3181 C C   . ASP C 1 114 ? 18.74400  13.88900 -23.22500 1.000 24.35260 ? 114 ASP A C   1 
ATOM   3182 O O   . ASP C 1 114 ? 19.45800  13.59200 -24.18500 1.000 23.04072 ? 114 ASP A O   1 
ATOM   3183 C CB  . ASP C 1 114 ? 16.55100  12.83700 -23.61400 1.000 22.13543 ? 114 ASP A CB  1 
ATOM   3184 C CG  . ASP C 1 114 ? 15.05700  12.94400 -23.80900 1.000 24.62495 ? 114 ASP A CG  1 
ATOM   3185 O OD1 . ASP C 1 114 ? 14.51600  14.05600 -23.85500 1.000 20.19494 ? 114 ASP A OD1 1 
ATOM   3186 O OD2 . ASP C 1 114 ? 14.41200  11.87200 -23.88300 1.000 25.79839 ? 114 ASP A OD2 1 
ATOM   3187 N N   . TYR C 1 115 ? 19.20100  13.90800 -21.96500 1.000 21.75494 ? 115 TYR A N   1 
ATOM   3188 C CA  . TYR C 1 115 ? 20.59800  13.55600 -21.66200 1.000 22.68693 ? 115 TYR A CA  1 
ATOM   3189 C C   . TYR C 1 115 ? 21.56900  14.44100 -22.43900 1.000 24.63933 ? 115 TYR A C   1 
ATOM   3190 O O   . TYR C 1 115 ? 22.66200  14.00900 -22.83000 1.000 21.55081 ? 115 TYR A O   1 
ATOM   3191 C CB  . TYR C 1 115 ? 20.88700  12.07800 -21.96600 1.000 22.88802 ? 115 TYR A CB  1 
ATOM   3192 C CG  . TYR C 1 115 ? 20.14300  11.07900 -21.10400 1.000 25.34150 ? 115 TYR A CG  1 
ATOM   3193 C CD1 . TYR C 1 115 ? 20.59200  10.76100 -19.82600 1.000 25.65173 ? 115 TYR A CD1 1 
ATOM   3194 C CD2 . TYR C 1 115 ? 18.99700  10.44500 -21.56500 1.000 27.10254 ? 115 TYR A CD2 1 
ATOM   3195 C CE1 . TYR C 1 115 ? 19.92600  9.83900  -19.03800 1.000 27.82060 ? 115 TYR A CE1 1 
ATOM   3196 C CE2 . TYR C 1 115 ? 18.31700  9.53300  -20.78200 1.000 27.62993 ? 115 TYR A CE2 1 
ATOM   3197 C CZ  . TYR C 1 115 ? 18.78400  9.23300  -19.51700 1.000 28.22875 ? 115 TYR A CZ  1 
ATOM   3198 O OH  . TYR C 1 115 ? 18.12200  8.30900  -18.74100 1.000 30.80541 ? 115 TYR A OH  1 
ATOM   3199 N N   . GLY C 1 116 ? 21.16000  15.67700 -22.71200 1.000 23.36132 ? 116 GLY A N   1 
ATOM   3200 C CA  . GLY C 1 116 ? 22.00500  16.59700 -23.42400 1.000 21.20186 ? 116 GLY A CA  1 
ATOM   3201 C C   . GLY C 1 116 ? 22.12500  16.33200 -24.90700 1.000 23.10572 ? 116 GLY A C   1 
ATOM   3202 O O   . GLY C 1 116 ? 22.97300  16.94300 -25.55600 1.000 26.07163 ? 116 GLY A O   1 
ATOM   3203 N N   . ARG C 1 117 ? 21.29600  15.44500 -25.47000 1.000 22.48284 ? 117 ARG A N   1 
ATOM   3204 C CA  . ARG C 1 117 ? 21.34100  15.13400 -26.89700 1.000 27.23921 ? 117 ARG A CA  1 
ATOM   3205 C C   . ARG C 1 117 ? 19.96900  15.30000 -27.52700 1.000 23.08913 ? 117 ARG A C   1 
ATOM   3206 O O   . ARG C 1 117 ? 18.94900  15.01600 -26.90000 1.000 23.25507 ? 117 ARG A O   1 
ATOM   3207 C CB  . ARG C 1 117 ? 21.84300  13.70400 -27.14300 1.000 28.03194 ? 117 ARG A CB  1 
ATOM   3208 C CG  . ARG C 1 117 ? 23.14300  13.41100 -26.44800 1.000 26.40001 ? 117 ARG A CG  1 
ATOM   3209 C CD  . ARG C 1 117 ? 24.26400  14.04900 -27.20100 1.000 30.91243 ? 117 ARG A CD  1 
ATOM   3210 N NE  . ARG C 1 117 ? 24.17900  13.74000 -28.62500 1.000 39.96254 ? 117 ARG A NE  1 
ATOM   3211 C CZ  . ARG C 1 117 ? 25.06000  12.99000 -29.27300 1.000 36.40973 ? 117 ARG A CZ  1 
ATOM   3212 N NH1 . ARG C 1 117 ? 26.04900  12.38300 -28.63800 1.000 38.96101 ? 117 ARG A NH1 1 
ATOM   3213 N NH2 . ARG C 1 117 ? 24.93300  12.82900 -30.58800 1.000 40.24551 ? 117 ARG A NH2 1 
ATOM   3214 N N   . PHE C 1 118 ? 19.95000  15.73000 -28.78400 1.000 25.12402 ? 118 PHE A N   1 
ATOM   3215 C CA  . PHE C 1 118 ? 18.68000  15.87800 -29.47800 1.000 20.92756 ? 118 PHE A CA  1 
ATOM   3216 C C   . PHE C 1 118 ? 18.07300  14.52100 -29.79500 1.000 26.37189 ? 118 PHE A C   1 
ATOM   3217 O O   . PHE C 1 118 ? 18.76400  13.59100 -30.22000 1.000 25.19471 ? 118 PHE A O   1 
ATOM   3218 C CB  . PHE C 1 118 ? 18.85500  16.68700 -30.75800 1.000 24.49348 ? 118 PHE A CB  1 
ATOM   3219 C CG  . PHE C 1 118 ? 19.03400  18.15100 -30.51700 1.000 23.67244 ? 118 PHE A CG  1 
ATOM   3220 C CD1 . PHE C 1 118 ? 17.93500  18.98100 -30.40200 1.000 19.78529 ? 118 PHE A CD1 1 
ATOM   3221 C CD2 . PHE C 1 118 ? 20.30200  18.70200 -30.39700 1.000 25.26531 ? 118 PHE A CD2 1 
ATOM   3222 C CE1 . PHE C 1 118 ? 18.09100  20.33200 -30.17600 1.000 19.13766 ? 118 PHE A CE1 1 
ATOM   3223 C CE2 . PHE C 1 118 ? 20.45600  20.04400 -30.16600 1.000 25.91629 ? 118 PHE A CE2 1 
ATOM   3224 C CZ  . PHE C 1 118 ? 19.35400  20.86500 -30.05600 1.000 22.06390 ? 118 PHE A CZ  1 
ATOM   3225 N N   . LEU C 1 119 ? 16.75800  14.42800 -29.61000 1.000 21.06241 ? 119 LEU A N   1 
ATOM   3226 C CA  . LEU C 1 119 ? 16.02900  13.20100 -29.85700 1.000 26.95085 ? 119 LEU A CA  1 
ATOM   3227 C C   . LEU C 1 119 ? 15.88700  12.92200 -31.35300 1.000 26.80872 ? 119 LEU A C   1 
ATOM   3228 O O   . LEU C 1 119 ? 15.90600  13.84700 -32.17600 1.000 26.14676 ? 119 LEU A O   1 
ATOM   3229 C CB  . LEU C 1 119 ? 14.63600  13.28300 -29.24100 1.000 25.16437 ? 119 LEU A CB  1 
ATOM   3230 C CG  . LEU C 1 119 ? 14.58800  13.30500 -27.71800 1.000 23.14008 ? 119 LEU A CG  1 
ATOM   3231 C CD1 . LEU C 1 119 ? 13.14400  13.44100 -27.28900 1.000 25.19568 ? 119 LEU A CD1 1 
ATOM   3232 C CD2 . LEU C 1 119 ? 15.20900  12.04200 -27.14800 1.000 28.19106 ? 119 LEU A CD2 1 
ATOM   3233 N N   . PRO C 1 120 ? 15.70900  11.64700 -31.72300 1.000 26.39973 ? 120 PRO A N   1 
ATOM   3234 C CA  . PRO C 1 120 ? 15.39600  11.30400 -33.11100 1.000 31.27815 ? 120 PRO A CA  1 
ATOM   3235 C C   . PRO C 1 120 ? 13.89800  11.25600 -33.31200 1.000 32.83060 ? 120 PRO A C   1 
ATOM   3236 O O   . PRO C 1 120 ? 13.14700  11.42600 -32.35100 1.000 29.51386 ? 120 PRO A O   1 
ATOM   3237 C CB  . PRO C 1 120 ? 15.99800  9.90700  -33.26300 1.000 31.51420 ? 120 PRO A CB  1 
ATOM   3238 C CG  . PRO C 1 120 ? 15.85900  9.30400  -31.88500 1.000 35.56754 ? 120 PRO A CG  1 
ATOM   3239 C CD  . PRO C 1 120 ? 15.70700  10.44400 -30.87200 1.000 32.96649 ? 120 PRO A CD  1 
ATOM   3240 N N   . GLN C 1 121 ? 13.44400  10.96100 -34.52600 1.000 37.98328 ? 121 GLN A N   1 
ATOM   3241 C CA  . GLN C 1 121 ? 12.01600  10.78400 -34.72400 1.000 35.98042 ? 121 GLN A CA  1 
ATOM   3242 C C   . GLN C 1 121 ? 11.55900  9.45400  -34.12500 1.000 38.74040 ? 121 GLN A C   1 
ATOM   3243 O O   . GLN C 1 121 ? 12.36100  8.52500  -33.98500 1.000 35.14567 ? 121 GLN A O   1 
ATOM   3244 C CB  . GLN C 1 121 ? 11.67400  10.86200 -36.20600 1.000 42.15577 ? 121 GLN A CB  1 
ATOM   3245 C CG  . GLN C 1 121 ? 12.22100  12.12000 -36.86600 1.000 42.07296 ? 121 GLN A CG  1 
ATOM   3246 C CD  . GLN C 1 121 ? 11.39300  13.36100 -36.53500 1.000 40.66261 ? 121 GLN A CD  1 
ATOM   3247 O OE1 . GLN C 1 121 ? 11.74600  14.47300 -36.92700 1.000 38.42126 ? 121 GLN A OE1 1 
ATOM   3248 N NE2 . GLN C 1 121 ? 10.29100  13.17400 -35.80500 1.000 38.82889 ? 121 GLN A NE2 1 
ATOM   3249 N N   . PRO C 1 122 ? 10.28100  9.34400  -33.74200 1.000 36.07213 ? 122 PRO A N   1 
ATOM   3250 C CA  . PRO C 1 122 ? 9.82500   8.12700  -33.05900 1.000 39.75794 ? 122 PRO A CA  1 
ATOM   3251 C C   . PRO C 1 122 ? 10.02400  6.89400  -33.92500 1.000 44.51118 ? 122 PRO A C   1 
ATOM   3252 O O   . PRO C 1 122 ? 9.81500   6.92700  -35.14000 1.000 40.95737 ? 122 PRO A O   1 
ATOM   3253 C CB  . PRO C 1 122 ? 8.33800   8.39900  -32.80200 1.000 38.63970 ? 122 PRO A CB  1 
ATOM   3254 C CG  . PRO C 1 122 ? 8.22400   9.89600  -32.79500 1.000 34.96116 ? 122 PRO A CG  1 
ATOM   3255 C CD  . PRO C 1 122 ? 9.19200   10.33300 -33.86500 1.000 36.61937 ? 122 PRO A CD  1 
ATOM   3256 N N   . GLY C 1 123 ? 10.43700  5.80000  -33.28100 1.000 42.20775 ? 123 GLY A N   1 
ATOM   3257 C CA  . GLY C 1 123 ? 10.76400  4.57400  -33.96600 1.000 45.30777 ? 123 GLY A CA  1 
ATOM   3258 C C   . GLY C 1 123 ? 12.22200  4.43700  -34.34700 1.000 45.59907 ? 123 GLY A C   1 
ATOM   3259 O O   . GLY C 1 123 ? 12.67200  3.32100  -34.63400 1.000 46.34642 ? 123 GLY A O   1 
ATOM   3260 N N   . HIS C 1 124 ? 12.97200  5.54000  -34.35100 1.000 44.59463 ? 124 HIS A N   1 
ATOM   3261 C CA  . HIS C 1 124 ? 14.38700  5.54500  -34.69200 1.000 42.97103 ? 124 HIS A CA  1 
ATOM   3262 C C   . HIS C 1 124 ? 15.27700  5.47700  -33.45900 1.000 42.12729 ? 124 HIS A C   1 
ATOM   3263 O O   . HIS C 1 124 ? 16.44200  5.88300  -33.52200 1.000 45.86961 ? 124 HIS A O   1 
ATOM   3264 C CB  . HIS C 1 124 ? 14.72900  6.79500  -35.50600 1.000 45.56532 ? 124 HIS A CB  1 
ATOM   3265 C CG  . HIS C 1 124 ? 14.50800  6.64000  -36.97800 1.000 50.12861 ? 124 HIS A CG  1 
ATOM   3266 N ND1 . HIS C 1 124 ? 14.04300  5.47200  -37.54400 1.000 53.02528 ? 124 HIS A ND1 1 
ATOM   3267 C CD2 . HIS C 1 124 ? 14.70100  7.50400  -38.00300 1.000 52.24431 ? 124 HIS A CD2 1 
ATOM   3268 C CE1 . HIS C 1 124 ? 13.95200  5.62600  -38.85400 1.000 54.17758 ? 124 HIS A CE1 1 
ATOM   3269 N NE2 . HIS C 1 124 ? 14.34400  6.85100  -39.15800 1.000 52.68820 ? 124 HIS A NE2 1 
ATOM   3270 N N   . GLU C 1 125 ? 14.75300  4.96200  -32.34600 1.000 40.33194 ? 125 GLU A N   1 
ATOM   3271 C CA  . GLU C 1 125 ? 15.45700  5.05100  -31.07100 1.000 43.46373 ? 125 GLU A CA  1 
ATOM   3272 C C   . GLU C 1 125 ? 16.70000  4.16800  -31.02500 1.000 45.39413 ? 125 GLU A C   1 
ATOM   3273 O O   . GLU C 1 125 ? 17.64100  4.47400  -30.28300 1.000 40.75193 ? 125 GLU A O   1 
ATOM   3274 C CB  . GLU C 1 125 ? 14.51500  4.67700  -29.93000 1.000 46.55308 ? 125 GLU A CB  1 
ATOM   3275 C CG  . GLU C 1 125 ? 13.47900  5.73700  -29.59400 1.000 41.88623 ? 125 GLU A CG  1 
ATOM   3276 C CD  . GLU C 1 125 ? 12.24100  5.62500  -30.46600 1.000 44.50099 ? 125 GLU A CD  1 
ATOM   3277 O OE1 . GLU C 1 125 ? 12.03800  4.55200  -31.07300 1.000 41.63224 ? 125 GLU A OE1 1 
ATOM   3278 O OE2 . GLU C 1 125 ? 11.44800  6.59100  -30.50400 1.000 38.91340 ? 125 GLU A OE2 1 
ATOM   3279 N N   . GLY C 1 126 ? 16.72500  3.07600  -31.78800 1.000 46.49067 ? 126 GLY A N   1 
ATOM   3280 C CA  . GLY C 1 126 ? 17.85300  2.16000  -31.75100 1.000 45.94647 ? 126 GLY A CA  1 
ATOM   3281 C C   . GLY C 1 126 ? 19.07700  2.69200  -32.46500 1.000 45.27471 ? 126 GLY A C   1 
ATOM   3282 O O   . GLY C 1 126 ? 20.19800  2.61900  -31.94800 1.000 46.55025 ? 126 GLY A O   1 
ATOM   3283 N N   . GLU C 1 127 ? 18.86000  3.21800  -33.67300 1.000 43.86932 ? 127 GLU A N   1 
ATOM   3284 C CA  . GLU C 1 127 ? 19.93900  3.81700  -34.45100 1.000 47.16792 ? 127 GLU A CA  1 
ATOM   3285 C C   . GLU C 1 127 ? 20.53000  5.02600  -33.73800 1.000 45.25837 ? 127 GLU A C   1 
ATOM   3286 O O   . GLU C 1 127 ? 21.75300  5.18900  -33.67600 1.000 43.24693 ? 127 GLU A O   1 
ATOM   3287 C CB  . GLU C 1 127 ? 19.40700  4.20100  -35.83400 1.000 44.00833 ? 127 GLU A CB  1 
ATOM   3288 C CG  . GLU C 1 127 ? 20.35000  5.00400  -36.71100 1.000 52.09916 ? 127 GLU A CG  1 
ATOM   3289 C CD  . GLU C 1 127 ? 19.61900  5.74400  -37.83300 1.000 57.18864 ? 127 GLU A CD  1 
ATOM   3290 O OE1 . GLU C 1 127 ? 18.49000  5.33900  -38.19700 1.000 54.68429 ? 127 GLU A OE1 1 
ATOM   3291 O OE2 . GLU C 1 127 ? 20.17300  6.74000  -38.34700 1.000 62.61330 ? 127 GLU A OE2 1 
ATOM   3292 N N   . TRP C 1 128 ? 19.66900  5.88200  -33.19300 1.000 43.29096 ? 128 TRP A N   1 
ATOM   3293 C CA  . TRP C 1 128 ? 20.12100  7.05600  -32.45400 1.000 41.54043 ? 128 TRP A CA  1 
ATOM   3294 C C   . TRP C 1 128 ? 21.00100  6.66100  -31.27700 1.000 39.88330 ? 128 TRP A C   1 
ATOM   3295 O O   . TRP C 1 128 ? 22.07000  7.24300  -31.06000 1.000 41.02777 ? 128 TRP A O   1 
ATOM   3296 C CB  . TRP C 1 128 ? 18.89300  7.83700  -31.98900 1.000 40.56844 ? 128 TRP A CB  1 
ATOM   3297 C CG  . TRP C 1 128 ? 19.10200  8.91600  -30.96300 1.000 39.26856 ? 128 TRP A CG  1 
ATOM   3298 C CD1 . TRP C 1 128 ? 19.44300  10.22000 -31.19900 1.000 36.48744 ? 128 TRP A CD1 1 
ATOM   3299 C CD2 . TRP C 1 128 ? 18.90800  8.80200  -29.54500 1.000 35.81844 ? 128 TRP A CD2 1 
ATOM   3300 N NE1 . TRP C 1 128 ? 19.50400  10.91200 -30.01300 1.000 33.98898 ? 128 TRP A NE1 1 
ATOM   3301 C CE2 . TRP C 1 128 ? 19.17300  10.06600 -28.98400 1.000 34.47636 ? 128 TRP A CE2 1 
ATOM   3302 C CE3 . TRP C 1 128 ? 18.56300  7.74700  -28.69600 1.000 34.59543 ? 128 TRP A CE3 1 
ATOM   3303 C CZ2 . TRP C 1 128 ? 19.10500  10.30300 -27.60700 1.000 37.82904 ? 128 TRP A CZ2 1 
ATOM   3304 C CZ3 . TRP C 1 128 ? 18.48700  7.98600  -27.33000 1.000 37.72459 ? 128 TRP A CZ3 1 
ATOM   3305 C CH2 . TRP C 1 128 ? 18.75600  9.25300  -26.80100 1.000 35.54483 ? 128 TRP A CH2 1 
ATOM   3306 N N   . PHE C 1 129 ? 20.57100  5.65500  -30.51500 1.000 39.00466 ? 129 PHE A N   1 
ATOM   3307 C CA  . PHE C 1 129 ? 21.29500  5.26300  -29.31100 1.000 41.83381 ? 129 PHE A CA  1 
ATOM   3308 C C   . PHE C 1 129 ? 22.69100  4.75100  -29.65000 1.000 45.04190 ? 129 PHE A C   1 
ATOM   3309 O O   . PHE C 1 129 ? 23.66200  5.04900  -28.94000 1.000 40.41140 ? 129 PHE A O   1 
ATOM   3310 C CB  . PHE C 1 129 ? 20.48800  4.20400  -28.55600 1.000 40.76193 ? 129 PHE A CB  1 
ATOM   3311 C CG  . PHE C 1 129 ? 21.15900  3.68500  -27.31900 1.000 40.33180 ? 129 PHE A CG  1 
ATOM   3312 C CD1 . PHE C 1 129 ? 21.15200  4.42700  -26.15200 1.000 38.71108 ? 129 PHE A CD1 1 
ATOM   3313 C CD2 . PHE C 1 129 ? 21.78500  2.45100  -27.32200 1.000 38.87940 ? 129 PHE A CD2 1 
ATOM   3314 C CE1 . PHE C 1 129 ? 21.76800  3.95000  -25.00500 1.000 41.60239 ? 129 PHE A CE1 1 
ATOM   3315 C CE2 . PHE C 1 129 ? 22.40000  1.96500  -26.18300 1.000 39.19432 ? 129 PHE A CE2 1 
ATOM   3316 C CZ  . PHE C 1 129 ? 22.39300  2.71300  -25.02300 1.000 42.99859 ? 129 PHE A CZ  1 
ATOM   3317 N N   . ASP C 1 130 ? 22.81100  3.98400  -30.74300 1.000 44.47360 ? 130 ASP A N   1 
ATOM   3318 C CA  . ASP C 1 130 ? 24.10300  3.43000  -31.13400 1.000 46.00295 ? 130 ASP A CA  1 
ATOM   3319 C C   . ASP C 1 130 ? 25.08800  4.51800  -31.54500 1.000 44.27690 ? 130 ASP A C   1 
ATOM   3320 O O   . ASP C 1 130 ? 26.29200  4.37400  -31.30500 1.000 45.77843 ? 130 ASP A O   1 
ATOM   3321 C CB  . ASP C 1 130 ? 23.93500  2.41600  -32.26900 1.000 47.24701 ? 130 ASP A CB  1 
ATOM   3322 C CG  . ASP C 1 130 ? 23.03600  1.25100  -31.89300 1.000 46.72846 ? 130 ASP A CG  1 
ATOM   3323 O OD1 . ASP C 1 130 ? 22.97600  0.89700  -30.69600 1.000 44.97352 ? 130 ASP A OD1 1 
ATOM   3324 O OD2 . ASP C 1 130 ? 22.42300  0.66100  -32.80900 1.000 50.72410 ? 130 ASP A OD2 1 
ATOM   3325 N N   . ASN C 1 131 ? 24.61000  5.60500  -32.16300 1.000 43.74053 ? 131 ASN A N   1 
ATOM   3326 C CA  . ASN C 1 131 ? 25.50200  6.71600  -32.48800 1.000 46.66923 ? 131 ASN A CA  1 
ATOM   3327 C C   . ASN C 1 131 ? 26.02700  7.46400  -31.27100 1.000 42.02772 ? 131 ASN A C   1 
ATOM   3328 O O   . ASN C 1 131 ? 27.05500  8.13800  -31.39000 1.000 41.10918 ? 131 ASN A O   1 
ATOM   3329 C CB  . ASN C 1 131 ? 24.82800  7.71900  -33.43100 1.000 47.17107 ? 131 ASN A CB  1 
ATOM   3330 C CG  . ASN C 1 131 ? 25.69800  8.05900  -34.63400 1.000 55.62455 ? 131 ASN A CG  1 
ATOM   3331 O OD1 . ASN C 1 131 ? 26.93100  8.06000  -34.53800 1.000 59.45778 ? 131 ASN A OD1 1 
ATOM   3332 N ND2 . ASN C 1 131 ? 25.06800  8.35200  -35.76600 1.000 58.87445 ? 131 ASN A ND2 1 
ATOM   3333 N N   . LEU C 1 132 ? 25.35800  7.39100  -30.11800 1.000 42.65617 ? 132 LEU A N   1 
ATOM   3334 C CA  . LEU C 1 132 ? 25.91100  8.07800  -28.95700 1.000 40.09249 ? 132 LEU A CA  1 
ATOM   3335 C C   . LEU C 1 132 ? 27.21100  7.42200  -28.49200 1.000 44.14263 ? 132 LEU A C   1 
ATOM   3336 O O   . LEU C 1 132 ? 27.53800  6.28700  -28.85600 1.000 42.64544 ? 132 LEU A O   1 
ATOM   3337 C CB  . LEU C 1 132 ? 24.91700  8.13000  -27.79200 1.000 35.82116 ? 132 LEU A CB  1 
ATOM   3338 C CG  . LEU C 1 132 ? 23.43300  8.27000  -28.11100 1.000 42.33010 ? 132 LEU A CG  1 
ATOM   3339 C CD1 . LEU C 1 132 ? 22.59600  7.84800  -26.92000 1.000 40.43106 ? 132 LEU A CD1 1 
ATOM   3340 C CD2 . LEU C 1 132 ? 23.11100  9.70700  -28.52600 1.000 40.96349 ? 132 LEU A CD2 1 
ATOM   3341 N N   . SER C 1 133 ? 27.95500  8.16600  -27.67500 1.000 38.03670 ? 133 SER A N   1 
ATOM   3342 C CA  . SER C 1 133 ? 29.24600  7.71400  -27.18400 1.000 42.64984 ? 133 SER A CA  1 
ATOM   3343 C C   . SER C 1 133 ? 29.07100  6.59200  -26.16400 1.000 39.84587 ? 133 SER A C   1 
ATOM   3344 O O   . SER C 1 133 ? 27.99300  6.38400  -25.61000 1.000 36.18221 ? 133 SER A O   1 
ATOM   3345 C CB  . SER C 1 133 ? 30.01200  8.87800  -26.55700 1.000 36.54115 ? 133 SER A CB  1 
ATOM   3346 O OG  . SER C 1 133 ? 29.67000  9.02100  -25.19200 1.000 43.58228 ? 133 SER A OG  1 
ATOM   3347 N N   . SER C 1 134 ? 30.16300  5.86200  -25.91600 1.000 41.22568 ? 134 SER A N   1 
ATOM   3348 C CA  . SER C 1 134 ? 30.09800  4.75400  -24.96900 1.000 39.70852 ? 134 SER A CA  1 
ATOM   3349 C C   . SER C 1 134 ? 29.68100  5.23700  -23.58400 1.000 36.82588 ? 134 SER A C   1 
ATOM   3350 O O   . SER C 1 134 ? 28.90900  4.56500  -22.88900 1.000 37.79266 ? 134 SER A O   1 
ATOM   3351 C CB  . SER C 1 134 ? 31.45000  4.05700  -24.88000 1.000 38.04322 ? 134 SER A CB  1 
ATOM   3352 O OG  . SER C 1 134 ? 32.42600  4.97100  -24.41100 1.000 38.87805 ? 134 SER A OG  1 
ATOM   3353 N N   . ASP C 1 135 ? 30.20200  6.39000  -23.15600 1.000 34.86010 ? 135 ASP A N   1 
ATOM   3354 C CA  . ASP C 1 135 ? 29.89700  6.87600  -21.81700 1.000 37.71343 ? 135 ASP A CA  1 
ATOM   3355 C C   . ASP C 1 135 ? 28.46500  7.37700  -21.71300 1.000 36.64561 ? 135 ASP A C   1 
ATOM   3356 O O   . ASP C 1 135 ? 27.85500  7.28900  -20.64000 1.000 34.93084 ? 135 ASP A O   1 
ATOM   3357 C CB  . ASP C 1 135 ? 30.88700  7.96500  -21.40800 1.000 40.70678 ? 135 ASP A CB  1 
ATOM   3358 C CG  . ASP C 1 135 ? 32.21900  7.38800  -20.95600 1.000 40.01023 ? 135 ASP A CG  1 
ATOM   3359 O OD1 . ASP C 1 135 ? 32.29300  6.15200  -20.81500 1.000 34.50173 ? 135 ASP A OD1 1 
ATOM   3360 O OD2 . ASP C 1 135 ? 33.18500  8.15300  -20.76000 1.000 38.89720 ? 135 ASP A OD2 1 
ATOM   3361 N N   . GLU C 1 136 ? 27.90600  7.88800  -22.80700 1.000 36.37922 ? 136 GLU A N   1 
ATOM   3362 C CA  . GLU C 1 136 ? 26.50900  8.29800  -22.77600 1.000 36.01624 ? 136 GLU A CA  1 
ATOM   3363 C C   . GLU C 1 136 ? 25.60200  7.08200  -22.68600 1.000 34.55302 ? 136 GLU A C   1 
ATOM   3364 O O   . GLU C 1 136 ? 24.67400  7.04800  -21.87000 1.000 33.93001 ? 136 GLU A O   1 
ATOM   3365 C CB  . GLU C 1 136 ? 26.18400  9.13800  -24.00900 1.000 34.79899 ? 136 GLU A CB  1 
ATOM   3366 C CG  . GLU C 1 136 ? 26.53800  10.60500 -23.86200 1.000 37.41162 ? 136 GLU A CG  1 
ATOM   3367 C CD  . GLU C 1 136 ? 26.54200  11.32600 -25.19200 1.000 41.32984 ? 136 GLU A CD  1 
ATOM   3368 O OE1 . GLU C 1 136 ? 26.90900  10.70100 -26.21400 1.000 41.93968 ? 136 GLU A OE1 1 
ATOM   3369 O OE2 . GLU C 1 136 ? 26.16900  12.51300 -25.22300 1.000 42.33313 ? 136 GLU A OE2 1 
ATOM   3370 N N   . ARG C 1 137 ? 25.87400  6.05700  -23.50200 1.000 36.16861 ? 137 ARG A N   1 
ATOM   3371 C CA  . ARG C 1 137 ? 25.06700  4.84500  -23.43200 1.000 34.90656 ? 137 ARG A CA  1 
ATOM   3372 C C   . ARG C 1 137 ? 25.20700  4.16500  -22.08400 1.000 34.93112 ? 137 ARG A C   1 
ATOM   3373 O O   . ARG C 1 137 ? 24.23300  3.62800  -21.55700 1.000 34.31527 ? 137 ARG A O   1 
ATOM   3374 C CB  . ARG C 1 137 ? 25.42600  3.86600  -24.55300 1.000 38.54330 ? 137 ARG A CB  1 
ATOM   3375 C CG  . ARG C 1 137 ? 25.66200  4.47200  -25.91800 1.000 38.99515 ? 137 ARG A CG  1 
ATOM   3376 C CD  . ARG C 1 137 ? 25.67600  3.36700  -26.95600 1.000 42.40431 ? 137 ARG A CD  1 
ATOM   3377 N NE  . ARG C 1 137 ? 26.87200  2.54800  -26.80800 1.000 41.11595 ? 137 ARG A NE  1 
ATOM   3378 C CZ  . ARG C 1 137 ? 28.07200  2.88300  -27.25500 1.000 42.75313 ? 137 ARG A CZ  1 
ATOM   3379 N NH1 . ARG C 1 137 ? 28.26500  3.99800  -27.93900 1.000 38.62852 ? 137 ARG A NH1 1 
ATOM   3380 N NH2 . ARG C 1 137 ? 29.10500  2.08300  -26.99900 1.000 44.90617 ? 137 ARG A NH2 1 
ATOM   3381 N N   . ALA C 1 138 ? 26.40700  4.18000  -21.50500 1.000 34.89046 ? 138 ALA A N   1 
ATOM   3382 C CA  . ALA C 1 138 ? 26.58200  3.55700  -20.20000 1.000 37.68853 ? 138 ALA A CA  1 
ATOM   3383 C C   . ALA C 1 138 ? 25.76100  4.27600  -19.14400 1.000 35.94496 ? 138 ALA A C   1 
ATOM   3384 O O   . ALA C 1 138 ? 25.08400  3.63600  -18.33300 1.000 37.27356 ? 138 ALA A O   1 
ATOM   3385 C CB  . ALA C 1 138 ? 28.06200  3.54100  -19.81400 1.000 34.80536 ? 138 ALA A CB  1 
ATOM   3386 N N   . PHE C 1 139 ? 25.80700  5.61000  -19.14000 1.000 36.56412 ? 139 PHE A N   1 
ATOM   3387 C CA  . PHE C 1 139 ? 25.01400  6.37500  -18.18800 1.000 34.58102 ? 139 PHE A CA  1 
ATOM   3388 C C   . PHE C 1 139 ? 23.53000  6.06600  -18.33100 1.000 34.69812 ? 139 PHE A C   1 
ATOM   3389 O O   . PHE C 1 139 ? 22.84200  5.82400  -17.33200 1.000 36.30776 ? 139 PHE A O   1 
ATOM   3390 C CB  . PHE C 1 139 ? 25.26100  7.86800  -18.36700 1.000 34.17893 ? 139 PHE A CB  1 
ATOM   3391 C CG  . PHE C 1 139 ? 24.49900  8.71100  -17.38900 1.000 41.63916 ? 139 PHE A CG  1 
ATOM   3392 C CD1 . PHE C 1 139 ? 24.87700  8.74200  -16.05300 1.000 38.83616 ? 139 PHE A CD1 1 
ATOM   3393 C CD2 . PHE C 1 139 ? 23.37100  9.42100  -17.78700 1.000 33.66204 ? 139 PHE A CD2 1 
ATOM   3394 C CE1 . PHE C 1 139 ? 24.16900  9.50500  -15.13100 1.000 40.08467 ? 139 PHE A CE1 1 
ATOM   3395 C CE2 . PHE C 1 139 ? 22.65000  10.17500 -16.87700 1.000 35.35958 ? 139 PHE A CE2 1 
ATOM   3396 C CZ  . PHE C 1 139 ? 23.05100  10.22300 -15.54500 1.000 40.87477 ? 139 PHE A CZ  1 
ATOM   3397 N N   . MET C 1 140 ? 23.02300  6.04400  -19.56800 1.000 33.60545 ? 140 MET A N   1 
ATOM   3398 C CA  . MET C 1 140 ? 21.59700  5.80700  -19.77600 1.000 33.67455 ? 140 MET A CA  1 
ATOM   3399 C C   . MET C 1 140 ? 21.20900  4.38200  -19.39000 1.000 34.38722 ? 140 MET A C   1 
ATOM   3400 O O   . MET C 1 140 ? 20.17700  4.17100  -18.74100 1.000 35.86278 ? 140 MET A O   1 
ATOM   3401 C CB  . MET C 1 140 ? 21.21100  6.11800  -21.23300 1.000 32.90641 ? 140 MET A CB  1 
ATOM   3402 C CG  . MET C 1 140 ? 21.60900  7.53500  -21.67800 1.000 32.57860 ? 140 MET A CG  1 
ATOM   3403 S SD  . MET C 1 140 ? 21.57400  7.97700  -23.45000 1.000 42.34349 ? 140 MET A SD  1 
ATOM   3404 C CE  . MET C 1 140 ? 20.24700  6.99400  -24.05100 1.000 38.84931 ? 140 MET A CE  1 
ATOM   3405 N N   . GLU C 1 141 ? 22.04200  3.39200  -19.73800 1.000 34.87374 ? 141 GLU A N   1 
ATOM   3406 C CA  . GLU C 1 141 ? 21.70800  1.99800  -19.44000 1.000 36.54482 ? 141 GLU A CA  1 
ATOM   3407 C C   . GLU C 1 141 ? 21.66000  1.69600  -17.94400 1.000 38.62206 ? 141 GLU A C   1 
ATOM   3408 O O   . GLU C 1 141 ? 21.01100  0.71800  -17.55300 1.000 39.26917 ? 141 GLU A O   1 
ATOM   3409 C CB  . GLU C 1 141 ? 22.68400  1.05000  -20.14400 1.000 36.63075 ? 141 GLU A CB  1 
ATOM   3410 C CG  . GLU C 1 141 ? 22.68100  1.20800  -21.65600 1.000 41.36469 ? 141 GLU A CG  1 
ATOM   3411 C CD  . GLU C 1 141 ? 23.45700  0.12000  -22.38300 1.000 43.70696 ? 141 GLU A CD  1 
ATOM   3412 O OE1 . GLU C 1 141 ? 24.63600  -0.11500 -22.02600 1.000 41.77593 ? 141 GLU A OE1 1 
ATOM   3413 O OE2 . GLU C 1 141 ? 22.88200  -0.49500 -23.31000 1.000 43.80403 ? 141 GLU A OE2 1 
ATOM   3414 N N   . THR C 1 142 ? 22.30500  2.50600  -17.09500 1.000 37.77009 ? 142 THR A N   1 
ATOM   3415 C CA  . THR C 1 142 ? 22.06900  2.34900  -15.66200 1.000 37.80247 ? 142 THR A CA  1 
ATOM   3416 C C   . THR C 1 142 ? 20.66400  2.78300  -15.25600 1.000 40.48022 ? 142 THR A C   1 
ATOM   3417 O O   . THR C 1 142 ? 20.21400  2.43400  -14.16000 1.000 36.95169 ? 142 THR A O   1 
ATOM   3418 C CB  . THR C 1 142 ? 23.10100  3.12900  -14.83400 1.000 40.52308 ? 142 THR A CB  1 
ATOM   3419 O OG1 . THR C 1 142 ? 22.65700  4.48000  -14.64300 1.000 45.87760 ? 142 THR A OG1 1 
ATOM   3420 C CG2 . THR C 1 142 ? 24.46700  3.11300  -15.47400 1.000 37.77278 ? 142 THR A CG2 1 
ATOM   3421 N N   . ASN C 1 143 ? 19.96000  3.52300  -16.10800 1.000 36.55689 ? 143 ASN A N   1 
ATOM   3422 C CA  . ASN C 1 143 ? 18.62500  4.02000  -15.77800 1.000 37.69375 ? 143 ASN A CA  1 
ATOM   3423 C C   . ASN C 1 143 ? 17.55700  3.08700  -16.34700 1.000 38.09866 ? 143 ASN A C   1 
ATOM   3424 O O   . ASN C 1 143 ? 16.66900  3.48000  -17.10900 1.000 38.48359 ? 143 ASN A O   1 
ATOM   3425 C CB  . ASN C 1 143 ? 18.44900  5.44700  -16.29100 1.000 33.81781 ? 143 ASN A CB  1 
ATOM   3426 C CG  . ASN C 1 143 ? 19.29200  6.44000  -15.53700 1.000 33.74365 ? 143 ASN A CG  1 
ATOM   3427 O OD1 . ASN C 1 143 ? 19.49500  6.30800  -14.33500 1.000 39.51038 ? 143 ASN A OD1 1 
ATOM   3428 N ND2 . ASN C 1 143 ? 19.80800  7.43700  -16.24400 1.000 37.34556 ? 143 ASN A ND2 1 
ATOM   3429 N N   . VAL C 1 144 ? 17.66200  1.81600  -15.97500 1.000 37.31632 ? 144 VAL A N   1 
ATOM   3430 C CA  . VAL C 1 144 ? 16.68500  0.81100  -16.36600 1.000 39.88357 ? 144 VAL A CA  1 
ATOM   3431 C C   . VAL C 1 144 ? 16.37200  -0.01600 -15.13300 1.000 41.30511 ? 144 VAL A C   1 
ATOM   3432 O O   . VAL C 1 144 ? 17.28600  -0.44200 -14.41900 1.000 42.97497 ? 144 VAL A O   1 
ATOM   3433 C CB  . VAL C 1 144 ? 17.19300  -0.08000 -17.52200 1.000 39.76277 ? 144 VAL A CB  1 
ATOM   3434 C CG1 . VAL C 1 144 ? 16.15800  -1.13500 -17.88200 1.000 41.75002 ? 144 VAL A CG1 1 
ATOM   3435 C CG2 . VAL C 1 144 ? 17.51800  0.76800  -18.74500 1.000 41.71045 ? 144 VAL A CG2 1 
ATOM   3436 N N   . ASP C 1 145 ? 15.08400  -0.22100 -14.87400 1.000 42.62810 ? 145 ASP A N   1 
ATOM   3437 C CA  . ASP C 1 145 ? 14.61600  -0.92400 -13.68500 1.000 45.22111 ? 145 ASP A CA  1 
ATOM   3438 C C   . ASP C 1 145 ? 14.01000  -2.26600 -14.08400 1.000 46.63765 ? 145 ASP A C   1 
ATOM   3439 O O   . ASP C 1 145 ? 14.60800  -3.31600 -13.85100 1.000 55.24342 ? 145 ASP A O   1 
ATOM   3440 C CB  . ASP C 1 145 ? 13.59000  -0.06700 -12.92800 1.000 36.90755 ? 145 ASP A CB  1 
ATOM   3441 C CG  . ASP C 1 145 ? 13.14400  -0.69800 -11.61500 1.000 42.70636 ? 145 ASP A CG  1 
ATOM   3442 O OD1 . ASP C 1 145 ? 13.80100  -0.43600 -10.58200 1.000 39.10504 ? 145 ASP A OD1 1 
ATOM   3443 O OD2 . ASP C 1 145 ? 12.13800  -1.43800 -11.61000 1.000 44.53343 ? 145 ASP A OD2 1 
HETATM 3444 S S   . SO4 D 3 .   ? 9.68100   34.01300 -26.86200 1.000 33.08186 ? 201 SO4 B S   1 
HETATM 3445 O O1  . SO4 D 3 .   ? 10.69200  34.95700 -27.17000 1.000 29.91329 ? 201 SO4 B O1  1 
HETATM 3446 O O2  . SO4 D 3 .   ? 9.41800   33.23700 -27.98100 1.000 23.76472 ? 201 SO4 B O2  1 
HETATM 3447 O O3  . SO4 D 3 .   ? 10.15800  33.19700 -25.83400 1.000 31.75617 ? 201 SO4 B O3  1 
HETATM 3448 O O4  . SO4 D 3 .   ? 8.57500   34.64600 -26.27800 1.000 27.73653 ? 201 SO4 B O4  1 
HETATM 3449 S S   . SO4 E 3 .   ? -10.94200 23.88700 -22.37800 1.000 39.80381 ? 201 SO4 C S   1 
HETATM 3450 O O1  . SO4 E 3 .   ? -10.70600 25.11900 -23.09100 1.000 32.30847 ? 201 SO4 C O1  1 
HETATM 3451 O O2  . SO4 E 3 .   ? -10.57200 22.88800 -23.31900 1.000 29.87263 ? 201 SO4 C O2  1 
HETATM 3452 O O3  . SO4 E 3 .   ? -10.02100 23.83900 -21.25400 1.000 32.98307 ? 201 SO4 C O3  1 
HETATM 3453 O O4  . SO4 E 3 .   ? -12.30500 23.80100 -21.86600 1.000 31.88130 ? 201 SO4 C O4  1 
HETATM 3454 S S   . SO4 F 3 .   ? 8.57700   10.32900 -26.71500 1.000 36.53392 ? 201 SO4 A S   1 
HETATM 3455 O O1  . SO4 F 3 .   ? 9.84100   11.06400 -26.71100 1.000 30.75941 ? 201 SO4 A O1  1 
HETATM 3456 O O2  . SO4 F 3 .   ? 7.67200   10.79100 -27.74400 1.000 27.26779 ? 201 SO4 A O2  1 
HETATM 3457 O O3  . SO4 F 3 .   ? 8.77900   8.89000  -26.83800 1.000 34.42973 ? 201 SO4 A O3  1 
HETATM 3458 O O4  . SO4 F 3 .   ? 7.89900   10.60200 -25.45000 1.000 38.54100 ? 201 SO4 A O4  1 
HETATM 3459 O O   . HOH G 4 .   ? 17.70000  44.37400 -22.78000 1.000 40.70899 ? 301 HOH B O   1 
HETATM 3460 O O   . HOH G 4 .   ? 24.24200  29.38200 -33.25500 1.000 37.80112 ? 302 HOH B O   1 
HETATM 3461 O O   . HOH G 4 .   ? 14.43900  18.48300 0.02000   1.000 30.93351 ? 303 HOH B O   1 
HETATM 3462 O O   . HOH G 4 .   ? 6.01300   23.92100 -33.24500 1.000 40.42481 ? 304 HOH B O   1 
HETATM 3463 O O   . HOH G 4 .   ? 9.53300   29.68900 -8.98500  1.000 26.76188 ? 305 HOH B O   1 
HETATM 3464 O O   . HOH G 4 .   ? 17.42800  29.27200 -3.07400  1.000 35.61587 ? 306 HOH B O   1 
HETATM 3465 O O   . HOH G 4 .   ? 20.78100  11.32500 -11.89400 1.000 39.14421 ? 307 HOH B O   1 
HETATM 3466 O O   . HOH G 4 .   ? 2.53700   24.28600 -27.69500 1.000 33.51601 ? 308 HOH B O   1 
HETATM 3467 O O   . HOH G 4 .   ? 17.54600  45.60100 -24.52500 1.000 44.73898 ? 309 HOH B O   1 
HETATM 3468 O O   . HOH G 4 .   ? 16.79600  48.22600 -18.28300 1.000 39.88346 ? 310 HOH B O   1 
HETATM 3469 O O   . HOH G 4 .   ? 27.87400  22.62600 -28.45500 1.000 34.16919 ? 311 HOH B O   1 
HETATM 3470 O O   . HOH G 4 .   ? 27.40700  26.93000 -10.15400 1.000 32.23825 ? 312 HOH B O   1 
HETATM 3471 O O   . HOH G 4 .   ? 12.43800  37.54500 -31.08900 1.000 28.03237 ? 313 HOH B O   1 
HETATM 3472 O O   . HOH G 4 .   ? 15.14400  3.25500  -8.17100  1.000 37.11290 ? 314 HOH B O   1 
HETATM 3473 O O   . HOH G 4 .   ? 20.39400  13.04200 -14.50100 1.000 33.54335 ? 315 HOH B O   1 
HETATM 3474 O O   . HOH G 4 .   ? 16.54200  16.78800 -10.28500 1.000 31.99306 ? 316 HOH B O   1 
HETATM 3475 O O   . HOH G 4 .   ? 15.11300  28.11900 -3.05300  1.000 33.72155 ? 317 HOH B O   1 
HETATM 3476 O O   . HOH G 4 .   ? 23.51200  17.83500 -28.44000 1.000 32.62445 ? 318 HOH B O   1 
HETATM 3477 O O   . HOH G 4 .   ? 24.00700  32.11600 -3.13700  1.000 37.14371 ? 319 HOH B O   1 
HETATM 3478 O O   . HOH G 4 .   ? 8.62300   36.69900 -24.07700 1.000 32.66830 ? 320 HOH B O   1 
HETATM 3479 O O   . HOH G 4 .   ? 24.45900  16.53700 -6.57100  1.000 37.01043 ? 321 HOH B O   1 
HETATM 3480 O O   . HOH G 4 .   ? 6.05300   22.54500 -17.51300 1.000 26.22237 ? 322 HOH B O   1 
HETATM 3481 O O   . HOH G 4 .   ? 3.58100   33.72300 -32.79100 1.000 24.31579 ? 323 HOH B O   1 
HETATM 3482 O O   . HOH G 4 .   ? -4.18600  32.49700 -30.71900 1.000 21.15619 ? 324 HOH B O   1 
HETATM 3483 O O   . HOH G 4 .   ? 9.34900   29.45600 -32.42200 1.000 19.63976 ? 325 HOH B O   1 
HETATM 3484 O O   . HOH G 4 .   ? 24.16800  26.74600 -30.19200 1.000 27.69423 ? 326 HOH B O   1 
HETATM 3485 O O   . HOH G 4 .   ? 15.36700  37.58400 -23.70900 1.000 29.71940 ? 327 HOH B O   1 
HETATM 3486 O O   . HOH G 4 .   ? 12.73100  43.94000 -10.09700 1.000 38.44633 ? 328 HOH B O   1 
HETATM 3487 O O   . HOH G 4 .   ? 14.32800  16.13600 -7.41700  1.000 24.34795 ? 329 HOH B O   1 
HETATM 3488 O O   . HOH G 4 .   ? 0.67900   52.08500 -17.15200 1.000 32.88872 ? 330 HOH B O   1 
HETATM 3489 O O   . HOH G 4 .   ? 17.45400  14.19100 -10.31600 1.000 34.95412 ? 331 HOH B O   1 
HETATM 3490 O O   . HOH G 4 .   ? 7.00500   28.02900 -34.92200 1.000 29.05996 ? 332 HOH B O   1 
HETATM 3491 O O   . HOH G 4 .   ? 16.517    24.673   1.285     1.000 26.67637 ? 333 HOH B O   1 
HETATM 3492 O O   . HOH G 4 .   ? 20.10400  23.97700 -35.50300 1.000 26.32118 ? 334 HOH B O   1 
HETATM 3493 O O   . HOH G 4 .   ? 24.50300  32.38500 -21.94500 1.000 24.78863 ? 335 HOH B O   1 
HETATM 3494 O O   . HOH G 4 .   ? 13.54000  35.41200 -33.51500 1.000 32.26258 ? 336 HOH B O   1 
HETATM 3495 O O   . HOH G 4 .   ? 2.57800   25.21800 -31.81900 1.000 31.42024 ? 337 HOH B O   1 
HETATM 3496 O O   . HOH G 4 .   ? 12.74700  44.58600 -32.35500 1.000 36.59908 ? 338 HOH B O   1 
HETATM 3497 O O   . HOH G 4 .   ? 10.30200  34.75100 -37.48400 1.000 23.39966 ? 339 HOH B O   1 
HETATM 3498 O O   . HOH G 4 .   ? 29.15900  18.31000 -19.64900 1.000 32.25437 ? 340 HOH B O   1 
HETATM 3499 O O   . HOH G 4 .   ? 18.71400  19.07200 -9.77100  1.000 20.26595 ? 341 HOH B O   1 
HETATM 3500 O O   . HOH G 4 .   ? 27.09500  40.63200 -15.92600 1.000 52.99616 ? 342 HOH B O   1 
HETATM 3501 O O   . HOH G 4 .   ? 5.15400   35.64900 -36.75500 1.000 36.10617 ? 343 HOH B O   1 
HETATM 3502 O O   . HOH G 4 .   ? 30.36300  22.02100 -16.31600 1.000 36.43034 ? 344 HOH B O   1 
HETATM 3503 O O   . HOH G 4 .   ? 27.50700  16.81400 -12.94600 1.000 30.60832 ? 345 HOH B O   1 
HETATM 3504 O O   . HOH G 4 .   ? 28.97100  20.85300 -9.26900  1.000 41.42212 ? 346 HOH B O   1 
HETATM 3505 O O   . HOH G 4 .   ? 5.67100   22.02700 -24.53000 1.000 24.24870 ? 347 HOH B O   1 
HETATM 3506 O O   . HOH G 4 .   ? -1.21400  49.53600 -20.58500 1.000 35.96883 ? 348 HOH B O   1 
HETATM 3507 O O   . HOH G 4 .   ? -4.53200  38.43000 -28.72100 1.000 23.51440 ? 349 HOH B O   1 
HETATM 3508 O O   . HOH G 4 .   ? 25.87100  34.18500 -9.70300  1.000 34.04729 ? 350 HOH B O   1 
HETATM 3509 O O   . HOH G 4 .   ? 9.23100   21.70400 -3.13600  1.000 31.66913 ? 351 HOH B O   1 
HETATM 3510 O O   . HOH G 4 .   ? 15.09300  13.90500 -0.35200  1.000 33.03443 ? 352 HOH B O   1 
HETATM 3511 O O   . HOH G 4 .   ? 0.39900   42.81100 -28.52700 1.000 34.92952 ? 353 HOH B O   1 
HETATM 3512 O O   . HOH G 4 .   ? 26.22000  26.47000 -27.73100 1.000 34.30107 ? 354 HOH B O   1 
HETATM 3513 O O   . HOH G 4 .   ? 0.37700   50.15200 -24.67200 1.000 36.16603 ? 355 HOH B O   1 
HETATM 3514 O O   . HOH G 4 .   ? 15.77400  35.58100 -16.11400 1.000 18.53288 ? 356 HOH B O   1 
HETATM 3515 O O   . HOH G 4 .   ? 13.66400  47.31300 -26.56700 1.000 32.94592 ? 357 HOH B O   1 
HETATM 3516 O O   . HOH G 4 .   ? 18.10000  24.00100 -6.64600  1.000 25.99260 ? 358 HOH B O   1 
HETATM 3517 O O   . HOH G 4 .   ? 5.03300   23.21300 -29.24300 1.000 32.27397 ? 359 HOH B O   1 
HETATM 3518 O O   . HOH G 4 .   ? 9.90300   24.88100 -36.60700 1.000 28.30982 ? 360 HOH B O   1 
HETATM 3519 O O   . HOH G 4 .   ? 11.58700  19.95900 -9.74600  1.000 20.34275 ? 361 HOH B O   1 
HETATM 3520 O O   . HOH G 4 .   ? 19.81000  12.90400 -17.28000 1.000 25.79691 ? 362 HOH B O   1 
HETATM 3521 O O   . HOH G 4 .   ? -1.71600  43.73000 -24.42300 1.000 21.73567 ? 363 HOH B O   1 
HETATM 3522 O O   . HOH G 4 .   ? 24.435    23.636   -4.204    1.000 33.55351 ? 364 HOH B O   1 
HETATM 3523 O O   . HOH G 4 .   ? 0.60000   45.73600 -17.83000 1.000 31.90256 ? 365 HOH B O   1 
HETATM 3524 O O   . HOH G 4 .   ? 31.87800  26.93100 -14.59500 1.000 41.60072 ? 366 HOH B O   1 
HETATM 3525 O O   . HOH G 4 .   ? 8.05000   28.99800 -37.04200 1.000 34.00051 ? 367 HOH B O   1 
HETATM 3526 O O   . HOH G 4 .   ? 11.67800  12.30000 -2.47600  1.000 28.78485 ? 368 HOH B O   1 
HETATM 3527 O O   . HOH G 4 .   ? -3.51700  44.11200 -18.80200 1.000 30.31911 ? 369 HOH B O   1 
HETATM 3528 O O   . HOH G 4 .   ? -0.95700  27.25500 -34.13800 1.000 40.95190 ? 370 HOH B O   1 
HETATM 3529 O O   . HOH G 4 .   ? 2.62000   55.53200 -17.80600 1.000 33.26226 ? 371 HOH B O   1 
HETATM 3530 O O   . HOH G 4 .   ? 14.14600  31.89900 -36.37900 1.000 23.28238 ? 372 HOH B O   1 
HETATM 3531 O O   . HOH G 4 .   ? 25.76900  33.27300 -15.90400 1.000 29.65352 ? 373 HOH B O   1 
HETATM 3532 O O   . HOH G 4 .   ? 16.35900  35.21300 -34.20200 1.000 31.85222 ? 374 HOH B O   1 
HETATM 3533 O O   . HOH G 4 .   ? 17.56900  9.62800  -4.22100  1.000 33.85909 ? 375 HOH B O   1 
HETATM 3534 O O   . HOH G 4 .   ? 17.38700  30.25100 -39.32000 1.000 34.43608 ? 376 HOH B O   1 
HETATM 3535 O O   . HOH G 4 .   ? 11.41700  29.82400 -30.60300 1.000 21.89194 ? 377 HOH B O   1 
HETATM 3536 O O   . HOH G 4 .   ? 16.44300  17.09300 -1.31700  1.000 26.43152 ? 378 HOH B O   1 
HETATM 3537 O O   . HOH G 4 .   ? 23.82300  20.82800 -31.71500 1.000 36.41006 ? 379 HOH B O   1 
HETATM 3538 O O   . HOH G 4 .   ? 21.17800  12.66500 -9.62200  1.000 30.74516 ? 380 HOH B O   1 
HETATM 3539 O O   . HOH G 4 .   ? 26.79300  17.56600 -10.24400 1.000 38.34552 ? 381 HOH B O   1 
HETATM 3540 O O   . HOH G 4 .   ? 9.68200   54.89000 -18.94600 1.000 35.31859 ? 382 HOH B O   1 
HETATM 3541 O O   . HOH G 4 .   ? 12.69300  25.16500 -2.18400  1.000 36.03878 ? 383 HOH B O   1 
HETATM 3542 O O   . HOH G 4 .   ? 6.91400   51.99700 -13.16700 1.000 38.83488 ? 384 HOH B O   1 
HETATM 3543 O O   . HOH G 4 .   ? 14.13600  42.43500 -31.23600 1.000 37.08376 ? 385 HOH B O   1 
HETATM 3544 O O   . HOH G 4 .   ? 15.27800  13.74700 -8.05800  1.000 26.24511 ? 386 HOH B O   1 
HETATM 3545 O O   . HOH G 4 .   ? 20.64800  34.32800 -34.11100 1.000 34.75084 ? 387 HOH B O   1 
HETATM 3546 O O   . HOH G 4 .   ? 10.39700  45.89100 -33.55700 1.000 37.59952 ? 388 HOH B O   1 
HETATM 3547 O O   . HOH G 4 .   ? 24.94500  43.25300 -12.39800 1.000 55.60012 ? 389 HOH B O   1 
HETATM 3548 O O   . HOH G 4 .   ? 14.20700  43.60200 -29.60900 1.000 40.42982 ? 390 HOH B O   1 
HETATM 3549 O O   . HOH G 4 .   ? 14.22800  17.67900 -11.72700 1.000 23.34501 ? 391 HOH B O   1 
HETATM 3550 O O   . HOH G 4 .   ? 21.19500  9.41700  -9.53700  1.000 38.12192 ? 392 HOH B O   1 
HETATM 3551 O O   . HOH G 4 .   ? 0.30800   54.17100 -15.80500 1.000 39.84848 ? 393 HOH B O   1 
HETATM 3552 O O   . HOH G 4 .   ? 29.26600  22.99900 -21.92100 1.000 33.05840 ? 394 HOH B O   1 
HETATM 3553 O O   . HOH G 4 .   ? 0.93700   45.27100 -26.82200 1.000 42.02289 ? 395 HOH B O   1 
HETATM 3554 O O   . HOH G 4 .   ? 28.01600  31.55700 -24.36700 1.000 42.11762 ? 396 HOH B O   1 
HETATM 3555 O O   . HOH G 4 .   ? 2.64100   47.48800 -27.78600 1.000 35.81633 ? 397 HOH B O   1 
HETATM 3556 O O   . HOH G 4 .   ? 25.00300  25.40800 -6.65400  1.000 28.19559 ? 398 HOH B O   1 
HETATM 3557 O O   . HOH G 4 .   ? 28.40100  29.90100 -11.77100 1.000 31.99271 ? 399 HOH B O   1 
HETATM 3558 O O   . HOH G 4 .   ? 26.46000  11.66000 -12.04800 1.000 48.63669 ? 400 HOH B O   1 
HETATM 3559 O O   . HOH G 4 .   ? 21.10200  40.32200 -29.33300 1.000 39.27352 ? 401 HOH B O   1 
HETATM 3560 O O   . HOH G 4 .   ? 27.208    27.409   -5.620    1.000 31.00863 ? 402 HOH B O   1 
HETATM 3561 O O   . HOH G 4 .   ? 16.92800  11.18600 -1.93100  1.000 43.67278 ? 403 HOH B O   1 
HETATM 3562 O O   . HOH G 4 .   ? 16.44000  31.71200 -38.53800 1.000 34.59375 ? 404 HOH B O   1 
HETATM 3563 O O   . HOH G 4 .   ? 3.54500   42.16300 -33.91300 1.000 36.28124 ? 405 HOH B O   1 
HETATM 3564 O O   . HOH G 4 .   ? 27.98100  10.69500 -12.88700 1.000 48.39928 ? 406 HOH B O   1 
HETATM 3565 O O   . HOH G 4 .   ? 17.77400  21.96500 -35.81700 1.000 31.99471 ? 407 HOH B O   1 
HETATM 3566 O O   . HOH G 4 .   ? 25.67900  24.88300 -8.75800  1.000 27.49871 ? 408 HOH B O   1 
HETATM 3567 O O   . HOH G 4 .   ? 22.28000  32.49400 -35.57800 1.000 48.21971 ? 409 HOH B O   1 
HETATM 3568 O O   . HOH G 4 .   ? 22.25000  23.56200 -32.94200 1.000 36.48114 ? 410 HOH B O   1 
HETATM 3569 O O   . HOH G 4 .   ? 1.29900   49.25900 -28.18700 1.000 44.11004 ? 411 HOH B O   1 
HETATM 3570 O O   . HOH G 4 .   ? 26.22100  42.67100 -14.28700 1.000 56.28937 ? 412 HOH B O   1 
HETATM 3571 O O   . HOH G 4 .   ? 27.66300  22.95200 -8.15500  1.000 35.03792 ? 413 HOH B O   1 
HETATM 3572 O O   . HOH G 4 .   ? 28.597    33.128   -4.578    1.000 41.18259 ? 414 HOH B O   1 
HETATM 3573 O O   . HOH G 4 .   ? 11.30500  9.85600  -2.04700  1.000 38.36375 ? 415 HOH B O   1 
HETATM 3574 O O   . HOH G 4 .   ? 13.60500  37.30800 -34.49400 1.000 37.22463 ? 416 HOH B O   1 
HETATM 3575 O O   . HOH G 4 .   ? 13.22800  48.97900 -27.74400 1.000 36.14270 ? 417 HOH B O   1 
HETATM 3576 O O   . HOH G 4 .   ? 13.09700  17.55700 -9.30000  1.000 25.06243 ? 418 HOH B O   1 
HETATM 3577 O O   . HOH G 4 .   ? 27.48300  20.38800 -29.23400 1.000 44.87362 ? 419 HOH B O   1 
HETATM 3578 O O   . HOH G 4 .   ? 23.25100  11.62600 -8.22300  1.000 39.61753 ? 420 HOH B O   1 
HETATM 3579 O O   . HOH G 4 .   ? 26.06300  33.54300 -20.53100 1.000 31.73625 ? 421 HOH B O   1 
HETATM 3580 O O   . HOH G 4 .   ? -3.97400  46.07000 -22.10300 1.000 38.01301 ? 422 HOH B O   1 
HETATM 3581 O O   . HOH G 4 .   ? 9.04500   50.96000 -12.05300 1.000 42.56060 ? 423 HOH B O   1 
HETATM 3582 O O   . HOH G 4 .   ? 4.72000   52.63400 -11.74800 1.000 46.96444 ? 424 HOH B O   1 
HETATM 3583 O O   . HOH G 4 .   ? 8.51000   36.54300 -36.77300 1.000 34.68620 ? 425 HOH B O   1 
HETATM 3584 O O   . HOH G 4 .   ? -2.24200  45.87300 -18.03000 1.000 33.44239 ? 426 HOH B O   1 
HETATM 3585 O O   . HOH G 4 .   ? 27.77900  28.57100 -8.15500  1.000 39.20630 ? 427 HOH B O   1 
HETATM 3586 O O   . HOH G 4 .   ? 24.20300  10.44600 -11.57600 1.000 40.27497 ? 428 HOH B O   1 
HETATM 3587 O O   . HOH G 4 .   ? -5.511    37.277   -33.478   1.000 35.81741 ? 429 HOH B O   1 
HETATM 3588 O O   . HOH G 4 .   ? 14.709    26.610   0.020     1.000 34.77488 ? 430 HOH B O   1 
HETATM 3589 O O   . HOH G 4 .   ? 12.93400  8.65800  -0.49600  1.000 48.63389 ? 431 HOH B O   1 
HETATM 3590 O O   . HOH G 4 .   ? 3.88700   24.18000 -24.83800 1.000 26.34635 ? 432 HOH B O   1 
HETATM 3591 O O   . HOH G 4 .   ? 26.48700  17.25000 -29.03400 1.000 38.95440 ? 433 HOH B O   1 
HETATM 3592 O O   . HOH G 4 .   ? -1.34500  50.38400 -17.46200 1.000 37.36209 ? 434 HOH B O   1 
HETATM 3593 O O   . HOH G 4 .   ? 12.827    34.661   -36.146   1.000 31.02807 ? 435 HOH B O   1 
HETATM 3594 O O   . HOH G 4 .   ? 30.90800  25.18400 -22.99000 1.000 41.00950 ? 436 HOH B O   1 
HETATM 3595 O O   . HOH G 4 .   ? 17.53900  32.03200 -39.94300 1.000 40.62484 ? 437 HOH B O   1 
HETATM 3596 O O   . HOH G 4 .   ? 26.90500  34.35300 -13.99800 1.000 34.22343 ? 438 HOH B O   1 
HETATM 3597 O O   . HOH G 4 .   ? -2.56700  40.03500 -29.75000 1.000 27.64011 ? 439 HOH B O   1 
HETATM 3598 O O   . HOH G 4 .   ? 19.49300  11.91800 -2.96500  1.000 43.00725 ? 440 HOH B O   1 
HETATM 3599 O O   . HOH G 4 .   ? 9.33200   48.95200 -10.17200 1.000 46.84487 ? 441 HOH B O   1 
HETATM 3600 O O   . HOH G 4 .   ? 25.29100  29.37500 -30.80700 1.000 38.66096 ? 442 HOH B O   1 
HETATM 3601 O O   . HOH G 4 .   ? -2.94300  44.24900 -26.70300 1.000 37.94978 ? 443 HOH B O   1 
HETATM 3602 O O   . HOH G 4 .   ? 12.94000  14.12600 1.24400   1.000 37.23644 ? 444 HOH B O   1 
HETATM 3603 O O   . HOH G 4 .   ? 4.71300   26.53900 -36.06600 1.000 36.39128 ? 445 HOH B O   1 
HETATM 3604 O O   . HOH G 4 .   ? 24.80000  24.50000 -32.62200 1.000 41.05995 ? 446 HOH B O   1 
HETATM 3605 O O   . HOH H 4 .   ? -24.15400 7.45100  -22.85500 1.000 41.60180 ? 301 HOH C O   1 
HETATM 3606 O O   . HOH H 4 .   ? 1.95300   42.96700 -4.92300  1.000 43.48587 ? 302 HOH C O   1 
HETATM 3607 O O   . HOH H 4 .   ? -25.67400 15.03900 -8.39200  1.000 48.05365 ? 303 HOH C O   1 
HETATM 3608 O O   . HOH H 4 .   ? -11.37500 32.13700 3.13600   1.000 28.03932 ? 304 HOH C O   1 
HETATM 3609 O O   . HOH H 4 .   ? -15.46100 27.00100 -26.37700 1.000 31.45116 ? 305 HOH C O   1 
HETATM 3610 O O   . HOH H 4 .   ? 8.15300   36.60900 -7.87800  1.000 27.29841 ? 306 HOH C O   1 
HETATM 3611 O O   . HOH H 4 .   ? -19.43700 11.34600 -22.06500 1.000 40.61648 ? 307 HOH C O   1 
HETATM 3612 O O   . HOH H 4 .   ? -6.238    45.934   -17.308   1.000 43.61510 ? 308 HOH C O   1 
HETATM 3613 O O   . HOH H 4 .   ? -15.72200 24.85200 -24.34000 1.000 35.14947 ? 309 HOH C O   1 
HETATM 3614 O O   . HOH H 4 .   ? -2.92500  26.75500 -31.63400 1.000 33.92577 ? 310 HOH C O   1 
HETATM 3615 O O   . HOH H 4 .   ? -19.70000 7.02200  -19.54600 1.000 39.19495 ? 311 HOH C O   1 
HETATM 3616 O O   . HOH H 4 .   ? 5.92400   47.98800 -8.18600  1.000 43.82493 ? 312 HOH C O   1 
HETATM 3617 O O   . HOH H 4 .   ? -9.28400  38.48700 -3.06300  1.000 31.94179 ? 313 HOH C O   1 
HETATM 3618 O O   . HOH H 4 .   ? -7.65300  28.28900 -0.45700  1.000 22.05871 ? 314 HOH C O   1 
HETATM 3619 O O   . HOH H 4 .   ? 9.108     29.952   1.483     1.000 35.27938 ? 315 HOH C O   1 
HETATM 3620 O O   . HOH H 4 .   ? -17.62000 5.49500  -16.99100 1.000 37.90235 ? 316 HOH C O   1 
HETATM 3621 O O   . HOH H 4 .   ? 5.16300   22.72400 -13.47500 1.000 17.67915 ? 317 HOH C O   1 
HETATM 3622 O O   . HOH H 4 .   ? -13.64000 35.89400 -13.10700 1.000 24.55016 ? 318 HOH C O   1 
HETATM 3623 O O   . HOH H 4 .   ? -8.94600  15.36200 -31.01200 1.000 26.01274 ? 319 HOH C O   1 
HETATM 3624 O O   . HOH H 4 .   ? -8.28100  11.85600 -34.19000 1.000 41.99871 ? 320 HOH C O   1 
HETATM 3625 O O   . HOH H 4 .   ? 5.71000   21.72500 -7.53900  1.000 29.63469 ? 321 HOH C O   1 
HETATM 3626 O O   . HOH H 4 .   ? -9.74700  38.96900 -32.33100 1.000 41.16620 ? 322 HOH C O   1 
HETATM 3627 O O   . HOH H 4 .   ? -24.074   7.851    -25.949   1.000 43.84970 ? 323 HOH C O   1 
HETATM 3628 O O   . HOH H 4 .   ? 0.99400   44.55300 -7.03600  1.000 34.32352 ? 324 HOH C O   1 
HETATM 3629 O O   . HOH H 4 .   ? 19.81200  34.72900 -6.43200  1.000 40.59935 ? 325 HOH C O   1 
HETATM 3630 O O   . HOH H 4 .   ? -22.66500 31.98100 -4.98000  1.000 45.02586 ? 326 HOH C O   1 
HETATM 3631 O O   . HOH H 4 .   ? -16.17000 37.87300 -19.53700 1.000 37.37345 ? 327 HOH C O   1 
HETATM 3632 O O   . HOH H 4 .   ? -3.30100  43.28200 -22.03400 1.000 31.41783 ? 328 HOH C O   1 
HETATM 3633 O O   . HOH H 4 .   ? 6.31200   34.44800 -7.95000  1.000 26.28629 ? 329 HOH C O   1 
HETATM 3634 O O   . HOH H 4 .   ? -18.56000 20.40300 -2.56300  1.000 33.52106 ? 330 HOH C O   1 
HETATM 3635 O O   . HOH H 4 .   ? -6.28200  30.02300 -32.69700 1.000 29.53492 ? 331 HOH C O   1 
HETATM 3636 O O   . HOH H 4 .   ? -8.93600  40.42900 -2.27500  1.000 44.18060 ? 332 HOH C O   1 
HETATM 3637 O O   . HOH H 4 .   ? 3.78900   24.42600 -16.89400 1.000 31.64215 ? 333 HOH C O   1 
HETATM 3638 O O   . HOH H 4 .   ? 0.32300   22.22600 -26.96000 1.000 30.90251 ? 334 HOH C O   1 
HETATM 3639 O O   . HOH H 4 .   ? -1.90000  22.75300 -30.83600 1.000 42.01796 ? 335 HOH C O   1 
HETATM 3640 O O   . HOH H 4 .   ? 14.27300  31.46500 -3.35300  1.000 29.26526 ? 336 HOH C O   1 
HETATM 3641 O O   . HOH H 4 .   ? 7.03300   40.26900 -11.30600 1.000 28.70950 ? 337 HOH C O   1 
HETATM 3642 O O   . HOH H 4 .   ? -11.54600 41.71700 -18.97000 1.000 38.98904 ? 338 HOH C O   1 
HETATM 3643 O O   . HOH H 4 .   ? -11.56700 38.89200 -9.37800  1.000 26.94395 ? 339 HOH C O   1 
HETATM 3644 O O   . HOH H 4 .   ? -11.32300 25.39300 -10.00400 1.000 19.59661 ? 340 HOH C O   1 
HETATM 3645 O O   . HOH H 4 .   ? -13.21100 41.60500 -15.65100 1.000 31.93105 ? 341 HOH C O   1 
HETATM 3646 O O   . HOH H 4 .   ? 1.82300   25.35400 -23.58300 1.000 22.09854 ? 342 HOH C O   1 
HETATM 3647 O O   . HOH H 4 .   ? -8.56300  26.45700 -28.15600 1.000 21.19551 ? 343 HOH C O   1 
HETATM 3648 O O   . HOH H 4 .   ? -6.84800  42.74100 -24.36400 1.000 29.63673 ? 344 HOH C O   1 
HETATM 3649 O O   . HOH H 4 .   ? 0.43900   27.25200 1.05500   1.000 37.05449 ? 345 HOH C O   1 
HETATM 3650 O O   . HOH H 4 .   ? -11.54700 39.99400 -21.57600 1.000 28.36030 ? 346 HOH C O   1 
HETATM 3651 O O   . HOH H 4 .   ? 3.34100   34.99600 -6.34500  1.000 21.94140 ? 347 HOH C O   1 
HETATM 3652 O O   . HOH H 4 .   ? -19.01700 5.05800  -12.87000 1.000 32.47700 ? 348 HOH C O   1 
HETATM 3653 O O   . HOH H 4 .   ? -13.92200 8.05500  -14.70200 1.000 36.29654 ? 349 HOH C O   1 
HETATM 3654 O O   . HOH H 4 .   ? 8.88400   32.23600 -6.31100  1.000 23.29713 ? 350 HOH C O   1 
HETATM 3655 O O   . HOH H 4 .   ? -15.75300 29.37800 -9.33300  1.000 35.39185 ? 351 HOH C O   1 
HETATM 3656 O O   . HOH H 4 .   ? -7.43400  25.81800 -31.54800 1.000 26.61693 ? 352 HOH C O   1 
HETATM 3657 O O   . HOH H 4 .   ? -1.06200  21.56200 -6.28600  1.000 27.92021 ? 353 HOH C O   1 
HETATM 3658 O O   . HOH H 4 .   ? -4.92900  13.02600 -30.47200 1.000 18.62681 ? 354 HOH C O   1 
HETATM 3659 O O   . HOH H 4 .   ? 6.20200   40.59200 -14.21100 1.000 22.54229 ? 355 HOH C O   1 
HETATM 3660 O O   . HOH H 4 .   ? -19.61100 15.55800 -27.01400 1.000 38.14487 ? 356 HOH C O   1 
HETATM 3661 O O   . HOH H 4 .   ? -23.29900 5.20500  -12.05000 1.000 34.59764 ? 357 HOH C O   1 
HETATM 3662 O O   . HOH H 4 .   ? -19.99300 9.40700  -7.18700  1.000 37.91085 ? 358 HOH C O   1 
HETATM 3663 O O   . HOH H 4 .   ? -5.48500  34.38400 -29.02300 1.000 21.64942 ? 359 HOH C O   1 
HETATM 3664 O O   . HOH H 4 .   ? 0.31400   34.80300 3.70800   1.000 37.68675 ? 360 HOH C O   1 
HETATM 3665 O O   . HOH H 4 .   ? -12.80900 20.77900 -32.52600 1.000 36.34206 ? 361 HOH C O   1 
HETATM 3666 O O   . HOH H 4 .   ? 6.06200   28.37000 -8.51500  1.000 19.22437 ? 362 HOH C O   1 
HETATM 3667 O O   . HOH H 4 .   ? -13.97400 30.14600 -29.91500 1.000 23.51195 ? 363 HOH C O   1 
HETATM 3668 O O   . HOH H 4 .   ? -17.40000 27.23200 -9.86700  1.000 33.68309 ? 364 HOH C O   1 
HETATM 3669 O O   . HOH H 4 .   ? 6.04200   44.26400 -5.76200  1.000 42.84479 ? 365 HOH C O   1 
HETATM 3670 O O   . HOH H 4 .   ? -14.98100 18.02900 -3.34800  1.000 32.00988 ? 366 HOH C O   1 
HETATM 3671 O O   . HOH H 4 .   ? 0.98000   31.62800 -2.43500  1.000 24.29480 ? 367 HOH C O   1 
HETATM 3672 O O   . HOH H 4 .   ? -25.99200 11.34200 -10.77400 1.000 32.87432 ? 368 HOH C O   1 
HETATM 3673 O O   . HOH H 4 .   ? -19.62400 28.76400 -25.42800 1.000 42.51293 ? 369 HOH C O   1 
HETATM 3674 O O   . HOH H 4 .   ? -6.03400  38.95800 -2.02100  1.000 33.60756 ? 370 HOH C O   1 
HETATM 3675 O O   . HOH H 4 .   ? 7.84900   40.32700 -2.30900  1.000 42.03206 ? 371 HOH C O   1 
HETATM 3676 O O   . HOH H 4 .   ? -9.86700  39.15900 -28.32000 1.000 36.10902 ? 372 HOH C O   1 
HETATM 3677 O O   . HOH H 4 .   ? -13.28100 8.17700  -21.64200 1.000 25.55559 ? 373 HOH C O   1 
HETATM 3678 O O   . HOH H 4 .   ? -12.69900 35.75000 -6.79600  1.000 26.36045 ? 374 HOH C O   1 
HETATM 3679 O O   . HOH H 4 .   ? -23.80100 19.76000 -18.29100 1.000 38.10732 ? 375 HOH C O   1 
HETATM 3680 O O   . HOH H 4 .   ? -15.57400 10.69500 -14.76400 1.000 35.13140 ? 376 HOH C O   1 
HETATM 3681 O O   . HOH H 4 .   ? -23.29000 16.04000 -6.78200  1.000 43.85787 ? 377 HOH C O   1 
HETATM 3682 O O   . HOH H 4 .   ? -15.02800 34.01100 -31.68100 1.000 36.94938 ? 378 HOH C O   1 
HETATM 3683 O O   . HOH H 4 .   ? 10.72200  41.88000 -7.18200  1.000 38.15370 ? 379 HOH C O   1 
HETATM 3684 O O   . HOH H 4 .   ? 5.84100   22.62600 -10.89300 1.000 19.19273 ? 380 HOH C O   1 
HETATM 3685 O O   . HOH H 4 .   ? -15.20100 25.63100 -31.27200 1.000 23.96398 ? 381 HOH C O   1 
HETATM 3686 O O   . HOH H 4 .   ? 10.31500  34.71300 -6.81300  1.000 24.43974 ? 382 HOH C O   1 
HETATM 3687 O O   . HOH H 4 .   ? -9.77700  19.42100 -29.48900 1.000 24.28001 ? 383 HOH C O   1 
HETATM 3688 O O   . HOH H 4 .   ? -8.86900  26.46900 -32.95300 1.000 31.24677 ? 384 HOH C O   1 
HETATM 3689 O O   . HOH H 4 .   ? 13.53100  42.45900 -7.92500  1.000 36.46117 ? 385 HOH C O   1 
HETATM 3690 O O   . HOH H 4 .   ? -9.06900  27.67200 -25.68700 1.000 26.00014 ? 386 HOH C O   1 
HETATM 3691 O O   . HOH H 4 .   ? 19.22300  39.66900 -8.73100  1.000 29.55298 ? 387 HOH C O   1 
HETATM 3692 O O   . HOH H 4 .   ? -10.60800 5.46100  -17.06900 1.000 35.36666 ? 388 HOH C O   1 
HETATM 3693 O O   . HOH H 4 .   ? -6.92500  33.14500 4.51000   1.000 21.56703 ? 389 HOH C O   1 
HETATM 3694 O O   . HOH H 4 .   ? 5.88500   32.27600 -9.82900  1.000 21.27349 ? 390 HOH C O   1 
HETATM 3695 O O   . HOH H 4 .   ? -22.93500 21.85700 -24.40800 1.000 43.81813 ? 391 HOH C O   1 
HETATM 3696 O O   . HOH H 4 .   ? -3.42200  38.71300 -1.66200  1.000 30.29617 ? 392 HOH C O   1 
HETATM 3697 O O   . HOH H 4 .   ? 12.13900  32.94800 0.38000   1.000 33.49032 ? 393 HOH C O   1 
HETATM 3698 O O   . HOH H 4 .   ? -3.06600  46.73100 -12.41500 1.000 30.38644 ? 394 HOH C O   1 
HETATM 3699 O O   . HOH H 4 .   ? -11.96300 34.40200 -0.68300  1.000 27.65071 ? 395 HOH C O   1 
HETATM 3700 O O   . HOH H 4 .   ? 13.74300  37.68400 -3.36000  1.000 31.79935 ? 396 HOH C O   1 
HETATM 3701 O O   . HOH H 4 .   ? 5.68800   39.71200 -2.22600  1.000 38.75667 ? 397 HOH C O   1 
HETATM 3702 O O   . HOH H 4 .   ? 4.02600   25.23500 -0.46600  1.000 35.00182 ? 398 HOH C O   1 
HETATM 3703 O O   . HOH H 4 .   ? -2.72300  36.88300 0.25400   1.000 23.96273 ? 399 HOH C O   1 
HETATM 3704 O O   . HOH H 4 .   ? -17.34300 30.19900 -26.43700 1.000 41.17667 ? 400 HOH C O   1 
HETATM 3705 O O   . HOH H 4 .   ? 7.85000   40.75400 -6.56500  1.000 35.73973 ? 401 HOH C O   1 
HETATM 3706 O O   . HOH H 4 .   ? -9.09200  9.13700  -27.45900 1.000 30.41304 ? 402 HOH C O   1 
HETATM 3707 O O   . HOH H 4 .   ? -2.70300  28.43200 1.65000   1.000 31.56413 ? 403 HOH C O   1 
HETATM 3708 O O   . HOH H 4 .   ? -5.498    20.886   -35.063   1.000 42.72454 ? 404 HOH C O   1 
HETATM 3709 O O   . HOH H 4 .   ? -5.25600  44.91200 -8.22000  1.000 36.88692 ? 405 HOH C O   1 
HETATM 3710 O O   . HOH H 4 .   ? -8.26400  18.53300 -32.43200 1.000 33.10027 ? 406 HOH C O   1 
HETATM 3711 O O   . HOH H 4 .   ? 9.476     32.284   0.585     1.000 34.65870 ? 407 HOH C O   1 
HETATM 3712 O O   . HOH H 4 .   ? -17.85600 31.46900 -3.46000  1.000 41.50957 ? 408 HOH C O   1 
HETATM 3713 O O   . HOH H 4 .   ? -14.94500 29.25800 -6.70700  1.000 28.87756 ? 409 HOH C O   1 
HETATM 3714 O O   . HOH H 4 .   ? -15.27900 36.06200 -10.95500 1.000 35.05986 ? 410 HOH C O   1 
HETATM 3715 O O   . HOH H 4 .   ? -2.18200  41.06300 -0.94400  1.000 43.43473 ? 411 HOH C O   1 
HETATM 3716 O O   . HOH H 4 .   ? 10.47000  24.21400 -2.73600  1.000 36.92908 ? 412 HOH C O   1 
HETATM 3717 O O   . HOH H 4 .   ? -15.70700 32.15000 -30.84400 1.000 36.75247 ? 413 HOH C O   1 
HETATM 3718 O O   . HOH H 4 .   ? 3.26700   46.31200 -7.23700  1.000 38.59664 ? 414 HOH C O   1 
HETATM 3719 O O   . HOH H 4 .   ? -19.31700 35.33100 -16.45900 1.000 48.33312 ? 415 HOH C O   1 
HETATM 3720 O O   . HOH H 4 .   ? -7.10800  14.00300 -34.58300 1.000 37.50829 ? 416 HOH C O   1 
HETATM 3721 O O   . HOH H 4 .   ? -17.44200 24.19200 -1.29200  1.000 41.95703 ? 417 HOH C O   1 
HETATM 3722 O O   . HOH H 4 .   ? -19.12600 11.32800 -24.95100 1.000 40.41994 ? 418 HOH C O   1 
HETATM 3723 O O   . HOH H 4 .   ? 7.49300   30.80100 -8.05100  1.000 20.32690 ? 419 HOH C O   1 
HETATM 3724 O O   . HOH H 4 .   ? -8.96700  37.25600 -0.45300  1.000 32.96292 ? 420 HOH C O   1 
HETATM 3725 O O   . HOH H 4 .   ? -12.75500 5.82100  -15.57700 1.000 38.81331 ? 421 HOH C O   1 
HETATM 3726 O O   . HOH H 4 .   ? -19.14100 13.43400 -26.24600 1.000 41.66889 ? 422 HOH C O   1 
HETATM 3727 O O   . HOH H 4 .   ? -2.761    21.388   -35.077   1.000 42.34098 ? 423 HOH C O   1 
HETATM 3728 O O   . HOH H 4 .   ? -16.69600 9.28800  -10.40600 1.000 36.38136 ? 424 HOH C O   1 
HETATM 3729 O O   . HOH H 4 .   ? -15.81900 33.02400 -2.02200  1.000 31.69748 ? 425 HOH C O   1 
HETATM 3730 O O   . HOH H 4 .   ? -13.45900 33.81700 -2.87700  1.000 24.72175 ? 426 HOH C O   1 
HETATM 3731 O O   . HOH H 4 .   ? -14.59600 35.90100 -33.28700 1.000 36.94576 ? 427 HOH C O   1 
HETATM 3732 O O   . HOH H 4 .   ? 16.87200  32.04900 -3.54100  1.000 38.36869 ? 428 HOH C O   1 
HETATM 3733 O O   . HOH H 4 .   ? -12.01000 38.86900 -6.72800  1.000 29.45828 ? 429 HOH C O   1 
HETATM 3734 O O   . HOH H 4 .   ? -17.91000 6.45800  -10.71200 1.000 41.38009 ? 430 HOH C O   1 
HETATM 3735 O O   . HOH H 4 .   ? -4.01400  47.03400 -9.55600  1.000 41.68342 ? 431 HOH C O   1 
HETATM 3736 O O   . HOH H 4 .   ? -16.91400 4.33900  -14.17200 1.000 32.87409 ? 432 HOH C O   1 
HETATM 3737 O O   . HOH H 4 .   ? -6.902    22.961   -34.847   1.000 37.50374 ? 433 HOH C O   1 
HETATM 3738 O O   . HOH H 4 .   ? -29.505   12.024   -21.555   1.000 43.51166 ? 434 HOH C O   1 
HETATM 3739 O O   . HOH H 4 .   ? -13.86200 36.63500 -8.57100  1.000 37.45675 ? 435 HOH C O   1 
HETATM 3740 O O   . HOH H 4 .   ? -21.44300 35.17100 -16.40300 1.000 52.86190 ? 436 HOH C O   1 
HETATM 3741 O O   . HOH H 4 .   ? 17.99400  33.03700 -1.81100  1.000 42.50928 ? 437 HOH C O   1 
HETATM 3742 O O   . HOH H 4 .   ? -16.31700 19.04400 -1.49600  1.000 32.65119 ? 438 HOH C O   1 
HETATM 3743 O O   . HOH H 4 .   ? -9.09200  41.95700 -24.95800 1.000 35.33928 ? 439 HOH C O   1 
HETATM 3744 O O   . HOH H 4 .   ? -15.86800 27.44100 -29.43300 1.000 38.18444 ? 440 HOH C O   1 
HETATM 3745 O O   . HOH H 4 .   ? -11.44900 10.32400 -27.58500 1.000 31.54265 ? 441 HOH C O   1 
HETATM 3746 O O   . HOH H 4 .   ? -1.04700  32.41200 4.71600   1.000 41.31479 ? 442 HOH C O   1 
HETATM 3747 O O   . HOH H 4 .   ? -5.470    24.518   -33.677   1.000 34.64173 ? 443 HOH C O   1 
HETATM 3748 O O   . HOH H 4 .   ? -13.78000 36.17500 -4.54100  1.000 28.40836 ? 444 HOH C O   1 
HETATM 3749 O O   . HOH H 4 .   ? -6.07500  40.44300 -27.68800 1.000 31.01836 ? 445 HOH C O   1 
HETATM 3750 O O   . HOH H 4 .   ? -11.31700 42.00000 -23.24800 1.000 36.47545 ? 446 HOH C O   1 
HETATM 3751 O O   . HOH H 4 .   ? -1.18200  27.42600 3.76700   1.000 47.88544 ? 447 HOH C O   1 
HETATM 3752 O O   . HOH H 4 .   ? -10.56700 44.52300 -22.28700 1.000 41.62517 ? 448 HOH C O   1 
HETATM 3753 O O   . HOH H 4 .   ? -12.77900 44.51200 -21.37400 1.000 48.24851 ? 449 HOH C O   1 
HETATM 3754 O O   . HOH H 4 .   ? -12.42100 38.06300 -2.92400  1.000 34.15618 ? 450 HOH C O   1 
HETATM 3755 O O   . HOH H 4 .   ? -17.02000 34.44100 -33.74400 1.000 47.44591 ? 451 HOH C O   1 
HETATM 3756 O O   . HOH H 4 .   ? -14.49900 40.03900 -3.34400  1.000 48.13945 ? 452 HOH C O   1 
HETATM 3757 O O   . HOH I 4 .   ? 15.29700  -0.39800 -22.18700 1.000 50.98743 ? 301 HOH A O   1 
HETATM 3758 O O   . HOH I 4 .   ? 33.50900  9.17800  -19.01600 1.000 37.39099 ? 302 HOH A O   1 
HETATM 3759 O O   . HOH I 4 .   ? 25.49800  -0.63500 -20.14200 1.000 40.54621 ? 303 HOH A O   1 
HETATM 3760 O O   . HOH I 4 .   ? 7.78500   17.67400 -1.12400  1.000 42.24358 ? 304 HOH A O   1 
HETATM 3761 O O   . HOH I 4 .   ? 10.86200  16.28400 -9.38800  1.000 25.83327 ? 305 HOH A O   1 
HETATM 3762 O O   . HOH I 4 .   ? 20.61800  -1.21400 -18.84200 1.000 42.53161 ? 306 HOH A O   1 
HETATM 3763 O O   . HOH I 4 .   ? 2.73100   19.37000 -31.89200 1.000 36.07346 ? 307 HOH A O   1 
HETATM 3764 O O   . HOH I 4 .   ? -6.02700  17.02400 -4.69900  1.000 31.96170 ? 308 HOH A O   1 
HETATM 3765 O O   . HOH I 4 .   ? -5.13500  4.41700  -1.56700  1.000 40.05062 ? 309 HOH A O   1 
HETATM 3766 O O   . HOH I 4 .   ? -1.11400  16.63400 -32.22900 1.000 32.29439 ? 310 HOH A O   1 
HETATM 3767 O O   . HOH I 4 .   ? -3.33100  16.20600 -5.51200  1.000 26.73810 ? 311 HOH A O   1 
HETATM 3768 O O   . HOH I 4 .   ? 9.15500   14.59600 -34.06400 1.000 27.35249 ? 312 HOH A O   1 
HETATM 3769 O O   . HOH I 4 .   ? 32.43000  7.47900  -24.68500 1.000 39.44280 ? 313 HOH A O   1 
HETATM 3770 O O   . HOH I 4 .   ? 3.15200   12.08900 -30.96500 1.000 17.50207 ? 314 HOH A O   1 
HETATM 3771 O O   . HOH I 4 .   ? -2.92100  20.73100 3.50700   1.000 31.94148 ? 315 HOH A O   1 
HETATM 3772 O O   . HOH I 4 .   ? 28.87400  2.02000  -22.94600 1.000 33.75806 ? 316 HOH A O   1 
HETATM 3773 O O   . HOH I 4 .   ? 1.95300   14.40200 -33.69600 1.000 26.78975 ? 317 HOH A O   1 
HETATM 3774 O O   . HOH I 4 .   ? 8.94500   10.14800 -1.25100  1.000 34.11265 ? 318 HOH A O   1 
HETATM 3775 O O   . HOH I 4 .   ? 12.08900  10.98300 -24.86000 1.000 30.58838 ? 319 HOH A O   1 
HETATM 3776 O O   . HOH I 4 .   ? 5.83100   5.66400  -31.82200 1.000 37.01158 ? 320 HOH A O   1 
HETATM 3777 O O   . HOH I 4 .   ? -2.16900  13.84500 -4.94900  1.000 27.20329 ? 321 HOH A O   1 
HETATM 3778 O O   . HOH I 4 .   ? 2.15800   -0.12600 -17.02600 1.000 30.54935 ? 322 HOH A O   1 
HETATM 3779 O O   . HOH I 4 .   ? 4.01500   -0.25300 -10.88500 1.000 37.71559 ? 323 HOH A O   1 
HETATM 3780 O O   . HOH I 4 .   ? 10.39200  4.34500  -22.48000 1.000 37.85020 ? 324 HOH A O   1 
HETATM 3781 O O   . HOH I 4 .   ? -9.33400  7.12300  -4.75600  1.000 33.08495 ? 325 HOH A O   1 
HETATM 3782 O O   . HOH I 4 .   ? -4.86800  1.28700  -23.33100 1.000 27.20440 ? 326 HOH A O   1 
HETATM 3783 O O   . HOH I 4 .   ? 17.69400  20.23900 -33.73800 1.000 23.33947 ? 327 HOH A O   1 
HETATM 3784 O O   . HOH I 4 .   ? -1.14900  -1.00400 -29.58100 1.000 44.56190 ? 328 HOH A O   1 
HETATM 3785 O O   . HOH I 4 .   ? -2.84700  24.16400 0.55000   1.000 24.17914 ? 329 HOH A O   1 
HETATM 3786 O O   . HOH I 4 .   ? 34.80000  5.35500  -25.60500 1.000 43.15499 ? 330 HOH A O   1 
HETATM 3787 O O   . HOH I 4 .   ? -5.27900  10.60600 -28.88700 1.000 23.14535 ? 331 HOH A O   1 
HETATM 3788 O O   . HOH I 4 .   ? 3.72600   21.14500 -17.07800 1.000 29.59875 ? 332 HOH A O   1 
HETATM 3789 O O   . HOH I 4 .   ? 1.57200   6.07200  -33.45600 1.000 19.34191 ? 333 HOH A O   1 
HETATM 3790 O O   . HOH I 4 .   ? 5.84800   11.62400 -0.16200  1.000 43.67054 ? 334 HOH A O   1 
HETATM 3791 O O   . HOH I 4 .   ? 3.28600   12.56100 -2.68900  1.000 29.87330 ? 335 HOH A O   1 
HETATM 3792 O O   . HOH I 4 .   ? -10.61600 14.40300 -10.36100 1.000 25.91575 ? 336 HOH A O   1 
HETATM 3793 O O   . HOH I 4 .   ? 14.57000  22.62400 -33.58400 1.000 22.77391 ? 337 HOH A O   1 
HETATM 3794 O O   . HOH I 4 .   ? -14.15200 1.04000  -13.29200 1.000 41.34786 ? 338 HOH A O   1 
HETATM 3795 O O   . HOH I 4 .   ? -11.59600 6.84600  -20.36300 1.000 33.27724 ? 339 HOH A O   1 
HETATM 3796 O O   . HOH I 4 .   ? 5.24300   7.57900  -36.24300 1.000 21.91159 ? 340 HOH A O   1 
HETATM 3797 O O   . HOH I 4 .   ? 10.82500  6.60800  -15.10800 1.000 24.32166 ? 341 HOH A O   1 
HETATM 3798 O O   . HOH I 4 .   ? -11.57400 23.34400 2.42800   1.000 33.64808 ? 342 HOH A O   1 
HETATM 3799 O O   . HOH I 4 .   ? -0.00600  2.47500  -3.61600  1.000 35.95129 ? 343 HOH A O   1 
HETATM 3800 O O   . HOH I 4 .   ? -0.07800  -0.61400 -12.19800 1.000 30.46694 ? 344 HOH A O   1 
HETATM 3801 O O   . HOH I 4 .   ? 22.37300  9.80800  -32.04600 1.000 45.00458 ? 345 HOH A O   1 
HETATM 3802 O O   . HOH I 4 .   ? -4.93200  19.58800 -3.17400  1.000 22.55371 ? 346 HOH A O   1 
HETATM 3803 O O   . HOH I 4 .   ? 2.93900   -3.68600 -22.87800 1.000 48.57614 ? 347 HOH A O   1 
HETATM 3804 O O   . HOH I 4 .   ? -2.05700  19.43500 -3.80600  1.000 24.61657 ? 348 HOH A O   1 
HETATM 3805 O O   . HOH I 4 .   ? 23.47300  -2.94000 -22.13000 1.000 44.34057 ? 349 HOH A O   1 
HETATM 3806 O O   . HOH I 4 .   ? 4.34700   18.89500 -37.14000 1.000 34.13180 ? 350 HOH A O   1 
HETATM 3807 O O   . HOH I 4 .   ? 1.62300   19.36800 -7.32100  1.000 20.01272 ? 351 HOH A O   1 
HETATM 3808 O O   . HOH I 4 .   ? -12.55900 28.96400 -5.77400  1.000 23.35232 ? 352 HOH A O   1 
HETATM 3809 O O   . HOH I 4 .   ? 12.08500  22.24500 -34.39900 1.000 22.06433 ? 353 HOH A O   1 
HETATM 3810 O O   . HOH I 4 .   ? 8.83300   5.59500  -30.28900 1.000 36.58536 ? 354 HOH A O   1 
HETATM 3811 O O   . HOH I 4 .   ? 8.70700   14.00100 -0.62000  1.000 37.45442 ? 355 HOH A O   1 
HETATM 3812 O O   . HOH I 4 .   ? -7.28600  4.74100  -29.12400 1.000 28.04453 ? 356 HOH A O   1 
HETATM 3813 O O   . HOH I 4 .   ? 28.58500  6.88400  -17.93200 1.000 36.84187 ? 357 HOH A O   1 
HETATM 3814 O O   . HOH I 4 .   ? -0.21000  17.39100 1.69300   1.000 33.34239 ? 358 HOH A O   1 
HETATM 3815 O O   . HOH I 4 .   ? -13.24500 22.03800 0.06200   1.000 35.93578 ? 359 HOH A O   1 
HETATM 3816 O O   . HOH I 4 .   ? 1.51400   -0.18100 -5.89700  1.000 33.90343 ? 360 HOH A O   1 
HETATM 3817 O O   . HOH I 4 .   ? -9.50800  0.32600  -19.90100 1.000 44.36448 ? 361 HOH A O   1 
HETATM 3818 O O   . HOH I 4 .   ? 0.92300   20.48000 -23.42500 1.000 19.45627 ? 362 HOH A O   1 
HETATM 3819 O O   . HOH I 4 .   ? -2.01200  17.65800 -7.99100  1.000 20.19549 ? 363 HOH A O   1 
HETATM 3820 O O   . HOH I 4 .   ? 22.68700  15.78000 -29.95700 1.000 30.75511 ? 364 HOH A O   1 
HETATM 3821 O O   . HOH I 4 .   ? -2.71800  13.06200 -33.71000 1.000 27.03696 ? 365 HOH A O   1 
HETATM 3822 O O   . HOH I 4 .   ? -10.80100 3.84100  -6.15400  1.000 42.92350 ? 366 HOH A O   1 
HETATM 3823 O O   . HOH I 4 .   ? 7.88000   8.51200  -36.57400 1.000 35.47916 ? 367 HOH A O   1 
HETATM 3824 O O   . HOH I 4 .   ? -0.59700  -3.04700 -17.90400 1.000 38.32008 ? 368 HOH A O   1 
HETATM 3825 O O   . HOH I 4 .   ? -11.86500 8.76500  -3.22800  1.000 42.53233 ? 369 HOH A O   1 
HETATM 3826 O O   . HOH I 4 .   ? 27.20200  1.59200  -31.16500 1.000 49.43184 ? 370 HOH A O   1 
HETATM 3827 O O   . HOH I 4 .   ? 6.59000   21.91700 -2.73500  1.000 32.54216 ? 371 HOH A O   1 
HETATM 3828 O O   . HOH I 4 .   ? 26.92900  -0.08900 -25.43800 1.000 40.96582 ? 372 HOH A O   1 
HETATM 3829 O O   . HOH I 4 .   ? 2.94000   10.40500 -28.58600 1.000 30.21831 ? 373 HOH A O   1 
HETATM 3830 O O   . HOH I 4 .   ? 30.90600  11.27800 -23.65700 1.000 45.97107 ? 374 HOH A O   1 
HETATM 3831 O O   . HOH I 4 .   ? -0.58600  5.15100  -2.44800  1.000 34.87530 ? 375 HOH A O   1 
HETATM 3832 O O   . HOH I 4 .   ? 15.09500  1.60400  -34.07700 1.000 47.43513 ? 376 HOH A O   1 
HETATM 3833 O O   . HOH I 4 .   ? -4.239    3.656    -35.892   1.000 37.12920 ? 377 HOH A O   1 
HETATM 3834 O O   . HOH I 4 .   ? 0.55600   19.49900 -28.22100 1.000 29.07669 ? 378 HOH A O   1 
HETATM 3835 O O   . HOH I 4 .   ? 11.74200  20.70200 -36.61300 1.000 29.42124 ? 379 HOH A O   1 
HETATM 3836 O O   . HOH I 4 .   ? 6.22500   -2.67400 -20.68700 1.000 38.53977 ? 380 HOH A O   1 
HETATM 3837 O O   . HOH I 4 .   ? 25.775    0.738    -17.503   1.000 36.85683 ? 381 HOH A O   1 
HETATM 3838 O O   . HOH I 4 .   ? 8.16000   16.51700 -35.66000 1.000 38.69031 ? 382 HOH A O   1 
HETATM 3839 O O   . HOH I 4 .   ? 3.22400   0.89300  -3.24900  1.000 39.63571 ? 383 HOH A O   1 
HETATM 3840 O O   . HOH I 4 .   ? -1.14300  -1.98800 -23.17000 1.000 45.78414 ? 384 HOH A O   1 
HETATM 3841 O O   . HOH I 4 .   ? -12.129   1.198    -18.403   1.000 46.16820 ? 385 HOH A O   1 
HETATM 3842 O O   . HOH I 4 .   ? 1.23500   5.82700  -0.75600  1.000 29.66570 ? 386 HOH A O   1 
HETATM 3843 O O   . HOH I 4 .   ? -1.53800  -2.57500 -13.65100 1.000 42.60318 ? 387 HOH A O   1 
HETATM 3844 O O   . HOH I 4 .   ? 24.46900  -1.41100 -26.17200 1.000 46.50346 ? 388 HOH A O   1 
HETATM 3845 O O   . HOH I 4 .   ? -4.23700  26.08500 1.79700   1.000 29.90757 ? 389 HOH A O   1 
HETATM 3846 O O   . HOH I 4 .   ? 1.14800   -5.36200 -21.57700 1.000 52.99628 ? 390 HOH A O   1 
HETATM 3847 O O   . HOH I 4 .   ? -0.95800  19.28400 -6.30500  1.000 25.80000 ? 391 HOH A O   1 
HETATM 3848 O O   . HOH I 4 .   ? 27.199    -2.255   -20.552   1.000 42.09463 ? 392 HOH A O   1 
HETATM 3849 O O   . HOH I 4 .   ? -5.367    15.628   2.709     1.000 40.47609 ? 393 HOH A O   1 
HETATM 3850 O O   . HOH I 4 .   ? 21.70000  9.83400  -34.92000 1.000 45.11155 ? 394 HOH A O   1 
HETATM 3851 O O   . HOH I 4 .   ? 3.27900   20.69700 -25.10200 1.000 31.72873 ? 395 HOH A O   1 
HETATM 3852 O O   . HOH I 4 .   ? 22.48000  -2.62800 -19.32900 1.000 47.58868 ? 396 HOH A O   1 
HETATM 3853 O O   . HOH I 4 .   ? -10.576   14.788   0.905     1.000 46.48068 ? 397 HOH A O   1 
HETATM 3854 O O   . HOH I 4 .   ? 0.87000   -3.45800 -25.14000 1.000 48.41446 ? 398 HOH A O   1 
HETATM 3855 O O   . HOH I 4 .   ? -4.229    5.501    -37.042   1.000 27.71973 ? 399 HOH A O   1 
HETATM 3856 O O   . HOH I 4 .   ? -14.66600 20.02500 0.62000   1.000 36.08903 ? 400 HOH A O   1 
HETATM 3857 O O   . HOH I 4 .   ? 3.137     16.266   -37.384   1.000 33.66207 ? 401 HOH A O   1 
HETATM 3858 O O   . HOH I 4 .   ? 4.704     14.336   -37.845   1.000 37.49338 ? 402 HOH A O   1 
HETATM 3859 O O   . HOH I 4 .   ? -9.22000  -0.13100 -22.06400 1.000 46.00565 ? 403 HOH A O   1 
HETATM 3860 O O   . HOH I 4 .   ? -0.87000  -3.40400 -27.17900 1.000 44.18238 ? 404 HOH A O   1 
HETATM 3861 O O   . HOH I 4 .   ? 10.64500  13.49200 0.17900   1.000 38.78605 ? 405 HOH A O   1 
HETATM 3862 O O   . HOH I 4 .   ? 1.49900   16.67500 -35.23400 1.000 36.31275 ? 406 HOH A O   1 
HETATM 3863 O O   . HOH I 4 .   ? 18.25300  17.53600 -34.55800 1.000 32.17387 ? 407 HOH A O   1 
HETATM 3864 O O   . HOH I 4 .   ? -0.00000  15.15300 -35.69850 0.50  44.84677 ? 408 HOH A O   1 
# 
