data_4B3E
# 
_entry.id   4B3E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4B3E         
PDBE  EBI-53451    
WWPDB D_1290053451 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE SUPEROXIDEDISMUTASE' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A, C111S' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A RESOLUTION' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER- ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU -ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2V0A unspecified 'ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE' 
PDB 2VR6 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION' 
PDB 2VR7 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION' 
PDB 2VR8 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION' 
PDB 2WKO unspecified 'STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.' 
PDB 2WYT unspecified '1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT' 
PDB 2WYZ unspecified 'L38V SOD1 MUTANT COMPLEXED WITH UMP' 
PDB 2WZ0 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH ANILINE.' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.' 
PDB 2WZ6 unspecified 'G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.' 
PDB 2XJK unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 2XJL unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS' 
PDB 4A7G unspecified 
'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -METHYLPIPERAZIN-1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.' 
PDB 4A7Q unspecified 
'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.' 
PDB 4A7R unspecified 
;STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL) QUINAZOLINE IN THE P21 SPACE GROUP
;
PDB 4A7S unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 5 -FLUOROURIDINE IN THE P21 SPACE GROUP' 
PDB 4A7T unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH ISOPROTERANOL IN THE P21 SPACE GROUP' 
PDB 4A7U unspecified 'STRUCTURE OF HUMAN I113T SOD1 COMPLEXED WITH ADRENALINE IN THE P21 SPACE GROUP.' 
PDB 4A7V unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH DOPAMINE IN THE P21 SPACE GROUP' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C-TERMINUS (THEORETICAL MODEL)
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4B3E 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2012-07-23 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strange, R.W.'  1 
'Hough, M.A.'    2 
'Antonyuk, S.V.' 3 
'Hasnain, S.S.'  4 
# 
_citation.id                        primary 
_citation.title                     
'Structural Evidence for a Copper-Bound Carbonate Intermediate in the Peroxidase and Dismutase Activities of Superoxide Dismutase.' 
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            7 
_citation.page_first                44811 
_citation.page_last                 ? 
_citation.year                      2012 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22984565 
_citation.pdbx_database_id_DOI      10.1371/JOURNAL.PONE.0044811 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strange, R.W.'  1 
primary 'Hough, M.A.'    2 
primary 'Antonyuk, S.V.' 3 
primary 'Hasnain, S.S.'  4 
# 
_cell.entry_id           4B3E 
_cell.length_a           165.994 
_cell.length_b           203.107 
_cell.length_c           144.384 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              80 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4B3E 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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 'SUPEROXIDE DISMUTASE [CU-ZN]' 15958.757 10   1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'              63.546    10   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    10   ?        ? ? ? 
4 non-polymer syn 'CARBONATE ION'                60.009    10   ?        ? ? ? 
5 non-polymer syn 'SULFATE ION'                  96.063    5    ?        ? ? ? 
6 water       nat water                          18.015    1587 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'SUPEROXIDE DISMUTASE 1, HSOD1, CU-ZN SUPEROXIDE DISMUTASE' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 CYS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_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      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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               
;BAKER'S YEAST
;
_entity_src_gen.pdbx_host_org_scientific_name      'SACCHAROMYCES CEREVISIAE' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4B3E A 1 ? 154 ? P00441 1 ? 154 ? 0 153 
2  1 4B3E B 1 ? 154 ? P00441 1 ? 154 ? 0 153 
3  1 4B3E C 1 ? 154 ? P00441 1 ? 154 ? 0 153 
4  1 4B3E D 1 ? 154 ? P00441 1 ? 154 ? 0 153 
5  1 4B3E E 1 ? 154 ? P00441 1 ? 154 ? 0 153 
6  1 4B3E F 1 ? 154 ? P00441 1 ? 154 ? 0 153 
7  1 4B3E G 1 ? 154 ? P00441 1 ? 154 ? 0 153 
8  1 4B3E H 1 ? 154 ? P00441 1 ? 154 ? 0 153 
9  1 4B3E I 1 ? 154 ? P00441 1 ? 154 ? 0 153 
10 1 4B3E J 1 ? 154 ? P00441 1 ? 154 ? 0 153 
# 
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 
CO3 non-polymer         . 'CARBONATE ION'   ? 'C O3 -2'        60.009  
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
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 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_exptl.entry_id          4B3E 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.8 
_exptl_crystal.density_percent_sol   68 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '1 M AMMONIUM SULPHATE, 50 MM TRIS PH 8.0 AND 50 MM NACL' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2007-09-21 
_diffrn_detector.details                MIRROR 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    SI111 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.87 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX9.6' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX9.6 
_diffrn_source.pdbx_wavelength             0.87 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4B3E 
_reflns.observed_criterion_sigma_I   . 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20.00 
_reflns.d_resolution_high            2.15 
_reflns.number_obs                   124983 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         94.7 
_reflns.pdbx_Rmerge_I_obs            0.12 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.10 
_reflns.B_iso_Wilson_estimate        28.0 
_reflns.pdbx_redundancy              5.5 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.15 
_reflns_shell.d_res_low              2.23 
_reflns_shell.percent_possible_all   96.3 
_reflns_shell.Rmerge_I_obs           0.68 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.20 
_reflns_shell.pdbx_redundancy        5.4 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4B3E 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     118562 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            2.15 
_refine.ls_percent_reflns_obs                    94.39 
_refine.ls_R_factor_obs                          0.17670 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17467 
_refine.ls_R_factor_R_free                       0.21496 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  6298 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.949 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.B_iso_mean                               28.335 
_refine.aniso_B[1][1]                            0.09 
_refine.aniso_B[2][2]                            -0.02 
_refine.aniso_B[3][3]                            -0.08 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.' 
_refine.pdbx_starting_model                      'PDB ENTRY 1SOS' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.170 
_refine.pdbx_overall_ESU_R_Free                  0.157 
_refine.overall_SU_ML                            0.096 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.871 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11100 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         85 
_refine_hist.number_atoms_solvent             1587 
_refine_hist.number_atoms_total               12772 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.019  ? 11384 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 7520  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.334  1.949  ? 15374 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.838  3.002  ? 18494 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.461  5.000  ? 1536  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       40.829 25.661 ? 484   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       12.586 15.000 ? 1860  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       9.432  15.000 ? 40    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.078  0.200  ? 1695  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.020  ? 13142 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 2058  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.148 
_refine_ls_shell.d_res_low                        2.203 
_refine_ls_shell.number_reflns_R_work             8365 
_refine_ls_shell.R_factor_R_work                  0.210 
_refine_ls_shell.percent_reflns_obs               95.26 
_refine_ls_shell.R_factor_R_free                  0.250 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             436 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  4B3E 
_struct.title                     'Structure of copper-zinc superoxide dismutase complexed with bicarbonate.' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE [CU-ZN] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4B3E 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 2 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 2 ? 
O  N N 3 ? 
P  N N 4 ? 
Q  N N 2 ? 
R  N N 3 ? 
S  N N 4 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 4 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 4 ? 
CA N N 5 ? 
DA N N 5 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 5 ? 
IA N N 2 ? 
JA N N 3 ? 
KA N N 4 ? 
LA N N 2 ? 
MA N N 3 ? 
NA N N 4 ? 
OA N N 2 ? 
PA N N 3 ? 
QA N N 4 ? 
RA N N 5 ? 
SA N N 5 ? 
TA N N 6 ? 
UA N N 6 ? 
VA N N 6 ? 
WA N N 6 ? 
XA N N 6 ? 
YA N N 6 ? 
ZA N N 6 ? 
AB N N 6 ? 
BB N N 6 ? 
CB N N 6 ? 
# 
_struct_biol.id   1 
# 
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  1  ALA A 56  ? GLY A 62  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  GLU A 134 ? GLY A 139 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3  3  ALA B 56  ? GLY B 62  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  4  GLU B 133 ? THR B 138 ? GLU B 132 THR B 137 1 ? 6 
HELX_P HELX_P5  5  ALA C 56  ? GLY C 62  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  6  ALA D 56  ? GLY D 62  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P7  7  ASN D 132 ? GLY D 139 ? ASN D 131 GLY D 138 1 ? 8 
HELX_P HELX_P8  8  ALA E 56  ? GLY E 62  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P9  9  GLU E 134 ? GLY E 139 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P10 10 ALA F 56  ? GLY F 62  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P11 11 ALA G 56  ? GLY G 62  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P12 12 SER G 108 ? HIS G 111 ? SER G 107 HIS G 110 5 ? 4 
HELX_P HELX_P13 13 GLU G 134 ? GLY G 139 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P14 14 ALA H 56  ? GLY H 62  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P15 15 GLU H 134 ? GLY H 139 ? GLU H 133 GLY H 138 1 ? 6 
HELX_P HELX_P16 16 ALA I 56  ? GLY I 62  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P17 17 ALA J 56  ? GLY J 62  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P18 18 GLU J 134 ? GLY J 139 ? GLU J 133 GLY J 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A  CYS 58 SG ? ? ? 1_555 A  CYS 147 SG  ? ? A CYS 57  A CYS 146  1_555 ? ? ? ? ? ? ? 2.111 ? 
disulf2  disulf ? ? B  CYS 58 SG ? ? ? 1_555 B  CYS 147 SG  ? ? B CYS 57  B CYS 146  1_555 ? ? ? ? ? ? ? 2.116 ? 
disulf3  disulf ? ? C  CYS 58 SG ? ? ? 1_555 C  CYS 147 SG  ? ? C CYS 57  C CYS 146  1_555 ? ? ? ? ? ? ? 2.112 ? 
disulf4  disulf ? ? D  CYS 58 SG ? ? ? 1_555 D  CYS 147 SG  ? ? D CYS 57  D CYS 146  1_555 ? ? ? ? ? ? ? 2.125 ? 
disulf5  disulf ? ? E  CYS 58 SG ? ? ? 1_555 E  CYS 147 SG  ? ? E CYS 57  E CYS 146  1_555 ? ? ? ? ? ? ? 2.092 ? 
disulf6  disulf ? ? F  CYS 58 SG ? ? ? 1_555 F  CYS 147 SG  ? ? F CYS 57  F CYS 146  1_555 ? ? ? ? ? ? ? 2.111 ? 
disulf7  disulf ? ? G  CYS 58 SG ? ? ? 1_555 G  CYS 147 SG  ? ? G CYS 57  G CYS 146  1_555 ? ? ? ? ? ? ? 2.107 ? 
disulf8  disulf ? ? H  CYS 58 SG ? ? ? 1_555 H  CYS 147 SG  ? ? H CYS 57  H CYS 146  1_555 ? ? ? ? ? ? ? 2.128 ? 
disulf9  disulf ? ? I  CYS 58 SG ? ? ? 1_555 I  CYS 147 SG  ? ? I CYS 57  I CYS 146  1_555 ? ? ? ? ? ? ? 2.106 ? 
disulf10 disulf ? ? J  CYS 58 SG ? ? ? 1_555 J  CYS 147 SG  ? ? J CYS 57  J CYS 146  1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc1  metalc ? ? K  CU  .  CU ? ? ? 1_555 A  HIS 47  ND1 ? ? A CU  154 A HIS 46   1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc2  metalc ? ? K  CU  .  CU ? ? ? 1_555 A  HIS 121 NE2 ? ? A CU  154 A HIS 120  1_555 ? ? ? ? ? ? ? 2.086 ? 
metalc3  metalc ? ? K  CU  .  CU ? ? ? 1_555 A  HIS 49  NE2 ? ? A CU  154 A HIS 48   1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc4  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A  ASP 84  OD1 ? ? A ZN  155 A ASP 83   1_555 ? ? ? ? ? ? ? 1.908 ? 
metalc5  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A  HIS 64  ND1 ? ? A ZN  155 A HIS 63   1_555 ? ? ? ? ? ? ? 1.939 ? 
metalc6  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A  HIS 81  ND1 ? ? A ZN  155 A HIS 80   1_555 ? ? ? ? ? ? ? 2.008 ? 
metalc7  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A  HIS 72  ND1 ? ? A ZN  155 A HIS 71   1_555 ? ? ? ? ? ? ? 2.062 ? 
metalc8  metalc ? ? M  CO3 .  O1 ? ? ? 1_555 K  CU  .   CU  ? ? A CO3 156 A CU  154  1_555 ? ? ? ? ? ? ? 2.279 ? 
metalc9  metalc ? ? N  CU  .  CU ? ? ? 1_555 B  HIS 49  NE2 ? ? B CU  154 B HIS 48   1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc10 metalc ? ? N  CU  .  CU ? ? ? 1_555 B  HIS 47  ND1 ? ? B CU  154 B HIS 46   1_555 ? ? ? ? ? ? ? 2.002 ? 
metalc11 metalc ? ? N  CU  .  CU ? ? ? 1_555 B  HIS 121 NE2 ? ? B CU  154 B HIS 120  1_555 ? ? ? ? ? ? ? 2.090 ? 
metalc12 metalc ? ? O  ZN  .  ZN ? ? ? 1_555 B  ASP 84  OD1 ? ? B ZN  155 B ASP 83   1_555 ? ? ? ? ? ? ? 1.851 ? 
metalc13 metalc ? ? O  ZN  .  ZN ? ? ? 1_555 B  HIS 64  ND1 ? ? B ZN  155 B HIS 63   1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc14 metalc ? ? O  ZN  .  ZN ? ? ? 1_555 B  HIS 72  ND1 ? ? B ZN  155 B HIS 71   1_555 ? ? ? ? ? ? ? 2.063 ? 
metalc15 metalc ? ? P  CO3 .  O2 ? ? ? 1_555 N  CU  .   CU  ? ? B CO3 156 B CU  154  1_555 ? ? ? ? ? ? ? 2.133 ? 
metalc16 metalc ? ? Q  CU  .  CU ? ? ? 1_555 C  HIS 47  ND1 ? ? C CU  154 C HIS 46   1_555 ? ? ? ? ? ? ? 2.143 ? 
metalc17 metalc ? ? Q  CU  .  CU ? ? ? 1_555 C  HIS 64  NE2 ? ? C CU  154 C HIS 63   1_555 ? ? ? ? ? ? ? 2.656 ? 
metalc18 metalc ? ? Q  CU  .  CU ? ? ? 1_555 C  HIS 121 NE2 ? ? C CU  154 C HIS 120  1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc19 metalc ? ? Q  CU  .  CU ? ? ? 1_555 VA HOH .   O   ? ? C CU  154 C HOH 2086 1_555 ? ? ? ? ? ? ? 2.618 ? 
metalc20 metalc ? ? Q  CU  .  CU ? ? ? 1_555 C  HIS 49  NE2 ? ? C CU  154 C HIS 48   1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc21 metalc ? ? R  ZN  .  ZN ? ? ? 1_555 C  HIS 81  ND1 ? ? C ZN  155 C HIS 80   1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc22 metalc ? ? R  ZN  .  ZN ? ? ? 1_555 C  ASP 84  OD1 ? ? C ZN  155 C ASP 83   1_555 ? ? ? ? ? ? ? 1.927 ? 
metalc23 metalc ? ? R  ZN  .  ZN ? ? ? 1_555 C  HIS 64  ND1 ? ? C ZN  155 C HIS 63   1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc24 metalc ? ? R  ZN  .  ZN ? ? ? 1_555 C  HIS 72  ND1 ? ? C ZN  155 C HIS 71   1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc25 metalc ? ? T  CU  .  CU ? ? ? 1_555 D  HIS 49  NE2 ? ? D CU  154 D HIS 48   1_555 ? ? ? ? ? ? ? 2.068 ? 
metalc26 metalc ? ? T  CU  .  CU ? ? ? 1_555 D  HIS 121 NE2 ? ? D CU  154 D HIS 120  1_555 ? ? ? ? ? ? ? 1.971 ? 
metalc27 metalc ? ? T  CU  .  CU ? ? ? 1_555 D  HIS 47  ND1 ? ? D CU  154 D HIS 46   1_555 ? ? ? ? ? ? ? 2.129 ? 
metalc28 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 D  ASP 84  OD1 ? ? D ZN  155 D ASP 83   1_555 ? ? ? ? ? ? ? 1.932 ? 
metalc29 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 D  HIS 72  ND1 ? ? D ZN  155 D HIS 71   1_555 ? ? ? ? ? ? ? 2.158 ? 
metalc30 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 D  HIS 64  ND1 ? ? D ZN  155 D HIS 63   1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc31 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 D  HIS 81  ND1 ? ? D ZN  155 D HIS 80   1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc32 metalc ? ? W  CU  .  CU ? ? ? 1_555 E  HIS 47  ND1 ? ? E CU  154 E HIS 46   1_555 ? ? ? ? ? ? ? 2.219 ? 
metalc33 metalc ? ? W  CU  .  CU ? ? ? 1_555 E  HIS 121 NE2 ? ? E CU  154 E HIS 120  1_555 ? ? ? ? ? ? ? 2.043 ? 
metalc34 metalc ? ? W  CU  .  CU ? ? ? 1_555 E  HIS 49  NE2 ? ? E CU  154 E HIS 48   1_555 ? ? ? ? ? ? ? 2.199 ? 
metalc35 metalc ? ? X  ZN  .  ZN ? ? ? 1_555 E  HIS 81  ND1 ? ? E ZN  155 E HIS 80   1_555 ? ? ? ? ? ? ? 2.091 ? 
metalc36 metalc ? ? X  ZN  .  ZN ? ? ? 1_555 E  HIS 72  ND1 ? ? E ZN  155 E HIS 71   1_555 ? ? ? ? ? ? ? 2.110 ? 
metalc37 metalc ? ? X  ZN  .  ZN ? ? ? 1_555 E  ASP 84  OD1 ? ? E ZN  155 E ASP 83   1_555 ? ? ? ? ? ? ? 1.936 ? 
metalc38 metalc ? ? X  ZN  .  ZN ? ? ? 1_555 E  HIS 64  ND1 ? ? E ZN  155 E HIS 63   1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc39 metalc ? ? Z  CU  .  CU ? ? ? 1_555 F  HIS 121 NE2 ? ? F CU  154 F HIS 120  1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc40 metalc ? ? Z  CU  .  CU ? ? ? 1_555 F  HIS 47  ND1 ? ? F CU  154 F HIS 46   1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc41 metalc ? ? Z  CU  .  CU ? ? ? 1_555 F  HIS 49  NE2 ? ? F CU  154 F HIS 48   1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc42 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 F  ASP 84  OD1 ? ? F ZN  155 F ASP 83   1_555 ? ? ? ? ? ? ? 1.915 ? 
metalc43 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 F  HIS 64  ND1 ? ? F ZN  155 F HIS 63   1_555 ? ? ? ? ? ? ? 1.889 ? 
metalc44 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 F  HIS 81  ND1 ? ? F ZN  155 F HIS 80   1_555 ? ? ? ? ? ? ? 2.067 ? 
metalc45 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 F  HIS 72  ND1 ? ? F ZN  155 F HIS 71   1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc46 metalc ? ? EA CU  .  CU ? ? ? 1_555 G  HIS 47  ND1 ? ? G CU  154 G HIS 46   1_555 ? ? ? ? ? ? ? 2.119 ? 
metalc47 metalc ? ? EA CU  .  CU ? ? ? 1_555 G  HIS 64  NE2 ? ? G CU  154 G HIS 63   1_555 ? ? ? ? ? ? ? 2.608 ? 
metalc48 metalc ? ? EA CU  .  CU ? ? ? 1_555 G  HIS 121 NE2 ? ? G CU  154 G HIS 120  1_555 ? ? ? ? ? ? ? 2.084 ? 
metalc49 metalc ? ? EA CU  .  CU ? ? ? 1_555 G  HIS 49  NE2 ? ? G CU  154 G HIS 48   1_555 ? ? ? ? ? ? ? 2.122 ? 
metalc50 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 G  HIS 64  ND1 ? ? G ZN  155 G HIS 63   1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc51 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 G  ASP 84  OD1 ? ? G ZN  155 G ASP 83   1_555 ? ? ? ? ? ? ? 1.909 ? 
metalc52 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 G  HIS 72  ND1 ? ? G ZN  155 G HIS 71   1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc53 metalc ? ? FA ZN  .  ZN ? ? ? 1_555 G  HIS 81  ND1 ? ? G ZN  155 G HIS 80   1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc54 metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 47  ND1 ? ? H CU  154 H HIS 46   1_555 ? ? ? ? ? ? ? 2.140 ? 
metalc55 metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 49  NE2 ? ? H CU  154 H HIS 48   1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc56 metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 121 NE2 ? ? H CU  154 H HIS 120  1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc57 metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 72  ND1 ? ? H ZN  155 H HIS 71   1_555 ? ? ? ? ? ? ? 2.099 ? 
metalc58 metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 64  ND1 ? ? H ZN  155 H HIS 63   1_555 ? ? ? ? ? ? ? 1.929 ? 
metalc59 metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 81  ND1 ? ? H ZN  155 H HIS 80   1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc60 metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  ASP 84  OD1 ? ? H ZN  155 H ASP 83   1_555 ? ? ? ? ? ? ? 1.904 ? 
metalc61 metalc ? ? LA CU  .  CU ? ? ? 1_555 BB HOH .   O   ? ? I CU  154 I HOH 2068 1_555 ? ? ? ? ? ? ? 1.716 ? 
metalc62 metalc ? ? LA CU  .  CU ? ? ? 1_555 I  HIS 47  ND1 ? ? I CU  154 I HIS 46   1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc63 metalc ? ? LA CU  .  CU ? ? ? 1_555 I  HIS 49  NE2 ? ? I CU  154 I HIS 48   1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc64 metalc ? ? LA CU  .  CU ? ? ? 1_555 I  HIS 121 NE2 ? ? I CU  154 I HIS 120  1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc65 metalc ? ? MA ZN  .  ZN ? ? ? 1_555 I  HIS 81  ND1 ? ? I ZN  155 I HIS 80   1_555 ? ? ? ? ? ? ? 2.016 ? 
metalc66 metalc ? ? MA ZN  .  ZN ? ? ? 1_555 I  HIS 64  ND1 ? ? I ZN  155 I HIS 63   1_555 ? ? ? ? ? ? ? 1.925 ? 
metalc67 metalc ? ? MA ZN  .  ZN ? ? ? 1_555 I  ASP 84  OD1 ? ? I ZN  155 I ASP 83   1_555 ? ? ? ? ? ? ? 1.905 ? 
metalc68 metalc ? ? MA ZN  .  ZN ? ? ? 1_555 I  HIS 72  ND1 ? ? I ZN  155 I HIS 71   1_555 ? ? ? ? ? ? ? 2.007 ? 
metalc69 metalc ? ? OA CU  .  CU ? ? ? 1_555 J  HIS 49  NE2 ? ? J CU  154 J HIS 48   1_555 ? ? ? ? ? ? ? 2.120 ? 
metalc70 metalc ? ? OA CU  .  CU ? ? ? 1_555 J  HIS 121 NE2 ? ? J CU  154 J HIS 120  1_555 ? ? ? ? ? ? ? 2.118 ? 
metalc71 metalc ? ? OA CU  .  CU ? ? ? 1_555 J  HIS 47  ND1 ? ? J CU  154 J HIS 46   1_555 ? ? ? ? ? ? ? 2.217 ? 
metalc72 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 J  HIS 72  ND1 ? ? J ZN  155 J HIS 71   1_555 ? ? ? ? ? ? ? 2.118 ? 
metalc73 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 J  HIS 64  ND1 ? ? J ZN  155 J HIS 63   1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc74 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 J  HIS 81  ND1 ? ? J ZN  155 J HIS 80   1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc75 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 J  ASP 84  OD1 ? ? J ZN  155 J ASP 83   1_555 ? ? ? ? ? ? ? 1.919 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
BA ? 5 ? 
BB ? 4 ? 
CA ? 5 ? 
CB ? 4 ? 
DA ? 5 ? 
DB ? 4 ? 
EA ? 5 ? 
EB ? 4 ? 
FA ? 5 ? 
FB ? 4 ? 
GA ? 5 ? 
GB ? 4 ? 
HA ? 5 ? 
HB ? 4 ? 
IA ? 5 ? 
IB ? 4 ? 
JA ? 5 ? 
JB ? 4 ? 
# 
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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CB 3 4 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 4 5 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
EA 1 2 ? anti-parallel 
EA 2 3 ? anti-parallel 
EA 3 4 ? anti-parallel 
EA 4 5 ? anti-parallel 
EB 1 2 ? anti-parallel 
EB 2 3 ? anti-parallel 
EB 3 4 ? anti-parallel 
FA 1 2 ? anti-parallel 
FA 2 3 ? anti-parallel 
FA 3 4 ? anti-parallel 
FA 4 5 ? anti-parallel 
FB 1 2 ? anti-parallel 
FB 2 3 ? anti-parallel 
FB 3 4 ? anti-parallel 
GA 1 2 ? anti-parallel 
GA 2 3 ? anti-parallel 
GA 3 4 ? anti-parallel 
GA 4 5 ? anti-parallel 
GB 1 2 ? anti-parallel 
GB 2 3 ? anti-parallel 
GB 3 4 ? anti-parallel 
HA 1 2 ? anti-parallel 
HA 2 3 ? anti-parallel 
HA 3 4 ? anti-parallel 
HA 4 5 ? anti-parallel 
HB 1 2 ? anti-parallel 
HB 2 3 ? anti-parallel 
HB 3 4 ? anti-parallel 
IA 1 2 ? anti-parallel 
IA 2 3 ? anti-parallel 
IA 3 4 ? anti-parallel 
IA 4 5 ? anti-parallel 
IB 1 2 ? anti-parallel 
IB 2 3 ? anti-parallel 
IB 3 4 ? anti-parallel 
JA 1 2 ? anti-parallel 
JA 2 3 ? anti-parallel 
JA 3 4 ? anti-parallel 
JA 4 5 ? anti-parallel 
JB 1 2 ? anti-parallel 
JB 2 3 ? anti-parallel 
JB 3 4 ? 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 
AA 1 ALA A 96  ? ASP A 102 ? ALA A 95  ASP A 101 
AA 2 VAL A 30  ? LYS A 37  ? VAL A 29  LYS A 36  
AA 3 GLN A 16  ? GLN A 23  ? GLN A 15  GLN A 22  
AA 4 THR A 3   ? LEU A 9   ? THR A 2   LEU A 8   
AA 5 GLY A 151 ? ILE A 152 ? GLY A 150 ILE A 151 
AB 1 ASP A 84  ? ALA A 90  ? ASP A 83  ALA A 89  
AB 2 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
AB 3 THR A 117 ? HIS A 121 ? THR A 116 HIS A 120 
AB 4 ARG A 144 ? VAL A 149 ? ARG A 143 VAL A 148 
BA 1 ALA B 96  ? ASP B 102 ? ALA B 95  ASP B 101 
BA 2 VAL B 30  ? LYS B 37  ? VAL B 29  LYS B 36  
BA 3 GLN B 16  ? GLN B 23  ? GLN B 15  GLN B 22  
BA 4 THR B 3   ? LEU B 9   ? THR B 2   LEU B 8   
BA 5 GLY B 151 ? ALA B 153 ? GLY B 150 ALA B 152 
BB 1 ASP B 84  ? ALA B 90  ? ASP B 83  ALA B 89  
BB 2 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
BB 3 THR B 117 ? HIS B 121 ? THR B 116 HIS B 120 
BB 4 ARG B 144 ? VAL B 149 ? ARG B 143 VAL B 148 
CA 1 ALA C 96  ? ASP C 102 ? ALA C 95  ASP C 101 
CA 2 VAL C 30  ? LYS C 37  ? VAL C 29  LYS C 36  
CA 3 GLN C 16  ? GLN C 23  ? GLN C 15  GLN C 22  
CA 4 THR C 3   ? LEU C 9   ? THR C 2   LEU C 8   
CA 5 GLY C 151 ? ILE C 152 ? GLY C 150 ILE C 151 
CB 1 ASP C 84  ? ALA C 90  ? ASP C 83  ALA C 89  
CB 2 GLY C 42  ? HIS C 49  ? GLY C 41  HIS C 48  
CB 3 THR C 117 ? HIS C 121 ? THR C 116 HIS C 120 
CB 4 ARG C 144 ? VAL C 149 ? ARG C 143 VAL C 148 
DA 1 ALA D 96  ? ASP D 102 ? ALA D 95  ASP D 101 
DA 2 VAL D 30  ? LYS D 37  ? VAL D 29  LYS D 36  
DA 3 GLN D 16  ? GLU D 22  ? GLN D 15  GLU D 21  
DA 4 LYS D 4   ? LEU D 9   ? LYS D 3   LEU D 8   
DA 5 GLY D 151 ? ILE D 152 ? GLY D 150 ILE D 151 
DB 1 ASP D 84  ? ALA D 90  ? ASP D 83  ALA D 89  
DB 2 GLY D 42  ? HIS D 49  ? GLY D 41  HIS D 48  
DB 3 THR D 117 ? HIS D 121 ? THR D 116 HIS D 120 
DB 4 ARG D 144 ? VAL D 149 ? ARG D 143 VAL D 148 
EA 1 ALA E 96  ? ASP E 102 ? ALA E 95  ASP E 101 
EA 2 VAL E 30  ? LYS E 37  ? VAL E 29  LYS E 36  
EA 3 GLN E 16  ? GLU E 22  ? GLN E 15  GLU E 21  
EA 4 LYS E 4   ? LYS E 10  ? LYS E 3   LYS E 9   
EA 5 GLY E 151 ? ILE E 152 ? GLY E 150 ILE E 151 
EB 1 ASP E 84  ? ALA E 90  ? ASP E 83  ALA E 89  
EB 2 GLY E 42  ? HIS E 49  ? GLY E 41  HIS E 48  
EB 3 THR E 117 ? HIS E 121 ? THR E 116 HIS E 120 
EB 4 ARG E 144 ? VAL E 149 ? ARG E 143 VAL E 148 
FA 1 ALA F 96  ? ASP F 102 ? ALA F 95  ASP F 101 
FA 2 VAL F 30  ? LYS F 37  ? VAL F 29  LYS F 36  
FA 3 GLN F 16  ? GLU F 22  ? GLN F 15  GLU F 21  
FA 4 LYS F 4   ? LYS F 10  ? LYS F 3   LYS F 9   
FA 5 GLY F 151 ? ILE F 152 ? GLY F 150 ILE F 151 
FB 1 ASP F 84  ? ALA F 90  ? ASP F 83  ALA F 89  
FB 2 GLY F 42  ? HIS F 49  ? GLY F 41  HIS F 48  
FB 3 THR F 117 ? HIS F 121 ? THR F 116 HIS F 120 
FB 4 ARG F 144 ? VAL F 149 ? ARG F 143 VAL F 148 
GA 1 ALA G 96  ? ASP G 102 ? ALA G 95  ASP G 101 
GA 2 VAL G 30  ? LYS G 37  ? VAL G 29  LYS G 36  
GA 3 GLN G 16  ? GLU G 22  ? GLN G 15  GLU G 21  
GA 4 LYS G 4   ? LYS G 10  ? LYS G 3   LYS G 9   
GA 5 GLY G 151 ? ILE G 152 ? GLY G 150 ILE G 151 
GB 1 ASP G 84  ? ALA G 90  ? ASP G 83  ALA G 89  
GB 2 GLY G 42  ? HIS G 49  ? GLY G 41  HIS G 48  
GB 3 THR G 117 ? HIS G 121 ? THR G 116 HIS G 120 
GB 4 ARG G 144 ? VAL G 149 ? ARG G 143 VAL G 148 
HA 1 ALA H 96  ? ASP H 102 ? ALA H 95  ASP H 101 
HA 2 VAL H 30  ? LYS H 37  ? VAL H 29  LYS H 36  
HA 3 GLN H 16  ? GLU H 22  ? GLN H 15  GLU H 21  
HA 4 LYS H 4   ? LEU H 9   ? LYS H 3   LEU H 8   
HA 5 GLY H 151 ? ILE H 152 ? GLY H 150 ILE H 151 
HB 1 ASP H 84  ? ALA H 90  ? ASP H 83  ALA H 89  
HB 2 GLY H 42  ? HIS H 49  ? GLY H 41  HIS H 48  
HB 3 THR H 117 ? HIS H 121 ? THR H 116 HIS H 120 
HB 4 ARG H 144 ? VAL H 149 ? ARG H 143 VAL H 148 
IA 1 ALA I 96  ? ASP I 102 ? ALA I 95  ASP I 101 
IA 2 VAL I 30  ? LYS I 37  ? VAL I 29  LYS I 36  
IA 3 GLN I 16  ? GLU I 22  ? GLN I 15  GLU I 21  
IA 4 LYS I 4   ? LEU I 9   ? LYS I 3   LEU I 8   
IA 5 GLY I 151 ? ILE I 152 ? GLY I 150 ILE I 151 
IB 1 ASP I 84  ? ALA I 90  ? ASP I 83  ALA I 89  
IB 2 GLY I 42  ? HIS I 49  ? GLY I 41  HIS I 48  
IB 3 THR I 117 ? HIS I 121 ? THR I 116 HIS I 120 
IB 4 ARG I 144 ? VAL I 149 ? ARG I 143 VAL I 148 
JA 1 ALA J 96  ? ASP J 102 ? ALA J 95  ASP J 101 
JA 2 VAL J 30  ? LYS J 37  ? VAL J 29  LYS J 36  
JA 3 GLN J 16  ? GLU J 22  ? GLN J 15  GLU J 21  
JA 4 LYS J 4   ? LYS J 10  ? LYS J 3   LYS J 9   
JA 5 GLY J 151 ? ILE J 152 ? GLY J 150 ILE J 151 
JB 1 ASP J 84  ? ALA J 90  ? ASP J 83  ALA J 89  
JB 2 GLY J 42  ? HIS J 49  ? GLY J 41  HIS J 48  
JB 3 THR J 117 ? HIS J 121 ? THR J 116 HIS J 120 
JB 4 ARG J 144 ? VAL J 149 ? ARG J 143 VAL J 148 
# 
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 
AA 1 2 N ASP A 102 ? N ASP A 101 O VAL A 30  ? O VAL A 29  
AA 2 3 N LYS A 37  ? N LYS A 36  O GLN A 16  ? O GLN A 15  
AA 3 4 N GLN A 23  ? N GLN A 22  O THR A 3   ? O THR A 2   
AA 4 5 N VAL A 6   ? N VAL A 5   O GLY A 151 ? O GLY A 150 
AB 1 2 N ALA A 90  ? N ALA A 89  O GLY A 42  ? O GLY A 41  
AB 2 3 N HIS A 49  ? N HIS A 48  O THR A 117 ? O THR A 116 
AB 3 4 O VAL A 120 ? O VAL A 119 N LEU A 145 ? N LEU A 144 
BA 1 2 N ASP B 102 ? N ASP B 101 O VAL B 30  ? O VAL B 29  
BA 2 3 N LYS B 37  ? N LYS B 36  O GLN B 16  ? O GLN B 15  
BA 3 4 N GLN B 23  ? N GLN B 22  O THR B 3   ? O THR B 2   
BA 4 5 N VAL B 6   ? N VAL B 5   O GLY B 151 ? O GLY B 150 
BB 1 2 N ALA B 90  ? N ALA B 89  O GLY B 42  ? O GLY B 41  
BB 2 3 N HIS B 49  ? N HIS B 48  O THR B 117 ? O THR B 116 
BB 3 4 O VAL B 120 ? O VAL B 119 N LEU B 145 ? N LEU B 144 
CA 1 2 N ASP C 102 ? N ASP C 101 O VAL C 30  ? O VAL C 29  
CA 2 3 N LYS C 37  ? N LYS C 36  O GLN C 16  ? O GLN C 15  
CA 3 4 N GLN C 23  ? N GLN C 22  O THR C 3   ? O THR C 2   
CA 4 5 N VAL C 6   ? N VAL C 5   O GLY C 151 ? O GLY C 150 
CB 1 2 N ALA C 90  ? N ALA C 89  O GLY C 42  ? O GLY C 41  
CB 2 3 N HIS C 49  ? N HIS C 48  O THR C 117 ? O THR C 116 
CB 3 4 O VAL C 120 ? O VAL C 119 N LEU C 145 ? N LEU C 144 
DA 1 2 N ASP D 102 ? N ASP D 101 O VAL D 30  ? O VAL D 29  
DA 2 3 N LYS D 37  ? N LYS D 36  O GLN D 16  ? O GLN D 15  
DA 3 4 N PHE D 21  ? N PHE D 20  O ALA D 5   ? O ALA D 4   
DA 4 5 N VAL D 6   ? N VAL D 5   O GLY D 151 ? O GLY D 150 
DB 1 2 N ALA D 90  ? N ALA D 89  O GLY D 42  ? O GLY D 41  
DB 2 3 N HIS D 49  ? N HIS D 48  O THR D 117 ? O THR D 116 
DB 3 4 O VAL D 120 ? O VAL D 119 N LEU D 145 ? N LEU D 144 
EA 1 2 N ASP E 102 ? N ASP E 101 O VAL E 30  ? O VAL E 29  
EA 2 3 N LYS E 37  ? N LYS E 36  O GLN E 16  ? O GLN E 15  
EA 3 4 N PHE E 21  ? N PHE E 20  O ALA E 5   ? O ALA E 4   
EA 4 5 N VAL E 6   ? N VAL E 5   O GLY E 151 ? O GLY E 150 
EB 1 2 N ALA E 90  ? N ALA E 89  O GLY E 42  ? O GLY E 41  
EB 2 3 N HIS E 49  ? N HIS E 48  O THR E 117 ? O THR E 116 
EB 3 4 O VAL E 120 ? O VAL E 119 N LEU E 145 ? N LEU E 144 
FA 1 2 N ASP F 102 ? N ASP F 101 O VAL F 30  ? O VAL F 29  
FA 2 3 N LYS F 37  ? N LYS F 36  O GLN F 16  ? O GLN F 15  
FA 3 4 N PHE F 21  ? N PHE F 20  O ALA F 5   ? O ALA F 4   
FA 4 5 N VAL F 6   ? N VAL F 5   O GLY F 151 ? O GLY F 150 
FB 1 2 N ALA F 90  ? N ALA F 89  O GLY F 42  ? O GLY F 41  
FB 2 3 N HIS F 49  ? N HIS F 48  O THR F 117 ? O THR F 116 
FB 3 4 O VAL F 120 ? O VAL F 119 N LEU F 145 ? N LEU F 144 
GA 1 2 N ASP G 102 ? N ASP G 101 O VAL G 30  ? O VAL G 29  
GA 2 3 N LYS G 37  ? N LYS G 36  O GLN G 16  ? O GLN G 15  
GA 3 4 N PHE G 21  ? N PHE G 20  O ALA G 5   ? O ALA G 4   
GA 4 5 N VAL G 6   ? N VAL G 5   O GLY G 151 ? O GLY G 150 
GB 1 2 N ALA G 90  ? N ALA G 89  O GLY G 42  ? O GLY G 41  
GB 2 3 N HIS G 49  ? N HIS G 48  O THR G 117 ? O THR G 116 
GB 3 4 O VAL G 120 ? O VAL G 119 N LEU G 145 ? N LEU G 144 
HA 1 2 N ASP H 102 ? N ASP H 101 O VAL H 30  ? O VAL H 29  
HA 2 3 N LYS H 37  ? N LYS H 36  O GLN H 16  ? O GLN H 15  
HA 3 4 N PHE H 21  ? N PHE H 20  O ALA H 5   ? O ALA H 4   
HA 4 5 N VAL H 6   ? N VAL H 5   O GLY H 151 ? O GLY H 150 
HB 1 2 N ALA H 90  ? N ALA H 89  O GLY H 42  ? O GLY H 41  
HB 2 3 N HIS H 49  ? N HIS H 48  O THR H 117 ? O THR H 116 
HB 3 4 O VAL H 120 ? O VAL H 119 N LEU H 145 ? N LEU H 144 
IA 1 2 N ASP I 102 ? N ASP I 101 O VAL I 30  ? O VAL I 29  
IA 2 3 N LYS I 37  ? N LYS I 36  O GLN I 16  ? O GLN I 15  
IA 3 4 N PHE I 21  ? N PHE I 20  O ALA I 5   ? O ALA I 4   
IA 4 5 N VAL I 6   ? N VAL I 5   O GLY I 151 ? O GLY I 150 
IB 1 2 N ALA I 90  ? N ALA I 89  O GLY I 42  ? O GLY I 41  
IB 2 3 N HIS I 49  ? N HIS I 48  O THR I 117 ? O THR I 116 
IB 3 4 O VAL I 120 ? O VAL I 119 N LEU I 145 ? N LEU I 144 
JA 1 2 N ASP J 102 ? N ASP J 101 O VAL J 30  ? O VAL J 29  
JA 2 3 N LYS J 37  ? N LYS J 36  O GLN J 16  ? O GLN J 15  
JA 3 4 N PHE J 21  ? N PHE J 20  O ALA J 5   ? O ALA J 4   
JA 4 5 N VAL J 6   ? N VAL J 5   O GLY J 151 ? O GLY J 150 
JB 1 2 N ALA J 90  ? N ALA J 89  O GLY J 42  ? O GLY J 41  
JB 2 3 N HIS J 49  ? N HIS J 48  O THR J 117 ? O THR J 116 
JB 3 4 O VAL J 120 ? O VAL J 119 N LEU J 145 ? N LEU J 144 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU A 154'   
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 155'   
AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CO3 A 156'  
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU B 154'   
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 155'   
AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE CO3 B 156'  
AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU C 154'   
AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN C 155'   
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CO3 C 156'  
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU D 154'   
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 155'   
BC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE CO3 D 156'  
BC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU E 154'   
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN E 155'   
BC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE CO3 E 156'  
BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU F 154'   
BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 155'   
BC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CO3 F 156'  
CC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU G 154'   
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN G 155'   
CC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CO3 G 156'  
CC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU H 154'   
CC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN H 155'   
CC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CO3 H 156'  
CC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU I 154'   
CC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 155'   
CC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CO3 I 156'  
DC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU J 154'   
DC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 155'   
DC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CO3 J 156'  
DC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 F 1154' 
DC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 G 1154' 
DC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 J 1154' 
DC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE SO4 J 1155' 
DC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 F 1155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5 HIS A  47  ? HIS A 46   . ? 1_555 ? 
2   AC1 5 HIS A  49  ? HIS A 48   . ? 1_555 ? 
3   AC1 5 HIS A  64  ? HIS A 63   . ? 1_555 ? 
4   AC1 5 HIS A  121 ? HIS A 120  . ? 1_555 ? 
5   AC1 5 CO3 M  .   ? CO3 A 156  . ? 1_555 ? 
6   AC2 4 HIS A  64  ? HIS A 63   . ? 1_555 ? 
7   AC2 4 HIS A  72  ? HIS A 71   . ? 1_555 ? 
8   AC2 4 HIS A  81  ? HIS A 80   . ? 1_555 ? 
9   AC2 4 ASP A  84  ? ASP A 83   . ? 1_555 ? 
10  AC3 7 HIS A  49  ? HIS A 48   . ? 1_555 ? 
11  AC3 7 HIS A  64  ? HIS A 63   . ? 1_555 ? 
12  AC3 7 HIS A  121 ? HIS A 120  . ? 1_555 ? 
13  AC3 7 THR A  138 ? THR A 137  . ? 1_555 ? 
14  AC3 7 ARG A  144 ? ARG A 143  . ? 1_555 ? 
15  AC3 7 CU  K  .   ? CU  A 154  . ? 1_555 ? 
16  AC3 7 HOH TA .   ? HOH A 2166 . ? 1_555 ? 
17  AC4 5 HIS B  47  ? HIS B 46   . ? 1_555 ? 
18  AC4 5 HIS B  49  ? HIS B 48   . ? 1_555 ? 
19  AC4 5 HIS B  64  ? HIS B 63   . ? 1_555 ? 
20  AC4 5 HIS B  121 ? HIS B 120  . ? 1_555 ? 
21  AC4 5 CO3 P  .   ? CO3 B 156  . ? 1_555 ? 
22  AC5 4 HIS B  64  ? HIS B 63   . ? 1_555 ? 
23  AC5 4 HIS B  72  ? HIS B 71   . ? 1_555 ? 
24  AC5 4 HIS B  81  ? HIS B 80   . ? 1_555 ? 
25  AC5 4 ASP B  84  ? ASP B 83   . ? 1_555 ? 
26  AC6 9 HIS B  47  ? HIS B 46   . ? 1_555 ? 
27  AC6 9 HIS B  49  ? HIS B 48   . ? 1_555 ? 
28  AC6 9 HIS B  64  ? HIS B 63   . ? 1_555 ? 
29  AC6 9 HIS B  121 ? HIS B 120  . ? 1_555 ? 
30  AC6 9 THR B  138 ? THR B 137  . ? 1_555 ? 
31  AC6 9 ARG B  144 ? ARG B 143  . ? 1_555 ? 
32  AC6 9 CU  N  .   ? CU  B 154  . ? 1_555 ? 
33  AC6 9 HOH UA .   ? HOH B 2120 . ? 1_555 ? 
34  AC6 9 HOH UA .   ? HOH B 2121 . ? 1_555 ? 
35  AC7 5 HIS C  47  ? HIS C 46   . ? 1_555 ? 
36  AC7 5 HIS C  49  ? HIS C 48   . ? 1_555 ? 
37  AC7 5 HIS C  64  ? HIS C 63   . ? 1_555 ? 
38  AC7 5 HIS C  121 ? HIS C 120  . ? 1_555 ? 
39  AC7 5 HOH VA .   ? HOH C 2086 . ? 1_555 ? 
40  AC8 5 HIS C  64  ? HIS C 63   . ? 1_555 ? 
41  AC8 5 HIS C  72  ? HIS C 71   . ? 1_555 ? 
42  AC8 5 HIS C  81  ? HIS C 80   . ? 1_555 ? 
43  AC8 5 ASP C  84  ? ASP C 83   . ? 1_555 ? 
44  AC8 5 LYS C  137 ? LYS C 136  . ? 1_555 ? 
45  AC9 4 ARG C  144 ? ARG C 143  . ? 1_555 ? 
46  AC9 4 HOH VA .   ? HOH C 2086 . ? 1_555 ? 
47  AC9 4 HOH VA .   ? HOH C 2187 . ? 1_555 ? 
48  AC9 4 HOH VA .   ? HOH C 2190 . ? 1_555 ? 
49  BC1 5 HIS D  47  ? HIS D 46   . ? 1_555 ? 
50  BC1 5 HIS D  49  ? HIS D 48   . ? 1_555 ? 
51  BC1 5 HIS D  64  ? HIS D 63   . ? 1_555 ? 
52  BC1 5 HIS D  121 ? HIS D 120  . ? 1_555 ? 
53  BC1 5 CO3 V  .   ? CO3 D 156  . ? 1_555 ? 
54  BC2 4 HIS D  64  ? HIS D 63   . ? 1_555 ? 
55  BC2 4 HIS D  72  ? HIS D 71   . ? 1_555 ? 
56  BC2 4 HIS D  81  ? HIS D 80   . ? 1_555 ? 
57  BC2 4 ASP D  84  ? ASP D 83   . ? 1_555 ? 
58  BC3 8 HIS D  49  ? HIS D 48   . ? 1_555 ? 
59  BC3 8 HIS D  64  ? HIS D 63   . ? 1_555 ? 
60  BC3 8 HIS D  121 ? HIS D 120  . ? 1_555 ? 
61  BC3 8 THR D  138 ? THR D 137  . ? 1_555 ? 
62  BC3 8 ARG D  144 ? ARG D 143  . ? 1_555 ? 
63  BC3 8 CU  T  .   ? CU  D 154  . ? 1_555 ? 
64  BC3 8 HOH WA .   ? HOH D 2069 . ? 1_555 ? 
65  BC3 8 HOH WA .   ? HOH D 2119 . ? 1_555 ? 
66  BC4 5 HIS E  47  ? HIS E 46   . ? 1_555 ? 
67  BC4 5 HIS E  49  ? HIS E 48   . ? 1_555 ? 
68  BC4 5 HIS E  64  ? HIS E 63   . ? 1_555 ? 
69  BC4 5 HIS E  121 ? HIS E 120  . ? 1_555 ? 
70  BC4 5 CO3 Y  .   ? CO3 E 156  . ? 1_555 ? 
71  BC5 4 HIS E  64  ? HIS E 63   . ? 1_555 ? 
72  BC5 4 HIS E  72  ? HIS E 71   . ? 1_555 ? 
73  BC5 4 HIS E  81  ? HIS E 80   . ? 1_555 ? 
74  BC5 4 ASP E  84  ? ASP E 83   . ? 1_555 ? 
75  BC6 7 HIS E  49  ? HIS E 48   . ? 1_555 ? 
76  BC6 7 HIS E  64  ? HIS E 63   . ? 1_555 ? 
77  BC6 7 HIS E  121 ? HIS E 120  . ? 1_555 ? 
78  BC6 7 THR E  138 ? THR E 137  . ? 1_555 ? 
79  BC6 7 ARG E  144 ? ARG E 143  . ? 1_555 ? 
80  BC6 7 CU  W  .   ? CU  E 154  . ? 1_555 ? 
81  BC6 7 HOH XA .   ? HOH E 2108 . ? 1_555 ? 
82  BC7 5 HIS F  47  ? HIS F 46   . ? 1_555 ? 
83  BC7 5 HIS F  49  ? HIS F 48   . ? 1_555 ? 
84  BC7 5 HIS F  64  ? HIS F 63   . ? 1_555 ? 
85  BC7 5 HIS F  121 ? HIS F 120  . ? 1_555 ? 
86  BC7 5 HOH YA .   ? HOH F 2122 . ? 1_555 ? 
87  BC8 4 HIS F  64  ? HIS F 63   . ? 1_555 ? 
88  BC8 4 HIS F  72  ? HIS F 71   . ? 1_555 ? 
89  BC8 4 HIS F  81  ? HIS F 80   . ? 1_555 ? 
90  BC8 4 ASP F  84  ? ASP F 83   . ? 1_555 ? 
91  BC9 6 HIS F  121 ? HIS F 120  . ? 1_555 ? 
92  BC9 6 GLY F  142 ? GLY F 141  . ? 1_555 ? 
93  BC9 6 ARG F  144 ? ARG F 143  . ? 1_555 ? 
94  BC9 6 HOH YA .   ? HOH F 2122 . ? 1_555 ? 
95  BC9 6 HOH YA .   ? HOH F 2218 . ? 1_555 ? 
96  BC9 6 HOH YA .   ? HOH F 2227 . ? 1_555 ? 
97  CC1 5 HIS G  47  ? HIS G 46   . ? 1_555 ? 
98  CC1 5 HIS G  49  ? HIS G 48   . ? 1_555 ? 
99  CC1 5 HIS G  64  ? HIS G 63   . ? 1_555 ? 
100 CC1 5 HIS G  121 ? HIS G 120  . ? 1_555 ? 
101 CC1 5 HOH ZA .   ? HOH G 2076 . ? 1_555 ? 
102 CC2 4 HIS G  64  ? HIS G 63   . ? 1_555 ? 
103 CC2 4 HIS G  72  ? HIS G 71   . ? 1_555 ? 
104 CC2 4 HIS G  81  ? HIS G 80   . ? 1_555 ? 
105 CC2 4 ASP G  84  ? ASP G 83   . ? 1_555 ? 
106 CC3 6 HIS G  121 ? HIS G 120  . ? 1_555 ? 
107 CC3 6 GLY G  142 ? GLY G 141  . ? 1_555 ? 
108 CC3 6 ARG G  144 ? ARG G 143  . ? 1_555 ? 
109 CC3 6 HOH ZA .   ? HOH G 2174 . ? 1_555 ? 
110 CC3 6 HOH ZA .   ? HOH G 2180 . ? 1_555 ? 
111 CC3 6 HOH ZA .   ? HOH G 2181 . ? 1_555 ? 
112 CC4 5 HIS H  47  ? HIS H 46   . ? 1_555 ? 
113 CC4 5 HIS H  49  ? HIS H 48   . ? 1_555 ? 
114 CC4 5 HIS H  64  ? HIS H 63   . ? 1_555 ? 
115 CC4 5 HIS H  121 ? HIS H 120  . ? 1_555 ? 
116 CC4 5 HOH AB .   ? HOH H 2065 . ? 1_555 ? 
117 CC5 4 HIS H  64  ? HIS H 63   . ? 1_555 ? 
118 CC5 4 HIS H  72  ? HIS H 71   . ? 1_555 ? 
119 CC5 4 HIS H  81  ? HIS H 80   . ? 1_555 ? 
120 CC5 4 ASP H  84  ? ASP H 83   . ? 1_555 ? 
121 CC6 4 ARG H  144 ? ARG H 143  . ? 1_555 ? 
122 CC6 4 HOH AB .   ? HOH H 2068 . ? 1_555 ? 
123 CC6 4 HOH AB .   ? HOH H 2130 . ? 1_555 ? 
124 CC6 4 HOH AB .   ? HOH H 2150 . ? 1_555 ? 
125 CC7 5 HIS I  47  ? HIS I 46   . ? 1_555 ? 
126 CC7 5 HIS I  49  ? HIS I 48   . ? 1_555 ? 
127 CC7 5 HIS I  64  ? HIS I 63   . ? 1_555 ? 
128 CC7 5 HIS I  121 ? HIS I 120  . ? 1_555 ? 
129 CC7 5 HOH BB .   ? HOH I 2068 . ? 1_555 ? 
130 CC8 4 HIS I  64  ? HIS I 63   . ? 1_555 ? 
131 CC8 4 HIS I  72  ? HIS I 71   . ? 1_555 ? 
132 CC8 4 HIS I  81  ? HIS I 80   . ? 1_555 ? 
133 CC8 4 ASP I  84  ? ASP I 83   . ? 1_555 ? 
134 CC9 4 ARG I  144 ? ARG I 143  . ? 1_555 ? 
135 CC9 4 HOH BB .   ? HOH I 2092 . ? 1_555 ? 
136 CC9 4 HOH BB .   ? HOH I 2141 . ? 1_555 ? 
137 CC9 4 HOH BB .   ? HOH I 2161 . ? 1_555 ? 
138 DC1 5 HIS J  47  ? HIS J 46   . ? 1_555 ? 
139 DC1 5 HIS J  49  ? HIS J 48   . ? 1_555 ? 
140 DC1 5 HIS J  64  ? HIS J 63   . ? 1_555 ? 
141 DC1 5 HIS J  121 ? HIS J 120  . ? 1_555 ? 
142 DC1 5 HOH CB .   ? HOH J 2041 . ? 1_555 ? 
143 DC2 4 HIS J  64  ? HIS J 63   . ? 1_555 ? 
144 DC2 4 HIS J  72  ? HIS J 71   . ? 1_555 ? 
145 DC2 4 HIS J  81  ? HIS J 80   . ? 1_555 ? 
146 DC2 4 ASP J  84  ? ASP J 83   . ? 1_555 ? 
147 DC3 5 GLY J  142 ? GLY J 141  . ? 1_555 ? 
148 DC3 5 ARG J  144 ? ARG J 143  . ? 1_555 ? 
149 DC3 5 HOH CB .   ? HOH J 2041 . ? 1_555 ? 
150 DC3 5 HOH CB .   ? HOH J 2060 . ? 1_555 ? 
151 DC3 5 HOH CB .   ? HOH J 2115 . ? 1_555 ? 
152 DC4 7 LYS F  76  ? LYS F 75   . ? 1_555 ? 
153 DC4 7 HOH YA .   ? HOH F 2205 . ? 1_555 ? 
154 DC4 7 HOH YA .   ? HOH F 2229 . ? 1_555 ? 
155 DC4 7 HOH YA .   ? HOH F 2231 . ? 1_555 ? 
156 DC4 7 HOH YA .   ? HOH F 2232 . ? 1_555 ? 
157 DC4 7 LYS G  129 ? LYS G 128  . ? 1_555 ? 
158 DC4 7 LYS H  129 ? LYS H 128  . ? 1_555 ? 
159 DC5 5 LYS G  123 ? LYS G 122  . ? 1_555 ? 
160 DC5 5 ALA G  124 ? ALA G 123  . ? 1_555 ? 
161 DC5 5 HOH ZA .   ? HOH G 2072 . ? 1_555 ? 
162 DC5 5 HOH ZA .   ? HOH G 2162 . ? 1_555 ? 
163 DC5 5 HOH ZA .   ? HOH G 2186 . ? 1_555 ? 
164 DC6 7 LYS C  129 ? LYS C 128  . ? 5_455 ? 
165 DC6 7 HOH VA .   ? HOH C 2128 . ? 5_455 ? 
166 DC6 7 LYS I  129 ? LYS I 128  . ? 1_555 ? 
167 DC6 7 LYS J  129 ? LYS J 128  . ? 1_555 ? 
168 DC6 7 SO4 SA .   ? SO4 J 1155 . ? 1_555 ? 
169 DC6 7 HOH CB .   ? HOH J 2105 . ? 1_555 ? 
170 DC6 7 HOH CB .   ? HOH J 2106 . ? 1_555 ? 
171 DC7 8 LYS C  129 ? LYS C 128  . ? 5_455 ? 
172 DC7 8 LYS I  129 ? LYS I 128  . ? 1_555 ? 
173 DC7 8 HOH BB .   ? HOH I 2154 . ? 1_555 ? 
174 DC7 8 LEU J  127 ? LEU J 126  . ? 1_555 ? 
175 DC7 8 LYS J  129 ? LYS J 128  . ? 1_555 ? 
176 DC7 8 SO4 RA .   ? SO4 J 1154 . ? 1_555 ? 
177 DC7 8 HOH CB .   ? HOH J 2099 . ? 1_555 ? 
178 DC7 8 HOH CB .   ? HOH J 2120 . ? 1_555 ? 
179 DC8 5 LYS F  129 ? LYS F 128  . ? 1_555 ? 
180 DC8 5 HOH YA .   ? HOH F 2233 . ? 1_555 ? 
181 DC8 5 HOH YA .   ? HOH F 2234 . ? 1_555 ? 
182 DC8 5 LYS G  129 ? LYS G 128  . ? 1_555 ? 
183 DC8 5 LYS H  129 ? LYS H 128  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4B3E 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4B3E 
_atom_sites.fract_transf_matrix[1][1]   0.006024 
_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]   0.004924 
_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]   0.006926 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A  1 2   ? 137.709 45.090  43.482 1.00   37.76 ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 2   ? 136.583 45.934  44.012 1.00   36.85 ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 2   ? 137.054 47.317  44.542 1.00   34.38 ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 2   ? 138.074 47.418  45.201 1.00   33.62 ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 2   ? 135.840 45.167  45.111 1.00   36.98 ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 3   ? 136.305 48.374  44.257 1.00   31.97 ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 3   ? 136.553 49.632  44.922 1.00   29.48 ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 3   ? 135.712 49.585  46.202 1.00   27.26 ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 3   ? 134.638 48.988  46.232 1.00   25.73 ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 3   ? 136.346 50.849  43.977 1.00   29.89 ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 3   ? 136.923 51.999  44.557 1.00   32.73 ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 3   ? 134.960 51.170  43.725 1.00   30.94 ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 4   ? 136.277 50.115  47.284 1.00   24.76 ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 4   ? 135.692 50.067  48.611 1.00   23.31 ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 4   ? 135.712 51.473  49.215 1.00   21.02 ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 4   ? 136.606 52.275  48.935 1.00   19.53 ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 4   ? 136.493 49.129  49.515 1.00   25.27 ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 4   ? 136.699 47.722  48.957 1.00   27.82 ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 4   ? 137.089 46.722  50.048 1.00   29.70 ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 4   ? 137.326 45.309  49.484 1.00   31.58 ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 4   ? 138.785 45.010  49.373 1.00   33.47 ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 5   ? 134.732 51.749  50.061 1.00   19.45 ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 5   ? 134.684 52.983  50.816 1.00   18.52 ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 5   ? 134.206 52.694  52.231 1.00   18.31 ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 5   ? 133.762 51.576  52.545 1.00   19.11 ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 5   ? 133.780 53.999  50.122 1.00   17.68 ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 6   ? 134.329 53.685  53.101 1.00   17.61 ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 6   ? 133.921 53.544  54.470 1.00   17.37 ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 6   ? 133.500 54.895  55.033 1.00   17.23 ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 6   ? 133.924 55.959  54.568 1.00   16.88 ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 6   ? 135.036 52.904  55.317 1.00   17.54 ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 6   ? 136.144 53.905  55.595 1.00   17.09 ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 6   ? 134.472 52.303  56.613 1.00   17.30 ? 5    VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 7   ? 132.626 54.839  56.011 1.00   17.37 ? 6    CYS A N   1 
ATOM   35    C  CA  . CYS A  1 7   ? 132.129 56.021  56.644 1.00   17.62 ? 6    CYS A CA  1 
ATOM   36    C  C   . CYS A  1 7   ? 131.924 55.758  58.127 1.00   18.01 ? 6    CYS A C   1 
ATOM   37    O  O   . CYS A  1 7   ? 131.254 54.774  58.519 1.00   18.40 ? 6    CYS A O   1 
ATOM   38    C  CB  . CYS A  1 7   ? 130.824 56.421  56.001 1.00   17.51 ? 6    CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 7   ? 130.198 57.961  56.665 1.00   17.89 ? 6    CYS A SG  1 
ATOM   40    N  N   . VAL A  1 8   ? 132.516 56.614  58.945 1.00   18.05 ? 7    VAL A N   1 
ATOM   41    C  CA  . VAL A  1 8   ? 132.279 56.603  60.378 1.00   18.43 ? 7    VAL A CA  1 
ATOM   42    C  C   . VAL A  1 8   ? 131.283 57.711  60.699 1.00   18.98 ? 7    VAL A C   1 
ATOM   43    O  O   . VAL A  1 8   ? 131.539 58.899  60.389 1.00   19.09 ? 7    VAL A O   1 
ATOM   44    C  CB  . VAL A  1 8   ? 133.590 56.868  61.153 1.00   18.53 ? 7    VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 8   ? 133.310 56.942  62.670 1.00   18.38 ? 7    VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 8   ? 134.593 55.783  60.795 1.00   18.18 ? 7    VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 9   ? 130.139 57.325  61.255 1.00   19.28 ? 8    LEU A N   1 
ATOM   48    C  CA  . LEU A  1 9   ? 129.074 58.260  61.563 1.00   19.66 ? 8    LEU A CA  1 
ATOM   49    C  C   . LEU A  1 9   ? 129.187 58.658  63.034 1.00   19.72 ? 8    LEU A C   1 
ATOM   50    O  O   . LEU A  1 9   ? 129.333 57.806  63.887 1.00   18.71 ? 8    LEU A O   1 
ATOM   51    C  CB  . LEU A  1 9   ? 127.699 57.625  61.319 1.00   20.49 ? 8    LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 9   ? 127.326 57.096  59.924 1.00   21.43 ? 8    LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 9   ? 126.398 55.893  60.051 1.00   22.46 ? 8    LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 9   ? 126.644 58.164  59.079 1.00   21.11 ? 8    LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 10  ? 129.104 59.964  63.289 1.00   20.11 ? 9    LYS A N   1 
ATOM   56    C  CA  . LYS A  1 10  ? 129.153 60.556  64.628 1.00   21.08 ? 9    LYS A CA  1 
ATOM   57    C  C   . LYS A  1 10  ? 128.260 61.782  64.657 1.00   20.84 ? 9    LYS A C   1 
ATOM   58    O  O   . LYS A  1 10  ? 128.023 62.398  63.625 1.00   19.74 ? 9    LYS A O   1 
ATOM   59    C  CB  . LYS A  1 10  ? 130.571 61.031  64.996 1.00   22.17 ? 9    LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 10  ? 131.582 59.933  65.259 1.00   23.68 ? 9    LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 10  ? 131.169 59.060  66.462 0.50   24.35 ? 9    LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 10  ? 132.063 57.832  66.613 0.50   24.57 ? 9    LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 10  ? 133.432 58.230  67.035 0.50   24.86 ? 9    LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 11  ? 127.813 62.165  65.851 1.00   21.75 ? 10   GLY A N   1 
ATOM   65    C  CA  . GLY A  1 11  ? 126.981 63.368  66.025 1.00   23.01 ? 10   GLY A CA  1 
ATOM   66    C  C   . GLY A  1 11  ? 127.160 63.953  67.410 1.00   24.63 ? 10   GLY A C   1 
ATOM   67    O  O   . GLY A  1 11  ? 128.106 63.621  68.081 1.00   24.64 ? 10   GLY A O   1 
ATOM   68    N  N   . ASP A  1 12  ? 126.244 64.808  67.840 1.00   26.98 ? 11   ASP A N   1 
ATOM   69    C  CA  . ASP A  1 12  ? 126.317 65.407  69.177 1.00   28.88 ? 11   ASP A CA  1 
ATOM   70    C  C   . ASP A  1 12  ? 125.761 64.491  70.266 1.00   29.37 ? 11   ASP A C   1 
ATOM   71    O  O   . ASP A  1 12  ? 126.164 64.599  71.424 1.00   30.76 ? 11   ASP A O   1 
ATOM   72    C  CB  . ASP A  1 12  ? 125.549 66.727  69.204 1.00   30.86 ? 11   ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 12  ? 126.137 67.759  68.252 1.00   33.25 ? 11   ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 12  ? 127.390 67.774  68.068 1.00   33.25 ? 11   ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 12  ? 125.335 68.556  67.701 1.00   36.71 ? 11   ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 13  ? 124.835 63.607  69.907 1.00   27.30 ? 12   GLY A N   1 
ATOM   77    C  CA  . GLY A  1 13  ? 124.320 62.614  70.850 1.00   25.98 ? 12   GLY A CA  1 
ATOM   78    C  C   . GLY A  1 13  ? 125.033 61.271  70.761 1.00   24.95 ? 12   GLY A C   1 
ATOM   79    O  O   . GLY A  1 13  ? 126.199 61.211  70.365 1.00   24.68 ? 12   GLY A O   1 
ATOM   80    N  N   . PRO A  1 14  ? 124.323 60.174  71.122 1.00   23.93 ? 13   PRO A N   1 
ATOM   81    C  CA  . PRO A  1 14  ? 124.880 58.827  71.203 1.00   23.36 ? 13   PRO A CA  1 
ATOM   82    C  C   . PRO A  1 14  ? 124.915 58.050  69.888 1.00   22.53 ? 13   PRO A C   1 
ATOM   83    O  O   . PRO A  1 14  ? 125.433 56.936  69.866 1.00   22.16 ? 13   PRO A O   1 
ATOM   84    C  CB  . PRO A  1 14  ? 123.910 58.129  72.165 1.00   23.49 ? 13   PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 14  ? 122.606 58.752  71.828 1.00   23.61 ? 13   PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 14  ? 122.900 60.185  71.521 1.00   23.55 ? 13   PRO A CD  1 
ATOM   87    N  N   . VAL A  1 15  ? 124.367 58.609  68.806 1.00   22.04 ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 15  ? 124.288 57.864  67.557 1.00   21.51 ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 15  ? 125.665 57.750  66.905 1.00   21.93 ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 15  ? 126.339 58.741  66.660 1.00   21.65 ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 15  ? 123.231 58.420  66.573 1.00   20.86 ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 15  ? 123.137 57.546  65.337 1.00   19.71 ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 15  ? 121.870 58.514  67.242 1.00   20.76 ? 14   VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 16  ? 126.082 56.514  66.645 1.00   23.33 ? 15   GLN A N   1 
ATOM   95    C  CA  . GLN A  1 16  ? 127.365 56.254  66.037 1.00   23.52 ? 15   GLN A CA  1 
ATOM   96    C  C   . GLN A  1 16  ? 127.385 54.928  65.316 1.00   22.73 ? 15   GLN A C   1 
ATOM   97    O  O   . GLN A  1 16  ? 126.666 53.994  65.669 1.00   22.26 ? 15   GLN A O   1 
ATOM   98    C  CB  . GLN A  1 16  ? 128.493 56.331  67.074 1.00   25.61 ? 15   GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 16  ? 128.493 55.302  68.184 1.00   28.29 ? 15   GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 16  ? 129.607 55.577  69.231 1.00   30.90 ? 15   GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 16  ? 130.458 54.719  69.524 1.00   33.33 ? 15   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 16  ? 129.612 56.784  69.764 1.00   31.44 ? 15   GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 17  ? 128.214 54.853  64.290 1.00   21.35 ? 16   GLY A N   1 
ATOM   104   C  CA  . GLY A  1 17  ? 128.339 53.630  63.557 1.00   21.15 ? 16   GLY A CA  1 
ATOM   105   C  C   . GLY A  1 17  ? 129.395 53.676  62.499 1.00   20.51 ? 16   GLY A C   1 
ATOM   106   O  O   . GLY A  1 17  ? 130.079 54.695  62.310 1.00   19.50 ? 16   GLY A O   1 
ATOM   107   N  N   . ILE A  1 18  ? 129.501 52.543  61.803 1.00   20.45 ? 17   ILE A N   1 
ATOM   108   C  CA  . ILE A  1 18  ? 130.431 52.349  60.723 1.00   20.03 ? 17   ILE A CA  1 
ATOM   109   C  C   . ILE A  1 18  ? 129.694 51.672  59.576 1.00   19.97 ? 17   ILE A C   1 
ATOM   110   O  O   . ILE A  1 18  ? 129.066 50.623  59.769 1.00   20.59 ? 17   ILE A O   1 
ATOM   111   C  CB  . ILE A  1 18  ? 131.621 51.485  61.169 1.00   20.36 ? 17   ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 18  ? 132.358 52.173  62.306 1.00   20.47 ? 17   ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 18  ? 132.568 51.220  59.993 1.00   20.21 ? 17   ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 18  ? 133.541 51.400  62.837 1.00   21.01 ? 17   ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 19  ? 129.753 52.289  58.396 1.00   19.08 ? 18   ILE A N   1 
ATOM   116   C  CA  . ILE A  1 19  ? 129.097 51.793  57.195 1.00   18.66 ? 18   ILE A CA  1 
ATOM   117   C  C   . ILE A  1 19  ? 130.139 51.546  56.109 1.00   18.86 ? 18   ILE A C   1 
ATOM   118   O  O   . ILE A  1 19  ? 130.939 52.441  55.771 1.00   19.02 ? 18   ILE A O   1 
ATOM   119   C  CB  . ILE A  1 19  ? 128.055 52.806  56.680 1.00   18.28 ? 18   ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 19  ? 126.922 52.987  57.705 1.00   18.31 ? 18   ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 19  ? 127.485 52.374  55.329 1.00   18.23 ? 18   ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 19  ? 126.130 51.728  57.983 1.00   18.22 ? 18   ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 20  ? 130.153 50.332  55.581 1.00   18.96 ? 19   ASN A N   1 
ATOM   124   C  CA  . ASN A  1 20  ? 131.056 49.963  54.514 1.00   19.24 ? 19   ASN A CA  1 
ATOM   125   C  C   . ASN A  1 20  ? 130.367 50.020  53.155 1.00   18.95 ? 19   ASN A C   1 
ATOM   126   O  O   . ASN A  1 20  ? 129.155 49.884  53.069 1.00   18.49 ? 19   ASN A O   1 
ATOM   127   C  CB  . ASN A  1 20  ? 131.603 48.582  54.768 1.00   20.13 ? 19   ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 20  ? 132.212 48.455  56.150 1.00   21.15 ? 19   ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 20  ? 131.559 47.942  57.085 1.00   22.38 ? 19   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 20  ? 133.443 48.949  56.309 1.00   21.01 ? 19   ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 21  ? 131.155 50.234  52.099 1.00   18.79 ? 20   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 21  ? 130.642 50.259  50.730 1.00   18.69 ? 20   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 21  ? 131.576 49.429  49.871 1.00   19.41 ? 20   PHE A C   1 
ATOM   134   O  O   . PHE A  1 21  ? 132.811 49.535  50.010 1.00   19.10 ? 20   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 21  ? 130.629 51.672  50.137 1.00   18.06 ? 20   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 21  ? 129.822 52.673  50.902 1.00   17.46 ? 20   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 21  ? 130.331 53.282  52.038 1.00   17.44 ? 20   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 21  ? 128.580 53.055  50.462 1.00   17.34 ? 20   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 21  ? 129.600 54.240  52.725 1.00   16.98 ? 20   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 21  ? 127.832 53.992  51.150 1.00   17.10 ? 20   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 21  ? 128.348 54.598  52.273 1.00   17.05 ? 20   PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 22  ? 131.007 48.624  48.966 1.00   20.04 ? 21   GLU A N   1 
ATOM   143   C  CA  . GLU A  1 22  ? 131.821 47.853  48.032 1.00   21.02 ? 21   GLU A CA  1 
ATOM   144   C  C   . GLU A  1 22  ? 131.181 47.796  46.650 1.00   21.18 ? 21   GLU A C   1 
ATOM   145   O  O   . GLU A  1 22  ? 129.986 47.532  46.522 1.00   20.70 ? 21   GLU A O   1 
ATOM   146   C  CB  . GLU A  1 22  ? 132.058 46.451  48.574 1.00   22.20 ? 21   GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 22  ? 132.871 45.587  47.642 1.00   23.88 ? 21   GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 22  ? 133.087 44.202  48.180 1.00   25.69 ? 21   GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 22  ? 133.974 44.051  49.050 0.70   26.94 ? 21   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 22  ? 132.336 43.289  47.755 0.70   27.39 ? 21   GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 23  ? 131.996 47.994  45.608 1.00   21.61 ? 22   GLN A N   1 
ATOM   152   C  CA  . GLN A  1 23  ? 131.517 47.977  44.227 1.00   21.99 ? 22   GLN A CA  1 
ATOM   153   C  C   . GLN A  1 23  ? 132.536 47.221  43.366 1.00   23.66 ? 22   GLN A C   1 
ATOM   154   O  O   . GLN A  1 23  ? 133.580 47.761  43.009 1.00   23.92 ? 22   GLN A O   1 
ATOM   155   C  CB  . GLN A  1 23  ? 131.334 49.419  43.732 1.00   21.12 ? 22   GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 23  ? 130.685 49.565  42.362 1.00   20.81 ? 22   GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 23  ? 130.522 51.024  41.932 1.00   20.31 ? 22   GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 23  ? 131.237 51.907  42.406 1.00   20.01 ? 22   GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 23  ? 129.581 51.282  41.033 1.00   19.96 ? 22   GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 24  ? 132.215 45.977  43.024 1.00   25.53 ? 23   LYS A N   1 
ATOM   161   C  CA  . LYS A  1 24  ? 133.137 45.101  42.314 1.00   27.54 ? 23   LYS A CA  1 
ATOM   162   C  C   . LYS A  1 24  ? 133.435 45.642  40.938 1.00   26.93 ? 23   LYS A C   1 
ATOM   163   O  O   . LYS A  1 24  ? 134.546 45.554  40.485 1.00   26.71 ? 23   LYS A O   1 
ATOM   164   C  CB  . LYS A  1 24  ? 132.559 43.689  42.171 1.00   30.29 ? 23   LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 24  ? 132.549 42.933  43.485 1.00   33.02 ? 23   LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 24  ? 131.705 41.660  43.428 0.50   34.25 ? 23   LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 24  ? 131.816 40.882  44.733 0.50   34.77 ? 23   LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 24  ? 131.335 39.481  44.600 0.50   36.14 ? 23   LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 25  ? 132.435 46.221  40.293 1.00   26.91 ? 24   GLU A N   1 
ATOM   170   C  CA  . GLU A  1 25  ? 132.591 46.714  38.940 1.00   28.09 ? 24   GLU A CA  1 
ATOM   171   C  C   . GLU A  1 25  ? 132.106 48.149  38.851 1.00   25.84 ? 24   GLU A C   1 
ATOM   172   O  O   . GLU A  1 25  ? 131.087 48.488  39.424 1.00   24.65 ? 24   GLU A O   1 
ATOM   173   C  CB  . GLU A  1 25  ? 131.794 45.790  38.014 1.00   30.94 ? 24   GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 25  ? 132.331 44.354  38.064 1.00   33.85 ? 24   GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 25  ? 131.277 43.291  37.943 1.00   37.52 ? 24   GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 25  ? 130.075 43.627  37.897 1.00   40.79 ? 24   GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 25  ? 131.664 42.097  37.860 1.00   43.49 ? 24   GLU A OE2 1 
ATOM   178   N  N   . SER A  1 26  ? 132.806 48.982  38.096 1.00   24.79 ? 25   SER A N   1 
ATOM   179   C  CA  . SER A  1 26  ? 132.428 50.394  38.013 1.00   24.10 ? 25   SER A CA  1 
ATOM   180   C  C   . SER A  1 26  ? 131.002 50.594  37.490 1.00   23.46 ? 25   SER A C   1 
ATOM   181   O  O   . SER A  1 26  ? 130.356 51.595  37.821 1.00   22.39 ? 25   SER A O   1 
ATOM   182   C  CB  . SER A  1 26  ? 133.414 51.170  37.137 1.00   23.98 ? 25   SER A CB  1 
ATOM   183   O  OG  . SER A  1 26  ? 133.356 50.728  35.797 1.00   23.81 ? 25   SER A OG  1 
ATOM   184   N  N   . ASN A  1 27  ? 130.517 49.655  36.671 1.00   23.41 ? 26   ASN A N   1 
ATOM   185   C  CA  . ASN A  1 27  ? 129.145 49.740  36.171 1.00   23.49 ? 26   ASN A CA  1 
ATOM   186   C  C   . ASN A  1 27  ? 128.186 48.795  36.894 1.00   23.58 ? 26   ASN A C   1 
ATOM   187   O  O   . ASN A  1 27  ? 127.108 48.493  36.390 1.00   24.37 ? 26   ASN A O   1 
ATOM   188   C  CB  . ASN A  1 27  ? 129.081 49.522  34.655 1.00   23.84 ? 26   ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 27  ? 129.487 48.119  34.253 1.00   24.29 ? 26   ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 27  ? 130.331 47.516  34.924 1.00   24.57 ? 26   ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 27  ? 128.924 47.607  33.146 1.00   23.81 ? 26   ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 28  ? 128.586 48.323  38.069 1.00   23.17 ? 27   GLY A N   1 
ATOM   193   C  CA  . GLY A  1 28  ? 127.727 47.451  38.863 1.00   22.99 ? 27   GLY A CA  1 
ATOM   194   C  C   . GLY A  1 28  ? 127.203 48.141  40.114 1.00   22.39 ? 27   GLY A C   1 
ATOM   195   O  O   . GLY A  1 28  ? 127.495 49.323  40.377 1.00   21.52 ? 27   GLY A O   1 
ATOM   196   N  N   . PRO A  1 29  ? 126.436 47.388  40.907 1.00   22.23 ? 28   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 29  ? 125.800 47.907  42.091 1.00   21.77 ? 28   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 29  ? 126.798 48.059  43.244 1.00   21.08 ? 28   PRO A C   1 
ATOM   199   O  O   . PRO A  1 29  ? 127.895 47.470  43.211 1.00   20.98 ? 28   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 29  ? 124.715 46.861  42.395 1.00   22.51 ? 28   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 29  ? 125.237 45.588  41.792 1.00   23.30 ? 28   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 29  ? 126.016 46.007  40.583 1.00   23.10 ? 28   PRO A CD  1 
ATOM   203   N  N   . VAL A  1 30  ? 126.442 48.903  44.214 1.00   20.58 ? 29   VAL A N   1 
ATOM   204   C  CA  . VAL A  1 30  ? 127.276 49.146  45.404 1.00   20.14 ? 29   VAL A CA  1 
ATOM   205   C  C   . VAL A  1 30  ? 126.593 48.400  46.546 1.00   20.98 ? 29   VAL A C   1 
ATOM   206   O  O   . VAL A  1 30  ? 125.390 48.588  46.766 1.00   20.68 ? 29   VAL A O   1 
ATOM   207   C  CB  . VAL A  1 30  ? 127.349 50.642  45.776 1.00   19.59 ? 29   VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 30  ? 128.280 50.859  46.962 1.00   18.84 ? 29   VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 30  ? 127.780 51.484  44.579 1.00   19.23 ? 29   VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 31  ? 127.338 47.548  47.246 1.00   21.78 ? 30   LYS A N   1 
ATOM   211   C  CA  . LYS A  1 31  ? 126.851 46.936  48.477 1.00   22.86 ? 30   LYS A CA  1 
ATOM   212   C  C   . LYS A  1 31  ? 127.151 47.890  49.613 1.00   22.05 ? 30   LYS A C   1 
ATOM   213   O  O   . LYS A  1 31  ? 128.273 48.417  49.687 1.00   21.62 ? 30   LYS A O   1 
ATOM   214   C  CB  . LYS A  1 31  ? 127.551 45.614  48.767 1.00   24.47 ? 30   LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 31  ? 127.186 44.465  47.850 1.00   26.93 ? 30   LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 31  ? 128.112 43.269  48.115 1.00   29.23 ? 30   LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 31  ? 127.768 42.034  47.272 1.00   31.71 ? 30   LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 31  ? 128.940 41.083  47.197 1.00   33.84 ? 30   LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 32  ? 126.168 48.088  50.490 1.00   21.34 ? 31   VAL A N   1 
ATOM   220   C  CA  . VAL A  1 32  ? 126.272 48.984  51.634 1.00   20.98 ? 31   VAL A CA  1 
ATOM   221   C  C   . VAL A  1 32  ? 125.899 48.223  52.909 1.00   21.34 ? 31   VAL A C   1 
ATOM   222   O  O   . VAL A  1 32  ? 124.784 47.687  53.009 1.00   21.52 ? 31   VAL A O   1 
ATOM   223   C  CB  . VAL A  1 32  ? 125.309 50.180  51.524 1.00   20.67 ? 31   VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 32  ? 125.481 51.094  52.737 1.00   20.53 ? 31   VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 32  ? 125.494 50.941  50.210 1.00   20.53 ? 31   VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 33  ? 126.808 48.176  53.878 1.00   21.14 ? 32   TRP A N   1 
ATOM   227   C  CA  . TRP A  1 33  ? 126.581 47.395  55.088 1.00   21.50 ? 32   TRP A CA  1 
ATOM   228   C  C   . TRP A  1 33  ? 127.375 47.831  56.273 1.00   21.89 ? 32   TRP A C   1 
ATOM   229   O  O   . TRP A  1 33  ? 128.482 48.379  56.166 1.00   21.11 ? 32   TRP A O   1 
ATOM   230   C  CB  . TRP A  1 33  ? 126.853 45.913  54.840 1.00   22.11 ? 32   TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 33  ? 128.300 45.516  54.928 1.00   22.36 ? 32   TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 33  ? 128.964 44.946  56.014 1.00   22.72 ? 32   TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 33  ? 129.315 45.626  53.876 1.00   22.36 ? 32   TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 33  ? 130.276 44.721  55.711 1.00   23.19 ? 32   TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 33  ? 130.549 45.100  54.441 1.00   22.71 ? 32   TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 33  ? 129.314 46.084  52.570 1.00   22.43 ? 32   TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 33  ? 131.726 45.057  53.717 1.00   23.09 ? 32   TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 33  ? 130.509 46.054  51.855 1.00   22.49 ? 32   TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 33  ? 131.689 45.547  52.412 1.00   22.72 ? 32   TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 34  ? 126.805 47.566  57.437 1.00   22.15 ? 33   GLY A N   1 
ATOM   241   C  CA  . GLY A  1 34  ? 127.413 47.967  58.675 1.00   22.50 ? 33   GLY A CA  1 
ATOM   242   C  C   . GLY A  1 34  ? 126.403 48.022  59.791 1.00   23.10 ? 33   GLY A C   1 
ATOM   243   O  O   . GLY A  1 34  ? 125.338 47.378  59.729 1.00   23.78 ? 33   GLY A O   1 
ATOM   244   N  N   . SER A  1 35  ? 126.726 48.815  60.795 1.00   23.24 ? 34   SER A N   1 
ATOM   245   C  CA  . SER A  1 35  ? 125.906 48.929  61.957 1.00   24.31 ? 34   SER A CA  1 
ATOM   246   C  C   . SER A  1 35  ? 125.950 50.350  62.519 1.00   24.15 ? 34   SER A C   1 
ATOM   247   O  O   . SER A  1 35  ? 127.010 50.995  62.518 1.00   24.34 ? 34   SER A O   1 
ATOM   248   C  CB  . SER A  1 35  ? 126.427 47.960  62.997 1.00   25.47 ? 34   SER A CB  1 
ATOM   249   O  OG  . SER A  1 35  ? 125.493 47.863  64.027 1.00   28.69 ? 34   SER A OG  1 
ATOM   250   N  N   . ILE A  1 36  ? 124.798 50.809  63.010 1.00   23.54 ? 35   ILE A N   1 
ATOM   251   C  CA  . ILE A  1 36  ? 124.649 52.099  63.651 1.00   23.26 ? 35   ILE A CA  1 
ATOM   252   C  C   . ILE A  1 36  ? 123.967 51.824  64.981 1.00   23.78 ? 35   ILE A C   1 
ATOM   253   O  O   . ILE A  1 36  ? 122.973 51.087  65.015 1.00   24.23 ? 35   ILE A O   1 
ATOM   254   C  CB  . ILE A  1 36  ? 123.758 53.058  62.822 1.00   23.04 ? 35   ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 36  ? 124.282 53.181  61.369 1.00   22.65 ? 35   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 36  ? 123.620 54.420  63.540 1.00   22.11 ? 35   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 36  ? 123.313 53.816  60.387 1.00   22.07 ? 35   ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 37  ? 124.514 52.371  66.073 1.00   23.54 ? 36   LYS A N   1 
ATOM   259   C  CA  . LYS A  1 37  ? 123.915 52.246  67.407 1.00   23.46 ? 36   LYS A CA  1 
ATOM   260   C  C   . LYS A  1 37  ? 123.469 53.577  67.988 1.00   22.86 ? 36   LYS A C   1 
ATOM   261   O  O   . LYS A  1 37  ? 123.783 54.634  67.447 1.00   21.87 ? 36   LYS A O   1 
ATOM   262   C  CB  . LYS A  1 37  ? 124.883 51.526  68.362 1.00   24.62 ? 36   LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 37  ? 126.115 52.305  68.823 1.00   24.97 ? 36   LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 37  ? 127.105 51.369  69.522 1.00   25.85 ? 36   LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 37  ? 128.424 52.083  69.848 1.00   26.62 ? 36   LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 37  ? 129.470 51.170  70.406 1.00   26.65 ? 36   LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 38  ? 122.726 53.517  69.097 1.00   22.57 ? 37   GLY A N   1 
ATOM   268   C  CA  . GLY A  1 38  ? 122.236 54.713  69.778 1.00   22.47 ? 37   GLY A CA  1 
ATOM   269   C  C   . GLY A  1 38  ? 120.955 55.308  69.198 1.00   22.17 ? 37   GLY A C   1 
ATOM   270   O  O   . GLY A  1 38  ? 120.592 56.456  69.518 1.00   22.22 ? 37   GLY A O   1 
ATOM   271   N  N   . LEU A  1 39  ? 120.264 54.534  68.364 1.00   21.70 ? 38   LEU A N   1 
ATOM   272   C  CA  . LEU A  1 39  ? 119.040 54.998  67.705 1.00   21.67 ? 38   LEU A CA  1 
ATOM   273   C  C   . LEU A  1 39  ? 117.776 54.586  68.478 1.00   22.78 ? 38   LEU A C   1 
ATOM   274   O  O   . LEU A  1 39  ? 117.779 53.575  69.187 1.00   23.54 ? 38   LEU A O   1 
ATOM   275   C  CB  . LEU A  1 39  ? 118.957 54.439  66.283 1.00   21.08 ? 38   LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 39  ? 119.919 54.956  65.193 1.00   20.38 ? 38   LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 39  ? 119.872 54.042  63.975 1.00   20.09 ? 38   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 39  ? 119.575 56.388  64.816 1.00   19.81 ? 38   LEU A CD2 1 
ATOM   279   N  N   . THR A  1 40  ? 116.699 55.363  68.336 1.00   22.81 ? 39   THR A N   1 
ATOM   280   C  CA  . THR A  1 40  ? 115.403 54.949  68.855 1.00   23.05 ? 39   THR A CA  1 
ATOM   281   C  C   . THR A  1 40  ? 114.908 53.804  67.963 1.00   23.00 ? 39   THR A C   1 
ATOM   282   O  O   . THR A  1 40  ? 115.179 53.774  66.744 1.00   21.90 ? 39   THR A O   1 
ATOM   283   C  CB  . THR A  1 40  ? 114.374 56.101  68.837 1.00   23.32 ? 39   THR A CB  1 
ATOM   284   O  OG1 . THR A  1 40  ? 114.332 56.659  67.513 1.00   22.67 ? 39   THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 40  ? 114.733 57.201  69.857 1.00   22.69 ? 39   THR A CG2 1 
ATOM   286   N  N   . GLU A  1 41  ? 114.188 52.862  68.570 1.00   23.23 ? 40   GLU A N   1 
ATOM   287   C  CA  . GLU A  1 41  ? 113.627 51.716  67.835 1.00   23.29 ? 40   GLU A CA  1 
ATOM   288   C  C   . GLU A  1 41  ? 112.758 52.209  66.690 1.00   23.08 ? 40   GLU A C   1 
ATOM   289   O  O   . GLU A  1 41  ? 111.981 53.150  66.864 1.00   23.33 ? 40   GLU A O   1 
ATOM   290   C  CB  . GLU A  1 41  ? 112.779 50.831  68.762 1.00   23.65 ? 40   GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 41  ? 112.231 49.573  68.096 1.00   23.95 ? 40   GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 41  ? 111.334 48.743  69.020 1.00   25.03 ? 40   GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 41  ? 111.103 49.148  70.171 1.00   24.59 ? 40   GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 41  ? 110.848 47.684  68.576 1.00   25.89 ? 40   GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 42  ? 112.897 51.580  65.525 1.00   23.08 ? 41   GLY A N   1 
ATOM   296   C  CA  . GLY A  1 42  ? 112.113 51.965  64.344 1.00   23.10 ? 41   GLY A CA  1 
ATOM   297   C  C   . GLY A  1 42  ? 112.965 52.507  63.197 1.00   22.64 ? 41   GLY A C   1 
ATOM   298   O  O   . GLY A  1 42  ? 114.183 52.290  63.149 1.00   21.94 ? 41   GLY A O   1 
ATOM   299   N  N   . LEU A  1 43  ? 112.296 53.211  62.283 1.00   22.40 ? 42   LEU A N   1 
ATOM   300   C  CA  . LEU A  1 43  ? 112.856 53.621  61.015 1.00   21.98 ? 42   LEU A CA  1 
ATOM   301   C  C   . LEU A  1 43  ? 113.573 54.961  61.080 1.00   21.38 ? 42   LEU A C   1 
ATOM   302   O  O   . LEU A  1 43  ? 113.063 55.911  61.671 1.00   22.03 ? 42   LEU A O   1 
ATOM   303   C  CB  . LEU A  1 43  ? 111.753 53.722  59.952 1.00   22.39 ? 42   LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 43  ? 110.989 52.433  59.644 1.00   23.12 ? 42   LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 43  ? 109.662 52.731  58.943 1.00   23.46 ? 42   LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 43  ? 111.867 51.511  58.835 1.00   22.85 ? 42   LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 44  ? 114.727 55.040  60.418 1.00   20.34 ? 43   HIS A N   1 
ATOM   308   C  CA  . HIS A  1 44  ? 115.499 56.268  60.365 1.00   19.79 ? 43   HIS A CA  1 
ATOM   309   C  C   . HIS A  1 44  ? 115.984 56.530  58.968 1.00   19.72 ? 43   HIS A C   1 
ATOM   310   O  O   . HIS A  1 44  ? 116.618 55.653  58.333 1.00   20.16 ? 43   HIS A O   1 
ATOM   311   C  CB  . HIS A  1 44  ? 116.681 56.176  61.332 1.00   19.32 ? 43   HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 44  ? 116.276 56.137  62.759 1.00   19.40 ? 43   HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 44  ? 116.043 57.261  63.484 1.00   19.37 ? 43   HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 44  ? 115.999 55.052  63.607 1.00   19.49 ? 43   HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 44  ? 115.662 56.904  64.731 1.00   19.44 ? 43   HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 44  ? 115.637 55.559  64.801 1.00   19.38 ? 43   HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 45  ? 115.696 57.729  58.458 1.00   19.42 ? 44   GLY A N   1 
ATOM   318   C  CA  . GLY A  1 45  ? 116.150 58.125  57.124 1.00   19.02 ? 44   GLY A CA  1 
ATOM   319   C  C   . GLY A  1 45  ? 117.665 58.063  57.020 1.00   18.64 ? 44   GLY A C   1 
ATOM   320   O  O   . GLY A  1 45  ? 118.389 58.342  57.981 1.00   18.45 ? 44   GLY A O   1 
ATOM   321   N  N   . PHE A  1 46  ? 118.123 57.733  55.822 1.00   18.56 ? 45   PHE A N   1 
ATOM   322   C  CA  . PHE A  1 46  ? 119.492 57.326  55.548 1.00   18.09 ? 45   PHE A CA  1 
ATOM   323   C  C   . PHE A  1 46  ? 119.804 57.850  54.149 1.00   18.48 ? 45   PHE A C   1 
ATOM   324   O  O   . PHE A  1 46  ? 119.267 57.362  53.144 1.00   18.65 ? 45   PHE A O   1 
ATOM   325   C  CB  . PHE A  1 46  ? 119.535 55.816  55.582 1.00   18.00 ? 45   PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 46  ? 120.905 55.220  55.587 1.00   17.56 ? 45   PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 46  ? 121.834 55.577  56.537 1.00   17.19 ? 45   PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 46  ? 121.220 54.220  54.688 1.00   17.44 ? 45   PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 46  ? 123.090 54.978  56.565 1.00   17.25 ? 45   PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 46  ? 122.467 53.624  54.693 1.00   17.44 ? 45   PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 46  ? 123.409 53.999  55.644 1.00   17.34 ? 45   PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 47  ? 120.619 58.895  54.092 1.00   18.44 ? 46   HIS A N   1 
ATOM   333   C  CA  . HIS A  1 47  ? 120.880 59.599  52.850 1.00   18.38 ? 46   HIS A CA  1 
ATOM   334   C  C   . HIS A  1 47  ? 122.302 59.966  52.682 1.00   17.63 ? 46   HIS A C   1 
ATOM   335   O  O   . HIS A  1 47  ? 123.012 60.237  53.672 1.00   17.41 ? 46   HIS A O   1 
ATOM   336   C  CB  . HIS A  1 47  ? 120.175 60.932  52.856 1.00   19.51 ? 46   HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 47  ? 118.735 60.863  53.184 1.00   20.34 ? 46   HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 47  ? 118.155 61.768  53.965 1.00   20.56 ? 46   HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 47  ? 117.730 59.994  52.757 1.00   21.29 ? 46   HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 47  ? 116.854 61.489  54.082 1.00   21.34 ? 46   HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 47  ? 116.591 60.394  53.345 1.00   21.57 ? 46   HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 48  ? 122.721 60.054  51.425 1.00   17.04 ? 47   VAL A N   1 
ATOM   343   C  CA  . VAL A  1 48  ? 123.960 60.732  51.096 1.00   16.46 ? 47   VAL A CA  1 
ATOM   344   C  C   . VAL A  1 48  ? 123.625 62.196  50.796 1.00   16.52 ? 47   VAL A C   1 
ATOM   345   O  O   . VAL A  1 48  ? 122.850 62.494  49.870 1.00   16.61 ? 47   VAL A O   1 
ATOM   346   C  CB  . VAL A  1 48  ? 124.679 60.097  49.894 1.00   16.14 ? 47   VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 48  ? 125.993 60.843  49.585 1.00   15.70 ? 47   VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 48  ? 124.918 58.607  50.136 1.00   15.77 ? 47   VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 49  ? 124.209 63.105  51.567 1.00   16.38 ? 48   HIS A N   1 
ATOM   350   C  CA  . HIS A  1 49  ? 124.039 64.541  51.308 1.00   16.63 ? 48   HIS A CA  1 
ATOM   351   C  C   . HIS A  1 49  ? 125.168 65.045  50.451 1.00   16.51 ? 48   HIS A C   1 
ATOM   352   O  O   . HIS A  1 49  ? 126.252 64.478  50.447 1.00   16.10 ? 48   HIS A O   1 
ATOM   353   C  CB  . HIS A  1 49  ? 123.965 65.321  52.583 1.00   16.71 ? 48   HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 49  ? 122.641 65.226  53.279 1.00   17.31 ? 48   HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 49  ? 121.930 66.311  53.631 1.00   17.79 ? 48   HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 49  ? 121.914 64.123  53.719 1.00   17.54 ? 48   HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 49  ? 120.794 65.917  54.243 1.00   18.31 ? 48   HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 49  ? 120.793 64.588  54.301 1.00   17.92 ? 48   HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 50  ? 124.918 66.130  49.730 1.00   16.77 ? 49   GLU A N   1 
ATOM   360   C  CA  . GLU A  1 50  ? 125.821 66.578  48.678 1.00   16.91 ? 49   GLU A CA  1 
ATOM   361   C  C   . GLU A  1 50  ? 127.279 66.866  49.089 1.00   16.43 ? 49   GLU A C   1 
ATOM   362   O  O   . GLU A  1 50  ? 128.219 66.438  48.396 1.00   16.36 ? 49   GLU A O   1 
ATOM   363   C  CB  . GLU A  1 50  ? 125.257 67.828  48.003 1.00   17.72 ? 49   GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 50  ? 126.046 68.182  46.758 1.00   18.26 ? 49   GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 50  ? 125.478 69.311  45.954 1.00   19.25 ? 49   GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 50  ? 124.350 69.743  46.190 1.00   20.38 ? 49   GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 50  ? 126.212 69.794  45.077 1.00   20.99 ? 49   GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 51  ? 127.476 67.619  50.165 1.00   16.07 ? 50   PHE A N   1 
ATOM   369   C  CA  . PHE A  1 51  ? 128.819 68.043  50.529 1.00   15.99 ? 50   PHE A CA  1 
ATOM   370   C  C   . PHE A  1 51  ? 129.434 67.280  51.679 1.00   15.52 ? 50   PHE A C   1 
ATOM   371   O  O   . PHE A  1 51  ? 128.785 67.004  52.685 1.00   15.61 ? 50   PHE A O   1 
ATOM   372   C  CB  . PHE A  1 51  ? 128.821 69.532  50.852 1.00   16.47 ? 50   PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 51  ? 128.189 70.351  49.784 1.00   16.89 ? 50   PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 51  ? 128.827 70.505  48.568 1.00   17.22 ? 50   PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 51  ? 126.973 70.944  49.990 1.00   17.25 ? 50   PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 51  ? 128.227 71.230  47.560 1.00   17.78 ? 50   PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 51  ? 126.375 71.682  49.001 1.00   17.95 ? 50   PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 51  ? 126.998 71.818  47.781 1.00   17.96 ? 50   PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 52  ? 130.713 66.985  51.535 1.00   15.20 ? 51   GLY A N   1 
ATOM   380   C  CA  . GLY A  1 52  ? 131.515 66.385  52.604 1.00   15.10 ? 51   GLY A CA  1 
ATOM   381   C  C   . GLY A  1 52  ? 132.134 67.415  53.521 1.00   15.16 ? 51   GLY A C   1 
ATOM   382   O  O   . GLY A  1 52  ? 133.332 67.358  53.830 1.00   15.14 ? 51   GLY A O   1 
ATOM   383   N  N   . ASP A  1 53  ? 131.271 68.291  54.025 1.00   15.44 ? 52   ASP A N   1 
ATOM   384   C  CA  . ASP A  1 53  ? 131.626 69.450  54.842 1.00   15.46 ? 52   ASP A CA  1 
ATOM   385   C  C   . ASP A  1 53  ? 130.988 69.265  56.213 1.00   15.53 ? 52   ASP A C   1 
ATOM   386   O  O   . ASP A  1 53  ? 129.780 69.379  56.380 1.00   15.38 ? 52   ASP A O   1 
ATOM   387   C  CB  . ASP A  1 53  ? 131.109 70.713  54.160 1.00   15.70 ? 52   ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 53  ? 131.517 71.979  54.881 1.00   16.20 ? 52   ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 53  ? 131.757 71.933  56.090 1.00   15.99 ? 52   ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 53  ? 131.590 73.042  54.228 1.00   16.99 ? 52   ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 54  ? 131.823 68.941  57.183 1.00   15.60 ? 53   ASN A N   1 
ATOM   392   C  CA  A ASN A  1 54  ? 131.466 68.678  58.559 0.50   15.91 ? 53   ASN A CA  1 
ATOM   393   C  CA  B ASN A  1 54  ? 131.306 68.754  58.513 0.50   15.63 ? 53   ASN A CA  1 
ATOM   394   C  C   . ASN A  1 54  ? 131.867 69.864  59.447 1.00   16.13 ? 53   ASN A C   1 
ATOM   395   O  O   . ASN A  1 54  ? 131.917 69.728  60.664 1.00   16.39 ? 53   ASN A O   1 
ATOM   396   C  CB  A ASN A  1 54  ? 132.230 67.432  59.027 0.50   16.11 ? 53   ASN A CB  1 
ATOM   397   C  CB  B ASN A  1 54  ? 131.537 67.302  58.979 0.50   15.36 ? 53   ASN A CB  1 
ATOM   398   C  CG  A ASN A  1 54  ? 131.743 66.890  60.368 0.50   16.49 ? 53   ASN A CG  1 
ATOM   399   C  CG  B ASN A  1 54  ? 130.706 66.261  58.185 0.50   15.05 ? 53   ASN A CG  1 
ATOM   400   O  OD1 A ASN A  1 54  ? 132.492 66.865  61.357 0.50   17.43 ? 53   ASN A OD1 1 
ATOM   401   O  OD1 B ASN A  1 54  ? 129.842 66.589  57.345 0.50   14.83 ? 53   ASN A OD1 1 
ATOM   402   N  ND2 A ASN A  1 54  ? 130.503 66.433  60.402 0.50   16.42 ? 53   ASN A ND2 1 
ATOM   403   N  ND2 B ASN A  1 54  ? 130.970 64.987  58.461 0.50   14.90 ? 53   ASN A ND2 1 
ATOM   404   N  N   . THR A  1 55  ? 132.195 71.013  58.843 1.00   16.09 ? 54   THR A N   1 
ATOM   405   C  CA  . THR A  1 55  ? 132.629 72.204  59.595 1.00   16.44 ? 54   THR A CA  1 
ATOM   406   C  C   . THR A  1 55  ? 131.548 72.719  60.559 1.00   16.86 ? 54   THR A C   1 
ATOM   407   O  O   . THR A  1 55  ? 131.862 73.357  61.563 1.00   17.05 ? 54   THR A O   1 
ATOM   408   C  CB  . THR A  1 55  ? 133.097 73.352  58.661 1.00   16.48 ? 54   THR A CB  1 
ATOM   409   O  OG1 . THR A  1 55  ? 132.012 73.816  57.829 1.00   16.32 ? 54   THR A OG1 1 
ATOM   410   C  CG2 . THR A  1 55  ? 134.288 72.892  57.795 1.00   16.16 ? 54   THR A CG2 1 
ATOM   411   N  N   . ALA A  1 56  ? 130.284 72.421  60.248 1.00   17.00 ? 55   ALA A N   1 
ATOM   412   C  CA  . ALA A  1 56  ? 129.145 72.707  61.138 1.00   17.53 ? 55   ALA A CA  1 
ATOM   413   C  C   . ALA A  1 56  ? 128.481 71.390  61.586 1.00   17.68 ? 55   ALA A C   1 
ATOM   414   O  O   . ALA A  1 56  ? 127.268 71.301  61.688 1.00   18.08 ? 55   ALA A O   1 
ATOM   415   C  CB  . ALA A  1 56  ? 128.128 73.591  60.429 1.00   17.45 ? 55   ALA A CB  1 
ATOM   416   N  N   . GLY A  1 57  ? 129.266 70.357  61.824 1.00   17.78 ? 56   GLY A N   1 
ATOM   417   C  CA  . GLY A  1 57  ? 128.678 69.029  62.026 1.00   17.82 ? 56   GLY A CA  1 
ATOM   418   C  C   . GLY A  1 57  ? 127.912 68.613  60.774 1.00   17.91 ? 56   GLY A C   1 
ATOM   419   O  O   . GLY A  1 57  ? 128.331 68.924  59.637 1.00   17.96 ? 56   GLY A O   1 
ATOM   420   N  N   . CYS A  1 58  ? 126.778 67.945  60.968 1.00   17.93 ? 57   CYS A N   1 
ATOM   421   C  CA  . CYS A  1 58  ? 125.939 67.483  59.861 1.00   17.90 ? 57   CYS A CA  1 
ATOM   422   C  C   . CYS A  1 58  ? 125.235 68.610  59.136 1.00   18.02 ? 57   CYS A C   1 
ATOM   423   O  O   . CYS A  1 58  ? 124.825 68.436  58.007 1.00   17.80 ? 57   CYS A O   1 
ATOM   424   C  CB  . CYS A  1 58  ? 124.888 66.498  60.379 1.00   18.26 ? 57   CYS A CB  1 
ATOM   425   S  SG  . CYS A  1 58  ? 125.630 65.093  61.238 1.00   17.94 ? 57   CYS A SG  1 
ATOM   426   N  N   . THR A  1 59  ? 125.096 69.767  59.781 1.00   18.32 ? 58   THR A N   1 
ATOM   427   C  CA  . THR A  1 59  ? 124.365 70.889  59.204 1.00   18.84 ? 58   THR A CA  1 
ATOM   428   C  C   . THR A  1 59  ? 124.990 71.477  57.929 1.00   18.65 ? 58   THR A C   1 
ATOM   429   O  O   . THR A  1 59  ? 124.284 72.005  57.077 1.00   19.72 ? 58   THR A O   1 
ATOM   430   C  CB  . THR A  1 59  ? 124.209 72.002  60.251 1.00   19.79 ? 58   THR A CB  1 
ATOM   431   O  OG1 . THR A  1 59  ? 123.776 71.413  61.498 1.00   20.07 ? 58   THR A OG1 1 
ATOM   432   C  CG2 . THR A  1 59  ? 123.179 72.999  59.788 1.00   20.61 ? 58   THR A CG2 1 
ATOM   433   N  N   . SER A  1 60  ? 126.305 71.368  57.776 1.00   17.68 ? 59   SER A N   1 
ATOM   434   C  CA  . SER A  1 60  ? 126.973 71.918  56.620 1.00   17.29 ? 59   SER A CA  1 
ATOM   435   C  C   . SER A  1 60  ? 127.033 70.969  55.414 1.00   16.93 ? 59   SER A C   1 
ATOM   436   O  O   . SER A  1 60  ? 127.635 71.314  54.403 1.00   16.30 ? 59   SER A O   1 
ATOM   437   C  CB  . SER A  1 60  ? 128.378 72.381  57.007 1.00   17.08 ? 59   SER A CB  1 
ATOM   438   O  OG  . SER A  1 60  ? 128.993 71.426  57.835 1.00   16.68 ? 59   SER A OG  1 
ATOM   439   N  N   . ALA A  1 61  ? 126.402 69.794  55.519 1.00   16.80 ? 60   ALA A N   1 
ATOM   440   C  CA  . ALA A  1 61  ? 126.413 68.795  54.433 1.00   16.76 ? 60   ALA A CA  1 
ATOM   441   C  C   . ALA A  1 61  ? 125.536 69.182  53.236 1.00   17.31 ? 60   ALA A C   1 
ATOM   442   O  O   . ALA A  1 61  ? 125.645 68.597  52.139 1.00   17.36 ? 60   ALA A O   1 
ATOM   443   C  CB  . ALA A  1 61  ? 125.982 67.429  54.953 1.00   16.44 ? 60   ALA A CB  1 
ATOM   444   N  N   . GLY A  1 62  ? 124.646 70.138  53.445 1.00   17.73 ? 61   GLY A N   1 
ATOM   445   C  CA  . GLY A  1 62  ? 123.739 70.573  52.395 1.00   18.32 ? 61   GLY A CA  1 
ATOM   446   C  C   . GLY A  1 62  ? 122.623 69.579  52.175 1.00   18.27 ? 61   GLY A C   1 
ATOM   447   O  O   . GLY A  1 62  ? 122.376 68.734  53.020 1.00   18.06 ? 61   GLY A O   1 
ATOM   448   N  N   . PRO A  1 63  ? 121.952 69.662  51.022 1.00   18.66 ? 62   PRO A N   1 
ATOM   449   C  CA  . PRO A  1 63  ? 120.788 68.833  50.718 1.00   18.86 ? 62   PRO A CA  1 
ATOM   450   C  C   . PRO A  1 63  ? 121.190 67.479  50.166 1.00   18.75 ? 62   PRO A C   1 
ATOM   451   O  O   . PRO A  1 63  ? 122.371 67.195  50.047 1.00   17.93 ? 62   PRO A O   1 
ATOM   452   C  CB  . PRO A  1 63  ? 120.097 69.621  49.612 1.00   19.40 ? 62   PRO A CB  1 
ATOM   453   C  CG  . PRO A  1 63  ? 121.230 70.248  48.867 1.00   19.21 ? 62   PRO A CG  1 
ATOM   454   C  CD  . PRO A  1 63  ? 122.255 70.598  49.920 1.00   18.96 ? 62   PRO A CD  1 
ATOM   455   N  N   . HIS A  1 64  ? 120.204 66.668  49.810 1.00   19.10 ? 63   HIS A N   1 
ATOM   456   C  CA  . HIS A  1 64  ? 120.465 65.332  49.262 1.00   19.68 ? 63   HIS A CA  1 
ATOM   457   C  C   . HIS A  1 64  ? 121.262 65.427  47.982 1.00   19.19 ? 63   HIS A C   1 
ATOM   458   O  O   . HIS A  1 64  ? 121.037 66.314  47.162 1.00   19.17 ? 63   HIS A O   1 
ATOM   459   C  CB  . HIS A  1 64  ? 119.157 64.580  48.995 1.00   20.34 ? 63   HIS A CB  1 
ATOM   460   C  CG  . HIS A  1 64  ? 118.334 64.331  50.229 1.00   21.24 ? 63   HIS A CG  1 
ATOM   461   N  ND1 . HIS A  1 64  ? 117.098 63.787  50.184 1.00   21.73 ? 63   HIS A ND1 1 
ATOM   462   C  CD2 . HIS A  1 64  ? 118.604 64.595  51.580 1.00   21.65 ? 63   HIS A CD2 1 
ATOM   463   C  CE1 . HIS A  1 64  ? 116.607 63.700  51.450 1.00   22.53 ? 63   HIS A CE1 1 
ATOM   464   N  NE2 . HIS A  1 64  ? 117.526 64.203  52.295 1.00   22.57 ? 63   HIS A NE2 1 
ATOM   465   N  N   . PHE A  1 65  ? 122.213 64.527  47.804 1.00   18.99 ? 64   PHE A N   1 
ATOM   466   C  CA  . PHE A  1 65  ? 122.999 64.539  46.585 1.00   19.26 ? 64   PHE A CA  1 
ATOM   467   C  C   . PHE A  1 65  ? 122.034 64.255  45.427 1.00   19.89 ? 64   PHE A C   1 
ATOM   468   O  O   . PHE A  1 65  ? 121.355 63.229  45.422 1.00   20.24 ? 64   PHE A O   1 
ATOM   469   C  CB  . PHE A  1 65  ? 124.126 63.531  46.692 1.00   18.84 ? 64   PHE A CB  1 
ATOM   470   C  CG  . PHE A  1 65  ? 124.963 63.401  45.449 1.00   18.49 ? 64   PHE A CG  1 
ATOM   471   C  CD1 . PHE A  1 65  ? 125.440 64.514  44.792 1.00   18.52 ? 64   PHE A CD1 1 
ATOM   472   C  CD2 . PHE A  1 65  ? 125.324 62.146  44.989 1.00   18.27 ? 64   PHE A CD2 1 
ATOM   473   C  CE1 . PHE A  1 65  ? 126.223 64.389  43.662 1.00   18.51 ? 64   PHE A CE1 1 
ATOM   474   C  CE2 . PHE A  1 65  ? 126.113 62.006  43.867 1.00   18.38 ? 64   PHE A CE2 1 
ATOM   475   C  CZ  . PHE A  1 65  ? 126.566 63.131  43.199 1.00   18.68 ? 64   PHE A CZ  1 
ATOM   476   N  N   . ASN A  1 66  ? 121.922 65.205  44.498 1.00   20.74 ? 65   ASN A N   1 
ATOM   477   C  CA  . ASN A  1 66  ? 120.864 65.195  43.474 1.00   21.70 ? 65   ASN A CA  1 
ATOM   478   C  C   . ASN A  1 66  ? 121.380 65.797  42.173 1.00   22.71 ? 65   ASN A C   1 
ATOM   479   O  O   . ASN A  1 66  ? 120.935 66.860  41.765 1.00   23.73 ? 65   ASN A O   1 
ATOM   480   C  CB  . ASN A  1 66  ? 119.672 66.022  43.972 1.00   22.03 ? 65   ASN A CB  1 
ATOM   481   C  CG  . ASN A  1 66  ? 118.472 65.976  43.036 1.00   22.51 ? 65   ASN A CG  1 
ATOM   482   O  OD1 . ASN A  1 66  ? 118.283 65.006  42.295 1.00   23.01 ? 65   ASN A OD1 1 
ATOM   483   N  ND2 . ASN A  1 66  ? 117.624 66.996  43.109 1.00   22.52 ? 65   ASN A ND2 1 
ATOM   484   N  N   . PRO A  1 67  ? 122.341 65.129  41.529 1.00   23.33 ? 66   PRO A N   1 
ATOM   485   C  CA  . PRO A  1 67  ? 122.918 65.664  40.322 1.00   24.27 ? 66   PRO A CA  1 
ATOM   486   C  C   . PRO A  1 67  ? 121.983 65.603  39.095 1.00   26.19 ? 66   PRO A C   1 
ATOM   487   O  O   . PRO A  1 67  ? 122.224 66.305  38.123 1.00   26.54 ? 66   PRO A O   1 
ATOM   488   C  CB  . PRO A  1 67  ? 124.162 64.781  40.125 1.00   23.66 ? 66   PRO A CB  1 
ATOM   489   C  CG  . PRO A  1 67  ? 123.782 63.480  40.730 1.00   22.99 ? 66   PRO A CG  1 
ATOM   490   C  CD  . PRO A  1 67  ? 123.002 63.871  41.944 1.00   22.97 ? 66   PRO A CD  1 
ATOM   491   N  N   . LEU A  1 68  ? 120.937 64.777  39.126 1.00   27.11 ? 67   LEU A N   1 
ATOM   492   C  CA  . LEU A  1 68  ? 119.958 64.768  38.017 1.00   28.57 ? 67   LEU A CA  1 
ATOM   493   C  C   . LEU A  1 68  ? 118.749 65.682  38.277 1.00   29.85 ? 67   LEU A C   1 
ATOM   494   O  O   . LEU A  1 68  ? 117.794 65.670  37.524 1.00   30.85 ? 67   LEU A O   1 
ATOM   495   C  CB  . LEU A  1 68  ? 119.518 63.337  37.680 1.00   28.72 ? 67   LEU A CB  1 
ATOM   496   C  CG  . LEU A  1 68  ? 120.639 62.451  37.120 1.00   29.24 ? 67   LEU A CG  1 
ATOM   497   C  CD1 . LEU A  1 68  ? 120.205 60.998  36.918 1.00   29.85 ? 67   LEU A CD1 1 
ATOM   498   C  CD2 . LEU A  1 68  ? 121.174 63.029  35.820 1.00   29.92 ? 67   LEU A CD2 1 
ATOM   499   N  N   . SER A  1 69  ? 118.813 66.491  39.329 1.00   30.54 ? 68   SER A N   1 
ATOM   500   C  CA  . SER A  1 69  ? 117.768 67.448  39.648 1.00   32.00 ? 68   SER A CA  1 
ATOM   501   C  C   . SER A  1 69  ? 116.376 66.815  39.656 1.00   33.24 ? 68   SER A C   1 
ATOM   502   O  O   . SER A  1 69  ? 115.461 67.311  39.004 1.00   34.47 ? 68   SER A O   1 
ATOM   503   C  CB  . SER A  1 69  ? 117.835 68.631  38.678 1.00   33.17 ? 68   SER A CB  1 
ATOM   504   O  OG  . SER A  1 69  ? 119.153 69.165  38.623 1.00   33.18 ? 68   SER A OG  1 
ATOM   505   N  N   . ARG A  1 70  ? 116.222 65.715  40.394 1.00   33.40 ? 69   ARG A N   1 
ATOM   506   C  CA  . ARG A  1 70  ? 114.931 65.040  40.519 1.00   33.68 ? 69   ARG A CA  1 
ATOM   507   C  C   . ARG A  1 70  ? 114.303 65.308  41.881 1.00   32.22 ? 69   ARG A C   1 
ATOM   508   O  O   . ARG A  1 70  ? 114.915 65.922  42.739 1.00   31.77 ? 69   ARG A O   1 
ATOM   509   C  CB  . ARG A  1 70  ? 115.094 63.540  40.303 1.00   35.03 ? 69   ARG A CB  1 
ATOM   510   C  CG  . ARG A  1 70  ? 115.858 63.199  39.041 1.00   37.19 ? 69   ARG A CG  1 
ATOM   511   C  CD  . ARG A  1 70  ? 115.073 62.277  38.133 1.00   41.07 ? 69   ARG A CD  1 
ATOM   512   N  NE  . ARG A  1 70  ? 115.623 62.278  36.778 1.00   44.78 ? 69   ARG A NE  1 
ATOM   513   C  CZ  . ARG A  1 70  ? 116.216 61.244  36.177 1.00   46.24 ? 69   ARG A CZ  1 
ATOM   514   N  NH1 . ARG A  1 70  ? 116.346 60.071  36.789 1.00   46.46 ? 69   ARG A NH1 1 
ATOM   515   N  NH2 . ARG A  1 70  ? 116.683 61.390  34.937 1.00   47.87 ? 69   ARG A NH2 1 
ATOM   516   N  N   . LYS A  1 71  ? 113.064 64.871  42.051 1.00   31.77 ? 70   LYS A N   1 
ATOM   517   C  CA  . LYS A  1 71  ? 112.359 64.961  43.322 1.00   31.87 ? 70   LYS A CA  1 
ATOM   518   C  C   . LYS A  1 71  ? 112.796 63.814  44.217 1.00   28.99 ? 70   LYS A C   1 
ATOM   519   O  O   . LYS A  1 71  ? 113.274 62.795  43.738 1.00   26.92 ? 70   LYS A O   1 
ATOM   520   C  CB  . LYS A  1 71  ? 110.832 64.862  43.110 1.00   34.81 ? 70   LYS A CB  1 
ATOM   521   C  CG  . LYS A  1 71  ? 110.212 66.007  42.313 1.00   37.21 ? 70   LYS A CG  1 
ATOM   522   C  CD  . LYS A  1 71  ? 108.675 65.975  42.394 1.00   40.50 ? 70   LYS A CD  1 
ATOM   523   C  CE  . LYS A  1 71  ? 108.041 66.842  41.299 1.00   43.17 ? 70   LYS A CE  1 
ATOM   524   N  NZ  . LYS A  1 71  ? 106.581 67.118  41.494 1.00   44.97 ? 70   LYS A NZ  1 
ATOM   525   N  N   . HIS A  1 72  ? 112.618 63.997  45.523 1.00   27.67 ? 71   HIS A N   1 
ATOM   526   C  CA  . HIS A  1 72  ? 112.960 62.975  46.525 1.00   26.60 ? 71   HIS A CA  1 
ATOM   527   C  C   . HIS A  1 72  ? 112.101 61.755  46.402 1.00   26.10 ? 71   HIS A C   1 
ATOM   528   O  O   . HIS A  1 72  ? 110.903 61.868  46.288 1.00   26.75 ? 71   HIS A O   1 
ATOM   529   C  CB  . HIS A  1 72  ? 112.779 63.550  47.931 1.00   26.01 ? 71   HIS A CB  1 
ATOM   530   C  CG  . HIS A  1 72  ? 113.104 62.589  49.034 1.00   25.55 ? 71   HIS A CG  1 
ATOM   531   N  ND1 . HIS A  1 72  ? 114.370 62.309  49.414 1.00   25.05 ? 71   HIS A ND1 1 
ATOM   532   C  CD2 . HIS A  1 72  ? 112.270 61.846  49.868 1.00   25.82 ? 71   HIS A CD2 1 
ATOM   533   C  CE1 . HIS A  1 72  ? 114.348 61.417  50.426 1.00   24.79 ? 71   HIS A CE1 1 
ATOM   534   N  NE2 . HIS A  1 72  ? 113.062 61.141  50.711 1.00   25.66 ? 71   HIS A NE2 1 
ATOM   535   N  N   . GLY A  1 73  ? 112.713 60.580  46.459 1.00   25.88 ? 72   GLY A N   1 
ATOM   536   C  CA  . GLY A  1 73  ? 111.978 59.329  46.633 1.00   25.92 ? 72   GLY A CA  1 
ATOM   537   C  C   . GLY A  1 73  ? 112.700 58.314  47.522 1.00   25.78 ? 72   GLY A C   1 
ATOM   538   O  O   . GLY A  1 73  ? 113.630 58.656  48.281 1.00   24.32 ? 72   GLY A O   1 
ATOM   539   N  N   . GLY A  1 74  ? 112.256 57.058  47.411 1.00   25.41 ? 73   GLY A N   1 
ATOM   540   C  CA  . GLY A  1 74  ? 112.931 55.912  47.995 1.00   24.75 ? 73   GLY A CA  1 
ATOM   541   C  C   . GLY A  1 74  ? 113.921 55.299  47.016 1.00   24.47 ? 73   GLY A C   1 
ATOM   542   O  O   . GLY A  1 74  ? 113.896 55.592  45.817 1.00   24.25 ? 73   GLY A O   1 
ATOM   543   N  N   . PRO A  1 75  ? 114.796 54.436  47.518 1.00   24.44 ? 74   PRO A N   1 
ATOM   544   C  CA  . PRO A  1 75  ? 115.856 53.896  46.675 1.00   25.22 ? 74   PRO A CA  1 
ATOM   545   C  C   . PRO A  1 75  ? 115.360 53.118  45.447 1.00   26.81 ? 74   PRO A C   1 
ATOM   546   O  O   . PRO A  1 75  ? 116.076 53.069  44.440 1.00   26.03 ? 74   PRO A O   1 
ATOM   547   C  CB  . PRO A  1 75  ? 116.651 52.992  47.631 1.00   24.66 ? 74   PRO A CB  1 
ATOM   548   C  CG  . PRO A  1 75  ? 115.756 52.778  48.817 1.00   24.65 ? 74   PRO A CG  1 
ATOM   549   C  CD  . PRO A  1 75  ? 114.901 53.987  48.917 1.00   24.24 ? 74   PRO A CD  1 
ATOM   550   N  N   . LYS A  1 76  ? 114.156 52.534  45.521 1.00   28.65 ? 75   LYS A N   1 
ATOM   551   C  CA  . LYS A  1 76  ? 113.631 51.729  44.421 1.00   31.29 ? 75   LYS A CA  1 
ATOM   552   C  C   . LYS A  1 76  ? 112.707 52.511  43.498 1.00   32.55 ? 75   LYS A C   1 
ATOM   553   O  O   . LYS A  1 76  ? 112.180 51.945  42.541 1.00   33.90 ? 75   LYS A O   1 
ATOM   554   C  CB  . LYS A  1 76  ? 112.931 50.469  44.970 1.00   32.97 ? 75   LYS A CB  1 
ATOM   555   C  CG  . LYS A  1 76  ? 113.842 49.594  45.834 1.00   33.81 ? 75   LYS A CG  1 
ATOM   556   C  CD  . LYS A  1 76  ? 115.206 49.456  45.157 1.00   35.44 ? 75   LYS A CD  1 
ATOM   557   C  CE  . LYS A  1 76  ? 116.151 48.431  45.770 1.00   36.19 ? 75   LYS A CE  1 
ATOM   558   N  NZ  . LYS A  1 76  ? 117.342 48.294  44.866 1.00   35.13 ? 75   LYS A NZ  1 
ATOM   559   N  N   . ASP A  1 77  ? 112.509 53.801  43.765 1.00   32.45 ? 76   ASP A N   1 
ATOM   560   C  CA  . ASP A  1 77  ? 111.759 54.649  42.847 1.00   33.48 ? 76   ASP A CA  1 
ATOM   561   C  C   . ASP A  1 77  ? 112.639 55.086  41.680 1.00   33.69 ? 76   ASP A C   1 
ATOM   562   O  O   . ASP A  1 77  ? 113.857 55.203  41.805 1.00   34.52 ? 76   ASP A O   1 
ATOM   563   C  CB  . ASP A  1 77  ? 111.238 55.918  43.547 1.00   33.75 ? 76   ASP A CB  1 
ATOM   564   C  CG  . ASP A  1 77  ? 110.265 55.628  44.668 1.00   34.51 ? 76   ASP A CG  1 
ATOM   565   O  OD1 . ASP A  1 77  ? 109.688 54.523  44.695 1.00   37.45 ? 76   ASP A OD1 1 
ATOM   566   O  OD2 . ASP A  1 77  ? 110.057 56.514  45.530 1.00   33.72 ? 76   ASP A OD2 1 
ATOM   567   N  N   . GLU A  1 78  ? 112.004 55.374  40.557 1.00   34.87 ? 77   GLU A N   1 
ATOM   568   C  CA  . GLU A  1 78  ? 112.688 55.943  39.397 1.00   35.70 ? 77   GLU A CA  1 
ATOM   569   C  C   . GLU A  1 78  ? 112.999 57.397  39.691 1.00   34.38 ? 77   GLU A C   1 
ATOM   570   O  O   . GLU A  1 78  ? 114.116 57.857  39.453 1.00   35.56 ? 77   GLU A O   1 
ATOM   571   C  CB  . GLU A  1 78  ? 111.801 55.874  38.137 1.00   37.35 ? 77   GLU A CB  1 
ATOM   572   C  CG  . GLU A  1 78  ? 112.587 55.697  36.841 1.00   38.64 ? 77   GLU A CG  1 
ATOM   573   C  CD  . GLU A  1 78  ? 112.980 54.250  36.589 0.50   38.79 ? 77   GLU A CD  1 
ATOM   574   O  OE1 . GLU A  1 78  ? 112.070 53.409  36.414 0.50   39.08 ? 77   GLU A OE1 1 
ATOM   575   O  OE2 . GLU A  1 78  ? 114.195 53.955  36.562 0.50   38.10 ? 77   GLU A OE2 1 
ATOM   576   N  N   . GLU A  1 79  ? 111.992 58.112  40.190 1.00   32.45 ? 78   GLU A N   1 
ATOM   577   C  CA  . GLU A  1 79  ? 112.139 59.492  40.579 1.00   31.86 ? 78   GLU A CA  1 
ATOM   578   C  C   . GLU A  1 79  ? 112.725 59.522  42.008 1.00   29.76 ? 78   GLU A C   1 
ATOM   579   O  O   . GLU A  1 79  ? 112.018 59.272  42.991 1.00   29.94 ? 78   GLU A O   1 
ATOM   580   C  CB  . GLU A  1 79  ? 110.784 60.198  40.523 1.00   33.66 ? 78   GLU A CB  1 
ATOM   581   C  CG  . GLU A  1 79  ? 110.826 61.690  40.823 1.00   35.15 ? 78   GLU A CG  1 
ATOM   582   C  CD  . GLU A  1 79  ? 111.478 62.504  39.707 1.00   37.36 ? 78   GLU A CD  1 
ATOM   583   O  OE1 . GLU A  1 79  ? 111.758 61.942  38.615 1.00   41.31 ? 78   GLU A OE1 1 
ATOM   584   O  OE2 . GLU A  1 79  ? 111.714 63.719  39.911 1.00   37.02 ? 78   GLU A OE2 1 
ATOM   585   N  N   . ARG A  1 80  ? 114.024 59.783  42.105 1.00   27.02 ? 79   ARG A N   1 
ATOM   586   C  CA  . ARG A  1 80  ? 114.712 59.871  43.396 1.00   25.15 ? 79   ARG A CA  1 
ATOM   587   C  C   . ARG A  1 80  ? 115.963 60.721  43.223 1.00   24.37 ? 79   ARG A C   1 
ATOM   588   O  O   . ARG A  1 80  ? 116.430 60.941  42.107 1.00   24.69 ? 79   ARG A O   1 
ATOM   589   C  CB  . ARG A  1 80  ? 115.110 58.486  43.908 1.00   24.05 ? 79   ARG A CB  1 
ATOM   590   C  CG  . ARG A  1 80  ? 116.124 57.768  43.022 1.00   23.89 ? 79   ARG A CG  1 
ATOM   591   C  CD  . ARG A  1 80  ? 116.628 56.471  43.630 1.00   23.27 ? 79   ARG A CD  1 
ATOM   592   N  NE  . ARG A  1 80  ? 117.910 56.639  44.309 1.00   22.74 ? 79   ARG A NE  1 
ATOM   593   C  CZ  . ARG A  1 80  ? 118.718 55.645  44.664 1.00   22.56 ? 79   ARG A CZ  1 
ATOM   594   N  NH1 . ARG A  1 80  ? 118.401 54.367  44.430 1.00   22.60 ? 79   ARG A NH1 1 
ATOM   595   N  NH2 . ARG A  1 80  ? 119.865 55.929  45.264 1.00   22.18 ? 79   ARG A NH2 1 
ATOM   596   N  N   . HIS A  1 81  ? 116.500 61.195  44.335 1.00   23.05 ? 80   HIS A N   1 
ATOM   597   C  CA  . HIS A  1 81  ? 117.830 61.758  44.346 1.00   22.08 ? 80   HIS A CA  1 
ATOM   598   C  C   . HIS A  1 81  ? 118.803 60.614  44.306 1.00   21.14 ? 80   HIS A C   1 
ATOM   599   O  O   . HIS A  1 81  ? 118.524 59.535  44.858 1.00   21.51 ? 80   HIS A O   1 
ATOM   600   C  CB  . HIS A  1 81  ? 118.040 62.556  45.612 1.00   21.71 ? 80   HIS A CB  1 
ATOM   601   C  CG  . HIS A  1 81  ? 117.033 63.638  45.830 1.00   22.37 ? 80   HIS A CG  1 
ATOM   602   N  ND1 . HIS A  1 81  ? 116.488 63.895  47.037 1.00   22.64 ? 80   HIS A ND1 1 
ATOM   603   C  CD2 . HIS A  1 81  ? 116.461 64.541  44.944 1.00   23.17 ? 80   HIS A CD2 1 
ATOM   604   C  CE1 . HIS A  1 81  ? 115.651 64.937  46.930 1.00   22.92 ? 80   HIS A CE1 1 
ATOM   605   N  NE2 . HIS A  1 81  ? 115.622 65.324  45.646 1.00   22.75 ? 80   HIS A NE2 1 
ATOM   606   N  N   . VAL A  1 82  ? 119.963 60.807  43.690 1.00   20.25 ? 81   VAL A N   1 
ATOM   607   C  CA  . VAL A  1 82  ? 121.042 59.795  43.807 1.00   19.50 ? 81   VAL A CA  1 
ATOM   608   C  C   . VAL A  1 82  ? 121.313 59.466  45.289 1.00   18.62 ? 81   VAL A C   1 
ATOM   609   O  O   . VAL A  1 82  ? 121.513 58.327  45.638 1.00   18.04 ? 81   VAL A O   1 
ATOM   610   C  CB  . VAL A  1 82  ? 122.339 60.223  43.065 1.00   19.42 ? 81   VAL A CB  1 
ATOM   611   C  CG1 . VAL A  1 82  ? 123.511 59.299  43.386 1.00   19.03 ? 81   VAL A CG1 1 
ATOM   612   C  CG2 . VAL A  1 82  ? 122.112 60.256  41.562 1.00   19.80 ? 81   VAL A CG2 1 
ATOM   613   N  N   . GLY A  1 83  ? 121.271 60.467  46.165 1.00   18.36 ? 82   GLY A N   1 
ATOM   614   C  CA  . GLY A  1 83  ? 121.499 60.247  47.596 1.00   18.00 ? 82   GLY A CA  1 
ATOM   615   C  C   . GLY A  1 83  ? 120.416 59.533  48.417 1.00   18.07 ? 82   GLY A C   1 
ATOM   616   O  O   . GLY A  1 83  ? 120.629 59.279  49.607 1.00   17.87 ? 82   GLY A O   1 
ATOM   617   N  N   . ASP A  1 84  ? 119.275 59.177  47.815 1.00   18.03 ? 83   ASP A N   1 
ATOM   618   C  CA  . ASP A  1 84  ? 118.152 58.579  48.583 1.00   17.99 ? 83   ASP A CA  1 
ATOM   619   C  C   . ASP A  1 84  ? 118.279 57.072  48.847 1.00   18.09 ? 83   ASP A C   1 
ATOM   620   O  O   . ASP A  1 84  ? 117.916 56.244  47.994 1.00   18.41 ? 83   ASP A O   1 
ATOM   621   C  CB  . ASP A  1 84  ? 116.839 58.824  47.857 1.00   18.06 ? 83   ASP A CB  1 
ATOM   622   C  CG  . ASP A  1 84  ? 116.476 60.283  47.786 1.00   18.06 ? 83   ASP A CG  1 
ATOM   623   O  OD1 . ASP A  1 84  ? 117.025 61.108  48.547 1.00   17.52 ? 83   ASP A OD1 1 
ATOM   624   O  OD2 . ASP A  1 84  ? 115.621 60.620  46.952 1.00   18.14 ? 83   ASP A OD2 1 
ATOM   625   N  N   . LEU A  1 85  ? 118.760 56.716  50.033 1.00   17.74 ? 84   LEU A N   1 
ATOM   626   C  CA  . LEU A  1 85  ? 118.937 55.307  50.399 1.00   17.73 ? 84   LEU A CA  1 
ATOM   627   C  C   . LEU A  1 85  ? 117.874 54.844  51.414 1.00   18.26 ? 84   LEU A C   1 
ATOM   628   O  O   . LEU A  1 85  ? 118.007 53.778  52.020 1.00   18.98 ? 84   LEU A O   1 
ATOM   629   C  CB  . LEU A  1 85  ? 120.353 55.043  50.894 1.00   17.05 ? 84   LEU A CB  1 
ATOM   630   C  CG  . LEU A  1 85  ? 121.526 55.271  49.930 1.00   16.90 ? 84   LEU A CG  1 
ATOM   631   C  CD1 . LEU A  1 85  ? 122.856 55.072  50.644 1.00   16.23 ? 84   LEU A CD1 1 
ATOM   632   C  CD2 . LEU A  1 85  ? 121.459 54.343  48.710 1.00   16.92 ? 84   LEU A CD2 1 
ATOM   633   N  N   . GLY A  1 86  ? 116.792 55.606  51.551 1.00   18.53 ? 85   GLY A N   1 
ATOM   634   C  CA  . GLY A  1 86  ? 115.611 55.129  52.253 1.00   18.96 ? 85   GLY A CA  1 
ATOM   635   C  C   . GLY A  1 86  ? 115.738 55.193  53.758 1.00   19.15 ? 85   GLY A C   1 
ATOM   636   O  O   . GLY A  1 86  ? 116.143 56.239  54.306 1.00   18.68 ? 85   GLY A O   1 
ATOM   637   N  N   . ASN A  1 87  ? 115.396 54.083  54.417 1.00   19.45 ? 86   ASN A N   1 
ATOM   638   C  CA  . ASN A  1 87  ? 115.399 53.975  55.866 1.00   19.94 ? 86   ASN A CA  1 
ATOM   639   C  C   . ASN A  1 87  ? 116.247 52.809  56.334 1.00   20.39 ? 86   ASN A C   1 
ATOM   640   O  O   . ASN A  1 87  ? 116.322 51.785  55.660 1.00   21.41 ? 86   ASN A O   1 
ATOM   641   C  CB  . ASN A  1 87  ? 113.984 53.740  56.374 1.00   20.63 ? 86   ASN A CB  1 
ATOM   642   C  CG  . ASN A  1 87  ? 113.112 54.989  56.312 1.00   20.87 ? 86   ASN A CG  1 
ATOM   643   O  OD1 . ASN A  1 87  ? 113.435 56.025  56.926 1.00   20.69 ? 86   ASN A OD1 1 
ATOM   644   N  ND2 . ASN A  1 87  ? 111.968 54.879  55.628 1.00   20.81 ? 86   ASN A ND2 1 
ATOM   645   N  N   . VAL A  1 88  ? 116.888 52.967  57.496 1.00   20.46 ? 87   VAL A N   1 
ATOM   646   C  CA  . VAL A  1 88  ? 117.449 51.842  58.219 1.00   20.39 ? 87   VAL A CA  1 
ATOM   647   C  C   . VAL A  1 88  ? 116.488 51.597  59.385 1.00   20.92 ? 87   VAL A C   1 
ATOM   648   O  O   . VAL A  1 88  ? 115.705 52.487  59.741 1.00   20.86 ? 87   VAL A O   1 
ATOM   649   C  CB  . VAL A  1 88  ? 118.903 52.092  58.710 1.00   20.13 ? 87   VAL A CB  1 
ATOM   650   C  CG1 . VAL A  1 88  ? 119.856 52.246  57.525 1.00   20.02 ? 87   VAL A CG1 1 
ATOM   651   C  CG2 . VAL A  1 88  ? 118.988 53.283  59.671 1.00   19.75 ? 87   VAL A CG2 1 
ATOM   652   N  N   . THR A  1 89  ? 116.528 50.391  59.948 1.00   21.15 ? 88   THR A N   1 
ATOM   653   C  CA  . THR A  1 89  ? 115.643 50.023  61.053 1.00   21.70 ? 88   THR A CA  1 
ATOM   654   C  C   . THR A  1 89  ? 116.453 49.657  62.281 1.00   21.78 ? 88   THR A C   1 
ATOM   655   O  O   . THR A  1 89  ? 117.273 48.751  62.220 1.00   22.25 ? 88   THR A O   1 
ATOM   656   C  CB  . THR A  1 89  ? 114.746 48.839  60.669 1.00   22.40 ? 88   THR A CB  1 
ATOM   657   O  OG1 . THR A  1 89  ? 114.083 49.143  59.431 1.00   22.66 ? 88   THR A OG1 1 
ATOM   658   C  CG2 . THR A  1 89  ? 113.698 48.541  61.799 1.00   22.74 ? 88   THR A CG2 1 
ATOM   659   N  N   . ALA A  1 90  ? 116.230 50.387  63.377 1.00   22.00 ? 89   ALA A N   1 
ATOM   660   C  CA  . ALA A  1 90  ? 116.856 50.113  64.672 1.00   22.28 ? 89   ALA A CA  1 
ATOM   661   C  C   . ALA A  1 90  ? 115.947 49.174  65.504 1.00   23.02 ? 89   ALA A C   1 
ATOM   662   O  O   . ALA A  1 90  ? 114.754 49.376  65.585 1.00   23.28 ? 89   ALA A O   1 
ATOM   663   C  CB  . ALA A  1 90  ? 117.118 51.423  65.431 1.00   21.14 ? 89   ALA A CB  1 
ATOM   664   N  N   . ASP A  1 91  ? 116.529 48.165  66.127 1.00   24.03 ? 90   ASP A N   1 
ATOM   665   C  CA  . ASP A  1 91  ? 115.788 47.221  66.955 1.00   25.18 ? 90   ASP A CA  1 
ATOM   666   C  C   . ASP A  1 91  ? 115.618 47.804  68.377 1.00   25.66 ? 90   ASP A C   1 
ATOM   667   O  O   . ASP A  1 91  ? 115.991 48.951  68.636 1.00   24.26 ? 90   ASP A O   1 
ATOM   668   C  CB  . ASP A  1 91  ? 116.539 45.885  66.983 1.00   25.57 ? 90   ASP A CB  1 
ATOM   669   C  CG  . ASP A  1 91  ? 117.900 45.992  67.672 1.00   26.01 ? 90   ASP A CG  1 
ATOM   670   O  OD1 . ASP A  1 91  ? 118.168 47.009  68.364 1.00   24.83 ? 90   ASP A OD1 1 
ATOM   671   O  OD2 . ASP A  1 91  ? 118.709 45.041  67.526 1.00   27.31 ? 90   ASP A OD2 1 
ATOM   672   N  N   . LYS A  1 92  ? 115.090 46.998  69.300 1.00   26.84 ? 91   LYS A N   1 
ATOM   673   C  CA  . LYS A  1 92  ? 114.738 47.475  70.641 1.00   27.98 ? 91   LYS A CA  1 
ATOM   674   C  C   . LYS A  1 92  ? 115.977 47.764  71.487 1.00   27.55 ? 91   LYS A C   1 
ATOM   675   O  O   . LYS A  1 92  ? 115.897 48.417  72.515 1.00   28.36 ? 91   LYS A O   1 
ATOM   676   C  CB  . LYS A  1 92  ? 113.834 46.449  71.349 1.00   29.79 ? 91   LYS A CB  1 
ATOM   677   C  CG  . LYS A  1 92  ? 114.588 45.237  71.888 1.00   31.31 ? 91   LYS A CG  1 
ATOM   678   C  CD  . LYS A  1 92  ? 113.645 44.060  72.172 1.00   33.76 ? 91   LYS A CD  1 
ATOM   679   C  CE  . LYS A  1 92  ? 114.249 43.066  73.165 1.00   35.23 ? 91   LYS A CE  1 
ATOM   680   N  NZ  . LYS A  1 92  ? 115.695 42.796  72.916 1.00   36.80 ? 91   LYS A NZ  1 
ATOM   681   N  N   . ASP A  1 93  ? 117.129 47.273  71.048 1.00   27.43 ? 92   ASP A N   1 
ATOM   682   C  CA  . ASP A  1 93  ? 118.388 47.651  71.649 1.00   27.65 ? 92   ASP A CA  1 
ATOM   683   C  C   . ASP A  1 93  ? 119.020 48.905  71.030 1.00   25.96 ? 92   ASP A C   1 
ATOM   684   O  O   . ASP A  1 93  ? 120.093 49.316  71.439 1.00   25.67 ? 92   ASP A O   1 
ATOM   685   C  CB  . ASP A  1 93  ? 119.327 46.461  71.603 1.00   28.91 ? 92   ASP A CB  1 
ATOM   686   C  CG  . ASP A  1 93  ? 118.837 45.353  72.481 1.00   31.36 ? 92   ASP A CG  1 
ATOM   687   O  OD1 . ASP A  1 93  ? 118.621 45.630  73.680 1.00   33.13 ? 92   ASP A OD1 1 
ATOM   688   O  OD2 . ASP A  1 93  ? 118.619 44.233  71.986 1.00   34.07 ? 92   ASP A OD2 1 
ATOM   689   N  N   . GLY A  1 94  ? 118.338 49.517  70.074 1.00   24.64 ? 93   GLY A N   1 
ATOM   690   C  CA  . GLY A  1 94  ? 118.818 50.736  69.454 1.00   24.02 ? 93   GLY A CA  1 
ATOM   691   C  C   . GLY A  1 94  ? 119.851 50.536  68.358 1.00   23.47 ? 93   GLY A C   1 
ATOM   692   O  O   . GLY A  1 94  ? 120.458 51.520  67.888 1.00   23.12 ? 93   GLY A O   1 
ATOM   693   N  N   . VAL A  1 95  ? 120.023 49.289  67.922 1.00   23.44 ? 94   VAL A N   1 
ATOM   694   C  CA  . VAL A  1 95  ? 120.995 48.938  66.892 1.00   23.76 ? 94   VAL A CA  1 
ATOM   695   C  C   . VAL A  1 95  ? 120.318 48.700  65.542 1.00   24.18 ? 94   VAL A C   1 
ATOM   696   O  O   . VAL A  1 95  ? 119.389 47.894  65.437 1.00   24.36 ? 94   VAL A O   1 
ATOM   697   C  CB  . VAL A  1 95  ? 121.775 47.675  67.251 1.00   24.16 ? 94   VAL A CB  1 
ATOM   698   C  CG1 . VAL A  1 95  ? 122.749 47.333  66.125 1.00   24.04 ? 94   VAL A CG1 1 
ATOM   699   C  CG2 . VAL A  1 95  ? 122.505 47.854  68.575 1.00   24.42 ? 94   VAL A CG2 1 
ATOM   700   N  N   . ALA A  1 96  ? 120.787 49.405  64.513 1.00   23.94 ? 95   ALA A N   1 
ATOM   701   C  CA  . ALA A  1 96  ? 120.310 49.218  63.144 1.00   24.57 ? 95   ALA A CA  1 
ATOM   702   C  C   . ALA A  1 96  ? 121.370 48.482  62.361 1.00   25.36 ? 95   ALA A C   1 
ATOM   703   O  O   . ALA A  1 96  ? 122.447 49.039  62.088 1.00   25.80 ? 95   ALA A O   1 
ATOM   704   C  CB  . ALA A  1 96  ? 120.011 50.565  62.489 1.00   24.12 ? 95   ALA A CB  1 
ATOM   705   N  N   . ASP A  1 97  ? 121.099 47.232  62.016 1.00   26.08 ? 96   ASP A N   1 
ATOM   706   C  CA  . ASP A  1 97  ? 122.024 46.484  61.179 1.00   27.30 ? 96   ASP A CA  1 
ATOM   707   C  C   . ASP A  1 97  ? 121.672 46.775  59.710 1.00   26.32 ? 96   ASP A C   1 
ATOM   708   O  O   . ASP A  1 97  ? 120.517 46.641  59.279 1.00   26.25 ? 96   ASP A O   1 
ATOM   709   C  CB  . ASP A  1 97  ? 122.041 44.984  61.538 1.00   29.67 ? 96   ASP A CB  1 
ATOM   710   C  CG  . ASP A  1 97  ? 122.746 44.703  62.908 1.00   31.62 ? 96   ASP A CG  1 
ATOM   711   O  OD1 . ASP A  1 97  ? 123.859 45.217  63.183 1.00   31.95 ? 96   ASP A OD1 1 
ATOM   712   O  OD2 . ASP A  1 97  ? 122.167 43.976  63.740 1.00   34.99 ? 96   ASP A OD2 1 
ATOM   713   N  N   . VAL A  1 98  ? 122.667 47.267  58.972 1.00   25.14 ? 97   VAL A N   1 
ATOM   714   C  CA  . VAL A  1 98  ? 122.434 47.800  57.651 1.00   24.11 ? 97   VAL A CA  1 
ATOM   715   C  C   . VAL A  1 98  ? 122.983 46.847  56.605 1.00   24.56 ? 97   VAL A C   1 
ATOM   716   O  O   . VAL A  1 98  ? 124.106 46.363  56.711 1.00   24.24 ? 97   VAL A O   1 
ATOM   717   C  CB  . VAL A  1 98  ? 123.079 49.173  57.472 1.00   23.39 ? 97   VAL A CB  1 
ATOM   718   C  CG1 . VAL A  1 98  ? 122.882 49.670  56.040 1.00   22.85 ? 97   VAL A CG1 1 
ATOM   719   C  CG2 . VAL A  1 98  ? 122.498 50.149  58.480 1.00   23.00 ? 97   VAL A CG2 1 
ATOM   720   N  N   . SER A  1 99  ? 122.175 46.597  55.589 1.00   24.83 ? 98   SER A N   1 
ATOM   721   C  CA  . SER A  1 99  ? 122.583 45.785  54.469 1.00   26.04 ? 98   SER A CA  1 
ATOM   722   C  C   . SER A  1 99  ? 121.678 46.142  53.306 1.00   26.43 ? 98   SER A C   1 
ATOM   723   O  O   . SER A  1 99  ? 120.491 45.872  53.352 1.00   25.91 ? 98   SER A O   1 
ATOM   724   C  CB  . SER A  1 99  ? 122.456 44.311  54.813 1.00   26.93 ? 98   SER A CB  1 
ATOM   725   O  OG  . SER A  1 99  ? 122.200 43.622  53.632 1.00   28.41 ? 98   SER A OG  1 
ATOM   726   N  N   . ILE A  1 100 ? 122.257 46.796  52.302 1.00   26.35 ? 99   ILE A N   1 
ATOM   727   C  CA  . ILE A  1 100 ? 121.542 47.438  51.207 1.00   26.73 ? 99   ILE A CA  1 
ATOM   728   C  C   . ILE A  1 100 ? 122.354 47.100  49.961 1.00   26.02 ? 99   ILE A C   1 
ATOM   729   O  O   . ILE A  1 100 ? 123.569 46.912  50.031 1.00   24.97 ? 99   ILE A O   1 
ATOM   730   C  CB  . ILE A  1 100 ? 121.565 48.993  51.359 1.00   27.70 ? 99   ILE A CB  1 
ATOM   731   C  CG1 . ILE A  1 100 ? 120.571 49.490  52.376 1.00   29.31 ? 99   ILE A CG1 1 
ATOM   732   C  CG2 . ILE A  1 100 ? 121.242 49.734  50.072 1.00   27.38 ? 99   ILE A CG2 1 
ATOM   733   C  CD1 . ILE A  1 100 ? 120.555 51.015  52.456 1.00   29.55 ? 99   ILE A CD1 1 
ATOM   734   N  N   . GLU A  1 101 ? 121.684 47.018  48.827 1.00   25.98 ? 100  GLU A N   1 
ATOM   735   C  CA  . GLU A  1 101 ? 122.360 47.069  47.541 1.00   26.54 ? 100  GLU A CA  1 
ATOM   736   C  C   . GLU A  1 101 ? 121.697 48.164  46.737 1.00   24.79 ? 100  GLU A C   1 
ATOM   737   O  O   . GLU A  1 101 ? 120.482 48.298  46.764 1.00   24.87 ? 100  GLU A O   1 
ATOM   738   C  CB  . GLU A  1 101 ? 122.263 45.724  46.807 1.00   28.51 ? 100  GLU A CB  1 
ATOM   739   C  CG  . GLU A  1 101 ? 123.113 45.680  45.549 1.00   29.87 ? 100  GLU A CG  1 
ATOM   740   C  CD  . GLU A  1 101 ? 123.013 44.349  44.817 1.00   32.71 ? 100  GLU A CD  1 
ATOM   741   O  OE1 . GLU A  1 101 ? 123.476 43.339  45.400 1.00   34.63 ? 100  GLU A OE1 1 
ATOM   742   O  OE2 . GLU A  1 101 ? 122.464 44.329  43.684 1.00   32.24 ? 100  GLU A OE2 1 
ATOM   743   N  N   . ASP A  1 102 ? 122.484 48.961  46.037 1.00   23.07 ? 101  ASP A N   1 
ATOM   744   C  CA  . ASP A  1 102 ? 121.923 50.066  45.276 1.00   22.67 ? 101  ASP A CA  1 
ATOM   745   C  C   . ASP A  1 102 ? 122.653 50.249  43.948 1.00   22.16 ? 101  ASP A C   1 
ATOM   746   O  O   . ASP A  1 102 ? 123.879 50.170  43.892 1.00   21.31 ? 101  ASP A O   1 
ATOM   747   C  CB  . ASP A  1 102 ? 122.011 51.355  46.093 1.00   22.17 ? 101  ASP A CB  1 
ATOM   748   C  CG  . ASP A  1 102 ? 121.153 52.463  45.519 1.00   22.44 ? 101  ASP A CG  1 
ATOM   749   O  OD1 . ASP A  1 102 ? 119.937 52.454  45.796 1.00   22.93 ? 101  ASP A OD1 1 
ATOM   750   O  OD2 . ASP A  1 102 ? 121.685 53.336  44.785 1.00   21.88 ? 101  ASP A OD2 1 
ATOM   751   N  N   . SER A  1 103 ? 121.914 50.536  42.887 1.00   22.09 ? 102  SER A N   1 
ATOM   752   C  CA  . SER A  1 103 ? 122.562 50.651  41.581 1.00   22.94 ? 102  SER A CA  1 
ATOM   753   C  C   . SER A  1 103 ? 122.496 52.062  41.016 1.00   22.33 ? 102  SER A C   1 
ATOM   754   O  O   . SER A  1 103 ? 122.786 52.268  39.838 1.00   23.65 ? 102  SER A O   1 
ATOM   755   C  CB  . SER A  1 103 ? 121.995 49.617  40.604 1.00   23.66 ? 102  SER A CB  1 
ATOM   756   O  OG  . SER A  1 103 ? 120.615 49.851  40.475 1.00   24.89 ? 102  SER A OG  1 
ATOM   757   N  N   . VAL A  1 104 ? 122.203 53.038  41.873 1.00   20.92 ? 103  VAL A N   1 
ATOM   758   C  CA  . VAL A  1 104 ? 122.134 54.420  41.457 1.00   19.97 ? 103  VAL A CA  1 
ATOM   759   C  C   . VAL A  1 104 ? 123.368 55.149  42.013 1.00   19.37 ? 103  VAL A C   1 
ATOM   760   O  O   . VAL A  1 104 ? 124.051 55.814  41.259 1.00   18.97 ? 103  VAL A O   1 
ATOM   761   C  CB  . VAL A  1 104 ? 120.788 55.034  41.890 1.00   20.21 ? 103  VAL A CB  1 
ATOM   762   C  CG1 . VAL A  1 104 ? 120.769 56.547  41.702 1.00   19.84 ? 103  VAL A CG1 1 
ATOM   763   C  CG2 . VAL A  1 104 ? 119.643 54.366  41.109 1.00   20.63 ? 103  VAL A CG2 1 
ATOM   764   N  N   . ILE A  1 105 ? 123.679 54.998  43.310 1.00   18.64 ? 104  ILE A N   1 
ATOM   765   C  CA  . ILE A  1 105 ? 124.966 55.471  43.825 1.00   18.11 ? 104  ILE A CA  1 
ATOM   766   C  C   . ILE A  1 105 ? 126.136 54.737  43.158 1.00   18.03 ? 104  ILE A C   1 
ATOM   767   O  O   . ILE A  1 105 ? 125.993 53.615  42.683 1.00   18.71 ? 104  ILE A O   1 
ATOM   768   C  CB  . ILE A  1 105 ? 125.076 55.379  45.360 1.00   17.74 ? 104  ILE A CB  1 
ATOM   769   C  CG1 . ILE A  1 105 ? 124.963 53.922  45.840 1.00   18.09 ? 104  ILE A CG1 1 
ATOM   770   C  CG2 . ILE A  1 105 ? 124.002 56.253  46.015 1.00   17.49 ? 104  ILE A CG2 1 
ATOM   771   C  CD1 . ILE A  1 105 ? 125.288 53.716  47.303 1.00   17.69 ? 104  ILE A CD1 1 
ATOM   772   N  N   . SER A  1 106 ? 127.293 55.380  43.122 1.00   17.47 ? 105  SER A N   1 
ATOM   773   C  CA  . SER A  1 106 ? 128.511 54.745  42.642 1.00   17.38 ? 105  SER A CA  1 
ATOM   774   C  C   . SER A  1 106 ? 129.695 55.171  43.513 1.00   17.32 ? 105  SER A C   1 
ATOM   775   O  O   . SER A  1 106 ? 129.615 56.157  44.246 1.00   17.02 ? 105  SER A O   1 
ATOM   776   C  CB  . SER A  1 106 ? 128.767 55.136  41.175 1.00   17.21 ? 105  SER A CB  1 
ATOM   777   O  OG  . SER A  1 106 ? 129.754 54.290  40.600 1.00   16.96 ? 105  SER A OG  1 
ATOM   778   N  N   . LEU A  1 107 ? 130.783 54.407  43.443 1.00   17.76 ? 106  LEU A N   1 
ATOM   779   C  CA  . LEU A  1 107 ? 132.033 54.779  44.097 1.00   17.69 ? 106  LEU A CA  1 
ATOM   780   C  C   . LEU A  1 107 ? 133.021 55.345  43.075 1.00   18.53 ? 106  LEU A C   1 
ATOM   781   O  O   . LEU A  1 107 ? 134.199 55.550  43.397 1.00   18.56 ? 106  LEU A O   1 
ATOM   782   C  CB  . LEU A  1 107 ? 132.643 53.607  44.838 1.00   17.62 ? 106  LEU A CB  1 
ATOM   783   C  CG  . LEU A  1 107 ? 131.830 52.903  45.917 1.00   17.51 ? 106  LEU A CG  1 
ATOM   784   C  CD1 . LEU A  1 107 ? 132.725 51.829  46.523 1.00   17.50 ? 106  LEU A CD1 1 
ATOM   785   C  CD2 . LEU A  1 107 ? 131.279 53.872  46.971 1.00   16.92 ? 106  LEU A CD2 1 
ATOM   786   N  N   . SER A  1 108 ? 132.533 55.634  41.861 1.00   19.15 ? 107  SER A N   1 
ATOM   787   C  CA  . SER A  1 108 ? 133.309 56.355  40.860 1.00   19.97 ? 107  SER A CA  1 
ATOM   788   C  C   . SER A  1 108 ? 132.348 57.028  39.872 1.00   20.76 ? 107  SER A C   1 
ATOM   789   O  O   . SER A  1 108 ? 131.143 56.771  39.893 1.00   19.67 ? 107  SER A O   1 
ATOM   790   C  CB  . SER A  1 108 ? 134.284 55.417  40.123 1.00   20.33 ? 107  SER A CB  1 
ATOM   791   O  OG  . SER A  1 108 ? 133.611 54.282  39.554 1.00   20.93 ? 107  SER A OG  1 
ATOM   792   N  N   . GLY A  1 109 ? 132.902 57.904  39.035 1.00   21.91 ? 108  GLY A N   1 
ATOM   793   C  CA  . GLY A  1 109 ? 132.147 58.654  38.033 1.00   23.22 ? 108  GLY A CA  1 
ATOM   794   C  C   . GLY A  1 109 ? 131.184 59.692  38.597 1.00   24.87 ? 108  GLY A C   1 
ATOM   795   O  O   . GLY A  1 109 ? 131.339 60.176  39.738 1.00   23.48 ? 108  GLY A O   1 
ATOM   796   N  N   . ASP A  1 110 ? 130.171 60.026  37.806 1.00   26.47 ? 109  ASP A N   1 
ATOM   797   C  CA  . ASP A  1 110 ? 129.330 61.185  38.115 1.00   28.36 ? 109  ASP A CA  1 
ATOM   798   C  C   . ASP A  1 110 ? 128.425 61.007  39.316 1.00   26.61 ? 109  ASP A C   1 
ATOM   799   O  O   . ASP A  1 110 ? 128.088 61.993  39.959 1.00   27.43 ? 109  ASP A O   1 
ATOM   800   C  CB  . ASP A  1 110 ? 128.462 61.591  36.905 1.00   32.31 ? 109  ASP A CB  1 
ATOM   801   C  CG  . ASP A  1 110 ? 129.258 62.299  35.823 1.00   34.94 ? 109  ASP A CG  1 
ATOM   802   O  OD1 . ASP A  1 110 ? 130.332 62.901  36.127 1.00   36.99 ? 109  ASP A OD1 1 
ATOM   803   O  OD2 . ASP A  1 110 ? 128.810 62.221  34.656 1.00   39.47 ? 109  ASP A OD2 1 
ATOM   804   N  N   . HIS A  1 111 ? 128.008 59.774  39.604 1.00   24.76 ? 110  HIS A N   1 
ATOM   805   C  CA  . HIS A  1 111 ? 127.238 59.498  40.815 1.00   23.94 ? 110  HIS A CA  1 
ATOM   806   C  C   . HIS A  1 111 ? 128.109 59.074  41.971 1.00   22.13 ? 110  HIS A C   1 
ATOM   807   O  O   . HIS A  1 111 ? 127.616 58.453  42.919 1.00   21.44 ? 110  HIS A O   1 
ATOM   808   C  CB  . HIS A  1 111 ? 126.168 58.436  40.525 1.00   24.38 ? 110  HIS A CB  1 
ATOM   809   C  CG  . HIS A  1 111 ? 125.082 58.923  39.599 1.00   25.75 ? 110  HIS A CG  1 
ATOM   810   N  ND1 . HIS A  1 111 ? 123.962 58.196  39.328 1.00   26.97 ? 110  HIS A ND1 1 
ATOM   811   C  CD2 . HIS A  1 111 ? 124.947 60.123  38.908 1.00   25.68 ? 110  HIS A CD2 1 
ATOM   812   C  CE1 . HIS A  1 111 ? 123.183 58.889  38.470 1.00   26.54 ? 110  HIS A CE1 1 
ATOM   813   N  NE2 . HIS A  1 111 ? 123.785 60.065  38.217 1.00   25.90 ? 110  HIS A NE2 1 
ATOM   814   N  N   . CYS A  1 112 ? 129.402 59.387  41.908 1.00   21.16 ? 111  CYS A N   1 
ATOM   815   C  CA  . CYS A  1 112 ? 130.323 59.050  42.992 1.00   21.03 ? 111  CYS A CA  1 
ATOM   816   C  C   . CYS A  1 112 ? 129.893 59.704  44.320 1.00   19.41 ? 111  CYS A C   1 
ATOM   817   O  O   . CYS A  1 112 ? 129.636 60.909  44.379 1.00   18.98 ? 111  CYS A O   1 
ATOM   818   C  CB  . CYS A  1 112 ? 131.753 59.490  42.668 1.00   22.11 ? 111  CYS A CB  1 
ATOM   819   S  SG  . CYS A  1 112 ? 133.022 58.869  43.804 1.00   24.98 ? 111  CYS A SG  1 
ATOM   820   N  N   . ILE A  1 113 ? 129.843 58.903  45.368 1.00   17.76 ? 112  ILE A N   1 
ATOM   821   C  CA  . ILE A  1 113 ? 129.492 59.391  46.693 1.00   17.14 ? 112  ILE A CA  1 
ATOM   822   C  C   . ILE A  1 113 ? 130.707 59.553  47.637 1.00   16.41 ? 112  ILE A C   1 
ATOM   823   O  O   . ILE A  1 113 ? 130.567 60.039  48.748 1.00   16.40 ? 112  ILE A O   1 
ATOM   824   C  CB  . ILE A  1 113 ? 128.391 58.507  47.324 1.00   17.04 ? 112  ILE A CB  1 
ATOM   825   C  CG1 . ILE A  1 113 ? 128.870 57.063  47.516 1.00   17.31 ? 112  ILE A CG1 1 
ATOM   826   C  CG2 . ILE A  1 113 ? 127.141 58.543  46.451 1.00   16.79 ? 112  ILE A CG2 1 
ATOM   827   C  CD1 . ILE A  1 113 ? 128.026 56.271  48.517 1.00   17.73 ? 112  ILE A CD1 1 
ATOM   828   N  N   . ILE A  1 114 ? 131.891 59.155  47.181 1.00   15.96 ? 113  ILE A N   1 
ATOM   829   C  CA  . ILE A  1 114 ? 133.118 59.388  47.904 1.00   15.55 ? 113  ILE A CA  1 
ATOM   830   C  C   . ILE A  1 114 ? 133.346 60.903  48.105 1.00   15.29 ? 113  ILE A C   1 
ATOM   831   O  O   . ILE A  1 114 ? 133.171 61.698  47.185 1.00   15.09 ? 113  ILE A O   1 
ATOM   832   C  CB  . ILE A  1 114 ? 134.286 58.689  47.177 1.00   15.89 ? 113  ILE A CB  1 
ATOM   833   C  CG1 . ILE A  1 114 ? 134.179 57.167  47.423 1.00   16.13 ? 113  ILE A CG1 1 
ATOM   834   C  CG2 . ILE A  1 114 ? 135.652 59.224  47.631 1.00   15.74 ? 113  ILE A CG2 1 
ATOM   835   C  CD1 . ILE A  1 114 ? 135.064 56.376  46.507 1.00   16.40 ? 113  ILE A CD1 1 
ATOM   836   N  N   . GLY A  1 115 ? 133.677 61.302  49.335 1.00   14.91 ? 114  GLY A N   1 
ATOM   837   C  CA  . GLY A  1 115 ? 133.862 62.726  49.663 1.00   14.74 ? 114  GLY A CA  1 
ATOM   838   C  C   . GLY A  1 115 ? 132.561 63.472  49.936 1.00   14.69 ? 114  GLY A C   1 
ATOM   839   O  O   . GLY A  1 115 ? 132.587 64.677  50.188 1.00   14.59 ? 114  GLY A O   1 
ATOM   840   N  N   . ARG A  1 116 ? 131.431 62.769  49.870 1.00   14.31 ? 115  ARG A N   1 
ATOM   841   C  CA  . ARG A  1 116 ? 130.150 63.332  50.273 1.00   14.36 ? 115  ARG A CA  1 
ATOM   842   C  C   . ARG A  1 116 ? 129.806 62.846  51.699 1.00   14.07 ? 115  ARG A C   1 
ATOM   843   O  O   . ARG A  1 116 ? 130.608 62.142  52.329 1.00   14.12 ? 115  ARG A O   1 
ATOM   844   C  CB  . ARG A  1 116 ? 129.069 62.991  49.230 1.00   14.50 ? 115  ARG A CB  1 
ATOM   845   C  CG  . ARG A  1 116 ? 129.499 63.431  47.838 1.00   14.77 ? 115  ARG A CG  1 
ATOM   846   C  CD  . ARG A  1 116 ? 128.409 63.390  46.784 1.00   15.11 ? 115  ARG A CD  1 
ATOM   847   N  NE  . ARG A  1 116 ? 128.961 63.670  45.467 1.00   15.26 ? 115  ARG A NE  1 
ATOM   848   C  CZ  . ARG A  1 116 ? 129.155 64.887  44.960 1.00   15.68 ? 115  ARG A CZ  1 
ATOM   849   N  NH1 . ARG A  1 116 ? 128.862 66.000  45.653 1.00   15.89 ? 115  ARG A NH1 1 
ATOM   850   N  NH2 . ARG A  1 116 ? 129.673 65.002  43.753 1.00   15.85 ? 115  ARG A NH2 1 
ATOM   851   N  N   . THR A  1 117 ? 128.652 63.233  52.218 1.00   13.90 ? 116  THR A N   1 
ATOM   852   C  CA  . THR A  1 117 ? 128.296 62.931  53.601 1.00   13.69 ? 116  THR A CA  1 
ATOM   853   C  C   . THR A  1 117 ? 127.153 61.952  53.716 1.00   13.89 ? 116  THR A C   1 
ATOM   854   O  O   . THR A  1 117 ? 126.084 62.170  53.169 1.00   14.07 ? 116  THR A O   1 
ATOM   855   C  CB  . THR A  1 117 ? 127.919 64.209  54.374 1.00   13.58 ? 116  THR A CB  1 
ATOM   856   O  OG1 . THR A  1 117 ? 129.030 65.096  54.391 1.00   13.23 ? 116  THR A OG1 1 
ATOM   857   C  CG2 . THR A  1 117 ? 127.534 63.874  55.832 1.00   13.43 ? 116  THR A CG2 1 
ATOM   858   N  N   . LEU A  1 118 ? 127.375 60.873  54.448 1.00   13.99 ? 117  LEU A N   1 
ATOM   859   C  CA  . LEU A  1 118 ? 126.300 59.982  54.836 1.00   14.22 ? 117  LEU A CA  1 
ATOM   860   C  C   . LEU A  1 118 ? 125.670 60.456  56.152 1.00   14.43 ? 117  LEU A C   1 
ATOM   861   O  O   . LEU A  1 118 ? 126.371 60.748  57.139 1.00   14.45 ? 117  LEU A O   1 
ATOM   862   C  CB  . LEU A  1 118 ? 126.835 58.556  54.971 1.00   14.34 ? 117  LEU A CB  1 
ATOM   863   C  CG  . LEU A  1 118 ? 125.848 57.409  55.202 1.00   14.51 ? 117  LEU A CG  1 
ATOM   864   C  CD1 . LEU A  1 118 ? 124.956 57.191  53.978 1.00   14.34 ? 117  LEU A CD1 1 
ATOM   865   C  CD2 . LEU A  1 118 ? 126.594 56.127  55.585 1.00   14.38 ? 117  LEU A CD2 1 
ATOM   866   N  N   . VAL A  1 119 ? 124.340 60.509  56.173 1.00   14.66 ? 118  VAL A N   1 
ATOM   867   C  CA  . VAL A  1 119 ? 123.584 61.017  57.312 1.00   14.79 ? 118  VAL A CA  1 
ATOM   868   C  C   . VAL A  1 119 ? 122.526 60.026  57.751 1.00   15.32 ? 118  VAL A C   1 
ATOM   869   O  O   . VAL A  1 119 ? 121.789 59.507  56.911 1.00   15.64 ? 118  VAL A O   1 
ATOM   870   C  CB  . VAL A  1 119 ? 122.881 62.330  56.921 1.00   14.69 ? 118  VAL A CB  1 
ATOM   871   C  CG1 . VAL A  1 119 ? 122.018 62.861  58.053 1.00   14.77 ? 118  VAL A CG1 1 
ATOM   872   C  CG2 . VAL A  1 119 ? 123.929 63.363  56.533 1.00   14.57 ? 118  VAL A CG2 1 
ATOM   873   N  N   . VAL A  1 120 ? 122.418 59.779  59.058 1.00   15.96 ? 119  VAL A N   1 
ATOM   874   C  CA  . VAL A  1 120 ? 121.260 59.045  59.621 1.00   16.50 ? 119  VAL A CA  1 
ATOM   875   C  C   . VAL A  1 120 ? 120.392 60.030  60.406 1.00   17.22 ? 119  VAL A C   1 
ATOM   876   O  O   . VAL A  1 120 ? 120.903 60.890  61.135 1.00   17.19 ? 119  VAL A O   1 
ATOM   877   C  CB  . VAL A  1 120 ? 121.671 57.804  60.458 1.00   16.52 ? 119  VAL A CB  1 
ATOM   878   C  CG1 . VAL A  1 120 ? 122.418 58.180  61.744 1.00   16.29 ? 119  VAL A CG1 1 
ATOM   879   C  CG2 . VAL A  1 120 ? 120.448 56.939  60.782 1.00   16.62 ? 119  VAL A CG2 1 
ATOM   880   N  N   . HIS A  1 121 ? 119.079 59.910  60.215 1.00   18.25 ? 120  HIS A N   1 
ATOM   881   C  CA  . HIS A  1 121 ? 118.110 60.895  60.658 1.00   19.31 ? 120  HIS A CA  1 
ATOM   882   C  C   . HIS A  1 121 ? 117.290 60.478  61.853 1.00   20.47 ? 120  HIS A C   1 
ATOM   883   O  O   . HIS A  1 121 ? 117.173 59.298  62.165 1.00   20.49 ? 120  HIS A O   1 
ATOM   884   C  CB  . HIS A  1 121 ? 117.141 61.213  59.511 1.00   19.79 ? 120  HIS A CB  1 
ATOM   885   C  CG  . HIS A  1 121 ? 117.654 62.231  58.544 1.00   20.00 ? 120  HIS A CG  1 
ATOM   886   N  ND1 . HIS A  1 121 ? 117.499 63.551  58.749 1.00   20.03 ? 120  HIS A ND1 1 
ATOM   887   C  CD2 . HIS A  1 121 ? 118.318 62.089  57.316 1.00   20.06 ? 120  HIS A CD2 1 
ATOM   888   C  CE1 . HIS A  1 121 ? 118.045 64.233  57.725 1.00   20.45 ? 120  HIS A CE1 1 
ATOM   889   N  NE2 . HIS A  1 121 ? 118.547 63.340  56.839 1.00   20.41 ? 120  HIS A NE2 1 
ATOM   890   N  N   . GLU A  1 122 ? 116.691 61.483  62.484 1.00   21.77 ? 121  GLU A N   1 
ATOM   891   C  CA  . GLU A  1 122 ? 115.822 61.356  63.646 1.00   23.54 ? 121  GLU A CA  1 
ATOM   892   C  C   . GLU A  1 122 ? 114.601 60.498  63.384 1.00   24.03 ? 121  GLU A C   1 
ATOM   893   O  O   . GLU A  1 122 ? 114.293 59.628  64.170 1.00   23.79 ? 121  GLU A O   1 
ATOM   894   C  CB  . GLU A  1 122 ? 115.357 62.770  64.062 1.00   24.67 ? 121  GLU A CB  1 
ATOM   895   C  CG  . GLU A  1 122 ? 114.447 62.855  65.295 1.00   25.99 ? 121  GLU A CG  1 
ATOM   896   C  CD  . GLU A  1 122 ? 113.753 64.212  65.423 1.00   27.75 ? 121  GLU A CD  1 
ATOM   897   O  OE1 . GLU A  1 122 ? 113.766 65.022  64.475 1.00   28.87 ? 121  GLU A OE1 1 
ATOM   898   O  OE2 . GLU A  1 122 ? 113.158 64.489  66.487 1.00   31.40 ? 121  GLU A OE2 1 
ATOM   899   N  N   . LYS A  1 123 ? 113.919 60.764  62.275 1.00   25.22 ? 122  LYS A N   1 
ATOM   900   C  CA  . LYS A  1 123 ? 112.630 60.141  61.940 1.00   26.83 ? 122  LYS A CA  1 
ATOM   901   C  C   . LYS A  1 123 ? 112.701 59.299  60.672 1.00   26.14 ? 122  LYS A C   1 
ATOM   902   O  O   . LYS A  1 123 ? 113.695 59.321  59.942 1.00   25.39 ? 122  LYS A O   1 
ATOM   903   C  CB  . LYS A  1 123 ? 111.574 61.220  61.661 1.00   28.95 ? 122  LYS A CB  1 
ATOM   904   C  CG  . LYS A  1 123 ? 111.299 62.218  62.762 1.00   31.74 ? 122  LYS A CG  1 
ATOM   905   C  CD  . LYS A  1 123 ? 110.443 63.350  62.199 1.00   34.45 ? 122  LYS A CD  1 
ATOM   906   C  CE  . LYS A  1 123 ? 109.958 64.283  63.294 1.00   37.29 ? 122  LYS A CE  1 
ATOM   907   N  NZ  . LYS A  1 123 ? 108.847 65.182  62.846 1.00   38.51 ? 122  LYS A NZ  1 
ATOM   908   N  N   . ALA A  1 124 ? 111.610 58.588  60.407 1.00   25.85 ? 123  ALA A N   1 
ATOM   909   C  CA  . ALA A  1 124 ? 111.430 57.871  59.150 1.00   25.66 ? 123  ALA A CA  1 
ATOM   910   C  C   . ALA A  1 124 ? 111.441 58.822  57.971 1.00   25.24 ? 123  ALA A C   1 
ATOM   911   O  O   . ALA A  1 124 ? 110.837 59.895  58.009 1.00   26.12 ? 123  ALA A O   1 
ATOM   912   C  CB  . ALA A  1 124 ? 110.123 57.092  59.149 1.00   25.80 ? 123  ALA A CB  1 
ATOM   913   N  N   . ASP A  1 125 ? 112.144 58.414  56.927 1.00   24.50 ? 124  ASP A N   1 
ATOM   914   C  CA  . ASP A  1 125 ? 111.946 58.972  55.612 1.00   24.89 ? 124  ASP A CA  1 
ATOM   915   C  C   . ASP A  1 125 ? 110.603 58.454  55.037 1.00   25.46 ? 124  ASP A C   1 
ATOM   916   O  O   . ASP A  1 125 ? 110.409 57.249  54.924 1.00   25.08 ? 124  ASP A O   1 
ATOM   917   C  CB  . ASP A  1 125 ? 113.087 58.519  54.713 1.00   24.09 ? 124  ASP A CB  1 
ATOM   918   C  CG  . ASP A  1 125 ? 113.153 59.288  53.412 1.00   24.10 ? 124  ASP A CG  1 
ATOM   919   O  OD1 . ASP A  1 125 ? 112.120 59.807  52.920 1.00   23.88 ? 124  ASP A OD1 1 
ATOM   920   O  OD2 . ASP A  1 125 ? 114.272 59.380  52.884 1.00   23.50 ? 124  ASP A OD2 1 
ATOM   921   N  N   . ASP A  1 126 ? 109.709 59.358  54.639 1.00   26.33 ? 125  ASP A N   1 
ATOM   922   C  CA  . ASP A  1 126 ? 108.427 58.941  54.063 1.00   27.76 ? 125  ASP A CA  1 
ATOM   923   C  C   . ASP A  1 126 ? 108.530 58.620  52.576 1.00   28.19 ? 125  ASP A C   1 
ATOM   924   O  O   . ASP A  1 126 ? 107.518 58.450  51.904 1.00   28.72 ? 125  ASP A O   1 
ATOM   925   C  CB  . ASP A  1 126 ? 107.312 59.970  54.316 1.00   28.27 ? 125  ASP A CB  1 
ATOM   926   C  CG  . ASP A  1 126 ? 107.546 61.285  53.608 1.00   28.96 ? 125  ASP A CG  1 
ATOM   927   O  OD1 . ASP A  1 126 ? 108.266 61.342  52.576 1.00   28.48 ? 125  ASP A OD1 1 
ATOM   928   O  OD2 . ASP A  1 126 ? 107.002 62.288  54.117 1.00   30.27 ? 125  ASP A OD2 1 
ATOM   929   N  N   . LEU A  1 127 ? 109.758 58.565  52.069 1.00   28.22 ? 126  LEU A N   1 
ATOM   930   C  CA  . LEU A  1 127 ? 110.053 58.170  50.688 1.00   27.98 ? 126  LEU A CA  1 
ATOM   931   C  C   . LEU A  1 127 ? 109.393 59.069  49.640 1.00   29.26 ? 126  LEU A C   1 
ATOM   932   O  O   . LEU A  1 127 ? 109.200 58.676  48.491 1.00   29.61 ? 126  LEU A O   1 
ATOM   933   C  CB  . LEU A  1 127 ? 109.721 56.690  50.482 1.00   27.54 ? 126  LEU A CB  1 
ATOM   934   C  CG  . LEU A  1 127 ? 110.382 55.769  51.527 1.00   26.93 ? 126  LEU A CG  1 
ATOM   935   C  CD1 . LEU A  1 127 ? 110.083 54.304  51.214 1.00   27.01 ? 126  LEU A CD1 1 
ATOM   936   C  CD2 . LEU A  1 127 ? 111.883 56.003  51.646 1.00   25.60 ? 126  LEU A CD2 1 
ATOM   937   N  N   . GLY A  1 128 ? 109.091 60.297  50.032 1.00   31.34 ? 127  GLY A N   1 
ATOM   938   C  CA  . GLY A  1 128 ? 108.506 61.268  49.118 1.00   34.50 ? 127  GLY A CA  1 
ATOM   939   C  C   . GLY A  1 128 ? 107.028 61.056  48.833 1.00   37.62 ? 127  GLY A C   1 
ATOM   940   O  O   . GLY A  1 128 ? 106.510 61.614  47.867 1.00   38.91 ? 127  GLY A O   1 
ATOM   941   N  N   . LYS A  1 129 ? 106.352 60.259  49.669 1.00   40.33 ? 128  LYS A N   1 
ATOM   942   C  CA  . LYS A  1 129 ? 104.936 59.948  49.470 1.00   42.80 ? 128  LYS A CA  1 
ATOM   943   C  C   . LYS A  1 129 ? 104.088 60.567  50.579 1.00   44.73 ? 128  LYS A C   1 
ATOM   944   O  O   . LYS A  1 129 ? 102.943 60.171  50.777 1.00   44.52 ? 128  LYS A O   1 
ATOM   945   C  CB  . LYS A  1 129 ? 104.680 58.432  49.433 1.00   44.11 ? 128  LYS A CB  1 
ATOM   946   C  CG  . LYS A  1 129 ? 105.839 57.531  49.030 1.00   44.67 ? 128  LYS A CG  1 
ATOM   947   C  CD  . LYS A  1 129 ? 106.264 57.668  47.580 1.00   46.49 ? 128  LYS A CD  1 
ATOM   948   C  CE  . LYS A  1 129 ? 107.253 56.563  47.211 1.00   45.84 ? 128  LYS A CE  1 
ATOM   949   N  NZ  . LYS A  1 129 ? 107.484 56.494  45.750 1.00   47.60 ? 128  LYS A NZ  1 
ATOM   950   N  N   . GLY A  1 130 ? 104.650 61.531  51.303 1.00   47.00 ? 129  GLY A N   1 
ATOM   951   C  CA  . GLY A  1 130 ? 103.969 62.149  52.440 1.00   48.68 ? 129  GLY A CA  1 
ATOM   952   C  C   . GLY A  1 130 ? 102.952 63.219  52.079 1.00   50.94 ? 129  GLY A C   1 
ATOM   953   O  O   . GLY A  1 130 ? 102.207 63.686  52.939 1.00   52.93 ? 129  GLY A O   1 
ATOM   954   N  N   . GLY A  1 131 ? 102.930 63.633  50.819 1.00   52.70 ? 130  GLY A N   1 
ATOM   955   C  CA  . GLY A  1 131 ? 101.889 64.545  50.342 1.00   55.09 ? 130  GLY A CA  1 
ATOM   956   C  C   . GLY A  1 131 ? 102.058 66.000  50.758 1.00   55.67 ? 130  GLY A C   1 
ATOM   957   O  O   . GLY A  1 131 ? 101.071 66.722  50.902 1.00   56.63 ? 130  GLY A O   1 
ATOM   958   N  N   . ASN A  1 132 ? 103.304 66.435  50.945 1.00   54.64 ? 131  ASN A N   1 
ATOM   959   C  CA  . ASN A  1 132 ? 103.618 67.856  51.168 1.00   53.30 ? 131  ASN A CA  1 
ATOM   960   C  C   . ASN A  1 132 ? 104.980 68.218  50.570 1.00   51.12 ? 131  ASN A C   1 
ATOM   961   O  O   . ASN A  1 132 ? 105.798 67.335  50.330 1.00   49.65 ? 131  ASN A O   1 
ATOM   962   C  CB  . ASN A  1 132 ? 103.554 68.208  52.662 1.00   52.72 ? 131  ASN A CB  1 
ATOM   963   C  CG  . ASN A  1 132 ? 104.374 67.268  53.533 1.00   52.34 ? 131  ASN A CG  1 
ATOM   964   O  OD1 . ASN A  1 132 ? 105.551 67.006  53.264 1.00   47.85 ? 131  ASN A OD1 1 
ATOM   965   N  ND2 . ASN A  1 132 ? 103.755 66.770  54.601 1.00   52.83 ? 131  ASN A ND2 1 
ATOM   966   N  N   . GLU A  1 133 ? 105.223 69.506  50.335 1.00   50.63 ? 132  GLU A N   1 
ATOM   967   C  CA  . GLU A  1 133 ? 106.439 69.949  49.624 1.00   49.77 ? 132  GLU A CA  1 
ATOM   968   C  C   . GLU A  1 133 ? 107.736 69.444  50.264 1.00   48.22 ? 132  GLU A C   1 
ATOM   969   O  O   . GLU A  1 133 ? 108.724 69.157  49.566 1.00   48.90 ? 132  GLU A O   1 
ATOM   970   C  CB  . GLU A  1 133 ? 106.476 71.479  49.516 1.00   51.66 ? 132  GLU A CB  1 
ATOM   971   C  CG  . GLU A  1 133 ? 105.544 72.034  48.445 1.00   53.96 ? 132  GLU A CG  1 
ATOM   972   C  CD  . GLU A  1 133 ? 105.287 73.528  48.585 0.50   53.84 ? 132  GLU A CD  1 
ATOM   973   O  OE1 . GLU A  1 133 ? 106.046 74.210  49.306 0.50   53.82 ? 132  GLU A OE1 1 
ATOM   974   O  OE2 . GLU A  1 133 ? 104.318 74.021  47.968 0.50   53.88 ? 132  GLU A OE2 1 
ATOM   975   N  N   . GLU A  1 134 ? 107.726 69.342  51.588 1.00   46.18 ? 133  GLU A N   1 
ATOM   976   C  CA  . GLU A  1 134 ? 108.860 68.823  52.330 1.00   44.40 ? 133  GLU A CA  1 
ATOM   977   C  C   . GLU A  1 134 ? 109.099 67.354  52.013 1.00   43.89 ? 133  GLU A C   1 
ATOM   978   O  O   . GLU A  1 134 ? 110.252 66.901  51.971 1.00   42.19 ? 133  GLU A O   1 
ATOM   979   C  CB  . GLU A  1 134 ? 108.648 69.000  53.837 1.00   44.67 ? 133  GLU A CB  1 
ATOM   980   C  CG  . GLU A  1 134 ? 109.918 68.847  54.656 1.00   44.47 ? 133  GLU A CG  1 
ATOM   981   C  CD  . GLU A  1 134 ? 111.017 69.790  54.183 1.00   46.01 ? 133  GLU A CD  1 
ATOM   982   O  OE1 . GLU A  1 134 ? 110.725 70.973  53.878 1.00   47.49 ? 133  GLU A OE1 1 
ATOM   983   O  OE2 . GLU A  1 134 ? 112.173 69.337  54.084 1.00   46.78 ? 133  GLU A OE2 1 
ATOM   984   N  N   . SER A  1 135 ? 108.020 66.605  51.791 1.00   42.78 ? 134  SER A N   1 
ATOM   985   C  CA  . SER A  1 135 ? 108.155 65.198  51.463 1.00   41.90 ? 134  SER A CA  1 
ATOM   986   C  C   . SER A  1 135 ? 109.011 65.044  50.210 1.00   42.62 ? 134  SER A C   1 
ATOM   987   O  O   . SER A  1 135 ? 109.853 64.144  50.148 1.00   40.70 ? 134  SER A O   1 
ATOM   988   C  CB  . SER A  1 135 ? 106.795 64.537  51.254 1.00   41.12 ? 134  SER A CB  1 
ATOM   989   O  OG  . SER A  1 135 ? 106.950 63.153  51.002 1.00   38.99 ? 134  SER A OG  1 
ATOM   990   N  N   . THR A  1 136 ? 108.797 65.925  49.228 1.00   44.11 ? 135  THR A N   1 
ATOM   991   C  CA  . THR A  1 136 ? 109.477 65.825  47.929 1.00   45.19 ? 135  THR A CA  1 
ATOM   992   C  C   . THR A  1 136 ? 110.858 66.495  47.941 1.00   43.93 ? 135  THR A C   1 
ATOM   993   O  O   . THR A  1 136 ? 111.574 66.442  46.939 1.00   43.92 ? 135  THR A O   1 
ATOM   994   C  CB  . THR A  1 136 ? 108.639 66.445  46.776 1.00   46.64 ? 135  THR A CB  1 
ATOM   995   O  OG1 . THR A  1 136 ? 108.512 67.856  46.978 1.00   48.99 ? 135  THR A OG1 1 
ATOM   996   C  CG2 . THR A  1 136 ? 107.264 65.840  46.695 1.00   47.35 ? 135  THR A CG2 1 
ATOM   997   N  N   . LYS A  1 137 ? 111.207 67.135  49.061 1.00   43.26 ? 136  LYS A N   1 
ATOM   998   C  CA  . LYS A  1 137 ? 112.533 67.707  49.265 1.00   43.05 ? 136  LYS A CA  1 
ATOM   999   C  C   . LYS A  1 137 ? 113.407 66.753  50.086 1.00   39.57 ? 136  LYS A C   1 
ATOM   1000  O  O   . LYS A  1 137 ? 114.508 66.369  49.658 1.00   36.44 ? 136  LYS A O   1 
ATOM   1001  C  CB  . LYS A  1 137 ? 112.442 69.071  49.974 1.00   46.80 ? 136  LYS A CB  1 
ATOM   1002  C  CG  . LYS A  1 137 ? 112.195 70.262  49.048 1.00   51.15 ? 136  LYS A CG  1 
ATOM   1003  C  CD  . LYS A  1 137 ? 111.846 71.564  49.794 1.00   53.09 ? 136  LYS A CD  1 
ATOM   1004  C  CE  . LYS A  1 137 ? 110.335 71.821  49.848 1.00   56.72 ? 136  LYS A CE  1 
ATOM   1005  N  NZ  . LYS A  1 137 ? 109.918 73.247  50.050 1.00   57.68 ? 136  LYS A NZ  1 
ATOM   1006  N  N   . THR A  1 138 ? 112.898 66.373  51.259 1.00   36.23 ? 137  THR A N   1 
ATOM   1007  C  CA  . THR A  1 138 ? 113.681 65.663  52.266 1.00   34.02 ? 137  THR A CA  1 
ATOM   1008  C  C   . THR A  1 138 ? 113.074 64.355  52.774 1.00   32.55 ? 137  THR A C   1 
ATOM   1009  O  O   . THR A  1 138 ? 113.718 63.623  53.530 1.00   31.07 ? 137  THR A O   1 
ATOM   1010  C  CB  . THR A  1 138 ? 113.872 66.552  53.509 1.00   33.76 ? 137  THR A CB  1 
ATOM   1011  O  OG1 . THR A  1 138 ? 112.595 66.823  54.103 1.00   34.28 ? 137  THR A OG1 1 
ATOM   1012  C  CG2 . THR A  1 138 ? 114.586 67.866  53.137 1.00   34.16 ? 137  THR A CG2 1 
ATOM   1013  N  N   . GLY A  1 139 ? 111.824 64.092  52.420 1.00   31.17 ? 138  GLY A N   1 
ATOM   1014  C  CA  . GLY A  1 139 ? 111.104 62.979  53.015 1.00   30.98 ? 138  GLY A CA  1 
ATOM   1015  C  C   . GLY A  1 139 ? 110.702 63.121  54.478 1.00   30.11 ? 138  GLY A C   1 
ATOM   1016  O  O   . GLY A  1 139 ? 110.338 62.132  55.096 1.00   31.21 ? 138  GLY A O   1 
ATOM   1017  N  N   . ASN A  1 140 ? 110.744 64.334  55.031 1.00   29.98 ? 139  ASN A N   1 
ATOM   1018  C  CA  . ASN A  1 140 ? 110.317 64.598  56.413 1.00   29.48 ? 139  ASN A CA  1 
ATOM   1019  C  C   . ASN A  1 140 ? 111.065 63.769  57.462 1.00   27.75 ? 139  ASN A C   1 
ATOM   1020  O  O   . ASN A  1 140 ? 110.496 63.362  58.484 1.00   27.83 ? 139  ASN A O   1 
ATOM   1021  C  CB  . ASN A  1 140 ? 108.791 64.390  56.566 1.00   31.40 ? 139  ASN A CB  1 
ATOM   1022  C  CG  . ASN A  1 140 ? 107.985 65.331  55.695 1.00   33.06 ? 139  ASN A CG  1 
ATOM   1023  O  OD1 . ASN A  1 140 ? 108.087 66.546  55.826 1.00   35.21 ? 139  ASN A OD1 1 
ATOM   1024  N  ND2 . ASN A  1 140 ? 107.187 64.774  54.791 1.00   33.94 ? 139  ASN A ND2 1 
ATOM   1025  N  N   . ALA A  1 141 ? 112.349 63.538  57.238 1.00   25.88 ? 140  ALA A N   1 
ATOM   1026  C  CA  . ALA A  1 141 ? 113.122 62.654  58.133 1.00   25.06 ? 140  ALA A CA  1 
ATOM   1027  C  C   . ALA A  1 141 ? 113.696 63.363  59.384 1.00   24.12 ? 140  ALA A C   1 
ATOM   1028  O  O   . ALA A  1 141 ? 114.395 62.748  60.181 1.00   23.40 ? 140  ALA A O   1 
ATOM   1029  C  CB  . ALA A  1 141 ? 114.219 61.932  57.353 1.00   23.95 ? 140  ALA A CB  1 
ATOM   1030  N  N   . GLY A  1 142 ? 113.370 64.638  59.569 1.00   24.14 ? 141  GLY A N   1 
ATOM   1031  C  CA  . GLY A  1 142 ? 113.748 65.361  60.768 1.00   23.90 ? 141  GLY A CA  1 
ATOM   1032  C  C   . GLY A  1 142 ? 115.246 65.579  60.889 1.00   23.75 ? 141  GLY A C   1 
ATOM   1033  O  O   . GLY A  1 142 ? 115.987 65.540  59.904 1.00   23.71 ? 141  GLY A O   1 
ATOM   1034  N  N   . SER A  1 143 ? 115.716 65.780  62.106 1.00   23.22 ? 142  SER A N   1 
ATOM   1035  C  CA  . SER A  1 143 ? 117.078 66.238  62.281 1.00   22.68 ? 142  SER A CA  1 
ATOM   1036  C  C   . SER A  1 143 ? 118.134 65.202  61.868 1.00   21.52 ? 142  SER A C   1 
ATOM   1037  O  O   . SER A  1 143 ? 117.854 64.006  61.671 1.00   21.21 ? 142  SER A O   1 
ATOM   1038  C  CB  . SER A  1 143 ? 117.287 66.696  63.724 1.00   23.35 ? 142  SER A CB  1 
ATOM   1039  O  OG  . SER A  1 143 ? 117.316 65.575  64.573 1.00   24.44 ? 142  SER A OG  1 
ATOM   1040  N  N   . ARG A  1 144 ? 119.357 65.684  61.720 1.00   20.45 ? 143  ARG A N   1 
ATOM   1041  C  CA  . ARG A  1 144 ? 120.482 64.839  61.317 1.00   19.69 ? 143  ARG A CA  1 
ATOM   1042  C  C   . ARG A  1 144 ? 121.168 64.413  62.606 1.00   19.78 ? 143  ARG A C   1 
ATOM   1043  O  O   . ARG A  1 144 ? 121.756 65.238  63.286 1.00   19.89 ? 143  ARG A O   1 
ATOM   1044  C  CB  . ARG A  1 144 ? 121.424 65.615  60.388 1.00   18.95 ? 143  ARG A CB  1 
ATOM   1045  C  CG  . ARG A  1 144 ? 120.703 66.289  59.242 1.00   18.92 ? 143  ARG A CG  1 
ATOM   1046  C  CD  . ARG A  1 144 ? 121.601 67.075  58.306 1.00   18.69 ? 143  ARG A CD  1 
ATOM   1047  N  NE  . ARG A  1 144 ? 120.793 67.679  57.254 1.00   18.34 ? 143  ARG A NE  1 
ATOM   1048  C  CZ  . ARG A  1 144 ? 121.246 68.487  56.304 1.00   18.24 ? 143  ARG A CZ  1 
ATOM   1049  N  NH1 . ARG A  1 144 ? 122.533 68.810  56.234 1.00   17.86 ? 143  ARG A NH1 1 
ATOM   1050  N  NH2 . ARG A  1 144 ? 120.404 68.963  55.405 1.00   18.34 ? 143  ARG A NH2 1 
ATOM   1051  N  N   . LEU A  1 145 ? 121.052 63.137  62.972 1.00   20.06 ? 144  LEU A N   1 
ATOM   1052  C  CA  . LEU A  1 145 ? 121.524 62.689  64.281 1.00   20.05 ? 144  LEU A CA  1 
ATOM   1053  C  C   . LEU A  1 145 ? 123.005 62.368  64.263 1.00   19.70 ? 144  LEU A C   1 
ATOM   1054  O  O   . LEU A  1 145 ? 123.708 62.581  65.258 1.00   20.13 ? 144  LEU A O   1 
ATOM   1055  C  CB  . LEU A  1 145 ? 120.751 61.469  64.741 1.00   20.64 ? 144  LEU A CB  1 
ATOM   1056  C  CG  . LEU A  1 145 ? 119.261 61.663  65.006 1.00   21.42 ? 144  LEU A CG  1 
ATOM   1057  C  CD1 . LEU A  1 145 ? 118.701 60.403  65.641 1.00   22.08 ? 144  LEU A CD1 1 
ATOM   1058  C  CD2 . LEU A  1 145 ? 119.017 62.880  65.895 1.00   21.99 ? 144  LEU A CD2 1 
ATOM   1059  N  N   . ALA A  1 146 ? 123.476 61.823  63.149 1.00   18.81 ? 145  ALA A N   1 
ATOM   1060  C  CA  . ALA A  1 146 ? 124.880 61.468  63.027 1.00   18.22 ? 145  ALA A CA  1 
ATOM   1061  C  C   . ALA A  1 146 ? 125.281 61.453  61.573 1.00   17.47 ? 145  ALA A C   1 
ATOM   1062  O  O   . ALA A  1 146 ? 124.465 61.188  60.701 1.00   17.42 ? 145  ALA A O   1 
ATOM   1063  C  CB  . ALA A  1 146 ? 125.154 60.110  63.670 1.00   18.30 ? 145  ALA A CB  1 
ATOM   1064  N  N   . CYS A  1 147 ? 126.553 61.709  61.312 1.00   16.96 ? 146  CYS A N   1 
ATOM   1065  C  CA  . CYS A  1 147 ? 127.025 61.747  59.944 1.00   16.41 ? 146  CYS A CA  1 
ATOM   1066  C  C   . CYS A  1 147 ? 128.503 61.583  59.841 1.00   15.67 ? 146  CYS A C   1 
ATOM   1067  O  O   . CYS A  1 147 ? 129.212 61.620  60.822 1.00   15.26 ? 146  CYS A O   1 
ATOM   1068  C  CB  . CYS A  1 147 ? 126.627 63.062  59.269 1.00   16.63 ? 146  CYS A CB  1 
ATOM   1069  S  SG  . CYS A  1 147 ? 127.294 64.532  60.066 1.00   17.62 ? 146  CYS A SG  1 
ATOM   1070  N  N   . GLY A  1 148 ? 128.964 61.407  58.609 1.00   15.17 ? 147  GLY A N   1 
ATOM   1071  C  CA  . GLY A  1 148 ? 130.391 61.322  58.343 1.00   14.73 ? 147  GLY A CA  1 
ATOM   1072  C  C   . GLY A  1 148 ? 130.698 61.416  56.863 1.00   14.17 ? 147  GLY A C   1 
ATOM   1073  O  O   . GLY A  1 148 ? 129.813 61.213  56.001 1.00   14.10 ? 147  GLY A O   1 
ATOM   1074  N  N   . VAL A  1 149 ? 131.942 61.755  56.566 1.00   13.75 ? 148  VAL A N   1 
ATOM   1075  C  CA  . VAL A  1 149 ? 132.403 61.849  55.186 1.00   13.55 ? 148  VAL A CA  1 
ATOM   1076  C  C   . VAL A  1 149 ? 132.801 60.451  54.711 1.00   13.51 ? 148  VAL A C   1 
ATOM   1077  O  O   . VAL A  1 149 ? 133.514 59.728  55.401 1.00   13.86 ? 148  VAL A O   1 
ATOM   1078  C  CB  . VAL A  1 149 ? 133.583 62.837  55.031 1.00   13.43 ? 148  VAL A CB  1 
ATOM   1079  C  CG1 . VAL A  1 149 ? 133.995 62.988  53.557 1.00   13.15 ? 148  VAL A CG1 1 
ATOM   1080  C  CG2 . VAL A  1 149 ? 133.218 64.197  55.655 1.00   13.38 ? 148  VAL A CG2 1 
ATOM   1081  N  N   . ILE A  1 150 ? 132.309 60.080  53.543 1.00   13.58 ? 149  ILE A N   1 
ATOM   1082  C  CA  . ILE A  1 150 ? 132.582 58.785  52.907 1.00   13.70 ? 149  ILE A CA  1 
ATOM   1083  C  C   . ILE A  1 150 ? 133.976 58.801  52.299 1.00   13.85 ? 149  ILE A C   1 
ATOM   1084  O  O   . ILE A  1 150 ? 134.286 59.659  51.461 1.00   13.80 ? 149  ILE A O   1 
ATOM   1085  C  CB  . ILE A  1 150 ? 131.534 58.494  51.808 1.00   13.77 ? 149  ILE A CB  1 
ATOM   1086  C  CG1 . ILE A  1 150 ? 130.111 58.459  52.415 1.00   13.73 ? 149  ILE A CG1 1 
ATOM   1087  C  CG2 . ILE A  1 150 ? 131.835 57.169  51.101 1.00   13.81 ? 149  ILE A CG2 1 
ATOM   1088  C  CD1 . ILE A  1 150 ? 128.959 58.607  51.411 1.00   13.79 ? 149  ILE A CD1 1 
ATOM   1089  N  N   . GLY A  1 151 ? 134.836 57.897  52.772 1.00   14.14 ? 150  GLY A N   1 
ATOM   1090  C  CA  . GLY A  1 151 ? 136.224 57.849  52.369 1.00   14.53 ? 150  GLY A CA  1 
ATOM   1091  C  C   . GLY A  1 151 ? 136.598 56.585  51.600 1.00   15.11 ? 150  GLY A C   1 
ATOM   1092  O  O   . GLY A  1 151 ? 135.953 55.542  51.744 1.00   15.07 ? 150  GLY A O   1 
ATOM   1093  N  N   . ILE A  1 152 ? 137.635 56.701  50.769 1.00   15.59 ? 151  ILE A N   1 
ATOM   1094  C  CA  . ILE A  1 152 ? 138.228 55.559  50.105 1.00   16.37 ? 151  ILE A CA  1 
ATOM   1095  C  C   . ILE A  1 152 ? 138.811 54.585  51.156 1.00   17.10 ? 151  ILE A C   1 
ATOM   1096  O  O   . ILE A  1 152 ? 139.505 55.010  52.074 1.00   16.84 ? 151  ILE A O   1 
ATOM   1097  C  CB  . ILE A  1 152 ? 139.359 56.004  49.142 1.00   16.57 ? 151  ILE A CB  1 
ATOM   1098  C  CG1 . ILE A  1 152 ? 138.795 56.901  48.042 1.00   16.61 ? 151  ILE A CG1 1 
ATOM   1099  C  CG2 . ILE A  1 152 ? 140.000 54.785  48.486 1.00   16.90 ? 151  ILE A CG2 1 
ATOM   1100  C  CD1 . ILE A  1 152 ? 139.846 57.713  47.291 1.00   16.67 ? 151  ILE A CD1 1 
ATOM   1101  N  N   . ALA A  1 153 ? 138.489 53.297  51.032 1.00   18.04 ? 152  ALA A N   1 
ATOM   1102  C  CA  . ALA A  1 153 ? 138.979 52.245  51.951 1.00   19.33 ? 152  ALA A CA  1 
ATOM   1103  C  C   . ALA A  1 153 ? 139.868 51.221  51.219 1.00   20.63 ? 152  ALA A C   1 
ATOM   1104  O  O   . ALA A  1 153 ? 139.794 51.077  50.019 1.00   20.72 ? 152  ALA A O   1 
ATOM   1105  C  CB  . ALA A  1 153 ? 137.808 51.510  52.599 1.00   18.92 ? 152  ALA A CB  1 
ATOM   1106  N  N   . GLN A  1 154 ? 140.697 50.520  51.973 1.00   22.78 ? 153  GLN A N   1 
ATOM   1107  C  CA  . GLN A  1 154 ? 141.601 49.531  51.421 1.00   24.86 ? 153  GLN A CA  1 
ATOM   1108  C  C   . GLN A  1 154 ? 140.817 48.272  51.112 1.00   26.28 ? 153  GLN A C   1 
ATOM   1109  O  O   . GLN A  1 154 ? 140.026 47.798  51.937 1.00   27.00 ? 153  GLN A O   1 
ATOM   1110  C  CB  . GLN A  1 154 ? 142.710 49.186  52.414 1.00   26.17 ? 153  GLN A CB  1 
ATOM   1111  C  CG  . GLN A  1 154 ? 143.808 48.310  51.816 1.00   27.93 ? 153  GLN A CG  1 
ATOM   1112  C  CD  . GLN A  1 154 ? 144.919 48.011  52.808 1.00   29.89 ? 153  GLN A CD  1 
ATOM   1113  O  OE1 . GLN A  1 154 ? 144.661 47.672  53.959 1.00   32.22 ? 153  GLN A OE1 1 
ATOM   1114  N  NE2 . GLN A  1 154 ? 146.157 48.130  52.367 1.00   31.26 ? 153  GLN A NE2 1 
ATOM   1115  O  OXT . GLN A  1 154 ? 141.008 47.714  50.038 1.00   28.15 ? 153  GLN A OXT 1 
ATOM   1116  N  N   . ALA B  1 2   ? 156.242 110.369 42.928 1.00   47.77 ? 1    ALA B N   1 
ATOM   1117  C  CA  . ALA B  1 2   ? 157.285 111.095 43.727 1.00   47.31 ? 1    ALA B CA  1 
ATOM   1118  C  C   . ALA B  1 2   ? 158.288 110.123 44.382 1.00   43.66 ? 1    ALA B C   1 
ATOM   1119  O  O   . ALA B  1 2   ? 157.873 109.205 45.082 1.00   43.13 ? 1    ALA B O   1 
ATOM   1120  C  CB  . ALA B  1 2   ? 156.611 111.958 44.799 1.00   48.00 ? 1    ALA B CB  1 
ATOM   1121  N  N   . THR B  1 3   ? 159.589 110.318 44.158 1.00   40.89 ? 2    THR B N   1 
ATOM   1122  C  CA  . THR B  1 3   ? 160.587 109.575 44.928 1.00   38.88 ? 2    THR B CA  1 
ATOM   1123  C  C   . THR B  1 3   ? 160.771 110.328 46.254 1.00   37.02 ? 2    THR B C   1 
ATOM   1124  O  O   . THR B  1 3   ? 160.761 111.571 46.304 1.00   36.17 ? 2    THR B O   1 
ATOM   1125  C  CB  . THR B  1 3   ? 161.939 109.364 44.185 1.00   38.94 ? 2    THR B CB  1 
ATOM   1126  O  OG1 . THR B  1 3   ? 161.729 109.303 42.776 1.00   43.77 ? 2    THR B OG1 1 
ATOM   1127  C  CG2 . THR B  1 3   ? 162.584 108.055 44.592 1.00   39.97 ? 2    THR B CG2 1 
ATOM   1128  N  N   . LYS B  1 4   ? 160.901 109.562 47.326 1.00   33.60 ? 3    LYS B N   1 
ATOM   1129  C  CA  . LYS B  1 4   ? 161.090 110.108 48.644 1.00   32.38 ? 3    LYS B CA  1 
ATOM   1130  C  C   . LYS B  1 4   ? 162.302 109.473 49.290 1.00   29.03 ? 3    LYS B C   1 
ATOM   1131  O  O   . LYS B  1 4   ? 162.597 108.310 49.078 1.00   26.82 ? 3    LYS B O   1 
ATOM   1132  C  CB  . LYS B  1 4   ? 159.860 109.894 49.516 1.00   34.78 ? 3    LYS B CB  1 
ATOM   1133  C  CG  . LYS B  1 4   ? 158.559 110.301 48.860 1.00   37.93 ? 3    LYS B CG  1 
ATOM   1134  C  CD  . LYS B  1 4   ? 157.476 110.625 49.879 1.00   40.34 ? 3    LYS B CD  1 
ATOM   1135  C  CE  . LYS B  1 4   ? 156.097 110.560 49.219 1.00   43.76 ? 3    LYS B CE  1 
ATOM   1136  N  NZ  . LYS B  1 4   ? 155.053 111.365 49.920 1.00   45.48 ? 3    LYS B NZ  1 
ATOM   1137  N  N   . ALA B  1 5   ? 163.025 110.268 50.050 1.00   26.73 ? 4    ALA B N   1 
ATOM   1138  C  CA  . ALA B  1 5   ? 164.175 109.773 50.772 1.00   25.96 ? 4    ALA B CA  1 
ATOM   1139  C  C   . ALA B  1 5   ? 164.129 110.310 52.202 1.00   25.34 ? 4    ALA B C   1 
ATOM   1140  O  O   . ALA B  1 5   ? 163.375 111.270 52.518 1.00   25.44 ? 4    ALA B O   1 
ATOM   1141  C  CB  . ALA B  1 5   ? 165.461 110.177 50.067 1.00   24.72 ? 4    ALA B CB  1 
ATOM   1142  N  N   . VAL B  1 6   ? 164.928 109.696 53.063 1.00   23.97 ? 5    VAL B N   1 
ATOM   1143  C  CA  . VAL B  1 6   ? 165.030 110.151 54.440 1.00   23.96 ? 5    VAL B CA  1 
ATOM   1144  C  C   . VAL B  1 6   ? 166.429 109.903 54.962 1.00   23.78 ? 5    VAL B C   1 
ATOM   1145  O  O   . VAL B  1 6   ? 167.167 109.087 54.420 1.00   24.05 ? 5    VAL B O   1 
ATOM   1146  C  CB  . VAL B  1 6   ? 163.956 109.466 55.319 1.00   24.01 ? 5    VAL B CB  1 
ATOM   1147  C  CG1 . VAL B  1 6   ? 164.239 107.980 55.470 1.00   23.09 ? 5    VAL B CG1 1 
ATOM   1148  C  CG2 . VAL B  1 6   ? 163.807 110.159 56.664 1.00   23.87 ? 5    VAL B CG2 1 
ATOM   1149  N  N   . CYS B  1 7   ? 166.803 110.634 55.997 1.00   23.38 ? 6    CYS B N   1 
ATOM   1150  C  CA  . CYS B  1 7   ? 168.085 110.452 56.629 1.00   23.30 ? 6    CYS B CA  1 
ATOM   1151  C  C   . CYS B  1 7   ? 167.952 110.722 58.126 1.00   24.31 ? 6    CYS B C   1 
ATOM   1152  O  O   . CYS B  1 7   ? 167.343 111.740 58.551 1.00   24.35 ? 6    CYS B O   1 
ATOM   1153  C  CB  . CYS B  1 7   ? 169.119 111.379 55.992 1.00   23.45 ? 6    CYS B CB  1 
ATOM   1154  S  SG  . CYS B  1 7   ? 170.782 111.290 56.696 1.00   23.28 ? 6    CYS B SG  1 
ATOM   1155  N  N   . VAL B  1 8   ? 168.502 109.809 58.923 1.00   23.79 ? 7    VAL B N   1 
ATOM   1156  C  CA  . VAL B  1 8   ? 168.565 109.988 60.364 1.00   24.06 ? 7    VAL B CA  1 
ATOM   1157  C  C   . VAL B  1 8   ? 169.985 110.397 60.731 1.00   24.36 ? 7    VAL B C   1 
ATOM   1158  O  O   . VAL B  1 8   ? 170.913 109.637 60.533 1.00   23.92 ? 7    VAL B O   1 
ATOM   1159  C  CB  . VAL B  1 8   ? 168.091 108.724 61.118 1.00   23.89 ? 7    VAL B CB  1 
ATOM   1160  C  CG1 . VAL B  1 8   ? 168.209 108.902 62.631 1.00   24.20 ? 7    VAL B CG1 1 
ATOM   1161  C  CG2 . VAL B  1 8   ? 166.639 108.442 60.768 1.00   24.01 ? 7    VAL B CG2 1 
ATOM   1162  N  N   . LEU B  1 9   ? 170.139 111.626 61.233 1.00   25.14 ? 8    LEU B N   1 
ATOM   1163  C  CA  . LEU B  1 9   ? 171.435 112.160 61.634 1.00   25.94 ? 8    LEU B CA  1 
ATOM   1164  C  C   . LEU B  1 9   ? 171.728 111.840 63.108 1.00   25.80 ? 8    LEU B C   1 
ATOM   1165  O  O   . LEU B  1 9   ? 170.901 112.112 64.001 1.00   25.40 ? 8    LEU B O   1 
ATOM   1166  C  CB  . LEU B  1 9   ? 171.462 113.685 61.449 1.00   27.14 ? 8    LEU B CB  1 
ATOM   1167  C  CG  . LEU B  1 9   ? 171.180 114.279 60.062 1.00   27.97 ? 8    LEU B CG  1 
ATOM   1168  C  CD1 . LEU B  1 9   ? 170.851 115.758 60.227 1.00   28.76 ? 8    LEU B CD1 1 
ATOM   1169  C  CD2 . LEU B  1 9   ? 172.398 114.125 59.167 1.00   27.65 ? 8    LEU B CD2 1 
ATOM   1170  N  N   . LYS B  1 10  ? 172.908 111.281 63.346 1.00   25.55 ? 9    LYS B N   1 
ATOM   1171  C  CA  . LYS B  1 10  ? 173.374 110.925 64.682 1.00   26.83 ? 9    LYS B CA  1 
ATOM   1172  C  C   . LYS B  1 10  ? 174.850 111.177 64.720 1.00   26.21 ? 9    LYS B C   1 
ATOM   1173  O  O   . LYS B  1 10  ? 175.498 111.138 63.690 1.00   24.98 ? 9    LYS B O   1 
ATOM   1174  C  CB  . LYS B  1 10  ? 173.153 109.439 64.980 1.00   28.28 ? 9    LYS B CB  1 
ATOM   1175  C  CG  . LYS B  1 10  ? 171.707 109.016 65.097 1.00   30.82 ? 9    LYS B CG  1 
ATOM   1176  C  CD  . LYS B  1 10  ? 171.622 107.560 65.570 1.00   32.24 ? 9    LYS B CD  1 
ATOM   1177  C  CE  . LYS B  1 10  ? 170.210 106.995 65.460 1.00   33.74 ? 9    LYS B CE  1 
ATOM   1178  N  NZ  . LYS B  1 10  ? 169.228 107.789 66.263 1.00   37.33 ? 9    LYS B NZ  1 
ATOM   1179  N  N   . GLY B  1 11  ? 175.380 111.418 65.917 1.00   27.05 ? 10   GLY B N   1 
ATOM   1180  C  CA  . GLY B  1 11  ? 176.823 111.546 66.131 1.00   27.58 ? 10   GLY B CA  1 
ATOM   1181  C  C   . GLY B  1 11  ? 177.199 111.076 67.530 1.00   28.84 ? 10   GLY B C   1 
ATOM   1182  O  O   . GLY B  1 11  ? 176.410 110.405 68.200 1.00   27.85 ? 10   GLY B O   1 
ATOM   1183  N  N   . ASP B  1 12  ? 178.401 111.429 67.973 1.00   30.62 ? 11   ASP B N   1 
ATOM   1184  C  CA  . ASP B  1 12  ? 178.833 111.096 69.331 1.00   33.09 ? 11   ASP B CA  1 
ATOM   1185  C  C   . ASP B  1 12  ? 178.343 112.112 70.381 1.00   32.01 ? 11   ASP B C   1 
ATOM   1186  O  O   . ASP B  1 12  ? 178.252 111.790 71.568 1.00   31.91 ? 11   ASP B O   1 
ATOM   1187  C  CB  . ASP B  1 12  ? 180.358 110.939 69.381 1.00   36.76 ? 11   ASP B CB  1 
ATOM   1188  C  CG  . ASP B  1 12  ? 180.854 109.807 68.473 1.00   40.31 ? 11   ASP B CG  1 
ATOM   1189  O  OD1 . ASP B  1 12  ? 180.318 108.666 68.570 1.00   41.84 ? 11   ASP B OD1 1 
ATOM   1190  O  OD2 . ASP B  1 12  ? 181.758 110.066 67.636 1.00   44.27 ? 11   ASP B OD2 1 
ATOM   1191  N  N   . GLY B  1 13  ? 178.008 113.321 69.939 1.00   29.86 ? 12   GLY B N   1 
ATOM   1192  C  CA  . GLY B  1 13  ? 177.483 114.346 70.818 1.00   29.76 ? 12   GLY B CA  1 
ATOM   1193  C  C   . GLY B  1 13  ? 175.966 114.428 70.750 1.00   28.77 ? 12   GLY B C   1 
ATOM   1194  O  O   . GLY B  1 13  ? 175.322 113.487 70.330 1.00   27.28 ? 12   GLY B O   1 
ATOM   1195  N  N   . PRO B  1 14  ? 175.393 115.586 71.126 1.00   29.15 ? 13   PRO B N   1 
ATOM   1196  C  CA  . PRO B  1 14  ? 173.940 115.739 71.243 1.00   29.28 ? 13   PRO B CA  1 
ATOM   1197  C  C   . PRO B  1 14  ? 173.175 116.019 69.939 1.00   29.13 ? 13   PRO B C   1 
ATOM   1198  O  O   . PRO B  1 14  ? 171.938 116.089 69.963 1.00   28.49 ? 13   PRO B O   1 
ATOM   1199  C  CB  . PRO B  1 14  ? 173.812 116.942 72.172 1.00   30.20 ? 13   PRO B CB  1 
ATOM   1200  C  CG  . PRO B  1 14  ? 175.023 117.770 71.870 1.00   30.60 ? 13   PRO B CG  1 
ATOM   1201  C  CD  . PRO B  1 14  ? 176.114 116.793 71.570 1.00   29.84 ? 13   PRO B CD  1 
ATOM   1202  N  N   . VAL B  1 15  ? 173.897 116.183 68.829 1.00   29.30 ? 14   VAL B N   1 
ATOM   1203  C  CA  . VAL B  1 15  ? 173.282 116.565 67.552 1.00   29.67 ? 14   VAL B CA  1 
ATOM   1204  C  C   . VAL B  1 15  ? 172.518 115.403 66.931 1.00   29.44 ? 14   VAL B C   1 
ATOM   1205  O  O   . VAL B  1 15  ? 173.089 114.352 66.629 1.00   28.69 ? 14   VAL B O   1 
ATOM   1206  C  CB  . VAL B  1 15  ? 174.316 117.108 66.534 1.00   29.96 ? 14   VAL B CB  1 
ATOM   1207  C  CG1 . VAL B  1 15  ? 173.613 117.561 65.257 1.00   29.39 ? 14   VAL B CG1 1 
ATOM   1208  C  CG2 . VAL B  1 15  ? 175.114 118.259 67.146 1.00   30.90 ? 14   VAL B CG2 1 
ATOM   1209  N  N   . GLN B  1 16  ? 171.215 115.586 66.759 1.00   29.87 ? 15   GLN B N   1 
ATOM   1210  C  CA  . GLN B  1 16  ? 170.407 114.579 66.131 1.00   30.07 ? 15   GLN B CA  1 
ATOM   1211  C  C   . GLN B  1 16  ? 169.294 115.223 65.354 1.00   30.27 ? 15   GLN B C   1 
ATOM   1212  O  O   . GLN B  1 16  ? 168.896 116.377 65.638 1.00   29.61 ? 15   GLN B O   1 
ATOM   1213  C  CB  . GLN B  1 16  ? 169.869 113.546 67.132 1.00   31.91 ? 15   GLN B CB  1 
ATOM   1214  C  CG  . GLN B  1 16  ? 169.147 114.090 68.343 1.00   34.60 ? 15   GLN B CG  1 
ATOM   1215  C  CD  . GLN B  1 16  ? 169.149 113.123 69.518 1.00   34.51 ? 15   GLN B CD  1 
ATOM   1216  O  OE1 . GLN B  1 16  ? 168.913 111.936 69.367 1.00   34.08 ? 15   GLN B OE1 1 
ATOM   1217  N  NE2 . GLN B  1 16  ? 169.370 113.653 70.704 1.00   37.86 ? 15   GLN B NE2 1 
ATOM   1218  N  N   . GLY B  1 17  ? 168.826 114.494 64.342 1.00   27.95 ? 16   GLY B N   1 
ATOM   1219  C  CA  . GLY B  1 17  ? 167.718 114.960 63.540 1.00   28.04 ? 16   GLY B CA  1 
ATOM   1220  C  C   . GLY B  1 17  ? 167.257 113.979 62.479 1.00   27.69 ? 16   GLY B C   1 
ATOM   1221  O  O   . GLY B  1 17  ? 167.777 112.855 62.359 1.00   25.98 ? 16   GLY B O   1 
ATOM   1222  N  N   . ILE B  1 18  ? 166.253 114.425 61.734 1.00   27.55 ? 17   ILE B N   1 
ATOM   1223  C  CA  . ILE B  1 18  ? 165.631 113.662 60.686 1.00   27.25 ? 17   ILE B CA  1 
ATOM   1224  C  C   . ILE B  1 18  ? 165.406 114.627 59.528 1.00   28.30 ? 17   ILE B C   1 
ATOM   1225  O  O   . ILE B  1 18  ? 164.796 115.701 59.707 1.00   27.99 ? 17   ILE B O   1 
ATOM   1226  C  CB  . ILE B  1 18  ? 164.278 113.097 61.114 1.00   27.73 ? 17   ILE B CB  1 
ATOM   1227  C  CG1 . ILE B  1 18  ? 164.427 112.153 62.321 1.00   27.47 ? 17   ILE B CG1 1 
ATOM   1228  C  CG2 . ILE B  1 18  ? 163.647 112.352 59.948 1.00   27.07 ? 17   ILE B CG2 1 
ATOM   1229  C  CD1 . ILE B  1 18  ? 163.108 111.539 62.756 1.00   27.58 ? 17   ILE B CD1 1 
ATOM   1230  N  N   . ILE B  1 19  ? 165.938 114.274 58.357 1.00   26.97 ? 18   ILE B N   1 
ATOM   1231  C  CA  . ILE B  1 19  ? 165.814 115.110 57.178 1.00   27.07 ? 18   ILE B CA  1 
ATOM   1232  C  C   . ILE B  1 19  ? 165.105 114.277 56.110 1.00   27.32 ? 18   ILE B C   1 
ATOM   1233  O  O   . ILE B  1 19  ? 165.452 113.107 55.897 1.00   26.01 ? 18   ILE B O   1 
ATOM   1234  C  CB  . ILE B  1 19  ? 167.199 115.605 56.710 1.00   26.92 ? 18   ILE B CB  1 
ATOM   1235  C  CG1 . ILE B  1 19  ? 167.804 116.561 57.750 1.00   27.65 ? 18   ILE B CG1 1 
ATOM   1236  C  CG2 . ILE B  1 19  ? 167.122 116.279 55.341 1.00   26.84 ? 18   ILE B CG2 1 
ATOM   1237  C  CD1 . ILE B  1 19  ? 166.993 117.815 57.988 1.00   27.42 ? 18   ILE B CD1 1 
ATOM   1238  N  N   . ASN B  1 20  ? 164.074 114.881 55.510 1.00   27.99 ? 19   ASN B N   1 
ATOM   1239  C  CA  . ASN B  1 20  ? 163.247 114.293 54.468 1.00   28.09 ? 19   ASN B CA  1 
ATOM   1240  C  C   . ASN B  1 20  ? 163.607 114.885 53.105 1.00   28.17 ? 19   ASN B C   1 
ATOM   1241  O  O   . ASN B  1 20  ? 164.055 116.034 53.026 1.00   29.74 ? 19   ASN B O   1 
ATOM   1242  C  CB  . ASN B  1 20  ? 161.764 114.583 54.739 1.00   28.92 ? 19   ASN B CB  1 
ATOM   1243  C  CG  . ASN B  1 20  ? 161.296 114.083 56.103 1.00   30.05 ? 19   ASN B CG  1 
ATOM   1244  O  OD1 . ASN B  1 20  ? 161.037 114.885 57.022 1.00   31.70 ? 19   ASN B OD1 1 
ATOM   1245  N  ND2 . ASN B  1 20  ? 161.162 112.780 56.242 1.00   27.83 ? 19   ASN B ND2 1 
ATOM   1246  N  N   . PHE B  1 21  ? 163.407 114.104 52.043 1.00   28.03 ? 20   PHE B N   1 
ATOM   1247  C  CA  . PHE B  1 21  ? 163.637 114.536 50.666 1.00   28.85 ? 20   PHE B CA  1 
ATOM   1248  C  C   . PHE B  1 21  ? 162.462 114.089 49.815 1.00   30.21 ? 20   PHE B C   1 
ATOM   1249  O  O   . PHE B  1 21  ? 162.002 112.943 49.935 1.00   29.43 ? 20   PHE B O   1 
ATOM   1250  C  CB  . PHE B  1 21  ? 164.898 113.931 50.052 1.00   28.13 ? 20   PHE B CB  1 
ATOM   1251  C  CG  . PHE B  1 21  ? 166.152 114.152 50.848 1.00   27.77 ? 20   PHE B CG  1 
ATOM   1252  C  CD1 . PHE B  1 21  ? 166.369 113.471 52.040 1.00   27.57 ? 20   PHE B CD1 1 
ATOM   1253  C  CD2 . PHE B  1 21  ? 167.140 114.992 50.383 1.00   27.83 ? 20   PHE B CD2 1 
ATOM   1254  C  CE1 . PHE B  1 21  ? 167.540 113.660 52.766 1.00   27.23 ? 20   PHE B CE1 1 
ATOM   1255  C  CE2 . PHE B  1 21  ? 168.300 115.201 51.118 1.00   27.97 ? 20   PHE B CE2 1 
ATOM   1256  C  CZ  . PHE B  1 21  ? 168.507 114.522 52.300 1.00   27.22 ? 20   PHE B CZ  1 
ATOM   1257  N  N   . GLU B  1 22  ? 161.972 114.992 48.964 1.00   31.97 ? 21   GLU B N   1 
ATOM   1258  C  CA  . GLU B  1 22  ? 160.929 114.656 47.998 1.00   33.37 ? 21   GLU B CA  1 
ATOM   1259  C  C   . GLU B  1 22  ? 161.241 115.270 46.632 1.00   33.51 ? 21   GLU B C   1 
ATOM   1260  O  O   . GLU B  1 22  ? 161.576 116.450 46.534 1.00   32.80 ? 21   GLU B O   1 
ATOM   1261  C  CB  . GLU B  1 22  ? 159.551 115.107 48.486 1.00   35.72 ? 21   GLU B CB  1 
ATOM   1262  C  CG  . GLU B  1 22  ? 158.421 114.704 47.539 1.00   37.12 ? 21   GLU B CG  1 
ATOM   1263  C  CD  . GLU B  1 22  ? 157.099 115.346 47.888 0.60   39.37 ? 21   GLU B CD  1 
ATOM   1264  O  OE1 . GLU B  1 22  ? 156.558 115.008 48.962 0.60   40.31 ? 21   GLU B OE1 1 
ATOM   1265  O  OE2 . GLU B  1 22  ? 156.616 116.197 47.097 0.60   40.05 ? 21   GLU B OE2 1 
ATOM   1266  N  N   . GLN B  1 23  ? 161.124 114.446 45.588 1.00   33.61 ? 22   GLN B N   1 
ATOM   1267  C  CA  . GLN B  1 23  ? 161.329 114.858 44.202 1.00   33.74 ? 22   GLN B CA  1 
ATOM   1268  C  C   . GLN B  1 23  ? 160.185 114.292 43.350 1.00   36.28 ? 22   GLN B C   1 
ATOM   1269  O  O   . GLN B  1 23  ? 160.131 113.083 43.091 1.00   34.31 ? 22   GLN B O   1 
ATOM   1270  C  CB  . GLN B  1 23  ? 162.680 114.351 43.711 1.00   32.35 ? 22   GLN B CB  1 
ATOM   1271  C  CG  . GLN B  1 23  ? 163.147 114.942 42.400 1.00   32.59 ? 22   GLN B CG  1 
ATOM   1272  C  CD  . GLN B  1 23  ? 164.455 114.356 41.896 1.00   31.77 ? 22   GLN B CD  1 
ATOM   1273  O  OE1 . GLN B  1 23  ? 164.840 113.231 42.253 1.00   31.30 ? 22   GLN B OE1 1 
ATOM   1274  N  NE2 . GLN B  1 23  ? 165.146 115.114 41.050 1.00   31.25 ? 22   GLN B NE2 1 
ATOM   1275  N  N   . LYS B  1 24  ? 159.263 115.171 42.945 1.00   38.97 ? 23   LYS B N   1 
ATOM   1276  C  CA  . LYS B  1 24  ? 158.046 114.764 42.247 1.00   41.55 ? 23   LYS B CA  1 
ATOM   1277  C  C   . LYS B  1 24  ? 158.366 114.251 40.856 1.00   41.57 ? 23   LYS B C   1 
ATOM   1278  O  O   . LYS B  1 24  ? 157.738 113.323 40.382 1.00   39.58 ? 23   LYS B O   1 
ATOM   1279  C  CB  . LYS B  1 24  ? 157.068 115.937 42.109 1.00   45.97 ? 23   LYS B CB  1 
ATOM   1280  C  CG  . LYS B  1 24  ? 156.417 116.398 43.409 1.00   48.66 ? 23   LYS B CG  1 
ATOM   1281  C  CD  . LYS B  1 24  ? 155.449 117.577 43.189 1.00   51.38 ? 23   LYS B CD  1 
ATOM   1282  C  CE  . LYS B  1 24  ? 154.055 117.127 42.735 1.00   52.79 ? 23   LYS B CE  1 
ATOM   1283  N  NZ  . LYS B  1 24  ? 153.021 118.201 42.882 1.00   54.82 ? 23   LYS B NZ  1 
ATOM   1284  N  N   . GLU B  1 25  ? 159.340 114.875 40.205 1.00   41.53 ? 24   GLU B N   1 
ATOM   1285  C  CA  . GLU B  1 25  ? 159.702 114.533 38.846 1.00   42.43 ? 24   GLU B CA  1 
ATOM   1286  C  C   . GLU B  1 25  ? 161.213 114.321 38.744 1.00   39.44 ? 24   GLU B C   1 
ATOM   1287  O  O   . GLU B  1 25  ? 161.986 115.065 39.340 1.00   37.31 ? 24   GLU B O   1 
ATOM   1288  C  CB  . GLU B  1 25  ? 159.248 115.675 37.922 1.00   47.91 ? 24   GLU B CB  1 
ATOM   1289  C  CG  . GLU B  1 25  ? 157.736 115.929 37.945 1.00   50.31 ? 24   GLU B CG  1 
ATOM   1290  C  CD  . GLU B  1 25  ? 157.363 117.370 37.649 1.00   54.96 ? 24   GLU B CD  1 
ATOM   1291  O  OE1 . GLU B  1 25  ? 158.261 118.176 37.292 1.00   56.68 ? 24   GLU B OE1 1 
ATOM   1292  O  OE2 . GLU B  1 25  ? 156.154 117.697 37.764 1.00   59.34 ? 24   GLU B OE2 1 
ATOM   1293  N  N   . SER B  1 26  ? 161.630 113.318 37.970 1.00   37.93 ? 25   SER B N   1 
ATOM   1294  C  CA  . SER B  1 26  ? 163.042 112.934 37.878 1.00   37.25 ? 25   SER B CA  1 
ATOM   1295  C  C   . SER B  1 26  ? 163.948 114.060 37.389 1.00   37.11 ? 25   SER B C   1 
ATOM   1296  O  O   . SER B  1 26  ? 165.127 114.117 37.755 1.00   36.83 ? 25   SER B O   1 
ATOM   1297  C  CB  . SER B  1 26  ? 163.222 111.682 36.985 1.00   37.92 ? 25   SER B CB  1 
ATOM   1298  O  OG  . SER B  1 26  ? 162.944 111.940 35.611 1.00   38.37 ? 25   SER B OG  1 
ATOM   1299  N  N   . ASN B  1 27  ? 163.404 114.942 36.554 1.00   38.00 ? 26   ASN B N   1 
ATOM   1300  C  CA  . ASN B  1 27  ? 164.148 116.093 36.053 1.00   39.15 ? 26   ASN B CA  1 
ATOM   1301  C  C   . ASN B  1 27  ? 163.787 117.394 36.778 1.00   39.95 ? 26   ASN B C   1 
ATOM   1302  O  O   . ASN B  1 27  ? 164.105 118.482 36.293 1.00   40.53 ? 26   ASN B O   1 
ATOM   1303  C  CB  . ASN B  1 27  ? 164.015 116.232 34.517 1.00   39.41 ? 26   ASN B CB  1 
ATOM   1304  C  CG  . ASN B  1 27  ? 162.592 116.537 34.062 1.00   40.13 ? 26   ASN B CG  1 
ATOM   1305  O  OD1 . ASN B  1 27  ? 161.623 115.996 34.613 1.00   38.84 ? 26   ASN B OD1 1 
ATOM   1306  N  ND2 . ASN B  1 27  ? 162.461 117.394 33.033 1.00   39.37 ? 26   ASN B ND2 1 
ATOM   1307  N  N   . GLY B  1 28  ? 163.149 117.260 37.948 1.00   39.33 ? 27   GLY B N   1 
ATOM   1308  C  CA  . GLY B  1 28  ? 162.715 118.407 38.761 1.00   38.81 ? 27   GLY B CA  1 
ATOM   1309  C  C   . GLY B  1 28  ? 163.536 118.581 40.022 1.00   37.85 ? 27   GLY B C   1 
ATOM   1310  O  O   . GLY B  1 28  ? 164.497 117.843 40.256 1.00   37.93 ? 27   GLY B O   1 
ATOM   1311  N  N   . PRO B  1 29  ? 163.170 119.568 40.849 1.00   37.68 ? 28   PRO B N   1 
ATOM   1312  C  CA  . PRO B  1 29  ? 163.970 119.848 42.038 1.00   36.67 ? 28   PRO B CA  1 
ATOM   1313  C  C   . PRO B  1 29  ? 163.626 118.922 43.199 1.00   34.76 ? 28   PRO B C   1 
ATOM   1314  O  O   . PRO B  1 29  ? 162.567 118.306 43.202 1.00   34.36 ? 28   PRO B O   1 
ATOM   1315  C  CB  . PRO B  1 29  ? 163.611 121.307 42.355 1.00   37.24 ? 28   PRO B CB  1 
ATOM   1316  C  CG  . PRO B  1 29  ? 162.209 121.461 41.873 1.00   37.97 ? 28   PRO B CG  1 
ATOM   1317  C  CD  . PRO B  1 29  ? 162.033 120.505 40.716 1.00   38.21 ? 28   PRO B CD  1 
ATOM   1318  N  N   . VAL B  1 30  ? 164.526 118.840 44.177 1.00   34.06 ? 29   VAL B N   1 
ATOM   1319  C  CA  . VAL B  1 30  ? 164.308 118.057 45.395 1.00   32.63 ? 29   VAL B CA  1 
ATOM   1320  C  C   . VAL B  1 30  ? 163.986 118.979 46.585 1.00   32.94 ? 29   VAL B C   1 
ATOM   1321  O  O   . VAL B  1 30  ? 164.740 119.900 46.880 1.00   32.88 ? 29   VAL B O   1 
ATOM   1322  C  CB  . VAL B  1 30  ? 165.548 117.197 45.702 1.00   31.70 ? 29   VAL B CB  1 
ATOM   1323  C  CG1 . VAL B  1 30  ? 165.333 116.343 46.949 1.00   30.02 ? 29   VAL B CG1 1 
ATOM   1324  C  CG2 . VAL B  1 30  ? 165.889 116.336 44.501 1.00   30.62 ? 29   VAL B CG2 1 
ATOM   1325  N  N   . LYS B  1 31  ? 162.859 118.738 47.253 1.00   33.61 ? 30   LYS B N   1 
ATOM   1326  C  CA  . LYS B  1 31  ? 162.522 119.446 48.498 1.00   35.22 ? 30   LYS B CA  1 
ATOM   1327  C  C   . LYS B  1 31  ? 163.146 118.714 49.699 1.00   33.92 ? 30   LYS B C   1 
ATOM   1328  O  O   . LYS B  1 31  ? 163.017 117.483 49.833 1.00   32.76 ? 30   LYS B O   1 
ATOM   1329  C  CB  . LYS B  1 31  ? 161.009 119.537 48.665 1.00   38.37 ? 30   LYS B CB  1 
ATOM   1330  C  CG  . LYS B  1 31  ? 160.332 120.307 47.535 1.00   42.80 ? 30   LYS B CG  1 
ATOM   1331  C  CD  . LYS B  1 31  ? 158.858 119.948 47.368 1.00   45.16 ? 30   LYS B CD  1 
ATOM   1332  C  CE  . LYS B  1 31  ? 158.096 121.047 46.632 1.00   46.82 ? 30   LYS B CE  1 
ATOM   1333  N  NZ  . LYS B  1 31  ? 156.631 120.754 46.617 1.00   48.22 ? 30   LYS B NZ  1 
ATOM   1334  N  N   . VAL B  1 32  ? 163.846 119.478 50.535 1.00   33.08 ? 31   VAL B N   1 
ATOM   1335  C  CA  . VAL B  1 32  ? 164.610 118.969 51.674 1.00   31.94 ? 31   VAL B CA  1 
ATOM   1336  C  C   . VAL B  1 32  ? 164.114 119.683 52.926 1.00   33.42 ? 31   VAL B C   1 
ATOM   1337  O  O   . VAL B  1 32  ? 164.190 120.917 53.008 1.00   34.95 ? 31   VAL B O   1 
ATOM   1338  C  CB  . VAL B  1 32  ? 166.112 119.285 51.524 1.00   30.78 ? 31   VAL B CB  1 
ATOM   1339  C  CG1 . VAL B  1 32  ? 166.940 118.582 52.594 1.00   29.37 ? 31   VAL B CG1 1 
ATOM   1340  C  CG2 . VAL B  1 32  ? 166.595 118.945 50.131 1.00   30.42 ? 31   VAL B CG2 1 
ATOM   1341  N  N   . TRP B  1 33  ? 163.603 118.922 53.887 1.00   33.55 ? 32   TRP B N   1 
ATOM   1342  C  CA  . TRP B  1 33  ? 163.057 119.497 55.100 1.00   33.80 ? 32   TRP B CA  1 
ATOM   1343  C  C   . TRP B  1 33  ? 163.044 118.556 56.278 1.00   33.95 ? 32   TRP B C   1 
ATOM   1344  O  O   . TRP B  1 33  ? 163.051 117.323 56.133 1.00   32.29 ? 32   TRP B O   1 
ATOM   1345  C  CB  . TRP B  1 33  ? 161.650 120.000 54.842 1.00   34.36 ? 32   TRP B CB  1 
ATOM   1346  C  CG  . TRP B  1 33  ? 160.601 118.936 54.877 1.00   34.30 ? 32   TRP B CG  1 
ATOM   1347  C  CD1 . TRP B  1 33  ? 159.725 118.656 55.907 1.00   34.61 ? 32   TRP B CD1 1 
ATOM   1348  C  CD2 . TRP B  1 33  ? 160.276 117.966 53.823 1.00   33.78 ? 32   TRP B CD2 1 
ATOM   1349  N  NE1 . TRP B  1 33  ? 158.908 117.606 55.583 1.00   35.18 ? 32   TRP B NE1 1 
ATOM   1350  C  CE2 . TRP B  1 33  ? 159.183 117.152 54.345 1.00   33.80 ? 32   TRP B CE2 1 
ATOM   1351  C  CE3 . TRP B  1 33  ? 160.767 117.700 52.562 1.00   33.53 ? 32   TRP B CE3 1 
ATOM   1352  C  CZ2 . TRP B  1 33  ? 158.614 116.133 53.613 1.00   34.03 ? 32   TRP B CZ2 1 
ATOM   1353  C  CZ3 . TRP B  1 33  ? 160.197 116.652 51.832 1.00   33.29 ? 32   TRP B CZ3 1 
ATOM   1354  C  CH2 . TRP B  1 33  ? 159.140 115.893 52.345 1.00   33.37 ? 32   TRP B CH2 1 
ATOM   1355  N  N   . GLY B  1 34  ? 162.993 119.152 57.465 1.00   33.95 ? 33   GLY B N   1 
ATOM   1356  C  CA  . GLY B  1 34  ? 163.002 118.410 58.720 1.00   34.17 ? 33   GLY B CA  1 
ATOM   1357  C  C   . GLY B  1 34  ? 163.573 119.292 59.807 1.00   35.20 ? 33   GLY B C   1 
ATOM   1358  O  O   . GLY B  1 34  ? 163.683 120.508 59.634 1.00   35.06 ? 33   GLY B O   1 
ATOM   1359  N  N   . SER B  1 35  ? 163.934 118.695 60.933 1.00   34.82 ? 34   SER B N   1 
ATOM   1360  C  CA  . SER B  1 35  ? 164.653 119.446 61.942 1.00   35.46 ? 34   SER B CA  1 
ATOM   1361  C  C   . SER B  1 35  ? 165.846 118.705 62.476 1.00   34.14 ? 34   SER B C   1 
ATOM   1362  O  O   . SER B  1 35  ? 165.914 117.471 62.454 1.00   32.63 ? 34   SER B O   1 
ATOM   1363  C  CB  . SER B  1 35  ? 163.749 119.917 63.090 1.00   37.47 ? 34   SER B CB  1 
ATOM   1364  O  OG  . SER B  1 35  ? 162.849 118.921 63.517 1.00   37.47 ? 34   SER B OG  1 
ATOM   1365  N  N   . ILE B  1 36  ? 166.812 119.499 62.903 1.00   33.27 ? 35   ILE B N   1 
ATOM   1366  C  CA  . ILE B  1 36  ? 167.968 119.012 63.604 1.00   32.80 ? 35   ILE B CA  1 
ATOM   1367  C  C   . ILE B  1 36  ? 167.970 119.725 64.942 1.00   33.75 ? 35   ILE B C   1 
ATOM   1368  O  O   . ILE B  1 36  ? 167.755 120.953 64.977 1.00   33.21 ? 35   ILE B O   1 
ATOM   1369  C  CB  . ILE B  1 36  ? 169.254 119.368 62.855 1.00   32.41 ? 35   ILE B CB  1 
ATOM   1370  C  CG1 . ILE B  1 36  ? 169.137 118.938 61.381 1.00   32.07 ? 35   ILE B CG1 1 
ATOM   1371  C  CG2 . ILE B  1 36  ? 170.449 118.743 63.566 1.00   31.56 ? 35   ILE B CG2 1 
ATOM   1372  C  CD1 . ILE B  1 36  ? 170.352 119.229 60.521 1.00   31.72 ? 35   ILE B CD1 1 
ATOM   1373  N  N   . LYS B  1 37  ? 168.226 118.968 66.021 1.00   33.76 ? 36   LYS B N   1 
ATOM   1374  C  CA  . LYS B  1 37  ? 168.328 119.520 67.368 1.00   34.14 ? 36   LYS B CA  1 
ATOM   1375  C  C   . LYS B  1 37  ? 169.705 119.256 67.996 1.00   33.37 ? 36   LYS B C   1 
ATOM   1376  O  O   . LYS B  1 37  ? 170.546 118.519 67.456 1.00   31.38 ? 36   LYS B O   1 
ATOM   1377  C  CB  . LYS B  1 37  ? 167.201 118.990 68.261 1.00   35.46 ? 36   LYS B CB  1 
ATOM   1378  C  CG  . LYS B  1 37  ? 167.240 117.496 68.541 1.00   36.03 ? 36   LYS B CG  1 
ATOM   1379  C  CD  . LYS B  1 37  ? 165.953 117.024 69.218 1.00   37.10 ? 36   LYS B CD  1 
ATOM   1380  C  CE  . LYS B  1 37  ? 165.896 115.497 69.338 1.00   36.83 ? 36   LYS B CE  1 
ATOM   1381  N  NZ  . LYS B  1 37  ? 164.672 115.027 70.063 1.00   37.64 ? 36   LYS B NZ  1 
ATOM   1382  N  N   . GLY B  1 38  ? 169.950 119.921 69.117 1.00   32.36 ? 37   GLY B N   1 
ATOM   1383  C  CA  . GLY B  1 38  ? 171.204 119.782 69.844 1.00   31.73 ? 37   GLY B CA  1 
ATOM   1384  C  C   . GLY B  1 38  ? 172.366 120.571 69.302 1.00   31.16 ? 37   GLY B C   1 
ATOM   1385  O  O   . GLY B  1 38  ? 173.499 120.375 69.750 1.00   29.84 ? 37   GLY B O   1 
ATOM   1386  N  N   . LEU B  1 39  ? 172.088 121.483 68.372 1.00   32.17 ? 38   LEU B N   1 
ATOM   1387  C  CA  . LEU B  1 39  ? 173.111 122.363 67.788 1.00   33.54 ? 38   LEU B CA  1 
ATOM   1388  C  C   . LEU B  1 39  ? 173.337 123.631 68.641 1.00   36.35 ? 38   LEU B C   1 
ATOM   1389  O  O   . LEU B  1 39  ? 172.445 124.057 69.383 1.00   36.77 ? 38   LEU B O   1 
ATOM   1390  C  CB  . LEU B  1 39  ? 172.689 122.871 66.398 1.00   33.40 ? 38   LEU B CB  1 
ATOM   1391  C  CG  . LEU B  1 39  ? 172.834 122.122 65.056 1.00   32.54 ? 38   LEU B CG  1 
ATOM   1392  C  CD1 . LEU B  1 39  ? 173.720 120.923 65.148 1.00   30.62 ? 38   LEU B CD1 1 
ATOM   1393  C  CD2 . LEU B  1 39  ? 171.450 121.830 64.479 1.00   32.67 ? 38   LEU B CD2 1 
ATOM   1394  N  N   . THR B  1 40  ? 174.506 124.253 68.460 1.00   37.05 ? 39   THR B N   1 
ATOM   1395  C  CA  . THR B  1 40  ? 174.777 125.548 69.024 1.00   39.30 ? 39   THR B CA  1 
ATOM   1396  C  C   . THR B  1 40  ? 174.080 126.577 68.134 1.00   40.33 ? 39   THR B C   1 
ATOM   1397  O  O   . THR B  1 40  ? 174.025 126.439 66.891 1.00   40.57 ? 39   THR B O   1 
ATOM   1398  C  CB  . THR B  1 40  ? 176.288 125.867 69.105 1.00   40.45 ? 39   THR B CB  1 
ATOM   1399  O  OG1 . THR B  1 40  ? 176.879 125.801 67.804 1.00   40.77 ? 39   THR B OG1 1 
ATOM   1400  C  CG2 . THR B  1 40  ? 177.011 124.907 70.036 1.00   40.44 ? 39   THR B CG2 1 
ATOM   1401  N  N   . GLU B  1 41  ? 173.531 127.600 68.774 1.00   40.47 ? 40   GLU B N   1 
ATOM   1402  C  CA  . GLU B  1 41  ? 172.751 128.611 68.084 1.00   40.97 ? 40   GLU B CA  1 
ATOM   1403  C  C   . GLU B  1 41  ? 173.548 129.154 66.897 1.00   40.33 ? 40   GLU B C   1 
ATOM   1404  O  O   . GLU B  1 41  ? 174.762 129.363 66.996 1.00   38.44 ? 40   GLU B O   1 
ATOM   1405  C  CB  . GLU B  1 41  ? 172.375 129.734 69.065 1.00   43.12 ? 40   GLU B CB  1 
ATOM   1406  C  CG  . GLU B  1 41  ? 171.418 130.754 68.480 1.00   45.06 ? 40   GLU B CG  1 
ATOM   1407  C  CD  . GLU B  1 41  ? 170.949 131.785 69.486 1.00   47.57 ? 40   GLU B CD  1 
ATOM   1408  O  OE1 . GLU B  1 41  ? 171.156 131.599 70.702 1.00   49.12 ? 40   GLU B OE1 1 
ATOM   1409  O  OE2 . GLU B  1 41  ? 170.359 132.785 69.047 1.00   50.71 ? 40   GLU B OE2 1 
ATOM   1410  N  N   . GLY B  1 42  ? 172.875 129.318 65.760 1.00   40.76 ? 41   GLY B N   1 
ATOM   1411  C  CA  . GLY B  1 42  ? 173.523 129.840 64.567 1.00   41.06 ? 41   GLY B CA  1 
ATOM   1412  C  C   . GLY B  1 42  ? 173.745 128.839 63.450 1.00   40.61 ? 41   GLY B C   1 
ATOM   1413  O  O   . GLY B  1 42  ? 173.004 127.855 63.313 1.00   40.21 ? 41   GLY B O   1 
ATOM   1414  N  N   . LEU B  1 43  ? 174.786 129.098 62.658 1.00   40.84 ? 42   LEU B N   1 
ATOM   1415  C  CA  . LEU B  1 43  ? 174.933 128.498 61.352 1.00   40.53 ? 42   LEU B CA  1 
ATOM   1416  C  C   . LEU B  1 43  ? 175.836 127.259 61.306 1.00   39.48 ? 42   LEU B C   1 
ATOM   1417  O  O   . LEU B  1 43  ? 176.914 127.230 61.880 1.00   39.08 ? 42   LEU B O   1 
ATOM   1418  C  CB  . LEU B  1 43  ? 175.441 129.531 60.359 1.00   42.16 ? 42   LEU B CB  1 
ATOM   1419  C  CG  . LEU B  1 43  ? 174.496 130.676 59.999 1.00   43.62 ? 42   LEU B CG  1 
ATOM   1420  C  CD1 . LEU B  1 43  ? 175.100 131.403 58.816 1.00   44.58 ? 42   LEU B CD1 1 
ATOM   1421  C  CD2 . LEU B  1 43  ? 173.100 130.154 59.660 1.00   43.64 ? 42   LEU B CD2 1 
ATOM   1422  N  N   . HIS B  1 44  ? 175.393 126.259 60.556 1.00   37.73 ? 43   HIS B N   1 
ATOM   1423  C  CA  . HIS B  1 44  ? 176.081 124.978 60.500 1.00   36.76 ? 43   HIS B CA  1 
ATOM   1424  C  C   . HIS B  1 44  ? 176.062 124.455 59.109 1.00   35.79 ? 43   HIS B C   1 
ATOM   1425  O  O   . HIS B  1 44  ? 174.986 124.308 58.515 1.00   36.04 ? 43   HIS B O   1 
ATOM   1426  C  CB  . HIS B  1 44  ? 175.375 124.002 61.404 1.00   36.14 ? 43   HIS B CB  1 
ATOM   1427  C  CG  . HIS B  1 44  ? 175.443 124.378 62.853 1.00   37.06 ? 43   HIS B CG  1 
ATOM   1428  N  ND1 . HIS B  1 44  ? 176.559 124.227 63.580 1.00   37.48 ? 43   HIS B ND1 1 
ATOM   1429  C  CD2 . HIS B  1 44  ? 174.486 124.928 63.704 1.00   37.85 ? 43   HIS B CD2 1 
ATOM   1430  C  CE1 . HIS B  1 44  ? 176.332 124.646 64.834 1.00   37.97 ? 43   HIS B CE1 1 
ATOM   1431  N  NE2 . HIS B  1 44  ? 175.059 125.063 64.912 1.00   38.06 ? 43   HIS B NE2 1 
ATOM   1432  N  N   . GLY B  1 45  ? 177.243 124.171 58.570 1.00   34.86 ? 44   GLY B N   1 
ATOM   1433  C  CA  . GLY B  1 45  ? 177.345 123.656 57.214 1.00   35.07 ? 44   GLY B CA  1 
ATOM   1434  C  C   . GLY B  1 45  ? 176.571 122.354 57.056 1.00   33.43 ? 44   GLY B C   1 
ATOM   1435  O  O   . GLY B  1 45  ? 176.477 121.566 57.994 1.00   33.11 ? 44   GLY B O   1 
ATOM   1436  N  N   . PHE B  1 46  ? 176.048 122.127 55.852 1.00   32.69 ? 45   PHE B N   1 
ATOM   1437  C  CA  . PHE B  1 46  ? 175.078 121.068 55.595 1.00   31.24 ? 45   PHE B CA  1 
ATOM   1438  C  C   . PHE B  1 46  ? 175.415 120.533 54.221 1.00   31.13 ? 45   PHE B C   1 
ATOM   1439  O  O   . PHE B  1 46  ? 175.207 121.220 53.222 1.00   32.05 ? 45   PHE B O   1 
ATOM   1440  C  CB  . PHE B  1 46  ? 173.693 121.701 55.624 1.00   31.30 ? 45   PHE B CB  1 
ATOM   1441  C  CG  . PHE B  1 46  ? 172.553 120.737 55.631 1.00   30.24 ? 45   PHE B CG  1 
ATOM   1442  C  CD1 . PHE B  1 46  ? 172.413 119.812 56.651 1.00   29.67 ? 45   PHE B CD1 1 
ATOM   1443  C  CD2 . PHE B  1 46  ? 171.563 120.820 54.656 1.00   29.66 ? 45   PHE B CD2 1 
ATOM   1444  C  CE1 . PHE B  1 46  ? 171.324 118.959 56.682 1.00   29.40 ? 45   PHE B CE1 1 
ATOM   1445  C  CE2 . PHE B  1 46  ? 170.476 119.975 54.674 1.00   29.70 ? 45   PHE B CE2 1 
ATOM   1446  C  CZ  . PHE B  1 46  ? 170.352 119.035 55.693 1.00   29.38 ? 45   PHE B CZ  1 
ATOM   1447  N  N   . HIS B  1 47  ? 175.970 119.325 54.180 1.00   30.01 ? 46   HIS B N   1 
ATOM   1448  C  CA  . HIS B  1 47  ? 176.563 118.760 52.977 1.00   29.69 ? 46   HIS B CA  1 
ATOM   1449  C  C   . HIS B  1 47  ? 176.188 117.324 52.779 1.00   28.24 ? 46   HIS B C   1 
ATOM   1450  O  O   . HIS B  1 47  ? 176.108 116.567 53.758 1.00   26.35 ? 46   HIS B O   1 
ATOM   1451  C  CB  . HIS B  1 47  ? 178.078 118.726 53.087 1.00   30.39 ? 46   HIS B CB  1 
ATOM   1452  C  CG  . HIS B  1 47  ? 178.716 120.009 53.518 1.00   32.55 ? 46   HIS B CG  1 
ATOM   1453  N  ND1 . HIS B  1 47  ? 179.900 120.024 54.136 1.00   33.25 ? 46   HIS B ND1 1 
ATOM   1454  C  CD2 . HIS B  1 47  ? 178.339 121.345 53.351 1.00   33.96 ? 46   HIS B CD2 1 
ATOM   1455  C  CE1 . HIS B  1 47  ? 180.263 121.304 54.390 1.00   34.57 ? 46   HIS B CE1 1 
ATOM   1456  N  NE2 . HIS B  1 47  ? 179.303 122.108 53.921 1.00   34.87 ? 46   HIS B NE2 1 
ATOM   1457  N  N   . VAL B  1 48  ? 176.025 116.926 51.519 1.00   27.41 ? 47   VAL B N   1 
ATOM   1458  C  CA  . VAL B  1 48  ? 176.033 115.494 51.149 1.00   27.05 ? 47   VAL B CA  1 
ATOM   1459  C  C   . VAL B  1 48  ? 177.474 115.100 50.846 1.00   26.86 ? 47   VAL B C   1 
ATOM   1460  O  O   . VAL B  1 48  ? 178.122 115.713 49.995 1.00   27.75 ? 47   VAL B O   1 
ATOM   1461  C  CB  . VAL B  1 48  ? 175.166 115.203 49.910 1.00   26.82 ? 47   VAL B CB  1 
ATOM   1462  C  CG1 . VAL B  1 48  ? 175.104 113.694 49.643 1.00   26.04 ? 47   VAL B CG1 1 
ATOM   1463  C  CG2 . VAL B  1 48  ? 173.775 115.804 50.076 1.00   26.31 ? 47   VAL B CG2 1 
ATOM   1464  N  N   . HIS B  1 49  ? 177.992 114.116 51.565 1.00   25.81 ? 48   HIS B N   1 
ATOM   1465  C  CA  . HIS B  1 49  ? 179.355 113.625 51.333 1.00   26.27 ? 48   HIS B CA  1 
ATOM   1466  C  C   . HIS B  1 49  ? 179.311 112.378 50.500 1.00   25.88 ? 48   HIS B C   1 
ATOM   1467  O  O   . HIS B  1 49  ? 178.284 111.711 50.455 1.00   24.73 ? 48   HIS B O   1 
ATOM   1468  C  CB  . HIS B  1 49  ? 180.046 113.326 52.646 1.00   26.14 ? 48   HIS B CB  1 
ATOM   1469  C  CG  . HIS B  1 49  ? 180.544 114.548 53.366 1.00   27.74 ? 48   HIS B CG  1 
ATOM   1470  N  ND1 . HIS B  1 49  ? 181.839 114.737 53.632 1.00   28.38 ? 48   HIS B ND1 1 
ATOM   1471  C  CD2 . HIS B  1 49  ? 179.867 115.656 53.890 1.00   28.17 ? 48   HIS B CD2 1 
ATOM   1472  C  CE1 . HIS B  1 49  ? 181.997 115.901 54.278 1.00   29.04 ? 48   HIS B CE1 1 
ATOM   1473  N  NE2 . HIS B  1 49  ? 180.785 116.457 54.446 1.00   28.61 ? 48   HIS B NE2 1 
ATOM   1474  N  N   . GLU B  1 50  ? 180.434 112.023 49.888 1.00   26.24 ? 49   GLU B N   1 
ATOM   1475  C  CA  . GLU B  1 50  ? 180.450 111.018 48.821 1.00   27.02 ? 49   GLU B CA  1 
ATOM   1476  C  C   . GLU B  1 50  ? 180.005 109.599 49.213 1.00   25.74 ? 49   GLU B C   1 
ATOM   1477  O  O   . GLU B  1 50  ? 179.251 108.964 48.475 1.00   24.59 ? 49   GLU B O   1 
ATOM   1478  C  CB  . GLU B  1 50  ? 181.832 110.939 48.193 1.00   28.45 ? 49   GLU B CB  1 
ATOM   1479  C  CG  . GLU B  1 50  ? 181.815 110.205 46.864 1.00   29.88 ? 49   GLU B CG  1 
ATOM   1480  C  CD  . GLU B  1 50  ? 183.188 110.014 46.273 1.00   31.27 ? 49   GLU B CD  1 
ATOM   1481  O  OE1 . GLU B  1 50  ? 184.190 110.522 46.825 1.00   34.51 ? 49   GLU B OE1 1 
ATOM   1482  O  OE2 . GLU B  1 50  ? 183.261 109.335 45.254 1.00   33.46 ? 49   GLU B OE2 1 
ATOM   1483  N  N   . PHE B  1 51  ? 180.456 109.108 50.363 1.00   25.63 ? 50   PHE B N   1 
ATOM   1484  C  CA  . PHE B  1 51  ? 180.206 107.712 50.759 1.00   25.14 ? 50   PHE B CA  1 
ATOM   1485  C  C   . PHE B  1 51  ? 179.206 107.512 51.892 1.00   23.86 ? 50   PHE B C   1 
ATOM   1486  O  O   . PHE B  1 51  ? 179.241 108.198 52.904 1.00   23.32 ? 50   PHE B O   1 
ATOM   1487  C  CB  . PHE B  1 51  ? 181.525 107.064 51.142 1.00   26.29 ? 50   PHE B CB  1 
ATOM   1488  C  CG  . PHE B  1 51  ? 182.560 107.187 50.083 1.00   28.40 ? 50   PHE B CG  1 
ATOM   1489  C  CD1 . PHE B  1 51  ? 182.367 106.585 48.840 1.00   29.41 ? 50   PHE B CD1 1 
ATOM   1490  C  CD2 . PHE B  1 51  ? 183.721 107.904 50.303 1.00   29.97 ? 50   PHE B CD2 1 
ATOM   1491  C  CE1 . PHE B  1 51  ? 183.321 106.714 47.843 1.00   30.82 ? 50   PHE B CE1 1 
ATOM   1492  C  CE2 . PHE B  1 51  ? 184.674 108.031 49.309 1.00   30.66 ? 50   PHE B CE2 1 
ATOM   1493  C  CZ  . PHE B  1 51  ? 184.477 107.434 48.082 1.00   31.18 ? 50   PHE B CZ  1 
ATOM   1494  N  N   . GLY B  1 52  ? 178.337 106.522 51.724 1.00   23.25 ? 51   GLY B N   1 
ATOM   1495  C  CA  . GLY B  1 52  ? 177.417 106.115 52.768 1.00   22.46 ? 51   GLY B CA  1 
ATOM   1496  C  C   . GLY B  1 52  ? 178.064 105.093 53.663 1.00   22.61 ? 51   GLY B C   1 
ATOM   1497  O  O   . GLY B  1 52  ? 177.485 104.028 53.880 1.00   22.39 ? 51   GLY B O   1 
ATOM   1498  N  N   . ASP B  1 53  ? 179.240 105.456 54.200 1.00   22.23 ? 52   ASP B N   1 
ATOM   1499  C  CA  . ASP B  1 53  ? 180.119 104.595 54.977 1.00   22.60 ? 52   ASP B CA  1 
ATOM   1500  C  C   . ASP B  1 53  ? 180.326 105.231 56.358 1.00   23.59 ? 52   ASP B C   1 
ATOM   1501  O  O   . ASP B  1 53  ? 181.064 106.217 56.498 1.00   24.92 ? 52   ASP B O   1 
ATOM   1502  C  CB  . ASP B  1 53  ? 181.463 104.453 54.247 1.00   22.60 ? 52   ASP B CB  1 
ATOM   1503  C  CG  . ASP B  1 53  ? 182.454 103.529 54.965 1.00   22.79 ? 52   ASP B CG  1 
ATOM   1504  O  OD1 . ASP B  1 53  ? 182.360 103.332 56.187 1.00   22.16 ? 52   ASP B OD1 1 
ATOM   1505  O  OD2 . ASP B  1 53  ? 183.356 102.999 54.284 1.00   23.33 ? 52   ASP B OD2 1 
ATOM   1506  N  N   . ASN B  1 54  ? 179.665 104.662 57.356 1.00   23.93 ? 53   ASN B N   1 
ATOM   1507  C  CA  . ASN B  1 54  ? 179.663 105.151 58.726 1.00   25.71 ? 53   ASN B CA  1 
ATOM   1508  C  C   . ASN B  1 54  ? 180.442 104.181 59.634 1.00   24.64 ? 53   ASN B C   1 
ATOM   1509  O  O   . ASN B  1 54  ? 180.195 104.115 60.833 1.00   24.96 ? 53   ASN B O   1 
ATOM   1510  C  CB  . ASN B  1 54  ? 178.200 105.252 59.152 1.00   27.86 ? 53   ASN B CB  1 
ATOM   1511  C  CG  . ASN B  1 54  ? 177.993 105.807 60.554 1.00   30.78 ? 53   ASN B CG  1 
ATOM   1512  O  OD1 . ASN B  1 54  ? 177.394 105.129 61.410 1.00   34.13 ? 53   ASN B OD1 1 
ATOM   1513  N  ND2 . ASN B  1 54  ? 178.414 107.053 60.785 1.00   32.73 ? 53   ASN B ND2 1 
ATOM   1514  N  N   . THR B  1 55  ? 181.380 103.431 59.057 1.00   23.49 ? 54   THR B N   1 
ATOM   1515  C  CA  . THR B  1 55  ? 182.146 102.441 59.806 1.00   23.23 ? 54   THR B CA  1 
ATOM   1516  C  C   . THR B  1 55  ? 183.137 103.078 60.797 1.00   23.91 ? 54   THR B C   1 
ATOM   1517  O  O   . THR B  1 55  ? 183.579 102.430 61.725 1.00   24.60 ? 54   THR B O   1 
ATOM   1518  C  CB  . THR B  1 55  ? 182.918 101.495 58.868 1.00   23.26 ? 54   THR B CB  1 
ATOM   1519  O  OG1 . THR B  1 55  ? 183.837 102.238 58.077 1.00   22.74 ? 54   THR B OG1 1 
ATOM   1520  C  CG2 . THR B  1 55  ? 181.955 100.693 57.937 1.00   22.62 ? 54   THR B CG2 1 
ATOM   1521  N  N   . ALA B  1 56  ? 183.473 104.341 60.600 1.00   24.42 ? 55   ALA B N   1 
ATOM   1522  C  CA  . ALA B  1 56  ? 184.264 105.102 61.559 1.00   25.82 ? 55   ALA B CA  1 
ATOM   1523  C  C   . ALA B  1 56  ? 183.533 106.405 61.873 1.00   26.07 ? 55   ALA B C   1 
ATOM   1524  O  O   . ALA B  1 56  ? 184.111 107.487 61.816 1.00   28.84 ? 55   ALA B O   1 
ATOM   1525  C  CB  . ALA B  1 56  ? 185.653 105.384 60.991 1.00   25.91 ? 55   ALA B CB  1 
ATOM   1526  N  N   . GLY B  1 57  ? 182.239 106.310 62.136 1.00   25.58 ? 56   GLY B N   1 
ATOM   1527  C  CA  . GLY B  1 57  ? 181.413 107.497 62.317 1.00   25.50 ? 56   GLY B CA  1 
ATOM   1528  C  C   . GLY B  1 57  ? 181.379 108.342 61.042 1.00   25.80 ? 56   GLY B C   1 
ATOM   1529  O  O   . GLY B  1 57  ? 181.515 107.825 59.934 1.00   25.82 ? 56   GLY B O   1 
ATOM   1530  N  N   . CYS B  1 58  ? 181.248 109.650 61.193 1.00   25.81 ? 57   CYS B N   1 
ATOM   1531  C  CA  . CYS B  1 58  ? 181.161 110.548 60.032 1.00   26.19 ? 57   CYS B CA  1 
ATOM   1532  C  C   . CYS B  1 58  ? 182.476 110.712 59.260 1.00   26.37 ? 57   CYS B C   1 
ATOM   1533  O  O   . CYS B  1 58  ? 182.479 111.184 58.135 1.00   26.70 ? 57   CYS B O   1 
ATOM   1534  C  CB  . CYS B  1 58  ? 180.625 111.899 60.480 1.00   26.41 ? 57   CYS B CB  1 
ATOM   1535  S  SG  . CYS B  1 58  ? 179.055 111.725 61.360 1.00   28.36 ? 57   CYS B SG  1 
ATOM   1536  N  N   . THR B  1 59  ? 183.584 110.277 59.840 1.00   27.01 ? 58   THR B N   1 
ATOM   1537  C  CA  . THR B  1 59  ? 184.889 110.413 59.206 1.00   27.54 ? 58   THR B CA  1 
ATOM   1538  C  C   . THR B  1 59  ? 185.024 109.578 57.934 1.00   26.75 ? 58   THR B C   1 
ATOM   1539  O  O   . THR B  1 59  ? 185.675 110.005 56.982 1.00   27.87 ? 58   THR B O   1 
ATOM   1540  C  CB  . THR B  1 59  ? 186.019 110.005 60.179 1.00   29.10 ? 58   THR B CB  1 
ATOM   1541  O  OG1 . THR B  1 59  ? 185.724 110.483 61.497 1.00   29.75 ? 58   THR B OG1 1 
ATOM   1542  C  CG2 . THR B  1 59  ? 187.340 110.573 59.723 1.00   30.46 ? 58   THR B CG2 1 
ATOM   1543  N  N   . SER B  1 60  ? 184.413 108.397 57.903 1.00   24.83 ? 59   SER B N   1 
ATOM   1544  C  CA  . SER B  1 60  ? 184.515 107.532 56.734 1.00   24.34 ? 59   SER B CA  1 
ATOM   1545  C  C   . SER B  1 60  ? 183.567 107.944 55.592 1.00   23.85 ? 59   SER B C   1 
ATOM   1546  O  O   . SER B  1 60  ? 183.552 107.295 54.542 1.00   23.83 ? 59   SER B O   1 
ATOM   1547  C  CB  . SER B  1 60  ? 184.349 106.048 57.114 1.00   23.96 ? 59   SER B CB  1 
ATOM   1548  O  OG  . SER B  1 60  ? 183.353 105.843 58.107 1.00   23.67 ? 59   SER B OG  1 
ATOM   1549  N  N   . ALA B  1 61  ? 182.830 109.039 55.759 1.00   23.38 ? 60   ALA B N   1 
ATOM   1550  C  CA  . ALA B  1 61  ? 181.916 109.505 54.707 1.00   24.31 ? 60   ALA B CA  1 
ATOM   1551  C  C   . ALA B  1 61  ? 182.642 110.145 53.493 1.00   25.49 ? 60   ALA B C   1 
ATOM   1552  O  O   . ALA B  1 61  ? 182.007 110.458 52.481 1.00   25.61 ? 60   ALA B O   1 
ATOM   1553  C  CB  . ALA B  1 61  ? 180.898 110.479 55.283 1.00   23.57 ? 60   ALA B CB  1 
ATOM   1554  N  N   . GLY B  1 62  ? 183.950 110.347 53.613 1.00   26.14 ? 61   GLY B N   1 
ATOM   1555  C  CA  . GLY B  1 62  ? 184.753 110.933 52.556 1.00   27.77 ? 61   GLY B CA  1 
ATOM   1556  C  C   . GLY B  1 62  ? 184.481 112.403 52.287 1.00   28.74 ? 61   GLY B C   1 
ATOM   1557  O  O   . GLY B  1 62  ? 183.874 113.102 53.115 1.00   27.76 ? 61   GLY B O   1 
ATOM   1558  N  N   . PRO B  1 63  ? 184.918 112.880 51.109 1.00   30.62 ? 62   PRO B N   1 
ATOM   1559  C  CA  . PRO B  1 63  ? 184.800 114.289 50.734 1.00   31.37 ? 62   PRO B CA  1 
ATOM   1560  C  C   . PRO B  1 63  ? 183.395 114.640 50.290 1.00   31.75 ? 62   PRO B C   1 
ATOM   1561  O  O   . PRO B  1 63  ? 182.510 113.775 50.280 1.00   30.58 ? 62   PRO B O   1 
ATOM   1562  C  CB  . PRO B  1 63  ? 185.783 114.421 49.573 1.00   32.24 ? 62   PRO B CB  1 
ATOM   1563  C  CG  . PRO B  1 63  ? 185.790 113.078 48.933 1.00   31.86 ? 62   PRO B CG  1 
ATOM   1564  C  CD  . PRO B  1 63  ? 185.551 112.078 50.039 1.00   31.27 ? 62   PRO B CD  1 
ATOM   1565  N  N   . HIS B  1 64  ? 183.193 115.901 49.919 1.00   32.17 ? 63   HIS B N   1 
ATOM   1566  C  CA  . HIS B  1 64  ? 181.896 116.353 49.421 1.00   32.72 ? 63   HIS B CA  1 
ATOM   1567  C  C   . HIS B  1 64  ? 181.572 115.620 48.150 1.00   31.36 ? 63   HIS B C   1 
ATOM   1568  O  O   . HIS B  1 64  ? 182.466 115.355 47.332 1.00   30.06 ? 63   HIS B O   1 
ATOM   1569  C  CB  . HIS B  1 64  ? 181.908 117.856 49.148 1.00   35.29 ? 63   HIS B CB  1 
ATOM   1570  C  CG  . HIS B  1 64  ? 182.113 118.714 50.390 1.00   37.83 ? 63   HIS B CG  1 
ATOM   1571  N  ND1 . HIS B  1 64  ? 181.582 119.948 50.514 1.00   39.85 ? 63   HIS B ND1 1 
ATOM   1572  C  CD2 . HIS B  1 64  ? 182.816 118.474 51.566 1.00   39.06 ? 63   HIS B CD2 1 
ATOM   1573  C  CE1 . HIS B  1 64  ? 181.940 120.472 51.705 1.00   40.69 ? 63   HIS B CE1 1 
ATOM   1574  N  NE2 . HIS B  1 64  ? 182.692 119.572 52.344 1.00   41.18 ? 63   HIS B NE2 1 
ATOM   1575  N  N   . PHE B  1 65  ? 180.300 115.266 47.978 1.00   30.90 ? 64   PHE B N   1 
ATOM   1576  C  CA  . PHE B  1 65  ? 179.858 114.582 46.758 1.00   30.44 ? 64   PHE B CA  1 
ATOM   1577  C  C   . PHE B  1 65  ? 180.077 115.579 45.625 1.00   31.73 ? 64   PHE B C   1 
ATOM   1578  O  O   . PHE B  1 65  ? 179.487 116.665 45.633 1.00   32.27 ? 64   PHE B O   1 
ATOM   1579  C  CB  . PHE B  1 65  ? 178.391 114.176 46.860 1.00   29.06 ? 64   PHE B CB  1 
ATOM   1580  C  CG  . PHE B  1 65  ? 177.836 113.508 45.616 1.00   28.89 ? 64   PHE B CG  1 
ATOM   1581  C  CD1 . PHE B  1 65  ? 178.573 112.563 44.914 1.00   28.93 ? 64   PHE B CD1 1 
ATOM   1582  C  CD2 . PHE B  1 65  ? 176.563 113.817 45.164 1.00   28.40 ? 64   PHE B CD2 1 
ATOM   1583  C  CE1 . PHE B  1 65  ? 178.040 111.940 43.791 1.00   29.47 ? 64   PHE B CE1 1 
ATOM   1584  C  CE2 . PHE B  1 65  ? 176.028 113.200 44.039 1.00   28.73 ? 64   PHE B CE2 1 
ATOM   1585  C  CZ  . PHE B  1 65  ? 176.764 112.259 43.351 1.00   28.92 ? 64   PHE B CZ  1 
ATOM   1586  N  N   . ASN B  1 66  ? 180.954 115.221 44.689 1.00   33.18 ? 65   ASN B N   1 
ATOM   1587  C  CA  . ASN B  1 66  ? 181.429 116.153 43.650 1.00   34.74 ? 65   ASN B CA  1 
ATOM   1588  C  C   . ASN B  1 66  ? 181.709 115.406 42.342 1.00   35.88 ? 65   ASN B C   1 
ATOM   1589  O  O   . ASN B  1 66  ? 182.861 115.300 41.918 1.00   38.03 ? 65   ASN B O   1 
ATOM   1590  C  CB  . ASN B  1 66  ? 182.689 116.854 44.159 1.00   35.38 ? 65   ASN B CB  1 
ATOM   1591  C  CG  . ASN B  1 66  ? 183.167 117.997 43.255 1.00   36.74 ? 65   ASN B CG  1 
ATOM   1592  O  OD1 . ASN B  1 66  ? 182.386 118.622 42.535 1.00   36.55 ? 65   ASN B OD1 1 
ATOM   1593  N  ND2 . ASN B  1 66  ? 184.463 118.293 43.330 1.00   35.52 ? 65   ASN B ND2 1 
ATOM   1594  N  N   . PRO B  1 67  ? 180.654 114.873 41.697 1.00   34.93 ? 66   PRO B N   1 
ATOM   1595  C  CA  . PRO B  1 67  ? 180.837 114.115 40.447 1.00   35.88 ? 66   PRO B CA  1 
ATOM   1596  C  C   . PRO B  1 67  ? 181.264 114.950 39.240 1.00   38.40 ? 66   PRO B C   1 
ATOM   1597  O  O   . PRO B  1 67  ? 181.813 114.406 38.283 1.00   37.70 ? 66   PRO B O   1 
ATOM   1598  C  CB  . PRO B  1 67  ? 179.452 113.506 40.193 1.00   34.94 ? 66   PRO B CB  1 
ATOM   1599  C  CG  . PRO B  1 67  ? 178.506 114.382 40.932 1.00   34.48 ? 66   PRO B CG  1 
ATOM   1600  C  CD  . PRO B  1 67  ? 179.245 114.925 42.120 1.00   33.70 ? 66   PRO B CD  1 
ATOM   1601  N  N   . LEU B  1 68  ? 181.020 116.255 39.284 1.00   40.14 ? 67   LEU B N   1 
ATOM   1602  C  CA  . LEU B  1 68  ? 181.423 117.132 38.194 1.00   42.94 ? 67   LEU B CA  1 
ATOM   1603  C  C   . LEU B  1 68  ? 182.744 117.849 38.492 1.00   44.00 ? 67   LEU B C   1 
ATOM   1604  O  O   . LEU B  1 68  ? 183.074 118.808 37.822 1.00   45.56 ? 67   LEU B O   1 
ATOM   1605  C  CB  . LEU B  1 68  ? 180.311 118.146 37.882 1.00   44.10 ? 67   LEU B CB  1 
ATOM   1606  C  CG  . LEU B  1 68  ? 179.055 117.631 37.169 1.00   44.12 ? 67   LEU B CG  1 
ATOM   1607  C  CD1 . LEU B  1 68  ? 177.982 118.711 37.186 1.00   44.87 ? 67   LEU B CD1 1 
ATOM   1608  C  CD2 . LEU B  1 68  ? 179.368 117.221 35.735 1.00   46.13 ? 67   LEU B CD2 1 
ATOM   1609  N  N   . SER B  1 69  ? 183.508 117.368 39.471 1.00   44.37 ? 68   SER B N   1 
ATOM   1610  C  CA  . SER B  1 69  ? 184.813 117.953 39.836 1.00   45.40 ? 68   SER B CA  1 
ATOM   1611  C  C   . SER B  1 69  ? 184.861 119.484 39.819 1.00   46.98 ? 68   SER B C   1 
ATOM   1612  O  O   . SER B  1 69  ? 185.754 120.061 39.222 1.00   47.20 ? 68   SER B O   1 
ATOM   1613  C  CB  . SER B  1 69  ? 185.907 117.428 38.911 1.00   46.22 ? 68   SER B CB  1 
ATOM   1614  O  OG  . SER B  1 69  ? 185.936 116.024 38.897 1.00   45.85 ? 68   SER B OG  1 
ATOM   1615  N  N   . ARG B  1 70  ? 183.895 120.126 40.462 1.00   47.94 ? 69   ARG B N   1 
ATOM   1616  C  CA  . ARG B  1 70  ? 183.870 121.584 40.596 1.00   50.04 ? 69   ARG B CA  1 
ATOM   1617  C  C   . ARG B  1 70  ? 184.395 121.968 41.994 1.00   49.94 ? 69   ARG B C   1 
ATOM   1618  O  O   . ARG B  1 70  ? 184.564 121.103 42.857 1.00   48.72 ? 69   ARG B O   1 
ATOM   1619  C  CB  . ARG B  1 70  ? 182.441 122.103 40.416 1.00   51.66 ? 69   ARG B CB  1 
ATOM   1620  C  CG  . ARG B  1 70  ? 181.716 121.561 39.191 1.00   54.04 ? 69   ARG B CG  1 
ATOM   1621  C  CD  . ARG B  1 70  ? 181.686 122.517 38.017 1.00   58.24 ? 69   ARG B CD  1 
ATOM   1622  N  NE  . ARG B  1 70  ? 180.395 123.218 37.926 1.00   61.42 ? 69   ARG B NE  1 
ATOM   1623  C  CZ  . ARG B  1 70  ? 179.346 122.826 37.194 1.00   61.03 ? 69   ARG B CZ  1 
ATOM   1624  N  NH1 . ARG B  1 70  ? 179.394 121.725 36.448 1.00   61.08 ? 69   ARG B NH1 1 
ATOM   1625  N  NH2 . ARG B  1 70  ? 178.229 123.549 37.208 1.00   60.64 ? 69   ARG B NH2 1 
ATOM   1626  N  N   . LYS B  1 71  ? 184.649 123.256 42.213 1.00   50.58 ? 70   LYS B N   1 
ATOM   1627  C  CA  . LYS B  1 71  ? 185.098 123.746 43.515 1.00   50.34 ? 70   LYS B CA  1 
ATOM   1628  C  C   . LYS B  1 71  ? 183.893 123.940 44.418 1.00   47.81 ? 70   LYS B C   1 
ATOM   1629  O  O   . LYS B  1 71  ? 182.754 123.969 43.943 1.00   46.97 ? 70   LYS B O   1 
ATOM   1630  C  CB  . LYS B  1 71  ? 185.851 125.078 43.375 1.00   54.20 ? 70   LYS B CB  1 
ATOM   1631  C  CG  . LYS B  1 71  ? 187.170 124.995 42.612 1.00   57.39 ? 70   LYS B CG  1 
ATOM   1632  C  CD  . LYS B  1 71  ? 188.258 124.280 43.412 1.00   59.64 ? 70   LYS B CD  1 
ATOM   1633  C  CE  . LYS B  1 71  ? 189.653 124.537 42.843 1.00   63.22 ? 70   LYS B CE  1 
ATOM   1634  N  NZ  . LYS B  1 71  ? 190.725 124.207 43.836 1.00   65.05 ? 70   LYS B NZ  1 
ATOM   1635  N  N   . HIS B  1 72  ? 184.158 124.094 45.714 1.00   45.81 ? 71   HIS B N   1 
ATOM   1636  C  CA  . HIS B  1 72  ? 183.119 124.214 46.725 1.00   44.07 ? 71   HIS B CA  1 
ATOM   1637  C  C   . HIS B  1 72  ? 182.445 125.562 46.631 1.00   44.93 ? 71   HIS B C   1 
ATOM   1638  O  O   . HIS B  1 72  ? 183.097 126.566 46.391 1.00   46.95 ? 71   HIS B O   1 
ATOM   1639  C  CB  . HIS B  1 72  ? 183.727 124.016 48.125 1.00   42.77 ? 71   HIS B CB  1 
ATOM   1640  C  CG  . HIS B  1 72  ? 182.734 124.170 49.253 1.00   41.54 ? 71   HIS B CG  1 
ATOM   1641  N  ND1 . HIS B  1 72  ? 181.889 123.184 49.630 1.00   40.52 ? 71   HIS B ND1 1 
ATOM   1642  C  CD2 . HIS B  1 72  ? 182.458 125.256 50.074 1.00   41.27 ? 71   HIS B CD2 1 
ATOM   1643  C  CE1 . HIS B  1 72  ? 181.104 123.630 50.628 1.00   39.92 ? 71   HIS B CE1 1 
ATOM   1644  N  NE2 . HIS B  1 72  ? 181.464 124.891 50.909 1.00   40.68 ? 71   HIS B NE2 1 
ATOM   1645  N  N   . GLY B  1 73  ? 181.132 125.596 46.840 1.00   43.98 ? 72   GLY B N   1 
ATOM   1646  C  CA  . GLY B  1 73  ? 180.392 126.850 46.969 1.00   44.06 ? 72   GLY B CA  1 
ATOM   1647  C  C   . GLY B  1 73  ? 179.119 126.638 47.762 1.00   43.28 ? 72   GLY B C   1 
ATOM   1648  O  O   . GLY B  1 73  ? 178.941 125.586 48.387 1.00   42.26 ? 72   GLY B O   1 
ATOM   1649  N  N   . GLY B  1 74  ? 178.241 127.636 47.756 1.00   43.04 ? 73   GLY B N   1 
ATOM   1650  C  CA  . GLY B  1 74  ? 176.889 127.491 48.316 1.00   42.62 ? 73   GLY B CA  1 
ATOM   1651  C  C   . GLY B  1 74  ? 175.890 126.948 47.302 1.00   41.85 ? 73   GLY B C   1 
ATOM   1652  O  O   . GLY B  1 74  ? 176.194 126.886 46.112 1.00   42.24 ? 73   GLY B O   1 
ATOM   1653  N  N   . PRO B  1 75  ? 174.683 126.566 47.764 1.00   41.46 ? 74   PRO B N   1 
ATOM   1654  C  CA  . PRO B  1 75  ? 173.677 125.928 46.905 1.00   41.38 ? 74   PRO B CA  1 
ATOM   1655  C  C   . PRO B  1 75  ? 173.200 126.798 45.742 1.00   42.99 ? 74   PRO B C   1 
ATOM   1656  O  O   . PRO B  1 75  ? 172.946 126.291 44.651 1.00   41.36 ? 74   PRO B O   1 
ATOM   1657  C  CB  . PRO B  1 75  ? 172.510 125.649 47.863 1.00   41.13 ? 74   PRO B CB  1 
ATOM   1658  C  CG  . PRO B  1 75  ? 172.731 126.547 49.038 1.00   40.87 ? 74   PRO B CG  1 
ATOM   1659  C  CD  . PRO B  1 75  ? 174.217 126.693 49.156 1.00   41.00 ? 74   PRO B CD  1 
ATOM   1660  N  N   . LYS B  1 76  ? 173.088 128.098 45.988 1.00   45.58 ? 75   LYS B N   1 
ATOM   1661  C  CA  . LYS B  1 76  ? 172.682 129.051 44.961 1.00   47.74 ? 75   LYS B CA  1 
ATOM   1662  C  C   . LYS B  1 76  ? 173.814 129.449 44.008 1.00   49.13 ? 75   LYS B C   1 
ATOM   1663  O  O   . LYS B  1 76  ? 173.562 130.158 43.044 1.00   49.34 ? 75   LYS B O   1 
ATOM   1664  C  CB  . LYS B  1 76  ? 172.091 130.310 45.605 1.00   49.14 ? 75   LYS B CB  1 
ATOM   1665  C  CG  . LYS B  1 76  ? 170.908 130.081 46.545 1.00   49.93 ? 75   LYS B CG  1 
ATOM   1666  C  CD  . LYS B  1 76  ? 169.730 129.370 45.865 1.00   49.91 ? 75   LYS B CD  1 
ATOM   1667  C  CE  . LYS B  1 76  ? 168.788 128.720 46.871 1.00   48.62 ? 75   LYS B CE  1 
ATOM   1668  N  NZ  . LYS B  1 76  ? 167.957 127.661 46.237 1.00   48.20 ? 75   LYS B NZ  1 
ATOM   1669  N  N   . ASP B  1 77  ? 175.048 129.011 44.257 1.00   48.97 ? 76   ASP B N   1 
ATOM   1670  C  CA  . ASP B  1 77  ? 176.136 129.280 43.314 1.00   50.30 ? 76   ASP B CA  1 
ATOM   1671  C  C   . ASP B  1 77  ? 176.100 128.264 42.195 1.00   53.52 ? 76   ASP B C   1 
ATOM   1672  O  O   . ASP B  1 77  ? 175.733 127.095 42.403 1.00   53.88 ? 76   ASP B O   1 
ATOM   1673  C  CB  . ASP B  1 77  ? 177.502 129.216 43.984 1.00   49.89 ? 76   ASP B CB  1 
ATOM   1674  C  CG  . ASP B  1 77  ? 177.688 130.291 45.062 1.00   50.24 ? 76   ASP B CG  1 
ATOM   1675  O  OD1 . ASP B  1 77  ? 177.175 131.423 44.891 1.00   50.52 ? 76   ASP B OD1 1 
ATOM   1676  O  OD2 . ASP B  1 77  ? 178.369 130.005 46.071 1.00   47.55 ? 76   ASP B OD2 1 
ATOM   1677  N  N   . GLU B  1 78  ? 176.488 128.705 41.004 1.00   55.62 ? 77   GLU B N   1 
ATOM   1678  C  CA  . GLU B  1 78  ? 176.594 127.808 39.871 1.00   57.90 ? 77   GLU B CA  1 
ATOM   1679  C  C   . GLU B  1 78  ? 177.830 126.935 40.054 1.00   55.88 ? 77   GLU B C   1 
ATOM   1680  O  O   . GLU B  1 78  ? 177.823 125.743 39.726 1.00   55.31 ? 77   GLU B O   1 
ATOM   1681  C  CB  . GLU B  1 78  ? 176.656 128.593 38.552 1.00   63.07 ? 77   GLU B CB  1 
ATOM   1682  C  CG  . GLU B  1 78  ? 176.300 127.767 37.329 1.00   67.14 ? 77   GLU B CG  1 
ATOM   1683  C  CD  . GLU B  1 78  ? 174.834 127.357 37.279 1.00   70.04 ? 77   GLU B CD  1 
ATOM   1684  O  OE1 . GLU B  1 78  ? 174.045 127.831 38.134 1.00   71.34 ? 77   GLU B OE1 1 
ATOM   1685  O  OE2 . GLU B  1 78  ? 174.467 126.565 36.375 1.00   72.05 ? 77   GLU B OE2 1 
ATOM   1686  N  N   . GLU B  1 79  ? 178.887 127.534 40.585 1.00   53.48 ? 78   GLU B N   1 
ATOM   1687  C  CA  . GLU B  1 79  ? 180.078 126.782 40.952 1.00   53.33 ? 78   GLU B CA  1 
ATOM   1688  C  C   . GLU B  1 79  ? 179.920 126.192 42.351 1.00   49.72 ? 78   GLU B C   1 
ATOM   1689  O  O   . GLU B  1 79  ? 180.002 126.910 43.353 1.00   48.50 ? 78   GLU B O   1 
ATOM   1690  C  CB  . GLU B  1 79  ? 181.329 127.666 40.885 1.00   55.43 ? 78   GLU B CB  1 
ATOM   1691  C  CG  . GLU B  1 79  ? 182.214 127.346 39.694 1.00   56.69 ? 78   GLU B CG  1 
ATOM   1692  C  CD  . GLU B  1 79  ? 183.041 126.099 39.909 1.00   55.22 ? 78   GLU B CD  1 
ATOM   1693  O  OE1 . GLU B  1 79  ? 183.662 125.990 40.981 1.00   53.60 ? 78   GLU B OE1 1 
ATOM   1694  O  OE2 . GLU B  1 79  ? 183.079 125.245 38.997 1.00   56.23 ? 78   GLU B OE2 1 
ATOM   1695  N  N   . ARG B  1 80  ? 179.688 124.879 42.396 1.00   47.07 ? 79   ARG B N   1 
ATOM   1696  C  CA  . ARG B  1 80  ? 179.506 124.145 43.652 1.00   43.32 ? 79   ARG B CA  1 
ATOM   1697  C  C   . ARG B  1 80  ? 179.758 122.656 43.460 1.00   41.41 ? 79   ARG B C   1 
ATOM   1698  O  O   . ARG B  1 80  ? 179.855 122.174 42.328 1.00   42.02 ? 79   ARG B O   1 
ATOM   1699  C  CB  . ARG B  1 80  ? 178.075 124.336 44.177 1.00   42.65 ? 79   ARG B CB  1 
ATOM   1700  C  CG  . ARG B  1 80  ? 176.993 123.857 43.215 1.00   42.09 ? 79   ARG B CG  1 
ATOM   1701  C  CD  . ARG B  1 80  ? 175.602 123.952 43.830 1.00   41.51 ? 79   ARG B CD  1 
ATOM   1702  N  NE  . ARG B  1 80  ? 175.191 122.710 44.465 1.00   39.54 ? 79   ARG B NE  1 
ATOM   1703  C  CZ  . ARG B  1 80  ? 173.981 122.485 44.973 1.00   40.19 ? 79   ARG B CZ  1 
ATOM   1704  N  NH1 . ARG B  1 80  ? 173.037 123.417 44.942 1.00   39.93 ? 79   ARG B NH1 1 
ATOM   1705  N  NH2 . ARG B  1 80  ? 173.702 121.305 45.513 1.00   39.32 ? 79   ARG B NH2 1 
ATOM   1706  N  N   . HIS B  1 81  ? 179.859 121.936 44.578 1.00   38.62 ? 80   HIS B N   1 
ATOM   1707  C  CA  . HIS B  1 81  ? 179.765 120.482 44.580 1.00   35.68 ? 80   HIS B CA  1 
ATOM   1708  C  C   . HIS B  1 81  ? 178.304 120.151 44.517 1.00   34.72 ? 80   HIS B C   1 
ATOM   1709  O  O   . HIS B  1 81  ? 177.479 120.916 45.027 1.00   35.23 ? 80   HIS B O   1 
ATOM   1710  C  CB  . HIS B  1 81  ? 180.288 119.883 45.877 1.00   34.56 ? 80   HIS B CB  1 
ATOM   1711  C  CG  . HIS B  1 81  ? 181.693 120.288 46.271 1.00   35.20 ? 80   HIS B CG  1 
ATOM   1712  N  ND1 . HIS B  1 81  ? 182.037 120.550 47.576 1.00   34.01 ? 80   HIS B ND1 1 
ATOM   1713  C  CD2 . HIS B  1 81  ? 182.861 120.418 45.523 1.00   35.04 ? 80   HIS B CD2 1 
ATOM   1714  C  CE1 . HIS B  1 81  ? 183.347 120.785 47.652 1.00   33.96 ? 80   HIS B CE1 1 
ATOM   1715  N  NE2 . HIS B  1 81  ? 183.858 120.727 46.391 1.00   35.89 ? 80   HIS B NE2 1 
ATOM   1716  N  N   . VAL B  1 82  ? 177.943 119.002 43.945 1.00   34.00 ? 81   VAL B N   1 
ATOM   1717  C  CA  . VAL B  1 82  ? 176.541 118.547 43.986 1.00   32.55 ? 81   VAL B CA  1 
ATOM   1718  C  C   . VAL B  1 82  ? 176.058 118.456 45.437 1.00   31.66 ? 81   VAL B C   1 
ATOM   1719  O  O   . VAL B  1 82  ? 174.908 118.787 45.738 1.00   32.15 ? 81   VAL B O   1 
ATOM   1720  C  CB  . VAL B  1 82  ? 176.329 117.197 43.239 1.00   32.43 ? 81   VAL B CB  1 
ATOM   1721  C  CG1 . VAL B  1 82  ? 174.965 116.580 43.552 1.00   31.07 ? 81   VAL B CG1 1 
ATOM   1722  C  CG2 . VAL B  1 82  ? 176.491 117.378 41.735 1.00   32.47 ? 81   VAL B CG2 1 
ATOM   1723  N  N   . GLY B  1 83  ? 176.940 118.055 46.343 1.00   30.68 ? 82   GLY B N   1 
ATOM   1724  C  CA  . GLY B  1 83  ? 176.568 117.910 47.755 1.00   30.22 ? 82   GLY B CA  1 
ATOM   1725  C  C   . GLY B  1 83  ? 176.516 119.171 48.613 1.00   31.02 ? 82   GLY B C   1 
ATOM   1726  O  O   . GLY B  1 83  ? 176.215 119.094 49.810 1.00   29.27 ? 82   GLY B O   1 
ATOM   1727  N  N   . ASP B  1 84  ? 176.775 120.340 48.016 1.00   32.13 ? 83   ASP B N   1 
ATOM   1728  C  CA  . ASP B  1 84  ? 176.841 121.594 48.775 1.00   32.24 ? 83   ASP B CA  1 
ATOM   1729  C  C   . ASP B  1 84  ? 175.467 122.180 49.062 1.00   32.43 ? 83   ASP B C   1 
ATOM   1730  O  O   . ASP B  1 84  ? 174.899 122.901 48.228 1.00   34.32 ? 83   ASP B O   1 
ATOM   1731  C  CB  . ASP B  1 84  ? 177.691 122.619 48.010 1.00   33.44 ? 83   ASP B CB  1 
ATOM   1732  C  CG  . ASP B  1 84  ? 179.168 122.250 47.979 1.00   33.65 ? 83   ASP B CG  1 
ATOM   1733  O  OD1 . ASP B  1 84  ? 179.593 121.385 48.788 1.00   31.33 ? 83   ASP B OD1 1 
ATOM   1734  O  OD2 . ASP B  1 84  ? 179.914 122.809 47.134 1.00   33.98 ? 83   ASP B OD2 1 
ATOM   1735  N  N   . LEU B  1 85  ? 174.942 121.913 50.250 1.00   32.09 ? 84   LEU B N   1 
ATOM   1736  C  CA  . LEU B  1 85  ? 173.613 122.378 50.619 1.00   32.85 ? 84   LEU B CA  1 
ATOM   1737  C  C   . LEU B  1 85  ? 173.641 123.574 51.586 1.00   33.97 ? 84   LEU B C   1 
ATOM   1738  O  O   . LEU B  1 85  ? 172.615 123.949 52.142 1.00   35.32 ? 84   LEU B O   1 
ATOM   1739  C  CB  . LEU B  1 85  ? 172.787 121.210 51.176 1.00   32.10 ? 84   LEU B CB  1 
ATOM   1740  C  CG  . LEU B  1 85  ? 172.365 120.150 50.146 1.00   32.22 ? 84   LEU B CG  1 
ATOM   1741  C  CD1 . LEU B  1 85  ? 171.594 119.024 50.818 1.00   30.82 ? 84   LEU B CD1 1 
ATOM   1742  C  CD2 . LEU B  1 85  ? 171.518 120.777 49.037 1.00   31.79 ? 84   LEU B CD2 1 
ATOM   1743  N  N   . GLY B  1 86  ? 174.811 124.173 51.781 1.00   34.73 ? 85   GLY B N   1 
ATOM   1744  C  CA  . GLY B  1 86  ? 174.905 125.476 52.448 1.00   35.76 ? 85   GLY B CA  1 
ATOM   1745  C  C   . GLY B  1 86  ? 174.820 125.408 53.966 1.00   36.24 ? 85   GLY B C   1 
ATOM   1746  O  O   . GLY B  1 86  ? 175.513 124.590 54.605 1.00   36.74 ? 85   GLY B O   1 
ATOM   1747  N  N   . ASN B  1 87  ? 173.963 126.243 54.550 1.00   35.19 ? 86   ASN B N   1 
ATOM   1748  C  CA  . ASN B  1 87  ? 173.885 126.345 55.993 1.00   35.83 ? 86   ASN B CA  1 
ATOM   1749  C  C   . ASN B  1 87  ? 172.473 126.111 56.517 1.00   35.79 ? 86   ASN B C   1 
ATOM   1750  O  O   . ASN B  1 87  ? 171.489 126.488 55.885 1.00   35.76 ? 86   ASN B O   1 
ATOM   1751  C  CB  . ASN B  1 87  ? 174.380 127.728 56.431 1.00   37.32 ? 86   ASN B CB  1 
ATOM   1752  C  CG  . ASN B  1 87  ? 175.887 127.883 56.288 1.00   37.38 ? 86   ASN B CG  1 
ATOM   1753  O  OD1 . ASN B  1 87  ? 176.660 127.157 56.922 1.00   36.36 ? 86   ASN B OD1 1 
ATOM   1754  N  ND2 . ASN B  1 87  ? 176.312 128.850 55.478 1.00   37.38 ? 86   ASN B ND2 1 
ATOM   1755  N  N   . VAL B  1 88  ? 172.386 125.449 57.663 1.00   35.72 ? 87   VAL B N   1 
ATOM   1756  C  CA  . VAL B  1 88  ? 171.142 125.391 58.423 1.00   35.81 ? 87   VAL B CA  1 
ATOM   1757  C  C   . VAL B  1 88  ? 171.309 126.357 59.599 1.00   36.65 ? 87   VAL B C   1 
ATOM   1758  O  O   . VAL B  1 88  ? 172.437 126.648 60.022 1.00   36.69 ? 87   VAL B O   1 
ATOM   1759  C  CB  . VAL B  1 88  ? 170.811 123.952 58.898 1.00   34.57 ? 87   VAL B CB  1 
ATOM   1760  C  CG1 . VAL B  1 88  ? 170.416 123.087 57.706 1.00   34.17 ? 87   VAL B CG1 1 
ATOM   1761  C  CG2 . VAL B  1 88  ? 171.981 123.338 59.653 1.00   34.02 ? 87   VAL B CG2 1 
ATOM   1762  N  N   . THR B  1 89  ? 170.195 126.873 60.104 1.00   37.10 ? 88   THR B N   1 
ATOM   1763  C  CA  . THR B  1 89  ? 170.227 127.850 61.189 1.00   37.96 ? 88   THR B CA  1 
ATOM   1764  C  C   . THR B  1 89  ? 169.553 127.270 62.413 1.00   37.43 ? 88   THR B C   1 
ATOM   1765  O  O   . THR B  1 89  ? 168.357 126.968 62.372 1.00   36.33 ? 88   THR B O   1 
ATOM   1766  C  CB  . THR B  1 89  ? 169.477 129.148 60.797 1.00   39.55 ? 88   THR B CB  1 
ATOM   1767  O  OG1 . THR B  1 89  ? 170.045 129.686 59.603 1.00   40.05 ? 88   THR B OG1 1 
ATOM   1768  C  CG2 . THR B  1 89  ? 169.572 130.201 61.917 1.00   40.76 ? 88   THR B CG2 1 
ATOM   1769  N  N   . ALA B  1 90  ? 170.319 127.122 63.494 1.00   38.09 ? 89   ALA B N   1 
ATOM   1770  C  CA  . ALA B  1 90  ? 169.784 126.704 64.792 1.00   39.27 ? 89   ALA B CA  1 
ATOM   1771  C  C   . ALA B  1 90  ? 169.352 127.922 65.636 1.00   42.09 ? 89   ALA B C   1 
ATOM   1772  O  O   . ALA B  1 90  ? 170.112 128.881 65.787 1.00   41.78 ? 89   ALA B O   1 
ATOM   1773  C  CB  . ALA B  1 90  ? 170.825 125.902 65.558 1.00   37.59 ? 89   ALA B CB  1 
ATOM   1774  N  N   . ASP B  1 91  ? 168.148 127.826 66.208 1.00   44.17 ? 90   ASP B N   1 
ATOM   1775  C  CA  . ASP B  1 91  ? 167.571 128.844 67.069 1.00   47.53 ? 90   ASP B CA  1 
ATOM   1776  C  C   . ASP B  1 91  ? 168.177 128.752 68.477 1.00   49.95 ? 90   ASP B C   1 
ATOM   1777  O  O   . ASP B  1 91  ? 169.000 127.874 68.751 1.00   48.72 ? 90   ASP B O   1 
ATOM   1778  C  CB  . ASP B  1 91  ? 166.027 128.730 67.083 1.00   47.44 ? 90   ASP B CB  1 
ATOM   1779  C  CG  . ASP B  1 91  ? 165.505 127.506 67.861 1.00   46.66 ? 90   ASP B CG  1 
ATOM   1780  O  OD1 . ASP B  1 91  ? 166.279 126.845 68.602 1.00   45.56 ? 90   ASP B OD1 1 
ATOM   1781  O  OD2 . ASP B  1 91  ? 164.291 127.218 67.743 1.00   44.70 ? 90   ASP B OD2 1 
ATOM   1782  N  N   . LYS B  1 92  ? 167.773 129.649 69.375 1.00   53.00 ? 91   LYS B N   1 
ATOM   1783  C  CA  . LYS B  1 92  ? 168.373 129.680 70.721 1.00   54.55 ? 91   LYS B CA  1 
ATOM   1784  C  C   . LYS B  1 92  ? 168.155 128.419 71.549 1.00   51.97 ? 91   LYS B C   1 
ATOM   1785  O  O   . LYS B  1 92  ? 168.890 128.182 72.501 1.00   49.86 ? 91   LYS B O   1 
ATOM   1786  C  CB  . LYS B  1 92  ? 167.954 130.925 71.518 1.00   59.12 ? 91   LYS B CB  1 
ATOM   1787  C  CG  . LYS B  1 92  ? 166.462 131.135 71.760 1.00   62.86 ? 91   LYS B CG  1 
ATOM   1788  C  CD  . LYS B  1 92  ? 166.259 132.228 72.817 1.00   65.82 ? 91   LYS B CD  1 
ATOM   1789  C  CE  . LYS B  1 92  ? 165.097 133.171 72.510 1.00   68.73 ? 91   LYS B CE  1 
ATOM   1790  N  NZ  . LYS B  1 92  ? 163.768 132.504 72.607 1.00   70.48 ? 91   LYS B NZ  1 
ATOM   1791  N  N   . ASP B  1 93  ? 167.168 127.613 71.168 1.00   49.64 ? 92   ASP B N   1 
ATOM   1792  C  CA  . ASP B  1 93  ? 166.938 126.309 71.773 1.00   48.50 ? 92   ASP B CA  1 
ATOM   1793  C  C   . ASP B  1 93  ? 167.804 125.210 71.127 1.00   46.19 ? 92   ASP B C   1 
ATOM   1794  O  O   . ASP B  1 93  ? 167.682 124.046 71.481 1.00   44.02 ? 92   ASP B O   1 
ATOM   1795  C  CB  . ASP B  1 93  ? 165.459 125.917 71.638 1.00   49.78 ? 92   ASP B CB  1 
ATOM   1796  C  CG  . ASP B  1 93  ? 164.513 126.959 72.221 1.00   52.69 ? 92   ASP B CG  1 
ATOM   1797  O  OD1 . ASP B  1 93  ? 164.429 127.061 73.467 1.00   54.13 ? 92   ASP B OD1 1 
ATOM   1798  O  OD2 . ASP B  1 93  ? 163.844 127.666 71.428 1.00   54.39 ? 92   ASP B OD2 1 
ATOM   1799  N  N   . GLY B  1 94  ? 168.659 125.578 70.180 1.00   45.26 ? 93   GLY B N   1 
ATOM   1800  C  CA  . GLY B  1 94  ? 169.469 124.616 69.447 1.00   43.26 ? 93   GLY B CA  1 
ATOM   1801  C  C   . GLY B  1 94  ? 168.735 123.844 68.354 1.00   41.23 ? 93   GLY B C   1 
ATOM   1802  O  O   . GLY B  1 94  ? 169.255 122.847 67.869 1.00   38.98 ? 93   GLY B O   1 
ATOM   1803  N  N   . VAL B  1 95  ? 167.549 124.310 67.956 1.00   40.58 ? 94   VAL B N   1 
ATOM   1804  C  CA  . VAL B  1 95  ? 166.731 123.639 66.936 1.00   39.98 ? 94   VAL B CA  1 
ATOM   1805  C  C   . VAL B  1 95  ? 166.777 124.361 65.588 1.00   40.50 ? 94   VAL B C   1 
ATOM   1806  O  O   . VAL B  1 95  ? 166.373 125.531 65.465 1.00   39.91 ? 94   VAL B O   1 
ATOM   1807  C  CB  . VAL B  1 95  ? 165.241 123.567 67.351 1.00   40.98 ? 94   VAL B CB  1 
ATOM   1808  C  CG1 . VAL B  1 95  ? 164.409 122.889 66.256 1.00   38.83 ? 94   VAL B CG1 1 
ATOM   1809  C  CG2 . VAL B  1 95  ? 165.085 122.859 68.685 1.00   40.06 ? 94   VAL B CG2 1 
ATOM   1810  N  N   . ALA B  1 96  ? 167.262 123.650 64.577 1.00   39.50 ? 95   ALA B N   1 
ATOM   1811  C  CA  . ALA B  1 96  ? 167.272 124.133 63.205 1.00   38.66 ? 95   ALA B CA  1 
ATOM   1812  C  C   . ALA B  1 96  ? 166.081 123.535 62.483 1.00   39.59 ? 95   ALA B C   1 
ATOM   1813  O  O   . ALA B  1 96  ? 165.977 122.318 62.372 1.00   39.09 ? 95   ALA B O   1 
ATOM   1814  C  CB  . ALA B  1 96  ? 168.562 123.729 62.514 1.00   36.82 ? 95   ALA B CB  1 
ATOM   1815  N  N   . ASP B  1 97  ? 165.173 124.378 62.005 1.00   40.58 ? 96   ASP B N   1 
ATOM   1816  C  CA  . ASP B  1 97  ? 164.073 123.904 61.180 1.00   42.09 ? 96   ASP B CA  1 
ATOM   1817  C  C   . ASP B  1 97  ? 164.465 124.081 59.718 1.00   40.92 ? 96   ASP B C   1 
ATOM   1818  O  O   . ASP B  1 97  ? 164.540 125.187 59.228 1.00   41.84 ? 96   ASP B O   1 
ATOM   1819  C  CB  . ASP B  1 97  ? 162.771 124.625 61.552 1.00   44.10 ? 96   ASP B CB  1 
ATOM   1820  C  CG  . ASP B  1 97  ? 162.259 124.218 62.943 1.00   46.29 ? 96   ASP B CG  1 
ATOM   1821  O  OD1 . ASP B  1 97  ? 162.213 123.002 63.276 1.00   47.08 ? 96   ASP B OD1 1 
ATOM   1822  O  OD2 . ASP B  1 97  ? 161.915 125.116 63.726 1.00   49.58 ? 96   ASP B OD2 1 
ATOM   1823  N  N   . VAL B  1 98  ? 164.767 122.978 59.042 1.00   40.91 ? 97   VAL B N   1 
ATOM   1824  C  CA  . VAL B  1 98  ? 165.302 123.011 57.670 1.00   40.68 ? 97   VAL B CA  1 
ATOM   1825  C  C   . VAL B  1 98  ? 164.165 122.981 56.658 1.00   40.71 ? 97   VAL B C   1 
ATOM   1826  O  O   . VAL B  1 98  ? 163.174 122.264 56.839 1.00   39.30 ? 97   VAL B O   1 
ATOM   1827  C  CB  . VAL B  1 98  ? 166.232 121.802 57.398 1.00   40.77 ? 97   VAL B CB  1 
ATOM   1828  C  CG1 . VAL B  1 98  ? 166.694 121.768 55.940 1.00   39.65 ? 97   VAL B CG1 1 
ATOM   1829  C  CG2 . VAL B  1 98  ? 167.427 121.808 58.346 1.00   39.62 ? 97   VAL B CG2 1 
ATOM   1830  N  N   . SER B  1 99  ? 164.305 123.789 55.609 1.00   42.56 ? 98   SER B N   1 
ATOM   1831  C  CA  . SER B  1 99  ? 163.385 123.782 54.461 1.00   43.03 ? 98   SER B CA  1 
ATOM   1832  C  C   . SER B  1 99  ? 164.120 124.387 53.285 1.00   43.39 ? 98   SER B C   1 
ATOM   1833  O  O   . SER B  1 99  ? 164.296 125.591 53.206 1.00   42.86 ? 98   SER B O   1 
ATOM   1834  C  CB  . SER B  1 99  ? 162.082 124.553 54.733 1.00   44.40 ? 98   SER B CB  1 
ATOM   1835  O  OG  . SER B  1 99  ? 161.029 124.040 53.910 1.00   45.14 ? 98   SER B OG  1 
ATOM   1836  N  N   . ILE B  1 100 ? 164.583 123.518 52.402 1.00   42.79 ? 99   ILE B N   1 
ATOM   1837  C  CA  . ILE B  1 100 ? 165.392 123.880 51.259 1.00   42.77 ? 99   ILE B CA  1 
ATOM   1838  C  C   . ILE B  1 100 ? 164.693 123.304 50.045 1.00   42.91 ? 99   ILE B C   1 
ATOM   1839  O  O   . ILE B  1 100 ? 163.898 122.356 50.144 1.00   40.44 ? 99   ILE B O   1 
ATOM   1840  C  CB  . ILE B  1 100 ? 166.786 123.209 51.331 1.00   43.50 ? 99   ILE B CB  1 
ATOM   1841  C  CG1 . ILE B  1 100 ? 167.546 123.610 52.581 1.00   45.69 ? 99   ILE B CG1 1 
ATOM   1842  C  CG2 . ILE B  1 100 ? 167.651 123.570 50.141 1.00   45.76 ? 99   ILE B CG2 1 
ATOM   1843  C  CD1 . ILE B  1 100 ? 168.809 122.790 52.772 1.00   44.79 ? 99   ILE B CD1 1 
ATOM   1844  N  N   . GLU B  1 101 ? 164.983 123.899 48.898 1.00   44.12 ? 100  GLU B N   1 
ATOM   1845  C  CA  . GLU B  1 101 ? 164.686 123.297 47.624 1.00   42.94 ? 100  GLU B CA  1 
ATOM   1846  C  C   . GLU B  1 101 ? 165.987 123.370 46.855 1.00   40.20 ? 100  GLU B C   1 
ATOM   1847  O  O   . GLU B  1 101 ? 166.736 124.325 47.032 1.00   39.29 ? 100  GLU B O   1 
ATOM   1848  C  CB  . GLU B  1 101 ? 163.562 124.047 46.927 1.00   47.08 ? 100  GLU B CB  1 
ATOM   1849  C  CG  . GLU B  1 101 ? 162.702 123.137 46.075 1.00   49.40 ? 100  GLU B CG  1 
ATOM   1850  C  CD  . GLU B  1 101 ? 161.661 123.892 45.289 1.00   53.19 ? 100  GLU B CD  1 
ATOM   1851  O  OE1 . GLU B  1 101 ? 162.052 124.613 44.345 1.00   55.93 ? 100  GLU B OE1 1 
ATOM   1852  O  OE2 . GLU B  1 101 ? 160.461 123.750 45.614 1.00   55.35 ? 100  GLU B OE2 1 
ATOM   1853  N  N   . ASP B  1 102 ? 166.285 122.350 46.051 1.00   37.51 ? 101  ASP B N   1 
ATOM   1854  C  CA  . ASP B  1 102 ? 167.556 122.296 45.312 1.00   36.81 ? 101  ASP B CA  1 
ATOM   1855  C  C   . ASP B  1 102 ? 167.423 121.567 43.981 1.00   36.24 ? 101  ASP B C   1 
ATOM   1856  O  O   . ASP B  1 102 ? 166.771 120.527 43.909 1.00   35.52 ? 101  ASP B O   1 
ATOM   1857  C  CB  . ASP B  1 102 ? 168.613 121.588 46.155 1.00   36.18 ? 101  ASP B CB  1 
ATOM   1858  C  CG  . ASP B  1 102 ? 170.018 121.800 45.638 1.00   36.35 ? 101  ASP B CG  1 
ATOM   1859  O  OD1 . ASP B  1 102 ? 170.601 122.862 45.925 1.00   38.71 ? 101  ASP B OD1 1 
ATOM   1860  O  OD2 . ASP B  1 102 ? 170.569 120.903 44.971 1.00   36.32 ? 101  ASP B OD2 1 
ATOM   1861  N  N   . SER B  1 103 ? 168.086 122.084 42.948 1.00   36.71 ? 102  SER B N   1 
ATOM   1862  C  CA  . SER B  1 103 ? 167.960 121.547 41.578 1.00   36.82 ? 102  SER B CA  1 
ATOM   1863  C  C   . SER B  1 103 ? 169.224 120.878 41.077 1.00   35.41 ? 102  SER B C   1 
ATOM   1864  O  O   . SER B  1 103 ? 169.287 120.465 39.920 1.00   34.97 ? 102  SER B O   1 
ATOM   1865  C  CB  . SER B  1 103 ? 167.620 122.662 40.605 1.00   38.73 ? 102  SER B CB  1 
ATOM   1866  O  OG  . SER B  1 103 ? 166.581 123.460 41.110 1.00   41.72 ? 102  SER B OG  1 
ATOM   1867  N  N   . VAL B  1 104 ? 170.234 120.772 41.929 1.00   34.28 ? 103  VAL B N   1 
ATOM   1868  C  CA  . VAL B  1 104 ? 171.480 120.141 41.526 1.00   33.39 ? 103  VAL B CA  1 
ATOM   1869  C  C   . VAL B  1 104 ? 171.532 118.699 42.029 1.00   32.75 ? 103  VAL B C   1 
ATOM   1870  O  O   . VAL B  1 104 ? 171.876 117.787 41.266 1.00   31.88 ? 103  VAL B O   1 
ATOM   1871  C  CB  . VAL B  1 104 ? 172.664 120.992 41.975 1.00   33.81 ? 103  VAL B CB  1 
ATOM   1872  C  CG1 . VAL B  1 104 ? 173.988 120.267 41.776 1.00   33.04 ? 103  VAL B CG1 1 
ATOM   1873  C  CG2 . VAL B  1 104 ? 172.622 122.311 41.194 1.00   34.63 ? 103  VAL B CG2 1 
ATOM   1874  N  N   . ILE B  1 105 ? 171.171 118.483 43.295 1.00   32.15 ? 104  ILE B N   1 
ATOM   1875  C  CA  . ILE B  1 105 ? 171.043 117.109 43.817 1.00   30.27 ? 104  ILE B CA  1 
ATOM   1876  C  C   . ILE B  1 105 ? 169.834 116.411 43.171 1.00   30.13 ? 104  ILE B C   1 
ATOM   1877  O  O   . ILE B  1 105 ? 168.845 117.062 42.796 1.00   30.37 ? 104  ILE B O   1 
ATOM   1878  C  CB  . ILE B  1 105 ? 170.892 117.068 45.354 1.00   29.24 ? 104  ILE B CB  1 
ATOM   1879  C  CG1 . ILE B  1 105 ? 169.558 117.679 45.809 1.00   29.59 ? 104  ILE B CG1 1 
ATOM   1880  C  CG2 . ILE B  1 105 ? 172.081 117.719 46.043 1.00   29.01 ? 104  ILE B CG2 1 
ATOM   1881  C  CD1 . ILE B  1 105 ? 169.394 117.711 47.307 1.00   29.76 ? 104  ILE B CD1 1 
ATOM   1882  N  N   . SER B  1 106 ? 169.907 115.090 43.054 1.00   29.40 ? 105  SER B N   1 
ATOM   1883  C  CA  . SER B  1 106 ? 168.771 114.296 42.619 1.00   28.99 ? 105  SER B CA  1 
ATOM   1884  C  C   . SER B  1 106 ? 168.556 113.057 43.492 1.00   28.28 ? 105  SER B C   1 
ATOM   1885  O  O   . SER B  1 106 ? 169.425 112.654 44.278 1.00   27.45 ? 105  SER B O   1 
ATOM   1886  C  CB  . SER B  1 106 ? 168.950 113.876 41.158 1.00   29.68 ? 105  SER B CB  1 
ATOM   1887  O  OG  . SER B  1 106 ? 167.706 113.463 40.605 1.00   28.92 ? 105  SER B OG  1 
ATOM   1888  N  N   . LEU B  1 107 ? 167.368 112.479 43.375 1.00   27.74 ? 106  LEU B N   1 
ATOM   1889  C  CA  . LEU B  1 107 ? 167.095 111.170 43.949 1.00   26.45 ? 106  LEU B CA  1 
ATOM   1890  C  C   . LEU B  1 107 ? 167.171 110.056 42.892 1.00   27.11 ? 106  LEU B C   1 
ATOM   1891  O  O   . LEU B  1 107 ? 166.923 108.916 43.218 1.00   26.79 ? 106  LEU B O   1 
ATOM   1892  C  CB  . LEU B  1 107 ? 165.757 111.147 44.689 1.00   25.88 ? 106  LEU B CB  1 
ATOM   1893  C  CG  . LEU B  1 107 ? 165.561 112.228 45.763 1.00   26.28 ? 106  LEU B CG  1 
ATOM   1894  C  CD1 . LEU B  1 107 ? 164.189 112.082 46.410 1.00   26.11 ? 106  LEU B CD1 1 
ATOM   1895  C  CD2 . LEU B  1 107 ? 166.676 112.245 46.807 1.00   25.69 ? 106  LEU B CD2 1 
ATOM   1896  N  N   . SER B  1 108 ? 167.522 110.384 41.645 1.00   28.18 ? 107  SER B N   1 
ATOM   1897  C  CA  . SER B  1 108 ? 167.809 109.366 40.622 1.00   29.31 ? 107  SER B CA  1 
ATOM   1898  C  C   . SER B  1 108 ? 168.919 109.854 39.689 1.00   30.56 ? 107  SER B C   1 
ATOM   1899  O  O   . SER B  1 108 ? 169.270 111.026 39.715 1.00   29.83 ? 107  SER B O   1 
ATOM   1900  C  CB  . SER B  1 108 ? 166.538 109.005 39.829 1.00   29.11 ? 107  SER B CB  1 
ATOM   1901  O  OG  . SER B  1 108 ? 165.912 110.161 39.293 1.00   29.19 ? 107  SER B OG  1 
ATOM   1902  N  N   . GLY B  1 109 ? 169.484 108.939 38.896 1.00   32.20 ? 108  GLY B N   1 
ATOM   1903  C  CA  . GLY B  1 109 ? 170.590 109.258 37.974 1.00   34.55 ? 108  GLY B CA  1 
ATOM   1904  C  C   . GLY B  1 109 ? 171.951 109.528 38.602 1.00   36.24 ? 108  GLY B C   1 
ATOM   1905  O  O   . GLY B  1 109 ? 172.197 109.214 39.771 1.00   36.57 ? 108  GLY B O   1 
ATOM   1906  N  N   . ASP B  1 110 ? 172.846 110.114 37.818 1.00   39.41 ? 109  ASP B N   1 
ATOM   1907  C  CA  . ASP B  1 110 ? 174.241 110.344 38.236 1.00   40.28 ? 109  ASP B CA  1 
ATOM   1908  C  C   . ASP B  1 110 ? 174.434 111.294 39.410 1.00   39.65 ? 109  ASP B C   1 
ATOM   1909  O  O   . ASP B  1 110 ? 175.439 111.208 40.128 1.00   38.76 ? 109  ASP B O   1 
ATOM   1910  C  CB  . ASP B  1 110 ? 175.067 110.890 37.065 1.00   44.02 ? 109  ASP B CB  1 
ATOM   1911  C  CG  . ASP B  1 110 ? 175.339 109.849 35.997 1.00   45.32 ? 109  ASP B CG  1 
ATOM   1912  O  OD1 . ASP B  1 110 ? 174.962 108.658 36.169 1.00   45.09 ? 109  ASP B OD1 1 
ATOM   1913  O  OD2 . ASP B  1 110 ? 175.955 110.243 34.982 1.00   47.96 ? 109  ASP B OD2 1 
ATOM   1914  N  N   . HIS B  1 111 ? 173.504 112.219 39.598 1.00   38.47 ? 110  HIS B N   1 
ATOM   1915  C  CA  . HIS B  1 111 ? 173.568 113.101 40.767 1.00   37.60 ? 110  HIS B CA  1 
ATOM   1916  C  C   . HIS B  1 111 ? 172.730 112.567 41.902 1.00   35.61 ? 110  HIS B C   1 
ATOM   1917  O  O   . HIS B  1 111 ? 172.415 113.306 42.846 1.00   35.66 ? 110  HIS B O   1 
ATOM   1918  C  CB  . HIS B  1 111 ? 173.160 114.536 40.402 1.00   39.02 ? 110  HIS B CB  1 
ATOM   1919  C  CG  . HIS B  1 111 ? 174.153 115.246 39.507 1.00   40.51 ? 110  HIS B CG  1 
ATOM   1920  N  ND1 . HIS B  1 111 ? 174.108 116.580 39.280 1.00   42.26 ? 110  HIS B ND1 1 
ATOM   1921  C  CD2 . HIS B  1 111 ? 175.240 114.764 38.781 1.00   40.92 ? 110  HIS B CD2 1 
ATOM   1922  C  CE1 . HIS B  1 111 ? 175.106 116.923 38.442 1.00   42.06 ? 110  HIS B CE1 1 
ATOM   1923  N  NE2 . HIS B  1 111 ? 175.802 115.814 38.146 1.00   42.27 ? 110  HIS B NE2 1 
ATOM   1924  N  N   . CYS B  1 112 ? 172.376 111.278 41.840 1.00   32.88 ? 111  CYS B N   1 
ATOM   1925  C  CA  . CYS B  1 112 ? 171.663 110.619 42.930 1.00   31.30 ? 111  CYS B CA  1 
ATOM   1926  C  C   . CYS B  1 112 ? 172.473 110.704 44.215 1.00   29.06 ? 111  CYS B C   1 
ATOM   1927  O  O   . CYS B  1 112 ? 173.662 110.376 44.218 1.00   29.04 ? 111  CYS B O   1 
ATOM   1928  C  CB  . CYS B  1 112 ? 171.426 109.142 42.610 1.00   32.83 ? 111  CYS B CB  1 
ATOM   1929  S  SG  . CYS B  1 112 ? 170.268 108.345 43.725 1.00   34.54 ? 111  CYS B SG  1 
ATOM   1930  N  N   . ILE B  1 113 ? 171.819 111.131 45.293 1.00   26.52 ? 112  ILE B N   1 
ATOM   1931  C  CA  . ILE B  1 113 ? 172.437 111.190 46.615 1.00   25.57 ? 112  ILE B CA  1 
ATOM   1932  C  C   . ILE B  1 113 ? 172.024 110.007 47.515 1.00   24.65 ? 112  ILE B C   1 
ATOM   1933  O  O   . ILE B  1 113 ? 172.560 109.827 48.601 1.00   23.86 ? 112  ILE B O   1 
ATOM   1934  C  CB  . ILE B  1 113 ? 172.150 112.539 47.321 1.00   24.81 ? 112  ILE B CB  1 
ATOM   1935  C  CG1 . ILE B  1 113 ? 170.648 112.751 47.567 1.00   24.45 ? 112  ILE B CG1 1 
ATOM   1936  C  CG2 . ILE B  1 113 ? 172.731 113.686 46.498 1.00   25.59 ? 112  ILE B CG2 1 
ATOM   1937  C  CD1 . ILE B  1 113 ? 170.334 114.014 48.351 1.00   24.41 ? 112  ILE B CD1 1 
ATOM   1938  N  N   . ILE B  1 114 ? 171.072 109.201 47.063 1.00   24.08 ? 113  ILE B N   1 
ATOM   1939  C  CA  . ILE B  1 114 ? 170.642 108.069 47.846 1.00   23.02 ? 113  ILE B CA  1 
ATOM   1940  C  C   . ILE B  1 114 ? 171.832 107.152 48.044 1.00   22.19 ? 113  ILE B C   1 
ATOM   1941  O  O   . ILE B  1 114 ? 172.604 106.927 47.121 1.00   22.07 ? 113  ILE B O   1 
ATOM   1942  C  CB  . ILE B  1 114 ? 169.497 107.310 47.176 1.00   23.23 ? 113  ILE B CB  1 
ATOM   1943  C  CG1 . ILE B  1 114 ? 168.228 108.150 47.204 1.00   23.29 ? 113  ILE B CG1 1 
ATOM   1944  C  CG2 . ILE B  1 114 ? 169.233 106.019 47.932 1.00   22.47 ? 113  ILE B CG2 1 
ATOM   1945  C  CD1 . ILE B  1 114 ? 167.138 107.562 46.347 1.00   23.92 ? 113  ILE B CD1 1 
ATOM   1946  N  N   . GLY B  1 115 ? 172.017 106.681 49.273 1.00   21.11 ? 114  GLY B N   1 
ATOM   1947  C  CA  . GLY B  1 115 ? 173.170 105.851 49.591 1.00   20.59 ? 114  GLY B CA  1 
ATOM   1948  C  C   . GLY B  1 115 ? 174.438 106.603 49.936 1.00   20.72 ? 114  GLY B C   1 
ATOM   1949  O  O   . GLY B  1 115 ? 175.466 105.979 50.220 1.00   19.71 ? 114  GLY B O   1 
ATOM   1950  N  N   . ARG B  1 116 ? 174.374 107.935 49.921 1.00   21.07 ? 115  ARG B N   1 
ATOM   1951  C  CA  . ARG B  1 116 ? 175.504 108.773 50.339 1.00   21.64 ? 115  ARG B CA  1 
ATOM   1952  C  C   . ARG B  1 116 ? 175.203 109.308 51.745 1.00   21.36 ? 115  ARG B C   1 
ATOM   1953  O  O   . ARG B  1 116 ? 174.185 108.964 52.322 1.00   21.75 ? 115  ARG B O   1 
ATOM   1954  C  CB  . ARG B  1 116 ? 175.745 109.883 49.294 1.00   22.29 ? 115  ARG B CB  1 
ATOM   1955  C  CG  . ARG B  1 116 ? 175.959 109.286 47.920 1.00   22.98 ? 115  ARG B CG  1 
ATOM   1956  C  CD  . ARG B  1 116 ? 176.328 110.262 46.815 1.00   24.08 ? 115  ARG B CD  1 
ATOM   1957  N  NE  . ARG B  1 116 ? 176.391 109.556 45.525 1.00   23.99 ? 115  ARG B NE  1 
ATOM   1958  C  CZ  . ARG B  1 116 ? 177.451 108.888 45.063 1.00   24.06 ? 115  ARG B CZ  1 
ATOM   1959  N  NH1 . ARG B  1 116 ? 178.590 108.801 45.753 1.00   23.95 ? 115  ARG B NH1 1 
ATOM   1960  N  NH2 . ARG B  1 116 ? 177.375 108.293 43.880 1.00   24.05 ? 115  ARG B NH2 1 
ATOM   1961  N  N   . THR B  1 117 ? 176.083 110.122 52.309 1.00   21.81 ? 116  THR B N   1 
ATOM   1962  C  CA  . THR B  1 117 ? 175.944 110.580 53.700 1.00   22.06 ? 116  THR B CA  1 
ATOM   1963  C  C   . THR B  1 117 ? 175.642 112.067 53.796 1.00   22.65 ? 116  THR B C   1 
ATOM   1964  O  O   . THR B  1 117 ? 176.406 112.876 53.302 1.00   23.41 ? 116  THR B O   1 
ATOM   1965  C  CB  . THR B  1 117 ? 177.245 110.278 54.457 1.00   22.15 ? 116  THR B CB  1 
ATOM   1966  O  OG1 . THR B  1 117 ? 177.387 108.861 54.542 1.00   21.66 ? 116  THR B OG1 1 
ATOM   1967  C  CG2 . THR B  1 117 ? 177.289 110.911 55.873 1.00   21.88 ? 116  THR B CG2 1 
ATOM   1968  N  N   . LEU B  1 118 ? 174.536 112.416 54.447 1.00   22.57 ? 117  LEU B N   1 
ATOM   1969  C  CA  . LEU B  1 118 ? 174.237 113.809 54.799 1.00   22.79 ? 117  LEU B CA  1 
ATOM   1970  C  C   . LEU B  1 118 ? 174.974 114.120 56.101 1.00   23.19 ? 117  LEU B C   1 
ATOM   1971  O  O   . LEU B  1 118 ? 174.959 113.317 57.016 1.00   22.37 ? 117  LEU B O   1 
ATOM   1972  C  CB  . LEU B  1 118 ? 172.737 113.984 55.010 1.00   22.57 ? 117  LEU B CB  1 
ATOM   1973  C  CG  . LEU B  1 118 ? 172.174 115.370 55.309 1.00   22.83 ? 117  LEU B CG  1 
ATOM   1974  C  CD1 . LEU B  1 118 ? 172.460 116.338 54.173 1.00   23.25 ? 117  LEU B CD1 1 
ATOM   1975  C  CD2 . LEU B  1 118 ? 170.683 115.268 55.559 1.00   22.93 ? 117  LEU B CD2 1 
ATOM   1976  N  N   . VAL B  1 119 ? 175.637 115.272 56.161 1.00   23.87 ? 118  VAL B N   1 
ATOM   1977  C  CA  . VAL B  1 119 ? 176.437 115.683 57.326 1.00   24.30 ? 118  VAL B CA  1 
ATOM   1978  C  C   . VAL B  1 119 ? 176.074 117.101 57.744 1.00   25.71 ? 118  VAL B C   1 
ATOM   1979  O  O   . VAL B  1 119 ? 175.940 117.986 56.886 1.00   27.36 ? 118  VAL B O   1 
ATOM   1980  C  CB  . VAL B  1 119 ? 177.943 115.674 56.996 1.00   24.11 ? 118  VAL B CB  1 
ATOM   1981  C  CG1 . VAL B  1 119 ? 178.766 116.357 58.098 1.00   24.68 ? 118  VAL B CG1 1 
ATOM   1982  C  CG2 . VAL B  1 119 ? 178.431 114.270 56.742 1.00   22.74 ? 118  VAL B CG2 1 
ATOM   1983  N  N   . VAL B  1 120 ? 175.912 117.318 59.047 1.00   26.15 ? 119  VAL B N   1 
ATOM   1984  C  CA  . VAL B  1 120 ? 175.746 118.670 59.614 1.00   27.05 ? 119  VAL B CA  1 
ATOM   1985  C  C   . VAL B  1 120 ? 176.991 118.990 60.420 1.00   28.12 ? 119  VAL B C   1 
ATOM   1986  O  O   . VAL B  1 120 ? 177.511 118.140 61.153 1.00   27.97 ? 119  VAL B O   1 
ATOM   1987  C  CB  . VAL B  1 120 ? 174.482 118.806 60.498 1.00   26.73 ? 119  VAL B CB  1 
ATOM   1988  C  CG1 . VAL B  1 120 ? 174.499 117.791 61.631 1.00   25.39 ? 119  VAL B CG1 1 
ATOM   1989  C  CG2 . VAL B  1 120 ? 174.337 120.239 61.018 1.00   26.92 ? 119  VAL B CG2 1 
ATOM   1990  N  N   . HIS B  1 121 ? 177.467 120.219 60.289 1.00   29.63 ? 120  HIS B N   1 
ATOM   1991  C  CA  . HIS B  1 121 ? 178.822 120.570 60.741 1.00   31.28 ? 120  HIS B CA  1 
ATOM   1992  C  C   . HIS B  1 121 ? 178.913 121.436 61.965 1.00   32.77 ? 120  HIS B C   1 
ATOM   1993  O  O   . HIS B  1 121 ? 177.940 122.050 62.405 1.00   32.47 ? 120  HIS B O   1 
ATOM   1994  C  CB  . HIS B  1 121 ? 179.561 121.278 59.620 1.00   31.89 ? 120  HIS B CB  1 
ATOM   1995  C  CG  . HIS B  1 121 ? 180.256 120.352 58.677 1.00   31.11 ? 120  HIS B CG  1 
ATOM   1996  N  ND1 . HIS B  1 121 ? 181.535 119.985 58.853 1.00   31.56 ? 120  HIS B ND1 1 
ATOM   1997  C  CD2 . HIS B  1 121 ? 179.817 119.729 57.511 1.00   30.57 ? 120  HIS B CD2 1 
ATOM   1998  C  CE1 . HIS B  1 121 ? 181.891 119.139 57.868 1.00   31.11 ? 120  HIS B CE1 1 
ATOM   1999  N  NE2 . HIS B  1 121 ? 180.841 118.993 57.038 1.00   30.18 ? 120  HIS B NE2 1 
ATOM   2000  N  N   . GLU B  1 122 ? 180.134 121.492 62.492 1.00   35.21 ? 121  GLU B N   1 
ATOM   2001  C  CA  . GLU B  1 122 ? 180.492 122.292 63.650 1.00   36.82 ? 121  GLU B CA  1 
ATOM   2002  C  C   . GLU B  1 122 ? 180.267 123.794 63.445 1.00   38.74 ? 121  GLU B C   1 
ATOM   2003  O  O   . GLU B  1 122 ? 179.569 124.442 64.232 1.00   38.89 ? 121  GLU B O   1 
ATOM   2004  C  CB  . GLU B  1 122 ? 181.963 122.040 63.946 1.00   39.02 ? 121  GLU B CB  1 
ATOM   2005  C  CG  . GLU B  1 122 ? 182.558 122.915 65.043 1.00   41.43 ? 121  GLU B CG  1 
ATOM   2006  C  CD  . GLU B  1 122 ? 183.972 122.504 65.379 1.00   43.37 ? 121  GLU B CD  1 
ATOM   2007  O  OE1 . GLU B  1 122 ? 184.792 122.307 64.457 1.00   42.71 ? 121  GLU B OE1 1 
ATOM   2008  O  OE2 . GLU B  1 122 ? 184.264 122.357 66.583 1.00   49.80 ? 121  GLU B OE2 1 
ATOM   2009  N  N   . LYS B  1 123 ? 180.865 124.325 62.380 1.00   39.74 ? 122  LYS B N   1 
ATOM   2010  C  CA  . LYS B  1 123 ? 180.872 125.757 62.087 1.00   41.27 ? 122  LYS B CA  1 
ATOM   2011  C  C   . LYS B  1 123 ? 179.994 126.106 60.878 1.00   40.66 ? 122  LYS B C   1 
ATOM   2012  O  O   . LYS B  1 123 ? 179.522 125.236 60.153 1.00   39.57 ? 122  LYS B O   1 
ATOM   2013  C  CB  . LYS B  1 123 ? 182.302 126.225 61.780 1.00   43.14 ? 122  LYS B CB  1 
ATOM   2014  C  CG  . LYS B  1 123 ? 183.374 125.845 62.805 1.00   45.00 ? 122  LYS B CG  1 
ATOM   2015  C  CD  . LYS B  1 123 ? 184.740 126.394 62.389 1.00   46.82 ? 122  LYS B CD  1 
ATOM   2016  C  CE  . LYS B  1 123 ? 185.904 125.618 62.995 1.00   47.99 ? 122  LYS B CE  1 
ATOM   2017  N  NZ  . LYS B  1 123 ? 186.345 126.162 64.315 1.00   49.71 ? 122  LYS B NZ  1 
ATOM   2018  N  N   . ALA B  1 124 ? 179.802 127.397 60.664 1.00   40.06 ? 123  ALA B N   1 
ATOM   2019  C  CA  . ALA B  1 124 ? 179.206 127.893 59.434 1.00   41.30 ? 123  ALA B CA  1 
ATOM   2020  C  C   . ALA B  1 124 ? 180.051 127.466 58.220 1.00   40.94 ? 123  ALA B C   1 
ATOM   2021  O  O   . ALA B  1 124 ? 181.294 127.409 58.298 1.00   40.09 ? 123  ALA B O   1 
ATOM   2022  C  CB  . ALA B  1 124 ? 179.045 129.423 59.479 1.00   40.46 ? 123  ALA B CB  1 
ATOM   2023  N  N   . ASP B  1 125 ? 179.353 127.119 57.136 1.00   39.77 ? 124  ASP B N   1 
ATOM   2024  C  CA  . ASP B  1 125 ? 179.958 126.989 55.815 1.00   41.11 ? 124  ASP B CA  1 
ATOM   2025  C  C   . ASP B  1 125 ? 180.140 128.389 55.224 1.00   43.14 ? 124  ASP B C   1 
ATOM   2026  O  O   . ASP B  1 125 ? 179.154 129.130 55.094 1.00   43.23 ? 124  ASP B O   1 
ATOM   2027  C  CB  . ASP B  1 125 ? 179.028 126.199 54.903 1.00   40.18 ? 124  ASP B CB  1 
ATOM   2028  C  CG  . ASP B  1 125 ? 179.694 125.754 53.614 1.00   40.64 ? 124  ASP B CG  1 
ATOM   2029  O  OD1 . ASP B  1 125 ? 180.621 126.423 53.120 1.00   42.69 ? 124  ASP B OD1 1 
ATOM   2030  O  OD2 . ASP B  1 125 ? 179.263 124.719 53.072 1.00   41.03 ? 124  ASP B OD2 1 
ATOM   2031  N  N   . ASP B  1 126 ? 181.369 128.737 54.833 1.00   44.70 ? 125  ASP B N   1 
ATOM   2032  C  CA  . ASP B  1 126 ? 181.641 130.089 54.294 1.00   47.56 ? 125  ASP B CA  1 
ATOM   2033  C  C   . ASP B  1 126 ? 181.283 130.193 52.803 1.00   47.68 ? 125  ASP B C   1 
ATOM   2034  O  O   . ASP B  1 126 ? 181.684 131.140 52.124 1.00   48.10 ? 125  ASP B O   1 
ATOM   2035  C  CB  . ASP B  1 126 ? 183.097 130.537 54.568 1.00   48.75 ? 125  ASP B CB  1 
ATOM   2036  C  CG  . ASP B  1 126 ? 184.140 129.717 53.804 1.00   49.46 ? 125  ASP B CG  1 
ATOM   2037  O  OD1 . ASP B  1 126 ? 183.846 129.216 52.702 1.00   50.72 ? 125  ASP B OD1 1 
ATOM   2038  O  OD2 . ASP B  1 126 ? 185.275 129.593 54.307 1.00   49.68 ? 125  ASP B OD2 1 
ATOM   2039  N  N   . LEU B  1 127 ? 180.543 129.200 52.309 1.00   46.08 ? 126  LEU B N   1 
ATOM   2040  C  CA  . LEU B  1 127 ? 180.054 129.152 50.933 1.00   46.15 ? 126  LEU B CA  1 
ATOM   2041  C  C   . LEU B  1 127 ? 181.158 129.302 49.887 1.00   47.82 ? 126  LEU B C   1 
ATOM   2042  O  O   . LEU B  1 127 ? 180.908 129.821 48.829 1.00   50.41 ? 126  LEU B O   1 
ATOM   2043  C  CB  . LEU B  1 127 ? 178.954 130.195 50.715 1.00   46.84 ? 126  LEU B CB  1 
ATOM   2044  C  CG  . LEU B  1 127 ? 177.910 130.403 51.826 1.00   46.94 ? 126  LEU B CG  1 
ATOM   2045  C  CD1 . LEU B  1 127 ? 177.027 131.608 51.497 1.00   47.55 ? 126  LEU B CD1 1 
ATOM   2046  C  CD2 . LEU B  1 127 ? 177.066 129.153 52.078 1.00   45.35 ? 126  LEU B CD2 1 
ATOM   2047  N  N   . GLY B  1 128 ? 182.372 128.851 50.183 1.00   50.98 ? 127  GLY B N   1 
ATOM   2048  C  CA  . GLY B  1 128 ? 183.488 128.920 49.229 1.00   54.70 ? 127  GLY B CA  1 
ATOM   2049  C  C   . GLY B  1 128 ? 184.188 130.275 49.096 1.00   61.92 ? 127  GLY B C   1 
ATOM   2050  O  O   . GLY B  1 128 ? 185.077 130.423 48.254 1.00   64.39 ? 127  GLY B O   1 
ATOM   2051  N  N   . LYS B  1 129 ? 183.831 131.248 49.939 1.00   65.65 ? 128  LYS B N   1 
ATOM   2052  C  CA  . LYS B  1 129 ? 184.280 132.640 49.767 1.00   69.98 ? 128  LYS B CA  1 
ATOM   2053  C  C   . LYS B  1 129 ? 185.217 133.129 50.869 1.00   73.76 ? 128  LYS B C   1 
ATOM   2054  O  O   . LYS B  1 129 ? 185.303 134.335 51.125 1.00   77.02 ? 128  LYS B O   1 
ATOM   2055  C  CB  . LYS B  1 129 ? 183.066 133.571 49.694 1.00   71.47 ? 128  LYS B CB  1 
ATOM   2056  C  CG  . LYS B  1 129 ? 182.090 133.242 48.578 1.00   72.06 ? 128  LYS B CG  1 
ATOM   2057  C  CD  . LYS B  1 129 ? 180.858 134.130 48.654 1.00   74.02 ? 128  LYS B CD  1 
ATOM   2058  C  CE  . LYS B  1 129 ? 179.765 133.685 47.690 1.00   75.55 ? 128  LYS B CE  1 
ATOM   2059  N  NZ  . LYS B  1 129 ? 180.235 133.527 46.284 1.00   77.45 ? 128  LYS B NZ  1 
ATOM   2060  N  N   . GLY B  1 130 ? 185.931 132.206 51.510 1.00   75.69 ? 129  GLY B N   1 
ATOM   2061  C  CA  . GLY B  1 130 ? 186.902 132.568 52.543 1.00   78.82 ? 129  GLY B CA  1 
ATOM   2062  C  C   . GLY B  1 130 ? 188.149 133.181 51.934 1.00   81.53 ? 129  GLY B C   1 
ATOM   2063  O  O   . GLY B  1 130 ? 188.453 134.351 52.164 1.00   87.44 ? 129  GLY B O   1 
ATOM   2064  N  N   . GLY B  1 131 ? 188.855 132.382 51.139 1.00   82.06 ? 130  GLY B N   1 
ATOM   2065  C  CA  . GLY B  1 131 ? 190.085 132.808 50.472 1.00   82.22 ? 130  GLY B CA  1 
ATOM   2066  C  C   . GLY B  1 131 ? 191.314 132.100 51.004 1.00   82.26 ? 130  GLY B C   1 
ATOM   2067  O  O   . GLY B  1 131 ? 192.381 132.699 51.084 1.00   82.20 ? 130  GLY B O   1 
ATOM   2068  N  N   . ASN B  1 132 ? 191.174 130.818 51.339 1.00   82.24 ? 131  ASN B N   1 
ATOM   2069  C  CA  . ASN B  1 132 ? 192.245 130.069 52.002 1.00   82.29 ? 131  ASN B CA  1 
ATOM   2070  C  C   . ASN B  1 132 ? 192.301 128.567 51.655 1.00   81.07 ? 131  ASN B C   1 
ATOM   2071  O  O   . ASN B  1 132 ? 192.616 127.740 52.518 1.00   81.50 ? 131  ASN B O   1 
ATOM   2072  C  CB  . ASN B  1 132 ? 192.128 130.265 53.520 1.00   82.91 ? 131  ASN B CB  1 
ATOM   2073  C  CG  . ASN B  1 132 ? 190.744 129.931 54.053 1.00   82.58 ? 131  ASN B CG  1 
ATOM   2074  O  OD1 . ASN B  1 132 ? 190.088 128.996 53.586 1.00   80.43 ? 131  ASN B OD1 1 
ATOM   2075  N  ND2 . ASN B  1 132 ? 190.294 130.698 55.042 1.00   81.94 ? 131  ASN B ND2 1 
ATOM   2076  N  N   . GLU B  1 133 ? 192.008 128.227 50.398 1.00   78.30 ? 132  GLU B N   1 
ATOM   2077  C  CA  . GLU B  1 133 ? 192.119 126.850 49.883 1.00   77.12 ? 132  GLU B CA  1 
ATOM   2078  C  C   . GLU B  1 133 ? 191.118 125.866 50.519 1.00   73.39 ? 132  GLU B C   1 
ATOM   2079  O  O   . GLU B  1 133 ? 190.308 125.278 49.806 1.00   72.48 ? 132  GLU B O   1 
ATOM   2080  C  CB  . GLU B  1 133 ? 193.556 126.308 50.008 1.00   78.89 ? 132  GLU B CB  1 
ATOM   2081  C  CG  . GLU B  1 133 ? 193.848 125.115 49.094 1.00   79.37 ? 132  GLU B CG  1 
ATOM   2082  C  CD  . GLU B  1 133 ? 195.023 124.268 49.559 1.00   78.82 ? 132  GLU B CD  1 
ATOM   2083  O  OE1 . GLU B  1 133 ? 195.989 124.832 50.114 0.10   79.99 ? 132  GLU B OE1 1 
ATOM   2084  O  OE2 . GLU B  1 133 ? 194.975 123.034 49.369 0.10   77.82 ? 132  GLU B OE2 1 
ATOM   2085  N  N   . GLU B  1 134 ? 191.175 125.672 51.837 1.00   70.54 ? 133  GLU B N   1 
ATOM   2086  C  CA  . GLU B  1 134 ? 190.183 124.826 52.511 1.00   68.61 ? 133  GLU B CA  1 
ATOM   2087  C  C   . GLU B  1 134 ? 188.755 125.318 52.258 1.00   65.08 ? 133  GLU B C   1 
ATOM   2088  O  O   . GLU B  1 134 ? 187.815 124.511 52.222 1.00   60.98 ? 133  GLU B O   1 
ATOM   2089  C  CB  . GLU B  1 134 ? 190.451 124.711 54.017 1.00   69.33 ? 133  GLU B CB  1 
ATOM   2090  C  CG  . GLU B  1 134 ? 191.386 123.568 54.386 1.00   71.26 ? 133  GLU B CG  1 
ATOM   2091  C  CD  . GLU B  1 134 ? 190.841 122.201 54.003 1.00   71.76 ? 133  GLU B CD  1 
ATOM   2092  O  OE1 . GLU B  1 134 ? 189.647 121.926 54.260 1.00   70.29 ? 133  GLU B OE1 1 
ATOM   2093  O  OE2 . GLU B  1 134 ? 191.612 121.397 53.434 1.00   75.10 ? 133  GLU B OE2 1 
ATOM   2094  N  N   . SER B  1 135 ? 188.598 126.630 52.080 1.00   62.34 ? 134  SER B N   1 
ATOM   2095  C  CA  . SER B  1 135 ? 187.325 127.189 51.614 1.00   61.69 ? 134  SER B CA  1 
ATOM   2096  C  C   . SER B  1 135 ? 186.886 126.532 50.302 1.00   59.64 ? 134  SER B C   1 
ATOM   2097  O  O   . SER B  1 135 ? 185.721 126.192 50.153 1.00   56.91 ? 134  SER B O   1 
ATOM   2098  C  CB  . SER B  1 135 ? 187.408 128.705 51.423 1.00   63.35 ? 134  SER B CB  1 
ATOM   2099  O  OG  . SER B  1 135 ? 186.109 129.259 51.265 1.00   63.25 ? 134  SER B OG  1 
ATOM   2100  N  N   . THR B  1 136 ? 187.831 126.341 49.382 1.00   59.52 ? 135  THR B N   1 
ATOM   2101  C  CA  . THR B  1 136 ? 187.556 125.763 48.064 1.00   60.53 ? 135  THR B CA  1 
ATOM   2102  C  C   . THR B  1 136 ? 187.377 124.230 48.075 1.00   60.19 ? 135  THR B C   1 
ATOM   2103  O  O   . THR B  1 136 ? 186.827 123.650 47.120 1.00   59.12 ? 135  THR B O   1 
ATOM   2104  C  CB  . THR B  1 136 ? 188.686 126.096 47.080 1.00   62.47 ? 135  THR B CB  1 
ATOM   2105  O  OG1 . THR B  1 136 ? 189.869 125.381 47.465 1.00   62.22 ? 135  THR B OG1 1 
ATOM   2106  C  CG2 . THR B  1 136 ? 188.959 127.609 47.058 1.00   61.83 ? 135  THR B CG2 1 
ATOM   2107  N  N   . LYS B  1 137 ? 187.871 123.584 49.133 1.00   58.31 ? 136  LYS B N   1 
ATOM   2108  C  CA  . LYS B  1 137 ? 187.594 122.175 49.374 1.00   55.91 ? 136  LYS B CA  1 
ATOM   2109  C  C   . LYS B  1 137 ? 186.339 121.987 50.238 1.00   53.09 ? 136  LYS B C   1 
ATOM   2110  O  O   . LYS B  1 137 ? 185.464 121.208 49.882 1.00   51.79 ? 136  LYS B O   1 
ATOM   2111  C  CB  . LYS B  1 137 ? 188.786 121.493 50.055 1.00   57.50 ? 136  LYS B CB  1 
ATOM   2112  C  CG  . LYS B  1 137 ? 190.021 121.371 49.178 1.00   59.55 ? 136  LYS B CG  1 
ATOM   2113  C  CD  . LYS B  1 137 ? 191.073 120.487 49.832 1.00   59.59 ? 136  LYS B CD  1 
ATOM   2114  C  CE  . LYS B  1 137 ? 192.436 120.664 49.178 0.10   60.63 ? 136  LYS B CE  1 
ATOM   2115  N  NZ  . LYS B  1 137 ? 193.498 119.880 49.868 0.10   60.50 ? 136  LYS B NZ  1 
ATOM   2116  N  N   . THR B  1 138 ? 186.245 122.702 51.362 1.00   50.28 ? 137  THR B N   1 
ATOM   2117  C  CA  . THR B  1 138 ? 185.262 122.360 52.394 1.00   47.82 ? 137  THR B CA  1 
ATOM   2118  C  C   . THR B  1 138 ? 184.371 123.474 52.935 1.00   46.91 ? 137  THR B C   1 
ATOM   2119  O  O   . THR B  1 138 ? 183.373 123.181 53.600 1.00   44.89 ? 137  THR B O   1 
ATOM   2120  C  CB  . THR B  1 138 ? 185.972 121.725 53.609 1.00   47.71 ? 137  THR B CB  1 
ATOM   2121  O  OG1 . THR B  1 138 ? 186.925 122.649 54.140 1.00   48.85 ? 137  THR B OG1 1 
ATOM   2122  C  CG2 . THR B  1 138 ? 186.694 120.436 53.200 1.00   46.95 ? 137  THR B CG2 1 
ATOM   2123  N  N   . GLY B  1 139 ? 184.716 124.736 52.681 1.00   46.51 ? 138  GLY B N   1 
ATOM   2124  C  CA  . GLY B  1 139 ? 183.984 125.853 53.279 1.00   46.03 ? 138  GLY B CA  1 
ATOM   2125  C  C   . GLY B  1 139 ? 184.351 126.140 54.741 1.00   46.67 ? 138  GLY B C   1 
ATOM   2126  O  O   . GLY B  1 139 ? 183.655 126.908 55.415 1.00   47.85 ? 138  GLY B O   1 
ATOM   2127  N  N   . ASN B  1 140 ? 185.444 125.542 55.220 1.00   45.83 ? 139  ASN B N   1 
ATOM   2128  C  CA  . ASN B  1 140 ? 185.876 125.647 56.611 1.00   46.68 ? 139  ASN B CA  1 
ATOM   2129  C  C   . ASN B  1 140 ? 184.728 125.426 57.595 1.00   45.39 ? 139  ASN B C   1 
ATOM   2130  O  O   . ASN B  1 140 ? 184.591 126.159 58.567 1.00   46.28 ? 139  ASN B O   1 
ATOM   2131  C  CB  . ASN B  1 140 ? 186.537 127.012 56.861 1.00   49.14 ? 139  ASN B CB  1 
ATOM   2132  C  CG  . ASN B  1 140 ? 187.693 127.270 55.921 1.00   50.74 ? 139  ASN B CG  1 
ATOM   2133  O  OD1 . ASN B  1 140 ? 188.748 126.651 56.037 1.00   52.42 ? 139  ASN B OD1 1 
ATOM   2134  N  ND2 . ASN B  1 140 ? 187.484 128.153 54.954 1.00   51.80 ? 139  ASN B ND2 1 
ATOM   2135  N  N   . ALA B  1 141 ? 183.912 124.407 57.345 1.00   42.11 ? 140  ALA B N   1 
ATOM   2136  C  CA  . ALA B  1 141 ? 182.736 124.131 58.178 1.00   40.63 ? 140  ALA B CA  1 
ATOM   2137  C  C   . ALA B  1 141 ? 183.111 123.354 59.447 1.00   40.09 ? 140  ALA B C   1 
ATOM   2138  O  O   . ALA B  1 141 ? 182.262 123.116 60.314 1.00   39.14 ? 140  ALA B O   1 
ATOM   2139  C  CB  . ALA B  1 141 ? 181.684 123.362 57.375 1.00   39.18 ? 140  ALA B CB  1 
ATOM   2140  N  N   . GLY B  1 142 ? 184.369 122.937 59.547 1.00   39.34 ? 141  GLY B N   1 
ATOM   2141  C  CA  . GLY B  1 142 ? 184.833 122.277 60.745 1.00   40.00 ? 141  GLY B CA  1 
ATOM   2142  C  C   . GLY B  1 142 ? 184.363 120.838 60.895 1.00   38.79 ? 141  GLY B C   1 
ATOM   2143  O  O   . GLY B  1 142 ? 184.049 120.154 59.906 1.00   38.08 ? 141  GLY B O   1 
ATOM   2144  N  N   . SER B  1 143 ? 184.319 120.376 62.142 1.00   38.07 ? 142  SER B N   1 
ATOM   2145  C  CA  . SER B  1 143 ? 184.092 118.958 62.402 1.00   37.14 ? 142  SER B CA  1 
ATOM   2146  C  C   . SER B  1 143 ? 182.666 118.520 62.035 1.00   34.90 ? 142  SER B C   1 
ATOM   2147  O  O   . SER B  1 143 ? 181.762 119.332 61.792 1.00   35.32 ? 142  SER B O   1 
ATOM   2148  C  CB  . SER B  1 143 ? 184.464 118.575 63.853 1.00   38.04 ? 142  SER B CB  1 
ATOM   2149  O  OG  . SER B  1 143 ? 183.352 118.685 64.720 1.00   39.03 ? 142  SER B OG  1 
ATOM   2150  N  N   . ARG B  1 144 ? 182.506 117.210 61.944 1.00   34.16 ? 143  ARG B N   1 
ATOM   2151  C  CA  . ARG B  1 144 ? 181.266 116.602 61.516 1.00   31.98 ? 143  ARG B CA  1 
ATOM   2152  C  C   . ARG B  1 144 ? 180.519 116.163 62.759 1.00   30.91 ? 143  ARG B C   1 
ATOM   2153  O  O   . ARG B  1 144 ? 180.871 115.173 63.364 1.00   31.32 ? 143  ARG B O   1 
ATOM   2154  C  CB  . ARG B  1 144 ? 181.583 115.407 60.623 1.00   31.20 ? 143  ARG B CB  1 
ATOM   2155  C  CG  . ARG B  1 144 ? 182.425 115.780 59.415 1.00   30.99 ? 143  ARG B CG  1 
ATOM   2156  C  CD  . ARG B  1 144 ? 182.827 114.562 58.610 1.00   30.86 ? 143  ARG B CD  1 
ATOM   2157  N  NE  . ARG B  1 144 ? 183.697 114.958 57.510 1.00   32.43 ? 143  ARG B NE  1 
ATOM   2158  C  CZ  . ARG B  1 144 ? 184.117 114.169 56.526 1.00   31.14 ? 143  ARG B CZ  1 
ATOM   2159  N  NH1 . ARG B  1 144 ? 183.759 112.900 56.484 1.00   31.13 ? 143  ARG B NH1 1 
ATOM   2160  N  NH2 . ARG B  1 144 ? 184.920 114.655 55.589 1.00   30.70 ? 143  ARG B NH2 1 
ATOM   2161  N  N   . LEU B  1 145 ? 179.485 116.896 63.140 1.00   30.04 ? 144  LEU B N   1 
ATOM   2162  C  CA  . LEU B  1 145 ? 178.816 116.638 64.409 1.00   29.34 ? 144  LEU B CA  1 
ATOM   2163  C  C   . LEU B  1 145 ? 177.834 115.477 64.331 1.00   27.78 ? 144  LEU B C   1 
ATOM   2164  O  O   . LEU B  1 145 ? 177.669 114.739 65.280 1.00   28.01 ? 144  LEU B O   1 
ATOM   2165  C  CB  . LEU B  1 145 ? 178.110 117.900 64.898 1.00   29.80 ? 144  LEU B CB  1 
ATOM   2166  C  CG  . LEU B  1 145 ? 178.987 119.163 64.971 1.00   31.26 ? 144  LEU B CG  1 
ATOM   2167  C  CD1 . LEU B  1 145 ? 178.183 120.333 65.526 1.00   31.84 ? 144  LEU B CD1 1 
ATOM   2168  C  CD2 . LEU B  1 145 ? 180.251 118.920 65.799 1.00   30.77 ? 144  LEU B CD2 1 
ATOM   2169  N  N   . ALA B  1 146 ? 177.169 115.325 63.200 1.00   27.38 ? 145  ALA B N   1 
ATOM   2170  C  CA  . ALA B  1 146 ? 176.237 114.220 62.999 1.00   25.97 ? 145  ALA B CA  1 
ATOM   2171  C  C   . ALA B  1 146 ? 176.104 113.928 61.521 1.00   25.68 ? 145  ALA B C   1 
ATOM   2172  O  O   . ALA B  1 146 ? 176.363 114.782 60.661 1.00   25.08 ? 145  ALA B O   1 
ATOM   2173  C  CB  . ALA B  1 146 ? 174.867 114.547 63.583 1.00   25.61 ? 145  ALA B CB  1 
ATOM   2174  N  N   . CYS B  1 147 ? 175.664 112.715 61.235 1.00   24.75 ? 146  CYS B N   1 
ATOM   2175  C  CA  . CYS B  1 147 ? 175.515 112.272 59.869 1.00   24.64 ? 146  CYS B CA  1 
ATOM   2176  C  C   . CYS B  1 147 ? 174.674 111.021 59.825 1.00   23.64 ? 146  CYS B C   1 
ATOM   2177  O  O   . CYS B  1 147 ? 174.466 110.365 60.854 1.00   22.52 ? 146  CYS B O   1 
ATOM   2178  C  CB  . CYS B  1 147 ? 176.876 111.959 59.255 1.00   24.85 ? 146  CYS B CB  1 
ATOM   2179  S  SG  . CYS B  1 147 ? 177.760 110.637 60.088 1.00   25.05 ? 146  CYS B SG  1 
ATOM   2180  N  N   . GLY B  1 148 ? 174.228 110.692 58.612 1.00   22.33 ? 147  GLY B N   1 
ATOM   2181  C  CA  . GLY B  1 148 ? 173.478 109.463 58.376 1.00   21.18 ? 147  GLY B CA  1 
ATOM   2182  C  C   . GLY B  1 148 ? 173.438 109.137 56.897 1.00   20.33 ? 147  GLY B C   1 
ATOM   2183  O  O   . GLY B  1 148 ? 173.602 110.025 56.040 1.00   20.38 ? 147  GLY B O   1 
ATOM   2184  N  N   . VAL B  1 149 ? 173.197 107.872 56.584 1.00   19.37 ? 148  VAL B N   1 
ATOM   2185  C  CA  . VAL B  1 149 ? 173.097 107.463 55.171 1.00   19.10 ? 148  VAL B CA  1 
ATOM   2186  C  C   . VAL B  1 149 ? 171.695 107.810 54.660 1.00   19.12 ? 148  VAL B C   1 
ATOM   2187  O  O   . VAL B  1 149 ? 170.712 107.574 55.349 1.00   19.77 ? 148  VAL B O   1 
ATOM   2188  C  CB  . VAL B  1 149 ? 173.421 105.968 54.999 1.00   18.55 ? 148  VAL B CB  1 
ATOM   2189  C  CG1 . VAL B  1 149 ? 173.409 105.570 53.516 1.00   18.15 ? 148  VAL B CG1 1 
ATOM   2190  C  CG2 . VAL B  1 149 ? 174.767 105.661 55.639 1.00   18.22 ? 148  VAL B CG2 1 
ATOM   2191  N  N   . ILE B  1 150 ? 171.611 108.412 53.477 1.00   19.10 ? 149  ILE B N   1 
ATOM   2192  C  CA  . ILE B  1 150 ? 170.339 108.811 52.891 1.00   19.17 ? 149  ILE B CA  1 
ATOM   2193  C  C   . ILE B  1 150 ? 169.702 107.587 52.252 1.00   19.11 ? 149  ILE B C   1 
ATOM   2194  O  O   . ILE B  1 150 ? 170.280 106.969 51.386 1.00   18.69 ? 149  ILE B O   1 
ATOM   2195  C  CB  . ILE B  1 150 ? 170.543 109.912 51.837 1.00   19.69 ? 149  ILE B CB  1 
ATOM   2196  C  CG1 . ILE B  1 150 ? 171.203 111.133 52.463 1.00   19.69 ? 149  ILE B CG1 1 
ATOM   2197  C  CG2 . ILE B  1 150 ? 169.217 110.330 51.210 1.00   20.03 ? 149  ILE B CG2 1 
ATOM   2198  C  CD1 . ILE B  1 150 ? 171.751 112.124 51.457 1.00   19.98 ? 149  ILE B CD1 1 
ATOM   2199  N  N   . GLY B  1 151 ? 168.517 107.214 52.713 1.00   19.67 ? 150  GLY B N   1 
ATOM   2200  C  CA  . GLY B  1 151 ? 167.877 105.987 52.273 1.00   20.11 ? 150  GLY B CA  1 
ATOM   2201  C  C   . GLY B  1 151 ? 166.573 106.261 51.556 1.00   20.63 ? 150  GLY B C   1 
ATOM   2202  O  O   . GLY B  1 151 ? 165.994 107.346 51.719 1.00   20.68 ? 150  GLY B O   1 
ATOM   2203  N  N   . ILE B  1 152 ? 166.136 105.282 50.760 1.00   20.42 ? 151  ILE B N   1 
ATOM   2204  C  CA  . ILE B  1 152 ? 164.854 105.339 50.091 1.00   21.15 ? 151  ILE B CA  1 
ATOM   2205  C  C   . ILE B  1 152 ? 163.734 105.281 51.122 1.00   21.56 ? 151  ILE B C   1 
ATOM   2206  O  O   . ILE B  1 152 ? 163.780 104.454 52.041 1.00   21.22 ? 151  ILE B O   1 
ATOM   2207  C  CB  . ILE B  1 152 ? 164.688 104.164 49.114 1.00   21.60 ? 151  ILE B CB  1 
ATOM   2208  C  CG1 . ILE B  1 152 ? 165.778 104.218 48.035 1.00   21.94 ? 151  ILE B CG1 1 
ATOM   2209  C  CG2 . ILE B  1 152 ? 163.302 104.216 48.465 1.00   22.49 ? 151  ILE B CG2 1 
ATOM   2210  C  CD1 . ILE B  1 152 ? 166.014 102.890 47.316 1.00   22.30 ? 151  ILE B CD1 1 
ATOM   2211  N  N   . ALA B  1 153 ? 162.744 106.160 50.967 1.00   22.34 ? 152  ALA B N   1 
ATOM   2212  C  CA  . ALA B  1 153 ? 161.618 106.306 51.888 1.00   23.36 ? 152  ALA B CA  1 
ATOM   2213  C  C   . ALA B  1 153 ? 160.314 105.975 51.181 1.00   25.27 ? 152  ALA B C   1 
ATOM   2214  O  O   . ALA B  1 153 ? 160.217 106.094 49.956 1.00   24.98 ? 152  ALA B O   1 
ATOM   2215  C  CB  . ALA B  1 153 ? 161.563 107.724 52.423 1.00   23.18 ? 152  ALA B CB  1 
ATOM   2216  N  N   . GLN B  1 154 ? 159.309 105.576 51.957 1.00   27.15 ? 153  GLN B N   1 
ATOM   2217  C  CA  . GLN B  1 154 ? 158.021 105.174 51.397 1.00   28.86 ? 153  GLN B CA  1 
ATOM   2218  C  C   . GLN B  1 154 ? 157.231 106.351 50.803 1.00   30.66 ? 153  GLN B C   1 
ATOM   2219  O  O   . GLN B  1 154 ? 156.596 106.208 49.752 1.00   32.99 ? 153  GLN B O   1 
ATOM   2220  C  CB  . GLN B  1 154 ? 157.175 104.493 52.465 1.00   30.16 ? 153  GLN B CB  1 
ATOM   2221  C  CG  . GLN B  1 154 ? 155.934 103.805 51.912 1.00   31.80 ? 153  GLN B CG  1 
ATOM   2222  C  CD  . GLN B  1 154 ? 155.019 103.307 53.004 1.00   32.76 ? 153  GLN B CD  1 
ATOM   2223  O  OE1 . GLN B  1 154 ? 154.665 102.148 53.042 1.00   34.38 ? 153  GLN B OE1 1 
ATOM   2224  N  NE2 . GLN B  1 154 ? 154.622 104.196 53.891 1.00   35.24 ? 153  GLN B NE2 1 
ATOM   2225  O  OXT . GLN B  1 154 ? 157.190 107.462 51.325 1.00   30.57 ? 153  GLN B OXT 1 
ATOM   2226  N  N   . ALA C  1 2   ? 204.330 62.864  43.426 1.00   33.41 ? 1    ALA C N   1 
ATOM   2227  C  CA  . ALA C  1 2   ? 204.096 61.405  43.664 1.00   32.63 ? 1    ALA C CA  1 
ATOM   2228  C  C   . ALA C  1 2   ? 202.649 61.071  44.107 1.00   30.79 ? 1    ALA C C   1 
ATOM   2229  O  O   . ALA C  1 2   ? 202.013 61.836  44.795 1.00   31.30 ? 1    ALA C O   1 
ATOM   2230  C  CB  . ALA C  1 2   ? 205.096 60.899  44.710 1.00   33.27 ? 1    ALA C CB  1 
ATOM   2231  N  N   . THR C  1 3   ? 202.141 59.902  43.747 1.00   29.35 ? 2    THR C N   1 
ATOM   2232  C  CA  . THR C  1 3   ? 200.983 59.395  44.460 1.00   28.23 ? 2    THR C CA  1 
ATOM   2233  C  C   . THR C  1 3   ? 201.518 58.814  45.826 1.00   25.62 ? 2    THR C C   1 
ATOM   2234  O  O   . THR C  1 3   ? 202.643 58.314  45.928 1.00   24.36 ? 2    THR C O   1 
ATOM   2235  C  CB  . THR C  1 3   ? 200.111 58.493  43.537 1.00   29.64 ? 2    THR C CB  1 
ATOM   2236  O  OG1 . THR C  1 3   ? 198.891 58.149  44.171 1.00   32.47 ? 2    THR C OG1 1 
ATOM   2237  C  CG2 . THR C  1 3   ? 200.789 57.244  43.197 1.00   32.78 ? 2    THR C CG2 1 
ATOM   2238  N  N   . LYS C  1 4   ? 200.737 58.991  46.887 1.00   22.58 ? 3    LYS C N   1 
ATOM   2239  C  CA  . LYS C  1 4   ? 201.104 58.600  48.204 1.00   21.23 ? 3    LYS C CA  1 
ATOM   2240  C  C   . LYS C  1 4   ? 199.929 57.891  48.873 1.00   19.11 ? 3    LYS C C   1 
ATOM   2241  O  O   . LYS C  1 4   ? 198.760 58.213  48.646 1.00   17.98 ? 3    LYS C O   1 
ATOM   2242  C  CB  . LYS C  1 4   ? 201.497 59.824  49.034 1.00   22.74 ? 3    LYS C CB  1 
ATOM   2243  C  CG  . LYS C  1 4   ? 202.822 60.472  48.657 1.00   24.74 ? 3    LYS C CG  1 
ATOM   2244  C  CD  . LYS C  1 4   ? 203.052 61.748  49.454 1.00   26.85 ? 3    LYS C CD  1 
ATOM   2245  C  CE  . LYS C  1 4   ? 204.538 62.100  49.533 1.00   29.03 ? 3    LYS C CE  1 
ATOM   2246  N  NZ  . LYS C  1 4   ? 204.815 63.571  49.442 1.00   29.70 ? 3    LYS C NZ  1 
ATOM   2247  N  N   . ALA C  1 5   ? 200.262 56.937  49.718 1.00   17.37 ? 4    ALA C N   1 
ATOM   2248  C  CA  . ALA C  1 5   ? 199.284 56.234  50.518 1.00   16.27 ? 4    ALA C CA  1 
ATOM   2249  C  C   . ALA C  1 5   ? 199.871 56.018  51.906 1.00   15.60 ? 4    ALA C C   1 
ATOM   2250  O  O   . ALA C  1 5   ? 201.068 56.229  52.128 1.00   15.61 ? 4    ALA C O   1 
ATOM   2251  C  CB  . ALA C  1 5   ? 198.912 54.904  49.869 1.00   15.81 ? 4    ALA C CB  1 
ATOM   2252  N  N   . VAL C  1 6   ? 199.009 55.631  52.839 1.00   14.87 ? 5    VAL C N   1 
ATOM   2253  C  CA  . VAL C  1 6   ? 199.394 55.433  54.216 1.00   14.66 ? 5    VAL C CA  1 
ATOM   2254  C  C   . VAL C  1 6   ? 198.474 54.356  54.780 1.00   14.39 ? 5    VAL C C   1 
ATOM   2255  O  O   . VAL C  1 6   ? 197.364 54.117  54.256 1.00   14.43 ? 5    VAL C O   1 
ATOM   2256  C  CB  . VAL C  1 6   ? 199.280 56.745  55.034 1.00   14.73 ? 5    VAL C CB  1 
ATOM   2257  C  CG1 . VAL C  1 6   ? 197.810 57.145  55.226 1.00   14.34 ? 5    VAL C CG1 1 
ATOM   2258  C  CG2 . VAL C  1 6   ? 200.018 56.615  56.382 1.00   14.74 ? 5    VAL C CG2 1 
ATOM   2259  N  N   . CYS C  1 7   ? 198.945 53.695  55.811 1.00   14.24 ? 6    CYS C N   1 
ATOM   2260  C  CA  . CYS C  1 7   ? 198.215 52.639  56.476 1.00   14.08 ? 6    CYS C CA  1 
ATOM   2261  C  C   . CYS C  1 7   ? 198.572 52.631  57.967 1.00   14.32 ? 6    CYS C C   1 
ATOM   2262  O  O   . CYS C  1 7   ? 199.732 52.620  58.324 1.00   14.24 ? 6    CYS C O   1 
ATOM   2263  C  CB  . CYS C  1 7   ? 198.564 51.306  55.847 1.00   13.90 ? 6    CYS C CB  1 
ATOM   2264  S  SG  . CYS C  1 7   ? 197.691 49.907  56.583 1.00   13.84 ? 6    CYS C SG  1 
ATOM   2265  N  N   . VAL C  1 8   ? 197.559 52.674  58.823 1.00   14.69 ? 7    VAL C N   1 
ATOM   2266  C  CA  . VAL C  1 8   ? 197.754 52.553  60.264 1.00   15.24 ? 7    VAL C CA  1 
ATOM   2267  C  C   . VAL C  1 8   ? 197.462 51.108  60.666 1.00   15.47 ? 7    VAL C C   1 
ATOM   2268  O  O   . VAL C  1 8   ? 196.362 50.597  60.450 1.00   15.50 ? 7    VAL C O   1 
ATOM   2269  C  CB  . VAL C  1 8   ? 196.873 53.564  61.049 1.00   15.40 ? 7    VAL C CB  1 
ATOM   2270  C  CG1 . VAL C  1 8   ? 197.090 53.391  62.553 1.00   15.60 ? 7    VAL C CG1 1 
ATOM   2271  C  CG2 . VAL C  1 8   ? 197.215 54.998  60.611 1.00   15.35 ? 7    VAL C CG2 1 
ATOM   2272  N  N   . LEU C  1 9   ? 198.466 50.430  61.197 1.00   16.14 ? 8    LEU C N   1 
ATOM   2273  C  CA  . LEU C  1 9   ? 198.300 49.022  61.542 1.00   16.77 ? 8    LEU C CA  1 
ATOM   2274  C  C   . LEU C  1 9   ? 197.905 48.946  63.001 1.00   17.30 ? 8    LEU C C   1 
ATOM   2275  O  O   . LEU C  1 9   ? 198.555 49.554  63.846 1.00   17.16 ? 8    LEU C O   1 
ATOM   2276  C  CB  . LEU C  1 9   ? 199.582 48.235  61.298 1.00   16.87 ? 8    LEU C CB  1 
ATOM   2277  C  CG  . LEU C  1 9   ? 200.103 48.143  59.881 1.00   16.90 ? 8    LEU C CG  1 
ATOM   2278  C  CD1 . LEU C  1 9   ? 201.552 47.661  59.914 1.00   17.67 ? 8    LEU C CD1 1 
ATOM   2279  C  CD2 . LEU C  1 9   ? 199.255 47.165  59.108 1.00   16.79 ? 8    LEU C CD2 1 
ATOM   2280  N  N   . LYS C  1 10  ? 196.829 48.209  63.268 1.00   18.31 ? 9    LYS C N   1 
ATOM   2281  C  CA  . LYS C  1 10  ? 196.348 47.933  64.638 1.00   19.39 ? 9    LYS C CA  1 
ATOM   2282  C  C   . LYS C  1 10  ? 195.852 46.517  64.759 1.00   19.87 ? 9    LYS C C   1 
ATOM   2283  O  O   . LYS C  1 10  ? 195.392 45.939  63.778 1.00   19.51 ? 9    LYS C O   1 
ATOM   2284  C  CB  . LYS C  1 10  ? 195.171 48.848  64.983 1.00   20.02 ? 9    LYS C CB  1 
ATOM   2285  C  CG  . LYS C  1 10  ? 195.560 50.285  65.257 1.00   20.70 ? 9    LYS C CG  1 
ATOM   2286  C  CD  . LYS C  1 10  ? 194.365 51.219  65.206 0.50   21.00 ? 9    LYS C CD  1 
ATOM   2287  C  CE  . LYS C  1 10  ? 194.834 52.668  65.314 0.50   21.39 ? 9    LYS C CE  1 
ATOM   2288  N  NZ  . LYS C  1 10  ? 193.709 53.626  65.190 0.50   21.75 ? 9    LYS C NZ  1 
ATOM   2289  N  N   . GLY C  1 11  ? 195.866 45.984  65.985 1.00   21.21 ? 10   GLY C N   1 
ATOM   2290  C  CA  . GLY C  1 11  ? 195.296 44.660  66.277 1.00   21.86 ? 10   GLY C CA  1 
ATOM   2291  C  C   . GLY C  1 11  ? 194.791 44.509  67.706 1.00   23.17 ? 10   GLY C C   1 
ATOM   2292  O  O   . GLY C  1 11  ? 194.545 45.500  68.411 1.00   23.44 ? 10   GLY C O   1 
ATOM   2293  N  N   . ASP C  1 12  ? 194.665 43.267  68.146 1.00   24.41 ? 11   ASP C N   1 
ATOM   2294  C  CA  . ASP C  1 12  ? 194.117 42.988  69.468 1.00   26.46 ? 11   ASP C CA  1 
ATOM   2295  C  C   . ASP C  1 12  ? 195.210 42.934  70.529 1.00   25.94 ? 11   ASP C C   1 
ATOM   2296  O  O   . ASP C  1 12  ? 194.919 42.982  71.720 1.00   26.55 ? 11   ASP C O   1 
ATOM   2297  C  CB  . ASP C  1 12  ? 193.326 41.679  69.432 1.00   28.39 ? 11   ASP C CB  1 
ATOM   2298  C  CG  . ASP C  1 12  ? 192.083 41.787  68.563 1.00   29.55 ? 11   ASP C CG  1 
ATOM   2299  O  OD1 . ASP C  1 12  ? 191.408 42.825  68.615 1.00   30.32 ? 11   ASP C OD1 1 
ATOM   2300  O  OD2 . ASP C  1 12  ? 191.790 40.842  67.813 1.00   31.65 ? 11   ASP C OD2 1 
ATOM   2301  N  N   . GLY C  1 13  ? 196.460 42.856  70.087 1.00   24.46 ? 12   GLY C N   1 
ATOM   2302  C  CA  . GLY C  1 13  ? 197.603 42.906  70.972 1.00   24.33 ? 12   GLY C CA  1 
ATOM   2303  C  C   . GLY C  1 13  ? 198.300 44.242  70.832 1.00   23.58 ? 12   GLY C C   1 
ATOM   2304  O  O   . GLY C  1 13  ? 197.685 45.210  70.423 1.00   24.17 ? 12   GLY C O   1 
ATOM   2305  N  N   . PRO C  1 14  ? 199.599 44.292  71.157 1.00   23.11 ? 13   PRO C N   1 
ATOM   2306  C  CA  . PRO C  1 14  ? 200.389 45.510  71.168 1.00   22.91 ? 13   PRO C CA  1 
ATOM   2307  C  C   . PRO C  1 14  ? 201.012 45.918  69.820 1.00   22.12 ? 13   PRO C C   1 
ATOM   2308  O  O   . PRO C  1 14  ? 201.681 46.944  69.763 1.00   21.84 ? 13   PRO C O   1 
ATOM   2309  C  CB  . PRO C  1 14  ? 201.516 45.165  72.145 1.00   23.22 ? 13   PRO C CB  1 
ATOM   2310  C  CG  . PRO C  1 14  ? 201.743 43.728  71.881 1.00   23.47 ? 13   PRO C CG  1 
ATOM   2311  C  CD  . PRO C  1 14  ? 200.378 43.143  71.665 1.00   23.33 ? 13   PRO C CD  1 
ATOM   2312  N  N   . VAL C  1 15  ? 200.809 45.144  68.756 1.00   21.44 ? 14   VAL C N   1 
ATOM   2313  C  CA  . VAL C  1 15  ? 201.449 45.466  67.487 1.00   20.95 ? 14   VAL C CA  1 
ATOM   2314  C  C   . VAL C  1 15  ? 200.749 46.664  66.825 1.00   21.08 ? 14   VAL C C   1 
ATOM   2315  O  O   . VAL C  1 15  ? 199.545 46.678  66.638 1.00   21.09 ? 14   VAL C O   1 
ATOM   2316  C  CB  . VAL C  1 15  ? 201.499 44.270  66.514 1.00   20.48 ? 14   VAL C CB  1 
ATOM   2317  C  CG1 . VAL C  1 15  ? 202.095 44.720  65.201 1.00   19.54 ? 14   VAL C CG1 1 
ATOM   2318  C  CG2 . VAL C  1 15  ? 202.308 43.100  67.108 1.00   20.64 ? 14   VAL C CG2 1 
ATOM   2319  N  N   . GLN C  1 16  ? 201.518 47.683  66.483 1.00   21.21 ? 15   GLN C N   1 
ATOM   2320  C  CA  . GLN C  1 16  ? 200.963 48.842  65.848 1.00   20.92 ? 15   GLN C CA  1 
ATOM   2321  C  C   . GLN C  1 16  ? 202.049 49.587  65.112 1.00   19.97 ? 15   GLN C C   1 
ATOM   2322  O  O   . GLN C  1 16  ? 203.225 49.486  65.434 1.00   19.37 ? 15   GLN C O   1 
ATOM   2323  C  CB  . GLN C  1 16  ? 200.273 49.755  66.874 1.00   22.46 ? 15   GLN C CB  1 
ATOM   2324  C  CG  . GLN C  1 16  ? 201.172 50.348  67.928 1.00   23.96 ? 15   GLN C CG  1 
ATOM   2325  C  CD  . GLN C  1 16  ? 200.396 51.232  68.898 1.00   26.10 ? 15   GLN C CD  1 
ATOM   2326  O  OE1 . GLN C  1 16  ? 199.570 52.049  68.485 1.00   28.33 ? 15   GLN C OE1 1 
ATOM   2327  N  NE2 . GLN C  1 16  ? 200.654 51.076  70.185 1.00   27.48 ? 15   GLN C NE2 1 
ATOM   2328  N  N   . GLY C  1 17  ? 201.640 50.320  64.090 1.00   18.88 ? 16   GLY C N   1 
ATOM   2329  C  CA  . GLY C  1 17  ? 202.598 51.087  63.304 1.00   18.19 ? 16   GLY C CA  1 
ATOM   2330  C  C   . GLY C  1 17  ? 201.923 51.847  62.196 1.00   17.29 ? 16   GLY C C   1 
ATOM   2331  O  O   . GLY C  1 17  ? 200.704 51.758  62.009 1.00   16.61 ? 16   GLY C O   1 
ATOM   2332  N  N   . ILE C  1 18  ? 202.744 52.610  61.485 1.00   16.76 ? 17   ILE C N   1 
ATOM   2333  C  CA  . ILE C  1 18  ? 202.318 53.440  60.393 1.00   16.34 ? 17   ILE C CA  1 
ATOM   2334  C  C   . ILE C  1 18  ? 203.250 53.123  59.228 1.00   15.93 ? 17   ILE C C   1 
ATOM   2335  O  O   . ILE C  1 18  ? 204.492 53.168  59.369 1.00   16.34 ? 17   ILE C O   1 
ATOM   2336  C  CB  . ILE C  1 18  ? 202.446 54.925  60.781 1.00   16.79 ? 17   ILE C CB  1 
ATOM   2337  C  CG1 . ILE C  1 18  ? 201.513 55.266  61.952 1.00   16.95 ? 17   ILE C CG1 1 
ATOM   2338  C  CG2 . ILE C  1 18  ? 202.179 55.827  59.588 1.00   16.40 ? 17   ILE C CG2 1 
ATOM   2339  C  CD1 . ILE C  1 18  ? 201.743 56.693  62.442 1.00   17.37 ? 17   ILE C CD1 1 
ATOM   2340  N  N   . ILE C  1 19  ? 202.662 52.741  58.099 1.00   15.17 ? 18   ILE C N   1 
ATOM   2341  C  CA  . ILE C  1 19  ? 203.416 52.430  56.911 1.00   14.78 ? 18   ILE C CA  1 
ATOM   2342  C  C   . ILE C  1 19  ? 203.030 53.424  55.828 1.00   14.85 ? 18   ILE C C   1 
ATOM   2343  O  O   . ILE C  1 19  ? 201.844 53.620  55.536 1.00   14.61 ? 18   ILE C O   1 
ATOM   2344  C  CB  . ILE C  1 19  ? 203.179 50.987  56.459 1.00   14.28 ? 18   ILE C CB  1 
ATOM   2345  C  CG1 . ILE C  1 19  ? 203.680 49.989  57.531 1.00   14.30 ? 18   ILE C CG1 1 
ATOM   2346  C  CG2 . ILE C  1 19  ? 203.867 50.712  55.131 1.00   14.10 ? 18   ILE C CG2 1 
ATOM   2347  C  CD1 . ILE C  1 19  ? 205.172 50.078  57.824 1.00   14.45 ? 18   ILE C CD1 1 
ATOM   2348  N  N   . ASN C  1 20  ? 204.051 54.059  55.269 1.00   15.20 ? 19   ASN C N   1 
ATOM   2349  C  CA  . ASN C  1 20  ? 203.935 54.963  54.133 1.00   15.43 ? 19   ASN C CA  1 
ATOM   2350  C  C   . ASN C  1 20  ? 204.205 54.276  52.799 1.00   15.40 ? 19   ASN C C   1 
ATOM   2351  O  O   . ASN C  1 20  ? 204.998 53.307  52.728 1.00   15.29 ? 19   ASN C O   1 
ATOM   2352  C  CB  . ASN C  1 20  ? 204.930 56.099  54.302 1.00   16.00 ? 19   ASN C CB  1 
ATOM   2353  C  CG  . ASN C  1 20  ? 204.782 56.801  55.638 1.00   16.26 ? 19   ASN C CG  1 
ATOM   2354  O  OD1 . ASN C  1 20  ? 205.645 56.647  56.529 1.00   16.84 ? 19   ASN C OD1 1 
ATOM   2355  N  ND2 . ASN C  1 20  ? 203.706 57.540  55.805 1.00   15.86 ? 19   ASN C ND2 1 
ATOM   2356  N  N   . PHE C  1 21  ? 203.555 54.775  51.748 1.00   15.34 ? 20   PHE C N   1 
ATOM   2357  C  CA  . PHE C  1 21  ? 203.769 54.296  50.383 1.00   15.51 ? 20   PHE C CA  1 
ATOM   2358  C  C   . PHE C  1 21  ? 203.955 55.494  49.447 1.00   16.13 ? 20   PHE C C   1 
ATOM   2359  O  O   . PHE C  1 21  ? 203.199 56.476  49.542 1.00   15.98 ? 20   PHE C O   1 
ATOM   2360  C  CB  . PHE C  1 21  ? 202.561 53.521  49.847 1.00   15.17 ? 20   PHE C CB  1 
ATOM   2361  C  CG  . PHE C  1 21  ? 202.161 52.327  50.671 1.00   14.70 ? 20   PHE C CG  1 
ATOM   2362  C  CD1 . PHE C  1 21  ? 201.348 52.480  51.801 1.00   14.50 ? 20   PHE C CD1 1 
ATOM   2363  C  CD2 . PHE C  1 21  ? 202.517 51.057  50.280 1.00   14.51 ? 20   PHE C CD2 1 
ATOM   2364  C  CE1 . PHE C  1 21  ? 200.969 51.374  52.547 1.00   14.19 ? 20   PHE C CE1 1 
ATOM   2365  C  CE2 . PHE C  1 21  ? 202.139 49.951  51.036 1.00   14.26 ? 20   PHE C CE2 1 
ATOM   2366  C  CZ  . PHE C  1 21  ? 201.353 50.120  52.160 1.00   13.99 ? 20   PHE C CZ  1 
ATOM   2367  N  N   . GLU C  1 22  ? 204.910 55.399  48.519 1.00   16.63 ? 21   GLU C N   1 
ATOM   2368  C  CA  . GLU C  1 22  ? 205.115 56.466  47.546 1.00   17.64 ? 21   GLU C CA  1 
ATOM   2369  C  C   . GLU C  1 22  ? 205.485 55.903  46.170 1.00   18.07 ? 21   GLU C C   1 
ATOM   2370  O  O   . GLU C  1 22  ? 206.343 55.012  46.050 1.00   17.98 ? 21   GLU C O   1 
ATOM   2371  C  CB  . GLU C  1 22  ? 206.180 57.457  48.027 1.00   18.31 ? 21   GLU C CB  1 
ATOM   2372  C  CG  . GLU C  1 22  ? 206.337 58.627  47.086 1.00   19.19 ? 21   GLU C CG  1 
ATOM   2373  C  CD  . GLU C  1 22  ? 207.334 59.660  47.553 0.50   19.76 ? 21   GLU C CD  1 
ATOM   2374  O  OE1 . GLU C  1 22  ? 208.510 59.322  47.785 0.50   20.06 ? 21   GLU C OE1 1 
ATOM   2375  O  OE2 . GLU C  1 22  ? 206.923 60.816  47.652 0.50   20.39 ? 21   GLU C OE2 1 
ATOM   2376  N  N   . GLN C  1 23  ? 204.840 56.445  45.148 1.00   18.42 ? 22   GLN C N   1 
ATOM   2377  C  CA  . GLN C  1 23  ? 205.047 56.027  43.776 1.00   19.46 ? 22   GLN C CA  1 
ATOM   2378  C  C   . GLN C  1 23  ? 205.095 57.291  42.923 1.00   21.04 ? 22   GLN C C   1 
ATOM   2379  O  O   . GLN C  1 23  ? 204.071 57.895  42.670 1.00   21.19 ? 22   GLN C O   1 
ATOM   2380  C  CB  . GLN C  1 23  ? 203.900 55.108  43.334 1.00   18.68 ? 22   GLN C CB  1 
ATOM   2381  C  CG  . GLN C  1 23  ? 204.178 54.293  42.107 1.00   18.64 ? 22   GLN C CG  1 
ATOM   2382  C  CD  . GLN C  1 23  ? 202.967 53.547  41.590 1.00   18.38 ? 22   GLN C CD  1 
ATOM   2383  O  OE1 . GLN C  1 23  ? 201.830 53.778  42.016 1.00   18.09 ? 22   GLN C OE1 1 
ATOM   2384  N  NE2 . GLN C  1 23  ? 203.210 52.610  40.675 1.00   18.46 ? 22   GLN C NE2 1 
ATOM   2385  N  N   . LYS C  1 24  ? 206.296 57.666  42.491 1.00   23.32 ? 23   LYS C N   1 
ATOM   2386  C  CA  . LYS C  1 24  ? 206.562 58.933  41.799 1.00   25.61 ? 23   LYS C CA  1 
ATOM   2387  C  C   . LYS C  1 24  ? 205.909 59.004  40.436 1.00   26.07 ? 23   LYS C C   1 
ATOM   2388  O  O   . LYS C  1 24  ? 205.423 60.049  40.033 1.00   26.00 ? 23   LYS C O   1 
ATOM   2389  C  CB  . LYS C  1 24  ? 208.076 59.117  41.604 1.00   27.94 ? 23   LYS C CB  1 
ATOM   2390  C  CG  . LYS C  1 24  ? 208.823 59.472  42.884 1.00   30.13 ? 23   LYS C CG  1 
ATOM   2391  C  CD  . LYS C  1 24  ? 208.121 60.618  43.615 1.00   31.18 ? 23   LYS C CD  1 
ATOM   2392  C  CE  . LYS C  1 24  ? 209.080 61.664  44.168 1.00   33.17 ? 23   LYS C CE  1 
ATOM   2393  N  NZ  . LYS C  1 24  ? 208.677 63.054  43.729 1.00   34.52 ? 23   LYS C NZ  1 
ATOM   2394  N  N   . GLU C  1 25  ? 205.927 57.886  39.725 1.00   26.22 ? 24   GLU C N   1 
ATOM   2395  C  CA  . GLU C  1 25  ? 205.186 57.768  38.496 1.00   27.66 ? 24   GLU C CA  1 
ATOM   2396  C  C   . GLU C  1 25  ? 204.383 56.508  38.481 1.00   25.78 ? 24   GLU C C   1 
ATOM   2397  O  O   . GLU C  1 25  ? 204.787 55.498  39.019 1.00   25.07 ? 24   GLU C O   1 
ATOM   2398  C  CB  . GLU C  1 25  ? 206.139 57.755  37.287 1.00   30.74 ? 24   GLU C CB  1 
ATOM   2399  C  CG  . GLU C  1 25  ? 206.997 59.003  37.184 1.00   32.84 ? 24   GLU C CG  1 
ATOM   2400  C  CD  . GLU C  1 25  ? 208.324 58.819  37.875 1.00   34.32 ? 24   GLU C CD  1 
ATOM   2401  O  OE1 . GLU C  1 25  ? 208.815 57.674  37.891 1.00   35.80 ? 24   GLU C OE1 1 
ATOM   2402  O  OE2 . GLU C  1 25  ? 208.870 59.818  38.391 1.00   37.34 ? 24   GLU C OE2 1 
ATOM   2403  N  N   . SER C  1 26  ? 203.270 56.565  37.782 1.00   24.93 ? 25   SER C N   1 
ATOM   2404  C  CA  . SER C  1 26  ? 202.309 55.468  37.747 1.00   24.10 ? 25   SER C CA  1 
ATOM   2405  C  C   . SER C  1 26  ? 202.908 54.167  37.225 1.00   23.48 ? 25   SER C C   1 
ATOM   2406  O  O   . SER C  1 26  ? 202.397 53.088  37.521 1.00   22.65 ? 25   SER C O   1 
ATOM   2407  C  CB  . SER C  1 26  ? 201.115 55.881  36.865 1.00   24.17 ? 25   SER C CB  1 
ATOM   2408  O  OG  . SER C  1 26  ? 201.568 56.269  35.589 1.00   24.30 ? 25   SER C OG  1 
ATOM   2409  N  N   . ASN C  1 27  ? 203.964 54.275  36.426 1.00   23.91 ? 26   ASN C N   1 
ATOM   2410  C  CA  . ASN C  1 27  ? 204.658 53.090  35.913 1.00   24.37 ? 26   ASN C CA  1 
ATOM   2411  C  C   . ASN C  1 27  ? 205.980 52.803  36.613 1.00   24.06 ? 26   ASN C C   1 
ATOM   2412  O  O   . ASN C  1 27  ? 206.770 51.983  36.139 1.00   24.95 ? 26   ASN C O   1 
ATOM   2413  C  CB  . ASN C  1 27  ? 204.861 53.178  34.390 1.00   25.31 ? 26   ASN C CB  1 
ATOM   2414  C  CG  . ASN C  1 27  ? 205.832 54.264  33.989 1.00   26.14 ? 26   ASN C CG  1 
ATOM   2415  O  OD1 . ASN C  1 27  ? 205.907 55.314  34.648 1.00   26.71 ? 26   ASN C OD1 1 
ATOM   2416  N  ND2 . ASN C  1 27  ? 206.576 54.028  32.915 1.00   26.18 ? 26   ASN C ND2 1 
ATOM   2417  N  N   . GLY C  1 28  ? 206.214 53.460  37.743 1.00   23.59 ? 27   GLY C N   1 
ATOM   2418  C  CA  . GLY C  1 28  ? 207.430 53.233  38.547 1.00   23.49 ? 27   GLY C CA  1 
ATOM   2419  C  C   . GLY C  1 28  ? 207.200 52.338  39.765 1.00   22.74 ? 27   GLY C C   1 
ATOM   2420  O  O   . GLY C  1 28  ? 206.086 51.889  40.020 1.00   22.20 ? 27   GLY C O   1 
ATOM   2421  N  N   . PRO C  1 29  ? 208.270 52.063  40.518 1.00   22.63 ? 28   PRO C N   1 
ATOM   2422  C  CA  . PRO C  1 29  ? 208.152 51.248  41.711 1.00   22.00 ? 28   PRO C CA  1 
ATOM   2423  C  C   . PRO C  1 29  ? 207.454 51.981  42.849 1.00   21.18 ? 28   PRO C C   1 
ATOM   2424  O  O   . PRO C  1 29  ? 207.365 53.220  42.848 1.00   21.33 ? 28   PRO C O   1 
ATOM   2425  C  CB  . PRO C  1 29  ? 209.594 50.952  42.109 1.00   22.13 ? 28   PRO C CB  1 
ATOM   2426  C  CG  . PRO C  1 29  ? 210.468 51.539  41.053 1.00   23.13 ? 28   PRO C CG  1 
ATOM   2427  C  CD  . PRO C  1 29  ? 209.649 52.535  40.299 1.00   23.45 ? 28   PRO C CD  1 
ATOM   2428  N  N   . VAL C  1 30  ? 206.982 51.204  43.804 1.00   20.04 ? 29   VAL C N   1 
ATOM   2429  C  CA  . VAL C  1 30  ? 206.425 51.752  45.025 1.00   19.84 ? 29   VAL C CA  1 
ATOM   2430  C  C   . VAL C  1 30  ? 207.429 51.572  46.174 1.00   20.10 ? 29   VAL C C   1 
ATOM   2431  O  O   . VAL C  1 30  ? 207.873 50.454  46.429 1.00   19.88 ? 29   VAL C O   1 
ATOM   2432  C  CB  . VAL C  1 30  ? 205.083 51.072  45.380 1.00   19.01 ? 29   VAL C CB  1 
ATOM   2433  C  CG1 . VAL C  1 30  ? 204.533 51.665  46.674 1.00   18.26 ? 29   VAL C CG1 1 
ATOM   2434  C  CG2 . VAL C  1 30  ? 204.085 51.208  44.223 1.00   18.69 ? 29   VAL C CG2 1 
ATOM   2435  N  N   . LYS C  1 31  ? 207.783 52.671  46.842 1.00   20.64 ? 30   LYS C N   1 
ATOM   2436  C  CA  . LYS C  1 31  ? 208.559 52.625  48.080 1.00   21.21 ? 30   LYS C CA  1 
ATOM   2437  C  C   . LYS C  1 31  ? 207.608 52.495  49.251 1.00   19.80 ? 30   LYS C C   1 
ATOM   2438  O  O   . LYS C  1 31  ? 206.606 53.217  49.305 1.00   18.59 ? 30   LYS C O   1 
ATOM   2439  C  CB  . LYS C  1 31  ? 209.394 53.898  48.269 1.00   23.42 ? 30   LYS C CB  1 
ATOM   2440  C  CG  . LYS C  1 31  ? 210.349 54.133  47.100 1.00   26.55 ? 30   LYS C CG  1 
ATOM   2441  C  CD  . LYS C  1 31  ? 211.301 55.319  47.300 1.00   28.93 ? 30   LYS C CD  1 
ATOM   2442  C  CE  . LYS C  1 31  ? 212.503 55.190  46.365 1.00   31.22 ? 30   LYS C CE  1 
ATOM   2443  N  NZ  . LYS C  1 31  ? 213.665 56.027  46.788 1.00   34.02 ? 30   LYS C NZ  1 
ATOM   2444  N  N   . VAL C  1 32  ? 207.939 51.576  50.165 1.00   18.72 ? 31   VAL C N   1 
ATOM   2445  C  CA  . VAL C  1 32  ? 207.145 51.249  51.342 1.00   18.08 ? 31   VAL C CA  1 
ATOM   2446  C  C   . VAL C  1 32  ? 208.066 51.409  52.562 1.00   18.34 ? 31   VAL C C   1 
ATOM   2447  O  O   . VAL C  1 32  ? 209.118 50.757  52.625 1.00   18.37 ? 31   VAL C O   1 
ATOM   2448  C  CB  . VAL C  1 32  ? 206.630 49.793  51.264 1.00   17.71 ? 31   VAL C CB  1 
ATOM   2449  C  CG1 . VAL C  1 32  ? 205.745 49.455  52.456 1.00   17.19 ? 31   VAL C CG1 1 
ATOM   2450  C  CG2 . VAL C  1 32  ? 205.881 49.559  49.963 1.00   17.43 ? 31   VAL C CG2 1 
ATOM   2451  N  N   . TRP C  1 33  ? 207.703 52.267  53.510 1.00   18.20 ? 32   TRP C N   1 
ATOM   2452  C  CA  . TRP C  1 33  ? 208.538 52.468  54.688 1.00   18.79 ? 32   TRP C CA  1 
ATOM   2453  C  C   . TRP C  1 33  ? 207.770 52.977  55.870 1.00   18.75 ? 32   TRP C C   1 
ATOM   2454  O  O   . TRP C  1 33  ? 206.733 53.633  55.719 1.00   18.40 ? 32   TRP C O   1 
ATOM   2455  C  CB  . TRP C  1 33  ? 209.681 53.426  54.390 1.00   19.30 ? 32   TRP C CB  1 
ATOM   2456  C  CG  . TRP C  1 33  ? 209.268 54.865  54.438 1.00   19.61 ? 32   TRP C CG  1 
ATOM   2457  C  CD1 . TRP C  1 33  ? 209.503 55.764  55.456 1.00   20.04 ? 32   TRP C CD1 1 
ATOM   2458  C  CD2 . TRP C  1 33  ? 208.549 55.617  53.412 1.00   19.74 ? 32   TRP C CD2 1 
ATOM   2459  N  NE1 . TRP C  1 33  ? 208.977 56.982  55.152 1.00   20.71 ? 32   TRP C NE1 1 
ATOM   2460  C  CE2 . TRP C  1 33  ? 208.402 56.969  53.931 1.00   20.26 ? 32   TRP C CE2 1 
ATOM   2461  C  CE3 . TRP C  1 33  ? 208.028 55.314  52.176 1.00   19.74 ? 32   TRP C CE3 1 
ATOM   2462  C  CZ2 . TRP C  1 33  ? 207.746 57.963  53.233 1.00   20.50 ? 32   TRP C CZ2 1 
ATOM   2463  C  CZ3 . TRP C  1 33  ? 207.366 56.321  51.472 1.00   20.18 ? 32   TRP C CZ3 1 
ATOM   2464  C  CH2 . TRP C  1 33  ? 207.231 57.627  51.991 1.00   20.27 ? 32   TRP C CH2 1 
ATOM   2465  N  N   . GLY C  1 34  ? 208.280 52.687  57.060 1.00   19.04 ? 33   GLY C N   1 
ATOM   2466  C  CA  . GLY C  1 34  ? 207.659 53.160  58.298 1.00   19.48 ? 33   GLY C CA  1 
ATOM   2467  C  C   . GLY C  1 34  ? 208.116 52.310  59.469 1.00   20.18 ? 33   GLY C C   1 
ATOM   2468  O  O   . GLY C  1 34  ? 209.108 51.619  59.365 1.00   20.89 ? 33   GLY C O   1 
ATOM   2469  N  N   . SER C  1 35  ? 207.409 52.380  60.586 1.00   20.61 ? 34   SER C N   1 
ATOM   2470  C  CA  . SER C  1 35  ? 207.769 51.616  61.777 1.00   21.49 ? 34   SER C CA  1 
ATOM   2471  C  C   . SER C  1 35  ? 206.619 50.822  62.280 1.00   20.67 ? 34   SER C C   1 
ATOM   2472  O  O   . SER C  1 35  ? 205.512 51.344  62.363 1.00   20.11 ? 34   SER C O   1 
ATOM   2473  C  CB  . SER C  1 35  ? 208.186 52.568  62.900 1.00   22.61 ? 34   SER C CB  1 
ATOM   2474  O  OG  . SER C  1 35  ? 209.530 52.912  62.684 1.00   25.27 ? 34   SER C OG  1 
ATOM   2475  N  N   . ILE C  1 36  ? 206.888 49.579  62.651 1.00   20.49 ? 35   ILE C N   1 
ATOM   2476  C  CA  . ILE C  1 36  ? 205.928 48.776  63.383 1.00   20.48 ? 35   ILE C CA  1 
ATOM   2477  C  C   . ILE C  1 36  ? 206.551 48.370  64.707 1.00   21.41 ? 35   ILE C C   1 
ATOM   2478  O  O   . ILE C  1 36  ? 207.654 47.813  64.734 1.00   21.71 ? 35   ILE C O   1 
ATOM   2479  C  CB  . ILE C  1 36  ? 205.551 47.504  62.619 1.00   20.03 ? 35   ILE C CB  1 
ATOM   2480  C  CG1 . ILE C  1 36  ? 205.112 47.827  61.192 1.00   19.73 ? 35   ILE C CG1 1 
ATOM   2481  C  CG2 . ILE C  1 36  ? 204.474 46.729  63.371 1.00   19.90 ? 35   ILE C CG2 1 
ATOM   2482  C  CD1 . ILE C  1 36  ? 204.979 46.605  60.299 1.00   19.31 ? 35   ILE C CD1 1 
ATOM   2483  N  N   . LYS C  1 37  ? 205.841 48.616  65.803 1.00   21.85 ? 36   LYS C N   1 
ATOM   2484  C  CA  . LYS C  1 37  ? 206.325 48.245  67.113 1.00   22.84 ? 36   LYS C CA  1 
ATOM   2485  C  C   . LYS C  1 37  ? 205.448 47.161  67.748 1.00   22.01 ? 36   LYS C C   1 
ATOM   2486  O  O   . LYS C  1 37  ? 204.426 46.755  67.197 1.00   21.23 ? 36   LYS C O   1 
ATOM   2487  C  CB  . LYS C  1 37  ? 206.474 49.489  68.014 1.00   24.40 ? 36   LYS C CB  1 
ATOM   2488  C  CG  . LYS C  1 37  ? 205.188 50.070  68.545 1.00   25.49 ? 36   LYS C CG  1 
ATOM   2489  C  CD  . LYS C  1 37  ? 205.430 51.462  69.124 1.00   27.19 ? 36   LYS C CD  1 
ATOM   2490  C  CE  . LYS C  1 37  ? 204.164 52.019  69.760 1.00   28.23 ? 36   LYS C CE  1 
ATOM   2491  N  NZ  . LYS C  1 37  ? 204.337 53.459  70.120 1.00   30.42 ? 36   LYS C NZ  1 
ATOM   2492  N  N   . GLY C  1 38  ? 205.895 46.671  68.891 1.00   21.73 ? 37   GLY C N   1 
ATOM   2493  C  CA  . GLY C  1 38  ? 205.222 45.607  69.611 1.00   21.66 ? 37   GLY C CA  1 
ATOM   2494  C  C   . GLY C  1 38  ? 205.428 44.216  69.040 1.00   20.98 ? 37   GLY C C   1 
ATOM   2495  O  O   . GLY C  1 38  ? 204.651 43.340  69.320 1.00   20.46 ? 37   GLY C O   1 
ATOM   2496  N  N   . LEU C  1 39  ? 206.479 44.021  68.245 1.00   21.36 ? 38   LEU C N   1 
ATOM   2497  C  CA  . LEU C  1 39  ? 206.743 42.744  67.579 1.00   21.49 ? 38   LEU C CA  1 
ATOM   2498  C  C   . LEU C  1 39  ? 207.815 41.944  68.306 1.00   23.08 ? 38   LEU C C   1 
ATOM   2499  O  O   . LEU C  1 39  ? 208.698 42.524  68.912 1.00   23.69 ? 38   LEU C O   1 
ATOM   2500  C  CB  . LEU C  1 39  ? 207.240 42.971  66.149 1.00   21.02 ? 38   LEU C CB  1 
ATOM   2501  C  CG  . LEU C  1 39  ? 206.222 43.494  65.116 1.00   20.00 ? 38   LEU C CG  1 
ATOM   2502  C  CD1 . LEU C  1 39  ? 206.943 44.014  63.894 1.00   19.51 ? 38   LEU C CD1 1 
ATOM   2503  C  CD2 . LEU C  1 39  ? 205.219 42.412  64.754 1.00   19.54 ? 38   LEU C CD2 1 
ATOM   2504  N  N   . THR C  1 40  ? 207.734 40.608  68.223 1.00   23.74 ? 39   THR C N   1 
ATOM   2505  C  CA  . THR C  1 40  ? 208.815 39.741  68.689 1.00   24.42 ? 39   THR C CA  1 
ATOM   2506  C  C   . THR C  1 40  ? 209.981 39.895  67.713 1.00   24.74 ? 39   THR C C   1 
ATOM   2507  O  O   . THR C  1 40  ? 209.788 40.105  66.512 1.00   24.07 ? 39   THR C O   1 
ATOM   2508  C  CB  . THR C  1 40  ? 208.401 38.258  68.746 1.00   24.39 ? 39   THR C CB  1 
ATOM   2509  O  OG1 . THR C  1 40  ? 207.954 37.846  67.443 1.00   24.66 ? 39   THR C OG1 1 
ATOM   2510  C  CG2 . THR C  1 40  ? 207.285 38.027  69.753 1.00   24.26 ? 39   THR C CG2 1 
ATOM   2511  N  N   . GLU C  1 41  ? 211.191 39.803  68.239 1.00   25.48 ? 40   GLU C N   1 
ATOM   2512  C  CA  . GLU C  1 41  ? 212.398 39.921  67.442 1.00   26.10 ? 40   GLU C CA  1 
ATOM   2513  C  C   . GLU C  1 41  ? 212.391 38.891  66.324 1.00   25.09 ? 40   GLU C C   1 
ATOM   2514  O  O   . GLU C  1 41  ? 211.964 37.753  66.530 1.00   25.46 ? 40   GLU C O   1 
ATOM   2515  C  CB  . GLU C  1 41  ? 213.625 39.719  68.337 1.00   27.85 ? 40   GLU C CB  1 
ATOM   2516  C  CG  . GLU C  1 41  ? 214.952 39.784  67.598 1.00   29.53 ? 40   GLU C CG  1 
ATOM   2517  C  CD  . GLU C  1 41  ? 216.167 39.698  68.524 1.00   31.83 ? 40   GLU C CD  1 
ATOM   2518  O  OE1 . GLU C  1 41  ? 216.016 39.314  69.721 1.00   32.97 ? 40   GLU C OE1 1 
ATOM   2519  O  OE2 . GLU C  1 41  ? 217.270 40.029  68.031 1.00   33.43 ? 40   GLU C OE2 1 
ATOM   2520  N  N   . GLY C  1 42  ? 212.848 39.296  65.138 1.00   24.06 ? 41   GLY C N   1 
ATOM   2521  C  CA  . GLY C  1 42  ? 212.908 38.396  63.980 1.00   22.99 ? 41   GLY C CA  1 
ATOM   2522  C  C   . GLY C  1 42  ? 211.950 38.717  62.837 1.00   21.98 ? 41   GLY C C   1 
ATOM   2523  O  O   . GLY C  1 42  ? 211.390 39.812  62.748 1.00   21.30 ? 41   GLY C O   1 
ATOM   2524  N  N   . LEU C  1 43  ? 211.748 37.719  61.985 1.00   21.31 ? 42   LEU C N   1 
ATOM   2525  C  CA  . LEU C  1 43  ? 210.999 37.858  60.758 1.00   20.61 ? 42   LEU C CA  1 
ATOM   2526  C  C   . LEU C  1 43  ? 209.478 37.785  60.941 1.00   19.50 ? 42   LEU C C   1 
ATOM   2527  O  O   . LEU C  1 43  ? 208.962 36.910  61.646 1.00   19.74 ? 42   LEU C O   1 
ATOM   2528  C  CB  . LEU C  1 43  ? 211.430 36.763  59.785 1.00   21.01 ? 42   LEU C CB  1 
ATOM   2529  C  CG  . LEU C  1 43  ? 212.863 36.747  59.264 1.00   21.36 ? 42   LEU C CG  1 
ATOM   2530  C  CD1 . LEU C  1 43  ? 213.112 35.459  58.477 1.00   21.16 ? 42   LEU C CD1 1 
ATOM   2531  C  CD2 . LEU C  1 43  ? 213.113 37.975  58.409 1.00   21.21 ? 42   LEU C CD2 1 
ATOM   2532  N  N   . HIS C  1 44  ? 208.766 38.681  60.257 1.00   18.24 ? 43   HIS C N   1 
ATOM   2533  C  CA  . HIS C  1 44  ? 207.309 38.627  60.170 1.00   17.52 ? 43   HIS C CA  1 
ATOM   2534  C  C   . HIS C  1 44  ? 206.806 38.827  58.765 1.00   16.86 ? 43   HIS C C   1 
ATOM   2535  O  O   . HIS C  1 44  ? 207.165 39.793  58.080 1.00   16.29 ? 43   HIS C O   1 
ATOM   2536  C  CB  . HIS C  1 44  ? 206.706 39.707  61.063 1.00   17.67 ? 43   HIS C CB  1 
ATOM   2537  C  CG  . HIS C  1 44  ? 207.028 39.523  62.516 1.00   18.19 ? 43   HIS C CG  1 
ATOM   2538  N  ND1 . HIS C  1 44  ? 206.183 38.916  63.381 1.00   18.24 ? 43   HIS C ND1 1 
ATOM   2539  C  CD2 . HIS C  1 44  ? 208.169 39.871  63.247 1.00   18.68 ? 43   HIS C CD2 1 
ATOM   2540  C  CE1 . HIS C  1 44  ? 206.756 38.887  64.608 1.00   18.88 ? 43   HIS C CE1 1 
ATOM   2541  N  NE2 . HIS C  1 44  ? 207.972 39.464  64.523 1.00   18.92 ? 43   HIS C NE2 1 
ATOM   2542  N  N   . GLY C  1 45  ? 205.902 37.949  58.350 1.00   16.50 ? 44   GLY C N   1 
ATOM   2543  C  CA  . GLY C  1 45  ? 205.252 38.087  57.064 1.00   16.02 ? 44   GLY C CA  1 
ATOM   2544  C  C   . GLY C  1 45  ? 204.569 39.434  56.948 1.00   15.53 ? 44   GLY C C   1 
ATOM   2545  O  O   . GLY C  1 45  ? 204.023 39.945  57.930 1.00   15.72 ? 44   GLY C O   1 
ATOM   2546  N  N   . PHE C  1 46  ? 204.599 39.984  55.742 1.00   15.09 ? 45   PHE C N   1 
ATOM   2547  C  CA  . PHE C  1 46  ? 204.154 41.346  55.456 1.00   14.77 ? 45   PHE C CA  1 
ATOM   2548  C  C   . PHE C  1 46  ? 203.474 41.318  54.091 1.00   14.47 ? 45   PHE C C   1 
ATOM   2549  O  O   . PHE C  1 46  ? 204.160 41.150  53.080 1.00   14.61 ? 45   PHE C O   1 
ATOM   2550  C  CB  . PHE C  1 46  ? 205.379 42.236  55.428 1.00   14.70 ? 45   PHE C CB  1 
ATOM   2551  C  CG  . PHE C  1 46  ? 205.090 43.709  55.407 1.00   14.73 ? 45   PHE C CG  1 
ATOM   2552  C  CD1 . PHE C  1 46  ? 204.415 44.311  56.460 1.00   14.78 ? 45   PHE C CD1 1 
ATOM   2553  C  CD2 . PHE C  1 46  ? 205.605 44.503  54.410 1.00   14.76 ? 45   PHE C CD2 1 
ATOM   2554  C  CE1 . PHE C  1 46  ? 204.204 45.678  56.488 1.00   14.92 ? 45   PHE C CE1 1 
ATOM   2555  C  CE2 . PHE C  1 46  ? 205.389 45.872  54.398 1.00   14.92 ? 45   PHE C CE2 1 
ATOM   2556  C  CZ  . PHE C  1 46  ? 204.686 46.470  55.437 1.00   14.95 ? 45   PHE C CZ  1 
ATOM   2557  N  N   . HIS C  1 47  ? 202.138 41.416  54.055 1.00   14.19 ? 46   HIS C N   1 
ATOM   2558  C  CA  . HIS C  1 47  ? 201.386 41.214  52.822 1.00   14.17 ? 46   HIS C CA  1 
ATOM   2559  C  C   . HIS C  1 47  ? 200.247 42.164  52.637 1.00   14.05 ? 46   HIS C C   1 
ATOM   2560  O  O   . HIS C  1 47  ? 199.618 42.618  53.598 1.00   13.81 ? 46   HIS C O   1 
ATOM   2561  C  CB  . HIS C  1 47  ? 200.768 39.827  52.758 1.00   14.53 ? 46   HIS C CB  1 
ATOM   2562  C  CG  . HIS C  1 47  ? 201.669 38.714  53.203 1.00   14.85 ? 46   HIS C CG  1 
ATOM   2563  N  ND1 . HIS C  1 47  ? 201.317 37.860  54.149 1.00   15.07 ? 46   HIS C ND1 1 
ATOM   2564  C  CD2 . HIS C  1 47  ? 202.922 38.314  52.762 1.00   15.18 ? 46   HIS C CD2 1 
ATOM   2565  C  CE1 . HIS C  1 47  ? 202.261 36.948  54.333 1.00   15.28 ? 46   HIS C CE1 1 
ATOM   2566  N  NE2 . HIS C  1 47  ? 203.266 37.225  53.486 1.00   15.47 ? 46   HIS C NE2 1 
ATOM   2567  N  N   . VAL C  1 48  ? 199.918 42.407  51.376 1.00   13.92 ? 47   VAL C N   1 
ATOM   2568  C  CA  . VAL C  1 48  ? 198.682 43.061  51.042 1.00   13.95 ? 47   VAL C CA  1 
ATOM   2569  C  C   . VAL C  1 48  ? 197.622 41.980  50.834 1.00   14.19 ? 47   VAL C C   1 
ATOM   2570  O  O   . VAL C  1 48  ? 197.759 41.121  49.984 1.00   14.25 ? 47   VAL C O   1 
ATOM   2571  C  CB  . VAL C  1 48  ? 198.819 43.956  49.785 1.00   13.89 ? 47   VAL C CB  1 
ATOM   2572  C  CG1 . VAL C  1 48  ? 197.494 44.669  49.489 1.00   13.90 ? 47   VAL C CG1 1 
ATOM   2573  C  CG2 . VAL C  1 48  ? 199.936 44.963  49.968 1.00   13.76 ? 47   VAL C CG2 1 
ATOM   2574  N  N   . HIS C  1 49  ? 196.589 42.013  51.662 1.00   14.62 ? 48   HIS C N   1 
ATOM   2575  C  CA  . HIS C  1 49  ? 195.439 41.150  51.502 1.00   15.18 ? 48   HIS C CA  1 
ATOM   2576  C  C   . HIS C  1 49  ? 194.376 41.805  50.652 1.00   15.67 ? 48   HIS C C   1 
ATOM   2577  O  O   . HIS C  1 49  ? 194.324 43.029  50.512 1.00   15.44 ? 48   HIS C O   1 
ATOM   2578  C  CB  . HIS C  1 49  ? 194.884 40.747  52.850 1.00   15.18 ? 48   HIS C CB  1 
ATOM   2579  C  CG  . HIS C  1 49  ? 195.731 39.741  53.558 1.00   15.26 ? 48   HIS C CG  1 
ATOM   2580  N  ND1 . HIS C  1 49  ? 195.273 38.539  53.910 1.00   15.76 ? 48   HIS C ND1 1 
ATOM   2581  C  CD2 . HIS C  1 49  ? 197.067 39.763  53.894 1.00   15.10 ? 48   HIS C CD2 1 
ATOM   2582  C  CE1 . HIS C  1 49  ? 196.269 37.839  54.491 1.00   15.82 ? 48   HIS C CE1 1 
ATOM   2583  N  NE2 . HIS C  1 49  ? 197.353 38.597  54.483 1.00   15.44 ? 48   HIS C NE2 1 
ATOM   2584  N  N   . GLU C  1 50  ? 193.514 40.971  50.095 1.00   16.51 ? 49   GLU C N   1 
ATOM   2585  C  CA  . GLU C  1 50  ? 192.605 41.375  49.035 1.00   17.16 ? 49   GLU C CA  1 
ATOM   2586  C  C   . GLU C  1 50  ? 191.591 42.462  49.394 1.00   17.04 ? 49   GLU C C   1 
ATOM   2587  O  O   . GLU C  1 50  ? 191.422 43.407  48.638 1.00   16.77 ? 49   GLU C O   1 
ATOM   2588  C  CB  . GLU C  1 50  ? 191.850 40.153  48.534 1.00   18.20 ? 49   GLU C CB  1 
ATOM   2589  C  CG  . GLU C  1 50  ? 190.961 40.470  47.345 1.00   19.11 ? 49   GLU C CG  1 
ATOM   2590  C  CD  . GLU C  1 50  ? 190.434 39.236  46.645 1.00   20.51 ? 49   GLU C CD  1 
ATOM   2591  O  OE1 . GLU C  1 50  ? 190.595 38.092  47.147 1.00   21.58 ? 49   GLU C OE1 1 
ATOM   2592  O  OE2 . GLU C  1 50  ? 189.826 39.435  45.579 1.00   22.15 ? 49   GLU C OE2 1 
ATOM   2593  N  N   . PHE C  1 51  ? 190.898 42.312  50.516 1.00   17.19 ? 50   PHE C N   1 
ATOM   2594  C  CA  . PHE C  1 51  ? 189.798 43.214  50.853 1.00   17.51 ? 50   PHE C CA  1 
ATOM   2595  C  C   . PHE C  1 51  ? 190.156 44.163  51.999 1.00   17.19 ? 50   PHE C C   1 
ATOM   2596  O  O   . PHE C  1 51  ? 190.834 43.778  52.960 1.00   16.78 ? 50   PHE C O   1 
ATOM   2597  C  CB  . PHE C  1 51  ? 188.556 42.428  51.222 1.00   18.26 ? 50   PHE C CB  1 
ATOM   2598  C  CG  . PHE C  1 51  ? 188.174 41.410  50.208 1.00   19.15 ? 50   PHE C CG  1 
ATOM   2599  C  CD1 . PHE C  1 51  ? 187.731 41.798  48.958 1.00   19.57 ? 50   PHE C CD1 1 
ATOM   2600  C  CD2 . PHE C  1 51  ? 188.250 40.052  50.508 1.00   19.82 ? 50   PHE C CD2 1 
ATOM   2601  C  CE1 . PHE C  1 51  ? 187.387 40.855  48.022 1.00   20.32 ? 50   PHE C CE1 1 
ATOM   2602  C  CE2 . PHE C  1 51  ? 187.894 39.095  49.571 1.00   20.41 ? 50   PHE C CE2 1 
ATOM   2603  C  CZ  . PHE C  1 51  ? 187.483 39.498  48.325 1.00   20.72 ? 50   PHE C CZ  1 
ATOM   2604  N  N   . GLY C  1 52  ? 189.730 45.415  51.868 1.00   16.97 ? 51   GLY C N   1 
ATOM   2605  C  CA  . GLY C  1 52  ? 189.882 46.406  52.932 1.00   16.99 ? 51   GLY C CA  1 
ATOM   2606  C  C   . GLY C  1 52  ? 188.669 46.366  53.842 1.00   17.49 ? 51   GLY C C   1 
ATOM   2607  O  O   . GLY C  1 52  ? 187.978 47.370  54.034 1.00   17.51 ? 51   GLY C O   1 
ATOM   2608  N  N   . ASP C  1 53  ? 188.438 45.188  54.404 1.00   18.23 ? 52   ASP C N   1 
ATOM   2609  C  CA  . ASP C  1 53  ? 187.276 44.869  55.241 1.00   18.99 ? 52   ASP C CA  1 
ATOM   2610  C  C   . ASP C  1 53  ? 187.779 44.451  56.619 1.00   19.63 ? 52   ASP C C   1 
ATOM   2611  O  O   . ASP C  1 53  ? 188.333 43.365  56.789 1.00   19.79 ? 52   ASP C O   1 
ATOM   2612  C  CB  . ASP C  1 53  ? 186.489 43.731  54.582 1.00   19.39 ? 52   ASP C CB  1 
ATOM   2613  C  CG  . ASP C  1 53  ? 185.204 43.346  55.340 1.00   19.60 ? 52   ASP C CG  1 
ATOM   2614  O  OD1 . ASP C  1 53  ? 185.089 43.574  56.554 1.00   19.50 ? 52   ASP C OD1 1 
ATOM   2615  O  OD2 . ASP C  1 53  ? 184.312 42.789  54.688 1.00   19.89 ? 52   ASP C OD2 1 
ATOM   2616  N  N   . ASN C  1 54  ? 187.573 45.331  57.587 1.00   20.53 ? 53   ASN C N   1 
ATOM   2617  C  CA  . ASN C  1 54  ? 187.957 45.117  58.960 1.00   21.67 ? 53   ASN C CA  1 
ATOM   2618  C  C   . ASN C  1 54  ? 186.740 44.823  59.856 1.00   21.21 ? 53   ASN C C   1 
ATOM   2619  O  O   . ASN C  1 54  ? 186.822 44.944  61.071 1.00   21.28 ? 53   ASN C O   1 
ATOM   2620  C  CB  . ASN C  1 54  ? 188.690 46.368  59.474 1.00   23.24 ? 53   ASN C CB  1 
ATOM   2621  C  CG  . ASN C  1 54  ? 189.417 46.127  60.771 1.00   25.01 ? 53   ASN C CG  1 
ATOM   2622  O  OD1 . ASN C  1 54  ? 190.163 45.156  60.894 1.00   27.64 ? 53   ASN C OD1 1 
ATOM   2623  N  ND2 . ASN C  1 54  ? 189.219 47.022  61.747 1.00   25.94 ? 53   ASN C ND2 1 
ATOM   2624  N  N   . THR C  1 55  ? 185.633 44.408  59.260 1.00   20.41 ? 54   THR C N   1 
ATOM   2625  C  CA  . THR C  1 55  ? 184.413 44.211  60.027 1.00   20.68 ? 54   THR C CA  1 
ATOM   2626  C  C   . THR C  1 55  ? 184.545 43.098  61.062 1.00   21.53 ? 54   THR C C   1 
ATOM   2627  O  O   . THR C  1 55  ? 183.891 43.163  62.077 1.00   22.03 ? 54   THR C O   1 
ATOM   2628  C  CB  . THR C  1 55  ? 183.185 43.929  59.140 1.00   20.34 ? 54   THR C CB  1 
ATOM   2629  O  OG1 . THR C  1 55  ? 183.418 42.761  58.334 1.00   20.02 ? 54   THR C OG1 1 
ATOM   2630  C  CG2 . THR C  1 55  ? 182.856 45.153  58.285 1.00   19.53 ? 54   THR C CG2 1 
ATOM   2631  N  N   . ALA C  1 56  ? 185.369 42.081  60.802 1.00   21.80 ? 55   ALA C N   1 
ATOM   2632  C  CA  . ALA C  1 56  ? 185.675 41.075  61.817 1.00   22.36 ? 55   ALA C CA  1 
ATOM   2633  C  C   . ALA C  1 56  ? 187.172 41.083  62.084 1.00   22.32 ? 55   ALA C C   1 
ATOM   2634  O  O   . ALA C  1 56  ? 187.809 40.029  62.089 1.00   23.61 ? 55   ALA C O   1 
ATOM   2635  C  CB  . ALA C  1 56  ? 185.200 39.686  61.384 1.00   22.60 ? 55   ALA C CB  1 
ATOM   2636  N  N   . GLY C  1 57  ? 187.749 42.265  62.289 1.00   21.57 ? 56   GLY C N   1 
ATOM   2637  C  CA  . GLY C  1 57  ? 189.185 42.355  62.537 1.00   21.15 ? 56   GLY C CA  1 
ATOM   2638  C  C   . GLY C  1 57  ? 189.980 42.023  61.284 1.00   21.02 ? 56   GLY C C   1 
ATOM   2639  O  O   . GLY C  1 57  ? 189.471 42.148  60.160 1.00   21.42 ? 56   GLY C O   1 
ATOM   2640  N  N   . CYS C  1 58  ? 191.219 41.587  61.462 1.00   20.50 ? 57   CYS C N   1 
ATOM   2641  C  CA  . CYS C  1 58  ? 192.071 41.263  60.321 1.00   20.17 ? 57   CYS C CA  1 
ATOM   2642  C  C   . CYS C  1 58  ? 191.566 40.070  59.510 1.00   20.35 ? 57   CYS C C   1 
ATOM   2643  O  O   . CYS C  1 58  ? 191.885 39.943  58.317 1.00   19.99 ? 57   CYS C O   1 
ATOM   2644  C  CB  . CYS C  1 58  ? 193.488 41.012  60.791 1.00   19.93 ? 57   CYS C CB  1 
ATOM   2645  S  SG  . CYS C  1 58  ? 194.211 42.455  61.577 1.00   19.86 ? 57   CYS C SG  1 
ATOM   2646  N  N   . THR C  1 59  ? 190.790 39.185  60.143 1.00   20.52 ? 58   THR C N   1 
ATOM   2647  C  CA  . THR C  1 59  ? 190.269 38.006  59.441 1.00   21.27 ? 58   THR C CA  1 
ATOM   2648  C  C   . THR C  1 59  ? 189.393 38.332  58.246 1.00   20.71 ? 58   THR C C   1 
ATOM   2649  O  O   . THR C  1 59  ? 189.373 37.599  57.292 1.00   21.05 ? 58   THR C O   1 
ATOM   2650  C  CB  . THR C  1 59  ? 189.403 37.135  60.361 1.00   22.64 ? 58   THR C CB  1 
ATOM   2651  O  OG1 . THR C  1 59  ? 190.047 37.048  61.633 1.00   24.25 ? 58   THR C OG1 1 
ATOM   2652  C  CG2 . THR C  1 59  ? 189.206 35.752  59.749 1.00   22.69 ? 58   THR C CG2 1 
ATOM   2653  N  N   . SER C  1 60  ? 188.653 39.422  58.270 1.00   20.49 ? 59   SER C N   1 
ATOM   2654  C  CA  . SER C  1 60  ? 187.830 39.729  57.094 1.00   20.62 ? 59   SER C CA  1 
ATOM   2655  C  C   . SER C  1 60  ? 188.598 40.315  55.913 1.00   19.76 ? 59   SER C C   1 
ATOM   2656  O  O   . SER C  1 60  ? 187.999 40.585  54.872 1.00   19.92 ? 59   SER C O   1 
ATOM   2657  C  CB  . SER C  1 60  ? 186.638 40.611  57.471 1.00   21.29 ? 59   SER C CB  1 
ATOM   2658  O  OG  . SER C  1 60  ? 186.937 41.415  58.585 1.00   22.00 ? 59   SER C OG  1 
ATOM   2659  N  N   . ALA C  1 61  ? 189.911 40.497  56.041 1.00   18.85 ? 60   ALA C N   1 
ATOM   2660  C  CA  . ALA C  1 61  ? 190.714 41.000  54.907 1.00   18.55 ? 60   ALA C CA  1 
ATOM   2661  C  C   . ALA C  1 61  ? 190.864 39.993  53.752 1.00   18.67 ? 60   ALA C C   1 
ATOM   2662  O  O   . ALA C  1 61  ? 191.372 40.342  52.677 1.00   18.63 ? 60   ALA C O   1 
ATOM   2663  C  CB  . ALA C  1 61  ? 192.087 41.455  55.401 1.00   18.08 ? 60   ALA C CB  1 
ATOM   2664  N  N   . GLY C  1 62  ? 190.474 38.738  53.985 1.00   18.89 ? 61   GLY C N   1 
ATOM   2665  C  CA  . GLY C  1 62  ? 190.560 37.693  52.973 1.00   19.00 ? 61   GLY C CA  1 
ATOM   2666  C  C   . GLY C  1 62  ? 191.981 37.246  52.698 1.00   18.69 ? 61   GLY C C   1 
ATOM   2667  O  O   . GLY C  1 62  ? 192.870 37.514  53.486 1.00   18.34 ? 61   GLY C O   1 
ATOM   2668  N  N   . PRO C  1 63  ? 192.204 36.571  51.563 1.00   19.06 ? 62   PRO C N   1 
ATOM   2669  C  CA  . PRO C  1 63  ? 193.520 36.017  51.227 1.00   18.95 ? 62   PRO C CA  1 
ATOM   2670  C  C   . PRO C  1 63  ? 194.408 37.091  50.623 1.00   18.52 ? 62   PRO C C   1 
ATOM   2671  O  O   . PRO C  1 63  ? 194.009 38.265  50.558 1.00   18.43 ? 62   PRO C O   1 
ATOM   2672  C  CB  . PRO C  1 63  ? 193.192 34.946  50.186 1.00   19.59 ? 62   PRO C CB  1 
ATOM   2673  C  CG  . PRO C  1 63  ? 191.995 35.519  49.462 1.00   19.86 ? 62   PRO C CG  1 
ATOM   2674  C  CD  . PRO C  1 63  ? 191.202 36.276  50.516 1.00   19.58 ? 62   PRO C CD  1 
ATOM   2675  N  N   . HIS C  1 64  ? 195.601 36.704  50.203 1.00   18.13 ? 63   HIS C N   1 
ATOM   2676  C  CA  . HIS C  1 64  ? 196.535 37.642  49.553 1.00   17.94 ? 63   HIS C CA  1 
ATOM   2677  C  C   . HIS C  1 64  ? 195.984 38.183  48.272 1.00   18.07 ? 63   HIS C C   1 
ATOM   2678  O  O   . HIS C  1 64  ? 195.275 37.484  47.547 1.00   18.48 ? 63   HIS C O   1 
ATOM   2679  C  CB  . HIS C  1 64  ? 197.884 36.988  49.322 1.00   17.89 ? 63   HIS C CB  1 
ATOM   2680  C  CG  . HIS C  1 64  ? 198.574 36.595  50.600 1.00   18.03 ? 63   HIS C CG  1 
ATOM   2681  N  ND1 . HIS C  1 64  ? 199.757 35.928  50.631 1.00   17.76 ? 63   HIS C ND1 1 
ATOM   2682  C  CD2 . HIS C  1 64  ? 198.181 36.783  51.930 1.00   18.00 ? 63   HIS C CD2 1 
ATOM   2683  C  CE1 . HIS C  1 64  ? 200.100 35.708  51.916 1.00   18.23 ? 63   HIS C CE1 1 
ATOM   2684  N  NE2 . HIS C  1 64  ? 199.142 36.241  52.717 1.00   18.41 ? 63   HIS C NE2 1 
ATOM   2685  N  N   . PHE C  1 65  ? 196.255 39.465  48.020 1.00   17.90 ? 64   PHE C N   1 
ATOM   2686  C  CA  . PHE C  1 65  ? 195.802 40.112  46.806 1.00   17.93 ? 64   PHE C CA  1 
ATOM   2687  C  C   . PHE C  1 65  ? 196.505 39.427  45.626 1.00   18.40 ? 64   PHE C C   1 
ATOM   2688  O  O   . PHE C  1 65  ? 197.734 39.408  45.561 1.00   17.92 ? 64   PHE C O   1 
ATOM   2689  C  CB  . PHE C  1 65  ? 196.091 41.613  46.855 1.00   17.25 ? 64   PHE C CB  1 
ATOM   2690  C  CG  . PHE C  1 65  ? 195.729 42.354  45.591 1.00   17.28 ? 64   PHE C CG  1 
ATOM   2691  C  CD1 . PHE C  1 65  ? 194.508 42.158  44.969 1.00   17.58 ? 64   PHE C CD1 1 
ATOM   2692  C  CD2 . PHE C  1 65  ? 196.613 43.265  45.026 1.00   17.18 ? 64   PHE C CD2 1 
ATOM   2693  C  CE1 . PHE C  1 65  ? 194.183 42.840  43.802 1.00   17.71 ? 64   PHE C CE1 1 
ATOM   2694  C  CE2 . PHE C  1 65  ? 196.289 43.949  43.862 1.00   17.29 ? 64   PHE C CE2 1 
ATOM   2695  C  CZ  . PHE C  1 65  ? 195.073 43.741  43.258 1.00   17.51 ? 64   PHE C CZ  1 
ATOM   2696  N  N   . ASN C  1 66  ? 195.700 38.882  44.709 1.00   19.30 ? 65   ASN C N   1 
ATOM   2697  C  CA  . ASN C  1 66  ? 196.164 37.918  43.698 1.00   20.40 ? 65   ASN C CA  1 
ATOM   2698  C  C   . ASN C  1 66  ? 195.352 38.017  42.396 1.00   21.64 ? 65   ASN C C   1 
ATOM   2699  O  O   . ASN C  1 66  ? 194.712 37.057  41.993 1.00   22.89 ? 65   ASN C O   1 
ATOM   2700  C  CB  . ASN C  1 66  ? 196.054 36.494  44.268 1.00   20.39 ? 65   ASN C CB  1 
ATOM   2701  C  CG  . ASN C  1 66  ? 196.759 35.436  43.410 1.00   20.81 ? 65   ASN C CG  1 
ATOM   2702  O  OD1 . ASN C  1 66  ? 197.660 35.736  42.607 1.00   20.91 ? 65   ASN C OD1 1 
ATOM   2703  N  ND2 . ASN C  1 66  ? 196.367 34.187  43.598 1.00   20.55 ? 65   ASN C ND2 1 
ATOM   2704  N  N   . PRO C  1 67  ? 195.390 39.169  41.723 1.00   22.14 ? 66   PRO C N   1 
ATOM   2705  C  CA  . PRO C  1 67  ? 194.574 39.320  40.520 1.00   23.63 ? 66   PRO C CA  1 
ATOM   2706  C  C   . PRO C  1 67  ? 195.040 38.431  39.356 1.00   24.74 ? 66   PRO C C   1 
ATOM   2707  O  O   . PRO C  1 67  ? 194.266 38.191  38.461 1.00   25.85 ? 66   PRO C O   1 
ATOM   2708  C  CB  . PRO C  1 67  ? 194.746 40.803  40.162 1.00   23.12 ? 66   PRO C CB  1 
ATOM   2709  C  CG  . PRO C  1 67  ? 196.096 41.144  40.699 1.00   22.40 ? 66   PRO C CG  1 
ATOM   2710  C  CD  . PRO C  1 67  ? 196.214 40.358  41.978 1.00   21.86 ? 66   PRO C CD  1 
ATOM   2711  N  N   . LEU C  1 68  ? 196.281 37.941  39.384 1.00   25.88 ? 67   LEU C N   1 
ATOM   2712  C  CA  . LEU C  1 68  ? 196.770 37.027  38.334 1.00   26.87 ? 67   LEU C CA  1 
ATOM   2713  C  C   . LEU C  1 68  ? 196.676 35.539  38.702 1.00   27.67 ? 67   LEU C C   1 
ATOM   2714  O  O   . LEU C  1 68  ? 197.138 34.675  37.961 1.00   29.60 ? 67   LEU C O   1 
ATOM   2715  C  CB  . LEU C  1 68  ? 198.177 37.411  37.920 1.00   26.81 ? 67   LEU C CB  1 
ATOM   2716  C  CG  . LEU C  1 68  ? 198.279 38.827  37.355 1.00   27.03 ? 67   LEU C CG  1 
ATOM   2717  C  CD1 . LEU C  1 68  ? 199.740 39.247  37.215 1.00   26.82 ? 67   LEU C CD1 1 
ATOM   2718  C  CD2 . LEU C  1 68  ? 197.547 38.905  36.010 1.00   28.19 ? 67   LEU C CD2 1 
ATOM   2719  N  N   . SER C  1 69  ? 196.047 35.234  39.825 1.00   27.89 ? 68   SER C N   1 
ATOM   2720  C  CA  . SER C  1 69  ? 195.775 33.853  40.212 1.00   28.82 ? 68   SER C CA  1 
ATOM   2721  C  C   . SER C  1 69  ? 197.034 33.017  40.199 1.00   29.52 ? 68   SER C C   1 
ATOM   2722  O  O   . SER C  1 69  ? 197.078 31.958  39.582 1.00   30.88 ? 68   SER C O   1 
ATOM   2723  C  CB  . SER C  1 69  ? 194.699 33.237  39.305 1.00   29.65 ? 68   SER C CB  1 
ATOM   2724  O  OG  . SER C  1 69  ? 193.502 34.008  39.369 1.00   29.55 ? 68   SER C OG  1 
ATOM   2725  N  N   . ARG C  1 70  ? 198.068 33.510  40.873 1.00   29.45 ? 69   ARG C N   1 
ATOM   2726  C  CA  . ARG C  1 70  ? 199.324 32.789  40.986 1.00   29.95 ? 69   ARG C CA  1 
ATOM   2727  C  C   . ARG C  1 70  ? 199.459 32.170  42.359 1.00   28.28 ? 69   ARG C C   1 
ATOM   2728  O  O   . ARG C  1 70  ? 198.600 32.352  43.211 1.00   27.04 ? 69   ARG C O   1 
ATOM   2729  C  CB  . ARG C  1 70  ? 200.500 33.705  40.681 1.00   31.34 ? 69   ARG C CB  1 
ATOM   2730  C  CG  . ARG C  1 70  ? 200.386 34.260  39.283 1.00   34.40 ? 69   ARG C CG  1 
ATOM   2731  C  CD  . ARG C  1 70  ? 201.720 34.549  38.620 1.00   37.71 ? 69   ARG C CD  1 
ATOM   2732  N  NE  . ARG C  1 70  ? 201.503 35.417  37.458 1.00   41.74 ? 69   ARG C NE  1 
ATOM   2733  C  CZ  . ARG C  1 70  ? 202.404 35.705  36.525 1.00   43.86 ? 69   ARG C CZ  1 
ATOM   2734  N  NH1 . ARG C  1 70  ? 203.640 35.200  36.575 1.00   45.89 ? 69   ARG C NH1 1 
ATOM   2735  N  NH2 . ARG C  1 70  ? 202.054 36.500  35.524 1.00   44.28 ? 69   ARG C NH2 1 
ATOM   2736  N  N   . LYS C  1 71  ? 200.529 31.411  42.546 1.00   27.61 ? 70   LYS C N   1 
ATOM   2737  C  CA  . LYS C  1 71  ? 200.859 30.860  43.858 1.00   27.38 ? 70   LYS C CA  1 
ATOM   2738  C  C   . LYS C  1 71  ? 201.719 31.845  44.648 1.00   24.84 ? 70   LYS C C   1 
ATOM   2739  O  O   . LYS C  1 71  ? 202.350 32.731  44.082 1.00   24.19 ? 70   LYS C O   1 
ATOM   2740  C  CB  . LYS C  1 71  ? 201.546 29.485  43.711 1.00   28.98 ? 70   LYS C CB  1 
ATOM   2741  C  CG  . LYS C  1 71  ? 200.527 28.377  43.450 1.00   31.23 ? 70   LYS C CG  1 
ATOM   2742  C  CD  . LYS C  1 71  ? 201.112 26.970  43.457 1.00   34.10 ? 70   LYS C CD  1 
ATOM   2743  C  CE  . LYS C  1 71  ? 201.648 26.559  42.085 1.00   36.23 ? 70   LYS C CE  1 
ATOM   2744  N  NZ  . LYS C  1 71  ? 201.689 25.069  41.939 1.00   38.51 ? 70   LYS C NZ  1 
ATOM   2745  N  N   . HIS C  1 72  ? 201.725 31.668  45.960 1.00   23.59 ? 71   HIS C N   1 
ATOM   2746  C  CA  . HIS C  1 72  ? 202.473 32.519  46.884 1.00   22.34 ? 71   HIS C CA  1 
ATOM   2747  C  C   . HIS C  1 72  ? 203.953 32.375  46.685 1.00   22.20 ? 71   HIS C C   1 
ATOM   2748  O  O   . HIS C  1 72  ? 204.420 31.281  46.475 1.00   22.91 ? 71   HIS C O   1 
ATOM   2749  C  CB  . HIS C  1 72  ? 202.126 32.166  48.322 1.00   21.42 ? 71   HIS C CB  1 
ATOM   2750  C  CG  . HIS C  1 72  ? 202.836 33.018  49.357 1.00   21.02 ? 71   HIS C CG  1 
ATOM   2751  N  ND1 . HIS C  1 72  ? 202.383 34.232  49.743 1.00   20.76 ? 71   HIS C ND1 1 
ATOM   2752  C  CD2 . HIS C  1 72  ? 203.996 32.776  50.101 1.00   20.45 ? 71   HIS C CD2 1 
ATOM   2753  C  CE1 . HIS C  1 72  ? 203.211 34.734  50.686 1.00   20.40 ? 71   HIS C CE1 1 
ATOM   2754  N  NE2 . HIS C  1 72  ? 204.201 33.843  50.896 1.00   20.32 ? 71   HIS C NE2 1 
ATOM   2755  N  N   . GLY C  1 73  ? 204.688 33.485  46.760 1.00   21.39 ? 72   GLY C N   1 
ATOM   2756  C  CA  . GLY C  1 73  ? 206.133 33.485  46.710 1.00   21.30 ? 72   GLY C CA  1 
ATOM   2757  C  C   . GLY C  1 73  ? 206.714 34.650  47.492 1.00   20.79 ? 72   GLY C C   1 
ATOM   2758  O  O   . GLY C  1 73  ? 205.993 35.363  48.198 1.00   20.81 ? 72   GLY C O   1 
ATOM   2759  N  N   . GLY C  1 74  ? 208.028 34.832  47.384 1.00   20.36 ? 73   GLY C N   1 
ATOM   2760  C  CA  . GLY C  1 74  ? 208.676 36.056  47.839 1.00   20.05 ? 73   GLY C CA  1 
ATOM   2761  C  C   . GLY C  1 74  ? 208.527 37.132  46.774 1.00   20.17 ? 73   GLY C C   1 
ATOM   2762  O  O   . GLY C  1 74  ? 208.213 36.825  45.603 1.00   20.00 ? 73   GLY C O   1 
ATOM   2763  N  N   . PRO C  1 75  ? 208.738 38.401  47.158 1.00   19.96 ? 74   PRO C N   1 
ATOM   2764  C  CA  . PRO C  1 75  ? 208.554 39.482  46.206 1.00   20.14 ? 74   PRO C CA  1 
ATOM   2765  C  C   . PRO C  1 75  ? 209.524 39.431  45.019 1.00   21.31 ? 74   PRO C C   1 
ATOM   2766  O  O   . PRO C  1 75  ? 209.205 39.970  43.943 1.00   21.16 ? 74   PRO C O   1 
ATOM   2767  C  CB  . PRO C  1 75  ? 208.804 40.737  47.048 1.00   19.78 ? 74   PRO C CB  1 
ATOM   2768  C  CG  . PRO C  1 75  ? 209.691 40.269  48.165 1.00   19.68 ? 74   PRO C CG  1 
ATOM   2769  C  CD  . PRO C  1 75  ? 209.191 38.896  48.471 1.00   19.66 ? 74   PRO C CD  1 
ATOM   2770  N  N   . LYS C  1 76  ? 210.685 38.801  45.198 1.00   22.33 ? 75   LYS C N   1 
ATOM   2771  C  CA  . LYS C  1 76  ? 211.625 38.630  44.083 1.00   24.01 ? 75   LYS C CA  1 
ATOM   2772  C  C   . LYS C  1 76  ? 211.214 37.572  43.061 1.00   24.43 ? 75   LYS C C   1 
ATOM   2773  O  O   . LYS C  1 76  ? 211.820 37.495  41.999 1.00   24.60 ? 75   LYS C O   1 
ATOM   2774  C  CB  . LYS C  1 76  ? 213.020 38.293  44.600 1.00   24.90 ? 75   LYS C CB  1 
ATOM   2775  C  CG  . LYS C  1 76  ? 213.652 39.417  45.404 1.00   25.72 ? 75   LYS C CG  1 
ATOM   2776  C  CD  . LYS C  1 76  ? 214.864 38.900  46.178 1.00   26.94 ? 75   LYS C CD  1 
ATOM   2777  C  CE  . LYS C  1 76  ? 215.977 38.380  45.270 1.00   28.09 ? 75   LYS C CE  1 
ATOM   2778  N  NZ  . LYS C  1 76  ? 217.128 37.802  46.041 1.00   28.43 ? 75   LYS C NZ  1 
ATOM   2779  N  N   . ASP C  1 77  ? 210.221 36.746  43.375 1.00   24.92 ? 76   ASP C N   1 
ATOM   2780  C  CA  . ASP C  1 77  ? 209.814 35.674  42.475 1.00   26.26 ? 76   ASP C CA  1 
ATOM   2781  C  C   . ASP C  1 77  ? 208.841 36.144  41.386 1.00   27.46 ? 76   ASP C C   1 
ATOM   2782  O  O   . ASP C  1 77  ? 208.018 37.017  41.610 1.00   27.67 ? 76   ASP C O   1 
ATOM   2783  C  CB  . ASP C  1 77  ? 209.125 34.530  43.241 1.00   26.16 ? 76   ASP C CB  1 
ATOM   2784  C  CG  . ASP C  1 77  ? 210.035 33.838  44.248 1.00   26.00 ? 76   ASP C CG  1 
ATOM   2785  O  OD1 . ASP C  1 77  ? 211.258 33.798  44.012 1.00   26.64 ? 76   ASP C OD1 1 
ATOM   2786  O  OD2 . ASP C  1 77  ? 209.516 33.329  45.271 1.00   25.05 ? 76   ASP C OD2 1 
ATOM   2787  N  N   . GLU C  1 78  ? 208.926 35.520  40.217 1.00   28.41 ? 77   GLU C N   1 
ATOM   2788  C  CA  A GLU C  1 78  ? 207.955 35.709  39.142 0.50   29.45 ? 77   GLU C CA  1 
ATOM   2789  C  CA  B GLU C  1 78  ? 207.939 35.762  39.171 0.50   29.34 ? 77   GLU C CA  1 
ATOM   2790  C  C   . GLU C  1 78  ? 206.600 35.104  39.536 1.00   28.72 ? 77   GLU C C   1 
ATOM   2791  O  O   . GLU C  1 78  ? 205.553 35.678  39.278 1.00   28.58 ? 77   GLU C O   1 
ATOM   2792  C  CB  A GLU C  1 78  ? 208.505 35.093  37.834 0.50   31.03 ? 77   GLU C CB  1 
ATOM   2793  C  CB  B GLU C  1 78  ? 208.450 35.312  37.790 0.50   30.77 ? 77   GLU C CB  1 
ATOM   2794  C  CG  A GLU C  1 78  ? 207.487 34.477  36.890 0.50   32.51 ? 77   GLU C CG  1 
ATOM   2795  C  CG  B GLU C  1 78  ? 209.674 36.085  37.296 0.50   31.92 ? 77   GLU C CG  1 
ATOM   2796  C  CD  A GLU C  1 78  ? 206.762 35.495  36.044 0.50   34.20 ? 77   GLU C CD  1 
ATOM   2797  C  CD  B GLU C  1 78  ? 209.420 37.577  37.079 0.50   33.22 ? 77   GLU C CD  1 
ATOM   2798  O  OE1 A GLU C  1 78  ? 206.901 36.713  36.295 0.50   35.57 ? 77   GLU C OE1 1 
ATOM   2799  O  OE1 B GLU C  1 78  ? 208.268 37.964  36.777 0.50   35.01 ? 77   GLU C OE1 1 
ATOM   2800  O  OE2 A GLU C  1 78  ? 206.040 35.075  35.115 0.50   36.21 ? 77   GLU C OE2 1 
ATOM   2801  O  OE2 B GLU C  1 78  ? 210.377 38.372  37.209 0.50   33.37 ? 77   GLU C OE2 1 
ATOM   2802  N  N   . GLU C  1 79  ? 206.635 33.921  40.138 1.00   27.87 ? 78   GLU C N   1 
ATOM   2803  C  CA  . GLU C  1 79  ? 205.422 33.267  40.689 1.00   27.46 ? 78   GLU C CA  1 
ATOM   2804  C  C   . GLU C  1 79  ? 205.208 33.813  42.123 1.00   25.60 ? 78   GLU C C   1 
ATOM   2805  O  O   . GLU C  1 79  ? 205.824 33.364  43.085 1.00   24.78 ? 78   GLU C O   1 
ATOM   2806  C  CB  . GLU C  1 79  ? 205.567 31.724  40.675 1.00   28.98 ? 78   GLU C CB  1 
ATOM   2807  C  CG  . GLU C  1 79  ? 204.301 30.898  40.932 1.00   30.54 ? 78   GLU C CG  1 
ATOM   2808  C  CD  . GLU C  1 79  ? 203.192 31.064  39.881 1.00   32.22 ? 78   GLU C CD  1 
ATOM   2809  O  OE1 . GLU C  1 79  ? 203.450 31.630  38.784 1.00   34.75 ? 78   GLU C OE1 1 
ATOM   2810  O  OE2 . GLU C  1 79  ? 202.038 30.624  40.151 1.00   31.95 ? 78   GLU C OE2 1 
ATOM   2811  N  N   . ARG C  1 80  ? 204.355 34.827  42.236 1.00   23.39 ? 79   ARG C N   1 
ATOM   2812  C  CA  . ARG C  1 80  ? 203.990 35.394  43.522 1.00   21.59 ? 79   ARG C CA  1 
ATOM   2813  C  C   . ARG C  1 80  ? 202.605 35.982  43.398 1.00   20.91 ? 79   ARG C C   1 
ATOM   2814  O  O   . ARG C  1 80  ? 202.097 36.198  42.290 1.00   21.33 ? 79   ARG C O   1 
ATOM   2815  C  CB  . ARG C  1 80  ? 204.960 36.498  43.914 1.00   20.56 ? 79   ARG C CB  1 
ATOM   2816  C  CG  . ARG C  1 80  ? 205.096 37.599  42.860 1.00   20.35 ? 79   ARG C CG  1 
ATOM   2817  C  CD  . ARG C  1 80  ? 205.946 38.760  43.345 1.00   19.64 ? 79   ARG C CD  1 
ATOM   2818  N  NE  . ARG C  1 80  ? 205.129 39.786  43.998 1.00   19.04 ? 79   ARG C NE  1 
ATOM   2819  C  CZ  . ARG C  1 80  ? 205.556 41.005  44.343 1.00   18.66 ? 79   ARG C CZ  1 
ATOM   2820  N  NH1 . ARG C  1 80  ? 206.812 41.380  44.148 1.00   18.44 ? 79   ARG C NH1 1 
ATOM   2821  N  NH2 . ARG C  1 80  ? 204.706 41.858  44.912 1.00   18.38 ? 79   ARG C NH2 1 
ATOM   2822  N  N   . HIS C  1 81  ? 201.999 36.246  44.540 1.00   19.91 ? 80   HIS C N   1 
ATOM   2823  C  CA  . HIS C  1 81  ? 200.846 37.108  44.583 1.00   19.32 ? 80   HIS C CA  1 
ATOM   2824  C  C   . HIS C  1 81  ? 201.309 38.545  44.466 1.00   18.60 ? 80   HIS C C   1 
ATOM   2825  O  O   . HIS C  1 81  ? 202.391 38.888  44.949 1.00   17.87 ? 80   HIS C O   1 
ATOM   2826  C  CB  . HIS C  1 81  ? 200.104 36.921  45.880 1.00   19.42 ? 80   HIS C CB  1 
ATOM   2827  C  CG  . HIS C  1 81  ? 199.688 35.496  46.172 1.00   19.89 ? 80   HIS C CG  1 
ATOM   2828  N  ND1 . HIS C  1 81  ? 199.726 34.976  47.408 1.00   19.90 ? 80   HIS C ND1 1 
ATOM   2829  C  CD2 . HIS C  1 81  ? 199.179 34.507  45.351 1.00   20.80 ? 80   HIS C CD2 1 
ATOM   2830  C  CE1 . HIS C  1 81  ? 199.247 33.713  47.374 1.00   20.36 ? 80   HIS C CE1 1 
ATOM   2831  N  NE2 . HIS C  1 81  ? 198.922 33.426  46.124 1.00   20.86 ? 80   HIS C NE2 1 
ATOM   2832  N  N   . VAL C  1 82  ? 200.500 39.404  43.830 1.00   18.28 ? 81   VAL C N   1 
ATOM   2833  C  CA  . VAL C  1 82  ? 200.796 40.834  43.784 1.00   17.84 ? 81   VAL C CA  1 
ATOM   2834  C  C   . VAL C  1 82  ? 201.036 41.355  45.199 1.00   17.31 ? 81   VAL C C   1 
ATOM   2835  O  O   . VAL C  1 82  ? 201.954 42.122  45.420 1.00   17.06 ? 81   VAL C O   1 
ATOM   2836  C  CB  . VAL C  1 82  ? 199.679 41.630  43.061 1.00   18.25 ? 81   VAL C CB  1 
ATOM   2837  C  CG1 . VAL C  1 82  ? 199.750 43.144  43.354 1.00   17.88 ? 81   VAL C CG1 1 
ATOM   2838  C  CG2 . VAL C  1 82  ? 199.742 41.336  41.569 1.00   18.73 ? 81   VAL C CG2 1 
ATOM   2839  N  N   . GLY C  1 83  ? 200.250 40.885  46.165 1.00   17.16 ? 82   GLY C N   1 
ATOM   2840  C  CA  . GLY C  1 83  ? 200.388 41.313  47.550 1.00   16.81 ? 82   GLY C CA  1 
ATOM   2841  C  C   . GLY C  1 83  ? 201.557 40.736  48.342 1.00   16.85 ? 82   GLY C C   1 
ATOM   2842  O  O   . GLY C  1 83  ? 201.713 41.044  49.520 1.00   16.77 ? 82   GLY C O   1 
ATOM   2843  N  N   . ASP C  1 84  ? 202.409 39.929  47.724 1.00   16.81 ? 83   ASP C N   1 
ATOM   2844  C  CA  . ASP C  1 84  ? 203.516 39.311  48.467 1.00   16.70 ? 83   ASP C CA  1 
ATOM   2845  C  C   . ASP C  1 84  ? 204.727 40.230  48.616 1.00   16.48 ? 83   ASP C C   1 
ATOM   2846  O  O   . ASP C  1 84  ? 205.570 40.309  47.733 1.00   16.88 ? 83   ASP C O   1 
ATOM   2847  C  CB  . ASP C  1 84  ? 203.945 38.021  47.791 1.00   16.92 ? 83   ASP C CB  1 
ATOM   2848  C  CG  . ASP C  1 84  ? 202.884 36.933  47.852 1.00   17.27 ? 83   ASP C CG  1 
ATOM   2849  O  OD1 . ASP C  1 84  ? 201.929 37.035  48.658 1.00   16.89 ? 83   ASP C OD1 1 
ATOM   2850  O  OD2 . ASP C  1 84  ? 203.025 35.930  47.098 1.00   17.57 ? 83   ASP C OD2 1 
ATOM   2851  N  N   . LEU C  1 85  ? 204.844 40.880  49.761 1.00   16.04 ? 84   LEU C N   1 
ATOM   2852  C  CA  . LEU C  1 85  ? 205.960 41.777  50.044 1.00   15.93 ? 84   LEU C CA  1 
ATOM   2853  C  C   . LEU C  1 85  ? 207.012 41.127  50.971 1.00   16.07 ? 84   LEU C C   1 
ATOM   2854  O  O   . LEU C  1 85  ? 207.866 41.817  51.540 1.00   16.15 ? 84   LEU C O   1 
ATOM   2855  C  CB  . LEU C  1 85  ? 205.424 43.069  50.661 1.00   15.51 ? 84   LEU C CB  1 
ATOM   2856  C  CG  . LEU C  1 85  ? 204.541 43.869  49.698 1.00   15.46 ? 84   LEU C CG  1 
ATOM   2857  C  CD1 . LEU C  1 85  ? 203.917 45.074  50.365 1.00   15.13 ? 84   LEU C CD1 1 
ATOM   2858  C  CD2 . LEU C  1 85  ? 205.362 44.287  48.482 1.00   15.65 ? 84   LEU C CD2 1 
ATOM   2859  N  N   . GLY C  1 86  ? 206.953 39.810  51.121 1.00   16.11 ? 85   GLY C N   1 
ATOM   2860  C  CA  . GLY C  1 86  ? 207.950 39.090  51.937 1.00   16.38 ? 85   GLY C CA  1 
ATOM   2861  C  C   . GLY C  1 86  ? 207.856 39.253  53.449 1.00   16.32 ? 85   GLY C C   1 
ATOM   2862  O  O   . GLY C  1 86  ? 206.765 39.154  54.045 1.00   16.43 ? 85   GLY C O   1 
ATOM   2863  N  N   . ASN C  1 87  ? 209.008 39.499  54.066 1.00   16.34 ? 86   ASN C N   1 
ATOM   2864  C  CA  . ASN C  1 87  ? 209.139 39.638  55.492 1.00   16.41 ? 86   ASN C CA  1 
ATOM   2865  C  C   . ASN C  1 87  ? 209.604 41.023  55.859 1.00   16.66 ? 86   ASN C C   1 
ATOM   2866  O  O   . ASN C  1 87  ? 210.271 41.684  55.045 1.00   16.92 ? 86   ASN C O   1 
ATOM   2867  C  CB  . ASN C  1 87  ? 210.175 38.640  56.023 1.00   16.40 ? 86   ASN C CB  1 
ATOM   2868  C  CG  . ASN C  1 87  ? 209.654 37.231  56.014 1.00   16.39 ? 86   ASN C CG  1 
ATOM   2869  O  OD1 . ASN C  1 87  ? 208.596 36.932  56.617 1.00   16.31 ? 86   ASN C OD1 1 
ATOM   2870  N  ND2 . ASN C  1 87  ? 210.361 36.352  55.321 1.00   16.26 ? 86   ASN C ND2 1 
ATOM   2871  N  N   . VAL C  1 88  ? 209.239 41.436  57.075 1.00   16.69 ? 87   VAL C N   1 
ATOM   2872  C  CA  . VAL C  1 88  ? 209.876 42.554  57.779 1.00   17.18 ? 87   VAL C CA  1 
ATOM   2873  C  C   . VAL C  1 88  ? 210.588 42.012  59.028 1.00   17.95 ? 87   VAL C C   1 
ATOM   2874  O  O   . VAL C  1 88  ? 210.232 40.957  59.550 1.00   18.23 ? 87   VAL C O   1 
ATOM   2875  C  CB  . VAL C  1 88  ? 208.868 43.673  58.152 1.00   16.92 ? 87   VAL C CB  1 
ATOM   2876  C  CG1 . VAL C  1 88  ? 208.336 44.343  56.875 1.00   16.41 ? 87   VAL C CG1 1 
ATOM   2877  C  CG2 . VAL C  1 88  ? 207.738 43.156  59.039 1.00   16.68 ? 87   VAL C CG2 1 
ATOM   2878  N  N   . THR C  1 89  ? 211.612 42.712  59.497 1.00   19.01 ? 88   THR C N   1 
ATOM   2879  C  CA  . THR C  1 89  ? 212.458 42.208  60.592 1.00   19.81 ? 88   THR C CA  1 
ATOM   2880  C  C   . THR C  1 89  ? 212.352 43.138  61.795 1.00   20.57 ? 88   THR C C   1 
ATOM   2881  O  O   . THR C  1 89  ? 212.661 44.325  61.689 1.00   20.59 ? 88   THR C O   1 
ATOM   2882  C  CB  . THR C  1 89  ? 213.934 42.119  60.174 1.00   20.31 ? 88   THR C CB  1 
ATOM   2883  O  OG1 . THR C  1 89  ? 214.066 41.236  59.049 1.00   20.49 ? 88   THR C OG1 1 
ATOM   2884  C  CG2 . THR C  1 89  ? 214.835 41.622  61.347 1.00   20.64 ? 88   THR C CG2 1 
ATOM   2885  N  N   . ALA C  1 90  ? 211.895 42.597  62.926 1.00   21.23 ? 89   ALA C N   1 
ATOM   2886  C  CA  . ALA C  1 90  ? 211.822 43.361  64.166 1.00   22.63 ? 89   ALA C CA  1 
ATOM   2887  C  C   . ALA C  1 90  ? 213.122 43.157  64.949 1.00   24.40 ? 89   ALA C C   1 
ATOM   2888  O  O   . ALA C  1 90  ? 213.570 42.028  65.118 1.00   24.37 ? 89   ALA C O   1 
ATOM   2889  C  CB  . ALA C  1 90  ? 210.647 42.902  65.004 1.00   22.17 ? 89   ALA C CB  1 
ATOM   2890  N  N   . ASP C  1 91  ? 213.688 44.255  65.434 1.00   26.56 ? 90   ASP C N   1 
ATOM   2891  C  CA  . ASP C  1 91  ? 214.921 44.239  66.210 1.00   28.56 ? 90   ASP C CA  1 
ATOM   2892  C  C   . ASP C  1 91  ? 214.664 43.792  67.648 1.00   30.21 ? 90   ASP C C   1 
ATOM   2893  O  O   . ASP C  1 91  ? 213.538 43.456  68.020 1.00   29.73 ? 90   ASP C O   1 
ATOM   2894  C  CB  . ASP C  1 91  ? 215.622 45.617  66.160 1.00   29.05 ? 90   ASP C CB  1 
ATOM   2895  C  CG  . ASP C  1 91  ? 214.813 46.737  66.812 1.00   29.31 ? 90   ASP C CG  1 
ATOM   2896  O  OD1 . ASP C  1 91  ? 213.920 46.489  67.653 1.00   29.09 ? 90   ASP C OD1 1 
ATOM   2897  O  OD2 . ASP C  1 91  ? 215.079 47.904  66.466 1.00   30.92 ? 90   ASP C OD2 1 
ATOM   2898  N  N   . LYS C  1 92  ? 215.727 43.794  68.447 1.00   32.88 ? 91   LYS C N   1 
ATOM   2899  C  CA  . LYS C  1 92  ? 215.673 43.318  69.832 1.00   34.76 ? 91   LYS C CA  1 
ATOM   2900  C  C   . LYS C  1 92  ? 214.745 44.152  70.699 1.00   34.08 ? 91   LYS C C   1 
ATOM   2901  O  O   . LYS C  1 92  ? 214.270 43.677  71.715 1.00   35.24 ? 91   LYS C O   1 
ATOM   2902  C  CB  . LYS C  1 92  ? 217.090 43.291  70.444 1.00   37.18 ? 91   LYS C CB  1 
ATOM   2903  C  CG  . LYS C  1 92  ? 217.734 44.658  70.679 1.00   39.62 ? 91   LYS C CG  1 
ATOM   2904  C  CD  . LYS C  1 92  ? 219.093 44.536  71.392 1.00   42.32 ? 91   LYS C CD  1 
ATOM   2905  C  CE  . LYS C  1 92  ? 219.875 45.845  71.296 1.00   44.00 ? 91   LYS C CE  1 
ATOM   2906  N  NZ  . LYS C  1 92  ? 221.310 45.698  71.689 1.00   46.17 ? 91   LYS C NZ  1 
ATOM   2907  N  N   . ASP C  1 93  ? 214.501 45.397  70.298 1.00   33.00 ? 92   ASP C N   1 
ATOM   2908  C  CA  . ASP C  1 93  ? 213.573 46.282  71.007 1.00   33.40 ? 92   ASP C CA  1 
ATOM   2909  C  C   . ASP C  1 93  ? 212.096 46.188  70.576 1.00   31.11 ? 92   ASP C C   1 
ATOM   2910  O  O   . ASP C  1 93  ? 211.267 46.920  71.101 1.00   32.03 ? 92   ASP C O   1 
ATOM   2911  C  CB  . ASP C  1 93  ? 214.081 47.718  70.888 1.00   34.97 ? 92   ASP C CB  1 
ATOM   2912  C  CG  . ASP C  1 93  ? 215.409 47.909  71.613 1.00   38.77 ? 92   ASP C CG  1 
ATOM   2913  O  OD1 . ASP C  1 93  ? 215.582 47.283  72.689 1.00   40.71 ? 92   ASP C OD1 1 
ATOM   2914  O  OD2 . ASP C  1 93  ? 216.276 48.665  71.123 1.00   40.93 ? 92   ASP C OD2 1 
ATOM   2915  N  N   . GLY C  1 94  ? 211.766 45.300  69.639 1.00   28.89 ? 93   GLY C N   1 
ATOM   2916  C  CA  . GLY C  1 94  ? 210.366 45.099  69.198 1.00   27.28 ? 93   GLY C CA  1 
ATOM   2917  C  C   . GLY C  1 94  ? 209.906 45.915  67.985 1.00   25.96 ? 93   GLY C C   1 
ATOM   2918  O  O   . GLY C  1 94  ? 208.707 45.963  67.678 1.00   25.43 ? 93   GLY C O   1 
ATOM   2919  N  N   . VAL C  1 95  ? 210.853 46.523  67.275 1.00   25.05 ? 94   VAL C N   1 
ATOM   2920  C  CA  . VAL C  1 95  ? 210.549 47.497  66.258 1.00   24.22 ? 94   VAL C CA  1 
ATOM   2921  C  C   . VAL C  1 95  ? 211.097 47.049  64.917 1.00   23.66 ? 94   VAL C C   1 
ATOM   2922  O  O   . VAL C  1 95  ? 212.293 46.745  64.793 1.00   24.26 ? 94   VAL C O   1 
ATOM   2923  C  CB  . VAL C  1 95  ? 211.163 48.879  66.602 1.00   24.68 ? 94   VAL C CB  1 
ATOM   2924  C  CG1 . VAL C  1 95  ? 210.964 49.837  65.438 1.00   23.66 ? 94   VAL C CG1 1 
ATOM   2925  C  CG2 . VAL C  1 95  ? 210.564 49.442  67.893 1.00   24.56 ? 94   VAL C CG2 1 
ATOM   2926  N  N   . ALA C  1 96  ? 210.222 47.012  63.913 1.00   22.73 ? 95   ALA C N   1 
ATOM   2927  C  CA  . ALA C  1 96  ? 210.620 46.751  62.548 1.00   22.33 ? 95   ALA C CA  1 
ATOM   2928  C  C   . ALA C  1 96  ? 210.583 48.070  61.808 1.00   22.47 ? 95   ALA C C   1 
ATOM   2929  O  O   . ALA C  1 96  ? 209.513 48.687  61.676 1.00   21.75 ? 95   ALA C O   1 
ATOM   2930  C  CB  . ALA C  1 96  ? 209.702 45.736  61.899 1.00   21.54 ? 95   ALA C CB  1 
ATOM   2931  N  N   . ASP C  1 97  ? 211.752 48.516  61.352 1.00   23.07 ? 96   ASP C N   1 
ATOM   2932  C  CA  . ASP C  1 97  ? 211.847 49.726  60.549 1.00   23.53 ? 96   ASP C CA  1 
ATOM   2933  C  C   . ASP C  1 97  ? 211.754 49.309  59.091 1.00   22.91 ? 96   ASP C C   1 
ATOM   2934  O  O   . ASP C  1 97  ? 212.742 48.974  58.471 1.00   23.32 ? 96   ASP C O   1 
ATOM   2935  C  CB  . ASP C  1 97  ? 213.149 50.465  60.827 1.00   24.87 ? 96   ASP C CB  1 
ATOM   2936  C  CG  . ASP C  1 97  ? 213.150 51.138  62.187 1.00   26.26 ? 96   ASP C CG  1 
ATOM   2937  O  OD1 . ASP C  1 97  ? 212.217 51.923  62.492 1.00   27.25 ? 96   ASP C OD1 1 
ATOM   2938  O  OD2 . ASP C  1 97  ? 214.083 50.878  62.950 1.00   27.96 ? 96   ASP C OD2 1 
ATOM   2939  N  N   . VAL C  1 98  ? 210.559 49.373  58.542 1.00   21.81 ? 97   VAL C N   1 
ATOM   2940  C  CA  . VAL C  1 98  ? 210.297 48.825  57.230 1.00   21.16 ? 97   VAL C CA  1 
ATOM   2941  C  C   . VAL C  1 98  ? 210.914 49.737  56.163 1.00   21.76 ? 97   VAL C C   1 
ATOM   2942  O  O   . VAL C  1 98  ? 210.835 50.960  56.247 1.00   21.59 ? 97   VAL C O   1 
ATOM   2943  C  CB  . VAL C  1 98  ? 208.770 48.656  57.018 1.00   20.09 ? 97   VAL C CB  1 
ATOM   2944  C  CG1 . VAL C  1 98  ? 208.474 48.010  55.671 1.00   19.11 ? 97   VAL C CG1 1 
ATOM   2945  C  CG2 . VAL C  1 98  ? 208.177 47.833  58.172 1.00   19.49 ? 97   VAL C CG2 1 
ATOM   2946  N  N   . SER C  1 99  ? 211.561 49.119  55.189 1.00   22.26 ? 98   SER C N   1 
ATOM   2947  C  CA  . SER C  1 99  ? 212.059 49.818  54.031 1.00   23.55 ? 98   SER C CA  1 
ATOM   2948  C  C   . SER C  1 99  ? 212.100 48.866  52.880 1.00   23.36 ? 98   SER C C   1 
ATOM   2949  O  O   . SER C  1 99  ? 213.024 48.077  52.779 1.00   24.83 ? 98   SER C O   1 
ATOM   2950  C  CB  . SER C  1 99  ? 213.468 50.364  54.263 1.00   24.70 ? 98   SER C CB  1 
ATOM   2951  O  OG  . SER C  1 99  ? 213.702 51.343  53.275 1.00   25.94 ? 98   SER C OG  1 
ATOM   2952  N  N   . ILE C  1 100 ? 211.103 48.948  52.013 1.00   22.98 ? 99   ILE C N   1 
ATOM   2953  C  CA  . ILE C  1 100 ? 210.885 47.988  50.948 1.00   23.50 ? 99   ILE C CA  1 
ATOM   2954  C  C   . ILE C  1 100 ? 210.661 48.809  49.678 1.00   23.59 ? 99   ILE C C   1 
ATOM   2955  O  O   . ILE C  1 100 ? 210.158 49.931  49.737 1.00   23.69 ? 99   ILE C O   1 
ATOM   2956  C  CB  . ILE C  1 100 ? 209.645 47.102  51.248 1.00   23.76 ? 99   ILE C CB  1 
ATOM   2957  C  CG1 . ILE C  1 100 ? 209.999 45.974  52.212 1.00   24.66 ? 99   ILE C CG1 1 
ATOM   2958  C  CG2 . ILE C  1 100 ? 209.069 46.464  49.995 1.00   23.95 ? 99   ILE C CG2 1 
ATOM   2959  C  CD1 . ILE C  1 100 ? 208.778 45.158  52.650 1.00   24.22 ? 99   ILE C CD1 1 
ATOM   2960  N  N   . GLU C  1 101 ? 211.084 48.281  48.545 1.00   23.62 ? 100  GLU C N   1 
ATOM   2961  C  CA  . GLU C  1 101 ? 210.690 48.845  47.258 1.00   24.05 ? 100  GLU C CA  1 
ATOM   2962  C  C   . GLU C  1 101 ? 210.144 47.699  46.433 1.00   22.43 ? 100  GLU C C   1 
ATOM   2963  O  O   . GLU C  1 101 ? 210.724 46.629  46.435 1.00   22.29 ? 100  GLU C O   1 
ATOM   2964  C  CB  . GLU C  1 101 ? 211.889 49.488  46.538 1.00   26.05 ? 100  GLU C CB  1 
ATOM   2965  C  CG  . GLU C  1 101 ? 211.484 50.135  45.215 1.00   28.01 ? 100  GLU C CG  1 
ATOM   2966  C  CD  . GLU C  1 101 ? 212.644 50.759  44.452 1.00   30.92 ? 100  GLU C CD  1 
ATOM   2967  O  OE1 . GLU C  1 101 ? 213.159 51.802  44.918 1.00   31.59 ? 100  GLU C OE1 1 
ATOM   2968  O  OE2 . GLU C  1 101 ? 213.039 50.175  43.392 1.00   33.97 ? 100  GLU C OE2 1 
ATOM   2969  N  N   . ASP C  1 102 ? 209.052 47.919  45.718 1.00   21.18 ? 101  ASP C N   1 
ATOM   2970  C  CA  . ASP C  1 102 ? 208.415 46.844  44.958 1.00   20.28 ? 101  ASP C CA  1 
ATOM   2971  C  C   . ASP C  1 102 ? 207.854 47.360  43.655 1.00   20.29 ? 101  ASP C C   1 
ATOM   2972  O  O   . ASP C  1 102 ? 207.225 48.421  43.625 1.00   20.01 ? 101  ASP C O   1 
ATOM   2973  C  CB  . ASP C  1 102 ? 207.287 46.203  45.769 1.00   19.66 ? 101  ASP C CB  1 
ATOM   2974  C  CG  . ASP C  1 102 ? 206.868 44.852  45.216 1.00   19.64 ? 101  ASP C CG  1 
ATOM   2975  O  OD1 . ASP C  1 102 ? 207.572 43.871  45.481 1.00   19.44 ? 101  ASP C OD1 1 
ATOM   2976  O  OD2 . ASP C  1 102 ? 205.839 44.758  44.499 1.00   19.60 ? 101  ASP C OD2 1 
ATOM   2977  N  N   . SER C  1 103 ? 208.043 46.576  42.589 1.00   20.14 ? 102  SER C N   1 
ATOM   2978  C  CA  . SER C  1 103 ? 207.627 46.971  41.256 1.00   20.26 ? 102  SER C CA  1 
ATOM   2979  C  C   . SER C  1 103 ? 206.385 46.224  40.746 1.00   19.83 ? 102  SER C C   1 
ATOM   2980  O  O   . SER C  1 103 ? 205.957 46.446  39.627 1.00   20.50 ? 102  SER C O   1 
ATOM   2981  C  CB  . SER C  1 103 ? 208.805 46.821  40.275 1.00   20.77 ? 102  SER C CB  1 
ATOM   2982  O  OG  . SER C  1 103 ? 209.648 47.960  40.356 0.50   20.89 ? 102  SER C OG  1 
ATOM   2983  N  N   . VAL C  1 104 ? 205.792 45.375  41.568 1.00   18.94 ? 103  VAL C N   1 
ATOM   2984  C  CA  . VAL C  1 104 ? 204.608 44.625  41.178 1.00   18.52 ? 103  VAL C CA  1 
ATOM   2985  C  C   . VAL C  1 104 ? 203.334 45.278  41.745 1.00   18.14 ? 103  VAL C C   1 
ATOM   2986  O  O   . VAL C  1 104 ? 202.328 45.398  41.047 1.00   18.08 ? 103  VAL C O   1 
ATOM   2987  C  CB  . VAL C  1 104 ? 204.759 43.151  41.607 1.00   18.36 ? 103  VAL C CB  1 
ATOM   2988  C  CG1 . VAL C  1 104 ? 203.497 42.343  41.301 1.00   18.00 ? 103  VAL C CG1 1 
ATOM   2989  C  CG2 . VAL C  1 104 ? 205.997 42.545  40.925 1.00   18.32 ? 103  VAL C CG2 1 
ATOM   2990  N  N   . ILE C  1 105 ? 203.362 45.694  43.009 1.00   17.44 ? 104  ILE C N   1 
ATOM   2991  C  CA  . ILE C  1 105 ? 202.264 46.481  43.557 1.00   16.92 ? 104  ILE C CA  1 
ATOM   2992  C  C   . ILE C  1 105 ? 202.268 47.843  42.877 1.00   17.16 ? 104  ILE C C   1 
ATOM   2993  O  O   . ILE C  1 105 ? 203.297 48.306  42.369 1.00   17.48 ? 104  ILE C O   1 
ATOM   2994  C  CB  . ILE C  1 105 ? 202.343 46.678  45.113 1.00   16.41 ? 104  ILE C CB  1 
ATOM   2995  C  CG1 . ILE C  1 105 ? 203.667 47.316  45.539 1.00   16.38 ? 104  ILE C CG1 1 
ATOM   2996  C  CG2 . ILE C  1 105 ? 202.129 45.369  45.852 1.00   15.96 ? 104  ILE C CG2 1 
ATOM   2997  C  CD1 . ILE C  1 105 ? 203.681 47.882  46.945 1.00   16.11 ? 104  ILE C CD1 1 
ATOM   2998  N  N   . SER C  1 106 ? 201.123 48.504  42.928 1.00   17.15 ? 105  SER C N   1 
ATOM   2999  C  CA  . SER C  1 106 ? 200.973 49.872  42.460 1.00   17.40 ? 105  SER C CA  1 
ATOM   3000  C  C   . SER C  1 106 ? 199.993 50.642  43.332 1.00   17.26 ? 105  SER C C   1 
ATOM   3001  O  O   . SER C  1 106 ? 199.193 50.041  44.061 1.00   16.89 ? 105  SER C O   1 
ATOM   3002  C  CB  . SER C  1 106 ? 200.428 49.876  41.027 1.00   17.66 ? 105  SER C CB  1 
ATOM   3003  O  OG  . SER C  1 106 ? 200.653 51.146  40.429 1.00   17.70 ? 105  SER C OG  1 
ATOM   3004  N  N   . LEU C  1 107 ? 200.029 51.972  43.212 1.00   17.64 ? 106  LEU C N   1 
ATOM   3005  C  CA  . LEU C  1 107 ? 199.014 52.827  43.825 1.00   17.54 ? 106  LEU C CA  1 
ATOM   3006  C  C   . LEU C  1 107 ? 197.980 53.316  42.797 1.00   18.40 ? 106  LEU C C   1 
ATOM   3007  O  O   . LEU C  1 107 ? 197.174 54.187  43.103 1.00   18.34 ? 106  LEU C O   1 
ATOM   3008  C  CB  . LEU C  1 107 ? 199.656 54.005  44.540 1.00   17.34 ? 106  LEU C CB  1 
ATOM   3009  C  CG  . LEU C  1 107 ? 200.761 53.688  45.551 1.00   17.02 ? 106  LEU C CG  1 
ATOM   3010  C  CD1 . LEU C  1 107 ? 201.304 54.967  46.181 1.00   16.98 ? 106  LEU C CD1 1 
ATOM   3011  C  CD2 . LEU C  1 107 ? 200.255 52.722  46.624 1.00   16.59 ? 106  LEU C CD2 1 
ATOM   3012  N  N   . SER C  1 108 ? 197.999 52.754  41.588 1.00   19.00 ? 107  SER C N   1 
ATOM   3013  C  CA  . SER C  1 108 ? 196.950 53.023  40.598 1.00   19.73 ? 107  SER C CA  1 
ATOM   3014  C  C   . SER C  1 108 ? 196.856 51.815  39.683 1.00   20.44 ? 107  SER C C   1 
ATOM   3015  O  O   . SER C  1 108 ? 197.718 50.944  39.748 1.00   19.62 ? 107  SER C O   1 
ATOM   3016  C  CB  . SER C  1 108 ? 197.226 54.324  39.814 1.00   20.05 ? 107  SER C CB  1 
ATOM   3017  O  OG  . SER C  1 108 ? 198.498 54.315  39.163 1.00   20.34 ? 107  SER C OG  1 
ATOM   3018  N  N   . GLY C  1 109 ? 195.794 51.746  38.874 1.00   21.84 ? 108  GLY C N   1 
ATOM   3019  C  CA  . GLY C  1 109 ? 195.618 50.659  37.897 1.00   23.60 ? 108  GLY C CA  1 
ATOM   3020  C  C   . GLY C  1 109 ? 195.208 49.301  38.450 1.00   24.67 ? 108  GLY C C   1 
ATOM   3021  O  O   . GLY C  1 109 ? 194.725 49.209  39.561 1.00   25.23 ? 108  GLY C O   1 
ATOM   3022  N  N   . ASP C  1 110 ? 195.445 48.236  37.681 1.00   26.53 ? 109  ASP C N   1 
ATOM   3023  C  CA  A ASP C  1 110 ? 194.975 46.895  38.057 0.50   26.45 ? 109  ASP C CA  1 
ATOM   3024  C  CA  B ASP C  1 110 ? 195.023 46.862  38.027 0.50   27.20 ? 109  ASP C CA  1 
ATOM   3025  C  C   . ASP C  1 110 ? 195.657 46.339  39.321 1.00   26.17 ? 109  ASP C C   1 
ATOM   3026  O  O   . ASP C  1 110 ? 195.042 45.594  40.076 1.00   26.97 ? 109  ASP C O   1 
ATOM   3027  C  CB  A ASP C  1 110 ? 195.168 45.902  36.901 0.50   27.36 ? 109  ASP C CB  1 
ATOM   3028  C  CB  B ASP C  1 110 ? 195.402 45.918  36.871 0.50   29.15 ? 109  ASP C CB  1 
ATOM   3029  C  CG  A ASP C  1 110 ? 194.233 46.160  35.708 0.50   27.79 ? 109  ASP C CG  1 
ATOM   3030  C  CG  B ASP C  1 110 ? 194.504 44.683  36.773 0.50   30.47 ? 109  ASP C CG  1 
ATOM   3031  O  OD1 A ASP C  1 110 ? 193.041 46.473  35.903 0.50   27.17 ? 109  ASP C OD1 1 
ATOM   3032  O  OD1 B ASP C  1 110 ? 194.484 43.852  37.721 0.50   31.42 ? 109  ASP C OD1 1 
ATOM   3033  O  OD2 A ASP C  1 110 ? 194.712 46.010  34.561 0.50   28.38 ? 109  ASP C OD2 1 
ATOM   3034  O  OD2 B ASP C  1 110 ? 193.846 44.535  35.706 0.50   31.32 ? 109  ASP C OD2 1 
ATOM   3035  N  N   . HIS C  1 111 ? 196.918 46.687  39.561 1.00   24.82 ? 110  HIS C N   1 
ATOM   3036  C  CA  . HIS C  1 111 ? 197.610 46.196  40.755 1.00   23.57 ? 110  HIS C CA  1 
ATOM   3037  C  C   . HIS C  1 111 ? 197.511 47.157  41.918 1.00   22.17 ? 110  HIS C C   1 
ATOM   3038  O  O   . HIS C  1 111 ? 198.297 47.066  42.878 1.00   21.02 ? 110  HIS C O   1 
ATOM   3039  C  CB  . HIS C  1 111 ? 199.074 45.902  40.420 1.00   23.80 ? 110  HIS C CB  1 
ATOM   3040  C  CG  . HIS C  1 111 ? 199.250 44.731  39.487 1.00   24.46 ? 110  HIS C CG  1 
ATOM   3041  N  ND1 . HIS C  1 111 ? 200.449 44.169  39.242 1.00   24.70 ? 110  HIS C ND1 1 
ATOM   3042  C  CD2 . HIS C  1 111 ? 198.320 44.009  38.760 1.00   24.91 ? 110  HIS C CD2 1 
ATOM   3043  C  CE1 . HIS C  1 111 ? 200.282 43.159  38.382 1.00   25.56 ? 110  HIS C CE1 1 
ATOM   3044  N  NE2 . HIS C  1 111 ? 198.978 43.067  38.091 1.00   25.07 ? 110  HIS C NE2 1 
ATOM   3045  N  N   . CYS C  1 112 ? 196.586 48.118  41.822 1.00   21.44 ? 111  CYS C N   1 
ATOM   3046  C  CA  . CYS C  1 112 ? 196.390 49.118  42.885 1.00   20.41 ? 111  CYS C CA  1 
ATOM   3047  C  C   . CYS C  1 112 ? 196.093 48.438  44.218 1.00   18.39 ? 111  CYS C C   1 
ATOM   3048  O  O   . CYS C  1 112 ? 195.211 47.597  44.293 1.00   17.81 ? 111  CYS C O   1 
ATOM   3049  C  CB  . CYS C  1 112 ? 195.233 50.063  42.540 1.00   21.73 ? 111  CYS C CB  1 
ATOM   3050  S  SG  . CYS C  1 112 ? 195.116 51.457  43.656 1.00   24.99 ? 111  CYS C SG  1 
ATOM   3051  N  N   . ILE C  1 113 ? 196.815 48.835  45.261 1.00   16.76 ? 112  ILE C N   1 
ATOM   3052  C  CA  . ILE C  1 113 ? 196.560 48.337  46.594 1.00   15.95 ? 112  ILE C CA  1 
ATOM   3053  C  C   . ILE C  1 113 ? 195.774 49.278  47.502 1.00   15.34 ? 112  ILE C C   1 
ATOM   3054  O  O   . ILE C  1 113 ? 195.502 48.944  48.653 1.00   14.73 ? 112  ILE C O   1 
ATOM   3055  C  CB  . ILE C  1 113 ? 197.870 47.901  47.272 1.00   15.76 ? 112  ILE C CB  1 
ATOM   3056  C  CG1 . ILE C  1 113 ? 198.848 49.077  47.410 1.00   15.64 ? 112  ILE C CG1 1 
ATOM   3057  C  CG2 . ILE C  1 113 ? 198.468 46.729  46.483 1.00   15.96 ? 112  ILE C CG2 1 
ATOM   3058  C  CD1 . ILE C  1 113 ? 200.076 48.813  48.283 1.00   15.59 ? 112  ILE C CD1 1 
ATOM   3059  N  N   . ILE C  1 114 ? 195.427 50.472  47.003 1.00   15.13 ? 113  ILE C N   1 
ATOM   3060  C  CA  A ILE C  1 114 ? 194.594 51.438  47.729 0.50   14.88 ? 113  ILE C CA  1 
ATOM   3061  C  CA  B ILE C  1 114 ? 194.669 51.380  47.836 0.50   14.75 ? 113  ILE C CA  1 
ATOM   3062  C  C   . ILE C  1 114 ? 193.276 50.772  48.068 1.00   14.64 ? 113  ILE C C   1 
ATOM   3063  O  O   . ILE C  1 114 ? 192.659 50.198  47.190 1.00   14.75 ? 113  ILE C O   1 
ATOM   3064  C  CB  A ILE C  1 114 ? 194.266 52.678  46.854 0.50   15.20 ? 113  ILE C CB  1 
ATOM   3065  C  CB  B ILE C  1 114 ? 194.644 52.818  47.281 0.50   14.90 ? 113  ILE C CB  1 
ATOM   3066  C  CG1 A ILE C  1 114 ? 195.531 53.506  46.609 0.50   15.38 ? 113  ILE C CG1 1 
ATOM   3067  C  CG1 B ILE C  1 114 ? 196.078 53.377  47.203 0.50   14.91 ? 113  ILE C CG1 1 
ATOM   3068  C  CG2 A ILE C  1 114 ? 193.172 53.526  47.502 0.50   15.12 ? 113  ILE C CG2 1 
ATOM   3069  C  CG2 B ILE C  1 114 ? 193.800 53.712  48.182 0.50   14.79 ? 113  ILE C CG2 1 
ATOM   3070  C  CD1 A ILE C  1 114 ? 196.410 53.621  47.836 0.50   15.17 ? 113  ILE C CD1 1 
ATOM   3071  C  CD1 B ILE C  1 114 ? 196.196 54.725  46.506 0.50   15.05 ? 113  ILE C CD1 1 
ATOM   3072  N  N   . GLY C  1 115 ? 192.823 50.851  49.318 1.00   14.33 ? 114  GLY C N   1 
ATOM   3073  C  CA  . GLY C  1 115 ? 191.570 50.252  49.715 1.00   14.13 ? 114  GLY C CA  1 
ATOM   3074  C  C   . GLY C  1 115 ? 191.642 48.757  50.006 1.00   13.98 ? 114  GLY C C   1 
ATOM   3075  O  O   . GLY C  1 115 ? 190.631 48.147  50.294 1.00   13.88 ? 114  GLY C O   1 
ATOM   3076  N  N   . ARG C  1 116 ? 192.830 48.176  49.929 1.00   13.83 ? 115  ARG C N   1 
ATOM   3077  C  CA  . ARG C  1 116 ? 193.060 46.798  50.371 1.00   13.90 ? 115  ARG C CA  1 
ATOM   3078  C  C   . ARG C  1 116 ? 193.686 46.825  51.780 1.00   13.61 ? 115  ARG C C   1 
ATOM   3079  O  O   . ARG C  1 116 ? 193.801 47.902  52.371 1.00   13.62 ? 115  ARG C O   1 
ATOM   3080  C  CB  . ARG C  1 116 ? 193.914 46.073  49.322 1.00   14.12 ? 115  ARG C CB  1 
ATOM   3081  C  CG  . ARG C  1 116 ? 193.214 46.137  47.971 1.00   14.59 ? 115  ARG C CG  1 
ATOM   3082  C  CD  . ARG C  1 116 ? 193.761 45.184  46.939 1.00   15.03 ? 115  ARG C CD  1 
ATOM   3083  N  NE  . ARG C  1 116 ? 193.162 45.423  45.623 1.00   15.48 ? 115  ARG C NE  1 
ATOM   3084  C  CZ  . ARG C  1 116 ? 192.036 44.869  45.173 1.00   16.03 ? 115  ARG C CZ  1 
ATOM   3085  N  NH1 . ARG C  1 116 ? 191.334 44.015  45.920 1.00   16.35 ? 115  ARG C NH1 1 
ATOM   3086  N  NH2 . ARG C  1 116 ? 191.618 45.144  43.953 1.00   16.31 ? 115  ARG C NH2 1 
ATOM   3087  N  N   . THR C  1 117 ? 194.058 45.675  52.332 1.00   13.50 ? 116  THR C N   1 
ATOM   3088  C  CA  . THR C  1 117 ? 194.547 45.609  53.712 1.00   13.32 ? 116  THR C CA  1 
ATOM   3089  C  C   . THR C  1 117 ? 195.991 45.149  53.791 1.00   13.34 ? 116  THR C C   1 
ATOM   3090  O  O   . THR C  1 117 ? 196.358 44.112  53.255 1.00   13.73 ? 116  THR C O   1 
ATOM   3091  C  CB  . THR C  1 117 ? 193.680 44.679  54.574 1.00   13.35 ? 116  THR C CB  1 
ATOM   3092  O  OG1 . THR C  1 117 ? 192.358 45.190  54.686 1.00   13.24 ? 116  THR C OG1 1 
ATOM   3093  C  CG2 . THR C  1 117 ? 194.234 44.497  55.979 1.00   13.25 ? 116  THR C CG2 1 
ATOM   3094  N  N   . LEU C  1 118 ? 196.808 45.927  54.472 1.00   13.31 ? 117  LEU C N   1 
ATOM   3095  C  CA  . LEU C  1 118 ? 198.158 45.541  54.811 1.00   13.32 ? 117  LEU C CA  1 
ATOM   3096  C  C   . LEU C  1 118 ? 198.147 44.800  56.149 1.00   13.50 ? 117  LEU C C   1 
ATOM   3097  O  O   . LEU C  1 118 ? 197.541 45.261  57.096 1.00   13.46 ? 117  LEU C O   1 
ATOM   3098  C  CB  . LEU C  1 118 ? 199.024 46.765  54.946 1.00   13.24 ? 117  LEU C CB  1 
ATOM   3099  C  CG  . LEU C  1 118 ? 200.505 46.512  55.173 1.00   13.31 ? 117  LEU C CG  1 
ATOM   3100  C  CD1 . LEU C  1 118 ? 201.081 45.879  53.910 1.00   13.23 ? 117  LEU C CD1 1 
ATOM   3101  C  CD2 . LEU C  1 118 ? 201.200 47.816  55.594 1.00   13.28 ? 117  LEU C CD2 1 
ATOM   3102  N  N   . VAL C  1 119 ? 198.811 43.653  56.191 1.00   13.65 ? 118  VAL C N   1 
ATOM   3103  C  CA  . VAL C  1 119 ? 198.801 42.755  57.356 1.00   13.95 ? 118  VAL C CA  1 
ATOM   3104  C  C   . VAL C  1 119 ? 200.248 42.446  57.728 1.00   14.27 ? 118  VAL C C   1 
ATOM   3105  O  O   . VAL C  1 119 ? 201.097 42.182  56.844 1.00   14.28 ? 118  VAL C O   1 
ATOM   3106  C  CB  . VAL C  1 119 ? 198.064 41.424  57.048 1.00   13.94 ? 118  VAL C CB  1 
ATOM   3107  C  CG1 . VAL C  1 119 ? 198.238 40.412  58.172 1.00   14.08 ? 118  VAL C CG1 1 
ATOM   3108  C  CG2 . VAL C  1 119 ? 196.588 41.663  56.792 1.00   13.92 ? 118  VAL C CG2 1 
ATOM   3109  N  N   . VAL C  1 120 ? 200.537 42.498  59.021 1.00   14.73 ? 119  VAL C N   1 
ATOM   3110  C  CA  . VAL C  1 120 ? 201.809 42.026  59.553 1.00   15.16 ? 119  VAL C CA  1 
ATOM   3111  C  C   . VAL C  1 120 ? 201.521 40.791  60.392 1.00   15.99 ? 119  VAL C C   1 
ATOM   3112  O  O   . VAL C  1 120 ? 200.583 40.780  61.231 1.00   15.89 ? 119  VAL C O   1 
ATOM   3113  C  CB  . VAL C  1 120 ? 202.555 43.113  60.341 1.00   15.27 ? 119  VAL C CB  1 
ATOM   3114  C  CG1 . VAL C  1 120 ? 201.763 43.531  61.583 1.00   15.47 ? 119  VAL C CG1 1 
ATOM   3115  C  CG2 . VAL C  1 120 ? 203.986 42.670  60.692 1.00   15.35 ? 119  VAL C CG2 1 
ATOM   3116  N  N   . HIS C  1 121 ? 202.307 39.742  60.125 1.00   16.55 ? 120  HIS C N   1 
ATOM   3117  C  CA  . HIS C  1 121 ? 202.041 38.409  60.642 1.00   17.53 ? 120  HIS C CA  1 
ATOM   3118  C  C   . HIS C  1 121 ? 202.883 37.967  61.807 1.00   18.41 ? 120  HIS C C   1 
ATOM   3119  O  O   . HIS C  1 121 ? 203.955 38.493  62.079 1.00   18.23 ? 120  HIS C O   1 
ATOM   3120  C  CB  . HIS C  1 121 ? 202.194 37.372  59.540 1.00   17.60 ? 120  HIS C CB  1 
ATOM   3121  C  CG  . HIS C  1 121 ? 201.023 37.299  58.604 1.00   17.63 ? 120  HIS C CG  1 
ATOM   3122  N  ND1 . HIS C  1 121 ? 199.943 36.524  58.850 1.00   18.06 ? 120  HIS C ND1 1 
ATOM   3123  C  CD2 . HIS C  1 121 ? 200.795 37.914  57.383 1.00   17.58 ? 120  HIS C CD2 1 
ATOM   3124  C  CE1 . HIS C  1 121 ? 199.077 36.636  57.842 1.00   17.95 ? 120  HIS C CE1 1 
ATOM   3125  N  NE2 . HIS C  1 121 ? 199.586 37.508  56.956 1.00   18.03 ? 120  HIS C NE2 1 
ATOM   3126  N  N   . GLU C  1 122 ? 202.351 36.965  62.496 1.00   19.83 ? 121  GLU C N   1 
ATOM   3127  C  CA  . GLU C  1 122 ? 202.969 36.323  63.656 1.00   21.15 ? 121  GLU C CA  1 
ATOM   3128  C  C   . GLU C  1 122 ? 204.355 35.758  63.380 1.00   21.16 ? 121  GLU C C   1 
ATOM   3129  O  O   . GLU C  1 122 ? 205.273 35.933  64.182 1.00   21.48 ? 121  GLU C O   1 
ATOM   3130  C  CB  . GLU C  1 122 ? 202.031 35.207  64.145 1.00   22.63 ? 121  GLU C CB  1 
ATOM   3131  C  CG  . GLU C  1 122 ? 202.586 34.280  65.220 1.00   24.17 ? 121  GLU C CG  1 
ATOM   3132  C  CD  . GLU C  1 122 ? 201.788 32.977  65.365 1.00   26.30 ? 121  GLU C CD  1 
ATOM   3133  O  OE1 . GLU C  1 122 ? 200.929 32.636  64.499 1.00   26.44 ? 121  GLU C OE1 1 
ATOM   3134  O  OE2 . GLU C  1 122 ? 202.063 32.252  66.359 1.00   29.01 ? 121  GLU C OE2 1 
ATOM   3135  N  N   . LYS C  1 123 ? 204.498 35.074  62.254 1.00   21.47 ? 122  LYS C N   1 
ATOM   3136  C  CA  . LYS C  1 123 ? 205.712 34.334  61.950 1.00   22.21 ? 122  LYS C CA  1 
ATOM   3137  C  C   . LYS C  1 123 ? 206.304 34.740  60.619 1.00   21.49 ? 122  LYS C C   1 
ATOM   3138  O  O   . LYS C  1 123 ? 205.715 35.504  59.885 1.00   21.48 ? 122  LYS C O   1 
ATOM   3139  C  CB  . LYS C  1 123 ? 205.406 32.824  61.882 1.00   23.35 ? 122  LYS C CB  1 
ATOM   3140  C  CG  . LYS C  1 123 ? 204.815 32.249  63.153 1.00   24.66 ? 122  LYS C CG  1 
ATOM   3141  C  CD  . LYS C  1 123 ? 204.599 30.754  63.028 1.00   25.63 ? 122  LYS C CD  1 
ATOM   3142  C  CE  . LYS C  1 123 ? 203.307 30.464  62.296 1.00   26.42 ? 122  LYS C CE  1 
ATOM   3143  N  NZ  . LYS C  1 123 ? 203.173 29.024  61.967 1.00   28.10 ? 122  LYS C NZ  1 
ATOM   3144  N  N   . ALA C  1 124 ? 207.454 34.150  60.309 1.00   20.88 ? 123  ALA C N   1 
ATOM   3145  C  CA  . ALA C  1 124 ? 208.153 34.332  59.076 1.00   20.60 ? 123  ALA C CA  1 
ATOM   3146  C  C   . ALA C  1 124 ? 207.359 33.752  57.914 1.00   20.33 ? 123  ALA C C   1 
ATOM   3147  O  O   . ALA C  1 124 ? 206.732 32.691  58.035 1.00   20.21 ? 123  ALA C O   1 
ATOM   3148  C  CB  . ALA C  1 124 ? 209.532 33.678  59.153 1.00   20.61 ? 123  ALA C CB  1 
ATOM   3149  N  N   . ASP C  1 125 ? 207.369 34.502  56.812 1.00   19.47 ? 124  ASP C N   1 
ATOM   3150  C  CA  . ASP C  1 125 ? 206.902 34.054  55.526 1.00   19.54 ? 124  ASP C CA  1 
ATOM   3151  C  C   . ASP C  1 125 ? 208.027 33.178  54.945 1.00   19.42 ? 124  ASP C C   1 
ATOM   3152  O  O   . ASP C  1 125 ? 209.155 33.633  54.818 1.00   19.04 ? 124  ASP C O   1 
ATOM   3153  C  CB  . ASP C  1 125 ? 206.669 35.280  54.631 1.00   19.44 ? 124  ASP C CB  1 
ATOM   3154  C  CG  . ASP C  1 125 ? 205.984 34.955  53.318 1.00   19.90 ? 124  ASP C CG  1 
ATOM   3155  O  OD1 . ASP C  1 125 ? 206.084 33.802  52.832 1.00   19.71 ? 124  ASP C OD1 1 
ATOM   3156  O  OD2 . ASP C  1 125 ? 205.332 35.889  52.766 1.00   19.93 ? 124  ASP C OD2 1 
ATOM   3157  N  N   . ASP C  1 126 ? 207.698 31.942  54.585 1.00   19.45 ? 125  ASP C N   1 
ATOM   3158  C  CA  . ASP C  1 126 ? 208.689 31.009  54.039 1.00   19.96 ? 125  ASP C CA  1 
ATOM   3159  C  C   . ASP C  1 126 ? 208.896 31.203  52.532 1.00   19.89 ? 125  ASP C C   1 
ATOM   3160  O  O   . ASP C  1 126 ? 209.676 30.489  51.910 1.00   20.40 ? 125  ASP C O   1 
ATOM   3161  C  CB  . ASP C  1 126 ? 208.359 29.553  54.442 1.00   20.22 ? 125  ASP C CB  1 
ATOM   3162  C  CG  . ASP C  1 126 ? 207.088 29.006  53.790 1.00   20.64 ? 125  ASP C CG  1 
ATOM   3163  O  OD1 . ASP C  1 126 ? 206.585 29.519  52.749 1.00   20.28 ? 125  ASP C OD1 1 
ATOM   3164  O  OD2 . ASP C  1 126 ? 206.611 27.998  54.326 1.00   21.36 ? 125  ASP C OD2 1 
ATOM   3165  N  N   . LEU C  1 127 ? 208.209 32.195  51.965 1.00   19.46 ? 126  LEU C N   1 
ATOM   3166  C  CA  . LEU C  1 127 ? 208.346 32.587  50.553 1.00   19.46 ? 126  LEU C CA  1 
ATOM   3167  C  C   . LEU C  1 127 ? 207.988 31.463  49.584 1.00   19.88 ? 126  LEU C C   1 
ATOM   3168  O  O   . LEU C  1 127 ? 208.501 31.410  48.469 1.00   19.87 ? 126  LEU C O   1 
ATOM   3169  C  CB  . LEU C  1 127 ? 209.749 33.139  50.253 1.00   19.35 ? 126  LEU C CB  1 
ATOM   3170  C  CG  . LEU C  1 127 ? 210.276 34.214  51.226 1.00   19.45 ? 126  LEU C CG  1 
ATOM   3171  C  CD1 . LEU C  1 127 ? 211.635 34.750  50.759 1.00   19.62 ? 126  LEU C CD1 1 
ATOM   3172  C  CD2 . LEU C  1 127 ? 209.301 35.367  51.424 1.00   18.73 ? 126  LEU C CD2 1 
ATOM   3173  N  N   . GLY C  1 128 ? 207.099 30.584  50.025 1.00   20.20 ? 127  GLY C N   1 
ATOM   3174  C  CA  . GLY C  1 128 ? 206.577 29.522  49.201 1.00   21.33 ? 127  GLY C CA  1 
ATOM   3175  C  C   . GLY C  1 128 ? 207.491 28.322  49.118 1.00   22.05 ? 127  GLY C C   1 
ATOM   3176  O  O   . GLY C  1 128 ? 207.239 27.426  48.348 1.00   21.71 ? 127  GLY C O   1 
ATOM   3177  N  N   . LYS C  1 129 ? 208.552 28.317  49.914 1.00   23.01 ? 128  LYS C N   1 
ATOM   3178  C  CA  . LYS C  1 129 ? 209.531 27.225  49.898 1.00   24.50 ? 128  LYS C CA  1 
ATOM   3179  C  C   . LYS C  1 129 ? 209.320 26.230  51.045 1.00   24.29 ? 128  LYS C C   1 
ATOM   3180  O  O   . LYS C  1 129 ? 210.220 25.464  51.350 1.00   24.68 ? 128  LYS C O   1 
ATOM   3181  C  CB  . LYS C  1 129 ? 210.946 27.787  50.012 1.00   25.71 ? 128  LYS C CB  1 
ATOM   3182  C  CG  . LYS C  1 129 ? 211.381 28.684  48.868 1.00   27.36 ? 128  LYS C CG  1 
ATOM   3183  C  CD  . LYS C  1 129 ? 212.851 29.034  49.071 1.00   28.75 ? 128  LYS C CD  1 
ATOM   3184  C  CE  . LYS C  1 129 ? 213.530 29.380  47.767 1.00   30.50 ? 128  LYS C CE  1 
ATOM   3185  N  NZ  . LYS C  1 129 ? 212.747 30.449  47.075 1.00   31.80 ? 128  LYS C NZ  1 
ATOM   3186  N  N   . GLY C  1 130 ? 208.145 26.242  51.672 1.00   23.65 ? 129  GLY C N   1 
ATOM   3187  C  CA  . GLY C  1 130 ? 207.893 25.411  52.841 1.00   24.23 ? 129  GLY C CA  1 
ATOM   3188  C  C   . GLY C  1 130 ? 207.455 23.965  52.608 1.00   24.84 ? 129  GLY C C   1 
ATOM   3189  O  O   . GLY C  1 130 ? 207.308 23.203  53.576 1.00   25.46 ? 129  GLY C O   1 
ATOM   3190  N  N   . GLY C  1 131 ? 207.221 23.584  51.362 1.00   24.94 ? 130  GLY C N   1 
ATOM   3191  C  CA  . GLY C  1 131 ? 206.894 22.186  51.031 1.00   26.59 ? 130  GLY C CA  1 
ATOM   3192  C  C   . GLY C  1 131 ? 205.459 21.703  51.244 1.00   27.86 ? 130  GLY C C   1 
ATOM   3193  O  O   . GLY C  1 131 ? 205.211 20.494  51.252 1.00   27.11 ? 130  GLY C O   1 
ATOM   3194  N  N   . ASN C  1 132 ? 204.505 22.626  51.405 1.00   30.11 ? 131  ASN C N   1 
ATOM   3195  C  CA  . ASN C  1 132 ? 203.082 22.250  51.589 1.00   32.14 ? 131  ASN C CA  1 
ATOM   3196  C  C   . ASN C  1 132 ? 202.125 23.261  51.011 1.00   33.48 ? 131  ASN C C   1 
ATOM   3197  O  O   . ASN C  1 132 ? 202.557 24.324  50.565 1.00   32.67 ? 131  ASN C O   1 
ATOM   3198  C  CB  . ASN C  1 132 ? 202.768 21.967  53.058 1.00   32.55 ? 131  ASN C CB  1 
ATOM   3199  C  CG  . ASN C  1 132 ? 202.980 23.156  53.968 1.00   33.50 ? 131  ASN C CG  1 
ATOM   3200  O  OD1 . ASN C  1 132 ? 203.031 24.330  53.537 1.00   32.30 ? 131  ASN C OD1 1 
ATOM   3201  N  ND2 . ASN C  1 132 ? 203.093 22.856  55.265 1.00   32.88 ? 131  ASN C ND2 1 
ATOM   3202  N  N   . GLU C  1 133 ? 200.832 22.924  50.988 1.00   35.29 ? 132  GLU C N   1 
ATOM   3203  C  CA  . GLU C  1 133 ? 199.835 23.814  50.371 1.00   36.49 ? 132  GLU C CA  1 
ATOM   3204  C  C   . GLU C  1 133 ? 199.812 25.163  51.055 1.00   32.36 ? 132  GLU C C   1 
ATOM   3205  O  O   . GLU C  1 133 ? 199.709 26.185  50.389 1.00   30.76 ? 132  GLU C O   1 
ATOM   3206  C  CB  . GLU C  1 133 ? 198.415 23.213  50.377 1.00   40.82 ? 132  GLU C CB  1 
ATOM   3207  C  CG  . GLU C  1 133 ? 198.209 22.038  49.418 1.00   46.27 ? 132  GLU C CG  1 
ATOM   3208  C  CD  . GLU C  1 133 ? 198.472 22.370  47.939 1.00   49.57 ? 132  GLU C CD  1 
ATOM   3209  O  OE1 . GLU C  1 133 ? 199.637 22.244  47.461 1.00   50.81 ? 132  GLU C OE1 1 
ATOM   3210  O  OE2 . GLU C  1 133 ? 197.494 22.726  47.237 1.00   55.69 ? 132  GLU C OE2 1 
ATOM   3211  N  N   . GLU C  1 134 ? 199.913 25.161  52.378 1.00   30.67 ? 133  GLU C N   1 
ATOM   3212  C  CA  . GLU C  1 134 ? 199.888 26.404  53.138 1.00   29.72 ? 133  GLU C CA  1 
ATOM   3213  C  C   . GLU C  1 134 ? 201.029 27.335  52.690 1.00   27.48 ? 133  GLU C C   1 
ATOM   3214  O  O   . GLU C  1 134 ? 200.848 28.544  52.593 1.00   25.41 ? 133  GLU C O   1 
ATOM   3215  C  CB  . GLU C  1 134 ? 199.982 26.121  54.635 1.00   31.17 ? 133  GLU C CB  1 
ATOM   3216  C  CG  . GLU C  1 134 ? 199.705 27.333  55.524 1.00   32.05 ? 133  GLU C CG  1 
ATOM   3217  C  CD  . GLU C  1 134 ? 198.291 27.848  55.366 1.00   33.37 ? 133  GLU C CD  1 
ATOM   3218  O  OE1 . GLU C  1 134 ? 197.348 27.051  55.527 1.00   35.29 ? 133  GLU C OE1 1 
ATOM   3219  O  OE2 . GLU C  1 134 ? 198.120 29.045  55.074 1.00   34.37 ? 133  GLU C OE2 1 
ATOM   3220  N  N   . SER C  1 135 ? 202.192 26.760  52.403 1.00   26.13 ? 134  SER C N   1 
ATOM   3221  C  CA  . SER C  1 135 ? 203.319 27.540  51.898 1.00   25.84 ? 134  SER C CA  1 
ATOM   3222  C  C   . SER C  1 135 ? 202.976 28.256  50.606 1.00   25.84 ? 134  SER C C   1 
ATOM   3223  O  O   . SER C  1 135 ? 203.388 29.404  50.415 1.00   25.04 ? 134  SER C O   1 
ATOM   3224  C  CB  . SER C  1 135 ? 204.549 26.658  51.644 1.00   25.55 ? 134  SER C CB  1 
ATOM   3225  O  OG  . SER C  1 135 ? 205.645 27.445  51.226 1.00   24.38 ? 134  SER C OG  1 
ATOM   3226  N  N   . THR C  1 136 ? 202.227 27.582  49.733 1.00   26.13 ? 135  THR C N   1 
ATOM   3227  C  CA  . THR C  1 136 ? 201.879 28.128  48.421 1.00   26.81 ? 135  THR C CA  1 
ATOM   3228  C  C   . THR C  1 136 ? 200.644 29.045  48.475 1.00   26.74 ? 135  THR C C   1 
ATOM   3229  O  O   . THR C  1 136 ? 200.226 29.585  47.441 1.00   25.32 ? 135  THR C O   1 
ATOM   3230  C  CB  . THR C  1 136 ? 201.623 27.007  47.364 1.00   27.53 ? 135  THR C CB  1 
ATOM   3231  O  OG1 . THR C  1 136 ? 200.449 26.273  47.727 1.00   29.61 ? 135  THR C OG1 1 
ATOM   3232  C  CG2 . THR C  1 136 ? 202.786 26.068  47.264 1.00   27.82 ? 135  THR C CG2 1 
ATOM   3233  N  N   . LYS C  1 137 ? 200.085 29.226  49.670 1.00   27.18 ? 136  LYS C N   1 
ATOM   3234  C  CA  . LYS C  1 137 ? 198.972 30.150  49.874 1.00   28.61 ? 136  LYS C CA  1 
ATOM   3235  C  C   . LYS C  1 137 ? 199.362 31.369  50.731 1.00   26.81 ? 136  LYS C C   1 
ATOM   3236  O  O   . LYS C  1 137 ? 199.106 32.502  50.336 1.00   25.12 ? 136  LYS C O   1 
ATOM   3237  C  CB  . LYS C  1 137 ? 197.808 29.438  50.556 1.00   31.58 ? 136  LYS C CB  1 
ATOM   3238  C  CG  . LYS C  1 137 ? 197.130 28.361  49.734 1.00   35.19 ? 136  LYS C CG  1 
ATOM   3239  C  CD  . LYS C  1 137 ? 195.946 27.789  50.507 1.00   38.28 ? 136  LYS C CD  1 
ATOM   3240  C  CE  . LYS C  1 137 ? 195.219 26.693  49.735 1.00   41.45 ? 136  LYS C CE  1 
ATOM   3241  N  NZ  . LYS C  1 137 ? 193.732 26.778  49.922 1.00   43.77 ? 136  LYS C NZ  1 
ATOM   3242  N  N   . THR C  1 138 ? 199.960 31.117  51.902 1.00   25.36 ? 137  THR C N   1 
ATOM   3243  C  CA  . THR C  1 138 ? 200.290 32.172  52.870 1.00   24.09 ? 137  THR C CA  1 
ATOM   3244  C  C   . THR C  1 138 ? 201.754 32.269  53.277 1.00   23.33 ? 137  THR C C   1 
ATOM   3245  O  O   . THR C  1 138 ? 202.149 33.183  54.037 1.00   23.26 ? 137  THR C O   1 
ATOM   3246  C  CB  . THR C  1 138 ? 199.511 31.970  54.179 1.00   24.39 ? 137  THR C CB  1 
ATOM   3247  O  OG1 . THR C  1 138 ? 199.989 30.791  54.840 1.00   24.73 ? 137  THR C OG1 1 
ATOM   3248  C  CG2 . THR C  1 138 ? 197.997 31.873  53.920 1.00   24.24 ? 137  THR C CG2 1 
ATOM   3249  N  N   . GLY C  1 139 ? 202.569 31.332  52.817 1.00   22.35 ? 138  GLY C N   1 
ATOM   3250  C  CA  . GLY C  1 139 ? 203.924 31.252  53.292 1.00   21.86 ? 138  GLY C CA  1 
ATOM   3251  C  C   . GLY C  1 139 ? 204.077 30.822  54.754 1.00   21.69 ? 138  GLY C C   1 
ATOM   3252  O  O   . GLY C  1 139 ? 205.126 31.036  55.342 1.00   20.94 ? 138  GLY C O   1 
ATOM   3253  N  N   . ASN C  1 140 ? 203.052 30.192  55.336 1.00   21.88 ? 139  ASN C N   1 
ATOM   3254  C  CA  . ASN C  1 140 ? 203.109 29.756  56.732 1.00   21.91 ? 139  ASN C CA  1 
ATOM   3255  C  C   . ASN C  1 140 ? 203.407 30.898  57.723 1.00   21.17 ? 139  ASN C C   1 
ATOM   3256  O  O   . ASN C  1 140 ? 204.009 30.670  58.771 1.00   21.28 ? 139  ASN C O   1 
ATOM   3257  C  CB  . ASN C  1 140 ? 204.141 28.626  56.882 1.00   22.60 ? 139  ASN C CB  1 
ATOM   3258  C  CG  . ASN C  1 140 ? 203.647 27.310  56.313 1.00   23.47 ? 139  ASN C CG  1 
ATOM   3259  O  OD1 . ASN C  1 140 ? 202.645 26.759  56.788 1.00   24.46 ? 139  ASN C OD1 1 
ATOM   3260  N  ND2 . ASN C  1 140 ? 204.342 26.798  55.300 1.00   23.16 ? 139  ASN C ND2 1 
ATOM   3261  N  N   . ALA C  1 141 ? 202.976 32.116  57.392 1.00   20.22 ? 140  ALA C N   1 
ATOM   3262  C  CA  . ALA C  1 141 ? 203.268 33.299  58.207 1.00   20.05 ? 140  ALA C CA  1 
ATOM   3263  C  C   . ALA C  1 141 ? 202.362 33.369  59.447 1.00   20.18 ? 140  ALA C C   1 
ATOM   3264  O  O   . ALA C  1 141 ? 202.575 34.197  60.329 1.00   20.55 ? 140  ALA C O   1 
ATOM   3265  C  CB  . ALA C  1 141 ? 203.155 34.586  57.374 1.00   19.30 ? 140  ALA C CB  1 
ATOM   3266  N  N   . GLY C  1 142 ? 201.363 32.499  59.516 1.00   20.46 ? 141  GLY C N   1 
ATOM   3267  C  CA  . GLY C  1 142 ? 200.553 32.350  60.719 1.00   20.64 ? 141  GLY C CA  1 
ATOM   3268  C  C   . GLY C  1 142 ? 199.567 33.490  60.898 1.00   20.52 ? 141  GLY C C   1 
ATOM   3269  O  O   . GLY C  1 142 ? 199.089 34.071  59.919 1.00   20.27 ? 141  GLY C O   1 
ATOM   3270  N  N   . SER C  1 143 ? 199.280 33.806  62.160 1.00   20.50 ? 142  SER C N   1 
ATOM   3271  C  CA  . SER C  1 143 ? 198.194 34.693  62.490 1.00   20.64 ? 142  SER C CA  1 
ATOM   3272  C  C   . SER C  1 143 ? 198.480 36.168  62.087 1.00   19.85 ? 142  SER C C   1 
ATOM   3273  O  O   . SER C  1 143 ? 199.630 36.591  61.861 1.00   19.18 ? 142  SER C O   1 
ATOM   3274  C  CB  . SER C  1 143 ? 197.829 34.564  63.994 1.00   21.03 ? 142  SER C CB  1 
ATOM   3275  O  OG  . SER C  1 143 ? 198.714 35.290  64.823 0.50   20.87 ? 142  SER C OG  1 
ATOM   3276  N  N   . ARG C  1 144 ? 197.398 36.925  62.019 1.00   19.56 ? 143  ARG C N   1 
ATOM   3277  C  CA  . ARG C  1 144 ? 197.433 38.315  61.612 1.00   19.02 ? 143  ARG C CA  1 
ATOM   3278  C  C   . ARG C  1 144 ? 197.513 39.156  62.872 1.00   18.89 ? 143  ARG C C   1 
ATOM   3279  O  O   . ARG C  1 144 ? 196.518 39.307  63.570 1.00   19.21 ? 143  ARG C O   1 
ATOM   3280  C  CB  . ARG C  1 144 ? 196.173 38.608  60.780 1.00   18.95 ? 143  ARG C CB  1 
ATOM   3281  C  CG  . ARG C  1 144 ? 195.948 37.558  59.719 1.00   19.12 ? 143  ARG C CG  1 
ATOM   3282  C  CD  . ARG C  1 144 ? 194.791 37.834  58.789 1.00   19.49 ? 143  ARG C CD  1 
ATOM   3283  N  NE  . ARG C  1 144 ? 194.728 36.815  57.748 1.00   19.59 ? 143  ARG C NE  1 
ATOM   3284  C  CZ  . ARG C  1 144 ? 193.882 36.802  56.732 1.00   19.67 ? 143  ARG C CZ  1 
ATOM   3285  N  NH1 . ARG C  1 144 ? 192.997 37.767  56.582 1.00   20.12 ? 143  ARG C NH1 1 
ATOM   3286  N  NH2 . ARG C  1 144 ? 193.931 35.816  55.851 1.00   19.87 ? 143  ARG C NH2 1 
ATOM   3287  N  N   . LEU C  1 145 ? 198.702 39.659  63.199 1.00   18.54 ? 144  LEU C N   1 
ATOM   3288  C  CA  . LEU C  1 145 ? 198.883 40.424  64.419 1.00   18.52 ? 144  LEU C CA  1 
ATOM   3289  C  C   . LEU C  1 145 ? 198.296 41.817  64.357 1.00   18.28 ? 144  LEU C C   1 
ATOM   3290  O  O   . LEU C  1 145 ? 197.809 42.341  65.364 1.00   18.80 ? 144  LEU C O   1 
ATOM   3291  C  CB  . LEU C  1 145 ? 200.347 40.532  64.778 1.00   18.68 ? 144  LEU C CB  1 
ATOM   3292  C  CG  . LEU C  1 145 ? 201.055 39.201  65.021 1.00   19.28 ? 144  LEU C CG  1 
ATOM   3293  C  CD1 . LEU C  1 145 ? 202.428 39.476  65.615 1.00   19.63 ? 144  LEU C CD1 1 
ATOM   3294  C  CD2 . LEU C  1 145 ? 200.234 38.240  65.880 1.00   19.42 ? 144  LEU C CD2 1 
ATOM   3295  N  N   . ALA C  1 146 ? 198.368 42.432  63.193 1.00   17.61 ? 145  ALA C N   1 
ATOM   3296  C  CA  . ALA C  1 146 ? 197.814 43.762  63.025 1.00   17.39 ? 145  ALA C CA  1 
ATOM   3297  C  C   . ALA C  1 146 ? 197.589 44.043  61.551 1.00   16.84 ? 145  ALA C C   1 
ATOM   3298  O  O   . ALA C  1 146 ? 198.260 43.450  60.672 1.00   16.66 ? 145  ALA C O   1 
ATOM   3299  C  CB  . ALA C  1 146 ? 198.735 44.796  63.656 1.00   17.29 ? 145  ALA C CB  1 
ATOM   3300  N  N   . CYS C  1 147 ? 196.647 44.932  61.277 1.00   16.59 ? 146  CYS C N   1 
ATOM   3301  C  CA  . CYS C  1 147 ? 196.310 45.274  59.916 1.00   16.42 ? 146  CYS C CA  1 
ATOM   3302  C  C   . CYS C  1 147 ? 195.714 46.661  59.874 1.00   15.91 ? 146  CYS C C   1 
ATOM   3303  O  O   . CYS C  1 147 ? 195.400 47.245  60.915 1.00   16.06 ? 146  CYS C O   1 
ATOM   3304  C  CB  . CYS C  1 147 ? 195.341 44.255  59.332 1.00   16.92 ? 146  CYS C CB  1 
ATOM   3305  S  SG  . CYS C  1 147 ? 193.819 44.095  60.305 1.00   18.21 ? 146  CYS C SG  1 
ATOM   3306  N  N   . GLY C  1 148 ? 195.582 47.180  58.654 1.00   15.18 ? 147  GLY C N   1 
ATOM   3307  C  CA  . GLY C  1 148 ? 194.873 48.444  58.408 1.00   14.64 ? 147  GLY C CA  1 
ATOM   3308  C  C   . GLY C  1 148 ? 194.521 48.551  56.951 1.00   14.17 ? 147  GLY C C   1 
ATOM   3309  O  O   . GLY C  1 148 ? 195.103 47.842  56.105 1.00   13.90 ? 147  GLY C O   1 
ATOM   3310  N  N   . VAL C  1 149 ? 193.541 49.395  56.644 1.00   13.83 ? 148  VAL C N   1 
ATOM   3311  C  CA  . VAL C  1 149 ? 193.178 49.636  55.253 1.00   13.63 ? 148  VAL C CA  1 
ATOM   3312  C  C   . VAL C  1 149 ? 194.122 50.672  54.664 1.00   13.58 ? 148  VAL C C   1 
ATOM   3313  O  O   . VAL C  1 149 ? 194.459 51.671  55.326 1.00   13.60 ? 148  VAL C O   1 
ATOM   3314  C  CB  . VAL C  1 149 ? 191.721 50.108  55.114 1.00   13.68 ? 148  VAL C CB  1 
ATOM   3315  C  CG1 . VAL C  1 149 ? 191.352 50.351  53.648 1.00   13.52 ? 148  VAL C CG1 1 
ATOM   3316  C  CG2 . VAL C  1 149 ? 190.772 49.090  55.754 1.00   13.75 ? 148  VAL C CG2 1 
ATOM   3317  N  N   . ILE C  1 150 ? 194.543 50.452  53.419 1.00   13.42 ? 149  ILE C N   1 
ATOM   3318  C  CA  . ILE C  1 150 ? 195.493 51.349  52.763 1.00   13.38 ? 149  ILE C CA  1 
ATOM   3319  C  C   . ILE C  1 150 ? 194.754 52.510  52.136 1.00   13.64 ? 149  ILE C C   1 
ATOM   3320  O  O   . ILE C  1 150 ? 193.832 52.324  51.336 1.00   13.75 ? 149  ILE C O   1 
ATOM   3321  C  CB  . ILE C  1 150 ? 196.362 50.613  51.716 1.00   13.33 ? 149  ILE C CB  1 
ATOM   3322  C  CG1 . ILE C  1 150 ? 197.155 49.488  52.364 1.00   13.27 ? 149  ILE C CG1 1 
ATOM   3323  C  CG2 . ILE C  1 150 ? 197.367 51.543  51.068 1.00   13.40 ? 149  ILE C CG2 1 
ATOM   3324  C  CD1 . ILE C  1 150 ? 197.670 48.428  51.379 1.00   13.21 ? 149  ILE C CD1 1 
ATOM   3325  N  N   . GLY C  1 151 ? 195.136 53.722  52.521 1.00   13.85 ? 150  GLY C N   1 
ATOM   3326  C  CA  . GLY C  1 151 ? 194.404 54.903  52.127 1.00   14.14 ? 150  GLY C CA  1 
ATOM   3327  C  C   . GLY C  1 151 ? 195.237 55.915  51.390 1.00   14.56 ? 150  GLY C C   1 
ATOM   3328  O  O   . GLY C  1 151 ? 196.464 55.953  51.551 1.00   14.63 ? 150  GLY C O   1 
ATOM   3329  N  N   . ILE C  1 152 ? 194.563 56.751  50.607 1.00   15.06 ? 151  ILE C N   1 
ATOM   3330  C  CA  . ILE C  1 152 ? 195.216 57.816  49.859 1.00   15.83 ? 151  ILE C CA  1 
ATOM   3331  C  C   . ILE C  1 152 ? 195.689 58.870  50.862 1.00   16.25 ? 151  ILE C C   1 
ATOM   3332  O  O   . ILE C  1 152 ? 194.928 59.286  51.774 1.00   16.22 ? 151  ILE C O   1 
ATOM   3333  C  CB  . ILE C  1 152 ? 194.256 58.449  48.830 1.00   16.20 ? 151  ILE C CB  1 
ATOM   3334  C  CG1 . ILE C  1 152 ? 193.827 57.401  47.791 1.00   16.45 ? 151  ILE C CG1 1 
ATOM   3335  C  CG2 . ILE C  1 152 ? 194.887 59.648  48.117 1.00   16.54 ? 151  ILE C CG2 1 
ATOM   3336  C  CD1 . ILE C  1 152 ? 192.529 57.776  47.054 1.00   16.48 ? 151  ILE C CD1 1 
ATOM   3337  N  N   . ALA C  1 153 ? 196.939 59.279  50.711 1.00   16.95 ? 152  ALA C N   1 
ATOM   3338  C  CA  . ALA C  1 153 ? 197.576 60.248  51.604 1.00   18.00 ? 152  ALA C CA  1 
ATOM   3339  C  C   . ALA C  1 153 ? 197.926 61.540  50.870 1.00   19.69 ? 152  ALA C C   1 
ATOM   3340  O  O   . ALA C  1 153 ? 198.067 61.544  49.637 1.00   19.57 ? 152  ALA C O   1 
ATOM   3341  C  CB  . ALA C  1 153 ? 198.833 59.651  52.196 1.00   17.67 ? 152  ALA C CB  1 
ATOM   3342  N  N   . GLN C  1 154 ? 198.103 62.613  51.646 1.00   21.69 ? 153  GLN C N   1 
ATOM   3343  C  CA  . GLN C  1 154 ? 198.479 63.916  51.097 1.00   24.22 ? 153  GLN C CA  1 
ATOM   3344  C  C   . GLN C  1 154 ? 199.955 63.900  50.704 1.00   25.94 ? 153  GLN C C   1 
ATOM   3345  O  O   . GLN C  1 154 ? 200.249 64.368  49.614 1.00   27.55 ? 153  GLN C O   1 
ATOM   3346  C  CB  . GLN C  1 154 ? 198.258 65.028  52.101 1.00   25.50 ? 153  GLN C CB  1 
ATOM   3347  C  CG  . GLN C  1 154 ? 198.265 66.413  51.469 1.00   27.77 ? 153  GLN C CG  1 
ATOM   3348  C  CD  . GLN C  1 154 ? 197.909 67.503  52.453 1.00   28.93 ? 153  GLN C CD  1 
ATOM   3349  O  OE1 . GLN C  1 154 ? 197.160 68.422  52.136 1.00   32.92 ? 153  GLN C OE1 1 
ATOM   3350  N  NE2 . GLN C  1 154 ? 198.437 67.406  53.645 1.00   29.39 ? 153  GLN C NE2 1 
ATOM   3351  O  OXT . GLN C  1 154 ? 200.845 63.432  51.444 1.00   25.45 ? 153  GLN C OXT 1 
ATOM   3352  N  N   . ALA D  1 2   ? 160.168 155.193 44.966 1.00   53.70 ? 1    ALA D N   1 
ATOM   3353  C  CA  . ALA D  1 2   ? 161.125 155.731 43.955 1.00   53.76 ? 1    ALA D CA  1 
ATOM   3354  C  C   . ALA D  1 2   ? 162.150 156.729 44.569 1.00   51.06 ? 1    ALA D C   1 
ATOM   3355  O  O   . ALA D  1 2   ? 163.340 156.654 44.277 1.00   51.36 ? 1    ALA D O   1 
ATOM   3356  C  CB  . ALA D  1 2   ? 160.350 156.368 42.798 1.00   54.22 ? 1    ALA D CB  1 
ATOM   3357  N  N   . THR D  1 3   ? 161.684 157.636 45.427 1.00   47.93 ? 2    THR D N   1 
ATOM   3358  C  CA  . THR D  1 3   ? 162.499 158.750 45.921 1.00   45.33 ? 2    THR D CA  1 
ATOM   3359  C  C   . THR D  1 3   ? 163.162 158.449 47.263 1.00   41.67 ? 2    THR D C   1 
ATOM   3360  O  O   . THR D  1 3   ? 164.246 158.953 47.521 1.00   38.70 ? 2    THR D O   1 
ATOM   3361  C  CB  . THR D  1 3   ? 161.651 160.039 46.085 1.00   46.41 ? 2    THR D CB  1 
ATOM   3362  O  OG1 . THR D  1 3   ? 160.948 160.296 44.877 1.00   49.96 ? 2    THR D OG1 1 
ATOM   3363  C  CG2 . THR D  1 3   ? 162.518 161.259 46.390 1.00   47.79 ? 2    THR D CG2 1 
ATOM   3364  N  N   . LYS D  1 4   ? 162.505 157.660 48.118 1.00   38.98 ? 3    LYS D N   1 
ATOM   3365  C  CA  . LYS D  1 4   ? 162.976 157.455 49.488 1.00   37.11 ? 3    LYS D CA  1 
ATOM   3366  C  C   . LYS D  1 4   ? 163.018 155.990 49.888 1.00   34.27 ? 3    LYS D C   1 
ATOM   3367  O  O   . LYS D  1 4   ? 162.168 155.184 49.486 1.00   32.26 ? 3    LYS D O   1 
ATOM   3368  C  CB  . LYS D  1 4   ? 162.081 158.178 50.485 1.00   39.25 ? 3    LYS D CB  1 
ATOM   3369  C  CG  . LYS D  1 4   ? 162.065 159.696 50.364 1.00   43.39 ? 3    LYS D CG  1 
ATOM   3370  C  CD  . LYS D  1 4   ? 161.242 160.289 51.500 1.00   45.09 ? 3    LYS D CD  1 
ATOM   3371  C  CE  . LYS D  1 4   ? 160.818 161.722 51.233 1.00   48.24 ? 3    LYS D CE  1 
ATOM   3372  N  NZ  . LYS D  1 4   ? 161.836 162.667 51.779 1.00   49.27 ? 3    LYS D NZ  1 
ATOM   3373  N  N   . ALA D  1 5   ? 163.990 155.662 50.727 1.00   30.95 ? 4    ALA D N   1 
ATOM   3374  C  CA  . ALA D  1 5   ? 164.088 154.326 51.294 1.00   28.69 ? 4    ALA D CA  1 
ATOM   3375  C  C   . ALA D  1 5   ? 164.619 154.385 52.717 1.00   27.07 ? 4    ALA D C   1 
ATOM   3376  O  O   . ALA D  1 5   ? 165.116 155.432 53.186 1.00   26.95 ? 4    ALA D O   1 
ATOM   3377  C  CB  . ALA D  1 5   ? 164.965 153.446 50.429 1.00   28.38 ? 4    ALA D CB  1 
ATOM   3378  N  N   . VAL D  1 6   ? 164.500 153.252 53.394 1.00   25.15 ? 5    VAL D N   1 
ATOM   3379  C  CA  . VAL D  1 6   ? 164.880 153.139 54.771 1.00   24.54 ? 5    VAL D CA  1 
ATOM   3380  C  C   . VAL D  1 6   ? 165.346 151.719 55.082 1.00   23.62 ? 5    VAL D C   1 
ATOM   3381  O  O   . VAL D  1 6   ? 164.952 150.755 54.420 1.00   22.66 ? 5    VAL D O   1 
ATOM   3382  C  CB  . VAL D  1 6   ? 163.708 153.542 55.679 1.00   24.94 ? 5    VAL D CB  1 
ATOM   3383  C  CG1 . VAL D  1 6   ? 162.615 152.489 55.638 1.00   24.44 ? 5    VAL D CG1 1 
ATOM   3384  C  CG2 . VAL D  1 6   ? 164.189 153.794 57.107 1.00   24.80 ? 5    VAL D CG2 1 
ATOM   3385  N  N   . CYS D  1 7   ? 166.203 151.602 56.085 1.00   23.45 ? 6    CYS D N   1 
ATOM   3386  C  CA  . CYS D  1 7   ? 166.774 150.321 56.477 1.00   23.18 ? 6    CYS D CA  1 
ATOM   3387  C  C   . CYS D  1 7   ? 166.956 150.285 57.980 1.00   22.95 ? 6    CYS D C   1 
ATOM   3388  O  O   . CYS D  1 7   ? 167.614 151.180 58.548 1.00   22.15 ? 6    CYS D O   1 
ATOM   3389  C  CB  . CYS D  1 7   ? 168.121 150.085 55.802 1.00   23.57 ? 6    CYS D CB  1 
ATOM   3390  S  SG  . CYS D  1 7   ? 168.807 148.458 56.213 1.00   24.14 ? 6    CYS D SG  1 
ATOM   3391  N  N   . VAL D  1 8   ? 166.341 149.287 58.620 1.00   22.49 ? 7    VAL D N   1 
ATOM   3392  C  CA  . VAL D  1 8   ? 166.564 149.029 60.048 1.00   22.91 ? 7    VAL D CA  1 
ATOM   3393  C  C   . VAL D  1 8   ? 167.650 147.956 60.187 1.00   23.34 ? 7    VAL D C   1 
ATOM   3394  O  O   . VAL D  1 8   ? 167.452 146.795 59.791 1.00   22.45 ? 7    VAL D O   1 
ATOM   3395  C  CB  . VAL D  1 8   ? 165.285 148.546 60.772 1.00   22.59 ? 7    VAL D CB  1 
ATOM   3396  C  CG1 . VAL D  1 8   ? 165.574 148.284 62.243 1.00   22.50 ? 7    VAL D CG1 1 
ATOM   3397  C  CG2 . VAL D  1 8   ? 164.162 149.567 60.653 1.00   22.83 ? 7    VAL D CG2 1 
ATOM   3398  N  N   . LEU D  1 9   ? 168.786 148.342 60.755 1.00   24.59 ? 8    LEU D N   1 
ATOM   3399  C  CA  . LEU D  1 9   ? 169.921 147.429 60.938 1.00   25.42 ? 8    LEU D CA  1 
ATOM   3400  C  C   . LEU D  1 9   ? 169.819 146.704 62.275 1.00   25.79 ? 8    LEU D C   1 
ATOM   3401  O  O   . LEU D  1 9   ? 169.610 147.338 63.310 1.00   25.79 ? 8    LEU D O   1 
ATOM   3402  C  CB  . LEU D  1 9   ? 171.239 148.191 60.889 1.00   26.45 ? 8    LEU D CB  1 
ATOM   3403  C  CG  . LEU D  1 9   ? 171.703 148.817 59.569 1.00   27.70 ? 8    LEU D CG  1 
ATOM   3404  C  CD1 . LEU D  1 9   ? 171.976 147.744 58.536 1.00   26.87 ? 8    LEU D CD1 1 
ATOM   3405  C  CD2 . LEU D  1 9   ? 170.677 149.812 59.045 1.00   29.08 ? 8    LEU D CD2 1 
ATOM   3406  N  N   . LYS D  1 10  ? 169.959 145.379 62.238 1.00   26.74 ? 9    LYS D N   1 
ATOM   3407  C  CA  . LYS D  1 10  ? 169.957 144.534 63.446 1.00   28.84 ? 9    LYS D CA  1 
ATOM   3408  C  C   . LYS D  1 10  ? 170.839 143.331 63.240 1.00   27.88 ? 9    LYS D C   1 
ATOM   3409  O  O   . LYS D  1 10  ? 171.060 142.912 62.096 1.00   27.32 ? 9    LYS D O   1 
ATOM   3410  C  CB  . LYS D  1 10  ? 168.566 143.988 63.755 1.00   32.08 ? 9    LYS D CB  1 
ATOM   3411  C  CG  . LYS D  1 10  ? 167.578 145.013 64.259 1.00   36.28 ? 9    LYS D CG  1 
ATOM   3412  C  CD  . LYS D  1 10  ? 166.376 144.307 64.879 1.00   40.49 ? 9    LYS D CD  1 
ATOM   3413  C  CE  . LYS D  1 10  ? 165.284 145.276 65.336 1.00   43.43 ? 9    LYS D CE  1 
ATOM   3414  N  NZ  . LYS D  1 10  ? 164.356 145.626 64.221 1.00   44.47 ? 9    LYS D NZ  1 
ATOM   3415  N  N   . GLY D  1 11  ? 171.300 142.754 64.348 1.00   27.91 ? 10   GLY D N   1 
ATOM   3416  C  CA  . GLY D  1 11  ? 172.145 141.568 64.315 1.00   28.50 ? 10   GLY D CA  1 
ATOM   3417  C  C   . GLY D  1 11  ? 171.981 140.722 65.564 1.00   29.54 ? 10   GLY D C   1 
ATOM   3418  O  O   . GLY D  1 11  ? 170.999 140.862 66.282 1.00   28.25 ? 10   GLY D O   1 
ATOM   3419  N  N   . ASP D  1 12  ? 172.946 139.836 65.799 1.00   31.51 ? 11   ASP D N   1 
ATOM   3420  C  CA  . ASP D  1 12  ? 172.949 138.942 66.974 1.00   33.83 ? 11   ASP D CA  1 
ATOM   3421  C  C   . ASP D  1 12  ? 173.509 139.605 68.223 1.00   34.78 ? 11   ASP D C   1 
ATOM   3422  O  O   . ASP D  1 12  ? 173.266 139.146 69.331 1.00   36.78 ? 11   ASP D O   1 
ATOM   3423  C  CB  . ASP D  1 12  ? 173.793 137.697 66.687 1.00   36.47 ? 11   ASP D CB  1 
ATOM   3424  C  CG  . ASP D  1 12  ? 173.271 136.889 65.490 1.00   37.31 ? 11   ASP D CG  1 
ATOM   3425  O  OD1 . ASP D  1 12  ? 172.029 136.796 65.305 1.00   35.24 ? 11   ASP D OD1 1 
ATOM   3426  O  OD2 . ASP D  1 12  ? 174.128 136.364 64.736 1.00   40.02 ? 11   ASP D OD2 1 
ATOM   3427  N  N   . GLY D  1 13  ? 174.288 140.664 68.032 1.00   32.64 ? 12   GLY D N   1 
ATOM   3428  C  CA  . GLY D  1 13  ? 174.873 141.417 69.126 1.00   32.15 ? 12   GLY D CA  1 
ATOM   3429  C  C   . GLY D  1 13  ? 174.075 142.685 69.313 1.00   30.91 ? 12   GLY D C   1 
ATOM   3430  O  O   . GLY D  1 13  ? 172.895 142.721 68.954 1.00   31.22 ? 12   GLY D O   1 
ATOM   3431  N  N   . PRO D  1 14  ? 174.715 143.739 69.849 1.00   29.16 ? 13   PRO D N   1 
ATOM   3432  C  CA  . PRO D  1 14  ? 174.033 144.974 70.218 1.00   28.57 ? 13   PRO D CA  1 
ATOM   3433  C  C   . PRO D  1 14  ? 173.967 146.033 69.116 1.00   26.88 ? 13   PRO D C   1 
ATOM   3434  O  O   . PRO D  1 14  ? 173.400 147.100 69.333 1.00   25.95 ? 13   PRO D O   1 
ATOM   3435  C  CB  . PRO D  1 14  ? 174.906 145.503 71.356 1.00   29.38 ? 13   PRO D CB  1 
ATOM   3436  C  CG  . PRO D  1 14  ? 176.279 145.080 70.951 1.00   29.61 ? 13   PRO D CG  1 
ATOM   3437  C  CD  . PRO D  1 14  ? 176.133 143.763 70.246 1.00   29.46 ? 13   PRO D CD  1 
ATOM   3438  N  N   . VAL D  1 15  ? 174.563 145.758 67.961 1.00   26.46 ? 14   VAL D N   1 
ATOM   3439  C  CA  . VAL D  1 15  ? 174.633 146.753 66.892 1.00   26.18 ? 14   VAL D CA  1 
ATOM   3440  C  C   . VAL D  1 15  ? 173.244 146.960 66.277 1.00   26.08 ? 14   VAL D C   1 
ATOM   3441  O  O   . VAL D  1 15  ? 172.599 146.017 65.813 1.00   25.72 ? 14   VAL D O   1 
ATOM   3442  C  CB  . VAL D  1 15  ? 175.650 146.365 65.799 1.00   25.77 ? 14   VAL D CB  1 
ATOM   3443  C  CG1 . VAL D  1 15  ? 175.586 147.356 64.659 1.00   24.78 ? 14   VAL D CG1 1 
ATOM   3444  C  CG2 . VAL D  1 15  ? 177.064 146.281 66.364 1.00   25.67 ? 14   VAL D CG2 1 
ATOM   3445  N  N   . GLN D  1 16  ? 172.773 148.198 66.307 1.00   26.81 ? 15   GLN D N   1 
ATOM   3446  C  CA  . GLN D  1 16  ? 171.477 148.509 65.765 1.00   27.78 ? 15   GLN D CA  1 
ATOM   3447  C  C   . GLN D  1 16  ? 171.428 149.921 65.230 1.00   26.96 ? 15   GLN D C   1 
ATOM   3448  O  O   . GLN D  1 16  ? 172.194 150.786 65.664 1.00   26.50 ? 15   GLN D O   1 
ATOM   3449  C  CB  . GLN D  1 16  ? 170.360 148.252 66.788 1.00   30.61 ? 15   GLN D CB  1 
ATOM   3450  C  CG  . GLN D  1 16  ? 170.483 148.948 68.123 1.00   34.05 ? 15   GLN D CG  1 
ATOM   3451  C  CD  . GLN D  1 16  ? 169.359 148.533 69.077 1.00   37.09 ? 15   GLN D CD  1 
ATOM   3452  O  OE1 . GLN D  1 16  ? 168.349 149.229 69.198 1.00   39.98 ? 15   GLN D OE1 1 
ATOM   3453  N  NE2 . GLN D  1 16  ? 169.520 147.384 69.730 1.00   37.55 ? 15   GLN D NE2 1 
ATOM   3454  N  N   . GLY D  1 17  ? 170.552 150.152 64.254 1.00   25.35 ? 16   GLY D N   1 
ATOM   3455  C  CA  . GLY D  1 17  ? 170.440 151.486 63.703 1.00   25.13 ? 16   GLY D CA  1 
ATOM   3456  C  C   . GLY D  1 17  ? 169.391 151.638 62.643 1.00   24.72 ? 16   GLY D C   1 
ATOM   3457  O  O   . GLY D  1 17  ? 168.714 150.682 62.259 1.00   23.83 ? 16   GLY D O   1 
ATOM   3458  N  N   . ILE D  1 18  ? 169.252 152.876 62.202 1.00   24.70 ? 17   ILE D N   1 
ATOM   3459  C  CA  . ILE D  1 18  ? 168.291 153.256 61.184 1.00   24.76 ? 17   ILE D CA  1 
ATOM   3460  C  C   . ILE D  1 18  ? 169.019 154.114 60.149 1.00   24.37 ? 17   ILE D C   1 
ATOM   3461  O  O   . ILE D  1 18  ? 169.607 155.129 60.502 1.00   25.32 ? 17   ILE D O   1 
ATOM   3462  C  CB  . ILE D  1 18  ? 167.126 154.042 61.812 1.00   25.17 ? 17   ILE D CB  1 
ATOM   3463  C  CG1 . ILE D  1 18  ? 166.341 153.123 62.747 1.00   25.85 ? 17   ILE D CG1 1 
ATOM   3464  C  CG2 . ILE D  1 18  ? 166.204 154.608 60.737 1.00   25.57 ? 17   ILE D CG2 1 
ATOM   3465  C  CD1 . ILE D  1 18  ? 165.251 153.811 63.542 1.00   26.71 ? 17   ILE D CD1 1 
ATOM   3466  N  N   . ILE D  1 19  ? 169.008 153.684 58.888 1.00   23.77 ? 18   ILE D N   1 
ATOM   3467  C  CA  . ILE D  1 19  ? 169.632 154.424 57.802 1.00   23.63 ? 18   ILE D CA  1 
ATOM   3468  C  C   . ILE D  1 19  ? 168.591 154.797 56.768 1.00   24.63 ? 18   ILE D C   1 
ATOM   3469  O  O   . ILE D  1 19  ? 167.797 153.951 56.334 1.00   23.75 ? 18   ILE D O   1 
ATOM   3470  C  CB  . ILE D  1 19  ? 170.748 153.613 57.145 1.00   23.34 ? 18   ILE D CB  1 
ATOM   3471  C  CG1 . ILE D  1 19  ? 171.811 153.247 58.186 1.00   22.91 ? 18   ILE D CG1 1 
ATOM   3472  C  CG2 . ILE D  1 19  ? 171.396 154.394 56.008 1.00   22.91 ? 18   ILE D CG2 1 
ATOM   3473  C  CD1 . ILE D  1 19  ? 172.605 154.447 58.659 1.00   23.45 ? 18   ILE D CD1 1 
ATOM   3474  N  N   . ASN D  1 20  ? 168.587 156.083 56.410 1.00   26.40 ? 19   ASN D N   1 
ATOM   3475  C  CA  . ASN D  1 20  ? 167.650 156.656 55.459 1.00   27.25 ? 19   ASN D CA  1 
ATOM   3476  C  C   . ASN D  1 20  ? 168.361 156.928 54.139 1.00   28.51 ? 19   ASN D C   1 
ATOM   3477  O  O   . ASN D  1 20  ? 169.558 157.229 54.133 1.00   28.30 ? 19   ASN D O   1 
ATOM   3478  C  CB  . ASN D  1 20  ? 167.104 157.974 55.991 1.00   28.54 ? 19   ASN D CB  1 
ATOM   3479  C  CG  . ASN D  1 20  ? 166.537 157.861 57.390 1.00   29.30 ? 19   ASN D CG  1 
ATOM   3480  O  OD1 . ASN D  1 20  ? 167.163 158.288 58.377 1.00   30.98 ? 19   ASN D OD1 1 
ATOM   3481  N  ND2 . ASN D  1 20  ? 165.349 157.308 57.491 1.00   28.82 ? 19   ASN D ND2 1 
ATOM   3482  N  N   . PHE D  1 21  ? 167.622 156.800 53.034 1.00   29.46 ? 20   PHE D N   1 
ATOM   3483  C  CA  . PHE D  1 21  ? 168.119 157.066 51.679 1.00   30.47 ? 20   PHE D CA  1 
ATOM   3484  C  C   . PHE D  1 21  ? 167.176 158.032 50.964 1.00   32.59 ? 20   PHE D C   1 
ATOM   3485  O  O   . PHE D  1 21  ? 165.953 157.937 51.096 1.00   32.92 ? 20   PHE D O   1 
ATOM   3486  C  CB  . PHE D  1 21  ? 168.169 155.792 50.830 1.00   29.71 ? 20   PHE D CB  1 
ATOM   3487  C  CG  . PHE D  1 21  ? 169.024 154.695 51.394 1.00   28.08 ? 20   PHE D CG  1 
ATOM   3488  C  CD1 . PHE D  1 21  ? 168.527 153.837 52.358 1.00   27.31 ? 20   PHE D CD1 1 
ATOM   3489  C  CD2 . PHE D  1 21  ? 170.292 154.473 50.903 1.00   27.94 ? 20   PHE D CD2 1 
ATOM   3490  C  CE1 . PHE D  1 21  ? 169.304 152.811 52.859 1.00   26.42 ? 20   PHE D CE1 1 
ATOM   3491  C  CE2 . PHE D  1 21  ? 171.073 153.444 51.396 1.00   27.56 ? 20   PHE D CE2 1 
ATOM   3492  C  CZ  . PHE D  1 21  ? 170.578 152.612 52.373 1.00   26.72 ? 20   PHE D CZ  1 
ATOM   3493  N  N   . GLU D  1 22  ? 167.734 158.937 50.180 1.00   35.59 ? 21   GLU D N   1 
ATOM   3494  C  CA  . GLU D  1 22  ? 166.921 159.876 49.414 1.00   39.29 ? 21   GLU D CA  1 
ATOM   3495  C  C   . GLU D  1 22  ? 167.567 160.142 48.056 1.00   41.08 ? 21   GLU D C   1 
ATOM   3496  O  O   . GLU D  1 22  ? 168.768 160.417 47.984 1.00   40.74 ? 21   GLU D O   1 
ATOM   3497  C  CB  . GLU D  1 22  ? 166.753 161.178 50.187 1.00   41.58 ? 21   GLU D CB  1 
ATOM   3498  C  CG  . GLU D  1 22  ? 165.581 162.021 49.716 1.00   44.39 ? 21   GLU D CG  1 
ATOM   3499  C  CD  . GLU D  1 22  ? 165.409 163.297 50.526 1.00   46.76 ? 21   GLU D CD  1 
ATOM   3500  O  OE1 . GLU D  1 22  ? 166.431 163.944 50.892 1.00   49.48 ? 21   GLU D OE1 1 
ATOM   3501  O  OE2 . GLU D  1 22  ? 164.248 163.662 50.788 1.00   48.18 ? 21   GLU D OE2 1 
ATOM   3502  N  N   . GLN D  1 23  ? 166.774 160.020 46.992 1.00   41.96 ? 22   GLN D N   1 
ATOM   3503  C  CA  . GLN D  1 23  ? 167.224 160.316 45.647 1.00   44.79 ? 22   GLN D CA  1 
ATOM   3504  C  C   . GLN D  1 23  ? 166.238 161.296 45.028 1.00   49.54 ? 22   GLN D C   1 
ATOM   3505  O  O   . GLN D  1 23  ? 165.173 160.891 44.545 1.00   48.77 ? 22   GLN D O   1 
ATOM   3506  C  CB  . GLN D  1 23  ? 167.308 159.042 44.818 1.00   43.56 ? 22   GLN D CB  1 
ATOM   3507  C  CG  . GLN D  1 23  ? 168.049 159.219 43.499 1.00   43.75 ? 22   GLN D CG  1 
ATOM   3508  C  CD  . GLN D  1 23  ? 168.363 157.885 42.843 1.00   43.00 ? 22   GLN D CD  1 
ATOM   3509  O  OE1 . GLN D  1 23  ? 167.606 156.920 42.980 1.00   41.93 ? 22   GLN D OE1 1 
ATOM   3510  N  NE2 . GLN D  1 23  ? 169.489 157.815 42.150 1.00   42.36 ? 22   GLN D NE2 1 
ATOM   3511  N  N   . LYS D  1 24  ? 166.590 162.583 45.083 1.00   54.77 ? 23   LYS D N   1 
ATOM   3512  C  CA  . LYS D  1 24  ? 165.699 163.671 44.640 1.00   60.07 ? 23   LYS D CA  1 
ATOM   3513  C  C   . LYS D  1 24  ? 165.360 163.580 43.154 1.00   62.69 ? 23   LYS D C   1 
ATOM   3514  O  O   . LYS D  1 24  ? 164.230 163.853 42.754 1.00   64.75 ? 23   LYS D O   1 
ATOM   3515  C  CB  . LYS D  1 24  ? 166.300 165.055 44.964 1.00   62.48 ? 23   LYS D CB  1 
ATOM   3516  C  CG  . LYS D  1 24  ? 167.636 165.358 44.279 1.00   65.87 ? 23   LYS D CG  1 
ATOM   3517  C  CD  . LYS D  1 24  ? 168.189 166.747 44.593 1.00   67.91 ? 23   LYS D CD  1 
ATOM   3518  C  CE  . LYS D  1 24  ? 168.925 166.783 45.929 1.00   68.40 ? 23   LYS D CE  1 
ATOM   3519  N  NZ  . LYS D  1 24  ? 170.113 165.878 45.991 1.00   66.25 ? 23   LYS D NZ  1 
ATOM   3520  N  N   . GLU D  1 25  ? 166.337 163.185 42.345 1.00   64.69 ? 24   GLU D N   1 
ATOM   3521  C  CA  . GLU D  1 25  ? 166.160 163.109 40.904 1.00   69.16 ? 24   GLU D CA  1 
ATOM   3522  C  C   . GLU D  1 25  ? 166.417 161.702 40.403 1.00   68.11 ? 24   GLU D C   1 
ATOM   3523  O  O   . GLU D  1 25  ? 167.353 161.043 40.835 1.00   65.97 ? 24   GLU D O   1 
ATOM   3524  C  CB  . GLU D  1 25  ? 167.099 164.098 40.210 1.00   73.69 ? 24   GLU D CB  1 
ATOM   3525  C  CG  . GLU D  1 25  ? 166.587 165.534 40.237 1.00   77.23 ? 24   GLU D CG  1 
ATOM   3526  C  CD  . GLU D  1 25  ? 167.676 166.536 40.563 1.00   79.21 ? 24   GLU D CD  1 
ATOM   3527  O  OE1 . GLU D  1 25  ? 168.759 166.458 39.948 1.00   80.85 ? 24   GLU D OE1 1 
ATOM   3528  O  OE2 . GLU D  1 25  ? 167.455 167.390 41.448 1.00   82.59 ? 24   GLU D OE2 1 
ATOM   3529  N  N   . SER D  1 26  ? 165.587 161.270 39.464 1.00   69.77 ? 25   SER D N   1 
ATOM   3530  C  CA  . SER D  1 26  ? 165.611 159.913 38.926 1.00   70.38 ? 25   SER D CA  1 
ATOM   3531  C  C   . SER D  1 26  ? 166.995 159.223 38.902 1.00   69.15 ? 25   SER D C   1 
ATOM   3532  O  O   . SER D  1 26  ? 167.153 158.130 39.444 1.00   72.45 ? 25   SER D O   1 
ATOM   3533  C  CB  . SER D  1 26  ? 164.987 159.940 37.529 1.00   72.78 ? 25   SER D CB  1 
ATOM   3534  O  OG  . SER D  1 26  ? 164.983 158.657 36.929 1.00   74.67 ? 25   SER D OG  1 
ATOM   3535  N  N   . ASN D  1 27  ? 167.979 159.868 38.288 1.00   68.61 ? 26   ASN D N   1 
ATOM   3536  C  CA  . ASN D  1 27  ? 169.338 159.316 38.141 1.00   68.08 ? 26   ASN D CA  1 
ATOM   3537  C  C   . ASN D  1 27  ? 170.341 159.861 39.164 1.00   65.19 ? 26   ASN D C   1 
ATOM   3538  O  O   . ASN D  1 27  ? 171.524 159.516 39.134 1.00   66.67 ? 26   ASN D O   1 
ATOM   3539  C  CB  . ASN D  1 27  ? 169.877 159.651 36.739 1.00   70.85 ? 26   ASN D CB  1 
ATOM   3540  C  CG  . ASN D  1 27  ? 169.847 161.153 36.436 1.00   73.83 ? 26   ASN D CG  1 
ATOM   3541  O  OD1 . ASN D  1 27  ? 169.055 161.901 37.021 1.00   74.21 ? 26   ASN D OD1 1 
ATOM   3542  N  ND2 . ASN D  1 27  ? 170.703 161.596 35.516 1.00   74.95 ? 26   ASN D ND2 1 
ATOM   3543  N  N   . GLY D  1 28  ? 169.882 160.734 40.051 1.00   60.81 ? 27   GLY D N   1 
ATOM   3544  C  CA  . GLY D  1 28  ? 170.787 161.594 40.790 1.00   59.03 ? 27   GLY D CA  1 
ATOM   3545  C  C   . GLY D  1 28  ? 171.536 160.933 41.931 1.00   55.17 ? 27   GLY D C   1 
ATOM   3546  O  O   . GLY D  1 28  ? 171.411 159.715 42.163 1.00   52.58 ? 27   GLY D O   1 
ATOM   3547  N  N   . PRO D  1 29  ? 172.329 161.739 42.658 1.00   53.35 ? 28   PRO D N   1 
ATOM   3548  C  CA  . PRO D  1 29  ? 172.981 161.281 43.884 1.00   50.14 ? 28   PRO D CA  1 
ATOM   3549  C  C   . PRO D  1 29  ? 171.966 160.810 44.926 1.00   48.10 ? 28   PRO D C   1 
ATOM   3550  O  O   . PRO D  1 29  ? 170.877 161.380 45.042 1.00   49.05 ? 28   PRO D O   1 
ATOM   3551  C  CB  . PRO D  1 29  ? 173.708 162.530 44.390 1.00   50.68 ? 28   PRO D CB  1 
ATOM   3552  C  CG  . PRO D  1 29  ? 173.873 163.399 43.189 1.00   53.55 ? 28   PRO D CG  1 
ATOM   3553  C  CD  . PRO D  1 29  ? 172.674 163.137 42.337 1.00   53.90 ? 28   PRO D CD  1 
ATOM   3554  N  N   . VAL D  1 30  ? 172.326 159.772 45.670 1.00   45.22 ? 29   VAL D N   1 
ATOM   3555  C  CA  . VAL D  1 30  ? 171.501 159.287 46.761 1.00   42.29 ? 29   VAL D CA  1 
ATOM   3556  C  C   . VAL D  1 30  ? 172.107 159.789 48.061 1.00   41.11 ? 29   VAL D C   1 
ATOM   3557  O  O   . VAL D  1 30  ? 173.259 159.482 48.371 1.00   40.94 ? 29   VAL D O   1 
ATOM   3558  C  CB  . VAL D  1 30  ? 171.450 157.750 46.782 1.00   40.97 ? 29   VAL D CB  1 
ATOM   3559  C  CG1 . VAL D  1 30  ? 170.466 157.272 47.841 1.00   39.00 ? 29   VAL D CG1 1 
ATOM   3560  C  CG2 . VAL D  1 30  ? 171.099 157.212 45.403 1.00   39.74 ? 29   VAL D CG2 1 
ATOM   3561  N  N   . LYS D  1 31  ? 171.349 160.590 48.803 1.00   40.80 ? 30   LYS D N   1 
ATOM   3562  C  CA  . LYS D  1 31  ? 171.709 160.926 50.175 1.00   40.55 ? 30   LYS D CA  1 
ATOM   3563  C  C   . LYS D  1 31  ? 171.511 159.672 51.039 1.00   37.42 ? 30   LYS D C   1 
ATOM   3564  O  O   . LYS D  1 31  ? 170.464 159.028 50.973 1.00   36.22 ? 30   LYS D O   1 
ATOM   3565  C  CB  . LYS D  1 31  ? 170.828 162.061 50.704 1.00   43.68 ? 30   LYS D CB  1 
ATOM   3566  C  CG  . LYS D  1 31  ? 171.200 163.436 50.177 1.00   48.69 ? 30   LYS D CG  1 
ATOM   3567  C  CD  . LYS D  1 31  ? 170.152 164.484 50.538 1.00   52.45 ? 30   LYS D CD  1 
ATOM   3568  C  CE  . LYS D  1 31  ? 170.646 165.901 50.231 1.00   56.03 ? 30   LYS D CE  1 
ATOM   3569  N  NZ  . LYS D  1 31  ? 169.521 166.878 50.125 1.00   57.80 ? 30   LYS D NZ  1 
ATOM   3570  N  N   . VAL D  1 32  ? 172.521 159.325 51.827 1.00   35.27 ? 31   VAL D N   1 
ATOM   3571  C  CA  . VAL D  1 32  ? 172.438 158.227 52.791 1.00   32.94 ? 31   VAL D CA  1 
ATOM   3572  C  C   . VAL D  1 32  ? 172.766 158.759 54.176 1.00   32.70 ? 31   VAL D C   1 
ATOM   3573  O  O   . VAL D  1 32  ? 173.862 159.287 54.405 1.00   32.21 ? 31   VAL D O   1 
ATOM   3574  C  CB  . VAL D  1 32  ? 173.435 157.122 52.447 1.00   32.36 ? 31   VAL D CB  1 
ATOM   3575  C  CG1 . VAL D  1 32  ? 173.370 156.002 53.490 1.00   31.93 ? 31   VAL D CG1 1 
ATOM   3576  C  CG2 . VAL D  1 32  ? 173.191 156.605 51.038 1.00   32.17 ? 31   VAL D CG2 1 
ATOM   3577  N  N   . TRP D  1 33  ? 171.835 158.633 55.115 1.00   32.74 ? 32   TRP D N   1 
ATOM   3578  C  CA  . TRP D  1 33  ? 172.093 159.137 56.467 1.00   32.13 ? 32   TRP D CA  1 
ATOM   3579  C  C   . TRP D  1 33  ? 171.300 158.475 57.550 1.00   31.50 ? 32   TRP D C   1 
ATOM   3580  O  O   . TRP D  1 33  ? 170.202 157.956 57.326 1.00   31.38 ? 32   TRP D O   1 
ATOM   3581  C  CB  . TRP D  1 33  ? 171.849 160.643 56.543 1.00   32.97 ? 32   TRP D CB  1 
ATOM   3582  C  CG  . TRP D  1 33  ? 170.386 161.009 56.680 1.00   33.77 ? 32   TRP D CG  1 
ATOM   3583  C  CD1 . TRP D  1 33  ? 169.690 161.368 57.838 1.00   33.81 ? 32   TRP D CD1 1 
ATOM   3584  C  CD2 . TRP D  1 33  ? 169.389 161.040 55.613 1.00   33.99 ? 32   TRP D CD2 1 
ATOM   3585  N  NE1 . TRP D  1 33  ? 168.367 161.608 57.559 1.00   34.66 ? 32   TRP D NE1 1 
ATOM   3586  C  CE2 . TRP D  1 33  ? 168.122 161.434 56.242 1.00   34.55 ? 32   TRP D CE2 1 
ATOM   3587  C  CE3 . TRP D  1 33  ? 169.423 160.806 54.250 1.00   34.31 ? 32   TRP D CE3 1 
ATOM   3588  C  CZ2 . TRP D  1 33  ? 166.964 161.582 55.514 1.00   34.93 ? 32   TRP D CZ2 1 
ATOM   3589  C  CZ3 . TRP D  1 33  ? 168.250 160.947 53.525 1.00   34.71 ? 32   TRP D CZ3 1 
ATOM   3590  C  CH2 . TRP D  1 33  ? 167.044 161.325 54.142 1.00   35.27 ? 32   TRP D CH2 1 
ATOM   3591  N  N   . GLY D  1 34  ? 171.869 158.510 58.752 1.00   31.27 ? 33   GLY D N   1 
ATOM   3592  C  CA  . GLY D  1 34  ? 171.192 158.034 59.939 1.00   31.43 ? 33   GLY D CA  1 
ATOM   3593  C  C   . GLY D  1 34  ? 172.172 157.785 61.060 1.00   30.85 ? 33   GLY D C   1 
ATOM   3594  O  O   . GLY D  1 34  ? 173.160 158.497 61.211 1.00   32.08 ? 33   GLY D O   1 
ATOM   3595  N  N   . SER D  1 35  ? 171.914 156.757 61.839 1.00   29.48 ? 34   SER D N   1 
ATOM   3596  C  CA  . SER D  1 35  ? 172.749 156.472 62.986 1.00   29.47 ? 34   SER D CA  1 
ATOM   3597  C  C   . SER D  1 35  ? 172.815 154.983 63.267 1.00   27.64 ? 34   SER D C   1 
ATOM   3598  O  O   . SER D  1 35  ? 171.848 154.264 63.027 1.00   25.96 ? 34   SER D O   1 
ATOM   3599  C  CB  . SER D  1 35  ? 172.191 157.185 64.215 1.00   30.88 ? 34   SER D CB  1 
ATOM   3600  O  OG  . SER D  1 35  ? 173.190 157.218 65.217 1.00   33.30 ? 34   SER D OG  1 
ATOM   3601  N  N   . ILE D  1 36  ? 173.974 154.546 63.761 1.00   27.19 ? 35   ILE D N   1 
ATOM   3602  C  CA  . ILE D  1 36  ? 174.205 153.172 64.194 1.00   26.45 ? 35   ILE D CA  1 
ATOM   3603  C  C   . ILE D  1 36  ? 174.883 153.221 65.557 1.00   26.78 ? 35   ILE D C   1 
ATOM   3604  O  O   . ILE D  1 36  ? 175.869 153.928 65.713 1.00   26.99 ? 35   ILE D O   1 
ATOM   3605  C  CB  . ILE D  1 36  ? 175.141 152.411 63.227 1.00   25.62 ? 35   ILE D CB  1 
ATOM   3606  C  CG1 . ILE D  1 36  ? 174.672 152.588 61.780 1.00   25.23 ? 35   ILE D CG1 1 
ATOM   3607  C  CG2 . ILE D  1 36  ? 175.228 150.933 63.632 1.00   24.66 ? 35   ILE D CG2 1 
ATOM   3608  C  CD1 . ILE D  1 36  ? 175.561 151.934 60.754 1.00   25.00 ? 35   ILE D CD1 1 
ATOM   3609  N  N   . LYS D  1 37  ? 174.363 152.456 66.517 1.00   26.86 ? 36   LYS D N   1 
ATOM   3610  C  CA  . LYS D  1 37  ? 174.943 152.340 67.856 1.00   27.15 ? 36   LYS D CA  1 
ATOM   3611  C  C   . LYS D  1 37  ? 175.337 150.885 68.146 1.00   26.02 ? 36   LYS D C   1 
ATOM   3612  O  O   . LYS D  1 37  ? 174.971 149.984 67.389 1.00   24.41 ? 36   LYS D O   1 
ATOM   3613  C  CB  . LYS D  1 37  ? 173.973 152.875 68.916 1.00   28.73 ? 36   LYS D CB  1 
ATOM   3614  C  CG  . LYS D  1 37  ? 172.624 152.171 68.980 1.00   30.34 ? 36   LYS D CG  1 
ATOM   3615  C  CD  . LYS D  1 37  ? 171.755 152.700 70.124 1.00   32.34 ? 36   LYS D CD  1 
ATOM   3616  C  CE  . LYS D  1 37  ? 170.455 151.908 70.246 1.00   33.03 ? 36   LYS D CE  1 
ATOM   3617  N  NZ  . LYS D  1 37  ? 169.393 152.674 70.956 1.00   34.67 ? 36   LYS D NZ  1 
ATOM   3618  N  N   . GLY D  1 38  ? 176.073 150.682 69.242 1.00   25.62 ? 37   GLY D N   1 
ATOM   3619  C  CA  . GLY D  1 38  ? 176.634 149.383 69.635 1.00   25.89 ? 37   GLY D CA  1 
ATOM   3620  C  C   . GLY D  1 38  ? 177.911 148.956 68.927 1.00   25.85 ? 37   GLY D C   1 
ATOM   3621  O  O   . GLY D  1 38  ? 178.290 147.784 68.977 1.00   26.44 ? 37   GLY D O   1 
ATOM   3622  N  N   . LEU D  1 39  ? 178.583 149.886 68.254 1.00   25.98 ? 38   LEU D N   1 
ATOM   3623  C  CA  . LEU D  1 39  ? 179.824 149.566 67.535 1.00   26.28 ? 38   LEU D CA  1 
ATOM   3624  C  C   . LEU D  1 39  ? 181.044 149.832 68.398 1.00   27.64 ? 38   LEU D C   1 
ATOM   3625  O  O   . LEU D  1 39  ? 180.971 150.582 69.360 1.00   28.75 ? 38   LEU D O   1 
ATOM   3626  C  CB  . LEU D  1 39  ? 179.944 150.410 66.267 1.00   24.89 ? 38   LEU D CB  1 
ATOM   3627  C  CG  . LEU D  1 39  ? 178.884 150.122 65.210 1.00   24.12 ? 38   LEU D CG  1 
ATOM   3628  C  CD1 . LEU D  1 39  ? 178.841 151.238 64.177 1.00   23.18 ? 38   LEU D CD1 1 
ATOM   3629  C  CD2 . LEU D  1 39  ? 179.127 148.752 64.583 1.00   23.58 ? 38   LEU D CD2 1 
ATOM   3630  N  N   . THR D  1 40  ? 182.170 149.219 68.052 1.00   28.31 ? 39   THR D N   1 
ATOM   3631  C  CA  . THR D  1 40  ? 183.437 149.565 68.689 1.00   29.57 ? 39   THR D CA  1 
ATOM   3632  C  C   . THR D  1 40  ? 183.914 150.891 68.076 1.00   29.81 ? 39   THR D C   1 
ATOM   3633  O  O   . THR D  1 40  ? 183.699 151.143 66.878 1.00   29.09 ? 39   THR D O   1 
ATOM   3634  C  CB  . THR D  1 40  ? 184.506 148.486 68.448 1.00   30.18 ? 39   THR D CB  1 
ATOM   3635  O  OG1 . THR D  1 40  ? 184.657 148.301 67.033 1.00   29.55 ? 39   THR D OG1 1 
ATOM   3636  C  CG2 . THR D  1 40  ? 184.131 147.147 69.128 1.00   30.26 ? 39   THR D CG2 1 
ATOM   3637  N  N   . GLU D  1 41  ? 184.542 151.737 68.892 1.00   30.16 ? 40   GLU D N   1 
ATOM   3638  C  CA  . GLU D  1 41  ? 185.064 153.010 68.432 1.00   30.89 ? 40   GLU D CA  1 
ATOM   3639  C  C   . GLU D  1 41  ? 185.980 152.698 67.283 1.00   31.26 ? 40   GLU D C   1 
ATOM   3640  O  O   . GLU D  1 41  ? 186.818 151.801 67.406 1.00   32.39 ? 40   GLU D O   1 
ATOM   3641  C  CB  . GLU D  1 41  ? 185.860 153.719 69.533 1.00   32.90 ? 40   GLU D CB  1 
ATOM   3642  C  CG  . GLU D  1 41  ? 186.429 155.064 69.116 1.00   33.89 ? 40   GLU D CG  1 
ATOM   3643  C  CD  . GLU D  1 41  ? 187.331 155.680 70.158 1.00   36.11 ? 40   GLU D CD  1 
ATOM   3644  O  OE1 . GLU D  1 41  ? 187.752 154.961 71.076 1.00   36.62 ? 40   GLU D OE1 1 
ATOM   3645  O  OE2 . GLU D  1 41  ? 187.633 156.889 70.053 1.00   39.28 ? 40   GLU D OE2 1 
ATOM   3646  N  N   . GLY D  1 42  ? 185.792 153.411 66.170 1.00   30.56 ? 41   GLY D N   1 
ATOM   3647  C  CA  . GLY D  1 42  ? 186.626 153.278 64.987 1.00   30.44 ? 41   GLY D CA  1 
ATOM   3648  C  C   . GLY D  1 42  ? 185.841 153.051 63.696 1.00   30.47 ? 41   GLY D C   1 
ATOM   3649  O  O   . GLY D  1 42  ? 184.621 153.268 63.619 1.00   28.59 ? 41   GLY D O   1 
ATOM   3650  N  N   . LEU D  1 43  ? 186.581 152.570 62.699 1.00   31.14 ? 42   LEU D N   1 
ATOM   3651  C  CA  . LEU D  1 43  ? 186.113 152.357 61.335 1.00   30.99 ? 42   LEU D CA  1 
ATOM   3652  C  C   . LEU D  1 43  ? 185.354 151.035 61.182 1.00   29.31 ? 42   LEU D C   1 
ATOM   3653  O  O   . LEU D  1 43  ? 185.817 150.003 61.640 1.00   28.05 ? 42   LEU D O   1 
ATOM   3654  C  CB  . LEU D  1 43  ? 187.319 152.321 60.381 1.00   32.59 ? 42   LEU D CB  1 
ATOM   3655  C  CG  . LEU D  1 43  ? 187.788 153.613 59.717 1.00   34.98 ? 42   LEU D CG  1 
ATOM   3656  C  CD1 . LEU D  1 43  ? 187.423 154.842 60.535 1.00   35.85 ? 42   LEU D CD1 1 
ATOM   3657  C  CD2 . LEU D  1 43  ? 189.293 153.525 59.478 1.00   36.23 ? 42   LEU D CD2 1 
ATOM   3658  N  N   . HIS D  1 44  ? 184.233 151.075 60.464 1.00   28.00 ? 43   HIS D N   1 
ATOM   3659  C  CA  . HIS D  1 44  ? 183.452 149.868 60.176 1.00   27.41 ? 43   HIS D CA  1 
ATOM   3660  C  C   . HIS D  1 44  ? 182.966 149.862 58.756 1.00   26.26 ? 43   HIS D C   1 
ATOM   3661  O  O   . HIS D  1 44  ? 182.341 150.826 58.318 1.00   26.11 ? 43   HIS D O   1 
ATOM   3662  C  CB  . HIS D  1 44  ? 182.264 149.767 61.134 1.00   26.75 ? 43   HIS D CB  1 
ATOM   3663  C  CG  . HIS D  1 44  ? 182.665 149.508 62.562 1.00   26.91 ? 43   HIS D CG  1 
ATOM   3664  N  ND1 . HIS D  1 44  ? 182.973 148.267 63.023 1.00   27.15 ? 43   HIS D ND1 1 
ATOM   3665  C  CD2 . HIS D  1 44  ? 182.816 150.378 63.642 1.00   27.37 ? 43   HIS D CD2 1 
ATOM   3666  C  CE1 . HIS D  1 44  ? 183.302 148.348 64.329 1.00   27.52 ? 43   HIS D CE1 1 
ATOM   3667  N  NE2 . HIS D  1 44  ? 183.214 149.640 64.707 1.00   27.08 ? 43   HIS D NE2 1 
ATOM   3668  N  N   . GLY D  1 45  ? 183.252 148.782 58.030 1.00   25.89 ? 44   GLY D N   1 
ATOM   3669  C  CA  . GLY D  1 45  ? 182.817 148.626 56.646 1.00   26.08 ? 44   GLY D CA  1 
ATOM   3670  C  C   . GLY D  1 45  ? 181.301 148.726 56.516 1.00   25.83 ? 44   GLY D C   1 
ATOM   3671  O  O   . GLY D  1 45  ? 180.557 148.301 57.409 1.00   24.97 ? 44   GLY D O   1 
ATOM   3672  N  N   . PHE D  1 46  ? 180.862 149.286 55.392 1.00   25.97 ? 45   PHE D N   1 
ATOM   3673  C  CA  . PHE D  1 46  ? 179.485 149.690 55.166 1.00   25.88 ? 45   PHE D CA  1 
ATOM   3674  C  C   . PHE D  1 46  ? 179.161 149.415 53.695 1.00   26.86 ? 45   PHE D C   1 
ATOM   3675  O  O   . PHE D  1 46  ? 179.713 150.073 52.786 1.00   26.48 ? 45   PHE D O   1 
ATOM   3676  C  CB  . PHE D  1 46  ? 179.386 151.172 55.499 1.00   26.18 ? 45   PHE D CB  1 
ATOM   3677  C  CG  . PHE D  1 46  ? 178.004 151.694 55.612 1.00   26.32 ? 45   PHE D CG  1 
ATOM   3678  C  CD1 . PHE D  1 46  ? 177.112 151.157 56.528 1.00   26.09 ? 45   PHE D CD1 1 
ATOM   3679  C  CD2 . PHE D  1 46  ? 177.610 152.783 54.859 1.00   26.52 ? 45   PHE D CD2 1 
ATOM   3680  C  CE1 . PHE D  1 46  ? 175.835 151.675 56.648 1.00   25.93 ? 45   PHE D CE1 1 
ATOM   3681  C  CE2 . PHE D  1 46  ? 176.338 153.296 54.971 1.00   26.85 ? 45   PHE D CE2 1 
ATOM   3682  C  CZ  . PHE D  1 46  ? 175.447 152.745 55.871 1.00   26.55 ? 45   PHE D CZ  1 
ATOM   3683  N  N   . HIS D  1 47  ? 178.302 148.412 53.457 1.00   26.52 ? 46   HIS D N   1 
ATOM   3684  C  CA  . HIS D  1 47  ? 178.047 147.919 52.103 1.00   26.68 ? 46   HIS D CA  1 
ATOM   3685  C  C   . HIS D  1 47  ? 176.629 147.534 51.836 1.00   25.24 ? 46   HIS D C   1 
ATOM   3686  O  O   . HIS D  1 47  ? 175.916 147.063 52.728 1.00   24.25 ? 46   HIS D O   1 
ATOM   3687  C  CB  . HIS D  1 47  ? 178.827 146.648 51.817 1.00   28.32 ? 46   HIS D CB  1 
ATOM   3688  C  CG  . HIS D  1 47  ? 180.249 146.674 52.237 1.00   29.96 ? 46   HIS D CG  1 
ATOM   3689  N  ND1 . HIS D  1 47  ? 180.783 145.694 52.983 1.00   31.28 ? 46   HIS D ND1 1 
ATOM   3690  C  CD2 . HIS D  1 47  ? 181.272 147.557 51.948 1.00   31.60 ? 46   HIS D CD2 1 
ATOM   3691  C  CE1 . HIS D  1 47  ? 182.081 145.955 53.186 1.00   31.93 ? 46   HIS D CE1 1 
ATOM   3692  N  NE2 . HIS D  1 47  ? 182.381 147.092 52.541 1.00   32.25 ? 46   HIS D NE2 1 
ATOM   3693  N  N   . VAL D  1 48  ? 176.219 147.670 50.580 1.00   24.62 ? 47   VAL D N   1 
ATOM   3694  C  CA  . VAL D  1 48  ? 174.997 147.026 50.130 1.00   24.06 ? 47   VAL D CA  1 
ATOM   3695  C  C   . VAL D  1 48  ? 175.362 145.668 49.544 1.00   24.69 ? 47   VAL D C   1 
ATOM   3696  O  O   . VAL D  1 48  ? 176.108 145.587 48.565 1.00   26.66 ? 47   VAL D O   1 
ATOM   3697  C  CB  . VAL D  1 48  ? 174.266 147.881 49.117 1.00   24.20 ? 47   VAL D CB  1 
ATOM   3698  C  CG1 . VAL D  1 48  ? 173.024 147.166 48.608 1.00   24.55 ? 47   VAL D CG1 1 
ATOM   3699  C  CG2 . VAL D  1 48  ? 173.927 149.226 49.726 1.00   24.03 ? 47   VAL D CG2 1 
ATOM   3700  N  N   . HIS D  1 49  ? 174.891 144.598 50.176 1.00   24.21 ? 48   HIS D N   1 
ATOM   3701  C  CA  . HIS D  1 49  ? 175.053 143.269 49.633 1.00   24.51 ? 48   HIS D CA  1 
ATOM   3702  C  C   . HIS D  1 49  ? 173.875 142.922 48.748 1.00   25.09 ? 48   HIS D C   1 
ATOM   3703  O  O   . HIS D  1 49  ? 172.796 143.514 48.844 1.00   24.03 ? 48   HIS D O   1 
ATOM   3704  C  CB  . HIS D  1 49  ? 175.185 142.256 50.754 1.00   24.31 ? 48   HIS D CB  1 
ATOM   3705  C  CG  . HIS D  1 49  ? 176.488 142.317 51.482 1.00   24.36 ? 48   HIS D CG  1 
ATOM   3706  N  ND1 . HIS D  1 49  ? 177.277 141.246 51.624 1.00   25.15 ? 48   HIS D ND1 1 
ATOM   3707  C  CD2 . HIS D  1 49  ? 177.140 143.372 52.109 1.00   24.60 ? 48   HIS D CD2 1 
ATOM   3708  C  CE1 . HIS D  1 49  ? 178.373 141.580 52.322 1.00   25.19 ? 48   HIS D CE1 1 
ATOM   3709  N  NE2 . HIS D  1 49  ? 178.291 142.883 52.624 1.00   24.99 ? 48   HIS D NE2 1 
ATOM   3710  N  N   . GLU D  1 50  ? 174.055 141.915 47.901 1.00   26.07 ? 49   GLU D N   1 
ATOM   3711  C  CA  . GLU D  1 50  ? 173.175 141.723 46.755 1.00   26.45 ? 49   GLU D CA  1 
ATOM   3712  C  C   . GLU D  1 50  ? 171.741 141.324 47.099 1.00   25.40 ? 49   GLU D C   1 
ATOM   3713  O  O   . GLU D  1 50  ? 170.803 141.830 46.489 1.00   25.48 ? 49   GLU D O   1 
ATOM   3714  C  CB  . GLU D  1 50  ? 173.759 140.677 45.806 1.00   27.58 ? 49   GLU D CB  1 
ATOM   3715  C  CG  . GLU D  1 50  ? 172.936 140.523 44.546 1.00   28.56 ? 49   GLU D CG  1 
ATOM   3716  C  CD  . GLU D  1 50  ? 173.546 139.582 43.527 1.00   30.04 ? 49   GLU D CD  1 
ATOM   3717  O  OE1 . GLU D  1 50  ? 174.624 139.002 43.780 1.00   30.54 ? 49   GLU D OE1 1 
ATOM   3718  O  OE2 . GLU D  1 50  ? 172.909 139.420 42.469 1.00   31.05 ? 49   GLU D OE2 1 
ATOM   3719  N  N   . PHE D  1 51  ? 171.581 140.403 48.042 1.00   24.63 ? 50   PHE D N   1 
ATOM   3720  C  CA  . PHE D  1 51  ? 170.284 139.803 48.308 1.00   24.80 ? 50   PHE D CA  1 
ATOM   3721  C  C   . PHE D  1 51  ? 169.656 140.310 49.604 1.00   23.42 ? 50   PHE D C   1 
ATOM   3722  O  O   . PHE D  1 51  ? 170.320 140.402 50.636 1.00   23.79 ? 50   PHE D O   1 
ATOM   3723  C  CB  . PHE D  1 51  ? 170.454 138.284 48.357 1.00   26.60 ? 50   PHE D CB  1 
ATOM   3724  C  CG  . PHE D  1 51  ? 171.092 137.715 47.112 1.00   28.48 ? 50   PHE D CG  1 
ATOM   3725  C  CD1 . PHE D  1 51  ? 170.439 137.790 45.888 1.00   29.75 ? 50   PHE D CD1 1 
ATOM   3726  C  CD2 . PHE D  1 51  ? 172.348 137.127 47.161 1.00   30.12 ? 50   PHE D CD2 1 
ATOM   3727  C  CE1 . PHE D  1 51  ? 171.029 137.276 44.735 1.00   31.16 ? 50   PHE D CE1 1 
ATOM   3728  C  CE2 . PHE D  1 51  ? 172.945 136.611 46.023 1.00   31.34 ? 50   PHE D CE2 1 
ATOM   3729  C  CZ  . PHE D  1 51  ? 172.282 136.689 44.808 1.00   31.79 ? 50   PHE D CZ  1 
ATOM   3730  N  N   . GLY D  1 52  ? 168.370 140.617 49.545 1.00   22.38 ? 51   GLY D N   1 
ATOM   3731  C  CA  . GLY D  1 52  ? 167.599 141.018 50.711 1.00   21.69 ? 51   GLY D CA  1 
ATOM   3732  C  C   . GLY D  1 52  ? 167.064 139.789 51.410 1.00   21.56 ? 51   GLY D C   1 
ATOM   3733  O  O   . GLY D  1 52  ? 165.871 139.665 51.621 1.00   21.35 ? 51   GLY D O   1 
ATOM   3734  N  N   . ASP D  1 53  ? 167.964 138.877 51.755 1.00   21.89 ? 52   ASP D N   1 
ATOM   3735  C  CA  . ASP D  1 53  ? 167.619 137.569 52.269 1.00   22.06 ? 52   ASP D CA  1 
ATOM   3736  C  C   . ASP D  1 53  ? 168.255 137.474 53.643 1.00   22.54 ? 52   ASP D C   1 
ATOM   3737  O  O   . ASP D  1 53  ? 169.471 137.354 53.748 1.00   22.12 ? 52   ASP D O   1 
ATOM   3738  C  CB  . ASP D  1 53  ? 168.152 136.476 51.336 1.00   22.62 ? 52   ASP D CB  1 
ATOM   3739  C  CG  . ASP D  1 53  ? 167.842 135.068 51.819 1.00   23.18 ? 52   ASP D CG  1 
ATOM   3740  O  OD1 . ASP D  1 53  ? 167.589 134.887 53.025 1.00   23.09 ? 52   ASP D OD1 1 
ATOM   3741  O  OD2 . ASP D  1 53  ? 167.874 134.125 50.985 1.00   24.36 ? 52   ASP D OD2 1 
ATOM   3742  N  N   . ASN D  1 54  ? 167.411 137.536 54.675 1.00   22.97 ? 53   ASN D N   1 
ATOM   3743  C  CA  . ASN D  1 54  ? 167.841 137.500 56.061 1.00   24.29 ? 53   ASN D CA  1 
ATOM   3744  C  C   . ASN D  1 54  ? 167.487 136.177 56.745 1.00   24.00 ? 53   ASN D C   1 
ATOM   3745  O  O   . ASN D  1 54  ? 167.447 136.128 57.967 1.00   24.17 ? 53   ASN D O   1 
ATOM   3746  C  CB  . ASN D  1 54  ? 167.152 138.638 56.809 1.00   26.43 ? 53   ASN D CB  1 
ATOM   3747  C  CG  . ASN D  1 54  ? 167.664 138.821 58.222 1.00   28.41 ? 53   ASN D CG  1 
ATOM   3748  O  OD1 . ASN D  1 54  ? 166.882 138.774 59.193 1.00   32.21 ? 53   ASN D OD1 1 
ATOM   3749  N  ND2 . ASN D  1 54  ? 168.964 139.020 58.357 1.00   28.15 ? 53   ASN D ND2 1 
ATOM   3750  N  N   . THR D  1 55  ? 167.236 135.117 55.967 1.00   23.28 ? 54   THR D N   1 
ATOM   3751  C  CA  . THR D  1 55  ? 166.805 133.849 56.529 1.00   23.81 ? 54   THR D CA  1 
ATOM   3752  C  C   . THR D  1 55  ? 167.874 133.243 57.435 1.00   25.52 ? 54   THR D C   1 
ATOM   3753  O  O   . THR D  1 55  ? 167.542 132.592 58.422 1.00   26.99 ? 54   THR D O   1 
ATOM   3754  C  CB  . THR D  1 55  ? 166.395 132.832 55.439 1.00   23.57 ? 54   THR D CB  1 
ATOM   3755  O  OG1 . THR D  1 55  ? 167.467 132.642 54.523 1.00   23.18 ? 54   THR D OG1 1 
ATOM   3756  C  CG2 . THR D  1 55  ? 165.168 133.310 54.664 1.00   22.45 ? 54   THR D CG2 1 
ATOM   3757  N  N   . ALA D  1 56  ? 169.151 133.456 57.104 1.00   25.79 ? 55   ALA D N   1 
ATOM   3758  C  CA  . ALA D  1 56  ? 170.262 132.987 57.932 1.00   26.83 ? 55   ALA D CA  1 
ATOM   3759  C  C   . ALA D  1 56  ? 170.990 134.205 58.499 1.00   26.70 ? 55   ALA D C   1 
ATOM   3760  O  O   . ALA D  1 56  ? 172.202 134.279 58.481 1.00   28.34 ? 55   ALA D O   1 
ATOM   3761  C  CB  . ALA D  1 56  ? 171.204 132.109 57.122 1.00   26.97 ? 55   ALA D CB  1 
ATOM   3762  N  N   . GLY D  1 57  ? 170.232 135.184 58.981 1.00   26.68 ? 56   GLY D N   1 
ATOM   3763  C  CA  . GLY D  1 57  ? 170.824 136.433 59.441 1.00   26.18 ? 56   GLY D CA  1 
ATOM   3764  C  C   . GLY D  1 57  ? 171.545 137.118 58.294 1.00   26.09 ? 56   GLY D C   1 
ATOM   3765  O  O   . GLY D  1 57  ? 171.132 136.995 57.136 1.00   24.87 ? 56   GLY D O   1 
ATOM   3766  N  N   . CYS D  1 58  ? 172.623 137.837 58.619 1.00   26.15 ? 57   CYS D N   1 
ATOM   3767  C  CA  . CYS D  1 58  ? 173.366 138.622 57.632 1.00   26.22 ? 57   CYS D CA  1 
ATOM   3768  C  C   . CYS D  1 58  ? 174.183 137.786 56.621 1.00   26.97 ? 57   CYS D C   1 
ATOM   3769  O  O   . CYS D  1 58  ? 174.545 138.282 55.552 1.00   26.46 ? 57   CYS D O   1 
ATOM   3770  C  CB  . CYS D  1 58  ? 174.270 139.609 58.369 1.00   27.14 ? 57   CYS D CB  1 
ATOM   3771  S  SG  . CYS D  1 58  ? 173.365 140.722 59.467 1.00   27.27 ? 57   CYS D SG  1 
ATOM   3772  N  N   . THR D  1 59  ? 174.445 136.520 56.939 1.00   27.99 ? 58   THR D N   1 
ATOM   3773  C  CA  . THR D  1 59  ? 175.195 135.624 56.049 1.00   29.45 ? 58   THR D CA  1 
ATOM   3774  C  C   . THR D  1 59  ? 174.502 135.312 54.706 1.00   29.33 ? 58   THR D C   1 
ATOM   3775  O  O   . THR D  1 59  ? 175.173 135.101 53.682 1.00   32.53 ? 58   THR D O   1 
ATOM   3776  C  CB  . THR D  1 59  ? 175.505 134.299 56.777 1.00   31.72 ? 58   THR D CB  1 
ATOM   3777  O  OG1 . THR D  1 59  ? 176.309 134.577 57.941 1.00   32.22 ? 58   THR D OG1 1 
ATOM   3778  C  CG2 . THR D  1 59  ? 176.281 133.321 55.850 1.00   33.27 ? 58   THR D CG2 1 
ATOM   3779  N  N   . SER D  1 60  ? 173.174 135.298 54.695 1.00   27.28 ? 59   SER D N   1 
ATOM   3780  C  CA  . SER D  1 60  ? 172.429 134.941 53.486 1.00   27.07 ? 59   SER D CA  1 
ATOM   3781  C  C   . SER D  1 60  ? 172.221 136.148 52.557 1.00   26.24 ? 59   SER D C   1 
ATOM   3782  O  O   . SER D  1 60  ? 171.659 136.001 51.491 1.00   26.57 ? 59   SER D O   1 
ATOM   3783  C  CB  . SER D  1 60  ? 171.095 134.269 53.856 1.00   26.61 ? 59   SER D CB  1 
ATOM   3784  O  OG  . SER D  1 60  ? 170.390 135.019 54.830 1.00   25.78 ? 59   SER D OG  1 
ATOM   3785  N  N   . ALA D  1 61  ? 172.700 137.327 52.948 1.00   25.52 ? 60   ALA D N   1 
ATOM   3786  C  CA  . ALA D  1 61  ? 172.706 138.485 52.060 1.00   26.04 ? 60   ALA D CA  1 
ATOM   3787  C  C   . ALA D  1 61  ? 173.668 138.353 50.844 1.00   26.98 ? 60   ALA D C   1 
ATOM   3788  O  O   . ALA D  1 61  ? 173.628 139.149 49.917 1.00   26.69 ? 60   ALA D O   1 
ATOM   3789  C  CB  . ALA D  1 61  ? 173.020 139.735 52.863 1.00   25.45 ? 60   ALA D CB  1 
ATOM   3790  N  N   . GLY D  1 62  ? 174.532 137.347 50.847 1.00   28.90 ? 61   GLY D N   1 
ATOM   3791  C  CA  . GLY D  1 62  ? 175.468 137.142 49.742 1.00   29.91 ? 61   GLY D CA  1 
ATOM   3792  C  C   . GLY D  1 62  ? 176.553 138.197 49.616 1.00   30.39 ? 61   GLY D C   1 
ATOM   3793  O  O   . GLY D  1 62  ? 176.849 138.930 50.575 1.00   28.85 ? 61   GLY D O   1 
ATOM   3794  N  N   . PRO D  1 63  ? 177.169 138.286 48.419 1.00   31.10 ? 62   PRO D N   1 
ATOM   3795  C  CA  . PRO D  1 63  ? 178.322 139.158 48.302 1.00   31.69 ? 62   PRO D CA  1 
ATOM   3796  C  C   . PRO D  1 63  ? 177.912 140.601 48.074 1.00   31.04 ? 62   PRO D C   1 
ATOM   3797  O  O   . PRO D  1 63  ? 176.727 140.902 47.977 1.00   29.65 ? 62   PRO D O   1 
ATOM   3798  C  CB  . PRO D  1 63  ? 179.026 138.613 47.064 1.00   32.91 ? 62   PRO D CB  1 
ATOM   3799  C  CG  . PRO D  1 63  ? 177.885 138.197 46.186 1.00   32.95 ? 62   PRO D CG  1 
ATOM   3800  C  CD  . PRO D  1 63  ? 176.829 137.671 47.124 1.00   31.84 ? 62   PRO D CD  1 
ATOM   3801  N  N   . HIS D  1 64  ? 178.908 141.467 47.944 1.00   31.13 ? 63   HIS D N   1 
ATOM   3802  C  CA  . HIS D  1 64  ? 178.690 142.874 47.660 1.00   31.27 ? 63   HIS D CA  1 
ATOM   3803  C  C   . HIS D  1 64  ? 177.955 142.968 46.396 1.00   31.64 ? 63   HIS D C   1 
ATOM   3804  O  O   . HIS D  1 64  ? 178.202 142.172 45.491 1.00   32.32 ? 63   HIS D O   1 
ATOM   3805  C  CB  . HIS D  1 64  ? 180.027 143.610 47.537 1.00   32.23 ? 63   HIS D CB  1 
ATOM   3806  C  CG  . HIS D  1 64  ? 180.809 143.646 48.821 1.00   32.49 ? 63   HIS D CG  1 
ATOM   3807  N  ND1 . HIS D  1 64  ? 181.930 144.378 48.973 1.00   32.97 ? 63   HIS D ND1 1 
ATOM   3808  C  CD2 . HIS D  1 64  ? 180.574 143.018 50.044 1.00   32.21 ? 63   HIS D CD2 1 
ATOM   3809  C  CE1 . HIS D  1 64  ? 182.397 144.221 50.231 1.00   33.21 ? 63   HIS D CE1 1 
ATOM   3810  N  NE2 . HIS D  1 64  ? 181.559 143.395 50.889 1.00   33.35 ? 63   HIS D NE2 1 
ATOM   3811  N  N   . PHE D  1 65  ? 177.035 143.925 46.301 1.00   31.59 ? 64   PHE D N   1 
ATOM   3812  C  CA  . PHE D  1 65  ? 176.260 144.066 45.072 1.00   32.95 ? 64   PHE D CA  1 
ATOM   3813  C  C   . PHE D  1 65  ? 177.195 144.495 43.958 1.00   34.93 ? 64   PHE D C   1 
ATOM   3814  O  O   . PHE D  1 65  ? 177.799 145.566 44.018 1.00   34.64 ? 64   PHE D O   1 
ATOM   3815  C  CB  . PHE D  1 65  ? 175.130 145.080 45.238 1.00   32.59 ? 64   PHE D CB  1 
ATOM   3816  C  CG  . PHE D  1 65  ? 174.236 145.215 44.025 1.00   33.20 ? 64   PHE D CG  1 
ATOM   3817  C  CD1 . PHE D  1 65  ? 173.858 144.107 43.291 1.00   33.16 ? 64   PHE D CD1 1 
ATOM   3818  C  CD2 . PHE D  1 65  ? 173.756 146.468 43.641 1.00   33.22 ? 64   PHE D CD2 1 
ATOM   3819  C  CE1 . PHE D  1 65  ? 173.033 144.242 42.185 1.00   34.84 ? 64   PHE D CE1 1 
ATOM   3820  C  CE2 . PHE D  1 65  ? 172.925 146.608 42.552 1.00   33.89 ? 64   PHE D CE2 1 
ATOM   3821  C  CZ  . PHE D  1 65  ? 172.560 145.498 41.818 1.00   34.62 ? 64   PHE D CZ  1 
ATOM   3822  N  N   . ASN D  1 66  ? 177.308 143.659 42.937 1.00   37.97 ? 65   ASN D N   1 
ATOM   3823  C  CA  . ASN D  1 66  ? 178.345 143.850 41.929 1.00   40.52 ? 65   ASN D CA  1 
ATOM   3824  C  C   . ASN D  1 66  ? 177.910 143.430 40.526 1.00   42.98 ? 65   ASN D C   1 
ATOM   3825  O  O   . ASN D  1 66  ? 178.411 142.435 39.998 1.00   45.69 ? 65   ASN D O   1 
ATOM   3826  C  CB  . ASN D  1 66  ? 179.590 143.073 42.349 1.00   41.06 ? 65   ASN D CB  1 
ATOM   3827  C  CG  . ASN D  1 66  ? 180.742 143.271 41.395 1.00   43.49 ? 65   ASN D CG  1 
ATOM   3828  O  OD1 . ASN D  1 66  ? 180.736 144.197 40.587 1.00   45.23 ? 65   ASN D OD1 1 
ATOM   3829  N  ND2 . ASN D  1 66  ? 181.736 142.410 41.486 1.00   42.11 ? 65   ASN D ND2 1 
ATOM   3830  N  N   . PRO D  1 67  ? 176.987 144.195 39.910 1.00   42.47 ? 66   PRO D N   1 
ATOM   3831  C  CA  . PRO D  1 67  ? 176.493 143.815 38.602 1.00   44.85 ? 66   PRO D CA  1 
ATOM   3832  C  C   . PRO D  1 67  ? 177.474 144.083 37.433 1.00   48.38 ? 66   PRO D C   1 
ATOM   3833  O  O   . PRO D  1 67  ? 177.154 143.724 36.302 1.00   53.55 ? 66   PRO D O   1 
ATOM   3834  C  CB  . PRO D  1 67  ? 175.200 144.636 38.464 1.00   43.47 ? 66   PRO D CB  1 
ATOM   3835  C  CG  . PRO D  1 67  ? 175.401 145.831 39.323 1.00   42.02 ? 66   PRO D CG  1 
ATOM   3836  C  CD  . PRO D  1 67  ? 176.427 145.481 40.365 1.00   41.62 ? 66   PRO D CD  1 
ATOM   3837  N  N   . LEU D  1 68  ? 178.635 144.688 37.713 1.00   50.80 ? 67   LEU D N   1 
ATOM   3838  C  CA  . LEU D  1 68  ? 179.679 144.977 36.715 1.00   54.65 ? 67   LEU D CA  1 
ATOM   3839  C  C   . LEU D  1 68  ? 180.947 144.117 36.885 1.00   57.12 ? 67   LEU D C   1 
ATOM   3840  O  O   . LEU D  1 68  ? 181.990 144.424 36.304 1.00   57.62 ? 67   LEU D O   1 
ATOM   3841  C  CB  . LEU D  1 68  ? 180.077 146.463 36.792 1.00   54.99 ? 67   LEU D CB  1 
ATOM   3842  C  CG  . LEU D  1 68  ? 178.937 147.488 36.737 1.00   54.63 ? 67   LEU D CG  1 
ATOM   3843  C  CD1 . LEU D  1 68  ? 179.373 148.883 37.150 1.00   56.02 ? 67   LEU D CD1 1 
ATOM   3844  C  CD2 . LEU D  1 68  ? 178.364 147.524 35.348 1.00   55.28 ? 67   LEU D CD2 1 
ATOM   3845  N  N   . SER D  1 69  ? 180.855 143.051 37.681 1.00   57.94 ? 68   SER D N   1 
ATOM   3846  C  CA  . SER D  1 69  ? 181.983 142.144 37.974 1.00   59.35 ? 68   SER D CA  1 
ATOM   3847  C  C   . SER D  1 69  ? 183.343 142.826 38.183 1.00   61.71 ? 68   SER D C   1 
ATOM   3848  O  O   . SER D  1 69  ? 184.387 142.286 37.793 1.00   61.37 ? 68   SER D O   1 
ATOM   3849  C  CB  . SER D  1 69  ? 182.093 141.076 36.889 1.00   60.76 ? 68   SER D CB  1 
ATOM   3850  O  OG  . SER D  1 69  ? 180.956 140.238 36.917 1.00   59.72 ? 68   SER D OG  1 
ATOM   3851  N  N   . ARG D  1 70  ? 183.324 144.001 38.810 1.00   62.01 ? 69   ARG D N   1 
ATOM   3852  C  CA  . ARG D  1 70  ? 184.551 144.740 39.094 1.00   63.72 ? 69   ARG D CA  1 
ATOM   3853  C  C   . ARG D  1 70  ? 185.149 144.210 40.389 1.00   62.27 ? 69   ARG D C   1 
ATOM   3854  O  O   . ARG D  1 70  ? 184.509 143.421 41.099 1.00   59.69 ? 69   ARG D O   1 
ATOM   3855  C  CB  . ARG D  1 70  ? 184.263 146.232 39.253 1.00   65.32 ? 69   ARG D CB  1 
ATOM   3856  C  CG  . ARG D  1 70  ? 183.668 146.937 38.036 1.00   68.57 ? 69   ARG D CG  1 
ATOM   3857  C  CD  . ARG D  1 70  ? 183.219 148.334 38.450 1.00   70.09 ? 69   ARG D CD  1 
ATOM   3858  N  NE  . ARG D  1 70  ? 183.000 149.288 37.361 1.00   73.71 ? 69   ARG D NE  1 
ATOM   3859  C  CZ  . ARG D  1 70  ? 183.937 150.057 36.799 1.00   76.78 ? 69   ARG D CZ  1 
ATOM   3860  N  NH1 . ARG D  1 70  ? 185.211 149.982 37.175 1.00   74.75 ? 69   ARG D NH1 1 
ATOM   3861  N  NH2 . ARG D  1 70  ? 183.594 150.902 35.828 1.00   79.01 ? 69   ARG D NH2 1 
ATOM   3862  N  N   . LYS D  1 71  ? 186.371 144.641 40.698 1.00   60.95 ? 70   LYS D N   1 
ATOM   3863  C  CA  . LYS D  1 71  ? 186.959 144.375 42.011 1.00   60.41 ? 70   LYS D CA  1 
ATOM   3864  C  C   . LYS D  1 71  ? 186.479 145.420 43.031 1.00   56.59 ? 70   LYS D C   1 
ATOM   3865  O  O   . LYS D  1 71  ? 185.922 146.463 42.660 1.00   57.46 ? 70   LYS D O   1 
ATOM   3866  C  CB  . LYS D  1 71  ? 188.493 144.343 41.946 1.00   63.09 ? 70   LYS D CB  1 
ATOM   3867  C  CG  . LYS D  1 71  ? 189.068 143.141 41.209 1.00   66.23 ? 70   LYS D CG  1 
ATOM   3868  C  CD  . LYS D  1 71  ? 190.596 143.155 41.209 1.00   68.25 ? 70   LYS D CD  1 
ATOM   3869  C  CE  . LYS D  1 71  ? 191.170 141.788 40.859 1.00   70.06 ? 70   LYS D CE  1 
ATOM   3870  N  NZ  . LYS D  1 71  ? 192.649 141.818 40.657 1.00   71.02 ? 70   LYS D NZ  1 
ATOM   3871  N  N   . HIS D  1 72  ? 186.713 145.120 44.308 1.00   52.48 ? 71   HIS D N   1 
ATOM   3872  C  CA  . HIS D  1 72  ? 186.273 145.945 45.439 1.00   49.89 ? 71   HIS D CA  1 
ATOM   3873  C  C   . HIS D  1 72  ? 187.052 147.237 45.558 1.00   50.95 ? 71   HIS D C   1 
ATOM   3874  O  O   . HIS D  1 72  ? 188.277 147.232 45.538 1.00   52.02 ? 71   HIS D O   1 
ATOM   3875  C  CB  . HIS D  1 72  ? 186.434 145.132 46.728 1.00   48.00 ? 71   HIS D CB  1 
ATOM   3876  C  CG  . HIS D  1 72  ? 186.056 145.872 47.991 1.00   46.19 ? 71   HIS D CG  1 
ATOM   3877  N  ND1 . HIS D  1 72  ? 184.777 146.076 48.365 1.00   43.89 ? 71   HIS D ND1 1 
ATOM   3878  C  CD2 . HIS D  1 72  ? 186.853 146.439 48.991 1.00   46.01 ? 71   HIS D CD2 1 
ATOM   3879  C  CE1 . HIS D  1 72  ? 184.754 146.746 49.533 1.00   42.86 ? 71   HIS D CE1 1 
ATOM   3880  N  NE2 . HIS D  1 72  ? 186.027 146.962 49.918 1.00   44.34 ? 71   HIS D NE2 1 
ATOM   3881  N  N   . GLY D  1 73  ? 186.344 148.354 45.705 1.00   50.51 ? 72   GLY D N   1 
ATOM   3882  C  CA  . GLY D  1 73  ? 186.971 149.646 45.956 1.00   48.60 ? 72   GLY D CA  1 
ATOM   3883  C  C   . GLY D  1 73  ? 186.283 150.423 47.058 1.00   46.49 ? 72   GLY D C   1 
ATOM   3884  O  O   . GLY D  1 73  ? 185.528 149.864 47.853 1.00   45.35 ? 72   GLY D O   1 
ATOM   3885  N  N   . GLY D  1 74  ? 186.581 151.717 47.113 1.00   44.52 ? 73   GLY D N   1 
ATOM   3886  C  CA  . GLY D  1 74  ? 185.937 152.649 48.024 1.00   41.96 ? 73   GLY D CA  1 
ATOM   3887  C  C   . GLY D  1 74  ? 184.926 153.433 47.234 1.00   41.39 ? 73   GLY D C   1 
ATOM   3888  O  O   . GLY D  1 74  ? 184.916 153.353 46.008 1.00   40.83 ? 73   GLY D O   1 
ATOM   3889  N  N   . PRO D  1 75  ? 184.060 154.192 47.925 1.00   41.09 ? 74   PRO D N   1 
ATOM   3890  C  CA  . PRO D  1 75  ? 182.970 154.847 47.204 1.00   42.42 ? 74   PRO D CA  1 
ATOM   3891  C  C   . PRO D  1 75  ? 183.428 155.873 46.153 1.00   45.06 ? 74   PRO D C   1 
ATOM   3892  O  O   . PRO D  1 75  ? 182.668 156.171 45.233 1.00   44.95 ? 74   PRO D O   1 
ATOM   3893  C  CB  . PRO D  1 75  ? 182.130 155.507 48.317 1.00   41.03 ? 74   PRO D CB  1 
ATOM   3894  C  CG  . PRO D  1 75  ? 182.963 155.465 49.544 1.00   40.13 ? 74   PRO D CG  1 
ATOM   3895  C  CD  . PRO D  1 75  ? 183.935 154.338 49.385 1.00   40.56 ? 74   PRO D CD  1 
ATOM   3896  N  N   . LYS D  1 76  ? 184.648 156.392 46.271 1.00   46.48 ? 75   LYS D N   1 
ATOM   3897  C  CA  . LYS D  1 76  ? 185.142 157.370 45.302 1.00   50.12 ? 75   LYS D CA  1 
ATOM   3898  C  C   . LYS D  1 76  ? 186.135 156.775 44.303 1.00   52.92 ? 75   LYS D C   1 
ATOM   3899  O  O   . LYS D  1 76  ? 186.754 157.512 43.538 1.00   55.25 ? 75   LYS D O   1 
ATOM   3900  C  CB  . LYS D  1 76  ? 185.764 158.571 46.026 1.00   51.01 ? 75   LYS D CB  1 
ATOM   3901  C  CG  . LYS D  1 76  ? 184.843 159.267 47.024 1.00   50.61 ? 75   LYS D CG  1 
ATOM   3902  C  CD  . LYS D  1 76  ? 183.459 159.536 46.450 1.00   51.91 ? 75   LYS D CD  1 
ATOM   3903  C  CE  . LYS D  1 76  ? 182.554 160.227 47.457 1.00   52.06 ? 75   LYS D CE  1 
ATOM   3904  N  NZ  . LYS D  1 76  ? 181.180 160.442 46.911 1.00   52.60 ? 75   LYS D NZ  1 
ATOM   3905  N  N   . ASP D  1 77  ? 186.266 155.451 44.290 1.00   53.25 ? 76   ASP D N   1 
ATOM   3906  C  CA  . ASP D  1 77  ? 187.144 154.772 43.344 1.00   56.05 ? 76   ASP D CA  1 
ATOM   3907  C  C   . ASP D  1 77  ? 186.454 154.486 42.001 1.00   56.88 ? 76   ASP D C   1 
ATOM   3908  O  O   . ASP D  1 77  ? 185.256 154.174 41.941 1.00   56.60 ? 76   ASP D O   1 
ATOM   3909  C  CB  . ASP D  1 77  ? 187.679 153.472 43.955 1.00   56.68 ? 76   ASP D CB  1 
ATOM   3910  C  CG  . ASP D  1 77  ? 188.609 153.717 45.133 1.00   58.41 ? 76   ASP D CG  1 
ATOM   3911  O  OD1 . ASP D  1 77  ? 188.871 154.895 45.474 1.00   62.07 ? 76   ASP D OD1 1 
ATOM   3912  O  OD2 . ASP D  1 77  ? 189.086 152.725 45.725 1.00   58.50 ? 76   ASP D OD2 1 
ATOM   3913  N  N   . GLU D  1 78  ? 187.231 154.600 40.927 1.00   58.54 ? 77   GLU D N   1 
ATOM   3914  C  CA  . GLU D  1 78  ? 186.778 154.237 39.587 1.00   59.20 ? 77   GLU D CA  1 
ATOM   3915  C  C   . GLU D  1 78  ? 186.377 152.776 39.603 1.00   57.91 ? 77   GLU D C   1 
ATOM   3916  O  O   . GLU D  1 78  ? 185.299 152.425 39.126 1.00   57.21 ? 77   GLU D O   1 
ATOM   3917  C  CB  . GLU D  1 78  ? 187.891 154.450 38.557 0.010  61.23 ? 77   GLU D CB  1 
ATOM   3918  C  CG  . GLU D  1 78  ? 188.291 155.901 38.342 0.010  62.25 ? 77   GLU D CG  1 
ATOM   3919  C  CD  . GLU D  1 78  ? 189.534 156.038 37.485 0.010  64.33 ? 77   GLU D CD  1 
ATOM   3920  O  OE1 . GLU D  1 78  ? 190.106 154.998 37.094 0.010  64.98 ? 77   GLU D OE1 1 
ATOM   3921  O  OE2 . GLU D  1 78  ? 189.941 157.184 37.203 0.010  65.40 ? 77   GLU D OE2 1 
ATOM   3922  N  N   . GLU D  1 79  ? 187.246 151.931 40.164 1.00   57.49 ? 78   GLU D N   1 
ATOM   3923  C  CA  A GLU D  1 79  ? 186.970 150.502 40.288 0.50   57.11 ? 78   GLU D CA  1 
ATOM   3924  C  CA  B GLU D  1 79  ? 186.934 150.509 40.289 0.50   56.46 ? 78   GLU D CA  1 
ATOM   3925  C  C   . GLU D  1 79  ? 186.321 150.207 41.650 1.00   53.62 ? 78   GLU D C   1 
ATOM   3926  O  O   . GLU D  1 79  ? 186.988 150.258 42.689 1.00   52.24 ? 78   GLU D O   1 
ATOM   3927  C  CB  A GLU D  1 79  ? 188.266 149.689 40.095 0.50   59.07 ? 78   GLU D CB  1 
ATOM   3928  C  CB  B GLU D  1 79  ? 188.149 149.608 40.052 0.50   57.60 ? 78   GLU D CB  1 
ATOM   3929  C  CG  A GLU D  1 79  ? 188.054 148.298 39.508 0.50   60.25 ? 78   GLU D CG  1 
ATOM   3930  C  CG  B GLU D  1 79  ? 187.738 148.140 40.006 0.50   56.94 ? 78   GLU D CG  1 
ATOM   3931  C  CD  A GLU D  1 79  ? 187.519 148.341 38.086 0.50   62.29 ? 78   GLU D CD  1 
ATOM   3932  C  CD  B GLU D  1 79  ? 188.860 147.212 39.623 0.50   57.87 ? 78   GLU D CD  1 
ATOM   3933  O  OE1 A GLU D  1 79  ? 187.823 149.319 37.373 0.50   63.28 ? 78   GLU D OE1 1 
ATOM   3934  O  OE1 B GLU D  1 79  ? 190.026 147.656 39.628 0.50   57.59 ? 78   GLU D OE1 1 
ATOM   3935  O  OE2 A GLU D  1 79  ? 186.773 147.418 37.685 0.50   61.11 ? 78   GLU D OE2 1 
ATOM   3936  O  OE2 B GLU D  1 79  ? 188.564 146.034 39.326 0.50   57.51 ? 78   GLU D OE2 1 
ATOM   3937  N  N   . ARG D  1 80  ? 185.029 149.903 41.631 1.00   51.40 ? 79   ARG D N   1 
ATOM   3938  C  CA  . ARG D  1 80  ? 184.292 149.543 42.838 1.00   46.86 ? 79   ARG D CA  1 
ATOM   3939  C  C   . ARG D  1 80  ? 183.091 148.686 42.510 1.00   45.69 ? 79   ARG D C   1 
ATOM   3940  O  O   . ARG D  1 80  ? 182.617 148.641 41.363 1.00   46.10 ? 79   ARG D O   1 
ATOM   3941  C  CB  . ARG D  1 80  ? 183.797 150.799 43.555 1.00   44.78 ? 79   ARG D CB  1 
ATOM   3942  C  CG  . ARG D  1 80  ? 182.820 151.632 42.746 1.00   44.13 ? 79   ARG D CG  1 
ATOM   3943  C  CD  . ARG D  1 80  ? 182.237 152.750 43.582 1.00   43.51 ? 79   ARG D CD  1 
ATOM   3944  N  NE  . ARG D  1 80  ? 180.990 152.352 44.238 1.00   42.33 ? 79   ARG D NE  1 
ATOM   3945  C  CZ  . ARG D  1 80  ? 180.186 153.184 44.894 1.00   41.28 ? 79   ARG D CZ  1 
ATOM   3946  N  NH1 . ARG D  1 80  ? 180.504 154.459 45.027 1.00   41.12 ? 79   ARG D NH1 1 
ATOM   3947  N  NH2 . ARG D  1 80  ? 179.053 152.733 45.427 1.00   41.24 ? 79   ARG D NH2 1 
ATOM   3948  N  N   . HIS D  1 81  ? 182.569 148.037 43.545 1.00   43.37 ? 80   HIS D N   1 
ATOM   3949  C  CA  . HIS D  1 81  ? 181.263 147.423 43.453 1.00   41.01 ? 80   HIS D CA  1 
ATOM   3950  C  C   . HIS D  1 81  ? 180.232 148.506 43.584 1.00   39.14 ? 80   HIS D C   1 
ATOM   3951  O  O   . HIS D  1 81  ? 180.467 149.530 44.224 1.00   39.04 ? 80   HIS D O   1 
ATOM   3952  C  CB  . HIS D  1 81  ? 181.088 146.393 44.548 1.00   40.40 ? 80   HIS D CB  1 
ATOM   3953  C  CG  . HIS D  1 81  ? 182.120 145.298 44.526 1.00   40.71 ? 80   HIS D CG  1 
ATOM   3954  N  ND1 . HIS D  1 81  ? 182.638 144.770 45.644 1.00   39.76 ? 80   HIS D ND1 1 
ATOM   3955  C  CD2 . HIS D  1 81  ? 182.715 144.631 43.461 1.00   41.73 ? 80   HIS D CD2 1 
ATOM   3956  C  CE1 . HIS D  1 81  ? 183.508 143.799 45.312 1.00   41.24 ? 80   HIS D CE1 1 
ATOM   3957  N  NE2 . HIS D  1 81  ? 183.553 143.719 43.975 1.00   41.89 ? 80   HIS D NE2 1 
ATOM   3958  N  N   . VAL D  1 82  ? 179.082 148.310 42.963 1.00   38.39 ? 81   VAL D N   1 
ATOM   3959  C  CA  . VAL D  1 82  ? 177.957 149.215 43.171 1.00   38.02 ? 81   VAL D CA  1 
ATOM   3960  C  C   . VAL D  1 82  ? 177.654 149.346 44.668 1.00   37.07 ? 81   VAL D C   1 
ATOM   3961  O  O   . VAL D  1 82  ? 177.315 150.436 45.142 1.00   37.07 ? 81   VAL D O   1 
ATOM   3962  C  CB  . VAL D  1 82  ? 176.708 148.724 42.410 1.00   38.00 ? 81   VAL D CB  1 
ATOM   3963  C  CG1 . VAL D  1 82  ? 175.484 149.556 42.760 1.00   36.88 ? 81   VAL D CG1 1 
ATOM   3964  C  CG2 . VAL D  1 82  ? 176.975 148.747 40.910 1.00   39.10 ? 81   VAL D CG2 1 
ATOM   3965  N  N   . GLY D  1 83  ? 177.819 148.246 45.408 1.00   35.51 ? 82   GLY D N   1 
ATOM   3966  C  CA  . GLY D  1 83  ? 177.541 148.232 46.848 1.00   35.00 ? 82   GLY D CA  1 
ATOM   3967  C  C   . GLY D  1 83  ? 178.575 148.845 47.775 1.00   34.41 ? 82   GLY D C   1 
ATOM   3968  O  O   . GLY D  1 83  ? 178.338 148.955 48.978 1.00   32.15 ? 82   GLY D O   1 
ATOM   3969  N  N   . ASP D  1 84  ? 179.725 149.262 47.243 1.00   34.96 ? 83   ASP D N   1 
ATOM   3970  C  CA  . ASP D  1 84  ? 180.804 149.732 48.106 1.00   33.69 ? 83   ASP D CA  1 
ATOM   3971  C  C   . ASP D  1 84  ? 180.589 151.151 48.655 1.00   33.82 ? 83   ASP D C   1 
ATOM   3972  O  O   . ASP D  1 84  ? 180.893 152.142 47.972 1.00   36.48 ? 83   ASP D O   1 
ATOM   3973  C  CB  . ASP D  1 84  ? 182.118 149.671 47.345 1.00   35.23 ? 83   ASP D CB  1 
ATOM   3974  C  CG  . ASP D  1 84  ? 182.547 148.260 47.020 1.00   35.50 ? 83   ASP D CG  1 
ATOM   3975  O  OD1 . ASP D  1 84  ? 182.101 147.301 47.688 1.00   32.54 ? 83   ASP D OD1 1 
ATOM   3976  O  OD2 . ASP D  1 84  ? 183.360 148.118 46.078 1.00   36.46 ? 83   ASP D OD2 1 
ATOM   3977  N  N   . LEU D  1 85  ? 180.108 151.272 49.890 1.00   31.59 ? 84   LEU D N   1 
ATOM   3978  C  CA  . LEU D  1 85  ? 179.947 152.594 50.497 1.00   31.13 ? 84   LEU D CA  1 
ATOM   3979  C  C   . LEU D  1 85  ? 181.000 152.919 51.563 1.00   30.95 ? 84   LEU D C   1 
ATOM   3980  O  O   . LEU D  1 85  ? 180.800 153.809 52.372 1.00   30.92 ? 84   LEU D O   1 
ATOM   3981  C  CB  . LEU D  1 85  ? 178.547 152.757 51.073 1.00   29.71 ? 84   LEU D CB  1 
ATOM   3982  C  CG  . LEU D  1 85  ? 177.414 152.564 50.071 1.00   30.21 ? 84   LEU D CG  1 
ATOM   3983  C  CD1 . LEU D  1 85  ? 176.074 152.528 50.805 1.00   28.38 ? 84   LEU D CD1 1 
ATOM   3984  C  CD2 . LEU D  1 85  ? 177.461 153.673 49.015 1.00   31.37 ? 84   LEU D CD2 1 
ATOM   3985  N  N   . GLY D  1 86  ? 182.116 152.199 51.560 1.00   31.72 ? 85   GLY D N   1 
ATOM   3986  C  CA  . GLY D  1 86  ? 183.266 152.563 52.394 1.00   32.23 ? 85   GLY D CA  1 
ATOM   3987  C  C   . GLY D  1 86  ? 183.140 152.220 53.871 1.00   31.43 ? 85   GLY D C   1 
ATOM   3988  O  O   . GLY D  1 86  ? 182.786 151.111 54.226 1.00   30.86 ? 85   GLY D O   1 
ATOM   3989  N  N   . ASN D  1 87  ? 183.449 153.185 54.723 1.00   31.37 ? 86   ASN D N   1 
ATOM   3990  C  CA  . ASN D  1 87  ? 183.456 153.001 56.158 1.00   30.72 ? 86   ASN D CA  1 
ATOM   3991  C  C   . ASN D  1 87  ? 182.531 154.022 56.786 1.00   29.37 ? 86   ASN D C   1 
ATOM   3992  O  O   . ASN D  1 87  ? 182.369 155.110 56.261 1.00   30.05 ? 86   ASN D O   1 
ATOM   3993  C  CB  . ASN D  1 87  ? 184.875 153.214 56.703 1.00   32.49 ? 86   ASN D CB  1 
ATOM   3994  C  CG  . ASN D  1 87  ? 185.804 152.033 56.433 1.00   33.38 ? 86   ASN D CG  1 
ATOM   3995  O  OD1 . ASN D  1 87  ? 185.530 150.903 56.843 1.00   32.84 ? 86   ASN D OD1 1 
ATOM   3996  N  ND2 . ASN D  1 87  ? 186.913 152.295 55.747 1.00   33.65 ? 86   ASN D ND2 1 
ATOM   3997  N  N   . VAL D  1 88  ? 181.903 153.647 57.896 1.00   28.06 ? 87   VAL D N   1 
ATOM   3998  C  CA  . VAL D  1 88  ? 181.348 154.594 58.840 1.00   26.81 ? 87   VAL D CA  1 
ATOM   3999  C  C   . VAL D  1 88  ? 182.318 154.621 60.030 1.00   27.19 ? 87   VAL D C   1 
ATOM   4000  O  O   . VAL D  1 88  ? 183.134 153.717 60.181 1.00   26.72 ? 87   VAL D O   1 
ATOM   4001  C  CB  . VAL D  1 88  ? 179.938 154.201 59.294 1.00   26.55 ? 87   VAL D CB  1 
ATOM   4002  C  CG1 . VAL D  1 88  ? 178.985 154.215 58.112 1.00   26.43 ? 87   VAL D CG1 1 
ATOM   4003  C  CG2 . VAL D  1 88  ? 179.926 152.833 60.014 1.00   25.97 ? 87   VAL D CG2 1 
ATOM   4004  N  N   . THR D  1 89  ? 182.235 155.671 60.843 1.00   27.19 ? 88   THR D N   1 
ATOM   4005  C  CA  . THR D  1 89  ? 183.114 155.857 61.989 1.00   27.96 ? 88   THR D CA  1 
ATOM   4006  C  C   . THR D  1 89  ? 182.288 155.969 63.268 1.00   27.81 ? 88   THR D C   1 
ATOM   4007  O  O   . THR D  1 89  ? 181.414 156.843 63.384 1.00   27.86 ? 88   THR D O   1 
ATOM   4008  C  CB  . THR D  1 89  ? 183.986 157.122 61.805 1.00   28.75 ? 88   THR D CB  1 
ATOM   4009  O  OG1 . THR D  1 89  ? 184.779 156.968 60.623 1.00   29.36 ? 88   THR D OG1 1 
ATOM   4010  C  CG2 . THR D  1 89  ? 184.917 157.335 62.991 1.00   28.12 ? 88   THR D CG2 1 
ATOM   4011  N  N   . ALA D  1 90  ? 182.546 155.063 64.207 1.00   27.92 ? 89   ALA D N   1 
ATOM   4012  C  CA  . ALA D  1 90  ? 181.939 155.109 65.539 1.00   28.35 ? 89   ALA D CA  1 
ATOM   4013  C  C   . ALA D  1 90  ? 182.833 155.928 66.494 1.00   29.25 ? 89   ALA D C   1 
ATOM   4014  O  O   . ALA D  1 90  ? 184.050 155.730 66.541 1.00   29.86 ? 89   ALA D O   1 
ATOM   4015  C  CB  . ALA D  1 90  ? 181.749 153.691 66.096 1.00   27.39 ? 89   ALA D CB  1 
ATOM   4016  N  N   . ASP D  1 91  ? 182.202 156.802 67.273 1.00   29.50 ? 90   ASP D N   1 
ATOM   4017  C  CA  . ASP D  1 91  ? 182.867 157.592 68.302 1.00   30.44 ? 90   ASP D CA  1 
ATOM   4018  C  C   . ASP D  1 91  ? 183.085 156.744 69.559 1.00   31.80 ? 90   ASP D C   1 
ATOM   4019  O  O   . ASP D  1 91  ? 182.711 155.581 69.591 1.00   32.43 ? 90   ASP D O   1 
ATOM   4020  C  CB  . ASP D  1 91  ? 182.033 158.850 68.600 1.00   30.29 ? 90   ASP D CB  1 
ATOM   4021  C  CG  . ASP D  1 91  ? 180.630 158.533 69.137 1.00   30.29 ? 90   ASP D CG  1 
ATOM   4022  O  OD1 . ASP D  1 91  ? 180.388 157.439 69.697 1.00   29.45 ? 90   ASP D OD1 1 
ATOM   4023  O  OD2 . ASP D  1 91  ? 179.751 159.404 69.004 1.00   31.12 ? 90   ASP D OD2 1 
ATOM   4024  N  N   . LYS D  1 92  ? 183.673 157.324 70.595 1.00   33.42 ? 91   LYS D N   1 
ATOM   4025  C  CA  . LYS D  1 92  ? 183.969 156.584 71.836 1.00   34.89 ? 91   LYS D CA  1 
ATOM   4026  C  C   . LYS D  1 92  ? 182.718 156.064 72.557 1.00   33.35 ? 91   LYS D C   1 
ATOM   4027  O  O   . LYS D  1 92  ? 182.814 155.127 73.346 1.00   33.37 ? 91   LYS D O   1 
ATOM   4028  C  CB  . LYS D  1 92  ? 184.800 157.443 72.788 1.00   37.27 ? 91   LYS D CB  1 
ATOM   4029  C  CG  . LYS D  1 92  ? 184.062 158.653 73.358 1.00   39.73 ? 91   LYS D CG  1 
ATOM   4030  C  CD  . LYS D  1 92  ? 185.038 159.680 73.919 1.00   42.62 ? 91   LYS D CD  1 
ATOM   4031  C  CE  . LYS D  1 92  ? 184.320 160.779 74.690 1.00   45.15 ? 91   LYS D CE  1 
ATOM   4032  N  NZ  . LYS D  1 92  ? 183.047 161.210 74.044 1.00   46.79 ? 91   LYS D NZ  1 
ATOM   4033  N  N   . ASP D  1 93  ? 181.561 156.668 72.279 1.00   31.77 ? 92   ASP D N   1 
ATOM   4034  C  CA  . ASP D  1 93  ? 180.275 156.157 72.772 1.00   31.42 ? 92   ASP D CA  1 
ATOM   4035  C  C   . ASP D  1 93  ? 179.651 155.033 71.933 1.00   30.49 ? 92   ASP D C   1 
ATOM   4036  O  O   . ASP D  1 93  ? 178.555 154.606 72.233 1.00   29.74 ? 92   ASP D O   1 
ATOM   4037  C  CB  . ASP D  1 93  ? 179.273 157.305 72.924 1.00   31.28 ? 92   ASP D CB  1 
ATOM   4038  C  CG  . ASP D  1 93  ? 179.662 158.247 74.021 0.50   31.86 ? 92   ASP D CG  1 
ATOM   4039  O  OD1 . ASP D  1 93  ? 179.718 157.789 75.177 0.50   32.81 ? 92   ASP D OD1 1 
ATOM   4040  O  OD2 . ASP D  1 93  ? 179.944 159.420 73.732 0.50   31.33 ? 92   ASP D OD2 1 
ATOM   4041  N  N   . GLY D  1 94  ? 180.344 154.560 70.894 1.00   30.22 ? 93   GLY D N   1 
ATOM   4042  C  CA  . GLY D  1 94  ? 179.855 153.455 70.062 1.00   29.14 ? 93   GLY D CA  1 
ATOM   4043  C  C   . GLY D  1 94  ? 178.824 153.876 69.029 1.00   29.32 ? 93   GLY D C   1 
ATOM   4044  O  O   . GLY D  1 94  ? 178.177 153.014 68.405 1.00   28.47 ? 93   GLY D O   1 
ATOM   4045  N  N   . VAL D  1 95  ? 178.676 155.193 68.836 1.00   29.40 ? 94   VAL D N   1 
ATOM   4046  C  CA  . VAL D  1 95  ? 177.677 155.740 67.922 1.00   29.93 ? 94   VAL D CA  1 
ATOM   4047  C  C   . VAL D  1 95  ? 178.364 156.266 66.665 1.00   30.28 ? 94   VAL D C   1 
ATOM   4048  O  O   . VAL D  1 95  ? 179.237 157.150 66.735 1.00   30.56 ? 94   VAL D O   1 
ATOM   4049  C  CB  . VAL D  1 95  ? 176.864 156.886 68.556 1.00   30.20 ? 94   VAL D CB  1 
ATOM   4050  C  CG1 . VAL D  1 95  ? 175.911 157.492 67.536 1.00   29.13 ? 94   VAL D CG1 1 
ATOM   4051  C  CG2 . VAL D  1 95  ? 176.106 156.406 69.786 1.00   29.95 ? 94   VAL D CG2 1 
ATOM   4052  N  N   . ALA D  1 96  ? 177.979 155.693 65.530 1.00   29.68 ? 95   ALA D N   1 
ATOM   4053  C  CA  . ALA D  1 96  ? 178.413 156.143 64.218 1.00   30.04 ? 95   ALA D CA  1 
ATOM   4054  C  C   . ALA D  1 96  ? 177.271 156.950 63.584 1.00   31.48 ? 95   ALA D C   1 
ATOM   4055  O  O   . ALA D  1 96  ? 176.200 156.418 63.297 1.00   30.48 ? 95   ALA D O   1 
ATOM   4056  C  CB  . ALA D  1 96  ? 178.784 154.950 63.345 1.00   28.57 ? 95   ALA D CB  1 
ATOM   4057  N  N   . ASP D  1 97  ? 177.474 158.245 63.407 1.00   33.39 ? 96   ASP D N   1 
ATOM   4058  C  CA  . ASP D  1 97  ? 176.490 159.059 62.707 1.00   36.01 ? 96   ASP D CA  1 
ATOM   4059  C  C   . ASP D  1 97  ? 176.915 159.073 61.239 1.00   35.48 ? 96   ASP D C   1 
ATOM   4060  O  O   . ASP D  1 97  ? 178.076 159.337 60.927 1.00   34.98 ? 96   ASP D O   1 
ATOM   4061  C  CB  . ASP D  1 97  ? 176.388 160.460 63.329 1.00   38.69 ? 96   ASP D CB  1 
ATOM   4062  C  CG  . ASP D  1 97  ? 175.917 160.413 64.800 1.00   40.87 ? 96   ASP D CG  1 
ATOM   4063  O  OD1 . ASP D  1 97  ? 174.769 159.965 65.072 1.00   41.14 ? 96   ASP D OD1 1 
ATOM   4064  O  OD2 . ASP D  1 97  ? 176.705 160.813 65.690 1.00   42.78 ? 96   ASP D OD2 1 
ATOM   4065  N  N   . VAL D  1 98  ? 175.981 158.712 60.363 1.00   35.34 ? 97   VAL D N   1 
ATOM   4066  C  CA  . VAL D  1 98  ? 176.259 158.516 58.942 1.00   35.60 ? 97   VAL D CA  1 
ATOM   4067  C  C   . VAL D  1 98  ? 175.693 159.646 58.084 1.00   36.90 ? 97   VAL D C   1 
ATOM   4068  O  O   . VAL D  1 98  ? 174.534 160.048 58.257 1.00   35.74 ? 97   VAL D O   1 
ATOM   4069  C  CB  . VAL D  1 98  ? 175.683 157.166 58.440 1.00   34.24 ? 97   VAL D CB  1 
ATOM   4070  C  CG1 . VAL D  1 98  ? 175.909 156.998 56.949 1.00   33.41 ? 97   VAL D CG1 1 
ATOM   4071  C  CG2 . VAL D  1 98  ? 176.332 156.007 59.191 1.00   33.86 ? 97   VAL D CG2 1 
ATOM   4072  N  N   . SER D  1 99  ? 176.541 160.137 57.170 1.00   37.14 ? 98   SER D N   1 
ATOM   4073  C  CA  . SER D  1 99  ? 176.178 161.099 56.139 1.00   39.10 ? 98   SER D CA  1 
ATOM   4074  C  C   . SER D  1 99  ? 177.059 160.858 54.907 1.00   40.71 ? 98   SER D C   1 
ATOM   4075  O  O   . SER D  1 99  ? 178.284 160.959 54.966 1.00   40.64 ? 98   SER D O   1 
ATOM   4076  C  CB  . SER D  1 99  ? 176.370 162.522 56.623 1.00   40.40 ? 98   SER D CB  1 
ATOM   4077  O  OG  . SER D  1 99  ? 175.328 163.334 56.123 1.00   42.61 ? 98   SER D OG  1 
ATOM   4078  N  N   . ILE D  1 100 ? 176.420 160.533 53.799 1.00   40.55 ? 99   ILE D N   1 
ATOM   4079  C  CA  . ILE D  1 100 ? 177.093 160.036 52.622 1.00   41.82 ? 99   ILE D CA  1 
ATOM   4080  C  C   . ILE D  1 100 ? 176.259 160.505 51.433 1.00   43.16 ? 99   ILE D C   1 
ATOM   4081  O  O   . ILE D  1 100 ? 175.028 160.552 51.521 1.00   41.30 ? 99   ILE D O   1 
ATOM   4082  C  CB  . ILE D  1 100 ? 177.122 158.483 52.653 1.00   41.62 ? 99   ILE D CB  1 
ATOM   4083  C  CG1 . ILE D  1 100 ? 178.190 157.963 53.605 1.00   42.98 ? 99   ILE D CG1 1 
ATOM   4084  C  CG2 . ILE D  1 100 ? 177.398 157.893 51.286 1.00   42.34 ? 99   ILE D CG2 1 
ATOM   4085  C  CD1 . ILE D  1 100 ? 178.176 156.450 53.760 1.00   41.68 ? 99   ILE D CD1 1 
ATOM   4086  N  N   . GLU D  1 101 ? 176.917 160.895 50.346 1.00   44.16 ? 100  GLU D N   1 
ATOM   4087  C  CA  . GLU D  1 101 ? 176.243 160.979 49.051 1.00   45.68 ? 100  GLU D CA  1 
ATOM   4088  C  C   . GLU D  1 101 ? 176.991 160.078 48.079 1.00   42.75 ? 100  GLU D C   1 
ATOM   4089  O  O   . GLU D  1 101 ? 178.210 160.139 47.968 1.00   42.13 ? 100  GLU D O   1 
ATOM   4090  C  CB  . GLU D  1 101 ? 176.172 162.419 48.533 1.00   50.48 ? 100  GLU D CB  1 
ATOM   4091  C  CG  . GLU D  1 101 ? 175.419 163.377 49.454 1.00   53.54 ? 100  GLU D CG  1 
ATOM   4092  C  CD  . GLU D  1 101 ? 174.760 164.555 48.726 1.00   57.46 ? 100  GLU D CD  1 
ATOM   4093  O  OE1 . GLU D  1 101 ? 174.954 164.712 47.491 1.00   57.96 ? 100  GLU D OE1 1 
ATOM   4094  O  OE2 . GLU D  1 101 ? 174.023 165.323 49.399 1.00   58.92 ? 100  GLU D OE2 1 
ATOM   4095  N  N   . ASP D  1 102 ? 176.265 159.215 47.400 1.00   40.73 ? 101  ASP D N   1 
ATOM   4096  C  CA  . ASP D  1 102 ? 176.880 158.313 46.441 1.00   41.61 ? 101  ASP D CA  1 
ATOM   4097  C  C   . ASP D  1 102 ? 176.102 158.401 45.148 1.00   43.68 ? 101  ASP D C   1 
ATOM   4098  O  O   . ASP D  1 102 ? 174.882 158.615 45.172 1.00   44.31 ? 101  ASP D O   1 
ATOM   4099  C  CB  . ASP D  1 102 ? 176.859 156.878 46.954 1.00   39.37 ? 101  ASP D CB  1 
ATOM   4100  C  CG  . ASP D  1 102 ? 177.749 155.949 46.143 1.00   39.08 ? 101  ASP D CG  1 
ATOM   4101  O  OD1 . ASP D  1 102 ? 178.975 156.005 46.315 1.00   39.54 ? 101  ASP D OD1 1 
ATOM   4102  O  OD2 . ASP D  1 102 ? 177.243 155.132 45.351 1.00   38.49 ? 101  ASP D OD2 1 
ATOM   4103  N  N   . SER D  1 103 ? 176.804 158.215 44.031 1.00   44.12 ? 102  SER D N   1 
ATOM   4104  C  CA  . SER D  1 103 ? 176.205 158.330 42.701 1.00   45.21 ? 102  SER D CA  1 
ATOM   4105  C  C   . SER D  1 103 ? 176.243 157.034 41.912 1.00   44.80 ? 102  SER D C   1 
ATOM   4106  O  O   . SER D  1 103 ? 175.838 157.015 40.746 1.00   44.76 ? 102  SER D O   1 
ATOM   4107  C  CB  . SER D  1 103 ? 176.934 159.418 41.912 1.00   47.38 ? 102  SER D CB  1 
ATOM   4108  O  OG  . SER D  1 103 ? 176.653 160.684 42.474 1.00   48.27 ? 102  SER D OG  1 
ATOM   4109  N  N   . VAL D  1 104 ? 176.733 155.958 42.529 1.00   43.04 ? 103  VAL D N   1 
ATOM   4110  C  CA  . VAL D  1 104 ? 176.751 154.657 41.865 1.00   41.89 ? 103  VAL D CA  1 
ATOM   4111  C  C   . VAL D  1 104 ? 175.510 153.864 42.278 1.00   40.20 ? 103  VAL D C   1 
ATOM   4112  O  O   . VAL D  1 104 ? 174.798 153.312 41.419 1.00   39.16 ? 103  VAL D O   1 
ATOM   4113  C  CB  . VAL D  1 104 ? 178.065 153.908 42.137 1.00   42.47 ? 103  VAL D CB  1 
ATOM   4114  C  CG1 . VAL D  1 104 ? 178.090 152.575 41.402 1.00   42.85 ? 103  VAL D CG1 1 
ATOM   4115  C  CG2 . VAL D  1 104 ? 179.250 154.773 41.691 1.00   44.24 ? 103  VAL D CG2 1 
ATOM   4116  N  N   . ILE D  1 105 ? 175.225 153.827 43.583 1.00   38.56 ? 104  ILE D N   1 
ATOM   4117  C  CA  . ILE D  1 105 ? 173.976 153.239 44.050 1.00   36.07 ? 104  ILE D CA  1 
ATOM   4118  C  C   . ILE D  1 105 ? 172.815 154.078 43.503 1.00   36.86 ? 104  ILE D C   1 
ATOM   4119  O  O   . ILE D  1 105 ? 172.988 155.238 43.126 1.00   38.38 ? 104  ILE D O   1 
ATOM   4120  C  CB  . ILE D  1 105 ? 173.880 153.128 45.602 1.00   34.10 ? 104  ILE D CB  1 
ATOM   4121  C  CG1 . ILE D  1 105 ? 173.974 154.493 46.286 1.00   33.80 ? 104  ILE D CG1 1 
ATOM   4122  C  CG2 . ILE D  1 105 ? 174.927 152.173 46.150 1.00   33.03 ? 104  ILE D CG2 1 
ATOM   4123  C  CD1 . ILE D  1 105 ? 173.488 154.482 47.716 1.00   32.72 ? 104  ILE D CD1 1 
ATOM   4124  N  N   . SER D  1 106 ? 171.634 153.483 43.455 1.00   35.69 ? 105  SER D N   1 
ATOM   4125  C  CA  . SER D  1 106 ? 170.439 154.211 43.065 1.00   36.00 ? 105  SER D CA  1 
ATOM   4126  C  C   . SER D  1 106 ? 169.220 153.576 43.719 1.00   35.09 ? 105  SER D C   1 
ATOM   4127  O  O   . SER D  1 106 ? 169.308 152.481 44.271 1.00   32.84 ? 105  SER D O   1 
ATOM   4128  C  CB  . SER D  1 106 ? 170.283 154.187 41.541 1.00   36.98 ? 105  SER D CB  1 
ATOM   4129  O  OG  . SER D  1 106 ? 169.213 155.015 41.141 1.00   37.73 ? 105  SER D OG  1 
ATOM   4130  N  N   . LEU D  1 107 ? 168.096 154.281 43.654 1.00   35.73 ? 106  LEU D N   1 
ATOM   4131  C  CA  . LEU D  1 107 ? 166.823 153.767 44.111 1.00   35.77 ? 106  LEU D CA  1 
ATOM   4132  C  C   . LEU D  1 107 ? 165.905 153.437 42.921 1.00   38.31 ? 106  LEU D C   1 
ATOM   4133  O  O   . LEU D  1 107 ? 164.728 153.169 43.120 1.00   39.20 ? 106  LEU D O   1 
ATOM   4134  C  CB  . LEU D  1 107 ? 166.158 154.762 45.060 1.00   34.65 ? 106  LEU D CB  1 
ATOM   4135  C  CG  . LEU D  1 107 ? 167.045 155.249 46.193 1.00   33.88 ? 106  LEU D CG  1 
ATOM   4136  C  CD1 . LEU D  1 107 ? 166.231 155.981 47.252 1.00   33.50 ? 106  LEU D CD1 1 
ATOM   4137  C  CD2 . LEU D  1 107 ? 167.801 154.087 46.800 1.00   32.66 ? 106  LEU D CD2 1 
ATOM   4138  N  N   . SER D  1 108 ? 166.465 153.455 41.702 1.00   41.25 ? 107  SER D N   1 
ATOM   4139  C  CA  . SER D  1 108 ? 165.845 152.894 40.477 1.00   42.53 ? 107  SER D CA  1 
ATOM   4140  C  C   . SER D  1 108 ? 166.925 152.284 39.548 1.00   41.78 ? 107  SER D C   1 
ATOM   4141  O  O   . SER D  1 108 ? 168.097 152.462 39.794 1.00   40.55 ? 107  SER D O   1 
ATOM   4142  C  CB  . SER D  1 108 ? 165.033 153.970 39.737 1.00   44.86 ? 107  SER D CB  1 
ATOM   4143  O  OG  . SER D  1 108 ? 165.575 155.265 39.965 1.00   49.48 ? 107  SER D OG  1 
ATOM   4144  N  N   . GLY D  1 109 ? 166.524 151.555 38.499 1.00   42.95 ? 108  GLY D N   1 
ATOM   4145  C  CA  . GLY D  1 109 ? 167.454 151.069 37.463 1.00   43.21 ? 108  GLY D CA  1 
ATOM   4146  C  C   . GLY D  1 109 ? 168.137 149.742 37.788 1.00   43.13 ? 108  GLY D C   1 
ATOM   4147  O  O   . GLY D  1 109 ? 167.732 149.039 38.697 1.00   39.53 ? 108  GLY D O   1 
ATOM   4148  N  N   . ASP D  1 110 ? 169.178 149.383 37.032 1.00   45.03 ? 109  ASP D N   1 
ATOM   4149  C  CA  . ASP D  1 110 ? 169.889 148.108 37.279 1.00   44.54 ? 109  ASP D CA  1 
ATOM   4150  C  C   . ASP D  1 110 ? 170.720 148.209 38.560 1.00   43.57 ? 109  ASP D C   1 
ATOM   4151  O  O   . ASP D  1 110 ? 171.005 147.189 39.207 1.00   42.35 ? 109  ASP D O   1 
ATOM   4152  C  CB  . ASP D  1 110 ? 170.782 147.701 36.086 1.00   46.15 ? 109  ASP D CB  1 
ATOM   4153  C  CG  . ASP D  1 110 ? 169.992 147.062 34.937 1.00   47.66 ? 109  ASP D CG  1 
ATOM   4154  O  OD1 . ASP D  1 110 ? 168.759 146.869 35.054 1.00   46.23 ? 109  ASP D OD1 1 
ATOM   4155  O  OD2 . ASP D  1 110 ? 170.617 146.752 33.901 1.00   50.36 ? 109  ASP D OD2 1 
ATOM   4156  N  N   . HIS D  1 111 ? 171.078 149.441 38.926 1.00   42.03 ? 110  HIS D N   1 
ATOM   4157  C  CA  . HIS D  1 111 ? 171.813 149.699 40.151 1.00   42.03 ? 110  HIS D CA  1 
ATOM   4158  C  C   . HIS D  1 111 ? 170.926 149.889 41.368 1.00   40.16 ? 110  HIS D C   1 
ATOM   4159  O  O   . HIS D  1 111 ? 171.437 150.120 42.473 1.00   38.25 ? 110  HIS D O   1 
ATOM   4160  C  CB  . HIS D  1 111 ? 172.778 150.881 39.945 1.00   43.24 ? 110  HIS D CB  1 
ATOM   4161  C  CG  . HIS D  1 111 ? 173.953 150.552 39.044 1.00   44.80 ? 110  HIS D CG  1 
ATOM   4162  N  ND1 . HIS D  1 111 ? 175.099 151.271 39.043 1.00   47.01 ? 110  HIS D ND1 1 
ATOM   4163  C  CD2 . HIS D  1 111 ? 174.141 149.518 38.125 1.00   46.14 ? 110  HIS D CD2 1 
ATOM   4164  C  CE1 . HIS D  1 111 ? 175.961 150.742 38.148 1.00   47.75 ? 110  HIS D CE1 1 
ATOM   4165  N  NE2 . HIS D  1 111 ? 175.377 149.667 37.590 1.00   48.34 ? 110  HIS D NE2 1 
ATOM   4166  N  N   . CYS D  1 112 ? 169.606 149.755 41.200 1.00   38.02 ? 111  CYS D N   1 
ATOM   4167  C  CA  . CYS D  1 112 ? 168.676 149.894 42.321 1.00   36.78 ? 111  CYS D CA  1 
ATOM   4168  C  C   . CYS D  1 112 ? 169.092 149.041 43.548 1.00   33.35 ? 111  CYS D C   1 
ATOM   4169  O  O   . CYS D  1 112 ? 169.462 147.873 43.409 1.00   32.05 ? 111  CYS D O   1 
ATOM   4170  C  CB  . CYS D  1 112 ? 167.260 149.512 41.891 1.00   38.20 ? 111  CYS D CB  1 
ATOM   4171  S  SG  . CYS D  1 112 ? 166.034 149.935 43.145 1.00   40.69 ? 111  CYS D SG  1 
ATOM   4172  N  N   . ILE D  1 113 ? 169.049 149.637 44.739 1.00   31.34 ? 112  ILE D N   1 
ATOM   4173  C  CA  . ILE D  1 113 ? 169.393 148.913 45.985 1.00   28.83 ? 112  ILE D CA  1 
ATOM   4174  C  C   . ILE D  1 113 ? 168.172 148.574 46.864 1.00   27.91 ? 112  ILE D C   1 
ATOM   4175  O  O   . ILE D  1 113 ? 168.317 147.936 47.917 1.00   27.05 ? 112  ILE D O   1 
ATOM   4176  C  CB  . ILE D  1 113 ? 170.488 149.630 46.787 1.00   27.58 ? 112  ILE D CB  1 
ATOM   4177  C  CG1 . ILE D  1 113 ? 170.031 150.998 47.290 1.00   27.46 ? 112  ILE D CG1 1 
ATOM   4178  C  CG2 . ILE D  1 113 ? 171.746 149.779 45.941 1.00   28.23 ? 112  ILE D CG2 1 
ATOM   4179  C  CD1 . ILE D  1 113 ? 171.040 151.650 48.225 1.00   26.30 ? 112  ILE D CD1 1 
ATOM   4180  N  N   . ILE D  1 114 ? 166.976 148.958 46.411 1.00   27.74 ? 113  ILE D N   1 
ATOM   4181  C  CA  . ILE D  1 114 ? 165.725 148.559 47.068 1.00   26.74 ? 113  ILE D CA  1 
ATOM   4182  C  C   . ILE D  1 114 ? 165.615 147.028 47.060 1.00   25.94 ? 113  ILE D C   1 
ATOM   4183  O  O   . ILE D  1 114 ? 165.810 146.384 46.036 1.00   25.86 ? 113  ILE D O   1 
ATOM   4184  C  CB  . ILE D  1 114 ? 164.474 149.150 46.367 1.00   27.85 ? 113  ILE D CB  1 
ATOM   4185  C  CG1 . ILE D  1 114 ? 164.491 150.690 46.351 1.00   28.83 ? 113  ILE D CG1 1 
ATOM   4186  C  CG2 . ILE D  1 114 ? 163.192 148.669 47.036 1.00   26.58 ? 113  ILE D CG2 1 
ATOM   4187  C  CD1 . ILE D  1 114 ? 164.735 151.306 47.716 1.00   29.80 ? 113  ILE D CD1 1 
ATOM   4188  N  N   . GLY D  1 115 ? 165.319 146.441 48.210 1.00   25.09 ? 114  GLY D N   1 
ATOM   4189  C  CA  . GLY D  1 115 ? 165.191 144.998 48.293 1.00   24.57 ? 114  GLY D CA  1 
ATOM   4190  C  C   . GLY D  1 115 ? 166.504 144.268 48.461 1.00   24.28 ? 114  GLY D C   1 
ATOM   4191  O  O   . GLY D  1 115 ? 166.530 143.036 48.438 1.00   25.02 ? 114  GLY D O   1 
ATOM   4192  N  N   . ARG D  1 116 ? 167.592 145.001 48.637 1.00   23.89 ? 115  ARG D N   1 
ATOM   4193  C  CA  . ARG D  1 116 ? 168.883 144.378 48.911 1.00   24.19 ? 115  ARG D CA  1 
ATOM   4194  C  C   . ARG D  1 116 ? 169.224 144.636 50.368 1.00   22.65 ? 115  ARG D C   1 
ATOM   4195  O  O   . ARG D  1 116 ? 168.392 145.158 51.089 1.00   22.52 ? 115  ARG D O   1 
ATOM   4196  C  CB  . ARG D  1 116 ? 169.933 144.897 47.920 1.00   25.46 ? 115  ARG D CB  1 
ATOM   4197  C  CG  . ARG D  1 116 ? 169.507 144.659 46.475 1.00   26.12 ? 115  ARG D CG  1 
ATOM   4198  C  CD  . ARG D  1 116 ? 170.590 144.989 45.473 1.00   27.99 ? 115  ARG D CD  1 
ATOM   4199  N  NE  . ARG D  1 116 ? 170.056 144.942 44.115 1.00   28.43 ? 115  ARG D NE  1 
ATOM   4200  C  CZ  . ARG D  1 116 ? 169.924 143.839 43.384 1.00   28.97 ? 115  ARG D CZ  1 
ATOM   4201  N  NH1 . ARG D  1 116 ? 170.299 142.652 43.842 1.00   28.47 ? 115  ARG D NH1 1 
ATOM   4202  N  NH2 . ARG D  1 116 ? 169.409 143.935 42.165 1.00   30.61 ? 115  ARG D NH2 1 
ATOM   4203  N  N   . THR D  1 117 ? 170.409 144.247 50.819 1.00   22.77 ? 116  THR D N   1 
ATOM   4204  C  CA  . THR D  1 117 ? 170.753 144.275 52.260 1.00   21.69 ? 116  THR D CA  1 
ATOM   4205  C  C   . THR D  1 117 ? 171.893 145.225 52.559 1.00   22.07 ? 116  THR D C   1 
ATOM   4206  O  O   . THR D  1 117 ? 172.963 145.113 51.954 1.00   23.30 ? 116  THR D O   1 
ATOM   4207  C  CB  . THR D  1 117 ? 171.133 142.879 52.790 1.00   21.45 ? 116  THR D CB  1 
ATOM   4208  O  OG1 . THR D  1 117 ? 170.022 141.987 52.614 1.00   21.03 ? 116  THR D OG1 1 
ATOM   4209  C  CG2 . THR D  1 117 ? 171.460 142.914 54.263 1.00   20.76 ? 116  THR D CG2 1 
ATOM   4210  N  N   . LEU D  1 118 ? 171.665 146.159 53.489 1.00   21.15 ? 117  LEU D N   1 
ATOM   4211  C  CA  . LEU D  1 118 ? 172.730 147.012 54.006 1.00   21.33 ? 117  LEU D CA  1 
ATOM   4212  C  C   . LEU D  1 118 ? 173.343 146.328 55.210 1.00   21.43 ? 117  LEU D C   1 
ATOM   4213  O  O   . LEU D  1 118 ? 172.610 145.833 56.102 1.00   21.26 ? 117  LEU D O   1 
ATOM   4214  C  CB  . LEU D  1 118 ? 172.171 148.371 54.393 1.00   21.50 ? 117  LEU D CB  1 
ATOM   4215  C  CG  . LEU D  1 118 ? 173.155 149.481 54.758 1.00   21.82 ? 117  LEU D CG  1 
ATOM   4216  C  CD1 . LEU D  1 118 ? 174.078 149.823 53.603 1.00   22.40 ? 117  LEU D CD1 1 
ATOM   4217  C  CD2 . LEU D  1 118 ? 172.377 150.707 55.215 1.00   22.00 ? 117  LEU D CD2 1 
ATOM   4218  N  N   . VAL D  1 119 ? 174.668 146.268 55.219 1.00   21.24 ? 118  VAL D N   1 
ATOM   4219  C  CA  . VAL D  1 119 ? 175.447 145.569 56.235 1.00   21.73 ? 118  VAL D CA  1 
ATOM   4220  C  C   . VAL D  1 119 ? 176.527 146.497 56.786 1.00   22.52 ? 118  VAL D C   1 
ATOM   4221  O  O   . VAL D  1 119 ? 177.198 147.208 56.022 1.00   23.86 ? 118  VAL D O   1 
ATOM   4222  C  CB  . VAL D  1 119 ? 176.215 144.361 55.658 1.00   22.10 ? 118  VAL D CB  1 
ATOM   4223  C  CG1 . VAL D  1 119 ? 177.015 143.660 56.753 1.00   21.95 ? 118  VAL D CG1 1 
ATOM   4224  C  CG2 . VAL D  1 119 ? 175.291 143.379 54.952 1.00   21.25 ? 118  VAL D CG2 1 
ATOM   4225  N  N   . VAL D  1 120 ? 176.677 146.490 58.105 1.00   22.56 ? 119  VAL D N   1 
ATOM   4226  C  CA  . VAL D  1 120 ? 177.800 147.106 58.779 1.00   22.96 ? 119  VAL D CA  1 
ATOM   4227  C  C   . VAL D  1 120 ? 178.685 146.018 59.384 1.00   24.37 ? 119  VAL D C   1 
ATOM   4228  O  O   . VAL D  1 120 ? 178.197 145.050 60.011 1.00   24.45 ? 119  VAL D O   1 
ATOM   4229  C  CB  . VAL D  1 120 ? 177.362 148.112 59.859 1.00   22.91 ? 119  VAL D CB  1 
ATOM   4230  C  CG1 . VAL D  1 120 ? 176.524 147.462 60.955 1.00   21.61 ? 119  VAL D CG1 1 
ATOM   4231  C  CG2 . VAL D  1 120 ? 178.584 148.823 60.445 1.00   23.14 ? 119  VAL D CG2 1 
ATOM   4232  N  N   . HIS D  1 121 ? 179.987 146.185 59.192 1.00   25.56 ? 120  HIS D N   1 
ATOM   4233  C  CA  . HIS D  1 121 ? 180.971 145.147 59.518 1.00   26.90 ? 120  HIS D CA  1 
ATOM   4234  C  C   . HIS D  1 121 ? 181.768 145.379 60.789 1.00   28.11 ? 120  HIS D C   1 
ATOM   4235  O  O   . HIS D  1 121 ? 181.825 146.488 61.355 1.00   26.25 ? 120  HIS D O   1 
ATOM   4236  C  CB  . HIS D  1 121 ? 181.941 144.995 58.359 1.00   28.02 ? 120  HIS D CB  1 
ATOM   4237  C  CG  . HIS D  1 121 ? 181.372 144.273 57.163 1.00   27.88 ? 120  HIS D CG  1 
ATOM   4238  N  ND1 . HIS D  1 121 ? 181.529 142.950 56.981 1.00   28.05 ? 120  HIS D ND1 1 
ATOM   4239  C  CD2 . HIS D  1 121 ? 180.651 144.742 56.062 1.00   27.64 ? 120  HIS D CD2 1 
ATOM   4240  C  CE1 . HIS D  1 121 ? 180.930 142.583 55.833 1.00   28.11 ? 120  HIS D CE1 1 
ATOM   4241  N  NE2 . HIS D  1 121 ? 180.390 143.680 55.272 1.00   27.91 ? 120  HIS D NE2 1 
ATOM   4242  N  N   . GLU D  1 122 ? 182.393 144.288 61.222 1.00   30.16 ? 121  GLU D N   1 
ATOM   4243  C  CA  . GLU D  1 122 ? 183.249 144.221 62.384 1.00   32.24 ? 121  GLU D CA  1 
ATOM   4244  C  C   . GLU D  1 122 ? 184.442 145.169 62.285 1.00   32.96 ? 121  GLU D C   1 
ATOM   4245  O  O   . GLU D  1 122 ? 184.698 145.913 63.215 1.00   32.13 ? 121  GLU D O   1 
ATOM   4246  C  CB  . GLU D  1 122 ? 183.764 142.776 62.515 1.00   34.82 ? 121  GLU D CB  1 
ATOM   4247  C  CG  . GLU D  1 122 ? 184.652 142.468 63.727 1.00   37.08 ? 121  GLU D CG  1 
ATOM   4248  C  CD  . GLU D  1 122 ? 185.352 141.113 63.609 1.00   39.95 ? 121  GLU D CD  1 
ATOM   4249  O  OE1 . GLU D  1 122 ? 185.289 140.454 62.538 1.00   38.94 ? 121  GLU D OE1 1 
ATOM   4250  O  OE2 . GLU D  1 122 ? 185.982 140.697 64.604 1.00   44.71 ? 121  GLU D OE2 1 
ATOM   4251  N  N   . LYS D  1 123 ? 185.159 145.117 61.158 1.00   34.33 ? 122  LYS D N   1 
ATOM   4252  C  CA  . LYS D  1 123 ? 186.444 145.785 61.002 1.00   36.04 ? 122  LYS D CA  1 
ATOM   4253  C  C   . LYS D  1 123 ? 186.350 146.868 59.941 1.00   36.55 ? 122  LYS D C   1 
ATOM   4254  O  O   . LYS D  1 123 ? 185.308 147.024 59.292 1.00   35.30 ? 122  LYS D O   1 
ATOM   4255  C  CB  . LYS D  1 123 ? 187.531 144.796 60.566 1.00   37.64 ? 122  LYS D CB  1 
ATOM   4256  C  CG  . LYS D  1 123 ? 187.760 143.622 61.490 1.00   39.76 ? 122  LYS D CG  1 
ATOM   4257  C  CD  . LYS D  1 123 ? 189.176 143.040 61.339 1.00   42.71 ? 122  LYS D CD  1 
ATOM   4258  C  CE  . LYS D  1 123 ? 189.244 141.786 60.472 1.00   44.37 ? 122  LYS D CE  1 
ATOM   4259  N  NZ  . LYS D  1 123 ? 189.102 140.531 61.280 1.00   45.70 ? 122  LYS D NZ  1 
ATOM   4260  N  N   . ALA D  1 124 ? 187.456 147.595 59.753 1.00   36.11 ? 123  ALA D N   1 
ATOM   4261  C  CA  . ALA D  1 124 ? 187.568 148.584 58.690 1.00   36.47 ? 123  ALA D CA  1 
ATOM   4262  C  C   . ALA D  1 124 ? 187.567 147.935 57.321 1.00   36.77 ? 123  ALA D C   1 
ATOM   4263  O  O   . ALA D  1 124 ? 188.130 146.861 57.126 1.00   36.62 ? 123  ALA D O   1 
ATOM   4264  C  CB  . ALA D  1 124 ? 188.847 149.400 58.849 1.00   37.34 ? 123  ALA D CB  1 
ATOM   4265  N  N   . ASP D  1 125 ? 186.927 148.612 56.375 1.00   37.35 ? 124  ASP D N   1 
ATOM   4266  C  CA  . ASP D  1 125 ? 187.049 148.302 54.956 1.00   38.10 ? 124  ASP D CA  1 
ATOM   4267  C  C   . ASP D  1 125 ? 188.347 148.981 54.519 1.00   40.12 ? 124  ASP D C   1 
ATOM   4268  O  O   . ASP D  1 125 ? 188.455 150.202 54.613 1.00   39.64 ? 124  ASP D O   1 
ATOM   4269  C  CB  . ASP D  1 125 ? 185.845 148.886 54.210 1.00   36.66 ? 124  ASP D CB  1 
ATOM   4270  C  CG  . ASP D  1 125 ? 185.777 148.466 52.753 1.00   38.99 ? 124  ASP D CG  1 
ATOM   4271  O  OD1 . ASP D  1 125 ? 186.853 148.182 52.163 1.00   40.94 ? 124  ASP D OD1 1 
ATOM   4272  O  OD2 . ASP D  1 125 ? 184.645 148.450 52.185 1.00   36.56 ? 124  ASP D OD2 1 
ATOM   4273  N  N   . ASP D  1 126 ? 189.321 148.191 54.059 1.00   41.88 ? 125  ASP D N   1 
ATOM   4274  C  CA  . ASP D  1 126 ? 190.605 148.735 53.568 1.00   44.22 ? 125  ASP D CA  1 
ATOM   4275  C  C   . ASP D  1 126 ? 190.476 149.334 52.158 1.00   44.66 ? 125  ASP D C   1 
ATOM   4276  O  O   . ASP D  1 126 ? 191.472 149.701 51.551 1.00   46.25 ? 125  ASP D O   1 
ATOM   4277  C  CB  . ASP D  1 126 ? 191.743 147.688 53.628 1.00   44.93 ? 125  ASP D CB  1 
ATOM   4278  C  CG  . ASP D  1 126 ? 191.560 146.536 52.636 1.00   45.88 ? 125  ASP D CG  1 
ATOM   4279  O  OD1 . ASP D  1 126 ? 190.884 146.713 51.596 1.00   46.06 ? 125  ASP D OD1 1 
ATOM   4280  O  OD2 . ASP D  1 126 ? 192.108 145.441 52.903 1.00   46.67 ? 125  ASP D OD2 1 
ATOM   4281  N  N   . LEU D  1 127 ? 189.240 149.406 51.656 1.00   43.52 ? 126  LEU D N   1 
ATOM   4282  C  CA  . LEU D  1 127 ? 188.897 150.023 50.381 1.00   43.21 ? 126  LEU D CA  1 
ATOM   4283  C  C   . LEU D  1 127 ? 189.564 149.319 49.195 1.00   45.68 ? 126  LEU D C   1 
ATOM   4284  O  O   . LEU D  1 127 ? 189.760 149.911 48.145 1.00   47.74 ? 126  LEU D O   1 
ATOM   4285  C  CB  . LEU D  1 127 ? 189.187 151.532 50.414 1.00   43.59 ? 126  LEU D CB  1 
ATOM   4286  C  CG  . LEU D  1 127 ? 188.539 152.310 51.572 1.00   42.19 ? 126  LEU D CG  1 
ATOM   4287  C  CD1 . LEU D  1 127 ? 188.767 153.814 51.454 1.00   41.55 ? 126  LEU D CD1 1 
ATOM   4288  C  CD2 . LEU D  1 127 ? 187.044 152.011 51.652 1.00   40.25 ? 126  LEU D CD2 1 
ATOM   4289  N  N   . GLY D  1 128 ? 189.883 148.044 49.365 1.00   47.12 ? 127  GLY D N   1 
ATOM   4290  C  CA  . GLY D  1 128 ? 190.441 147.246 48.295 1.00   50.27 ? 127  GLY D CA  1 
ATOM   4291  C  C   . GLY D  1 128 ? 191.886 147.552 47.961 1.00   55.35 ? 127  GLY D C   1 
ATOM   4292  O  O   . GLY D  1 128 ? 192.293 147.374 46.808 1.00   57.41 ? 127  GLY D O   1 
ATOM   4293  N  N   . LYS D  1 129 ? 192.659 148.006 48.956 1.00   57.47 ? 128  LYS D N   1 
ATOM   4294  C  CA  . LYS D  1 129 ? 194.077 148.354 48.763 1.00   60.78 ? 128  LYS D CA  1 
ATOM   4295  C  C   . LYS D  1 129 ? 194.956 147.551 49.710 1.00   62.36 ? 128  LYS D C   1 
ATOM   4296  O  O   . LYS D  1 129 ? 195.933 148.071 50.248 1.00   64.39 ? 128  LYS D O   1 
ATOM   4297  C  CB  . LYS D  1 129 ? 194.322 149.845 49.018 1.00   61.62 ? 128  LYS D CB  1 
ATOM   4298  C  CG  . LYS D  1 129 ? 193.246 150.795 48.506 1.00   61.90 ? 128  LYS D CG  1 
ATOM   4299  C  CD  . LYS D  1 129 ? 193.003 150.687 47.012 1.00   62.55 ? 128  LYS D CD  1 
ATOM   4300  C  CE  . LYS D  1 129 ? 191.994 151.735 46.580 1.00   62.20 ? 128  LYS D CE  1 
ATOM   4301  N  NZ  . LYS D  1 129 ? 191.464 151.458 45.223 1.00   63.51 ? 128  LYS D NZ  1 
ATOM   4302  N  N   . GLY D  1 130 ? 194.608 146.285 49.907 1.00   63.14 ? 129  GLY D N   1 
ATOM   4303  C  CA  . GLY D  1 130 ? 195.285 145.435 50.883 1.00   65.17 ? 129  GLY D CA  1 
ATOM   4304  C  C   . GLY D  1 130 ? 196.451 144.638 50.329 1.00   68.38 ? 129  GLY D C   1 
ATOM   4305  O  O   . GLY D  1 130 ? 197.282 144.151 51.092 1.00   70.80 ? 129  GLY D O   1 
ATOM   4306  N  N   . GLY D  1 131 ? 196.514 144.490 49.008 1.00   70.76 ? 130  GLY D N   1 
ATOM   4307  C  CA  . GLY D  1 131 ? 197.572 143.701 48.375 1.00   75.05 ? 130  GLY D CA  1 
ATOM   4308  C  C   . GLY D  1 131 ? 197.428 142.192 48.542 1.00   77.27 ? 130  GLY D C   1 
ATOM   4309  O  O   . GLY D  1 131 ? 198.416 141.455 48.443 1.00   76.55 ? 130  GLY D O   1 
ATOM   4310  N  N   . ASN D  1 132 ? 196.197 141.737 48.789 1.00   77.77 ? 131  ASN D N   1 
ATOM   4311  C  CA  . ASN D  1 132 ? 195.880 140.309 48.892 1.00   79.88 ? 131  ASN D CA  1 
ATOM   4312  C  C   . ASN D  1 132 ? 194.528 140.010 48.235 1.00   78.30 ? 131  ASN D C   1 
ATOM   4313  O  O   . ASN D  1 132 ? 193.753 140.932 47.972 1.00   76.42 ? 131  ASN D O   1 
ATOM   4314  C  CB  . ASN D  1 132 ? 195.865 139.874 50.359 1.00   80.27 ? 131  ASN D CB  1 
ATOM   4315  C  CG  . ASN D  1 132 ? 194.710 140.482 51.135 1.00   80.09 ? 131  ASN D CG  1 
ATOM   4316  O  OD1 . ASN D  1 132 ? 194.317 141.619 50.888 1.00   78.75 ? 131  ASN D OD1 1 
ATOM   4317  N  ND2 . ASN D  1 132 ? 194.158 139.723 52.077 1.00   80.02 ? 131  ASN D ND2 1 
ATOM   4318  N  N   . GLU D  1 133 ? 194.247 138.732 47.976 1.00   79.52 ? 132  GLU D N   1 
ATOM   4319  C  CA  . GLU D  1 133 ? 193.014 138.330 47.272 1.00   79.94 ? 132  GLU D CA  1 
ATOM   4320  C  C   . GLU D  1 133 ? 191.754 138.880 47.952 1.00   75.47 ? 132  GLU D C   1 
ATOM   4321  O  O   . GLU D  1 133 ? 190.874 139.436 47.287 1.00   70.70 ? 132  GLU D O   1 
ATOM   4322  C  CB  . GLU D  1 133 ? 192.918 136.797 47.164 1.00   82.71 ? 132  GLU D CB  1 
ATOM   4323  C  CG  . GLU D  1 133 ? 191.738 136.290 46.331 1.00   84.95 ? 132  GLU D CG  1 
ATOM   4324  C  CD  . GLU D  1 133 ? 191.388 134.830 46.603 1.00   87.26 ? 132  GLU D CD  1 
ATOM   4325  O  OE1 . GLU D  1 133 ? 192.322 134.021 46.779 1.00   91.31 ? 132  GLU D OE1 1 
ATOM   4326  O  OE2 . GLU D  1 133 ? 190.179 134.488 46.636 1.00   86.10 ? 132  GLU D OE2 1 
ATOM   4327  N  N   . GLU D  1 134 ? 191.689 138.727 49.276 1.00   75.00 ? 133  GLU D N   1 
ATOM   4328  C  CA  . GLU D  1 134 ? 190.505 139.116 50.066 1.00   72.83 ? 133  GLU D CA  1 
ATOM   4329  C  C   . GLU D  1 134 ? 190.175 140.608 49.986 1.00   70.52 ? 133  GLU D C   1 
ATOM   4330  O  O   . GLU D  1 134 ? 189.001 140.988 50.023 1.00   67.89 ? 133  GLU D O   1 
ATOM   4331  C  CB  . GLU D  1 134 ? 190.664 138.710 51.545 1.00   72.60 ? 133  GLU D CB  1 
ATOM   4332  C  CG  . GLU D  1 134 ? 189.824 137.512 51.960 1.00   73.62 ? 133  GLU D CG  1 
ATOM   4333  C  CD  . GLU D  1 134 ? 188.332 137.802 51.914 1.00   71.17 ? 133  GLU D CD  1 
ATOM   4334  O  OE1 . GLU D  1 134 ? 187.834 138.494 52.823 1.00   69.34 ? 133  GLU D OE1 1 
ATOM   4335  O  OE2 . GLU D  1 134 ? 187.660 137.339 50.969 1.00   72.39 ? 133  GLU D OE2 1 
ATOM   4336  N  N   . SER D  1 135 ? 191.209 141.443 49.888 1.00   67.32 ? 134  SER D N   1 
ATOM   4337  C  CA  . SER D  1 135 ? 191.027 142.888 49.791 1.00   65.16 ? 134  SER D CA  1 
ATOM   4338  C  C   . SER D  1 135 ? 190.217 143.268 48.557 1.00   64.35 ? 134  SER D C   1 
ATOM   4339  O  O   . SER D  1 135 ? 189.381 144.163 48.621 1.00   63.62 ? 134  SER D O   1 
ATOM   4340  C  CB  . SER D  1 135 ? 192.383 143.605 49.786 1.00   65.48 ? 134  SER D CB  1 
ATOM   4341  O  OG  . SER D  1 135 ? 192.245 144.985 49.520 1.00   63.39 ? 134  SER D OG  1 
ATOM   4342  N  N   . THR D  1 136 ? 190.444 142.576 47.445 1.00   64.41 ? 135  THR D N   1 
ATOM   4343  C  CA  . THR D  1 136 ? 189.742 142.887 46.197 1.00   63.59 ? 135  THR D CA  1 
ATOM   4344  C  C   . THR D  1 136 ? 188.340 142.266 46.117 1.00   62.44 ? 135  THR D C   1 
ATOM   4345  O  O   . THR D  1 136 ? 187.568 142.597 45.212 1.00   59.87 ? 135  THR D O   1 
ATOM   4346  C  CB  . THR D  1 136 ? 190.547 142.422 44.974 1.00   65.97 ? 135  THR D CB  1 
ATOM   4347  O  OG1 . THR D  1 136 ? 190.570 140.990 44.949 1.00   69.05 ? 135  THR D OG1 1 
ATOM   4348  C  CG2 . THR D  1 136 ? 191.989 142.972 45.015 1.00   66.95 ? 135  THR D CG2 1 
ATOM   4349  N  N   . LYS D  1 137 ? 188.017 141.368 47.049 1.00   62.69 ? 136  LYS D N   1 
ATOM   4350  C  CA  . LYS D  1 137 ? 186.674 140.798 47.130 1.00   63.57 ? 136  LYS D CA  1 
ATOM   4351  C  C   . LYS D  1 137 ? 185.819 141.532 48.170 1.00   60.23 ? 136  LYS D C   1 
ATOM   4352  O  O   . LYS D  1 137 ? 184.707 141.973 47.866 1.00   59.63 ? 136  LYS D O   1 
ATOM   4353  C  CB  . LYS D  1 137 ? 186.734 139.295 47.437 1.00   65.84 ? 136  LYS D CB  1 
ATOM   4354  C  CG  . LYS D  1 137 ? 187.509 138.498 46.396 1.00   71.05 ? 136  LYS D CG  1 
ATOM   4355  C  CD  . LYS D  1 137 ? 187.071 137.038 46.327 1.00   74.49 ? 136  LYS D CD  1 
ATOM   4356  C  CE  . LYS D  1 137 ? 187.284 136.304 47.644 1.00   74.62 ? 136  LYS D CE  1 
ATOM   4357  N  NZ  . LYS D  1 137 ? 187.477 134.840 47.446 1.00   75.33 ? 136  LYS D NZ  1 
ATOM   4358  N  N   . THR D  1 138 ? 186.349 141.682 49.383 1.00   56.52 ? 137  THR D N   1 
ATOM   4359  C  CA  . THR D  1 138 ? 185.555 142.153 50.518 1.00   53.86 ? 137  THR D CA  1 
ATOM   4360  C  C   . THR D  1 138 ? 186.119 143.343 51.302 1.00   52.66 ? 137  THR D C   1 
ATOM   4361  O  O   . THR D  1 138 ? 185.446 143.856 52.199 1.00   50.30 ? 137  THR D O   1 
ATOM   4362  C  CB  . THR D  1 138 ? 185.346 141.006 51.520 1.00   54.09 ? 137  THR D CB  1 
ATOM   4363  O  OG1 . THR D  1 138 ? 186.563 140.752 52.237 1.00   54.96 ? 137  THR D OG1 1 
ATOM   4364  C  CG2 . THR D  1 138 ? 184.903 139.735 50.799 1.00   55.81 ? 137  THR D CG2 1 
ATOM   4365  N  N   . GLY D  1 139 ? 187.349 143.768 51.005 1.00   51.46 ? 138  GLY D N   1 
ATOM   4366  C  CA  . GLY D  1 139 ? 187.972 144.867 51.753 1.00   49.13 ? 138  GLY D CA  1 
ATOM   4367  C  C   . GLY D  1 139 ? 188.487 144.480 53.133 1.00   47.04 ? 138  GLY D C   1 
ATOM   4368  O  O   . GLY D  1 139 ? 188.932 145.338 53.888 1.00   44.26 ? 138  GLY D O   1 
ATOM   4369  N  N   . ASN D  1 140 ? 188.426 143.184 53.451 1.00   47.78 ? 139  ASN D N   1 
ATOM   4370  C  CA  . ASN D  1 140 ? 188.848 142.646 54.747 1.00   47.88 ? 139  ASN D CA  1 
ATOM   4371  C  C   . ASN D  1 140 ? 188.092 143.235 55.934 1.00   44.72 ? 139  ASN D C   1 
ATOM   4372  O  O   . ASN D  1 140 ? 188.656 143.397 57.019 1.00   43.07 ? 139  ASN D O   1 
ATOM   4373  C  CB  . ASN D  1 140 ? 190.363 142.814 54.938 1.00   52.45 ? 139  ASN D CB  1 
ATOM   4374  C  CG  . ASN D  1 140 ? 191.158 141.978 53.967 1.00   56.29 ? 139  ASN D CG  1 
ATOM   4375  O  OD1 . ASN D  1 140 ? 191.340 140.772 54.173 1.00   57.62 ? 139  ASN D OD1 1 
ATOM   4376  N  ND2 . ASN D  1 140 ? 191.628 142.609 52.891 1.00   59.18 ? 139  ASN D ND2 1 
ATOM   4377  N  N   . ALA D  1 141 ? 186.801 143.504 55.740 1.00   41.69 ? 140  ALA D N   1 
ATOM   4378  C  CA  . ALA D  1 141 ? 186.002 144.170 56.765 1.00   39.25 ? 140  ALA D CA  1 
ATOM   4379  C  C   . ALA D  1 141 ? 185.488 143.212 57.831 1.00   37.80 ? 140  ALA D C   1 
ATOM   4380  O  O   . ALA D  1 141 ? 184.787 143.633 58.745 1.00   37.06 ? 140  ALA D O   1 
ATOM   4381  C  CB  . ALA D  1 141 ? 184.857 144.943 56.133 1.00   38.18 ? 140  ALA D CB  1 
ATOM   4382  N  N   . GLY D  1 142 ? 185.840 141.932 57.736 1.00   38.05 ? 141  GLY D N   1 
ATOM   4383  C  CA  . GLY D  1 142 ? 185.478 140.972 58.786 1.00   37.67 ? 141  GLY D CA  1 
ATOM   4384  C  C   . GLY D  1 142 ? 183.991 140.654 58.843 1.00   36.45 ? 141  GLY D C   1 
ATOM   4385  O  O   . GLY D  1 142 ? 183.275 140.810 57.854 1.00   36.19 ? 141  GLY D O   1 
ATOM   4386  N  N   . SER D  1 143 ? 183.520 140.215 60.010 1.00   35.85 ? 142  SER D N   1 
ATOM   4387  C  CA  . SER D  1 143 ? 182.172 139.634 60.123 1.00   34.91 ? 142  SER D CA  1 
ATOM   4388  C  C   . SER D  1 143 ? 181.077 140.688 59.932 1.00   32.30 ? 142  SER D C   1 
ATOM   4389  O  O   . SER D  1 143 ? 181.337 141.886 59.967 1.00   31.70 ? 142  SER D O   1 
ATOM   4390  C  CB  . SER D  1 143 ? 182.002 138.906 61.467 1.00   35.72 ? 142  SER D CB  1 
ATOM   4391  O  OG  . SER D  1 143 ? 181.796 139.832 62.519 1.00   36.10 ? 142  SER D OG  1 
ATOM   4392  N  N   . ARG D  1 144 ? 179.852 140.222 59.732 1.00   30.60 ? 143  ARG D N   1 
ATOM   4393  C  CA  . ARG D  1 144 ? 178.716 141.100 59.490 1.00   28.33 ? 143  ARG D CA  1 
ATOM   4394  C  C   . ARG D  1 144 ? 177.999 141.297 60.807 1.00   27.17 ? 143  ARG D C   1 
ATOM   4395  O  O   . ARG D  1 144 ? 177.392 140.375 61.313 1.00   26.69 ? 143  ARG D O   1 
ATOM   4396  C  CB  . ARG D  1 144 ? 177.780 140.471 58.456 1.00   27.60 ? 143  ARG D CB  1 
ATOM   4397  C  CG  . ARG D  1 144 ? 178.514 139.992 57.224 1.00   27.98 ? 143  ARG D CG  1 
ATOM   4398  C  CD  . ARG D  1 144 ? 177.601 139.431 56.136 1.00   27.85 ? 143  ARG D CD  1 
ATOM   4399  N  NE  . ARG D  1 144 ? 178.414 139.073 54.975 1.00   28.28 ? 143  ARG D NE  1 
ATOM   4400  C  CZ  . ARG D  1 144 ? 177.973 138.509 53.857 1.00   28.98 ? 143  ARG D CZ  1 
ATOM   4401  N  NH1 . ARG D  1 144 ? 176.695 138.209 53.703 1.00   29.00 ? 143  ARG D NH1 1 
ATOM   4402  N  NH2 . ARG D  1 144 ? 178.832 138.240 52.877 1.00   29.83 ? 143  ARG D NH2 1 
ATOM   4403  N  N   . LEU D  1 145 ? 178.051 142.506 61.359 1.00   26.25 ? 144  LEU D N   1 
ATOM   4404  C  CA  . LEU D  1 145 ? 177.580 142.715 62.720 1.00   25.31 ? 144  LEU D CA  1 
ATOM   4405  C  C   . LEU D  1 145 ? 176.083 142.953 62.774 1.00   24.40 ? 144  LEU D C   1 
ATOM   4406  O  O   . LEU D  1 145 ? 175.427 142.422 63.643 1.00   24.66 ? 144  LEU D O   1 
ATOM   4407  C  CB  . LEU D  1 145 ? 178.324 143.864 63.399 1.00   25.29 ? 144  LEU D CB  1 
ATOM   4408  C  CG  . LEU D  1 145 ? 179.807 143.649 63.700 1.00   26.33 ? 144  LEU D CG  1 
ATOM   4409  C  CD1 . LEU D  1 145 ? 180.314 144.797 64.552 1.00   27.00 ? 144  LEU D CD1 1 
ATOM   4410  C  CD2 . LEU D  1 145 ? 180.091 142.320 64.381 1.00   26.36 ? 144  LEU D CD2 1 
ATOM   4411  N  N   . ALA D  1 146 ? 175.562 143.791 61.877 1.00   23.92 ? 145  ALA D N   1 
ATOM   4412  C  CA  . ALA D  1 146 ? 174.116 144.004 61.731 1.00   23.16 ? 145  ALA D CA  1 
ATOM   4413  C  C   . ALA D  1 146 ? 173.768 144.280 60.273 1.00   22.69 ? 145  ALA D C   1 
ATOM   4414  O  O   . ALA D  1 146 ? 174.600 144.731 59.499 1.00   22.32 ? 145  ALA D O   1 
ATOM   4415  C  CB  . ALA D  1 146 ? 173.630 145.145 62.610 1.00   22.96 ? 145  ALA D CB  1 
ATOM   4416  N  N   . CYS D  1 147 ? 172.525 144.017 59.914 1.00   22.98 ? 146  CYS D N   1 
ATOM   4417  C  CA  . CYS D  1 147 ? 172.058 144.233 58.555 1.00   22.75 ? 146  CYS D CA  1 
ATOM   4418  C  C   . CYS D  1 147 ? 170.558 144.427 58.534 1.00   21.98 ? 146  CYS D C   1 
ATOM   4419  O  O   . CYS D  1 147 ? 169.898 144.158 59.508 1.00   23.16 ? 146  CYS D O   1 
ATOM   4420  C  CB  . CYS D  1 147 ? 172.408 143.034 57.690 1.00   23.55 ? 146  CYS D CB  1 
ATOM   4421  S  SG  . CYS D  1 147 ? 171.745 141.484 58.322 1.00   25.29 ? 146  CYS D SG  1 
ATOM   4422  N  N   . GLY D  1 148 ? 170.028 144.932 57.429 1.00   21.37 ? 147  GLY D N   1 
ATOM   4423  C  CA  . GLY D  1 148 ? 168.587 144.944 57.206 1.00   21.00 ? 147  GLY D CA  1 
ATOM   4424  C  C   . GLY D  1 148 ? 168.288 145.055 55.731 1.00   20.66 ? 147  GLY D C   1 
ATOM   4425  O  O   . GLY D  1 148 ? 169.152 145.429 54.928 1.00   20.87 ? 147  GLY D O   1 
ATOM   4426  N  N   . VAL D  1 149 ? 167.070 144.703 55.362 1.00   20.12 ? 148  VAL D N   1 
ATOM   4427  C  CA  . VAL D  1 149 ? 166.600 144.873 54.003 1.00   19.97 ? 148  VAL D CA  1 
ATOM   4428  C  C   . VAL D  1 149 ? 166.199 146.320 53.805 1.00   20.36 ? 148  VAL D C   1 
ATOM   4429  O  O   . VAL D  1 149 ? 165.511 146.907 54.631 1.00   20.69 ? 148  VAL D O   1 
ATOM   4430  C  CB  . VAL D  1 149 ? 165.416 143.929 53.696 1.00   19.75 ? 148  VAL D CB  1 
ATOM   4431  C  CG1 . VAL D  1 149 ? 165.035 143.965 52.217 1.00   19.59 ? 148  VAL D CG1 1 
ATOM   4432  C  CG2 . VAL D  1 149 ? 165.783 142.502 54.090 1.00   20.00 ? 148  VAL D CG2 1 
ATOM   4433  N  N   . ILE D  1 150 ? 166.635 146.896 52.696 1.00   21.40 ? 149  ILE D N   1 
ATOM   4434  C  CA  . ILE D  1 150 ? 166.328 148.267 52.362 1.00   21.91 ? 149  ILE D CA  1 
ATOM   4435  C  C   . ILE D  1 150 ? 164.929 148.344 51.753 1.00   22.87 ? 149  ILE D C   1 
ATOM   4436  O  O   . ILE D  1 150 ? 164.654 147.754 50.698 1.00   23.28 ? 149  ILE D O   1 
ATOM   4437  C  CB  . ILE D  1 150 ? 167.351 148.815 51.355 1.00   22.73 ? 149  ILE D CB  1 
ATOM   4438  C  CG1 . ILE D  1 150 ? 168.756 148.815 51.973 1.00   22.38 ? 149  ILE D CG1 1 
ATOM   4439  C  CG2 . ILE D  1 150 ? 166.965 150.240 50.920 1.00   23.06 ? 149  ILE D CG2 1 
ATOM   4440  C  CD1 . ILE D  1 150 ? 169.883 148.879 50.966 1.00   22.20 ? 149  ILE D CD1 1 
ATOM   4441  N  N   . GLY D  1 151 ? 164.039 149.067 52.416 1.00   23.28 ? 150  GLY D N   1 
ATOM   4442  C  CA  . GLY D  1 151 ? 162.647 149.138 51.995 1.00   24.20 ? 150  GLY D CA  1 
ATOM   4443  C  C   . GLY D  1 151 ? 162.251 150.497 51.435 1.00   25.27 ? 150  GLY D C   1 
ATOM   4444  O  O   . GLY D  1 151 ? 162.882 151.511 51.744 1.00   24.57 ? 150  GLY D O   1 
ATOM   4445  N  N   . ILE D  1 152 ? 161.201 150.508 50.610 1.00   25.86 ? 151  ILE D N   1 
ATOM   4446  C  CA  . ILE D  1 152 ? 160.584 151.767 50.151 1.00   27.41 ? 151  ILE D CA  1 
ATOM   4447  C  C   . ILE D  1 152 ? 159.980 152.521 51.345 1.00   28.39 ? 151  ILE D C   1 
ATOM   4448  O  O   . ILE D  1 152 ? 159.254 151.934 52.161 1.00   29.52 ? 151  ILE D O   1 
ATOM   4449  C  CB  . ILE D  1 152 ? 159.499 151.507 49.078 1.00   27.91 ? 151  ILE D CB  1 
ATOM   4450  C  CG1 . ILE D  1 152 ? 160.109 150.773 47.877 1.00   27.86 ? 151  ILE D CG1 1 
ATOM   4451  C  CG2 . ILE D  1 152 ? 158.865 152.819 48.629 1.00   28.28 ? 151  ILE D CG2 1 
ATOM   4452  C  CD1 . ILE D  1 152 ? 159.102 150.371 46.803 1.00   28.73 ? 151  ILE D CD1 1 
ATOM   4453  N  N   . ALA D  1 153 ? 160.303 153.806 51.469 1.00   30.61 ? 152  ALA D N   1 
ATOM   4454  C  CA  . ALA D  1 153 ? 159.790 154.665 52.562 1.00   31.41 ? 152  ALA D CA  1 
ATOM   4455  C  C   . ALA D  1 153 ? 158.853 155.756 52.050 1.00   34.05 ? 152  ALA D C   1 
ATOM   4456  O  O   . ALA D  1 153 ? 158.911 156.142 50.883 1.00   33.20 ? 152  ALA D O   1 
ATOM   4457  C  CB  . ALA D  1 153 ? 160.940 155.307 53.316 1.00   30.17 ? 152  ALA D CB  1 
ATOM   4458  N  N   . GLN D  1 154 ? 158.001 156.251 52.941 1.00   36.17 ? 153  GLN D N   1 
ATOM   4459  C  CA  . GLN D  1 154 ? 157.076 157.319 52.602 1.00   40.38 ? 153  GLN D CA  1 
ATOM   4460  C  C   . GLN D  1 154 ? 157.825 158.646 52.490 1.00   42.86 ? 153  GLN D C   1 
ATOM   4461  O  O   . GLN D  1 154 ? 157.490 159.428 51.611 1.00   46.12 ? 153  GLN D O   1 
ATOM   4462  C  CB  . GLN D  1 154 ? 155.987 157.452 53.660 1.00   41.47 ? 153  GLN D CB  1 
ATOM   4463  C  CG  . GLN D  1 154 ? 154.849 158.385 53.268 1.00   43.28 ? 153  GLN D CG  1 
ATOM   4464  C  CD  . GLN D  1 154 ? 153.855 158.554 54.394 1.00   44.09 ? 153  GLN D CD  1 
ATOM   4465  O  OE1 . GLN D  1 154 ? 154.254 158.746 55.534 1.00   46.29 ? 153  GLN D OE1 1 
ATOM   4466  N  NE2 . GLN D  1 154 ? 152.565 158.467 54.090 1.00   43.66 ? 153  GLN D NE2 1 
ATOM   4467  O  OXT . GLN D  1 154 ? 158.747 158.960 53.261 1.00   43.84 ? 153  GLN D OXT 1 
ATOM   4468  N  N   . ALA E  1 2   ? 136.486 99.438  36.698 1.00   52.12 ? 1    ALA E N   1 
ATOM   4469  C  CA  . ALA E  1 2   ? 136.660 98.975  38.113 1.00   52.03 ? 1    ALA E CA  1 
ATOM   4470  C  C   . ALA E  1 2   ? 137.050 97.495  38.147 1.00   48.96 ? 1    ALA E C   1 
ATOM   4471  O  O   . ALA E  1 2   ? 136.253 96.641  37.794 1.00   49.33 ? 1    ALA E O   1 
ATOM   4472  C  CB  . ALA E  1 2   ? 135.379 99.207  38.918 1.00   51.42 ? 1    ALA E CB  1 
ATOM   4473  N  N   . THR E  1 3   ? 138.280 97.205  38.561 1.00   46.57 ? 2    THR E N   1 
ATOM   4474  C  CA  . THR E  1 3   ? 138.741 95.829  38.694 1.00   44.18 ? 2    THR E CA  1 
ATOM   4475  C  C   . THR E  1 3   ? 138.634 95.337  40.142 1.00   41.34 ? 2    THR E C   1 
ATOM   4476  O  O   . THR E  1 3   ? 138.801 94.142  40.409 1.00   39.45 ? 2    THR E O   1 
ATOM   4477  C  CB  . THR E  1 3   ? 140.200 95.679  38.218 1.00   45.84 ? 2    THR E CB  1 
ATOM   4478  O  OG1 . THR E  1 3   ? 141.052 96.529  38.996 1.00   45.97 ? 2    THR E OG1 1 
ATOM   4479  C  CG2 . THR E  1 3   ? 140.328 96.046  36.744 1.00   47.35 ? 2    THR E CG2 1 
ATOM   4480  N  N   . LYS E  1 4   ? 138.366 96.249  41.078 1.00   38.77 ? 3    LYS E N   1 
ATOM   4481  C  CA  . LYS E  1 4   ? 138.196 95.873  42.475 1.00   36.86 ? 3    LYS E CA  1 
ATOM   4482  C  C   . LYS E  1 4   ? 137.010 96.595  43.118 1.00   34.48 ? 3    LYS E C   1 
ATOM   4483  O  O   . LYS E  1 4   ? 136.730 97.765  42.827 1.00   32.69 ? 3    LYS E O   1 
ATOM   4484  C  CB  . LYS E  1 4   ? 139.473 96.147  43.265 1.00   39.12 ? 3    LYS E CB  1 
ATOM   4485  C  CG  . LYS E  1 4   ? 140.628 95.227  42.906 1.00   41.42 ? 3    LYS E CG  1 
ATOM   4486  C  CD  . LYS E  1 4   ? 141.906 95.585  43.643 1.00   43.07 ? 3    LYS E CD  1 
ATOM   4487  C  CE  . LYS E  1 4   ? 142.950 94.486  43.494 1.00   46.16 ? 3    LYS E CE  1 
ATOM   4488  N  NZ  . LYS E  1 4   ? 144.304 94.902  43.981 1.00   49.14 ? 3    LYS E NZ  1 
ATOM   4489  N  N   . ALA E  1 5   ? 136.322 95.863  43.987 1.00   30.97 ? 4    ALA E N   1 
ATOM   4490  C  CA  . ALA E  1 5   ? 135.187 96.368  44.725 1.00   29.06 ? 4    ALA E CA  1 
ATOM   4491  C  C   . ALA E  1 5   ? 135.179 95.702  46.109 1.00   27.63 ? 4    ALA E C   1 
ATOM   4492  O  O   . ALA E  1 5   ? 135.846 94.683  46.320 1.00   26.97 ? 4    ALA E O   1 
ATOM   4493  C  CB  . ALA E  1 5   ? 133.904 96.082  43.958 1.00   29.00 ? 4    ALA E CB  1 
ATOM   4494  N  N   . VAL E  1 6   ? 134.459 96.296  47.060 1.00   26.69 ? 5    VAL E N   1 
ATOM   4495  C  CA  . VAL E  1 6   ? 134.405 95.777  48.429 1.00   25.22 ? 5    VAL E CA  1 
ATOM   4496  C  C   . VAL E  1 6   ? 133.028 96.048  49.019 1.00   25.02 ? 5    VAL E C   1 
ATOM   4497  O  O   . VAL E  1 6   ? 132.325 96.947  48.566 1.00   25.27 ? 5    VAL E O   1 
ATOM   4498  C  CB  . VAL E  1 6   ? 135.525 96.401  49.303 1.00   25.51 ? 5    VAL E CB  1 
ATOM   4499  C  CG1 . VAL E  1 6   ? 135.346 97.918  49.469 1.00   25.00 ? 5    VAL E CG1 1 
ATOM   4500  C  CG2 . VAL E  1 6   ? 135.634 95.701  50.656 1.00   24.63 ? 5    VAL E CG2 1 
ATOM   4501  N  N   . CYS E  1 7   ? 132.652 95.273  50.029 1.00   24.39 ? 6    CYS E N   1 
ATOM   4502  C  CA  . CYS E  1 7   ? 131.362 95.421  50.706 1.00   24.16 ? 6    CYS E CA  1 
ATOM   4503  C  C   . CYS E  1 7   ? 131.488 95.056  52.187 1.00   23.61 ? 6    CYS E C   1 
ATOM   4504  O  O   . CYS E  1 7   ? 132.010 93.977  52.544 1.00   22.14 ? 6    CYS E O   1 
ATOM   4505  C  CB  . CYS E  1 7   ? 130.338 94.507  50.036 1.00   25.29 ? 6    CYS E CB  1 
ATOM   4506  S  SG  . CYS E  1 7   ? 128.674 94.680  50.700 1.00   27.12 ? 6    CYS E SG  1 
ATOM   4507  N  N   . VAL E  1 8   ? 131.040 95.965  53.047 1.00   23.40 ? 7    VAL E N   1 
ATOM   4508  C  CA  . VAL E  1 8   ? 131.013 95.736  54.473 1.00   24.13 ? 7    VAL E CA  1 
ATOM   4509  C  C   . VAL E  1 8   ? 129.590 95.334  54.795 1.00   24.97 ? 7    VAL E C   1 
ATOM   4510  O  O   . VAL E  1 8   ? 128.663 96.106  54.540 1.00   25.59 ? 7    VAL E O   1 
ATOM   4511  C  CB  . VAL E  1 8   ? 131.385 96.998  55.276 1.00   24.34 ? 7    VAL E CB  1 
ATOM   4512  C  CG1 . VAL E  1 8   ? 131.216 96.744  56.777 1.00   24.54 ? 7    VAL E CG1 1 
ATOM   4513  C  CG2 . VAL E  1 8   ? 132.809 97.431  54.955 1.00   23.93 ? 7    VAL E CG2 1 
ATOM   4514  N  N   . LEU E  1 9   ? 129.420 94.130  55.332 1.00   25.33 ? 8    LEU E N   1 
ATOM   4515  C  CA  . LEU E  1 9   ? 128.099 93.592  55.649 1.00   26.32 ? 8    LEU E CA  1 
ATOM   4516  C  C   . LEU E  1 9   ? 127.835 93.805  57.133 1.00   26.93 ? 8    LEU E C   1 
ATOM   4517  O  O   . LEU E  1 9   ? 128.655 93.442  57.989 1.00   25.63 ? 8    LEU E O   1 
ATOM   4518  C  CB  . LEU E  1 9   ? 128.005 92.078  55.351 1.00   26.75 ? 8    LEU E CB  1 
ATOM   4519  C  CG  . LEU E  1 9   ? 128.347 91.489  53.981 1.00   27.53 ? 8    LEU E CG  1 
ATOM   4520  C  CD1 . LEU E  1 9   ? 128.508 89.975  54.125 1.00   29.29 ? 8    LEU E CD1 1 
ATOM   4521  C  CD2 . LEU E  1 9   ? 127.255 91.773  52.950 1.00   27.88 ? 8    LEU E CD2 1 
ATOM   4522  N  N   . LYS E  1 10  ? 126.676 94.384  57.412 1.00   28.38 ? 9    LYS E N   1 
ATOM   4523  C  CA  . LYS E  1 10  ? 126.192 94.614  58.772 1.00   30.59 ? 9    LYS E CA  1 
ATOM   4524  C  C   . LYS E  1 10  ? 124.675 94.513  58.773 1.00   30.46 ? 9    LYS E C   1 
ATOM   4525  O  O   . LYS E  1 10  ? 124.018 94.734  57.744 1.00   29.26 ? 9    LYS E O   1 
ATOM   4526  C  CB  . LYS E  1 10  ? 126.621 95.996  59.279 1.00   32.23 ? 9    LYS E CB  1 
ATOM   4527  C  CG  . LYS E  1 10  ? 128.116 96.127  59.544 1.00   33.86 ? 9    LYS E CG  1 
ATOM   4528  C  CD  . LYS E  1 10  ? 128.487 97.568  59.864 1.00   36.56 ? 9    LYS E CD  1 
ATOM   4529  C  CE  . LYS E  1 10  ? 129.996 97.787  60.020 1.00   37.19 ? 9    LYS E CE  1 
ATOM   4530  N  NZ  . LYS E  1 10  ? 130.342 99.190  59.605 1.00   38.46 ? 9    LYS E NZ  1 
ATOM   4531  N  N   . GLY E  1 11  ? 124.119 94.191  59.932 1.00   32.60 ? 10   GLY E N   1 
ATOM   4532  C  CA  . GLY E  1 11  ? 122.661 94.126  60.090 1.00   34.65 ? 10   GLY E CA  1 
ATOM   4533  C  C   . GLY E  1 11  ? 122.234 94.622  61.460 1.00   36.61 ? 10   GLY E C   1 
ATOM   4534  O  O   . GLY E  1 11  ? 122.979 95.351  62.117 1.00   37.30 ? 10   GLY E O   1 
ATOM   4535  N  N   . ASP E  1 12  ? 121.040 94.202  61.883 1.00   39.47 ? 11   ASP E N   1 
ATOM   4536  C  CA  . ASP E  1 12  ? 120.483 94.533  63.206 1.00   42.23 ? 11   ASP E CA  1 
ATOM   4537  C  C   . ASP E  1 12  ? 121.009 93.610  64.307 1.00   42.00 ? 11   ASP E C   1 
ATOM   4538  O  O   . ASP E  1 12  ? 121.026 93.988  65.480 1.00   43.85 ? 11   ASP E O   1 
ATOM   4539  C  CB  . ASP E  1 12  ? 118.949 94.436  63.177 1.00   44.86 ? 11   ASP E CB  1 
ATOM   4540  C  CG  . ASP E  1 12  ? 118.295 95.576  62.389 1.00   47.87 ? 11   ASP E CG  1 
ATOM   4541  O  OD1 . ASP E  1 12  ? 118.928 96.645  62.200 1.00   46.74 ? 11   ASP E OD1 1 
ATOM   4542  O  OD2 . ASP E  1 12  ? 117.127 95.399  61.973 1.00   51.06 ? 11   ASP E OD2 1 
ATOM   4543  N  N   . GLY E  1 13  ? 121.415 92.398  63.933 1.00   39.18 ? 12   GLY E N   1 
ATOM   4544  C  CA  . GLY E  1 13  ? 121.978 91.454  64.882 1.00   38.09 ? 12   GLY E CA  1 
ATOM   4545  C  C   . GLY E  1 13  ? 123.501 91.426  64.824 1.00   36.36 ? 12   GLY E C   1 
ATOM   4546  O  O   . GLY E  1 13  ? 124.141 92.404  64.394 1.00   34.53 ? 12   GLY E O   1 
ATOM   4547  N  N   . PRO E  1 14  ? 124.096 90.291  65.227 1.00   34.70 ? 13   PRO E N   1 
ATOM   4548  C  CA  . PRO E  1 14  ? 125.547 90.153  65.320 1.00   34.18 ? 13   PRO E CA  1 
ATOM   4549  C  C   . PRO E  1 14  ? 126.270 89.799  64.011 1.00   32.86 ? 13   PRO E C   1 
ATOM   4550  O  O   . PRO E  1 14  ? 127.495 89.669  64.016 1.00   33.77 ? 13   PRO E O   1 
ATOM   4551  C  CB  . PRO E  1 14  ? 125.705 89.008  66.322 1.00   35.07 ? 13   PRO E CB  1 
ATOM   4552  C  CG  . PRO E  1 14  ? 124.489 88.146  66.102 1.00   34.77 ? 13   PRO E CG  1 
ATOM   4553  C  CD  . PRO E  1 14  ? 123.404 89.029  65.552 1.00   35.03 ? 13   PRO E CD  1 
ATOM   4554  N  N   . VAL E  1 15  ? 125.541 89.640  62.907 1.00   31.58 ? 14   VAL E N   1 
ATOM   4555  C  CA  . VAL E  1 15  ? 126.157 89.195  61.662 1.00   30.31 ? 14   VAL E CA  1 
ATOM   4556  C  C   . VAL E  1 15  ? 126.922 90.328  60.975 1.00   30.90 ? 14   VAL E C   1 
ATOM   4557  O  O   . VAL E  1 15  ? 126.358 91.389  60.658 1.00   29.98 ? 14   VAL E O   1 
ATOM   4558  C  CB  . VAL E  1 15  ? 125.130 88.580  60.678 1.00   29.62 ? 14   VAL E CB  1 
ATOM   4559  C  CG1 . VAL E  1 15  ? 125.815 88.220  59.370 1.00   26.87 ? 14   VAL E CG1 1 
ATOM   4560  C  CG2 . VAL E  1 15  ? 124.439 87.354  61.301 1.00   29.23 ? 14   VAL E CG2 1 
ATOM   4561  N  N   . GLN E  1 16  ? 128.213 90.095  60.744 1.00   31.14 ? 15   GLN E N   1 
ATOM   4562  C  CA  . GLN E  1 16  ? 129.036 91.095  60.092 1.00   31.86 ? 15   GLN E CA  1 
ATOM   4563  C  C   . GLN E  1 16  ? 130.243 90.507  59.343 1.00   30.18 ? 15   GLN E C   1 
ATOM   4564  O  O   . GLN E  1 16  ? 130.800 89.464  59.725 1.00   28.47 ? 15   GLN E O   1 
ATOM   4565  C  CB  . GLN E  1 16  ? 129.491 92.134  61.112 1.00   34.24 ? 15   GLN E CB  1 
ATOM   4566  C  CG  . GLN E  1 16  ? 130.559 91.646  62.062 1.00   37.37 ? 15   GLN E CG  1 
ATOM   4567  C  CD  . GLN E  1 16  ? 130.578 92.422  63.367 1.00   41.49 ? 15   GLN E CD  1 
ATOM   4568  O  OE1 . GLN E  1 16  ? 129.533 92.815  63.882 1.00   46.31 ? 15   GLN E OE1 1 
ATOM   4569  N  NE2 . GLN E  1 16  ? 131.767 92.624  63.919 1.00   42.82 ? 15   GLN E NE2 1 
ATOM   4570  N  N   . GLY E  1 17  ? 130.639 91.196  58.277 1.00   27.69 ? 16   GLY E N   1 
ATOM   4571  C  CA  . GLY E  1 17  ? 131.760 90.752  57.483 1.00   26.58 ? 16   GLY E CA  1 
ATOM   4572  C  C   . GLY E  1 17  ? 132.163 91.689  56.364 1.00   25.75 ? 16   GLY E C   1 
ATOM   4573  O  O   . GLY E  1 17  ? 131.545 92.735  56.142 1.00   25.08 ? 16   GLY E O   1 
ATOM   4574  N  N   . ILE E  1 18  ? 133.225 91.286  55.675 1.00   24.29 ? 17   ILE E N   1 
ATOM   4575  C  CA  . ILE E  1 18  ? 133.832 92.042  54.618 1.00   24.21 ? 17   ILE E CA  1 
ATOM   4576  C  C   . ILE E  1 18  ? 133.999 91.084  53.449 1.00   24.05 ? 17   ILE E C   1 
ATOM   4577  O  O   . ILE E  1 18  ? 134.603 89.992  53.581 1.00   24.35 ? 17   ILE E O   1 
ATOM   4578  C  CB  . ILE E  1 18  ? 135.203 92.597  55.051 1.00   24.59 ? 17   ILE E CB  1 
ATOM   4579  C  CG1 . ILE E  1 18  ? 135.032 93.599  56.198 1.00   24.80 ? 17   ILE E CG1 1 
ATOM   4580  C  CG2 . ILE E  1 18  ? 135.925 93.219  53.864 1.00   24.57 ? 17   ILE E CG2 1 
ATOM   4581  C  CD1 . ILE E  1 18  ? 136.341 94.164  56.737 1.00   25.85 ? 17   ILE E CD1 1 
ATOM   4582  N  N   . ILE E  1 19  ? 133.431 91.464  52.320 1.00   23.08 ? 18   ILE E N   1 
ATOM   4583  C  CA  . ILE E  1 19  ? 133.547 90.691  51.109 1.00   23.11 ? 18   ILE E CA  1 
ATOM   4584  C  C   . ILE E  1 19  ? 134.235 91.531  50.030 1.00   24.28 ? 18   ILE E C   1 
ATOM   4585  O  O   . ILE E  1 19  ? 133.792 92.652  49.721 1.00   24.27 ? 18   ILE E O   1 
ATOM   4586  C  CB  . ILE E  1 19  ? 132.165 90.238  50.630 1.00   22.15 ? 18   ILE E CB  1 
ATOM   4587  C  CG1 . ILE E  1 19  ? 131.509 89.323  51.685 1.00   22.42 ? 18   ILE E CG1 1 
ATOM   4588  C  CG2 . ILE E  1 19  ? 132.273 89.562  49.270 1.00   22.12 ? 18   ILE E CG2 1 
ATOM   4589  C  CD1 . ILE E  1 19  ? 132.209 87.982  51.906 1.00   22.52 ? 18   ILE E CD1 1 
ATOM   4590  N  N   . ASN E  1 20  ? 135.300 90.968  49.471 1.00   24.94 ? 19   ASN E N   1 
ATOM   4591  C  CA  . ASN E  1 20  ? 136.070 91.563  48.375 1.00   26.70 ? 19   ASN E CA  1 
ATOM   4592  C  C   . ASN E  1 20  ? 135.679 90.979  47.021 1.00   26.76 ? 19   ASN E C   1 
ATOM   4593  O  O   . ASN E  1 20  ? 135.280 89.812  46.927 1.00   26.51 ? 19   ASN E O   1 
ATOM   4594  C  CB  . ASN E  1 20  ? 137.560 91.298  48.570 1.00   28.03 ? 19   ASN E CB  1 
ATOM   4595  C  CG  . ASN E  1 20  ? 138.045 91.689  49.943 1.00   29.55 ? 19   ASN E CG  1 
ATOM   4596  O  OD1 . ASN E  1 20  ? 138.316 90.823  50.792 1.00   32.16 ? 19   ASN E OD1 1 
ATOM   4597  N  ND2 . ASN E  1 20  ? 138.138 92.987  50.185 1.00   28.96 ? 19   ASN E ND2 1 
ATOM   4598  N  N   . PHE E  1 21  ? 135.829 91.797  45.984 1.00   27.43 ? 20   PHE E N   1 
ATOM   4599  C  CA  . PHE E  1 21  ? 135.527 91.422  44.599 1.00   28.49 ? 20   PHE E CA  1 
ATOM   4600  C  C   . PHE E  1 21  ? 136.690 91.830  43.723 1.00   30.57 ? 20   PHE E C   1 
ATOM   4601  O  O   . PHE E  1 21  ? 137.222 92.932  43.882 1.00   30.74 ? 20   PHE E O   1 
ATOM   4602  C  CB  . PHE E  1 21  ? 134.288 92.155  44.084 1.00   27.29 ? 20   PHE E CB  1 
ATOM   4603  C  CG  . PHE E  1 21  ? 133.038 91.839  44.832 1.00   26.29 ? 20   PHE E CG  1 
ATOM   4604  C  CD1 . PHE E  1 21  ? 132.758 92.465  46.048 1.00   26.44 ? 20   PHE E CD1 1 
ATOM   4605  C  CD2 . PHE E  1 21  ? 132.132 90.926  44.325 1.00   26.07 ? 20   PHE E CD2 1 
ATOM   4606  C  CE1 . PHE E  1 21  ? 131.590 92.183  46.731 1.00   25.45 ? 20   PHE E CE1 1 
ATOM   4607  C  CE2 . PHE E  1 21  ? 130.967 90.626  45.009 1.00   25.53 ? 20   PHE E CE2 1 
ATOM   4608  C  CZ  . PHE E  1 21  ? 130.695 91.249  46.212 1.00   25.83 ? 20   PHE E CZ  1 
ATOM   4609  N  N   . GLU E  1 22  ? 137.078 90.957  42.792 1.00   32.61 ? 21   GLU E N   1 
ATOM   4610  C  CA  . GLU E  1 22  ? 138.124 91.290  41.847 1.00   35.10 ? 21   GLU E CA  1 
ATOM   4611  C  C   . GLU E  1 22  ? 137.829 90.749  40.441 1.00   36.42 ? 21   GLU E C   1 
ATOM   4612  O  O   . GLU E  1 22  ? 137.425 89.596  40.279 1.00   37.67 ? 21   GLU E O   1 
ATOM   4613  C  CB  . GLU E  1 22  ? 139.479 90.803  42.342 1.00   37.43 ? 21   GLU E CB  1 
ATOM   4614  C  CG  . GLU E  1 22  ? 140.608 91.230  41.414 1.00   42.15 ? 21   GLU E CG  1 
ATOM   4615  C  CD  . GLU E  1 22  ? 141.972 90.788  41.884 1.00   45.89 ? 21   GLU E CD  1 
ATOM   4616  O  OE1 . GLU E  1 22  ? 142.332 89.613  41.664 1.00   53.36 ? 21   GLU E OE1 1 
ATOM   4617  O  OE2 . GLU E  1 22  ? 142.700 91.630  42.444 1.00   50.81 ? 21   GLU E OE2 1 
ATOM   4618  N  N   . GLN E  1 23  ? 138.043 91.590  39.435 1.00   37.50 ? 22   GLN E N   1 
ATOM   4619  C  CA  . GLN E  1 23  ? 137.860 91.212  38.038 1.00   40.23 ? 22   GLN E CA  1 
ATOM   4620  C  C   . GLN E  1 23  ? 138.979 91.843  37.214 1.00   44.13 ? 22   GLN E C   1 
ATOM   4621  O  O   . GLN E  1 23  ? 138.955 93.045  36.957 1.00   46.27 ? 22   GLN E O   1 
ATOM   4622  C  CB  . GLN E  1 23  ? 136.492 91.696  37.545 1.00   38.98 ? 22   GLN E CB  1 
ATOM   4623  C  CG  . GLN E  1 23  ? 136.033 91.103  36.223 1.00   39.05 ? 22   GLN E CG  1 
ATOM   4624  C  CD  . GLN E  1 23  ? 134.690 91.654  35.782 1.00   38.85 ? 22   GLN E CD  1 
ATOM   4625  O  OE1 . GLN E  1 23  ? 134.389 92.812  36.022 1.00   40.09 ? 22   GLN E OE1 1 
ATOM   4626  N  NE2 . GLN E  1 23  ? 133.863 90.816  35.170 1.00   38.94 ? 22   GLN E NE2 1 
ATOM   4627  N  N   . LYS E  1 24  ? 139.964 91.048  36.806 1.00   47.90 ? 23   LYS E N   1 
ATOM   4628  C  CA  . LYS E  1 24  ? 141.113 91.612  36.070 1.00   52.61 ? 23   LYS E CA  1 
ATOM   4629  C  C   . LYS E  1 24  ? 140.886 91.742  34.561 1.00   54.32 ? 23   LYS E C   1 
ATOM   4630  O  O   . LYS E  1 24  ? 141.560 92.544  33.907 1.00   56.59 ? 23   LYS E O   1 
ATOM   4631  C  CB  . LYS E  1 24  ? 142.440 90.885  36.377 1.00   55.25 ? 23   LYS E CB  1 
ATOM   4632  C  CG  . LYS E  1 24  ? 142.421 89.363  36.402 1.00   57.10 ? 23   LYS E CG  1 
ATOM   4633  C  CD  . LYS E  1 24  ? 143.594 88.834  37.221 1.00   59.69 ? 23   LYS E CD  1 
ATOM   4634  C  CE  . LYS E  1 24  ? 143.413 89.117  38.713 1.00   60.86 ? 23   LYS E CE  1 
ATOM   4635  N  NZ  . LYS E  1 24  ? 144.574 89.839  39.308 1.00   61.48 ? 23   LYS E NZ  1 
ATOM   4636  N  N   . GLU E  1 25  ? 139.938 90.972  34.023 1.00   53.66 ? 24   GLU E N   1 
ATOM   4637  C  CA  . GLU E  1 25  ? 139.568 91.044  32.608 1.00   55.13 ? 24   GLU E CA  1 
ATOM   4638  C  C   . GLU E  1 25  ? 138.166 91.631  32.499 1.00   54.21 ? 24   GLU E C   1 
ATOM   4639  O  O   . GLU E  1 25  ? 137.286 91.242  33.264 1.00   52.10 ? 24   GLU E O   1 
ATOM   4640  C  CB  . GLU E  1 25  ? 139.586 89.642  31.972 1.00   56.21 ? 24   GLU E CB  1 
ATOM   4641  C  CG  . GLU E  1 25  ? 140.911 88.888  32.064 0.50   57.15 ? 24   GLU E CG  1 
ATOM   4642  C  CD  . GLU E  1 25  ? 141.949 89.352  31.057 0.50   59.39 ? 24   GLU E CD  1 
ATOM   4643  O  OE1 . GLU E  1 25  ? 141.577 89.757  29.932 0.50   60.07 ? 24   GLU E OE1 1 
ATOM   4644  O  OE2 . GLU E  1 25  ? 143.153 89.296  31.390 0.50   60.50 ? 24   GLU E OE2 1 
ATOM   4645  N  N   . SER E  1 26  ? 137.963 92.518  31.521 1.00   54.61 ? 25   SER E N   1 
ATOM   4646  C  CA  . SER E  1 26  ? 136.769 93.384  31.415 1.00   57.54 ? 25   SER E CA  1 
ATOM   4647  C  C   . SER E  1 26  ? 135.414 92.723  31.651 1.00   57.67 ? 25   SER E C   1 
ATOM   4648  O  O   . SER E  1 26  ? 134.537 93.312  32.313 1.00   59.04 ? 25   SER E O   1 
ATOM   4649  C  CB  . SER E  1 26  ? 136.717 94.072  30.043 1.00   59.31 ? 25   SER E CB  1 
ATOM   4650  O  OG  . SER E  1 26  ? 137.878 94.844  29.820 1.00   61.98 ? 25   SER E OG  1 
ATOM   4651  N  N   . ASN E  1 27  ? 135.215 91.545  31.067 1.00   56.31 ? 26   ASN E N   1 
ATOM   4652  C  CA  . ASN E  1 27  ? 134.032 90.747  31.387 1.00   56.22 ? 26   ASN E CA  1 
ATOM   4653  C  C   . ASN E  1 27  ? 134.410 89.288  31.645 1.00   52.78 ? 26   ASN E C   1 
ATOM   4654  O  O   . ASN E  1 27  ? 133.710 88.366  31.247 1.00   53.77 ? 26   ASN E O   1 
ATOM   4655  C  CB  . ASN E  1 27  ? 132.948 90.901  30.310 1.00   59.69 ? 26   ASN E CB  1 
ATOM   4656  C  CG  . ASN E  1 27  ? 131.544 91.063  30.908 1.00   62.08 ? 26   ASN E CG  1 
ATOM   4657  O  OD1 . ASN E  1 27  ? 130.877 90.076  31.260 1.00   63.23 ? 26   ASN E OD1 1 
ATOM   4658  N  ND2 . ASN E  1 27  ? 131.089 92.316  31.024 1.00   59.95 ? 26   ASN E ND2 1 
ATOM   4659  N  N   . GLY E  1 28  ? 135.533 89.110  32.332 1.00   50.44 ? 27   GLY E N   1 
ATOM   4660  C  CA  . GLY E  1 28  ? 135.994 87.800  32.781 1.00   50.25 ? 27   GLY E CA  1 
ATOM   4661  C  C   . GLY E  1 28  ? 135.418 87.472  34.152 1.00   48.03 ? 27   GLY E C   1 
ATOM   4662  O  O   . GLY E  1 28  ? 134.570 88.217  34.677 1.00   45.45 ? 27   GLY E O   1 
ATOM   4663  N  N   . PRO E  1 29  ? 135.881 86.362  34.756 1.00   47.24 ? 28   PRO E N   1 
ATOM   4664  C  CA  . PRO E  1 29  ? 135.310 85.923  36.025 1.00   44.32 ? 28   PRO E CA  1 
ATOM   4665  C  C   . PRO E  1 29  ? 135.593 86.904  37.175 1.00   41.77 ? 28   PRO E C   1 
ATOM   4666  O  O   . PRO E  1 29  ? 136.602 87.632  37.150 1.00   41.87 ? 28   PRO E O   1 
ATOM   4667  C  CB  . PRO E  1 29  ? 135.996 84.576  36.265 1.00   45.76 ? 28   PRO E CB  1 
ATOM   4668  C  CG  . PRO E  1 29  ? 137.298 84.689  35.549 1.00   47.46 ? 28   PRO E CG  1 
ATOM   4669  C  CD  . PRO E  1 29  ? 137.017 85.519  34.338 1.00   48.21 ? 28   PRO E CD  1 
ATOM   4670  N  N   . VAL E  1 30  ? 134.685 86.939  38.151 1.00   38.30 ? 29   VAL E N   1 
ATOM   4671  C  CA  . VAL E  1 30  ? 134.860 87.768  39.347 1.00   36.09 ? 29   VAL E CA  1 
ATOM   4672  C  C   . VAL E  1 30  ? 135.171 86.838  40.513 1.00   35.29 ? 29   VAL E C   1 
ATOM   4673  O  O   . VAL E  1 30  ? 134.412 85.904  40.806 1.00   35.68 ? 29   VAL E O   1 
ATOM   4674  C  CB  . VAL E  1 30  ? 133.615 88.622  39.678 1.00   34.77 ? 29   VAL E CB  1 
ATOM   4675  C  CG1 . VAL E  1 30  ? 133.888 89.530  40.868 1.00   33.29 ? 29   VAL E CG1 1 
ATOM   4676  C  CG2 . VAL E  1 30  ? 133.185 89.458  38.480 1.00   34.97 ? 29   VAL E CG2 1 
ATOM   4677  N  N   . LYS E  1 31  ? 136.307 87.084  41.151 1.00   34.43 ? 30   LYS E N   1 
ATOM   4678  C  CA  . LYS E  1 31  ? 136.694 86.389  42.366 1.00   33.46 ? 30   LYS E CA  1 
ATOM   4679  C  C   . LYS E  1 31  ? 136.035 87.128  43.538 1.00   31.06 ? 30   LYS E C   1 
ATOM   4680  O  O   . LYS E  1 31  ? 136.204 88.350  43.695 1.00   30.33 ? 30   LYS E O   1 
ATOM   4681  C  CB  . LYS E  1 31  ? 138.222 86.398  42.476 1.00   35.85 ? 30   LYS E CB  1 
ATOM   4682  C  CG  . LYS E  1 31  ? 138.840 85.824  43.743 1.00   37.38 ? 30   LYS E CG  1 
ATOM   4683  C  CD  . LYS E  1 31  ? 140.355 86.055  43.727 1.00   40.17 ? 30   LYS E CD  1 
ATOM   4684  C  CE  . LYS E  1 31  ? 141.021 85.785  45.071 1.00   41.05 ? 30   LYS E CE  1 
ATOM   4685  N  NZ  . LYS E  1 31  ? 140.712 84.411  45.552 1.00   41.85 ? 30   LYS E NZ  1 
ATOM   4686  N  N   . VAL E  1 32  ? 135.280 86.378  44.337 1.00   28.55 ? 31   VAL E N   1 
ATOM   4687  C  CA  . VAL E  1 32  ? 134.569 86.893  45.508 1.00   27.46 ? 31   VAL E CA  1 
ATOM   4688  C  C   . VAL E  1 32  ? 135.055 86.154  46.747 1.00   27.97 ? 31   VAL E C   1 
ATOM   4689  O  O   . VAL E  1 32  ? 134.948 84.924  46.849 1.00   28.21 ? 31   VAL E O   1 
ATOM   4690  C  CB  . VAL E  1 32  ? 133.043 86.678  45.404 1.00   26.47 ? 31   VAL E CB  1 
ATOM   4691  C  CG1 . VAL E  1 32  ? 132.333 87.278  46.615 1.00   25.75 ? 31   VAL E CG1 1 
ATOM   4692  C  CG2 . VAL E  1 32  ? 132.492 87.229  44.096 1.00   25.91 ? 31   VAL E CG2 1 
ATOM   4693  N  N   . TRP E  1 33  ? 135.597 86.892  47.698 1.00   27.74 ? 32   TRP E N   1 
ATOM   4694  C  CA  . TRP E  1 33  ? 136.127 86.260  48.878 1.00   28.18 ? 32   TRP E CA  1 
ATOM   4695  C  C   . TRP E  1 33  ? 136.163 87.192  50.027 1.00   27.46 ? 32   TRP E C   1 
ATOM   4696  O  O   . TRP E  1 33  ? 136.167 88.420  49.866 1.00   27.46 ? 32   TRP E O   1 
ATOM   4697  C  CB  . TRP E  1 33  ? 137.525 85.719  48.617 1.00   28.77 ? 32   TRP E CB  1 
ATOM   4698  C  CG  . TRP E  1 33  ? 138.594 86.770  48.733 1.00   29.45 ? 32   TRP E CG  1 
ATOM   4699  C  CD1 . TRP E  1 33  ? 139.438 86.997  49.807 1.00   29.80 ? 32   TRP E CD1 1 
ATOM   4700  C  CD2 . TRP E  1 33  ? 138.941 87.803  47.747 1.00   30.31 ? 32   TRP E CD2 1 
ATOM   4701  N  NE1 . TRP E  1 33  ? 140.267 88.057  49.555 1.00   31.85 ? 32   TRP E NE1 1 
ATOM   4702  C  CE2 . TRP E  1 33  ? 140.027 88.576  48.331 1.00   30.85 ? 32   TRP E CE2 1 
ATOM   4703  C  CE3 . TRP E  1 33  ? 138.481 88.137  46.484 1.00   30.92 ? 32   TRP E CE3 1 
ATOM   4704  C  CZ2 . TRP E  1 33  ? 140.618 89.636  47.666 1.00   32.37 ? 32   TRP E CZ2 1 
ATOM   4705  C  CZ3 . TRP E  1 33  ? 139.094 89.204  45.806 1.00   31.95 ? 32   TRP E CZ3 1 
ATOM   4706  C  CH2 . TRP E  1 33  ? 140.134 89.938  46.388 1.00   32.43 ? 32   TRP E CH2 1 
ATOM   4707  N  N   . GLY E  1 34  ? 136.212 86.599  51.208 1.00   27.05 ? 33   GLY E N   1 
ATOM   4708  C  CA  . GLY E  1 34  ? 136.186 87.350  52.450 1.00   26.92 ? 33   GLY E CA  1 
ATOM   4709  C  C   . GLY E  1 34  ? 135.693 86.447  53.552 1.00   26.95 ? 33   GLY E C   1 
ATOM   4710  O  O   . GLY E  1 34  ? 135.810 85.210  53.462 1.00   26.72 ? 33   GLY E O   1 
ATOM   4711  N  N   . SER E  1 35  ? 135.141 87.061  54.585 1.00   26.63 ? 34   SER E N   1 
ATOM   4712  C  CA  . SER E  1 35  ? 134.728 86.354  55.768 1.00   27.47 ? 34   SER E CA  1 
ATOM   4713  C  C   . SER E  1 35  ? 133.487 87.014  56.370 1.00   26.73 ? 34   SER E C   1 
ATOM   4714  O  O   . SER E  1 35  ? 133.316 88.246  56.274 1.00   26.11 ? 34   SER E O   1 
ATOM   4715  C  CB  . SER E  1 35  ? 135.893 86.340  56.774 1.00   29.35 ? 34   SER E CB  1 
ATOM   4716  O  OG  . SER E  1 35  ? 135.665 85.355  57.765 1.00   31.94 ? 34   SER E OG  1 
ATOM   4717  N  N   . ILE E  1 36  ? 132.609 86.191  56.955 1.00   25.68 ? 35   ILE E N   1 
ATOM   4718  C  CA  . ILE E  1 36  ? 131.397 86.666  57.638 1.00   25.17 ? 35   ILE E CA  1 
ATOM   4719  C  C   . ILE E  1 36  ? 131.302 85.932  58.983 1.00   26.46 ? 35   ILE E C   1 
ATOM   4720  O  O   . ILE E  1 36  ? 131.466 84.686  59.053 1.00   27.55 ? 35   ILE E O   1 
ATOM   4721  C  CB  . ILE E  1 36  ? 130.110 86.422  56.807 1.00   24.68 ? 35   ILE E CB  1 
ATOM   4722  C  CG1 . ILE E  1 36  ? 130.276 86.934  55.373 1.00   24.28 ? 35   ILE E CG1 1 
ATOM   4723  C  CG2 . ILE E  1 36  ? 128.892 87.080  57.468 1.00   24.55 ? 35   ILE E CG2 1 
ATOM   4724  C  CD1 . ILE E  1 36  ? 129.140 86.589  54.435 1.00   23.23 ? 35   ILE E CD1 1 
ATOM   4725  N  N   . LYS E  1 37  ? 131.056 86.683  60.049 1.00   25.96 ? 36   LYS E N   1 
ATOM   4726  C  CA  . LYS E  1 37  ? 130.942 86.116  61.376 1.00   26.74 ? 36   LYS E CA  1 
ATOM   4727  C  C   . LYS E  1 37  ? 129.578 86.407  62.010 1.00   27.00 ? 36   LYS E C   1 
ATOM   4728  O  O   . LYS E  1 37  ? 128.810 87.221  61.511 1.00   26.72 ? 36   LYS E O   1 
ATOM   4729  C  CB  . LYS E  1 37  ? 132.085 86.603  62.270 1.00   28.06 ? 36   LYS E CB  1 
ATOM   4730  C  CG  . LYS E  1 37  ? 131.993 88.037  62.737 1.00   28.66 ? 36   LYS E CG  1 
ATOM   4731  C  CD  . LYS E  1 37  ? 133.227 88.417  63.555 1.00   30.05 ? 36   LYS E CD  1 
ATOM   4732  C  CE  . LYS E  1 37  ? 133.176 89.890  63.944 1.00   30.79 ? 36   LYS E CE  1 
ATOM   4733  N  NZ  . LYS E  1 37  ? 134.450 90.354  64.561 1.00   32.21 ? 36   LYS E NZ  1 
ATOM   4734  N  N   . GLY E  1 38  ? 129.289 85.715  63.110 1.00   27.84 ? 37   GLY E N   1 
ATOM   4735  C  CA  . GLY E  1 38  ? 128.042 85.896  63.853 1.00   28.45 ? 37   GLY E CA  1 
ATOM   4736  C  C   . GLY E  1 38  ? 126.860 85.112  63.313 1.00   28.46 ? 37   GLY E C   1 
ATOM   4737  O  O   . GLY E  1 38  ? 125.705 85.374  63.702 1.00   28.98 ? 37   GLY E O   1 
ATOM   4738  N  N   . LEU E  1 39  ? 127.137 84.157  62.424 1.00   27.12 ? 38   LEU E N   1 
ATOM   4739  C  CA  . LEU E  1 39  ? 126.091 83.359  61.795 1.00   27.20 ? 38   LEU E CA  1 
ATOM   4740  C  C   . LEU E  1 39  ? 125.777 82.118  62.619 1.00   27.49 ? 38   LEU E C   1 
ATOM   4741  O  O   . LEU E  1 39  ? 126.634 81.623  63.346 1.00   27.75 ? 38   LEU E O   1 
ATOM   4742  C  CB  . LEU E  1 39  ? 126.508 82.922  60.378 1.00   26.88 ? 38   LEU E CB  1 
ATOM   4743  C  CG  . LEU E  1 39  ? 126.636 84.031  59.310 1.00   26.47 ? 38   LEU E CG  1 
ATOM   4744  C  CD1 . LEU E  1 39  ? 127.577 83.586  58.191 1.00   24.94 ? 38   LEU E CD1 1 
ATOM   4745  C  CD2 . LEU E  1 39  ? 125.271 84.444  58.750 1.00   26.27 ? 38   LEU E CD2 1 
ATOM   4746  N  N   . THR E  1 40  ? 124.536 81.642  62.514 1.00   27.79 ? 39   THR E N   1 
ATOM   4747  C  CA  . THR E  1 40  ? 124.196 80.282  62.913 1.00   27.85 ? 39   THR E CA  1 
ATOM   4748  C  C   . THR E  1 40  ? 124.959 79.315  61.987 1.00   27.53 ? 39   THR E C   1 
ATOM   4749  O  O   . THR E  1 40  ? 125.109 79.559  60.773 1.00   27.33 ? 39   THR E O   1 
ATOM   4750  C  CB  . THR E  1 40  ? 122.678 79.999  62.812 1.00   28.01 ? 39   THR E CB  1 
ATOM   4751  O  OG1 . THR E  1 40  ? 122.224 80.243  61.469 1.00   26.92 ? 39   THR E OG1 1 
ATOM   4752  C  CG2 . THR E  1 40  ? 121.879 80.894  63.828 1.00   28.67 ? 39   THR E CG2 1 
ATOM   4753  N  N   . GLU E  1 41  ? 125.445 78.227  62.554 1.00   27.56 ? 40   GLU E N   1 
ATOM   4754  C  CA  . GLU E  1 41  ? 126.162 77.219  61.780 1.00   27.30 ? 40   GLU E CA  1 
ATOM   4755  C  C   . GLU E  1 41  ? 125.303 76.695  60.625 1.00   26.35 ? 40   GLU E C   1 
ATOM   4756  O  O   . GLU E  1 41  ? 124.078 76.582  60.748 1.00   27.65 ? 40   GLU E O   1 
ATOM   4757  C  CB  . GLU E  1 41  ? 126.631 76.077  62.702 1.00   28.06 ? 40   GLU E CB  1 
ATOM   4758  C  CG  . GLU E  1 41  ? 125.529 75.182  63.245 1.00   28.93 ? 40   GLU E CG  1 
ATOM   4759  C  CD  . GLU E  1 41  ? 126.054 74.134  64.243 1.00   29.98 ? 40   GLU E CD  1 
ATOM   4760  O  OE1 . GLU E  1 41  ? 127.293 73.988  64.402 1.00   29.87 ? 40   GLU E OE1 1 
ATOM   4761  O  OE2 . GLU E  1 41  ? 125.224 73.429  64.853 1.00   30.61 ? 40   GLU E OE2 1 
ATOM   4762  N  N   . GLY E  1 42  ? 125.936 76.437  59.488 1.00   24.42 ? 41   GLY E N   1 
ATOM   4763  C  CA  . GLY E  1 42  ? 125.233 75.881  58.330 1.00   24.39 ? 41   GLY E CA  1 
ATOM   4764  C  C   . GLY E  1 42  ? 125.136 76.812  57.145 1.00   23.56 ? 41   GLY E C   1 
ATOM   4765  O  O   . GLY E  1 42  ? 125.895 77.792  57.053 1.00   23.61 ? 41   GLY E O   1 
ATOM   4766  N  N   . LEU E  1 43  ? 124.208 76.516  56.239 1.00   22.65 ? 42   LEU E N   1 
ATOM   4767  C  CA  . LEU E  1 43  ? 124.142 77.221  54.943 1.00   22.83 ? 42   LEU E CA  1 
ATOM   4768  C  C   . LEU E  1 43  ? 123.375 78.540  54.986 1.00   23.39 ? 42   LEU E C   1 
ATOM   4769  O  O   . LEU E  1 43  ? 122.319 78.622  55.597 1.00   24.40 ? 42   LEU E O   1 
ATOM   4770  C  CB  . LEU E  1 43  ? 123.499 76.333  53.865 1.00   22.27 ? 42   LEU E CB  1 
ATOM   4771  C  CG  . LEU E  1 43  ? 124.448 75.327  53.220 1.00   21.60 ? 42   LEU E CG  1 
ATOM   4772  C  CD1 . LEU E  1 43  ? 124.999 74.344  54.247 1.00   21.27 ? 42   LEU E CD1 1 
ATOM   4773  C  CD2 . LEU E  1 43  ? 123.751 74.624  52.072 1.00   21.91 ? 42   LEU E CD2 1 
ATOM   4774  N  N   . HIS E  1 44  ? 123.862 79.535  54.253 1.00   23.50 ? 43   HIS E N   1 
ATOM   4775  C  CA  . HIS E  1 44  ? 123.181 80.819  54.154 1.00   23.48 ? 43   HIS E CA  1 
ATOM   4776  C  C   . HIS E  1 44  ? 123.151 81.344  52.752 1.00   23.86 ? 43   HIS E C   1 
ATOM   4777  O  O   . HIS E  1 44  ? 124.195 81.450  52.073 1.00   23.28 ? 43   HIS E O   1 
ATOM   4778  C  CB  . HIS E  1 44  ? 123.851 81.825  55.068 1.00   23.70 ? 43   HIS E CB  1 
ATOM   4779  C  CG  . HIS E  1 44  ? 123.735 81.473  56.531 1.00   24.07 ? 43   HIS E CG  1 
ATOM   4780  N  ND1 . HIS E  1 44  ? 122.681 81.859  57.291 1.00   24.60 ? 43   HIS E ND1 1 
ATOM   4781  C  CD2 . HIS E  1 44  ? 124.569 80.714  57.362 1.00   24.68 ? 43   HIS E CD2 1 
ATOM   4782  C  CE1 . HIS E  1 44  ? 122.849 81.408  58.549 1.00   25.55 ? 43   HIS E CE1 1 
ATOM   4783  N  NE2 . HIS E  1 44  ? 124.001 80.692  58.593 1.00   25.00 ? 43   HIS E NE2 1 
ATOM   4784  N  N   . GLY E  1 45  ? 121.946 81.689  52.303 1.00   23.48 ? 44   GLY E N   1 
ATOM   4785  C  CA  . GLY E  1 45  ? 121.770 82.375  51.049 1.00   23.89 ? 44   GLY E CA  1 
ATOM   4786  C  C   . GLY E  1 45  ? 122.638 83.611  50.942 1.00   23.71 ? 44   GLY E C   1 
ATOM   4787  O  O   . GLY E  1 45  ? 122.866 84.317  51.916 1.00   23.22 ? 44   GLY E O   1 
ATOM   4788  N  N   . PHE E  1 46  ? 123.115 83.852  49.734 1.00   24.24 ? 45   PHE E N   1 
ATOM   4789  C  CA  . PHE E  1 46  ? 124.106 84.869  49.454 1.00   24.75 ? 45   PHE E CA  1 
ATOM   4790  C  C   . PHE E  1 46  ? 123.813 85.434  48.059 1.00   25.16 ? 45   PHE E C   1 
ATOM   4791  O  O   . PHE E  1 46  ? 124.041 84.767  47.053 1.00   24.61 ? 45   PHE E O   1 
ATOM   4792  C  CB  . PHE E  1 46  ? 125.467 84.191  49.508 1.00   24.00 ? 45   PHE E CB  1 
ATOM   4793  C  CG  . PHE E  1 46  ? 126.640 85.119  49.517 1.00   23.47 ? 45   PHE E CG  1 
ATOM   4794  C  CD1 . PHE E  1 46  ? 126.845 86.001  50.557 1.00   24.16 ? 45   PHE E CD1 1 
ATOM   4795  C  CD2 . PHE E  1 46  ? 127.609 85.020  48.537 1.00   23.78 ? 45   PHE E CD2 1 
ATOM   4796  C  CE1 . PHE E  1 46  ? 127.973 86.813  50.593 1.00   23.58 ? 45   PHE E CE1 1 
ATOM   4797  C  CE2 . PHE E  1 46  ? 128.738 85.813  48.562 1.00   23.30 ? 45   PHE E CE2 1 
ATOM   4798  C  CZ  . PHE E  1 46  ? 128.920 86.713  49.586 1.00   23.72 ? 45   PHE E CZ  1 
ATOM   4799  N  N   . HIS E  1 47  ? 123.280 86.651  48.016 1.00   26.31 ? 46   HIS E N   1 
ATOM   4800  C  CA  . HIS E  1 47  ? 122.739 87.243  46.775 1.00   27.44 ? 46   HIS E CA  1 
ATOM   4801  C  C   . HIS E  1 47  ? 123.108 88.684  46.602 1.00   27.51 ? 46   HIS E C   1 
ATOM   4802  O  O   . HIS E  1 47  ? 123.256 89.421  47.591 1.00   26.82 ? 46   HIS E O   1 
ATOM   4803  C  CB  . HIS E  1 47  ? 121.226 87.208  46.776 1.00   29.11 ? 46   HIS E CB  1 
ATOM   4804  C  CG  . HIS E  1 47  ? 120.635 85.878  47.141 1.00   30.28 ? 46   HIS E CG  1 
ATOM   4805  N  ND1 . HIS E  1 47  ? 119.763 85.742  48.145 1.00   31.25 ? 46   HIS E ND1 1 
ATOM   4806  C  CD2 . HIS E  1 47  ? 120.804 84.614  46.585 1.00   30.55 ? 46   HIS E CD2 1 
ATOM   4807  C  CE1 . HIS E  1 47  ? 119.393 84.455  48.245 1.00   32.69 ? 46   HIS E CE1 1 
ATOM   4808  N  NE2 . HIS E  1 47  ? 120.031 83.764  47.282 1.00   32.25 ? 46   HIS E NE2 1 
ATOM   4809  N  N   . VAL E  1 48  ? 123.244 89.109  45.345 1.00   28.21 ? 47   VAL E N   1 
ATOM   4810  C  CA  . VAL E  1 48  ? 123.266 90.537  45.044 1.00   28.32 ? 47   VAL E CA  1 
ATOM   4811  C  C   . VAL E  1 48  ? 121.831 90.964  44.748 1.00   29.62 ? 47   VAL E C   1 
ATOM   4812  O  O   . VAL E  1 48  ? 121.154 90.401  43.856 1.00   30.56 ? 47   VAL E O   1 
ATOM   4813  C  CB  . VAL E  1 48  ? 124.190 90.906  43.858 1.00   28.84 ? 47   VAL E CB  1 
ATOM   4814  C  CG1 . VAL E  1 48  ? 124.149 92.406  43.608 1.00   27.47 ? 47   VAL E CG1 1 
ATOM   4815  C  CG2 . VAL E  1 48  ? 125.630 90.429  44.117 1.00   27.95 ? 47   VAL E CG2 1 
ATOM   4816  N  N   . HIS E  1 49  ? 121.366 91.936  45.524 1.00   29.14 ? 48   HIS E N   1 
ATOM   4817  C  CA  . HIS E  1 49  ? 120.066 92.535  45.326 1.00   30.54 ? 48   HIS E CA  1 
ATOM   4818  C  C   . HIS E  1 49  ? 120.181 93.803  44.535 1.00   31.03 ? 48   HIS E C   1 
ATOM   4819  O  O   . HIS E  1 49  ? 121.203 94.506  44.593 1.00   29.98 ? 48   HIS E O   1 
ATOM   4820  C  CB  . HIS E  1 49  ? 119.404 92.814  46.664 1.00   30.82 ? 48   HIS E CB  1 
ATOM   4821  C  CG  . HIS E  1 49  ? 118.888 91.584  47.333 1.00   31.62 ? 48   HIS E CG  1 
ATOM   4822  N  ND1 . HIS E  1 49  ? 117.582 91.388  47.572 1.00   33.67 ? 48   HIS E ND1 1 
ATOM   4823  C  CD2 . HIS E  1 49  ? 119.549 90.447  47.785 1.00   31.04 ? 48   HIS E CD2 1 
ATOM   4824  C  CE1 . HIS E  1 49  ? 117.409 90.196  48.162 1.00   32.74 ? 48   HIS E CE1 1 
ATOM   4825  N  NE2 . HIS E  1 49  ? 118.616 89.621  48.292 1.00   32.35 ? 48   HIS E NE2 1 
ATOM   4826  N  N   . GLU E  1 50  ? 119.095 94.123  43.836 1.00   32.38 ? 49   GLU E N   1 
ATOM   4827  C  CA  . GLU E  1 50  ? 119.078 95.159  42.790 1.00   32.89 ? 49   GLU E CA  1 
ATOM   4828  C  C   . GLU E  1 50  ? 119.530 96.554  43.225 1.00   31.78 ? 49   GLU E C   1 
ATOM   4829  O  O   . GLU E  1 50  ? 120.351 97.164  42.559 1.00   31.99 ? 49   GLU E O   1 
ATOM   4830  C  CB  . GLU E  1 50  ? 117.669 95.260  42.189 1.00   34.80 ? 49   GLU E CB  1 
ATOM   4831  C  CG  . GLU E  1 50  ? 117.616 96.152  40.970 1.00   35.57 ? 49   GLU E CG  1 
ATOM   4832  C  CD  . GLU E  1 50  ? 116.259 96.158  40.304 1.00   37.52 ? 49   GLU E CD  1 
ATOM   4833  O  OE1 . GLU E  1 50  ? 115.285 95.606  40.880 1.00   38.10 ? 49   GLU E OE1 1 
ATOM   4834  O  OE2 . GLU E  1 50  ? 116.184 96.738  39.198 1.00   38.73 ? 49   GLU E OE2 1 
ATOM   4835  N  N   . PHE E  1 51  ? 118.996 97.050  44.333 1.00   31.71 ? 50   PHE E N   1 
ATOM   4836  C  CA  . PHE E  1 51  ? 119.248 98.424  44.758 1.00   32.59 ? 50   PHE E CA  1 
ATOM   4837  C  C   . PHE E  1 51  ? 120.243 98.529  45.901 1.00   30.90 ? 50   PHE E C   1 
ATOM   4838  O  O   . PHE E  1 51  ? 120.186 97.742  46.862 1.00   30.12 ? 50   PHE E O   1 
ATOM   4839  C  CB  . PHE E  1 51  ? 117.933 99.076  45.174 1.00   34.87 ? 50   PHE E CB  1 
ATOM   4840  C  CG  . PHE E  1 51  ? 116.879 98.986  44.123 1.00   36.66 ? 50   PHE E CG  1 
ATOM   4841  C  CD1 . PHE E  1 51  ? 117.056 99.635  42.908 1.00   37.36 ? 50   PHE E CD1 1 
ATOM   4842  C  CD2 . PHE E  1 51  ? 115.726 98.250  44.338 1.00   37.87 ? 50   PHE E CD2 1 
ATOM   4843  C  CE1 . PHE E  1 51  ? 116.100 99.550  41.922 1.00   39.08 ? 50   PHE E CE1 1 
ATOM   4844  C  CE2 . PHE E  1 51  ? 114.750 98.164  43.353 1.00   40.04 ? 50   PHE E CE2 1 
ATOM   4845  C  CZ  . PHE E  1 51  ? 114.940 98.817  42.141 1.00   40.06 ? 50   PHE E CZ  1 
ATOM   4846  N  N   . GLY E  1 52  ? 121.154 99.500  45.772 1.00   30.05 ? 51   GLY E N   1 
ATOM   4847  C  CA  . GLY E  1 52  ? 122.074 99.904  46.840 1.00   28.31 ? 51   GLY E CA  1 
ATOM   4848  C  C   . GLY E  1 52  ? 121.425 100.871 47.812 1.00   28.44 ? 51   GLY E C   1 
ATOM   4849  O  O   . GLY E  1 52  ? 121.968 101.953 48.111 1.00   26.85 ? 51   GLY E O   1 
ATOM   4850  N  N   . ASP E  1 53  ? 120.265 100.461 48.315 1.00   28.97 ? 52   ASP E N   1 
ATOM   4851  C  CA  . ASP E  1 53  ? 119.414 101.289 49.151 1.00   29.46 ? 52   ASP E CA  1 
ATOM   4852  C  C   . ASP E  1 53  ? 119.213 100.569 50.473 1.00   29.45 ? 52   ASP E C   1 
ATOM   4853  O  O   . ASP E  1 53  ? 118.498 99.555  50.530 1.00   29.69 ? 52   ASP E O   1 
ATOM   4854  C  CB  . ASP E  1 53  ? 118.080 101.513 48.437 1.00   30.86 ? 52   ASP E CB  1 
ATOM   4855  C  CG  . ASP E  1 53  ? 117.088 102.354 49.246 1.00   32.53 ? 52   ASP E CG  1 
ATOM   4856  O  OD1 . ASP E  1 53  ? 117.232 102.496 50.492 1.00   31.90 ? 52   ASP E OD1 1 
ATOM   4857  O  OD2 . ASP E  1 53  ? 116.131 102.858 48.609 1.00   34.24 ? 52   ASP E OD2 1 
ATOM   4858  N  N   . ASN E  1 54  ? 119.833 101.095 51.532 1.00   29.16 ? 53   ASN E N   1 
ATOM   4859  C  CA  . ASN E  1 54  ? 119.698 100.537 52.877 1.00   29.44 ? 53   ASN E CA  1 
ATOM   4860  C  C   . ASN E  1 54  ? 118.988 101.492 53.852 1.00   30.93 ? 53   ASN E C   1 
ATOM   4861  O  O   . ASN E  1 54  ? 119.190 101.434 55.073 1.00   30.96 ? 53   ASN E O   1 
ATOM   4862  C  CB  . ASN E  1 54  ? 121.084 100.120 53.405 1.00   29.05 ? 53   ASN E CB  1 
ATOM   4863  C  CG  . ASN E  1 54  ? 121.724 98.972  52.589 0.50   28.14 ? 53   ASN E CG  1 
ATOM   4864  O  OD1 . ASN E  1 54  ? 121.056 98.284  51.795 0.50   28.36 ? 53   ASN E OD1 1 
ATOM   4865  N  ND2 . ASN E  1 54  ? 123.026 98.762  52.790 0.50   26.91 ? 53   ASN E ND2 1 
ATOM   4866  N  N   . THR E  1 55  ? 118.126 102.356 53.325 1.00   32.19 ? 54   THR E N   1 
ATOM   4867  C  CA  . THR E  1 55  ? 117.444 103.361 54.159 1.00   33.54 ? 54   THR E CA  1 
ATOM   4868  C  C   . THR E  1 55  ? 116.482 102.733 55.169 1.00   34.99 ? 54   THR E C   1 
ATOM   4869  O  O   . THR E  1 55  ? 116.283 103.277 56.238 1.00   36.63 ? 54   THR E O   1 
ATOM   4870  C  CB  . THR E  1 55  ? 116.668 104.368 53.301 1.00   33.73 ? 54   THR E CB  1 
ATOM   4871  O  OG1 . THR E  1 55  ? 115.721 103.649 52.503 1.00   34.46 ? 54   THR E OG1 1 
ATOM   4872  C  CG2 . THR E  1 55  ? 117.632 105.174 52.390 1.00   32.08 ? 54   THR E CG2 1 
ATOM   4873  N  N   . ALA E  1 56  ? 115.891 101.590 54.845 1.00   36.32 ? 55   ALA E N   1 
ATOM   4874  C  CA  . ALA E  1 56  ? 115.124 100.822 55.849 1.00   38.75 ? 55   ALA E CA  1 
ATOM   4875  C  C   . ALA E  1 56  ? 115.799 99.482  56.108 1.00   37.93 ? 55   ALA E C   1 
ATOM   4876  O  O   . ALA E  1 56  ? 115.166 98.441  56.144 1.00   38.68 ? 55   ALA E O   1 
ATOM   4877  C  CB  . ALA E  1 56  ? 113.666 100.638 55.419 1.00   40.35 ? 55   ALA E CB  1 
ATOM   4878  N  N   . GLY E  1 57  ? 117.109 99.524  56.300 1.00   38.10 ? 56   GLY E N   1 
ATOM   4879  C  CA  . GLY E  1 57  ? 117.884 98.308  56.505 1.00   36.88 ? 56   GLY E CA  1 
ATOM   4880  C  C   . GLY E  1 57  ? 117.946 97.530  55.212 1.00   36.07 ? 56   GLY E C   1 
ATOM   4881  O  O   . GLY E  1 57  ? 117.764 98.098  54.124 1.00   35.57 ? 56   GLY E O   1 
ATOM   4882  N  N   . CYS E  1 58  ? 118.176 96.227  55.329 1.00   34.01 ? 57   CYS E N   1 
ATOM   4883  C  CA  . CYS E  1 58  ? 118.286 95.373  54.158 1.00   34.02 ? 57   CYS E CA  1 
ATOM   4884  C  C   . CYS E  1 58  ? 117.002 95.233  53.330 1.00   33.67 ? 57   CYS E C   1 
ATOM   4885  O  O   . CYS E  1 58  ? 117.080 94.855  52.159 1.00   32.56 ? 57   CYS E O   1 
ATOM   4886  C  CB  . CYS E  1 58  ? 118.808 93.994  54.554 1.00   33.70 ? 57   CYS E CB  1 
ATOM   4887  S  SG  . CYS E  1 58  ? 120.358 94.075  55.473 1.00   33.84 ? 57   CYS E SG  1 
ATOM   4888  N  N   . THR E  1 59  ? 115.847 95.548  53.915 1.00   34.63 ? 58   THR E N   1 
ATOM   4889  C  CA  . THR E  1 59  ? 114.565 95.457  53.200 1.00   36.65 ? 58   THR E CA  1 
ATOM   4890  C  C   . THR E  1 59  ? 114.489 96.320  51.948 1.00   36.25 ? 58   THR E C   1 
ATOM   4891  O  O   . THR E  1 59  ? 113.884 95.905  50.950 1.00   37.43 ? 58   THR E O   1 
ATOM   4892  C  CB  . THR E  1 59  ? 113.378 95.849  54.097 1.00   38.96 ? 58   THR E CB  1 
ATOM   4893  O  OG1 . THR E  1 59  ? 113.468 95.125  55.326 1.00   40.30 ? 58   THR E OG1 1 
ATOM   4894  C  CG2 . THR E  1 59  ? 112.037 95.523  53.413 1.00   40.00 ? 58   THR E CG2 1 
ATOM   4895  N  N   . SER E  1 60  ? 115.086 97.510  51.984 1.00   35.24 ? 59   SER E N   1 
ATOM   4896  C  CA  . SER E  1 60  ? 114.975 98.432  50.836 1.00   35.18 ? 59   SER E CA  1 
ATOM   4897  C  C   . SER E  1 60  ? 115.900 98.063  49.673 1.00   34.53 ? 59   SER E C   1 
ATOM   4898  O  O   . SER E  1 60  ? 115.846 98.714  48.627 1.00   34.28 ? 59   SER E O   1 
ATOM   4899  C  CB  . SER E  1 60  ? 115.159 99.903  51.255 1.00   35.54 ? 59   SER E CB  1 
ATOM   4900  O  OG  . SER E  1 60  ? 115.895 100.039 52.453 1.00   34.55 ? 59   SER E OG  1 
ATOM   4901  N  N   . ALA E  1 61  ? 116.708 97.001  49.825 1.00   33.75 ? 60   ALA E N   1 
ATOM   4902  C  CA  . ALA E  1 61  ? 117.590 96.549  48.738 1.00   33.21 ? 60   ALA E CA  1 
ATOM   4903  C  C   . ALA E  1 61  ? 116.811 95.976  47.562 1.00   33.77 ? 60   ALA E C   1 
ATOM   4904  O  O   . ALA E  1 61  ? 117.377 95.770  46.479 1.00   33.19 ? 60   ALA E O   1 
ATOM   4905  C  CB  . ALA E  1 61  ? 118.613 95.523  49.232 1.00   32.19 ? 60   ALA E CB  1 
ATOM   4906  N  N   . GLY E  1 62  ? 115.524 95.710  47.772 1.00   35.03 ? 61   GLY E N   1 
ATOM   4907  C  CA  . GLY E  1 62  ? 114.662 95.221  46.702 1.00   36.53 ? 61   GLY E CA  1 
ATOM   4908  C  C   . GLY E  1 62  ? 114.893 93.740  46.489 1.00   36.90 ? 61   GLY E C   1 
ATOM   4909  O  O   . GLY E  1 62  ? 115.385 93.058  47.389 1.00   35.75 ? 61   GLY E O   1 
ATOM   4910  N  N   . PRO E  1 63  ? 114.564 93.241  45.289 1.00   38.81 ? 62   PRO E N   1 
ATOM   4911  C  CA  . PRO E  1 63  ? 114.738 91.841  44.936 1.00   39.16 ? 62   PRO E CA  1 
ATOM   4912  C  C   . PRO E  1 63  ? 116.114 91.502  44.353 1.00   38.86 ? 62   PRO E C   1 
ATOM   4913  O  O   . PRO E  1 63  ? 116.983 92.375  44.201 1.00   36.35 ? 62   PRO E O   1 
ATOM   4914  C  CB  . PRO E  1 63  ? 113.647 91.621  43.889 1.00   40.91 ? 62   PRO E CB  1 
ATOM   4915  C  CG  . PRO E  1 63  ? 113.526 92.943  43.207 1.00   41.26 ? 62   PRO E CG  1 
ATOM   4916  C  CD  . PRO E  1 63  ? 113.950 94.005  44.185 1.00   40.46 ? 62   PRO E CD  1 
ATOM   4917  N  N   . HIS E  1 64  ? 116.296 90.224  44.033 1.00   39.30 ? 63   HIS E N   1 
ATOM   4918  C  CA  . HIS E  1 64  ? 117.538 89.737  43.429 1.00   39.81 ? 63   HIS E CA  1 
ATOM   4919  C  C   . HIS E  1 64  ? 117.833 90.498  42.168 1.00   39.11 ? 63   HIS E C   1 
ATOM   4920  O  O   . HIS E  1 64  ? 116.942 90.737  41.364 1.00   39.82 ? 63   HIS E O   1 
ATOM   4921  C  CB  . HIS E  1 64  ? 117.431 88.233  43.139 1.00   40.63 ? 63   HIS E CB  1 
ATOM   4922  C  CG  . HIS E  1 64  ? 117.320 87.380  44.382 1.00   40.87 ? 63   HIS E CG  1 
ATOM   4923  N  ND1 . HIS E  1 64  ? 117.321 86.023  44.345 1.00   40.91 ? 63   HIS E ND1 1 
ATOM   4924  C  CD2 . HIS E  1 64  ? 117.218 87.737  45.728 1.00   40.44 ? 63   HIS E CD2 1 
ATOM   4925  C  CE1 . HIS E  1 64  ? 117.215 85.544  45.603 1.00   40.77 ? 63   HIS E CE1 1 
ATOM   4926  N  NE2 . HIS E  1 64  ? 117.150 86.590  46.448 1.00   41.04 ? 63   HIS E NE2 1 
ATOM   4927  N  N   . PHE E  1 65  ? 119.081 90.918  41.991 1.00   38.54 ? 64   PHE E N   1 
ATOM   4928  C  CA  . PHE E  1 65  ? 119.479 91.579  40.751 1.00   38.97 ? 64   PHE E CA  1 
ATOM   4929  C  C   . PHE E  1 65  ? 119.243 90.616  39.594 1.00   40.27 ? 64   PHE E C   1 
ATOM   4930  O  O   . PHE E  1 65  ? 119.771 89.501  39.594 1.00   40.28 ? 64   PHE E O   1 
ATOM   4931  C  CB  . PHE E  1 65  ? 120.952 91.995  40.797 1.00   37.87 ? 64   PHE E CB  1 
ATOM   4932  C  CG  . PHE E  1 65  ? 121.419 92.771  39.587 1.00   38.06 ? 64   PHE E CG  1 
ATOM   4933  C  CD1 . PHE E  1 65  ? 120.593 93.713  38.961 1.00   38.90 ? 64   PHE E CD1 1 
ATOM   4934  C  CD2 . PHE E  1 65  ? 122.714 92.603  39.108 1.00   37.47 ? 64   PHE E CD2 1 
ATOM   4935  C  CE1 . PHE E  1 65  ? 121.041 94.434  37.863 1.00   39.01 ? 64   PHE E CE1 1 
ATOM   4936  C  CE2 . PHE E  1 65  ? 123.169 93.328  38.015 1.00   38.93 ? 64   PHE E CE2 1 
ATOM   4937  C  CZ  . PHE E  1 65  ? 122.332 94.250  37.392 1.00   38.93 ? 64   PHE E CZ  1 
ATOM   4938  N  N   . ASN E  1 66  ? 118.471 91.081  38.613 1.00   41.93 ? 65   ASN E N   1 
ATOM   4939  C  CA  . ASN E  1 66  ? 117.903 90.242  37.572 1.00   43.46 ? 65   ASN E CA  1 
ATOM   4940  C  C   . ASN E  1 66  ? 117.666 91.028  36.280 1.00   45.45 ? 65   ASN E C   1 
ATOM   4941  O  O   . ASN E  1 66  ? 116.529 91.174  35.848 1.00   45.30 ? 65   ASN E O   1 
ATOM   4942  C  CB  . ASN E  1 66  ? 116.569 89.680  38.073 1.00   43.53 ? 65   ASN E CB  1 
ATOM   4943  C  CG  . ASN E  1 66  ? 116.008 88.597  37.174 1.00   44.52 ? 65   ASN E CG  1 
ATOM   4944  O  OD1 . ASN E  1 66  ? 116.732 87.966  36.394 1.00   43.46 ? 65   ASN E OD1 1 
ATOM   4945  N  ND2 . ASN E  1 66  ? 114.709 88.351  37.304 1.00   45.26 ? 65   ASN E ND2 1 
ATOM   4946  N  N   . PRO E  1 67  ? 118.740 91.551  35.662 1.00   46.38 ? 66   PRO E N   1 
ATOM   4947  C  CA  . PRO E  1 67  ? 118.548 92.311  34.423 1.00   47.44 ? 66   PRO E CA  1 
ATOM   4948  C  C   . PRO E  1 67  ? 117.854 91.496  33.334 1.00   49.27 ? 66   PRO E C   1 
ATOM   4949  O  O   . PRO E  1 67  ? 116.938 91.998  32.699 1.00   51.16 ? 66   PRO E O   1 
ATOM   4950  C  CB  . PRO E  1 67  ? 119.975 92.685  34.003 1.00   47.07 ? 66   PRO E CB  1 
ATOM   4951  C  CG  . PRO E  1 67  ? 120.864 91.733  34.729 1.00   46.27 ? 66   PRO E CG  1 
ATOM   4952  C  CD  . PRO E  1 67  ? 120.164 91.427  36.018 1.00   45.27 ? 66   PRO E CD  1 
ATOM   4953  N  N   . LEU E  1 68  ? 118.251 90.233  33.167 1.00   50.26 ? 67   LEU E N   1 
ATOM   4954  C  CA  . LEU E  1 68  ? 117.737 89.374  32.076 1.00   51.60 ? 67   LEU E CA  1 
ATOM   4955  C  C   . LEU E  1 68  ? 116.394 88.684  32.371 1.00   52.55 ? 67   LEU E C   1 
ATOM   4956  O  O   . LEU E  1 68  ? 116.011 87.761  31.651 1.00   57.10 ? 67   LEU E O   1 
ATOM   4957  C  CB  . LEU E  1 68  ? 118.782 88.311  31.702 1.00   50.23 ? 67   LEU E CB  1 
ATOM   4958  C  CG  . LEU E  1 68  ? 120.199 88.812  31.389 1.00   50.02 ? 67   LEU E CG  1 
ATOM   4959  C  CD1 . LEU E  1 68  ? 121.140 87.632  31.198 1.00   49.65 ? 67   LEU E CD1 1 
ATOM   4960  C  CD2 . LEU E  1 68  ? 120.217 89.746  30.179 1.00   51.08 ? 67   LEU E CD2 1 
ATOM   4961  N  N   . SER E  1 69  ? 115.686 89.116  33.416 1.00   51.91 ? 68   SER E N   1 
ATOM   4962  C  CA  . SER E  1 69  ? 114.330 88.630  33.704 1.00   53.01 ? 68   SER E CA  1 
ATOM   4963  C  C   . SER E  1 69  ? 114.231 87.115  33.601 1.00   54.08 ? 68   SER E C   1 
ATOM   4964  O  O   . SER E  1 69  ? 113.466 86.589  32.799 1.00   54.37 ? 68   SER E O   1 
ATOM   4965  C  CB  . SER E  1 69  ? 113.314 89.262  32.749 1.00   54.19 ? 68   SER E CB  1 
ATOM   4966  O  OG  . SER E  1 69  ? 113.422 90.669  32.774 1.00   54.81 ? 68   SER E OG  1 
ATOM   4967  N  N   . ARG E  1 70  ? 115.022 86.423  34.413 1.00   53.72 ? 69   ARG E N   1 
ATOM   4968  C  CA  . ARG E  1 70  ? 114.981 84.977  34.481 1.00   53.61 ? 69   ARG E CA  1 
ATOM   4969  C  C   . ARG E  1 70  ? 114.481 84.535  35.851 1.00   51.37 ? 69   ARG E C   1 
ATOM   4970  O  O   . ARG E  1 70  ? 114.215 85.362  36.723 1.00   49.41 ? 69   ARG E O   1 
ATOM   4971  C  CB  . ARG E  1 70  ? 116.366 84.415  34.179 1.00   55.85 ? 69   ARG E CB  1 
ATOM   4972  C  CG  . ARG E  1 70  ? 116.874 84.826  32.804 1.00   59.85 ? 69   ARG E CG  1 
ATOM   4973  C  CD  . ARG E  1 70  ? 117.963 83.901  32.277 1.00   62.43 ? 69   ARG E CD  1 
ATOM   4974  N  NE  . ARG E  1 70  ? 118.522 84.387  31.013 1.00   65.90 ? 69   ARG E NE  1 
ATOM   4975  C  CZ  . ARG E  1 70  ? 119.579 83.863  30.391 1.00   68.01 ? 69   ARG E CZ  1 
ATOM   4976  N  NH1 . ARG E  1 70  ? 120.214 82.807  30.895 1.00   68.41 ? 69   ARG E NH1 1 
ATOM   4977  N  NH2 . ARG E  1 70  ? 120.005 84.397  29.248 1.00   69.58 ? 69   ARG E NH2 1 
ATOM   4978  N  N   . LYS E  1 71  ? 114.316 83.230  36.023 1.00   50.34 ? 70   LYS E N   1 
ATOM   4979  C  CA  . LYS E  1 71  ? 113.881 82.673  37.293 1.00   49.44 ? 70   LYS E CA  1 
ATOM   4980  C  C   . LYS E  1 71  ? 115.107 82.455  38.186 1.00   45.58 ? 70   LYS E C   1 
ATOM   4981  O  O   . LYS E  1 71  ? 116.236 82.372  37.698 1.00   42.65 ? 70   LYS E O   1 
ATOM   4982  C  CB  . LYS E  1 71  ? 113.159 81.327  37.090 1.00   51.62 ? 70   LYS E CB  1 
ATOM   4983  C  CG  . LYS E  1 71  ? 111.895 81.374  36.241 1.00   55.28 ? 70   LYS E CG  1 
ATOM   4984  C  CD  . LYS E  1 71  ? 110.766 82.159  36.905 1.00   56.31 ? 70   LYS E CD  1 
ATOM   4985  C  CE  . LYS E  1 71  ? 109.504 82.162  36.038 1.00   58.80 ? 70   LYS E CE  1 
ATOM   4986  N  NZ  . LYS E  1 71  ? 108.759 83.451  36.153 1.00   58.76 ? 70   LYS E NZ  1 
ATOM   4987  N  N   . HIS E  1 72  ? 114.851 82.329  39.488 1.00   44.35 ? 71   HIS E N   1 
ATOM   4988  C  CA  . HIS E  1 72  ? 115.878 82.019  40.490 1.00   42.56 ? 71   HIS E CA  1 
ATOM   4989  C  C   . HIS E  1 72  ? 116.464 80.630  40.321 1.00   41.72 ? 71   HIS E C   1 
ATOM   4990  O  O   . HIS E  1 72  ? 115.743 79.646  40.107 1.00   42.00 ? 71   HIS E O   1 
ATOM   4991  C  CB  . HIS E  1 72  ? 115.293 82.141  41.900 1.00   41.74 ? 71   HIS E CB  1 
ATOM   4992  C  CG  . HIS E  1 72  ? 116.308 81.942  43.005 1.00   40.17 ? 71   HIS E CG  1 
ATOM   4993  N  ND1 . HIS E  1 72  ? 117.255 82.853  43.290 1.00   38.03 ? 71   HIS E ND1 1 
ATOM   4994  C  CD2 . HIS E  1 72  ? 116.496 80.880  43.900 1.00   39.08 ? 71   HIS E CD2 1 
ATOM   4995  C  CE1 . HIS E  1 72  ? 118.019 82.403  44.303 1.00   37.39 ? 71   HIS E CE1 1 
ATOM   4996  N  NE2 . HIS E  1 72  ? 117.551 81.195  44.680 1.00   37.99 ? 71   HIS E NE2 1 
ATOM   4997  N  N   . GLY E  1 73  ? 117.786 80.551  40.419 1.00   40.04 ? 72   GLY E N   1 
ATOM   4998  C  CA  . GLY E  1 73  ? 118.500 79.273  40.492 1.00   38.71 ? 72   GLY E CA  1 
ATOM   4999  C  C   . GLY E  1 73  ? 119.741 79.416  41.359 1.00   37.62 ? 72   GLY E C   1 
ATOM   5000  O  O   . GLY E  1 73  ? 119.878 80.393  42.127 1.00   37.40 ? 72   GLY E O   1 
ATOM   5001  N  N   . GLY E  1 74  ? 120.628 78.435  41.253 1.00   36.13 ? 73   GLY E N   1 
ATOM   5002  C  CA  . GLY E  1 74  ? 121.941 78.488  41.867 1.00   35.55 ? 73   GLY E CA  1 
ATOM   5003  C  C   . GLY E  1 74  ? 122.921 79.054  40.860 1.00   36.30 ? 73   GLY E C   1 
ATOM   5004  O  O   . GLY E  1 74  ? 122.574 79.190  39.679 1.00   36.80 ? 73   GLY E O   1 
ATOM   5005  N  N   . PRO E  1 75  ? 124.144 79.402  41.313 1.00   35.61 ? 74   PRO E N   1 
ATOM   5006  C  CA  . PRO E  1 75  ? 125.159 80.008  40.442 1.00   37.03 ? 74   PRO E CA  1 
ATOM   5007  C  C   . PRO E  1 75  ? 125.532 79.156  39.225 1.00   39.10 ? 74   PRO E C   1 
ATOM   5008  O  O   . PRO E  1 75  ? 125.840 79.711  38.168 1.00   41.79 ? 74   PRO E O   1 
ATOM   5009  C  CB  . PRO E  1 75  ? 126.377 80.190  41.373 1.00   36.29 ? 74   PRO E CB  1 
ATOM   5010  C  CG  . PRO E  1 75  ? 126.116 79.279  42.536 1.00   34.99 ? 74   PRO E CG  1 
ATOM   5011  C  CD  . PRO E  1 75  ? 124.630 79.258  42.696 1.00   34.79 ? 74   PRO E CD  1 
ATOM   5012  N  N   . LYS E  1 76  ? 125.471 77.831  39.360 1.00   40.22 ? 75   LYS E N   1 
ATOM   5013  C  CA  . LYS E  1 76  ? 125.782 76.909  38.246 1.00   42.42 ? 75   LYS E CA  1 
ATOM   5014  C  C   . LYS E  1 76  ? 124.666 76.736  37.199 1.00   43.15 ? 75   LYS E C   1 
ATOM   5015  O  O   . LYS E  1 76  ? 124.912 76.203  36.126 1.00   43.44 ? 75   LYS E O   1 
ATOM   5016  C  CB  . LYS E  1 76  ? 126.197 75.535  38.795 1.00   43.73 ? 75   LYS E CB  1 
ATOM   5017  C  CG  . LYS E  1 76  ? 127.652 75.486  39.252 1.00   45.48 ? 75   LYS E CG  1 
ATOM   5018  C  CD  . LYS E  1 76  ? 127.838 74.779  40.597 1.00   47.45 ? 75   LYS E CD  1 
ATOM   5019  C  CE  . LYS E  1 76  ? 127.696 73.269  40.505 1.00   48.14 ? 75   LYS E CE  1 
ATOM   5020  N  NZ  . LYS E  1 76  ? 128.167 72.635  41.771 1.00   50.99 ? 75   LYS E NZ  1 
ATOM   5021  N  N   . ASP E  1 77  ? 123.450 77.175  37.493 1.00   42.93 ? 76   ASP E N   1 
ATOM   5022  C  CA  . ASP E  1 77  ? 122.349 77.009  36.543 1.00   44.92 ? 76   ASP E CA  1 
ATOM   5023  C  C   . ASP E  1 77  ? 122.397 78.081  35.447 1.00   47.55 ? 76   ASP E C   1 
ATOM   5024  O  O   . ASP E  1 77  ? 122.759 79.238  35.709 1.00   44.88 ? 76   ASP E O   1 
ATOM   5025  C  CB  . ASP E  1 77  ? 121.005 77.059  37.276 1.00   44.61 ? 76   ASP E CB  1 
ATOM   5026  C  CG  . ASP E  1 77  ? 120.943 76.082  38.435 1.00   44.35 ? 76   ASP E CG  1 
ATOM   5027  O  OD1 . ASP E  1 77  ? 121.496 74.967  38.290 1.00   45.94 ? 76   ASP E OD1 1 
ATOM   5028  O  OD2 . ASP E  1 77  ? 120.349 76.416  39.486 1.00   41.82 ? 76   ASP E OD2 1 
ATOM   5029  N  N   . GLU E  1 78  ? 122.043 77.682  34.221 1.00   50.16 ? 77   GLU E N   1 
ATOM   5030  C  CA  . GLU E  1 78  ? 121.816 78.621  33.111 1.00   52.11 ? 77   GLU E CA  1 
ATOM   5031  C  C   . GLU E  1 78  ? 120.689 79.568  33.466 1.00   50.22 ? 77   GLU E C   1 
ATOM   5032  O  O   . GLU E  1 78  ? 120.781 80.783  33.247 1.00   52.30 ? 77   GLU E O   1 
ATOM   5033  C  CB  . GLU E  1 78  ? 121.422 77.865  31.835 1.00   58.04 ? 77   GLU E CB  1 
ATOM   5034  C  CG  . GLU E  1 78  ? 122.550 77.080  31.184 1.00   61.56 ? 77   GLU E CG  1 
ATOM   5035  C  CD  . GLU E  1 78  ? 123.373 77.914  30.214 1.00   65.47 ? 77   GLU E CD  1 
ATOM   5036  O  OE1 . GLU E  1 78  ? 123.348 79.164  30.310 1.00   66.99 ? 77   GLU E OE1 1 
ATOM   5037  O  OE2 . GLU E  1 78  ? 124.046 77.306  29.350 1.00   70.86 ? 77   GLU E OE2 1 
ATOM   5038  N  N   . GLU E  1 79  ? 119.617 78.997  34.003 1.00   48.96 ? 78   GLU E N   1 
ATOM   5039  C  CA  . GLU E  1 79  ? 118.474 79.766  34.476 1.00   48.73 ? 78   GLU E CA  1 
ATOM   5040  C  C   . GLU E  1 79  ? 118.724 80.232  35.916 1.00   45.25 ? 78   GLU E C   1 
ATOM   5041  O  O   . GLU E  1 79  ? 118.547 79.473  36.877 1.00   43.92 ? 78   GLU E O   1 
ATOM   5042  C  CB  . GLU E  1 79  ? 117.190 78.924  34.395 1.00   50.53 ? 78   GLU E CB  1 
ATOM   5043  C  CG  . GLU E  1 79  ? 115.902 79.697  34.663 1.00   51.90 ? 78   GLU E CG  1 
ATOM   5044  C  CD  . GLU E  1 79  ? 115.565 80.702  33.572 1.00   54.40 ? 78   GLU E CD  1 
ATOM   5045  O  OE1 . GLU E  1 79  ? 116.256 80.717  32.528 1.00   57.11 ? 78   GLU E OE1 1 
ATOM   5046  O  OE2 . GLU E  1 79  ? 114.603 81.481  33.763 1.00   53.51 ? 78   GLU E OE2 1 
ATOM   5047  N  N   . ARG E  1 80  ? 119.141 81.484  36.044 1.00   42.59 ? 79   ARG E N   1 
ATOM   5048  C  CA  . ARG E  1 80  ? 119.397 82.101  37.346 1.00   40.80 ? 79   ARG E CA  1 
ATOM   5049  C  C   . ARG E  1 80  ? 119.311 83.593  37.186 1.00   39.58 ? 79   ARG E C   1 
ATOM   5050  O  O   . ARG E  1 80  ? 119.412 84.099  36.073 1.00   40.89 ? 79   ARG E O   1 
ATOM   5051  C  CB  . ARG E  1 80  ? 120.809 81.773  37.833 1.00   38.73 ? 79   ARG E CB  1 
ATOM   5052  C  CG  . ARG E  1 80  ? 121.888 82.125  36.820 1.00   38.47 ? 79   ARG E CG  1 
ATOM   5053  C  CD  . ARG E  1 80  ? 123.282 81.965  37.383 1.00   37.70 ? 79   ARG E CD  1 
ATOM   5054  N  NE  . ARG E  1 80  ? 123.706 83.140  38.140 1.00   36.42 ? 79   ARG E NE  1 
ATOM   5055  C  CZ  . ARG E  1 80  ? 124.949 83.341  38.579 1.00   36.32 ? 79   ARG E CZ  1 
ATOM   5056  N  NH1 . ARG E  1 80  ? 125.906 82.437  38.352 1.00   35.44 ? 79   ARG E NH1 1 
ATOM   5057  N  NH2 . ARG E  1 80  ? 125.246 84.462  39.238 1.00   35.07 ? 79   ARG E NH2 1 
ATOM   5058  N  N   . HIS E  1 81  ? 119.162 84.292  38.305 1.00   38.25 ? 80   HIS E N   1 
ATOM   5059  C  CA  . HIS E  1 81  ? 119.383 85.734  38.332 1.00   37.55 ? 80   HIS E CA  1 
ATOM   5060  C  C   . HIS E  1 81  ? 120.865 86.004  38.280 1.00   35.65 ? 80   HIS E C   1 
ATOM   5061  O  O   . HIS E  1 81  ? 121.676 85.142  38.607 1.00   34.90 ? 80   HIS E O   1 
ATOM   5062  C  CB  . HIS E  1 81  ? 118.767 86.369  39.577 1.00   37.66 ? 80   HIS E CB  1 
ATOM   5063  C  CG  . HIS E  1 81  ? 117.313 86.006  39.804 1.00   39.42 ? 80   HIS E CG  1 
ATOM   5064  N  ND1 . HIS E  1 81  ? 116.806 85.757  41.027 1.00   39.09 ? 80   HIS E ND1 1 
ATOM   5065  C  CD2 . HIS E  1 81  ? 116.258 85.864  38.908 1.00   40.89 ? 80   HIS E CD2 1 
ATOM   5066  C  CE1 . HIS E  1 81  ? 115.494 85.480  40.918 1.00   39.81 ? 80   HIS E CE1 1 
ATOM   5067  N  NE2 . HIS E  1 81  ? 115.160 85.546  39.623 1.00   41.36 ? 80   HIS E NE2 1 
ATOM   5068  N  N   . VAL E  1 82  ? 121.245 87.196  37.839 1.00   35.41 ? 81   VAL E N   1 
ATOM   5069  C  CA  . VAL E  1 82  ? 122.649 87.606  37.892 1.00   34.44 ? 81   VAL E CA  1 
ATOM   5070  C  C   . VAL E  1 82  ? 123.174 87.569  39.340 1.00   32.60 ? 81   VAL E C   1 
ATOM   5071  O  O   . VAL E  1 82  ? 124.294 87.126  39.598 1.00   31.70 ? 81   VAL E O   1 
ATOM   5072  C  CB  . VAL E  1 82  ? 122.843 89.003  37.274 1.00   35.50 ? 81   VAL E CB  1 
ATOM   5073  C  CG1 . VAL E  1 82  ? 124.210 89.570  37.644 1.00   34.26 ? 81   VAL E CG1 1 
ATOM   5074  C  CG2 . VAL E  1 82  ? 122.653 88.932  35.755 1.00   35.51 ? 81   VAL E CG2 1 
ATOM   5075  N  N   . GLY E  1 83  ? 122.350 87.996  40.289 1.00   32.13 ? 82   GLY E N   1 
ATOM   5076  C  CA  . GLY E  1 83  ? 122.780 88.085  41.686 1.00   31.38 ? 82   GLY E CA  1 
ATOM   5077  C  C   . GLY E  1 83  ? 122.790 86.797  42.495 1.00   30.24 ? 82   GLY E C   1 
ATOM   5078  O  O   . GLY E  1 83  ? 123.146 86.815  43.670 1.00   30.53 ? 82   GLY E O   1 
ATOM   5079  N  N   . ASP E  1 84  ? 122.418 85.688  41.871 1.00   30.62 ? 83   ASP E N   1 
ATOM   5080  C  CA  . ASP E  1 84  ? 122.313 84.397  42.552 1.00   30.44 ? 83   ASP E CA  1 
ATOM   5081  C  C   . ASP E  1 84  ? 123.678 83.755  42.797 1.00   29.28 ? 83   ASP E C   1 
ATOM   5082  O  O   . ASP E  1 84  ? 124.187 83.008  41.954 1.00   30.83 ? 83   ASP E O   1 
ATOM   5083  C  CB  . ASP E  1 84  ? 121.439 83.441  41.717 1.00   31.68 ? 83   ASP E CB  1 
ATOM   5084  C  CG  . ASP E  1 84  ? 119.966 83.828  41.709 1.00   32.76 ? 83   ASP E CG  1 
ATOM   5085  O  OD1 . ASP E  1 84  ? 119.572 84.771  42.441 1.00   32.96 ? 83   ASP E OD1 1 
ATOM   5086  O  OD2 . ASP E  1 84  ? 119.191 83.183  40.972 1.00   32.59 ? 83   ASP E OD2 1 
ATOM   5087  N  N   . LEU E  1 85  ? 124.263 84.015  43.958 1.00   28.15 ? 84   LEU E N   1 
ATOM   5088  C  CA  . LEU E  1 85  ? 125.584 83.466  44.288 1.00   27.29 ? 84   LEU E CA  1 
ATOM   5089  C  C   . LEU E  1 85  ? 125.485 82.270  45.235 1.00   26.94 ? 84   LEU E C   1 
ATOM   5090  O  O   . LEU E  1 85  ? 126.479 81.847  45.810 1.00   27.22 ? 84   LEU E O   1 
ATOM   5091  C  CB  . LEU E  1 85  ? 126.492 84.558  44.870 1.00   26.37 ? 84   LEU E CB  1 
ATOM   5092  C  CG  . LEU E  1 85  ? 126.794 85.706  43.904 1.00   26.74 ? 84   LEU E CG  1 
ATOM   5093  C  CD1 . LEU E  1 85  ? 127.520 86.854  44.584 1.00   25.65 ? 84   LEU E CD1 1 
ATOM   5094  C  CD2 . LEU E  1 85  ? 127.598 85.169  42.729 1.00   26.87 ? 84   LEU E CD2 1 
ATOM   5095  N  N   . GLY E  1 86  ? 124.292 81.716  45.386 1.00   27.97 ? 85   GLY E N   1 
ATOM   5096  C  CA  . GLY E  1 86  ? 124.124 80.436  46.076 1.00   28.13 ? 85   GLY E CA  1 
ATOM   5097  C  C   . GLY E  1 86  ? 124.224 80.532  47.587 1.00   27.62 ? 85   GLY E C   1 
ATOM   5098  O  O   . GLY E  1 86  ? 123.564 81.379  48.215 1.00   27.93 ? 85   GLY E O   1 
ATOM   5099  N  N   . ASN E  1 87  ? 125.049 79.662  48.175 1.00   26.41 ? 86   ASN E N   1 
ATOM   5100  C  CA  . ASN E  1 87  ? 125.172 79.590  49.626 1.00   25.28 ? 86   ASN E CA  1 
ATOM   5101  C  C   . ASN E  1 87  ? 126.592 79.738  50.102 1.00   23.99 ? 86   ASN E C   1 
ATOM   5102  O  O   . ASN E  1 87  ? 127.525 79.292  49.442 1.00   23.16 ? 86   ASN E O   1 
ATOM   5103  C  CB  . ASN E  1 87  ? 124.634 78.253  50.154 1.00   26.51 ? 86   ASN E CB  1 
ATOM   5104  C  CG  . ASN E  1 87  ? 123.142 78.112  49.956 1.00   27.58 ? 86   ASN E CG  1 
ATOM   5105  O  OD1 . ASN E  1 87  ? 122.354 78.825  50.590 1.00   29.40 ? 86   ASN E OD1 1 
ATOM   5106  N  ND2 . ASN E  1 87  ? 122.744 77.226  49.048 1.00   27.49 ? 86   ASN E ND2 1 
ATOM   5107  N  N   . VAL E  1 88  ? 126.733 80.350  51.273 1.00   22.35 ? 87   VAL E N   1 
ATOM   5108  C  CA  . VAL E  1 88  ? 127.987 80.345  52.002 1.00   21.67 ? 87   VAL E CA  1 
ATOM   5109  C  C   . VAL E  1 88  ? 127.745 79.434  53.183 1.00   21.86 ? 87   VAL E C   1 
ATOM   5110  O  O   . VAL E  1 88  ? 126.590 79.223  53.567 1.00   22.41 ? 87   VAL E O   1 
ATOM   5111  C  CB  . VAL E  1 88  ? 128.412 81.785  52.418 1.00   21.31 ? 87   VAL E CB  1 
ATOM   5112  C  CG1 . VAL E  1 88  ? 128.758 82.601  51.161 1.00   20.57 ? 87   VAL E CG1 1 
ATOM   5113  C  CG2 . VAL E  1 88  ? 127.318 82.460  53.240 1.00   21.47 ? 87   VAL E CG2 1 
ATOM   5114  N  N   . THR E  1 89  ? 128.817 78.876  53.738 1.00   21.77 ? 88   THR E N   1 
ATOM   5115  C  CA  . THR E  1 89  ? 128.713 77.916  54.818 1.00   21.88 ? 88   THR E CA  1 
ATOM   5116  C  C   . THR E  1 89  ? 129.443 78.404  56.071 1.00   22.38 ? 88   THR E C   1 
ATOM   5117  O  O   . THR E  1 89  ? 130.664 78.589  56.043 1.00   22.06 ? 88   THR E O   1 
ATOM   5118  C  CB  . THR E  1 89  ? 129.256 76.529  54.388 1.00   21.63 ? 88   THR E CB  1 
ATOM   5119  O  OG1 . THR E  1 89  ? 128.511 76.065  53.252 1.00   21.59 ? 88   THR E OG1 1 
ATOM   5120  C  CG2 . THR E  1 89  ? 129.123 75.525  55.541 1.00   21.88 ? 88   THR E CG2 1 
ATOM   5121  N  N   . ALA E  1 90  ? 128.675 78.603  57.158 1.00   22.49 ? 89   ALA E N   1 
ATOM   5122  C  CA  . ALA E  1 90  ? 129.230 78.948  58.460 1.00   23.21 ? 89   ALA E CA  1 
ATOM   5123  C  C   . ALA E  1 90  ? 129.579 77.679  59.241 1.00   24.13 ? 89   ALA E C   1 
ATOM   5124  O  O   . ALA E  1 90  ? 128.783 76.723  59.316 1.00   23.22 ? 89   ALA E O   1 
ATOM   5125  C  CB  . ALA E  1 90  ? 128.258 79.811  59.269 1.00   23.35 ? 89   ALA E CB  1 
ATOM   5126  N  N   . ASP E  1 91  ? 130.780 77.685  59.819 1.00   24.28 ? 90   ASP E N   1 
ATOM   5127  C  CA  . ASP E  1 91  ? 131.229 76.615  60.682 1.00   24.65 ? 90   ASP E CA  1 
ATOM   5128  C  C   . ASP E  1 91  ? 130.566 76.698  62.060 1.00   26.20 ? 90   ASP E C   1 
ATOM   5129  O  O   . ASP E  1 91  ? 129.727 77.561  62.317 1.00   25.80 ? 90   ASP E O   1 
ATOM   5130  C  CB  . ASP E  1 91  ? 132.759 76.605  60.778 1.00   24.64 ? 90   ASP E CB  1 
ATOM   5131  C  CG  . ASP E  1 91  ? 133.338 77.841  61.457 1.00   24.66 ? 90   ASP E CG  1 
ATOM   5132  O  OD1 . ASP E  1 91  ? 132.630 78.558  62.194 1.00   24.36 ? 90   ASP E OD1 1 
ATOM   5133  O  OD2 . ASP E  1 91  ? 134.537 78.075  61.246 1.00   25.14 ? 90   ASP E OD2 1 
ATOM   5134  N  N   . LYS E  1 92  ? 130.931 75.777  62.934 1.00   27.92 ? 91   LYS E N   1 
ATOM   5135  C  CA  . LYS E  1 92  ? 130.348 75.696  64.269 1.00   30.73 ? 91   LYS E CA  1 
ATOM   5136  C  C   . LYS E  1 92  ? 130.656 76.930  65.139 1.00   31.66 ? 91   LYS E C   1 
ATOM   5137  O  O   . LYS E  1 92  ? 129.969 77.170  66.126 1.00   32.07 ? 91   LYS E O   1 
ATOM   5138  C  CB  . LYS E  1 92  ? 130.814 74.415  64.971 1.00   32.23 ? 91   LYS E CB  1 
ATOM   5139  C  CG  . LYS E  1 92  ? 132.304 74.419  65.263 1.00   36.29 ? 91   LYS E CG  1 
ATOM   5140  C  CD  . LYS E  1 92  ? 132.785 73.112  65.897 1.00   39.82 ? 91   LYS E CD  1 
ATOM   5141  C  CE  . LYS E  1 92  ? 134.150 73.271  66.560 1.00   41.27 ? 91   LYS E CE  1 
ATOM   5142  N  NZ  . LYS E  1 92  ? 134.591 71.958  67.135 1.00   44.84 ? 91   LYS E NZ  1 
ATOM   5143  N  N   . ASP E  1 93  ? 131.681 77.703  64.779 1.00   30.89 ? 92   ASP E N   1 
ATOM   5144  C  CA  . ASP E  1 93  ? 131.952 78.972  65.451 1.00   31.44 ? 92   ASP E CA  1 
ATOM   5145  C  C   . ASP E  1 93  ? 131.163 80.150  64.850 1.00   29.93 ? 92   ASP E C   1 
ATOM   5146  O  O   . ASP E  1 93  ? 131.331 81.298  65.272 1.00   29.72 ? 92   ASP E O   1 
ATOM   5147  C  CB  . ASP E  1 93  ? 133.459 79.270  65.394 1.00   33.01 ? 92   ASP E CB  1 
ATOM   5148  C  CG  . ASP E  1 93  ? 134.286 78.253  66.167 1.00   35.08 ? 92   ASP E CG  1 
ATOM   5149  O  OD1 . ASP E  1 93  ? 133.880 77.870  67.287 1.00   35.87 ? 92   ASP E OD1 1 
ATOM   5150  O  OD2 . ASP E  1 93  ? 135.358 77.852  65.664 1.00   37.84 ? 92   ASP E OD2 1 
ATOM   5151  N  N   . GLY E  1 94  ? 130.334 79.876  63.846 1.00   27.51 ? 93   GLY E N   1 
ATOM   5152  C  CA  . GLY E  1 94  ? 129.538 80.912  63.208 1.00   26.34 ? 93   GLY E CA  1 
ATOM   5153  C  C   . GLY E  1 94  ? 130.280 81.751  62.190 1.00   25.09 ? 93   GLY E C   1 
ATOM   5154  O  O   . GLY E  1 94  ? 129.835 82.854  61.864 1.00   24.73 ? 93   GLY E O   1 
ATOM   5155  N  N   . VAL E  1 95  ? 131.388 81.220  61.666 1.00   24.55 ? 94   VAL E N   1 
ATOM   5156  C  CA  . VAL E  1 95  ? 132.222 81.923  60.669 1.00   23.84 ? 94   VAL E CA  1 
ATOM   5157  C  C   . VAL E  1 95  ? 132.078 81.297  59.267 1.00   23.06 ? 94   VAL E C   1 
ATOM   5158  O  O   . VAL E  1 95  ? 132.330 80.110  59.087 1.00   22.27 ? 94   VAL E O   1 
ATOM   5159  C  CB  . VAL E  1 95  ? 133.707 81.934  61.089 1.00   23.99 ? 94   VAL E CB  1 
ATOM   5160  C  CG1 . VAL E  1 95  ? 134.574 82.604  60.017 1.00   23.10 ? 94   VAL E CG1 1 
ATOM   5161  C  CG2 . VAL E  1 95  ? 133.877 82.626  62.450 1.00   24.57 ? 94   VAL E CG2 1 
ATOM   5162  N  N   . ALA E  1 96  ? 131.638 82.083  58.287 1.00   23.03 ? 95   ALA E N   1 
ATOM   5163  C  CA  . ALA E  1 96  ? 131.656 81.630  56.885 1.00   23.19 ? 95   ALA E CA  1 
ATOM   5164  C  C   . ALA E  1 96  ? 132.847 82.291  56.222 1.00   23.61 ? 95   ALA E C   1 
ATOM   5165  O  O   . ALA E  1 96  ? 132.894 83.523  56.066 1.00   22.62 ? 95   ALA E O   1 
ATOM   5166  C  CB  . ALA E  1 96  ? 130.367 81.974  56.148 1.00   21.98 ? 95   ALA E CB  1 
ATOM   5167  N  N   . ASP E  1 97  ? 133.823 81.465  55.867 1.00   24.64 ? 96   ASP E N   1 
ATOM   5168  C  CA  . ASP E  1 97  ? 134.885 81.888  54.958 1.00   26.35 ? 96   ASP E CA  1 
ATOM   5169  C  C   . ASP E  1 97  ? 134.400 81.724  53.513 1.00   25.97 ? 96   ASP E C   1 
ATOM   5170  O  O   . ASP E  1 97  ? 134.110 80.615  53.062 1.00   25.32 ? 96   ASP E O   1 
ATOM   5171  C  CB  . ASP E  1 97  ? 136.146 81.100  55.229 1.00   28.53 ? 96   ASP E CB  1 
ATOM   5172  C  CG  . ASP E  1 97  ? 136.757 81.460  56.581 1.00   31.20 ? 96   ASP E CG  1 
ATOM   5173  O  OD1 . ASP E  1 97  ? 136.864 82.677  56.910 1.00   32.39 ? 96   ASP E OD1 1 
ATOM   5174  O  OD2 . ASP E  1 97  ? 137.114 80.531  57.331 1.00   34.56 ? 96   ASP E OD2 1 
ATOM   5175  N  N   . VAL E  1 98  ? 134.270 82.853  52.821 1.00   24.98 ? 97   VAL E N   1 
ATOM   5176  C  CA  . VAL E  1 98  ? 133.686 82.906  51.498 1.00   24.28 ? 97   VAL E CA  1 
ATOM   5177  C  C   . VAL E  1 98  ? 134.790 82.863  50.448 1.00   25.20 ? 97   VAL E C   1 
ATOM   5178  O  O   . VAL E  1 98  ? 135.807 83.565  50.565 1.00   25.06 ? 97   VAL E O   1 
ATOM   5179  C  CB  . VAL E  1 98  ? 132.867 84.203  51.331 1.00   23.86 ? 97   VAL E CB  1 
ATOM   5180  C  CG1 . VAL E  1 98  ? 132.424 84.378  49.885 1.00   23.07 ? 97   VAL E CG1 1 
ATOM   5181  C  CG2 . VAL E  1 98  ? 131.661 84.212  52.295 1.00   23.16 ? 97   VAL E CG2 1 
ATOM   5182  N  N   . SER E  1 99  ? 134.579 82.035  49.424 1.00   25.76 ? 98   SER E N   1 
ATOM   5183  C  CA  . SER E  1 99  ? 135.515 81.898  48.299 1.00   27.19 ? 98   SER E CA  1 
ATOM   5184  C  C   . SER E  1 99  ? 134.760 81.362  47.080 1.00   27.76 ? 98   SER E C   1 
ATOM   5185  O  O   . SER E  1 99  ? 134.464 80.159  46.969 1.00   26.76 ? 98   SER E O   1 
ATOM   5186  C  CB  . SER E  1 99  ? 136.692 80.999  48.658 1.00   27.74 ? 98   SER E CB  1 
ATOM   5187  O  OG  . SER E  1 99  ? 137.695 81.090  47.654 1.00   30.18 ? 98   SER E OG  1 
ATOM   5188  N  N   . ILE E  1 100 ? 134.421 82.289  46.196 1.00   28.34 ? 99   ILE E N   1 
ATOM   5189  C  CA  . ILE E  1 100 ? 133.513 82.057  45.081 1.00   29.68 ? 99   ILE E CA  1 
ATOM   5190  C  C   . ILE E  1 100 ? 134.172 82.642  43.838 1.00   30.97 ? 99   ILE E C   1 
ATOM   5191  O  O   . ILE E  1 100 ? 134.815 83.693  43.893 1.00   29.60 ? 99   ILE E O   1 
ATOM   5192  C  CB  . ILE E  1 100 ? 132.162 82.795  45.310 1.00   29.89 ? 99   ILE E CB  1 
ATOM   5193  C  CG1 . ILE E  1 100 ? 131.353 82.159  46.441 1.00   30.90 ? 99   ILE E CG1 1 
ATOM   5194  C  CG2 . ILE E  1 100 ? 131.294 82.832  44.057 1.00   30.46 ? 99   ILE E CG2 1 
ATOM   5195  C  CD1 . ILE E  1 100 ? 130.028 82.880  46.728 1.00   30.44 ? 99   ILE E CD1 1 
ATOM   5196  N  N   . GLU E  1 101 ? 134.040 81.934  42.721 1.00   33.77 ? 100  GLU E N   1 
ATOM   5197  C  CA  . GLU E  1 101 ? 134.281 82.525  41.418 1.00   35.33 ? 100  GLU E CA  1 
ATOM   5198  C  C   . GLU E  1 101 ? 133.002 82.439  40.615 1.00   35.60 ? 100  GLU E C   1 
ATOM   5199  O  O   . GLU E  1 101 ? 132.359 81.376  40.568 1.00   36.09 ? 100  GLU E O   1 
ATOM   5200  C  CB  . GLU E  1 101 ? 135.434 81.844  40.688 1.00   38.60 ? 100  GLU E CB  1 
ATOM   5201  C  CG  . GLU E  1 101 ? 136.000 82.735  39.590 1.00   41.43 ? 100  GLU E CG  1 
ATOM   5202  C  CD  . GLU E  1 101 ? 137.188 82.117  38.905 1.00   44.80 ? 100  GLU E CD  1 
ATOM   5203  O  OE1 . GLU E  1 101 ? 136.984 81.133  38.157 1.00   46.74 ? 100  GLU E OE1 1 
ATOM   5204  O  OE2 . GLU E  1 101 ? 138.316 82.621  39.116 1.00   47.93 ? 100  GLU E OE2 1 
ATOM   5205  N  N   . ASP E  1 102 ? 132.619 83.561  40.006 1.00   34.59 ? 101  ASP E N   1 
ATOM   5206  C  CA  . ASP E  1 102 ? 131.394 83.635  39.218 1.00   34.62 ? 101  ASP E CA  1 
ATOM   5207  C  C   . ASP E  1 102 ? 131.650 84.457  37.980 1.00   35.86 ? 101  ASP E C   1 
ATOM   5208  O  O   . ASP E  1 102 ? 132.309 85.489  38.054 1.00   36.84 ? 101  ASP E O   1 
ATOM   5209  C  CB  . ASP E  1 102 ? 130.283 84.279  40.041 1.00   34.11 ? 101  ASP E CB  1 
ATOM   5210  C  CG  . ASP E  1 102 ? 128.911 84.100  39.421 1.00   34.32 ? 101  ASP E CG  1 
ATOM   5211  O  OD1 . ASP E  1 102 ? 128.302 83.015  39.588 1.00   34.87 ? 101  ASP E OD1 1 
ATOM   5212  O  OD2 . ASP E  1 102 ? 128.424 85.052  38.793 1.00   33.56 ? 101  ASP E OD2 1 
ATOM   5213  N  N   . SER E  1 103 ? 131.110 84.010  36.849 1.00   37.10 ? 102  SER E N   1 
ATOM   5214  C  CA  . SER E  1 103 ? 131.317 84.676  35.562 1.00   38.67 ? 102  SER E CA  1 
ATOM   5215  C  C   . SER E  1 103 ? 130.043 85.320  35.008 1.00   38.88 ? 102  SER E C   1 
ATOM   5216  O  O   . SER E  1 103 ? 130.047 85.811  33.878 1.00   39.27 ? 102  SER E O   1 
ATOM   5217  C  CB  . SER E  1 103 ? 131.837 83.668  34.543 1.00   40.26 ? 102  SER E CB  1 
ATOM   5218  O  OG  . SER E  1 103 ? 130.772 82.800  34.173 1.00   42.34 ? 102  SER E OG  1 
ATOM   5219  N  N   . VAL E  1 104 ? 128.962 85.306  35.791 1.00   38.05 ? 103  VAL E N   1 
ATOM   5220  C  CA  . VAL E  1 104 ? 127.712 85.971  35.409 1.00   38.02 ? 103  VAL E CA  1 
ATOM   5221  C  C   . VAL E  1 104 ? 127.658 87.394  35.980 1.00   37.53 ? 103  VAL E C   1 
ATOM   5222  O  O   . VAL E  1 104 ? 127.266 88.322  35.274 1.00   38.44 ? 103  VAL E O   1 
ATOM   5223  C  CB  . VAL E  1 104 ? 126.492 85.156  35.874 1.00   37.55 ? 103  VAL E CB  1 
ATOM   5224  C  CG1 . VAL E  1 104 ? 125.213 85.966  35.758 1.00   36.99 ? 103  VAL E CG1 1 
ATOM   5225  C  CG2 . VAL E  1 104 ? 126.394 83.872  35.071 1.00   36.51 ? 103  VAL E CG2 1 
ATOM   5226  N  N   . ILE E  1 105 ? 128.055 87.574  37.242 1.00   35.69 ? 104  ILE E N   1 
ATOM   5227  C  CA  . ILE E  1 105 ? 128.213 88.926  37.803 1.00   34.91 ? 104  ILE E CA  1 
ATOM   5228  C  C   . ILE E  1 105 ? 129.406 89.589  37.142 1.00   34.95 ? 104  ILE E C   1 
ATOM   5229  O  O   . ILE E  1 105 ? 130.260 88.910  36.570 1.00   34.90 ? 104  ILE E O   1 
ATOM   5230  C  CB  . ILE E  1 105 ? 128.464 88.947  39.336 1.00   34.27 ? 104  ILE E CB  1 
ATOM   5231  C  CG1 . ILE E  1 105 ? 129.774 88.211  39.695 1.00   33.98 ? 104  ILE E CG1 1 
ATOM   5232  C  CG2 . ILE E  1 105 ? 127.260 88.393  40.096 1.00   33.81 ? 104  ILE E CG2 1 
ATOM   5233  C  CD1 . ILE E  1 105 ? 130.155 88.296  41.162 1.00   34.06 ? 104  ILE E CD1 1 
ATOM   5234  N  N   . SER E  1 106 ? 129.466 90.910  37.244 1.00   34.67 ? 105  SER E N   1 
ATOM   5235  C  CA  . SER E  1 106 ? 130.585 91.695  36.723 1.00   35.00 ? 105  SER E CA  1 
ATOM   5236  C  C   . SER E  1 106 ? 130.757 92.977  37.541 1.00   34.96 ? 105  SER E C   1 
ATOM   5237  O  O   . SER E  1 106 ? 129.836 93.406  38.253 1.00   33.85 ? 105  SER E O   1 
ATOM   5238  C  CB  . SER E  1 106 ? 130.348 92.065  35.252 1.00   36.10 ? 105  SER E CB  1 
ATOM   5239  O  OG  . SER E  1 106 ? 131.491 92.697  34.687 1.00   35.71 ? 105  SER E OG  1 
ATOM   5240  N  N   . LEU E  1 107 ? 131.940 93.572  37.427 1.00   35.13 ? 106  LEU E N   1 
ATOM   5241  C  CA  . LEU E  1 107 ? 132.220 94.858  38.027 1.00   36.21 ? 106  LEU E CA  1 
ATOM   5242  C  C   . LEU E  1 107 ? 132.143 95.972  36.984 1.00   38.02 ? 106  LEU E C   1 
ATOM   5243  O  O   . LEU E  1 107 ? 132.480 97.108  37.292 1.00   37.48 ? 106  LEU E O   1 
ATOM   5244  C  CB  . LEU E  1 107 ? 133.600 94.849  38.715 1.00   35.17 ? 106  LEU E CB  1 
ATOM   5245  C  CG  . LEU E  1 107 ? 133.763 93.808  39.823 1.00   34.15 ? 106  LEU E CG  1 
ATOM   5246  C  CD1 . LEU E  1 107 ? 135.009 94.095  40.646 1.00   32.68 ? 106  LEU E CD1 1 
ATOM   5247  C  CD2 . LEU E  1 107 ? 132.525 93.740  40.711 1.00   32.79 ? 106  LEU E CD2 1 
ATOM   5248  N  N   . SER E  1 108 ? 131.718 95.631  35.761 1.00   40.31 ? 107  SER E N   1 
ATOM   5249  C  CA  . SER E  1 108 ? 131.356 96.618  34.738 1.00   42.55 ? 107  SER E CA  1 
ATOM   5250  C  C   . SER E  1 108 ? 130.295 96.079  33.762 1.00   43.82 ? 107  SER E C   1 
ATOM   5251  O  O   . SER E  1 108 ? 130.128 94.871  33.610 1.00   41.10 ? 107  SER E O   1 
ATOM   5252  C  CB  . SER E  1 108 ? 132.595 97.072  33.960 1.00   44.47 ? 107  SER E CB  1 
ATOM   5253  O  OG  . SER E  1 108 ? 133.056 96.046  33.102 1.00   46.99 ? 107  SER E OG  1 
ATOM   5254  N  N   . GLY E  1 109 ? 129.572 96.995  33.115 1.00   45.95 ? 108  GLY E N   1 
ATOM   5255  C  CA  . GLY E  1 109 ? 128.616 96.644  32.067 1.00   47.64 ? 108  GLY E CA  1 
ATOM   5256  C  C   . GLY E  1 109 ? 127.185 96.528  32.567 1.00   49.22 ? 108  GLY E C   1 
ATOM   5257  O  O   . GLY E  1 109 ? 126.826 97.081  33.609 1.00   50.04 ? 108  GLY E O   1 
ATOM   5258  N  N   . ASP E  1 110 ? 126.369 95.789  31.823 1.00   52.14 ? 109  ASP E N   1 
ATOM   5259  C  CA  . ASP E  1 110 ? 124.948 95.634  32.142 1.00   53.21 ? 109  ASP E CA  1 
ATOM   5260  C  C   . ASP E  1 110 ? 124.754 94.813  33.414 1.00   51.10 ? 109  ASP E C   1 
ATOM   5261  O  O   . ASP E  1 110 ? 123.826 95.068  34.187 1.00   50.73 ? 109  ASP E O   1 
ATOM   5262  C  CB  . ASP E  1 110 ? 124.210 94.947  30.979 1.00   56.86 ? 109  ASP E CB  1 
ATOM   5263  C  CG  . ASP E  1 110 ? 124.379 95.682  29.646 1.00   59.13 ? 109  ASP E CG  1 
ATOM   5264  O  OD1 . ASP E  1 110 ? 124.709 96.894  29.648 1.00   57.12 ? 109  ASP E OD1 1 
ATOM   5265  O  OD2 . ASP E  1 110 ? 124.180 95.029  28.596 1.00   62.39 ? 109  ASP E OD2 1 
ATOM   5266  N  N   . HIS E  1 111 ? 125.633 93.827  33.613 1.00   48.73 ? 110  HIS E N   1 
ATOM   5267  C  CA  . HIS E  1 111 ? 125.610 92.969  34.805 1.00   47.62 ? 110  HIS E CA  1 
ATOM   5268  C  C   . HIS E  1 111 ? 126.458 93.519  35.925 1.00   43.74 ? 110  HIS E C   1 
ATOM   5269  O  O   . HIS E  1 111 ? 126.868 92.775  36.812 1.00   42.32 ? 110  HIS E O   1 
ATOM   5270  C  CB  . HIS E  1 111 ? 126.078 91.552  34.448 1.00   49.25 ? 110  HIS E CB  1 
ATOM   5271  C  CG  . HIS E  1 111 ? 125.171 90.835  33.469 1.00   53.13 ? 110  HIS E CG  1 
ATOM   5272  N  ND1 . HIS E  1 111 ? 125.261 89.500  33.234 1.00   56.10 ? 110  HIS E ND1 1 
ATOM   5273  C  CD2 . HIS E  1 111 ? 124.131 91.307  32.668 1.00   54.40 ? 110  HIS E CD2 1 
ATOM   5274  C  CE1 . HIS E  1 111 ? 124.331 89.145  32.328 1.00   57.46 ? 110  HIS E CE1 1 
ATOM   5275  N  NE2 . HIS E  1 111 ? 123.639 90.252  31.982 1.00   58.31 ? 110  HIS E NE2 1 
ATOM   5276  N  N   . CYS E  1 112 ? 126.726 94.825  35.903 1.00   42.12 ? 111  CYS E N   1 
ATOM   5277  C  CA  . CYS E  1 112 ? 127.586 95.459  36.901 1.00   40.21 ? 111  CYS E CA  1 
ATOM   5278  C  C   . CYS E  1 112 ? 126.885 95.442  38.240 1.00   36.69 ? 111  CYS E C   1 
ATOM   5279  O  O   . CYS E  1 112 ? 125.720 95.790  38.313 1.00   35.86 ? 111  CYS E O   1 
ATOM   5280  C  CB  . CYS E  1 112 ? 127.893 96.909  36.515 1.00   41.63 ? 111  CYS E CB  1 
ATOM   5281  S  SG  . CYS E  1 112 ? 129.115 97.695  37.578 1.00   42.42 ? 111  CYS E SG  1 
ATOM   5282  N  N   . ILE E  1 113 ? 127.595 95.046  39.295 1.00   34.87 ? 112  ILE E N   1 
ATOM   5283  C  CA  . ILE E  1 113 ? 127.010 94.995  40.645 1.00   33.33 ? 112  ILE E CA  1 
ATOM   5284  C  C   . ILE E  1 113 ? 127.471 96.134  41.568 1.00   32.22 ? 112  ILE E C   1 
ATOM   5285  O  O   . ILE E  1 113 ? 127.022 96.210  42.714 1.00   31.70 ? 112  ILE E O   1 
ATOM   5286  C  CB  . ILE E  1 113 ? 127.250 93.620  41.333 1.00   33.03 ? 112  ILE E CB  1 
ATOM   5287  C  CG1 . ILE E  1 113 ? 128.745 93.369  41.626 1.00   32.71 ? 112  ILE E CG1 1 
ATOM   5288  C  CG2 . ILE E  1 113 ? 126.653 92.489  40.485 1.00   33.63 ? 112  ILE E CG2 1 
ATOM   5289  C  CD1 . ILE E  1 113 ? 129.019 92.067  42.381 1.00   31.66 ? 112  ILE E CD1 1 
ATOM   5290  N  N   . ILE E  1 114 ? 128.352 97.016  41.084 1.00   31.87 ? 113  ILE E N   1 
ATOM   5291  C  CA  . ILE E  1 114 ? 128.822 98.154  41.892 1.00   30.78 ? 113  ILE E CA  1 
ATOM   5292  C  C   . ILE E  1 114 ? 127.615 99.018  42.235 1.00   30.27 ? 113  ILE E C   1 
ATOM   5293  O  O   . ILE E  1 114 ? 126.808 99.300  41.370 1.00   30.35 ? 113  ILE E O   1 
ATOM   5294  C  CB  . ILE E  1 114 ? 129.848 99.054  41.140 1.00   31.38 ? 113  ILE E CB  1 
ATOM   5295  C  CG1 . ILE E  1 114 ? 131.082 98.277  40.697 1.00   31.97 ? 113  ILE E CG1 1 
ATOM   5296  C  CG2 . ILE E  1 114 ? 130.320 100.207 42.019 1.00   30.06 ? 113  ILE E CG2 1 
ATOM   5297  C  CD1 . ILE E  1 114 ? 132.003 97.901  41.820 1.00   31.96 ? 113  ILE E CD1 1 
ATOM   5298  N  N   . GLY E  1 115 ? 127.483 99.420  43.498 1.00   30.06 ? 114  GLY E N   1 
ATOM   5299  C  CA  . GLY E  1 115 ? 126.372 100.272 43.940 1.00   29.39 ? 114  GLY E CA  1 
ATOM   5300  C  C   . GLY E  1 115 ? 125.061 99.527  44.153 1.00   30.02 ? 114  GLY E C   1 
ATOM   5301  O  O   . GLY E  1 115 ? 124.007 100.147 44.338 1.00   29.10 ? 114  GLY E O   1 
ATOM   5302  N  N   . ARG E  1 116 ? 125.121 98.196  44.105 1.00   29.45 ? 115  ARG E N   1 
ATOM   5303  C  CA  . ARG E  1 116 ? 123.992 97.340  44.487 1.00   29.70 ? 115  ARG E CA  1 
ATOM   5304  C  C   . ARG E  1 116 ? 124.293 96.719  45.853 1.00   27.72 ? 115  ARG E C   1 
ATOM   5305  O  O   . ARG E  1 116 ? 125.330 97.005  46.441 1.00   26.32 ? 115  ARG E O   1 
ATOM   5306  C  CB  . ARG E  1 116 ? 123.749 96.280  43.403 1.00   31.01 ? 115  ARG E CB  1 
ATOM   5307  C  CG  . ARG E  1 116 ? 123.442 96.928  42.051 1.00   32.36 ? 115  ARG E CG  1 
ATOM   5308  C  CD  . ARG E  1 116 ? 123.001 95.944  40.992 1.00   33.28 ? 115  ARG E CD  1 
ATOM   5309  N  NE  . ARG E  1 116 ? 122.940 96.575  39.675 1.00   34.35 ? 115  ARG E NE  1 
ATOM   5310  C  CZ  . ARG E  1 116 ? 121.941 97.343  39.236 1.00   36.05 ? 115  ARG E CZ  1 
ATOM   5311  N  NH1 . ARG E  1 116 ? 120.890 97.614  40.007 1.00   35.73 ? 115  ARG E NH1 1 
ATOM   5312  N  NH2 . ARG E  1 116 ? 122.004 97.861  38.009 1.00   37.17 ? 115  ARG E NH2 1 
ATOM   5313  N  N   . THR E  1 117 ? 123.387 95.894  46.363 1.00   27.00 ? 116  THR E N   1 
ATOM   5314  C  CA  . THR E  1 117 ? 123.501 95.398  47.731 1.00   26.54 ? 116  THR E CA  1 
ATOM   5315  C  C   . THR E  1 117 ? 123.833 93.920  47.786 1.00   26.01 ? 116  THR E C   1 
ATOM   5316  O  O   . THR E  1 117 ? 123.201 93.106  47.105 1.00   27.41 ? 116  THR E O   1 
ATOM   5317  C  CB  . THR E  1 117 ? 122.217 95.690  48.531 1.00   26.97 ? 116  THR E CB  1 
ATOM   5318  O  OG1 . THR E  1 117 ? 122.066 97.111  48.666 1.00   27.32 ? 116  THR E OG1 1 
ATOM   5319  C  CG2 . THR E  1 117 ? 122.270 95.082  49.931 1.00   26.17 ? 116  THR E CG2 1 
ATOM   5320  N  N   . LEU E  1 118 ? 124.840 93.581  48.583 1.00   25.02 ? 117  LEU E N   1 
ATOM   5321  C  CA  . LEU E  1 118 ? 125.160 92.181  48.894 1.00   24.08 ? 117  LEU E CA  1 
ATOM   5322  C  C   . LEU E  1 118 ? 124.415 91.828  50.188 1.00   23.86 ? 117  LEU E C   1 
ATOM   5323  O  O   . LEU E  1 118 ? 124.469 92.591  51.159 1.00   23.38 ? 117  LEU E O   1 
ATOM   5324  C  CB  . LEU E  1 118 ? 126.671 92.004  49.070 1.00   23.68 ? 117  LEU E CB  1 
ATOM   5325  C  CG  . LEU E  1 118 ? 127.152 90.563  49.296 1.00   23.64 ? 117  LEU E CG  1 
ATOM   5326  C  CD1 . LEU E  1 118 ? 126.784 89.740  48.050 1.00   23.06 ? 117  LEU E CD1 1 
ATOM   5327  C  CD2 . LEU E  1 118 ? 128.652 90.486  49.643 1.00   21.87 ? 117  LEU E CD2 1 
ATOM   5328  N  N   . VAL E  1 119 ? 123.705 90.698  50.184 1.00   23.04 ? 118  VAL E N   1 
ATOM   5329  C  CA  . VAL E  1 119 ? 122.904 90.262  51.326 1.00   22.82 ? 118  VAL E CA  1 
ATOM   5330  C  C   . VAL E  1 119 ? 123.270 88.817  51.723 1.00   22.53 ? 118  VAL E C   1 
ATOM   5331  O  O   . VAL E  1 119 ? 123.388 87.950  50.865 1.00   22.12 ? 118  VAL E O   1 
ATOM   5332  C  CB  . VAL E  1 119 ? 121.386 90.276  51.002 1.00   23.26 ? 118  VAL E CB  1 
ATOM   5333  C  CG1 . VAL E  1 119 ? 120.569 89.818  52.204 1.00   23.25 ? 118  VAL E CG1 1 
ATOM   5334  C  CG2 . VAL E  1 119 ? 120.922 91.648  50.507 1.00   23.69 ? 118  VAL E CG2 1 
ATOM   5335  N  N   . VAL E  1 120 ? 123.445 88.578  53.021 1.00   22.53 ? 119  VAL E N   1 
ATOM   5336  C  CA  . VAL E  1 120 ? 123.544 87.234  53.557 1.00   22.72 ? 119  VAL E CA  1 
ATOM   5337  C  C   . VAL E  1 120 ? 122.251 86.921  54.323 1.00   24.17 ? 119  VAL E C   1 
ATOM   5338  O  O   . VAL E  1 120 ? 121.706 87.773  55.047 1.00   24.51 ? 119  VAL E O   1 
ATOM   5339  C  CB  . VAL E  1 120 ? 124.805 87.036  54.420 1.00   22.66 ? 119  VAL E CB  1 
ATOM   5340  C  CG1 . VAL E  1 120 ? 124.748 87.888  55.683 1.00   22.43 ? 119  VAL E CG1 1 
ATOM   5341  C  CG2 . VAL E  1 120 ? 124.981 85.542  54.741 1.00   22.16 ? 119  VAL E CG2 1 
ATOM   5342  N  N   . HIS E  1 121 ? 121.738 85.716  54.108 1.00   24.63 ? 120  HIS E N   1 
ATOM   5343  C  CA  . HIS E  1 121 ? 120.391 85.342  54.539 1.00   26.30 ? 120  HIS E CA  1 
ATOM   5344  C  C   . HIS E  1 121 ? 120.330 84.453  55.752 1.00   26.15 ? 120  HIS E C   1 
ATOM   5345  O  O   . HIS E  1 121 ? 121.320 83.830  56.169 1.00   24.84 ? 120  HIS E O   1 
ATOM   5346  C  CB  . HIS E  1 121 ? 119.631 84.677  53.387 1.00   26.89 ? 120  HIS E CB  1 
ATOM   5347  C  CG  . HIS E  1 121 ? 118.972 85.659  52.470 1.00   28.14 ? 120  HIS E CG  1 
ATOM   5348  N  ND1 . HIS E  1 121 ? 117.738 86.155  52.712 1.00   30.21 ? 120  HIS E ND1 1 
ATOM   5349  C  CD2 . HIS E  1 121 ? 119.427 86.273  51.300 1.00   27.71 ? 120  HIS E CD2 1 
ATOM   5350  C  CE1 . HIS E  1 121 ? 117.418 87.027  51.733 1.00   30.05 ? 120  HIS E CE1 1 
ATOM   5351  N  NE2 . HIS E  1 121 ? 118.452 87.094  50.871 1.00   28.42 ? 120  HIS E NE2 1 
ATOM   5352  N  N   . GLU E  1 122 ? 119.137 84.427  56.326 1.00   27.36 ? 121  GLU E N   1 
ATOM   5353  C  CA  . GLU E  1 122 ? 118.808 83.616  57.484 1.00   29.19 ? 121  GLU E CA  1 
ATOM   5354  C  C   . GLU E  1 122 ? 119.000 82.114  57.212 1.00   28.58 ? 121  GLU E C   1 
ATOM   5355  O  O   . GLU E  1 122 ? 119.507 81.402  58.061 1.00   27.92 ? 121  GLU E O   1 
ATOM   5356  C  CB  . GLU E  1 122 ? 117.351 83.902  57.859 1.00   31.67 ? 121  GLU E CB  1 
ATOM   5357  C  CG  . GLU E  1 122 ? 116.736 83.058  58.971 1.00   33.67 ? 121  GLU E CG  1 
ATOM   5358  C  CD  . GLU E  1 122 ? 115.219 83.278  59.074 1.00   35.61 ? 121  GLU E CD  1 
ATOM   5359  O  OE1 . GLU E  1 122 ? 114.676 84.177  58.396 1.00   36.40 ? 121  GLU E OE1 1 
ATOM   5360  O  OE2 . GLU E  1 122 ? 114.555 82.535  59.815 1.00   38.01 ? 121  GLU E OE2 1 
ATOM   5361  N  N   . LYS E  1 123 ? 118.597 81.654  56.030 1.00   29.28 ? 122  LYS E N   1 
ATOM   5362  C  CA  . LYS E  1 123 ? 118.554 80.226  55.735 1.00   30.65 ? 122  LYS E CA  1 
ATOM   5363  C  C   . LYS E  1 123 ? 119.216 79.885  54.414 1.00   29.64 ? 122  LYS E C   1 
ATOM   5364  O  O   . LYS E  1 123 ? 119.545 80.768  53.608 1.00   28.32 ? 122  LYS E O   1 
ATOM   5365  C  CB  . LYS E  1 123 ? 117.102 79.750  55.643 1.00   33.46 ? 122  LYS E CB  1 
ATOM   5366  C  CG  . LYS E  1 123 ? 116.172 80.193  56.761 1.00   35.62 ? 122  LYS E CG  1 
ATOM   5367  C  CD  . LYS E  1 123 ? 114.763 79.677  56.489 1.00   37.63 ? 122  LYS E CD  1 
ATOM   5368  C  CE  . LYS E  1 123 ? 113.731 80.391  57.350 1.00   40.16 ? 122  LYS E CE  1 
ATOM   5369  N  NZ  . LYS E  1 123 ? 112.376 79.788  57.208 1.00   42.45 ? 122  LYS E NZ  1 
ATOM   5370  N  N   . ALA E  1 124 ? 119.339 78.582  54.183 1.00   29.49 ? 123  ALA E N   1 
ATOM   5371  C  CA  . ALA E  1 124 ? 119.836 78.039  52.929 1.00   29.63 ? 123  ALA E CA  1 
ATOM   5372  C  C   . ALA E  1 124 ? 118.959 78.459  51.749 1.00   30.62 ? 123  ALA E C   1 
ATOM   5373  O  O   . ALA E  1 124 ? 117.733 78.439  51.821 1.00   32.42 ? 123  ALA E O   1 
ATOM   5374  C  CB  . ALA E  1 124 ? 119.918 76.516  53.021 1.00   29.35 ? 123  ALA E CB  1 
ATOM   5375  N  N   . ASP E  1 125 ? 119.605 78.898  50.683 1.00   30.51 ? 124  ASP E N   1 
ATOM   5376  C  CA  . ASP E  1 125 ? 118.954 79.113  49.400 1.00   31.52 ? 124  ASP E CA  1 
ATOM   5377  C  C   . ASP E  1 125 ? 118.721 77.710  48.832 1.00   31.71 ? 124  ASP E C   1 
ATOM   5378  O  O   . ASP E  1 125 ? 119.673 76.932  48.707 1.00   29.44 ? 124  ASP E O   1 
ATOM   5379  C  CB  . ASP E  1 125 ? 119.932 79.913  48.523 1.00   31.57 ? 124  ASP E CB  1 
ATOM   5380  C  CG  . ASP E  1 125 ? 119.373 80.302  47.165 1.00   32.76 ? 124  ASP E CG  1 
ATOM   5381  O  OD1 . ASP E  1 125 ? 118.482 79.615  46.604 1.00   34.10 ? 124  ASP E OD1 1 
ATOM   5382  O  OD2 . ASP E  1 125 ? 119.875 81.321  46.641 1.00   31.84 ? 124  ASP E OD2 1 
ATOM   5383  N  N   . ASP E  1 126 ? 117.474 77.369  48.503 1.00   33.69 ? 125  ASP E N   1 
ATOM   5384  C  CA  . ASP E  1 126 ? 117.187 76.056  47.890 1.00   34.36 ? 125  ASP E CA  1 
ATOM   5385  C  C   . ASP E  1 126 ? 117.527 75.997  46.394 1.00   34.09 ? 125  ASP E C   1 
ATOM   5386  O  O   . ASP E  1 126 ? 117.268 74.992  45.729 1.00   33.88 ? 125  ASP E O   1 
ATOM   5387  C  CB  . ASP E  1 126 ? 115.736 75.618  48.145 1.00   36.61 ? 125  ASP E CB  1 
ATOM   5388  C  CG  . ASP E  1 126 ? 114.706 76.485  47.427 1.00   38.31 ? 125  ASP E CG  1 
ATOM   5389  O  OD1 . ASP E  1 126 ? 115.025 77.112  46.392 1.00   38.37 ? 125  ASP E OD1 1 
ATOM   5390  O  OD2 . ASP E  1 126 ? 113.557 76.529  47.913 1.00   40.37 ? 125  ASP E OD2 1 
ATOM   5391  N  N   . LEU E  1 127 ? 118.088 77.089  45.872 1.00   34.04 ? 126  LEU E N   1 
ATOM   5392  C  CA  . LEU E  1 127 ? 118.601 77.161  44.500 1.00   34.55 ? 126  LEU E CA  1 
ATOM   5393  C  C   . LEU E  1 127 ? 117.514 76.945  43.430 1.00   37.22 ? 126  LEU E C   1 
ATOM   5394  O  O   . LEU E  1 127 ? 117.801 76.435  42.347 1.00   37.44 ? 126  LEU E O   1 
ATOM   5395  C  CB  . LEU E  1 127 ? 119.750 76.166  44.295 1.00   32.48 ? 126  LEU E CB  1 
ATOM   5396  C  CG  . LEU E  1 127 ? 120.834 76.139  45.374 1.00   31.54 ? 126  LEU E CG  1 
ATOM   5397  C  CD1 . LEU E  1 127 ? 121.902 75.121  44.987 1.00   30.10 ? 126  LEU E CD1 1 
ATOM   5398  C  CD2 . LEU E  1 127 ? 121.444 77.531  45.618 1.00   29.45 ? 126  LEU E CD2 1 
ATOM   5399  N  N   . GLY E  1 128 ? 116.283 77.349  43.729 1.00   40.15 ? 127  GLY E N   1 
ATOM   5400  C  CA  . GLY E  1 128 ? 115.189 77.264  42.758 1.00   45.10 ? 127  GLY E CA  1 
ATOM   5401  C  C   . GLY E  1 128 ? 114.661 75.859  42.539 1.00   48.51 ? 127  GLY E C   1 
ATOM   5402  O  O   . GLY E  1 128 ? 114.026 75.583  41.516 1.00   52.37 ? 127  GLY E O   1 
ATOM   5403  N  N   . LYS E  1 129 ? 114.910 74.982  43.509 1.00   51.58 ? 128  LYS E N   1 
ATOM   5404  C  CA  . LYS E  1 129 ? 114.566 73.565  43.415 1.00   55.43 ? 128  LYS E CA  1 
ATOM   5405  C  C   . LYS E  1 129 ? 113.707 73.110  44.598 1.00   57.10 ? 128  LYS E C   1 
ATOM   5406  O  O   . LYS E  1 129 ? 113.645 71.920  44.912 1.00   55.60 ? 128  LYS E O   1 
ATOM   5407  C  CB  . LYS E  1 129 ? 115.855 72.744  43.330 1.00   56.44 ? 128  LYS E CB  1 
ATOM   5408  C  CG  . LYS E  1 129 ? 116.550 72.876  41.983 1.00   58.46 ? 128  LYS E CG  1 
ATOM   5409  C  CD  . LYS E  1 129 ? 118.062 72.979  42.128 1.00   60.02 ? 128  LYS E CD  1 
ATOM   5410  C  CE  . LYS E  1 129 ? 118.780 72.676  40.817 1.00   60.67 ? 128  LYS E CE  1 
ATOM   5411  N  NZ  . LYS E  1 129 ? 118.977 71.210  40.637 1.00   59.46 ? 128  LYS E NZ  1 
ATOM   5412  N  N   . GLY E  1 130 ? 113.031 74.061  45.242 1.00   59.70 ? 129  GLY E N   1 
ATOM   5413  C  CA  . GLY E  1 130 ? 112.122 73.755  46.347 1.00   62.96 ? 129  GLY E CA  1 
ATOM   5414  C  C   . GLY E  1 130 ? 110.707 73.404  45.902 1.00   66.84 ? 129  GLY E C   1 
ATOM   5415  O  O   . GLY E  1 130 ? 109.885 72.989  46.726 1.00   67.88 ? 129  GLY E O   1 
ATOM   5416  N  N   . GLY E  1 131 ? 110.417 73.602  44.613 1.00   69.99 ? 130  GLY E N   1 
ATOM   5417  C  CA  . GLY E  1 131 ? 109.118 73.251  44.019 1.00   73.23 ? 130  GLY E CA  1 
ATOM   5418  C  C   . GLY E  1 131 ? 107.924 74.063  44.500 1.00   74.95 ? 130  GLY E C   1 
ATOM   5419  O  O   . GLY E  1 131 ? 106.937 73.486  44.979 1.00   76.05 ? 130  GLY E O   1 
ATOM   5420  N  N   . ASN E  1 132 ? 108.003 75.391  44.363 1.00   73.67 ? 131  ASN E N   1 
ATOM   5421  C  CA  . ASN E  1 132 ? 106.941 76.288  44.840 1.00   74.53 ? 131  ASN E CA  1 
ATOM   5422  C  C   . ASN E  1 132 ? 107.075 77.730  44.341 1.00   75.92 ? 131  ASN E C   1 
ATOM   5423  O  O   . ASN E  1 132 ? 108.043 78.074  43.660 1.00   76.11 ? 131  ASN E O   1 
ATOM   5424  C  CB  . ASN E  1 132 ? 106.870 76.268  46.379 1.00   73.78 ? 131  ASN E CB  1 
ATOM   5425  C  CG  . ASN E  1 132 ? 108.201 76.601  47.039 1.00   71.72 ? 131  ASN E CG  1 
ATOM   5426  O  OD1 . ASN E  1 132 ? 108.839 77.600  46.712 1.00   66.32 ? 131  ASN E OD1 1 
ATOM   5427  N  ND2 . ASN E  1 132 ? 108.613 75.765  47.991 1.00   71.35 ? 131  ASN E ND2 1 
ATOM   5428  N  N   . GLU E  1 133 ? 106.085 78.555  44.684 1.00   77.25 ? 132  GLU E N   1 
ATOM   5429  C  CA  . GLU E  1 133 ? 106.072 79.988  44.367 1.00   79.59 ? 132  GLU E CA  1 
ATOM   5430  C  C   . GLU E  1 133 ? 107.406 80.659  44.694 1.00   76.72 ? 132  GLU E C   1 
ATOM   5431  O  O   . GLU E  1 133 ? 108.093 81.193  43.818 1.00   75.66 ? 132  GLU E O   1 
ATOM   5432  C  CB  . GLU E  1 133 ? 104.948 80.673  45.168 1.00   82.50 ? 132  GLU E CB  1 
ATOM   5433  C  CG  . GLU E  1 133 ? 104.877 82.198  45.063 1.00   83.97 ? 132  GLU E CG  1 
ATOM   5434  C  CD  . GLU E  1 133 ? 104.022 82.698  43.904 1.00   86.88 ? 132  GLU E CD  1 
ATOM   5435  O  OE1 . GLU E  1 133 ? 103.328 81.882  43.260 1.00   86.31 ? 132  GLU E OE1 1 
ATOM   5436  O  OE2 . GLU E  1 133 ? 104.038 83.923  43.646 1.00   87.65 ? 132  GLU E OE2 1 
ATOM   5437  N  N   . GLU E  1 134 ? 107.761 80.610  45.972 1.00   74.54 ? 133  GLU E N   1 
ATOM   5438  C  CA  . GLU E  1 134 ? 108.893 81.356  46.505 1.00   71.10 ? 133  GLU E CA  1 
ATOM   5439  C  C   . GLU E  1 134 ? 110.252 80.855  45.993 1.00   66.17 ? 133  GLU E C   1 
ATOM   5440  O  O   . GLU E  1 134 ? 111.142 81.656  45.707 1.00   63.00 ? 133  GLU E O   1 
ATOM   5441  C  CB  . GLU E  1 134 ? 108.846 81.298  48.037 1.00   71.17 ? 133  GLU E CB  1 
ATOM   5442  C  CG  . GLU E  1 134 ? 109.668 82.363  48.736 1.00   71.08 ? 133  GLU E CG  1 
ATOM   5443  C  CD  . GLU E  1 134 ? 109.294 83.765  48.293 1.00   71.50 ? 133  GLU E CD  1 
ATOM   5444  O  OE1 . GLU E  1 134 ? 108.090 84.011  48.052 1.00   73.38 ? 133  GLU E OE1 1 
ATOM   5445  O  OE2 . GLU E  1 134 ? 110.207 84.611  48.176 1.00   69.46 ? 133  GLU E OE2 1 
ATOM   5446  N  N   . SER E  1 135 ? 110.401 79.539  45.863 1.00   63.31 ? 134  SER E N   1 
ATOM   5447  C  CA  . SER E  1 135 ? 111.659 78.943  45.405 1.00   61.45 ? 134  SER E CA  1 
ATOM   5448  C  C   . SER E  1 135 ? 112.144 79.582  44.101 1.00   61.05 ? 134  SER E C   1 
ATOM   5449  O  O   . SER E  1 135 ? 113.334 79.862  43.948 1.00   58.25 ? 134  SER E O   1 
ATOM   5450  C  CB  . SER E  1 135 ? 111.507 77.426  45.231 1.00   61.62 ? 134  SER E CB  1 
ATOM   5451  O  OG  . SER E  1 135 ? 112.727 76.821  44.854 1.00   58.33 ? 134  SER E OG  1 
ATOM   5452  N  N   . THR E  1 136 ? 111.214 79.846  43.184 1.00   60.45 ? 135  THR E N   1 
ATOM   5453  C  CA  . THR E  1 136 ? 111.547 80.443  41.883 1.00   59.88 ? 135  THR E CA  1 
ATOM   5454  C  C   . THR E  1 136 ? 111.860 81.941  41.949 1.00   58.12 ? 135  THR E C   1 
ATOM   5455  O  O   . THR E  1 136 ? 112.338 82.508  40.967 1.00   57.19 ? 135  THR E O   1 
ATOM   5456  C  CB  . THR E  1 136 ? 110.398 80.280  40.872 1.00   62.19 ? 135  THR E CB  1 
ATOM   5457  O  OG1 . THR E  1 136 ? 109.305 81.126  41.259 1.00   63.27 ? 135  THR E OG1 1 
ATOM   5458  C  CG2 . THR E  1 136 ? 109.939 78.830  40.796 1.00   61.85 ? 135  THR E CG2 1 
ATOM   5459  N  N   . LYS E  1 137 ? 111.569 82.581  43.081 1.00   58.19 ? 136  LYS E N   1 
ATOM   5460  C  CA  . LYS E  1 137 ? 111.849 84.012  43.269 1.00   58.68 ? 136  LYS E CA  1 
ATOM   5461  C  C   . LYS E  1 137 ? 113.088 84.242  44.137 1.00   55.49 ? 136  LYS E C   1 
ATOM   5462  O  O   . LYS E  1 137 ? 113.961 85.039  43.785 1.00   51.76 ? 136  LYS E O   1 
ATOM   5463  C  CB  . LYS E  1 137 ? 110.657 84.720  43.929 1.00   62.02 ? 136  LYS E CB  1 
ATOM   5464  C  CG  . LYS E  1 137 ? 109.325 84.612  43.191 1.00   66.09 ? 136  LYS E CG  1 
ATOM   5465  C  CD  . LYS E  1 137 ? 108.214 85.226  44.038 1.00   69.38 ? 136  LYS E CD  1 
ATOM   5466  C  CE  . LYS E  1 137 ? 106.868 85.259  43.328 1.00   72.44 ? 136  LYS E CE  1 
ATOM   5467  N  NZ  . LYS E  1 137 ? 106.687 86.480  42.490 1.00   74.77 ? 136  LYS E NZ  1 
ATOM   5468  N  N   . THR E  1 138 ? 113.149 83.549  45.276 1.00   52.77 ? 137  THR E N   1 
ATOM   5469  C  CA  . THR E  1 138 ? 114.138 83.854  46.314 1.00   49.97 ? 137  THR E CA  1 
ATOM   5470  C  C   . THR E  1 138 ? 114.935 82.678  46.870 1.00   47.14 ? 137  THR E C   1 
ATOM   5471  O  O   . THR E  1 138 ? 115.878 82.885  47.651 1.00   45.59 ? 137  THR E O   1 
ATOM   5472  C  CB  . THR E  1 138 ? 113.446 84.510  47.516 1.00   50.62 ? 137  THR E CB  1 
ATOM   5473  O  OG1 . THR E  1 138 ? 112.455 83.609  48.023 1.00   50.19 ? 137  THR E OG1 1 
ATOM   5474  C  CG2 . THR E  1 138 ? 112.810 85.854  47.107 1.00   51.05 ? 137  THR E CG2 1 
ATOM   5475  N  N   . GLY E  1 139 ? 114.549 81.455  46.510 1.00   45.99 ? 138  GLY E N   1 
ATOM   5476  C  CA  . GLY E  1 139 ? 115.191 80.256  47.043 1.00   43.55 ? 138  GLY E CA  1 
ATOM   5477  C  C   . GLY E  1 139 ? 114.809 79.948  48.483 1.00   42.70 ? 138  GLY E C   1 
ATOM   5478  O  O   . GLY E  1 139 ? 115.472 79.137  49.135 1.00   40.29 ? 138  GLY E O   1 
ATOM   5479  N  N   . ASN E  1 140 ? 113.743 80.589  48.974 1.00   42.48 ? 139  ASN E N   1 
ATOM   5480  C  CA  . ASN E  1 140 ? 113.281 80.424  50.358 1.00   42.95 ? 139  ASN E CA  1 
ATOM   5481  C  C   . ASN E  1 140 ? 114.388 80.668  51.419 1.00   40.97 ? 139  ASN E C   1 
ATOM   5482  O  O   . ASN E  1 140 ? 114.396 80.054  52.490 1.00   40.77 ? 139  ASN E O   1 
ATOM   5483  C  CB  . ASN E  1 140 ? 112.622 79.040  50.527 1.00   44.22 ? 139  ASN E CB  1 
ATOM   5484  C  CG  . ASN E  1 140 ? 111.329 78.905  49.720 1.00   46.95 ? 139  ASN E CG  1 
ATOM   5485  O  OD1 . ASN E  1 140 ? 110.311 79.489  50.074 1.00   49.43 ? 139  ASN E OD1 1 
ATOM   5486  N  ND2 . ASN E  1 140 ? 111.366 78.127  48.642 1.00   46.79 ? 139  ASN E ND2 1 
ATOM   5487  N  N   . ALA E  1 141 ? 115.298 81.600  51.135 1.00   39.57 ? 140  ALA E N   1 
ATOM   5488  C  CA  . ALA E  1 141 ? 116.455 81.863  52.025 1.00   37.15 ? 140  ALA E CA  1 
ATOM   5489  C  C   . ALA E  1 141 ? 116.086 82.647  53.286 1.00   37.50 ? 140  ALA E C   1 
ATOM   5490  O  O   . ALA E  1 141 ? 116.958 82.984  54.096 1.00   37.45 ? 140  ALA E O   1 
ATOM   5491  C  CB  . ALA E  1 141 ? 117.548 82.590  51.262 1.00   35.06 ? 140  ALA E CB  1 
ATOM   5492  N  N   . GLY E  1 142 ? 114.804 82.960  53.452 1.00   37.65 ? 141  GLY E N   1 
ATOM   5493  C  CA  . GLY E  1 142 ? 114.351 83.653  54.641 1.00   37.54 ? 141  GLY E CA  1 
ATOM   5494  C  C   . GLY E  1 142 ? 114.872 85.073  54.716 1.00   36.44 ? 141  GLY E C   1 
ATOM   5495  O  O   . GLY E  1 142 ? 115.242 85.678  53.698 1.00   36.02 ? 141  GLY E O   1 
ATOM   5496  N  N   . SER E  1 143 ? 114.924 85.589  55.936 1.00   36.29 ? 142  SER E N   1 
ATOM   5497  C  CA  . SER E  1 143 ? 115.191 86.998  56.157 1.00   36.75 ? 142  SER E CA  1 
ATOM   5498  C  C   . SER E  1 143 ? 116.645 87.406  55.834 1.00   35.33 ? 142  SER E C   1 
ATOM   5499  O  O   . SER E  1 143 ? 117.511 86.569  55.508 1.00   34.24 ? 142  SER E O   1 
ATOM   5500  C  CB  . SER E  1 143 ? 114.811 87.388  57.588 1.00   38.06 ? 142  SER E CB  1 
ATOM   5501  O  OG  . SER E  1 143 ? 115.830 87.038  58.499 1.00   38.88 ? 142  SER E OG  1 
ATOM   5502  N  N   . ARG E  1 144 ? 116.881 88.710  55.888 1.00   34.21 ? 143  ARG E N   1 
ATOM   5503  C  CA  . ARG E  1 144 ? 118.147 89.292  55.492 1.00   33.42 ? 143  ARG E CA  1 
ATOM   5504  C  C   . ARG E  1 144 ? 118.864 89.680  56.773 1.00   32.91 ? 143  ARG E C   1 
ATOM   5505  O  O   . ARG E  1 144 ? 118.469 90.626  57.429 1.00   34.69 ? 143  ARG E O   1 
ATOM   5506  C  CB  . ARG E  1 144 ? 117.886 90.507  54.594 1.00   33.90 ? 143  ARG E CB  1 
ATOM   5507  C  CG  . ARG E  1 144 ? 117.084 90.174  53.339 1.00   34.13 ? 143  ARG E CG  1 
ATOM   5508  C  CD  . ARG E  1 144 ? 116.703 91.395  52.517 1.00   34.76 ? 143  ARG E CD  1 
ATOM   5509  N  NE  . ARG E  1 144 ? 115.822 91.022  51.409 1.00   35.86 ? 143  ARG E NE  1 
ATOM   5510  C  CZ  . ARG E  1 144 ? 115.334 91.856  50.486 1.00   36.22 ? 143  ARG E CZ  1 
ATOM   5511  N  NH1 . ARG E  1 144 ? 115.626 93.161  50.502 1.00   35.70 ? 143  ARG E NH1 1 
ATOM   5512  N  NH2 . ARG E  1 144 ? 114.523 91.376  49.539 1.00   35.79 ? 143  ARG E NH2 1 
ATOM   5513  N  N   . LEU E  1 145 ? 119.887 88.921  57.154 1.00   31.65 ? 144  LEU E N   1 
ATOM   5514  C  CA  . LEU E  1 145 ? 120.569 89.127  58.436 1.00   31.51 ? 144  LEU E CA  1 
ATOM   5515  C  C   . LEU E  1 145 ? 121.542 90.298  58.349 1.00   29.79 ? 144  LEU E C   1 
ATOM   5516  O  O   . LEU E  1 145 ? 121.726 91.018  59.319 1.00   29.95 ? 144  LEU E O   1 
ATOM   5517  C  CB  . LEU E  1 145 ? 121.341 87.878  58.880 1.00   31.87 ? 144  LEU E CB  1 
ATOM   5518  C  CG  . LEU E  1 145 ? 120.627 86.518  59.008 1.00   32.67 ? 144  LEU E CG  1 
ATOM   5519  C  CD1 . LEU E  1 145 ? 121.656 85.401  59.153 1.00   32.44 ? 144  LEU E CD1 1 
ATOM   5520  C  CD2 . LEU E  1 145 ? 119.650 86.490  60.164 1.00   32.89 ? 144  LEU E CD2 1 
ATOM   5521  N  N   . ALA E  1 146 ? 122.203 90.454  57.206 1.00   28.31 ? 145  ALA E N   1 
ATOM   5522  C  CA  . ALA E  1 146 ? 123.144 91.568  57.023 1.00   27.91 ? 145  ALA E CA  1 
ATOM   5523  C  C   . ALA E  1 146 ? 123.315 91.871  55.548 1.00   27.41 ? 145  ALA E C   1 
ATOM   5524  O  O   . ALA E  1 146 ? 123.095 91.016  54.677 1.00   26.40 ? 145  ALA E O   1 
ATOM   5525  C  CB  . ALA E  1 146 ? 124.501 91.271  57.677 1.00   25.99 ? 145  ALA E CB  1 
ATOM   5526  N  N   . CYS E  1 147 ? 123.696 93.109  55.280 1.00   27.22 ? 146  CYS E N   1 
ATOM   5527  C  CA  . CYS E  1 147 ? 123.899 93.561  53.925 1.00   26.61 ? 146  CYS E CA  1 
ATOM   5528  C  C   . CYS E  1 147 ? 124.815 94.780  53.893 1.00   25.37 ? 146  CYS E C   1 
ATOM   5529  O  O   . CYS E  1 147 ? 125.131 95.352  54.930 1.00   24.82 ? 146  CYS E O   1 
ATOM   5530  C  CB  . CYS E  1 147 ? 122.557 93.936  53.333 1.00   28.04 ? 146  CYS E CB  1 
ATOM   5531  S  SG  . CYS E  1 147 ? 121.692 95.186  54.305 1.00   30.77 ? 146  CYS E SG  1 
ATOM   5532  N  N   . GLY E  1 148 ? 125.219 95.164  52.688 1.00   24.84 ? 147  GLY E N   1 
ATOM   5533  C  CA  . GLY E  1 148 ? 126.017 96.379  52.461 1.00   24.44 ? 147  GLY E CA  1 
ATOM   5534  C  C   . GLY E  1 148 ? 126.005 96.739  50.988 1.00   23.77 ? 147  GLY E C   1 
ATOM   5535  O  O   . GLY E  1 148 ? 125.687 95.905  50.147 1.00   24.40 ? 147  GLY E O   1 
ATOM   5536  N  N   . VAL E  1 149 ? 126.344 97.983  50.677 1.00   23.62 ? 148  VAL E N   1 
ATOM   5537  C  CA  . VAL E  1 149 ? 126.423 98.445  49.309 1.00   23.47 ? 148  VAL E CA  1 
ATOM   5538  C  C   . VAL E  1 149 ? 127.798 98.109  48.755 1.00   23.30 ? 148  VAL E C   1 
ATOM   5539  O  O   . VAL E  1 149 ? 128.797 98.306  49.425 1.00   24.58 ? 148  VAL E O   1 
ATOM   5540  C  CB  . VAL E  1 149 ? 126.154 99.959  49.220 1.00   24.00 ? 148  VAL E CB  1 
ATOM   5541  C  CG1 . VAL E  1 149 ? 126.201 100.423 47.783 1.00   23.74 ? 148  VAL E CG1 1 
ATOM   5542  C  CG2 . VAL E  1 149 ? 124.791 100.296 49.826 1.00   24.38 ? 148  VAL E CG2 1 
ATOM   5543  N  N   . ILE E  1 150 ? 127.846 97.578  47.541 1.00   23.22 ? 149  ILE E N   1 
ATOM   5544  C  CA  . ILE E  1 150 ? 129.101 97.172  46.914 1.00   23.46 ? 149  ILE E CA  1 
ATOM   5545  C  C   . ILE E  1 150 ? 129.757 98.421  46.318 1.00   23.95 ? 149  ILE E C   1 
ATOM   5546  O  O   . ILE E  1 150 ? 129.174 99.079  45.470 1.00   24.10 ? 149  ILE E O   1 
ATOM   5547  C  CB  . ILE E  1 150 ? 128.851 96.107  45.819 1.00   23.71 ? 149  ILE E CB  1 
ATOM   5548  C  CG1 . ILE E  1 150 ? 128.192 94.866  46.421 1.00   24.06 ? 149  ILE E CG1 1 
ATOM   5549  C  CG2 . ILE E  1 150 ? 130.135 95.709  45.098 1.00   23.27 ? 149  ILE E CG2 1 
ATOM   5550  C  CD1 . ILE E  1 150 ? 127.903 93.783  45.379 1.00   24.75 ? 149  ILE E CD1 1 
ATOM   5551  N  N   . GLY E  1 151 ? 130.942 98.773  46.814 1.00   23.99 ? 150  GLY E N   1 
ATOM   5552  C  CA  . GLY E  1 151 ? 131.602 100.022 46.449 1.00   24.94 ? 150  GLY E CA  1 
ATOM   5553  C  C   . GLY E  1 151 ? 132.888 99.771  45.697 1.00   25.74 ? 150  GLY E C   1 
ATOM   5554  O  O   . GLY E  1 151 ? 133.471 98.684  45.798 1.00   25.39 ? 150  GLY E O   1 
ATOM   5555  N  N   . ILE E  1 152 ? 133.322 100.775 44.944 1.00   26.42 ? 151  ILE E N   1 
ATOM   5556  C  CA  . ILE E  1 152 ? 134.586 100.712 44.222 1.00   27.61 ? 151  ILE E CA  1 
ATOM   5557  C  C   . ILE E  1 152 ? 135.721 100.709 45.259 1.00   28.40 ? 151  ILE E C   1 
ATOM   5558  O  O   . ILE E  1 152 ? 135.679 101.487 46.222 1.00   26.98 ? 151  ILE E O   1 
ATOM   5559  C  CB  . ILE E  1 152 ? 134.761 101.904 43.249 1.00   28.70 ? 151  ILE E CB  1 
ATOM   5560  C  CG1 . ILE E  1 152 ? 133.588 101.975 42.246 1.00   29.77 ? 151  ILE E CG1 1 
ATOM   5561  C  CG2 . ILE E  1 152 ? 136.076 101.795 42.481 1.00   28.25 ? 151  ILE E CG2 1 
ATOM   5562  C  CD1 . ILE E  1 152 ? 133.471 103.303 41.519 1.00   30.36 ? 151  ILE E CD1 1 
ATOM   5563  N  N   . ALA E  1 153 ? 136.708 99.823  45.067 1.00   29.04 ? 152  ALA E N   1 
ATOM   5564  C  CA  . ALA E  1 153 ? 137.873 99.717  45.967 1.00   30.90 ? 152  ALA E CA  1 
ATOM   5565  C  C   . ALA E  1 153 ? 139.145 100.068 45.213 1.00   32.70 ? 152  ALA E C   1 
ATOM   5566  O  O   . ALA E  1 153 ? 139.214 99.916  43.994 1.00   32.81 ? 152  ALA E O   1 
ATOM   5567  C  CB  . ALA E  1 153 ? 137.997 98.300  46.540 1.00   29.43 ? 152  ALA E CB  1 
ATOM   5568  N  N   . GLN E  1 154 ? 140.162 100.495 45.950 1.00   35.31 ? 153  GLN E N   1 
ATOM   5569  C  CA  . GLN E  1 154 ? 141.456 100.803 45.355 1.00   38.48 ? 153  GLN E CA  1 
ATOM   5570  C  C   . GLN E  1 154 ? 142.161 99.519  44.975 1.00   39.96 ? 153  GLN E C   1 
ATOM   5571  O  O   . GLN E  1 154 ? 142.103 98.537  45.726 1.00   38.42 ? 153  GLN E O   1 
ATOM   5572  C  CB  . GLN E  1 154 ? 142.341 101.565 46.324 1.00   40.67 ? 153  GLN E CB  1 
ATOM   5573  C  CG  . GLN E  1 154 ? 143.626 102.061 45.684 1.00   43.27 ? 153  GLN E CG  1 
ATOM   5574  C  CD  . GLN E  1 154 ? 144.428 102.943 46.623 1.00   45.62 ? 153  GLN E CD  1 
ATOM   5575  O  OE1 . GLN E  1 154 ? 144.621 102.600 47.786 1.00   47.92 ? 153  GLN E OE1 1 
ATOM   5576  N  NE2 . GLN E  1 154 ? 144.902 104.086 46.121 1.00   47.51 ? 153  GLN E NE2 1 
ATOM   5577  O  OXT . GLN E  1 154 ? 142.797 99.470  43.916 1.00   42.62 ? 153  GLN E OXT 1 
ATOM   5578  N  N   . ALA F  1 2   ? 135.306 68.741  41.238 1.00   32.61 ? 1    ALA F N   1 
ATOM   5579  C  CA  . ALA F  1 2   ? 135.433 69.638  42.442 1.00   30.91 ? 1    ALA F CA  1 
ATOM   5580  C  C   . ALA F  1 2   ? 136.336 70.852  42.190 1.00   28.37 ? 1    ALA F C   1 
ATOM   5581  O  O   . ALA F  1 2   ? 137.400 70.749  41.621 1.00   27.95 ? 1    ALA F O   1 
ATOM   5582  C  CB  . ALA F  1 2   ? 135.935 68.856  43.648 1.00   29.22 ? 1    ALA F CB  1 
ATOM   5583  N  N   . THR F  1 3   ? 135.873 72.014  42.606 1.00   26.29 ? 2    THR F N   1 
ATOM   5584  C  CA  . THR F  1 3   ? 136.721 73.162  42.631 1.00   24.77 ? 2    THR F CA  1 
ATOM   5585  C  C   . THR F  1 3   ? 137.019 73.506  44.087 1.00   22.42 ? 2    THR F C   1 
ATOM   5586  O  O   . THR F  1 3   ? 137.965 74.214  44.339 1.00   20.78 ? 2    THR F O   1 
ATOM   5587  C  CB  . THR F  1 3   ? 136.111 74.349  41.844 1.00   25.87 ? 2    THR F CB  1 
ATOM   5588  O  OG1 . THR F  1 3   ? 134.923 74.815  42.489 1.00   25.70 ? 2    THR F OG1 1 
ATOM   5589  C  CG2 . THR F  1 3   ? 135.735 73.920  40.446 1.00   26.83 ? 2    THR F CG2 1 
ATOM   5590  N  N   . LYS F  1 4   ? 136.220 72.989  45.032 1.00   20.99 ? 3    LYS F N   1 
ATOM   5591  C  CA  . LYS F  1 4   ? 136.473 73.174  46.454 1.00   19.91 ? 3    LYS F CA  1 
ATOM   5592  C  C   . LYS F  1 4   ? 136.323 71.891  47.286 1.00   18.27 ? 3    LYS F C   1 
ATOM   5593  O  O   . LYS F  1 4   ? 135.504 71.007  46.990 1.00   17.47 ? 3    LYS F O   1 
ATOM   5594  C  CB  . LYS F  1 4   ? 135.563 74.244  47.049 1.00   21.24 ? 3    LYS F CB  1 
ATOM   5595  C  CG  . LYS F  1 4   ? 135.543 75.572  46.303 1.00   22.94 ? 3    LYS F CG  1 
ATOM   5596  C  CD  . LYS F  1 4   ? 135.623 76.773  47.249 1.00   24.21 ? 3    LYS F CD  1 
ATOM   5597  C  CE  . LYS F  1 4   ? 134.338 77.049  47.994 1.00   24.90 ? 3    LYS F CE  1 
ATOM   5598  N  NZ  . LYS F  1 4   ? 134.418 78.269  48.852 1.00   25.70 ? 3    LYS F NZ  1 
ATOM   5599  N  N   . ALA F  1 5   ? 137.138 71.813  48.331 1.00   16.71 ? 4    ALA F N   1 
ATOM   5600  C  CA  . ALA F  1 5   ? 137.081 70.731  49.273 1.00   16.18 ? 4    ALA F CA  1 
ATOM   5601  C  C   . ALA F  1 5   ? 137.403 71.274  50.661 1.00   15.62 ? 4    ALA F C   1 
ATOM   5602  O  O   . ALA F  1 5   ? 137.929 72.384  50.800 1.00   15.61 ? 4    ALA F O   1 
ATOM   5603  C  CB  . ALA F  1 5   ? 138.036 69.588  48.887 1.00   15.64 ? 4    ALA F CB  1 
ATOM   5604  N  N   . VAL F  1 6   ? 137.083 70.473  51.677 1.00   15.15 ? 5    VAL F N   1 
ATOM   5605  C  CA  . VAL F  1 6   ? 137.266 70.870  53.055 1.00   14.90 ? 5    VAL F CA  1 
ATOM   5606  C  C   . VAL F  1 6   ? 137.547 69.641  53.917 1.00   14.83 ? 5    VAL F C   1 
ATOM   5607  O  O   . VAL F  1 6   ? 137.200 68.513  53.575 1.00   14.59 ? 5    VAL F O   1 
ATOM   5608  C  CB  . VAL F  1 6   ? 136.046 71.687  53.554 1.00   15.06 ? 5    VAL F CB  1 
ATOM   5609  C  CG1 . VAL F  1 6   ? 134.818 70.804  53.726 1.00   14.98 ? 5    VAL F CG1 1 
ATOM   5610  C  CG2 . VAL F  1 6   ? 136.380 72.473  54.849 1.00   15.02 ? 5    VAL F CG2 1 
ATOM   5611  N  N   . CYS F  1 7   ? 138.207 69.872  55.033 1.00   14.99 ? 6    CYS F N   1 
ATOM   5612  C  CA  . CYS F  1 7   ? 138.593 68.812  55.928 1.00   15.24 ? 6    CYS F CA  1 
ATOM   5613  C  C   . CYS F  1 7   ? 138.576 69.357  57.339 1.00   15.55 ? 6    CYS F C   1 
ATOM   5614  O  O   . CYS F  1 7   ? 139.149 70.429  57.603 1.00   15.35 ? 6    CYS F O   1 
ATOM   5615  C  CB  . CYS F  1 7   ? 140.005 68.353  55.575 1.00   15.23 ? 6    CYS F CB  1 
ATOM   5616  S  SG  . CYS F  1 7   ? 140.603 67.038  56.640 1.00   15.39 ? 6    CYS F SG  1 
ATOM   5617  N  N   . VAL F  1 8   ? 137.919 68.617  58.234 1.00   15.94 ? 7    VAL F N   1 
ATOM   5618  C  CA  . VAL F  1 8   ? 137.930 68.907  59.651 1.00   16.43 ? 7    VAL F CA  1 
ATOM   5619  C  C   . VAL F  1 8   ? 138.938 67.958  60.303 1.00   16.80 ? 7    VAL F C   1 
ATOM   5620  O  O   . VAL F  1 8   ? 138.792 66.741  60.225 1.00   16.83 ? 7    VAL F O   1 
ATOM   5621  C  CB  . VAL F  1 8   ? 136.518 68.705  60.267 1.00   16.74 ? 7    VAL F CB  1 
ATOM   5622  C  CG1 . VAL F  1 8   ? 136.528 68.918  61.791 1.00   16.74 ? 7    VAL F CG1 1 
ATOM   5623  C  CG2 . VAL F  1 8   ? 135.533 69.637  59.585 1.00   17.03 ? 7    VAL F CG2 1 
ATOM   5624  N  N   . LEU F  1 9   ? 139.961 68.524  60.931 1.00   17.42 ? 8    LEU F N   1 
ATOM   5625  C  CA  . LEU F  1 9   ? 140.984 67.756  61.641 1.00   18.11 ? 8    LEU F CA  1 
ATOM   5626  C  C   . LEU F  1 9   ? 140.611 67.585  63.112 1.00   18.91 ? 8    LEU F C   1 
ATOM   5627  O  O   . LEU F  1 9   ? 140.303 68.561  63.791 1.00   18.81 ? 8    LEU F O   1 
ATOM   5628  C  CB  . LEU F  1 9   ? 142.344 68.470  61.524 1.00   18.09 ? 8    LEU F CB  1 
ATOM   5629  C  CG  . LEU F  1 9   ? 142.959 68.560  60.100 1.00   18.00 ? 8    LEU F CG  1 
ATOM   5630  C  CD1 . LEU F  1 9   ? 144.118 69.552  60.071 1.00   18.00 ? 8    LEU F CD1 1 
ATOM   5631  C  CD2 . LEU F  1 9   ? 143.466 67.226  59.612 1.00   17.72 ? 8    LEU F CD2 1 
ATOM   5632  N  N   . LYS F  1 10  ? 140.679 66.345  63.581 1.00   20.06 ? 9    LYS F N   1 
ATOM   5633  C  CA  . LYS F  1 10  ? 140.365 65.943  64.947 1.00   21.98 ? 9    LYS F CA  1 
ATOM   5634  C  C   . LYS F  1 10  ? 141.289 64.790  65.338 1.00   22.49 ? 9    LYS F C   1 
ATOM   5635  O  O   . LYS F  1 10  ? 141.615 63.952  64.502 1.00   21.11 ? 9    LYS F O   1 
ATOM   5636  C  CB  . LYS F  1 10  ? 138.908 65.449  65.060 1.00   23.84 ? 9    LYS F CB  1 
ATOM   5637  C  CG  . LYS F  1 10  ? 137.859 66.548  64.884 1.00   26.03 ? 9    LYS F CG  1 
ATOM   5638  C  CD  . LYS F  1 10  ? 136.421 66.042  65.143 1.00   28.55 ? 9    LYS F CD  1 
ATOM   5639  C  CE  . LYS F  1 10  ? 135.365 67.166  64.991 1.00   29.89 ? 9    LYS F CE  1 
ATOM   5640  N  NZ  . LYS F  1 10  ? 135.921 68.481  65.450 1.00   30.74 ? 9    LYS F NZ  1 
ATOM   5641  N  N   . GLY F  1 11  ? 141.691 64.739  66.606 1.00   23.16 ? 10   GLY F N   1 
ATOM   5642  C  CA  . GLY F  1 11  ? 142.508 63.628  67.098 1.00   24.79 ? 10   GLY F CA  1 
ATOM   5643  C  C   . GLY F  1 11  ? 142.155 63.197  68.505 1.00   26.54 ? 10   GLY F C   1 
ATOM   5644  O  O   . GLY F  1 11  ? 141.101 63.559  69.024 1.00   27.24 ? 10   GLY F O   1 
ATOM   5645  N  N   . ASP F  1 12  ? 143.048 62.438  69.134 1.00   28.57 ? 11   ASP F N   1 
ATOM   5646  C  CA  . ASP F  1 12  ? 142.838 62.013  70.520 1.00   30.54 ? 11   ASP F CA  1 
ATOM   5647  C  C   . ASP F  1 12  ? 143.185 63.126  71.526 1.00   29.91 ? 11   ASP F C   1 
ATOM   5648  O  O   . ASP F  1 12  ? 142.619 63.186  72.626 1.00   31.19 ? 11   ASP F O   1 
ATOM   5649  C  CB  . ASP F  1 12  ? 143.671 60.768  70.817 1.00   32.93 ? 11   ASP F CB  1 
ATOM   5650  C  CG  . ASP F  1 12  ? 143.230 59.561  70.017 1.00   34.78 ? 11   ASP F CG  1 
ATOM   5651  O  OD1 . ASP F  1 12  ? 142.029 59.440  69.676 1.00   36.40 ? 11   ASP F OD1 1 
ATOM   5652  O  OD2 . ASP F  1 12  ? 144.099 58.712  69.745 1.00   37.28 ? 11   ASP F OD2 1 
ATOM   5653  N  N   . GLY F  1 13  ? 144.110 64.004  71.151 1.00   27.54 ? 12   GLY F N   1 
ATOM   5654  C  CA  . GLY F  1 13  ? 144.527 65.108  72.007 1.00   26.15 ? 12   GLY F CA  1 
ATOM   5655  C  C   . GLY F  1 13  ? 143.870 66.410  71.605 1.00   24.92 ? 12   GLY F C   1 
ATOM   5656  O  O   . GLY F  1 13  ? 142.788 66.418  71.048 1.00   24.21 ? 12   GLY F O   1 
ATOM   5657  N  N   . PRO F  1 14  ? 144.535 67.535  71.874 1.00   23.90 ? 13   PRO F N   1 
ATOM   5658  C  CA  . PRO F  1 14  ? 143.904 68.828  71.633 1.00   23.47 ? 13   PRO F CA  1 
ATOM   5659  C  C   . PRO F  1 14  ? 143.994 69.359  70.205 1.00   22.16 ? 13   PRO F C   1 
ATOM   5660  O  O   . PRO F  1 14  ? 143.486 70.432  69.941 1.00   22.33 ? 13   PRO F O   1 
ATOM   5661  C  CB  . PRO F  1 14  ? 144.705 69.754  72.557 1.00   24.01 ? 13   PRO F CB  1 
ATOM   5662  C  CG  . PRO F  1 14  ? 146.077 69.160  72.531 1.00   23.78 ? 13   PRO F CG  1 
ATOM   5663  C  CD  . PRO F  1 14  ? 145.821 67.677  72.570 1.00   24.05 ? 13   PRO F CD  1 
ATOM   5664  N  N   . VAL F  1 15  ? 144.659 68.665  69.286 1.00   21.52 ? 14   VAL F N   1 
ATOM   5665  C  CA  . VAL F  1 15  ? 144.880 69.263  67.974 1.00   20.46 ? 14   VAL F CA  1 
ATOM   5666  C  C   . VAL F  1 15  ? 143.607 69.263  67.137 1.00   20.11 ? 14   VAL F C   1 
ATOM   5667  O  O   . VAL F  1 15  ? 142.973 68.236  66.996 1.00   20.21 ? 14   VAL F O   1 
ATOM   5668  C  CB  . VAL F  1 15  ? 146.031 68.600  67.217 1.00   20.51 ? 14   VAL F CB  1 
ATOM   5669  C  CG1 . VAL F  1 15  ? 146.162 69.232  65.822 1.00   19.53 ? 14   VAL F CG1 1 
ATOM   5670  C  CG2 . VAL F  1 15  ? 147.318 68.730  68.024 1.00   20.26 ? 14   VAL F CG2 1 
ATOM   5671  N  N   . GLN F  1 16  ? 143.224 70.420  66.596 1.00   19.79 ? 15   GLN F N   1 
ATOM   5672  C  CA  . GLN F  1 16  ? 141.995 70.517  65.831 1.00   19.86 ? 15   GLN F CA  1 
ATOM   5673  C  C   . GLN F  1 16  ? 142.016 71.692  64.879 1.00   18.57 ? 15   GLN F C   1 
ATOM   5674  O  O   . GLN F  1 16  ? 142.677 72.691  65.117 1.00   18.11 ? 15   GLN F O   1 
ATOM   5675  C  CB  . GLN F  1 16  ? 140.749 70.576  66.746 1.00   21.69 ? 15   GLN F CB  1 
ATOM   5676  C  CG  . GLN F  1 16  ? 140.654 71.759  67.689 1.00   23.57 ? 15   GLN F CG  1 
ATOM   5677  C  CD  . GLN F  1 16  ? 139.308 71.816  68.403 1.00   26.04 ? 15   GLN F CD  1 
ATOM   5678  O  OE1 . GLN F  1 16  ? 138.247 71.877  67.765 1.00   28.53 ? 15   GLN F OE1 1 
ATOM   5679  N  NE2 . GLN F  1 16  ? 139.342 71.786  69.742 1.00   27.98 ? 15   GLN F NE2 1 
ATOM   5680  N  N   . GLY F  1 17  ? 141.309 71.560  63.774 1.00   17.32 ? 16   GLY F N   1 
ATOM   5681  C  CA  . GLY F  1 17  ? 141.245 72.657  62.826 1.00   16.78 ? 16   GLY F CA  1 
ATOM   5682  C  C   . GLY F  1 17  ? 140.453 72.327  61.595 1.00   16.07 ? 16   GLY F C   1 
ATOM   5683  O  O   . GLY F  1 17  ? 139.928 71.222  61.479 1.00   16.14 ? 16   GLY F O   1 
ATOM   5684  N  N   . ILE F  1 18  ? 140.325 73.320  60.725 1.00   15.43 ? 17   ILE F N   1 
ATOM   5685  C  CA  . ILE F  1 18  ? 139.616 73.208  59.466 1.00   15.00 ? 17   ILE F CA  1 
ATOM   5686  C  C   . ILE F  1 18  ? 140.559 73.630  58.343 1.00   14.54 ? 17   ILE F C   1 
ATOM   5687  O  O   . ILE F  1 18  ? 141.139 74.733  58.379 1.00   14.62 ? 17   ILE F O   1 
ATOM   5688  C  CB  . ILE F  1 18  ? 138.379 74.133  59.440 1.00   15.26 ? 17   ILE F CB  1 
ATOM   5689  C  CG1 . ILE F  1 18  ? 137.338 73.687  60.472 1.00   15.45 ? 17   ILE F CG1 1 
ATOM   5690  C  CG2 . ILE F  1 18  ? 137.750 74.137  58.049 1.00   15.24 ? 17   ILE F CG2 1 
ATOM   5691  C  CD1 . ILE F  1 18  ? 136.214 74.695  60.695 1.00   15.73 ? 17   ILE F CD1 1 
ATOM   5692  N  N   . ILE F  1 19  ? 140.716 72.767  57.350 1.00   14.06 ? 18   ILE F N   1 
ATOM   5693  C  CA  . ILE F  1 19  ? 141.583 73.068  56.217 1.00   13.77 ? 18   ILE F CA  1 
ATOM   5694  C  C   . ILE F  1 19  ? 140.701 73.088  54.977 1.00   13.98 ? 18   ILE F C   1 
ATOM   5695  O  O   . ILE F  1 19  ? 139.927 72.133  54.729 1.00   13.76 ? 18   ILE F O   1 
ATOM   5696  C  CB  . ILE F  1 19  ? 142.747 72.069  56.084 1.00   13.29 ? 18   ILE F CB  1 
ATOM   5697  C  CG1 . ILE F  1 19  ? 143.694 72.209  57.289 1.00   13.22 ? 18   ILE F CG1 1 
ATOM   5698  C  CG2 . ILE F  1 19  ? 143.469 72.251  54.759 1.00   13.14 ? 18   ILE F CG2 1 
ATOM   5699  C  CD1 . ILE F  1 19  ? 144.397 73.541  57.452 1.00   13.08 ? 18   ILE F CD1 1 
ATOM   5700  N  N   . ASN F  1 20  ? 140.828 74.190  54.229 1.00   14.28 ? 19   ASN F N   1 
ATOM   5701  C  CA  . ASN F  1 20  ? 140.148 74.403  52.957 1.00   14.72 ? 19   ASN F CA  1 
ATOM   5702  C  C   . ASN F  1 20  ? 141.051 74.133  51.767 1.00   14.72 ? 19   ASN F C   1 
ATOM   5703  O  O   . ASN F  1 20  ? 142.240 74.411  51.827 1.00   14.48 ? 19   ASN F O   1 
ATOM   5704  C  CB  . ASN F  1 20  ? 139.667 75.860  52.855 1.00   15.13 ? 19   ASN F CB  1 
ATOM   5705  C  CG  . ASN F  1 20  ? 138.807 76.256  54.039 1.00   15.49 ? 19   ASN F CG  1 
ATOM   5706  O  OD1 . ASN F  1 20  ? 137.644 75.864  54.129 1.00   16.05 ? 19   ASN F OD1 1 
ATOM   5707  N  ND2 . ASN F  1 20  ? 139.384 77.011  54.966 1.00   15.57 ? 19   ASN F ND2 1 
ATOM   5708  N  N   . PHE F  1 21  ? 140.463 73.582  50.705 1.00   14.94 ? 20   PHE F N   1 
ATOM   5709  C  CA  . PHE F  1 21  ? 141.146 73.348  49.451 1.00   15.22 ? 20   PHE F CA  1 
ATOM   5710  C  C   . PHE F  1 21  ? 140.365 74.040  48.320 1.00   16.01 ? 20   PHE F C   1 
ATOM   5711  O  O   . PHE F  1 21  ? 139.142 73.931  48.243 1.00   15.84 ? 20   PHE F O   1 
ATOM   5712  C  CB  . PHE F  1 21  ? 141.236 71.864  49.127 1.00   14.82 ? 20   PHE F CB  1 
ATOM   5713  C  CG  . PHE F  1 21  ? 141.931 71.035  50.172 1.00   14.45 ? 20   PHE F CG  1 
ATOM   5714  C  CD1 . PHE F  1 21  ? 141.261 70.638  51.323 1.00   14.38 ? 20   PHE F CD1 1 
ATOM   5715  C  CD2 . PHE F  1 21  ? 143.225 70.623  49.989 1.00   14.19 ? 20   PHE F CD2 1 
ATOM   5716  C  CE1 . PHE F  1 21  ? 141.880 69.837  52.260 1.00   14.10 ? 20   PHE F CE1 1 
ATOM   5717  C  CE2 . PHE F  1 21  ? 143.859 69.852  50.940 1.00   14.10 ? 20   PHE F CE2 1 
ATOM   5718  C  CZ  . PHE F  1 21  ? 143.180 69.449  52.069 1.00   14.01 ? 20   PHE F CZ  1 
ATOM   5719  N  N   . GLU F  1 22  ? 141.094 74.715  47.442 1.00   16.89 ? 21   GLU F N   1 
ATOM   5720  C  CA  . GLU F  1 22  ? 140.487 75.378  46.276 1.00   18.33 ? 21   GLU F CA  1 
ATOM   5721  C  C   . GLU F  1 22  ? 141.323 75.134  45.032 1.00   18.66 ? 21   GLU F C   1 
ATOM   5722  O  O   . GLU F  1 22  ? 142.541 75.281  45.031 1.00   18.23 ? 21   GLU F O   1 
ATOM   5723  C  CB  . GLU F  1 22  ? 140.357 76.885  46.518 1.00   19.16 ? 21   GLU F CB  1 
ATOM   5724  C  CG  . GLU F  1 22  ? 139.527 77.587  45.444 1.00   20.53 ? 21   GLU F CG  1 
ATOM   5725  C  CD  . GLU F  1 22  ? 139.027 78.954  45.878 0.50   21.25 ? 21   GLU F CD  1 
ATOM   5726  O  OE1 . GLU F  1 22  ? 139.837 79.727  46.437 0.50   21.77 ? 21   GLU F OE1 1 
ATOM   5727  O  OE2 . GLU F  1 22  ? 137.827 79.234  45.667 0.50   21.73 ? 21   GLU F OE2 1 
ATOM   5728  N  N   . GLN F  1 23  ? 140.655 74.760  43.971 1.00   19.88 ? 22   GLN F N   1 
ATOM   5729  C  CA  . GLN F  1 23  ? 141.282 74.551  42.688 1.00   21.39 ? 22   GLN F CA  1 
ATOM   5730  C  C   . GLN F  1 23  ? 140.346 75.103  41.619 1.00   23.91 ? 22   GLN F C   1 
ATOM   5731  O  O   . GLN F  1 23  ? 139.334 74.494  41.289 1.00   24.22 ? 22   GLN F O   1 
ATOM   5732  C  CB  . GLN F  1 23  ? 141.496 73.055  42.490 1.00   20.84 ? 22   GLN F CB  1 
ATOM   5733  C  CG  . GLN F  1 23  ? 142.352 72.691  41.292 1.00   20.74 ? 22   GLN F CG  1 
ATOM   5734  C  CD  . GLN F  1 23  ? 142.473 71.196  41.106 1.00   20.25 ? 22   GLN F CD  1 
ATOM   5735  O  OE1 . GLN F  1 23  ? 141.572 70.451  41.479 1.00   20.00 ? 22   GLN F OE1 1 
ATOM   5736  N  NE2 . GLN F  1 23  ? 143.592 70.745  40.533 1.00   19.86 ? 22   GLN F NE2 1 
ATOM   5737  N  N   . LYS F  1 24  ? 140.669 76.266  41.085 1.00   27.62 ? 23   LYS F N   1 
ATOM   5738  C  CA  . LYS F  1 24  ? 139.740 76.937  40.173 1.00   30.92 ? 23   LYS F CA  1 
ATOM   5739  C  C   . LYS F  1 24  ? 139.836 76.365  38.764 1.00   31.84 ? 23   LYS F C   1 
ATOM   5740  O  O   . LYS F  1 24  ? 138.869 76.412  38.014 1.00   32.32 ? 23   LYS F O   1 
ATOM   5741  C  CB  . LYS F  1 24  ? 139.923 78.452  40.183 1.00   33.91 ? 23   LYS F CB  1 
ATOM   5742  C  CG  . LYS F  1 24  ? 141.287 78.971  39.774 1.00   36.99 ? 23   LYS F CG  1 
ATOM   5743  C  CD  . LYS F  1 24  ? 141.291 80.501  39.856 1.00   39.98 ? 23   LYS F CD  1 
ATOM   5744  C  CE  . LYS F  1 24  ? 141.966 81.167  38.661 1.00   42.15 ? 23   LYS F CE  1 
ATOM   5745  N  NZ  . LYS F  1 24  ? 143.438 81.301  38.865 1.00   44.49 ? 23   LYS F NZ  1 
ATOM   5746  N  N   . GLU F  1 25  ? 140.984 75.787  38.437 1.00   32.02 ? 24   GLU F N   1 
ATOM   5747  C  CA  . GLU F  1 25  ? 141.185 75.130  37.154 1.00   33.12 ? 24   GLU F CA  1 
ATOM   5748  C  C   . GLU F  1 25  ? 141.692 73.707  37.370 1.00   32.53 ? 24   GLU F C   1 
ATOM   5749  O  O   . GLU F  1 25  ? 142.600 73.486  38.181 1.00   32.77 ? 24   GLU F O   1 
ATOM   5750  C  CB  . GLU F  1 25  ? 142.214 75.922  36.353 1.00   34.40 ? 24   GLU F CB  1 
ATOM   5751  C  CG  . GLU F  1 25  ? 141.852 77.382  36.117 1.00   34.98 ? 24   GLU F CG  1 
ATOM   5752  C  CD  . GLU F  1 25  ? 143.041 78.219  35.656 0.50   35.60 ? 24   GLU F CD  1 
ATOM   5753  O  OE1 . GLU F  1 25  ? 144.137 77.652  35.418 0.50   35.08 ? 24   GLU F OE1 1 
ATOM   5754  O  OE2 . GLU F  1 25  ? 142.876 79.455  35.525 0.50   36.00 ? 24   GLU F OE2 1 
ATOM   5755  N  N   . SER F  1 26  ? 141.132 72.747  36.645 1.00   33.27 ? 25   SER F N   1 
ATOM   5756  C  CA  . SER F  1 26  ? 141.517 71.339  36.810 1.00   34.66 ? 25   SER F CA  1 
ATOM   5757  C  C   . SER F  1 26  ? 142.979 71.060  36.445 1.00   34.54 ? 25   SER F C   1 
ATOM   5758  O  O   . SER F  1 26  ? 143.601 70.122  36.927 1.00   34.52 ? 25   SER F O   1 
ATOM   5759  C  CB  . SER F  1 26  ? 140.601 70.440  35.987 1.00   36.88 ? 25   SER F CB  1 
ATOM   5760  O  OG  . SER F  1 26  ? 140.811 70.621  34.598 1.00   38.07 ? 25   SER F OG  1 
ATOM   5761  N  N   . ASN F  1 27  ? 143.534 71.894  35.594 1.00   34.85 ? 26   ASN F N   1 
ATOM   5762  C  CA  . ASN F  1 27  ? 144.944 71.772  35.222 1.00   37.53 ? 26   ASN F CA  1 
ATOM   5763  C  C   . ASN F  1 27  ? 145.859 72.529  36.169 1.00   35.58 ? 26   ASN F C   1 
ATOM   5764  O  O   . ASN F  1 27  ? 147.019 72.799  35.820 1.00   37.90 ? 26   ASN F O   1 
ATOM   5765  C  CB  . ASN F  1 27  ? 145.156 72.356  33.809 1.00   39.83 ? 26   ASN F CB  1 
ATOM   5766  C  CG  . ASN F  1 27  ? 144.375 73.646  33.594 1.00   41.59 ? 26   ASN F CG  1 
ATOM   5767  O  OD1 . ASN F  1 27  ? 143.149 73.673  33.783 1.00   46.20 ? 26   ASN F OD1 1 
ATOM   5768  N  ND2 . ASN F  1 27  ? 145.053 74.694  33.180 1.00   39.16 ? 26   ASN F ND2 1 
ATOM   5769  N  N   . GLY F  1 28  ? 145.343 72.898  37.342 1.00   31.46 ? 27   GLY F N   1 
ATOM   5770  C  CA  . GLY F  1 28  ? 145.917 74.007  38.076 1.00   28.58 ? 27   GLY F CA  1 
ATOM   5771  C  C   . GLY F  1 28  ? 146.275 73.680  39.511 1.00   25.25 ? 27   GLY F C   1 
ATOM   5772  O  O   . GLY F  1 28  ? 145.913 72.632  40.021 1.00   24.62 ? 27   GLY F O   1 
ATOM   5773  N  N   . PRO F  1 29  ? 146.994 74.597  40.157 1.00   22.68 ? 28   PRO F N   1 
ATOM   5774  C  CA  . PRO F  1 29  ? 147.419 74.484  41.531 1.00   21.02 ? 28   PRO F CA  1 
ATOM   5775  C  C   . PRO F  1 29  ? 146.229 74.421  42.492 1.00   19.25 ? 28   PRO F C   1 
ATOM   5776  O  O   . PRO F  1 29  ? 145.193 74.986  42.219 1.00   18.55 ? 28   PRO F O   1 
ATOM   5777  C  CB  . PRO F  1 29  ? 148.202 75.773  41.780 1.00   21.52 ? 28   PRO F CB  1 
ATOM   5778  C  CG  . PRO F  1 29  ? 148.329 76.476  40.486 1.00   22.53 ? 28   PRO F CG  1 
ATOM   5779  C  CD  . PRO F  1 29  ? 147.295 75.918  39.578 1.00   23.24 ? 28   PRO F CD  1 
ATOM   5780  N  N   . VAL F  1 30  ? 146.401 73.719  43.600 1.00   17.77 ? 29   VAL F N   1 
ATOM   5781  C  CA  . VAL F  1 30  ? 145.407 73.695  44.654 1.00   17.10 ? 29   VAL F CA  1 
ATOM   5782  C  C   . VAL F  1 30  ? 145.869 74.646  45.740 1.00   16.89 ? 29   VAL F C   1 
ATOM   5783  O  O   . VAL F  1 30  ? 146.998 74.535  46.204 1.00   16.39 ? 29   VAL F O   1 
ATOM   5784  C  CB  . VAL F  1 30  ? 145.252 72.286  45.236 1.00   16.74 ? 29   VAL F CB  1 
ATOM   5785  C  CG1 . VAL F  1 30  ? 144.151 72.255  46.309 1.00   16.26 ? 29   VAL F CG1 1 
ATOM   5786  C  CG2 . VAL F  1 30  ? 144.976 71.306  44.113 1.00   16.70 ? 29   VAL F CG2 1 
ATOM   5787  N  N   . LYS F  1 31  ? 145.011 75.573  46.138 1.00   17.13 ? 30   LYS F N   1 
ATOM   5788  C  CA  . LYS F  1 31  ? 145.283 76.405  47.318 1.00   17.60 ? 30   LYS F CA  1 
ATOM   5789  C  C   . LYS F  1 31  ? 144.824 75.641  48.549 1.00   16.44 ? 30   LYS F C   1 
ATOM   5790  O  O   . LYS F  1 31  ? 143.705 75.177  48.568 1.00   16.07 ? 30   LYS F O   1 
ATOM   5791  C  CB  . LYS F  1 31  ? 144.519 77.721  47.256 1.00   18.90 ? 30   LYS F CB  1 
ATOM   5792  C  CG  . LYS F  1 31  ? 145.292 78.870  46.689 1.00   20.94 ? 30   LYS F CG  1 
ATOM   5793  C  CD  . LYS F  1 31  ? 144.435 80.137  46.511 0.50   21.64 ? 30   LYS F CD  1 
ATOM   5794  C  CE  . LYS F  1 31  ? 145.212 81.215  45.757 0.50   22.76 ? 30   LYS F CE  1 
ATOM   5795  N  NZ  . LYS F  1 31  ? 144.419 82.472  45.544 0.50   23.64 ? 30   LYS F NZ  1 
ATOM   5796  N  N   . VAL F  1 32  ? 145.689 75.516  49.553 1.00   15.81 ? 31   VAL F N   1 
ATOM   5797  C  CA  . VAL F  1 32  ? 145.370 74.839  50.827 1.00   15.44 ? 31   VAL F CA  1 
ATOM   5798  C  C   . VAL F  1 32  ? 145.522 75.877  51.951 1.00   15.73 ? 31   VAL F C   1 
ATOM   5799  O  O   . VAL F  1 32  ? 146.609 76.436  52.127 1.00   15.72 ? 31   VAL F O   1 
ATOM   5800  C  CB  . VAL F  1 32  ? 146.305 73.642  51.095 1.00   15.01 ? 31   VAL F CB  1 
ATOM   5801  C  CG1 . VAL F  1 32  ? 145.936 72.909  52.377 1.00   14.57 ? 31   VAL F CG1 1 
ATOM   5802  C  CG2 . VAL F  1 32  ? 146.340 72.657  49.927 1.00   14.87 ? 31   VAL F CG2 1 
ATOM   5803  N  N   . TRP F  1 33  ? 144.462 76.141  52.713 1.00   15.97 ? 32   TRP F N   1 
ATOM   5804  C  CA  . TRP F  1 33  ? 144.561 77.104  53.804 1.00   16.46 ? 32   TRP F CA  1 
ATOM   5805  C  C   . TRP F  1 33  ? 143.562 76.864  54.911 1.00   16.29 ? 32   TRP F C   1 
ATOM   5806  O  O   . TRP F  1 33  ? 142.514 76.273  54.691 1.00   15.99 ? 32   TRP F O   1 
ATOM   5807  C  CB  . TRP F  1 33  ? 144.432 78.526  53.253 1.00   17.46 ? 32   TRP F CB  1 
ATOM   5808  C  CG  . TRP F  1 33  ? 143.035 78.866  52.853 1.00   18.70 ? 32   TRP F CG  1 
ATOM   5809  C  CD1 . TRP F  1 33  ? 142.379 78.593  51.636 1.00   19.21 ? 32   TRP F CD1 1 
ATOM   5810  C  CD2 . TRP F  1 33  ? 142.039 79.498  53.700 1.00   19.62 ? 32   TRP F CD2 1 
ATOM   5811  N  NE1 . TRP F  1 33  ? 141.077 79.037  51.690 1.00   20.14 ? 32   TRP F NE1 1 
ATOM   5812  C  CE2 . TRP F  1 33  ? 140.826 79.607  52.905 1.00   20.16 ? 32   TRP F CE2 1 
ATOM   5813  C  CE3 . TRP F  1 33  ? 142.042 79.970  55.000 1.00   20.57 ? 32   TRP F CE3 1 
ATOM   5814  C  CZ2 . TRP F  1 33  ? 139.675 80.162  53.411 1.00   21.43 ? 32   TRP F CZ2 1 
ATOM   5815  C  CZ3 . TRP F  1 33  ? 140.875 80.548  55.511 1.00   21.29 ? 32   TRP F CZ3 1 
ATOM   5816  C  CH2 . TRP F  1 33  ? 139.717 80.640  54.732 1.00   21.94 ? 32   TRP F CH2 1 
ATOM   5817  N  N   . GLY F  1 34  ? 143.910 77.300  56.121 1.00   16.16 ? 33   GLY F N   1 
ATOM   5818  C  CA  . GLY F  1 34  ? 143.008 77.257  57.262 1.00   16.52 ? 33   GLY F CA  1 
ATOM   5819  C  C   . GLY F  1 34  ? 143.796 77.351  58.548 1.00   16.85 ? 33   GLY F C   1 
ATOM   5820  O  O   . GLY F  1 34  ? 144.944 77.752  58.546 1.00   17.19 ? 33   GLY F O   1 
ATOM   5821  N  N   . SER F  1 35  ? 143.184 76.975  59.654 1.00   17.10 ? 34   SER F N   1 
ATOM   5822  C  CA  . SER F  1 35  ? 143.776 77.154  60.969 1.00   17.09 ? 34   SER F CA  1 
ATOM   5823  C  C   . SER F  1 35  ? 143.717 75.840  61.734 1.00   17.02 ? 34   SER F C   1 
ATOM   5824  O  O   . SER F  1 35  ? 142.648 75.209  61.806 1.00   17.08 ? 34   SER F O   1 
ATOM   5825  C  CB  . SER F  1 35  ? 143.020 78.246  61.734 1.00   17.51 ? 34   SER F CB  1 
ATOM   5826  O  OG  . SER F  1 35  ? 143.723 78.593  62.898 0.50   17.94 ? 34   SER F OG  1 
ATOM   5827  N  N   . ILE F  1 36  ? 144.860 75.431  62.285 1.00   16.94 ? 35   ILE F N   1 
ATOM   5828  C  CA  . ILE F  1 36  ? 144.962 74.301  63.194 1.00   17.08 ? 35   ILE F CA  1 
ATOM   5829  C  C   . ILE F  1 36  ? 145.453 74.844  64.530 1.00   17.83 ? 35   ILE F C   1 
ATOM   5830  O  O   . ILE F  1 36  ? 146.445 75.598  64.552 1.00   17.96 ? 35   ILE F O   1 
ATOM   5831  C  CB  . ILE F  1 36  ? 145.955 73.237  62.678 1.00   16.74 ? 35   ILE F CB  1 
ATOM   5832  C  CG1 . ILE F  1 36  ? 145.712 72.943  61.175 1.00   16.68 ? 35   ILE F CG1 1 
ATOM   5833  C  CG2 . ILE F  1 36  ? 145.864 71.969  63.533 1.00   16.51 ? 35   ILE F CG2 1 
ATOM   5834  C  CD1 . ILE F  1 36  ? 146.771 72.067  60.522 1.00   16.51 ? 35   ILE F CD1 1 
ATOM   5835  N  N   . LYS F  1 37  ? 144.782 74.468  65.632 1.00   18.29 ? 36   LYS F N   1 
ATOM   5836  C  CA  . LYS F  1 37  ? 145.186 74.920  66.963 1.00   19.23 ? 36   LYS F CA  1 
ATOM   5837  C  C   . LYS F  1 37  ? 145.548 73.754  67.866 1.00   18.56 ? 36   LYS F C   1 
ATOM   5838  O  O   . LYS F  1 37  ? 145.274 72.598  67.541 1.00   17.81 ? 36   LYS F O   1 
ATOM   5839  C  CB  . LYS F  1 37  ? 144.086 75.773  67.612 1.00   20.96 ? 36   LYS F CB  1 
ATOM   5840  C  CG  . LYS F  1 37  ? 142.912 74.972  68.182 1.00   22.44 ? 36   LYS F CG  1 
ATOM   5841  C  CD  . LYS F  1 37  ? 141.919 75.917  68.895 1.00   24.03 ? 36   LYS F CD  1 
ATOM   5842  C  CE  . LYS F  1 37  ? 140.596 75.221  69.197 1.00   24.85 ? 36   LYS F CE  1 
ATOM   5843  N  NZ  . LYS F  1 37  ? 139.549 76.221  69.549 1.00   26.05 ? 36   LYS F NZ  1 
ATOM   5844  N  N   . GLY F  1 38  ? 146.166 74.073  69.005 1.00   18.24 ? 37   GLY F N   1 
ATOM   5845  C  CA  . GLY F  1 38  ? 146.575 73.064  69.966 1.00   17.87 ? 37   GLY F CA  1 
ATOM   5846  C  C   . GLY F  1 38  ? 147.850 72.327  69.608 1.00   17.37 ? 37   GLY F C   1 
ATOM   5847  O  O   . GLY F  1 38  ? 148.161 71.291  70.186 1.00   17.47 ? 37   GLY F O   1 
ATOM   5848  N  N   . LEU F  1 39  ? 148.640 72.895  68.710 1.00   16.99 ? 38   LEU F N   1 
ATOM   5849  C  CA  . LEU F  1 39  ? 149.925 72.293  68.295 1.00   16.53 ? 38   LEU F CA  1 
ATOM   5850  C  C   . LEU F  1 39  ? 151.051 72.861  69.160 1.00   16.85 ? 38   LEU F C   1 
ATOM   5851  O  O   . LEU F  1 39  ? 150.922 73.947  69.692 1.00   17.13 ? 38   LEU F O   1 
ATOM   5852  C  CB  . LEU F  1 39  ? 150.195 72.614  66.827 1.00   16.06 ? 38   LEU F CB  1 
ATOM   5853  C  CG  . LEU F  1 39  ? 149.392 71.853  65.762 1.00   15.71 ? 38   LEU F CG  1 
ATOM   5854  C  CD1 . LEU F  1 39  ? 149.365 72.604  64.430 1.00   15.41 ? 38   LEU F CD1 1 
ATOM   5855  C  CD2 . LEU F  1 39  ? 149.927 70.438  65.612 1.00   15.30 ? 38   LEU F CD2 1 
ATOM   5856  N  N   . THR F  1 40  ? 152.149 72.130  69.310 1.00   16.84 ? 39   THR F N   1 
ATOM   5857  C  CA  . THR F  1 40  ? 153.375 72.712  69.882 1.00   17.15 ? 39   THR F CA  1 
ATOM   5858  C  C   . THR F  1 40  ? 153.986 73.683  68.857 1.00   17.27 ? 39   THR F C   1 
ATOM   5859  O  O   . THR F  1 40  ? 153.927 73.434  67.648 1.00   16.89 ? 39   THR F O   1 
ATOM   5860  C  CB  . THR F  1 40  ? 154.438 71.642  70.173 1.00   17.09 ? 39   THR F CB  1 
ATOM   5861  O  OG1 . THR F  1 40  ? 154.643 70.866  68.984 1.00   16.71 ? 39   THR F OG1 1 
ATOM   5862  C  CG2 . THR F  1 40  ? 154.031 70.719  71.316 1.00   17.19 ? 39   THR F CG2 1 
ATOM   5863  N  N   . GLU F  1 41  ? 154.593 74.763  69.339 1.00   17.85 ? 40   GLU F N   1 
ATOM   5864  C  CA  . GLU F  1 41  ? 155.275 75.713  68.489 1.00   18.07 ? 40   GLU F CA  1 
ATOM   5865  C  C   . GLU F  1 41  ? 156.306 75.002  67.600 1.00   17.75 ? 40   GLU F C   1 
ATOM   5866  O  O   . GLU F  1 41  ? 157.065 74.152  68.063 1.00   18.34 ? 40   GLU F O   1 
ATOM   5867  C  CB  . GLU F  1 41  ? 155.978 76.819  69.314 1.00   18.80 ? 40   GLU F CB  1 
ATOM   5868  C  CG  . GLU F  1 41  ? 156.677 77.833  68.411 1.00   19.18 ? 40   GLU F CG  1 
ATOM   5869  C  CD  . GLU F  1 41  ? 157.319 79.012  69.146 1.00   20.36 ? 40   GLU F CD  1 
ATOM   5870  O  OE1 . GLU F  1 41  ? 157.337 78.998  70.385 1.00   20.71 ? 40   GLU F OE1 1 
ATOM   5871  O  OE2 . GLU F  1 41  ? 157.817 79.946  68.444 1.00   20.88 ? 40   GLU F OE2 1 
ATOM   5872  N  N   . GLY F  1 42  ? 156.328 75.357  66.327 1.00   16.98 ? 41   GLY F N   1 
ATOM   5873  C  CA  . GLY F  1 42  ? 157.322 74.813  65.405 1.00   16.59 ? 41   GLY F CA  1 
ATOM   5874  C  C   . GLY F  1 42  ? 156.715 74.039  64.248 1.00   15.94 ? 41   GLY F C   1 
ATOM   5875  O  O   . GLY F  1 42  ? 155.528 74.207  63.937 1.00   15.78 ? 41   GLY F O   1 
ATOM   5876  N  N   . LEU F  1 43  ? 157.526 73.171  63.653 1.00   15.52 ? 42   LEU F N   1 
ATOM   5877  C  CA  . LEU F  1 43  ? 157.204 72.492  62.395 1.00   15.22 ? 42   LEU F CA  1 
ATOM   5878  C  C   . LEU F  1 43  ? 156.467 71.190  62.620 1.00   14.80 ? 42   LEU F C   1 
ATOM   5879  O  O   . LEU F  1 43  ? 156.843 70.429  63.523 1.00   15.25 ? 42   LEU F O   1 
ATOM   5880  C  CB  . LEU F  1 43  ? 158.480 72.187  61.603 1.00   15.34 ? 42   LEU F CB  1 
ATOM   5881  C  CG  . LEU F  1 43  ? 159.230 73.364  60.975 1.00   15.58 ? 42   LEU F CG  1 
ATOM   5882  C  CD1 . LEU F  1 43  ? 160.640 72.956  60.546 1.00   15.78 ? 42   LEU F CD1 1 
ATOM   5883  C  CD2 . LEU F  1 43  ? 158.441 73.968  59.800 1.00   15.42 ? 42   LEU F CD2 1 
ATOM   5884  N  N   . HIS F  1 44  ? 155.428 70.945  61.818 1.00   14.09 ? 43   HIS F N   1 
ATOM   5885  C  CA  . HIS F  1 44  ? 154.650 69.688  61.835 1.00   13.73 ? 43   HIS F CA  1 
ATOM   5886  C  C   . HIS F  1 44  ? 154.385 69.140  60.456 1.00   13.30 ? 43   HIS F C   1 
ATOM   5887  O  O   . HIS F  1 44  ? 153.913 69.845  59.589 1.00   12.85 ? 43   HIS F O   1 
ATOM   5888  C  CB  . HIS F  1 44  ? 153.318 69.930  62.515 1.00   13.86 ? 43   HIS F CB  1 
ATOM   5889  C  CG  . HIS F  1 44  ? 153.463 70.332  63.953 1.00   14.26 ? 43   HIS F CG  1 
ATOM   5890  N  ND1 . HIS F  1 44  ? 153.543 69.419  64.973 1.00   14.42 ? 43   HIS F ND1 1 
ATOM   5891  C  CD2 . HIS F  1 44  ? 153.625 71.590  64.531 1.00   14.40 ? 43   HIS F CD2 1 
ATOM   5892  C  CE1 . HIS F  1 44  ? 153.728 70.086  66.131 1.00   14.82 ? 43   HIS F CE1 1 
ATOM   5893  N  NE2 . HIS F  1 44  ? 153.768 71.408  65.866 1.00   14.55 ? 43   HIS F NE2 1 
ATOM   5894  N  N   . GLY F  1 45  ? 154.693 67.862  60.247 1.00   13.18 ? 44   GLY F N   1 
ATOM   5895  C  CA  . GLY F  1 45  ? 154.437 67.184  58.980 1.00   12.99 ? 44   GLY F CA  1 
ATOM   5896  C  C   . GLY F  1 45  ? 152.964 67.251  58.649 1.00   12.83 ? 44   GLY F C   1 
ATOM   5897  O  O   . GLY F  1 45  ? 152.124 67.235  59.554 1.00   13.02 ? 44   GLY F O   1 
ATOM   5898  N  N   . PHE F  1 46  ? 152.666 67.325  57.361 1.00   12.66 ? 45   PHE F N   1 
ATOM   5899  C  CA  . PHE F  1 46  ? 151.354 67.643  56.813 1.00   12.58 ? 45   PHE F CA  1 
ATOM   5900  C  C   . PHE F  1 46  ? 151.241 66.878  55.511 1.00   12.62 ? 45   PHE F C   1 
ATOM   5901  O  O   . PHE F  1 46  ? 151.880 67.238  54.494 1.00   12.53 ? 45   PHE F O   1 
ATOM   5902  C  CB  . PHE F  1 46  ? 151.290 69.148  56.525 1.00   12.58 ? 45   PHE F CB  1 
ATOM   5903  C  CG  . PHE F  1 46  ? 149.898 69.705  56.340 1.00   12.55 ? 45   PHE F CG  1 
ATOM   5904  C  CD1 . PHE F  1 46  ? 148.961 69.629  57.364 1.00   12.63 ? 45   PHE F CD1 1 
ATOM   5905  C  CD2 . PHE F  1 46  ? 149.541 70.351  55.163 1.00   12.55 ? 45   PHE F CD2 1 
ATOM   5906  C  CE1 . PHE F  1 46  ? 147.683 70.195  57.224 1.00   12.67 ? 45   PHE F CE1 1 
ATOM   5907  C  CE2 . PHE F  1 46  ? 148.267 70.917  55.011 1.00   12.58 ? 45   PHE F CE2 1 
ATOM   5908  C  CZ  . PHE F  1 46  ? 147.342 70.841  56.045 1.00   12.64 ? 45   PHE F CZ  1 
ATOM   5909  N  N   . HIS F  1 47  ? 150.475 65.787  55.536 1.00   12.68 ? 46   HIS F N   1 
ATOM   5910  C  CA  . HIS F  1 47  ? 150.385 64.900  54.389 1.00   12.68 ? 46   HIS F CA  1 
ATOM   5911  C  C   . HIS F  1 47  ? 148.996 64.449  54.093 1.00   12.61 ? 46   HIS F C   1 
ATOM   5912  O  O   . HIS F  1 47  ? 148.180 64.324  55.013 1.00   12.55 ? 46   HIS F O   1 
ATOM   5913  C  CB  . HIS F  1 47  ? 151.167 63.646  54.644 1.00   12.91 ? 46   HIS F CB  1 
ATOM   5914  C  CG  . HIS F  1 47  ? 152.493 63.882  55.277 1.00   13.10 ? 46   HIS F CG  1 
ATOM   5915  N  ND1 . HIS F  1 47  ? 152.886 63.224  56.374 1.00   13.16 ? 46   HIS F ND1 1 
ATOM   5916  C  CD2 . HIS F  1 47  ? 153.550 64.702  54.899 1.00   13.00 ? 46   HIS F CD2 1 
ATOM   5917  C  CE1 . HIS F  1 47  ? 154.116 63.634  56.706 1.00   13.27 ? 46   HIS F CE1 1 
ATOM   5918  N  NE2 . HIS F  1 47  ? 154.527 64.526  55.783 1.00   13.13 ? 46   HIS F NE2 1 
ATOM   5919  N  N   . VAL F  1 48  ? 148.735 64.139  52.821 1.00   12.53 ? 47   VAL F N   1 
ATOM   5920  C  CA  . VAL F  1 48  ? 147.564 63.385  52.473 1.00   12.64 ? 47   VAL F CA  1 
ATOM   5921  C  C   . VAL F  1 48  ? 147.926 61.904  52.499 1.00   12.94 ? 47   VAL F C   1 
ATOM   5922  O  O   . VAL F  1 48  ? 148.883 61.470  51.871 1.00   13.01 ? 47   VAL F O   1 
ATOM   5923  C  CB  . VAL F  1 48  ? 146.947 63.806  51.129 1.00   12.60 ? 47   VAL F CB  1 
ATOM   5924  C  CG1 . VAL F  1 48  ? 145.736 62.933  50.797 1.00   12.60 ? 47   VAL F CG1 1 
ATOM   5925  C  CG2 . VAL F  1 48  ? 146.548 65.279  51.170 1.00   12.40 ? 47   VAL F CG2 1 
ATOM   5926  N  N   . HIS F  1 49  ? 147.168 61.140  53.265 1.00   13.31 ? 48   HIS F N   1 
ATOM   5927  C  CA  . HIS F  1 49  ? 147.368 59.699  53.367 1.00   13.87 ? 48   HIS F CA  1 
ATOM   5928  C  C   . HIS F  1 49  ? 146.346 59.015  52.535 1.00   14.38 ? 48   HIS F C   1 
ATOM   5929  O  O   . HIS F  1 49  ? 145.300 59.599  52.230 1.00   14.39 ? 48   HIS F O   1 
ATOM   5930  C  CB  . HIS F  1 49  ? 147.224 59.236  54.791 1.00   13.97 ? 48   HIS F CB  1 
ATOM   5931  C  CG  . HIS F  1 49  ? 148.404 59.539  55.634 1.00   13.95 ? 48   HIS F CG  1 
ATOM   5932  N  ND1 . HIS F  1 49  ? 149.095 58.580  56.275 1.00   14.26 ? 48   HIS F ND1 1 
ATOM   5933  C  CD2 . HIS F  1 49  ? 149.036 60.738  55.903 1.00   13.80 ? 48   HIS F CD2 1 
ATOM   5934  C  CE1 . HIS F  1 49  ? 150.111 59.155  56.930 1.00   14.34 ? 48   HIS F CE1 1 
ATOM   5935  N  NE2 . HIS F  1 49  ? 150.054 60.476  56.710 1.00   14.05 ? 48   HIS F NE2 1 
ATOM   5936  N  N   . GLU F  1 50  ? 146.627 57.764  52.188 1.00   14.98 ? 49   GLU F N   1 
ATOM   5937  C  CA  . GLU F  1 50  ? 145.909 57.075  51.138 1.00   15.58 ? 49   GLU F CA  1 
ATOM   5938  C  C   . GLU F  1 50  ? 144.406 56.864  51.370 1.00   15.78 ? 49   GLU F C   1 
ATOM   5939  O  O   . GLU F  1 50  ? 143.612 57.103  50.454 1.00   16.21 ? 49   GLU F O   1 
ATOM   5940  C  CB  . GLU F  1 50  ? 146.589 55.729  50.832 1.00   16.12 ? 49   GLU F CB  1 
ATOM   5941  C  CG  . GLU F  1 50  ? 146.016 55.065  49.606 1.00   16.66 ? 49   GLU F CG  1 
ATOM   5942  C  CD  . GLU F  1 50  ? 146.743 53.787  49.198 1.00   17.43 ? 49   GLU F CD  1 
ATOM   5943  O  OE1 . GLU F  1 50  ? 147.684 53.347  49.915 1.00   17.65 ? 49   GLU F OE1 1 
ATOM   5944  O  OE2 . GLU F  1 50  ? 146.306 53.214  48.171 1.00   17.84 ? 49   GLU F OE2 1 
ATOM   5945  N  N   . PHE F  1 51  ? 144.019 56.401  52.550 1.00   15.96 ? 50   PHE F N   1 
ATOM   5946  C  CA  . PHE F  1 51  ? 142.625 55.972  52.809 1.00   16.41 ? 50   PHE F CA  1 
ATOM   5947  C  C   . PHE F  1 51  ? 141.847 56.946  53.672 1.00   16.24 ? 50   PHE F C   1 
ATOM   5948  O  O   . PHE F  1 51  ? 142.404 57.552  54.579 1.00   15.83 ? 50   PHE F O   1 
ATOM   5949  C  CB  . PHE F  1 51  ? 142.613 54.580  53.445 1.00   16.78 ? 50   PHE F CB  1 
ATOM   5950  C  CG  . PHE F  1 51  ? 143.356 53.553  52.623 1.00   17.30 ? 50   PHE F CG  1 
ATOM   5951  C  CD1 . PHE F  1 51  ? 142.905 53.207  51.358 1.00   17.60 ? 50   PHE F CD1 1 
ATOM   5952  C  CD2 . PHE F  1 51  ? 144.513 52.952  53.098 1.00   17.72 ? 50   PHE F CD2 1 
ATOM   5953  C  CE1 . PHE F  1 51  ? 143.584 52.272  50.592 1.00   18.05 ? 50   PHE F CE1 1 
ATOM   5954  C  CE2 . PHE F  1 51  ? 145.186 51.998  52.339 1.00   18.04 ? 50   PHE F CE2 1 
ATOM   5955  C  CZ  . PHE F  1 51  ? 144.721 51.674  51.075 1.00   18.16 ? 50   PHE F CZ  1 
ATOM   5956  N  N   . GLY F  1 52  ? 140.576 57.152  53.312 1.00   16.44 ? 51   GLY F N   1 
ATOM   5957  C  CA  . GLY F  1 52  ? 139.658 57.986  54.079 1.00   16.48 ? 51   GLY F CA  1 
ATOM   5958  C  C   . GLY F  1 52  ? 138.948 57.170  55.142 1.00   16.87 ? 51   GLY F C   1 
ATOM   5959  O  O   . GLY F  1 52  ? 137.727 57.227  55.255 1.00   16.60 ? 51   GLY F O   1 
ATOM   5960  N  N   . ASP F  1 53  ? 139.741 56.443  55.930 1.00   17.50 ? 52   ASP F N   1 
ATOM   5961  C  CA  . ASP F  1 53  ? 139.254 55.428  56.882 1.00   18.40 ? 52   ASP F CA  1 
ATOM   5962  C  C   . ASP F  1 53  ? 139.641 55.880  58.280 1.00   19.25 ? 52   ASP F C   1 
ATOM   5963  O  O   . ASP F  1 53  ? 140.820 55.830  58.680 1.00   19.37 ? 52   ASP F O   1 
ATOM   5964  C  CB  . ASP F  1 53  ? 139.871 54.080  56.545 1.00   18.48 ? 52   ASP F CB  1 
ATOM   5965  C  CG  . ASP F  1 53  ? 139.322 52.933  57.389 1.00   18.93 ? 52   ASP F CG  1 
ATOM   5966  O  OD1 . ASP F  1 53  ? 138.808 53.129  58.534 1.00   18.97 ? 52   ASP F OD1 1 
ATOM   5967  O  OD2 . ASP F  1 53  ? 139.434 51.800  56.890 1.00   19.41 ? 52   ASP F OD2 1 
ATOM   5968  N  N   . ASN F  1 54  ? 138.653 56.349  59.016 1.00   20.22 ? 53   ASN F N   1 
ATOM   5969  C  CA  . ASN F  1 54  ? 138.865 56.805  60.379 1.00   21.38 ? 53   ASN F CA  1 
ATOM   5970  C  C   . ASN F  1 54  ? 138.356 55.755  61.373 1.00   21.30 ? 53   ASN F C   1 
ATOM   5971  O  O   . ASN F  1 54  ? 138.087 56.101  62.496 1.00   20.92 ? 53   ASN F O   1 
ATOM   5972  C  CB  . ASN F  1 54  ? 138.104 58.126  60.595 1.00   22.76 ? 53   ASN F CB  1 
ATOM   5973  C  CG  . ASN F  1 54  ? 138.377 58.771  61.953 1.00   24.47 ? 53   ASN F CG  1 
ATOM   5974  O  OD1 . ASN F  1 54  ? 137.436 59.206  62.653 1.00   26.87 ? 53   ASN F OD1 1 
ATOM   5975  N  ND2 . ASN F  1 54  ? 139.652 58.859  62.328 1.00   24.60 ? 53   ASN F ND2 1 
ATOM   5976  N  N   . THR F  1 55  ? 138.251 54.488  60.966 1.00   20.89 ? 54   THR F N   1 
ATOM   5977  C  CA  . THR F  1 55  ? 137.655 53.464  61.838 1.00   21.07 ? 54   THR F CA  1 
ATOM   5978  C  C   . THR F  1 55  ? 138.515 53.146  63.048 1.00   21.61 ? 54   THR F C   1 
ATOM   5979  O  O   . THR F  1 55  ? 137.984 52.790  64.087 1.00   22.03 ? 54   THR F O   1 
ATOM   5980  C  CB  . THR F  1 55  ? 137.317 52.133  61.110 1.00   20.74 ? 54   THR F CB  1 
ATOM   5981  O  OG1 . THR F  1 55  ? 138.499 51.550  60.552 1.00   20.17 ? 54   THR F OG1 1 
ATOM   5982  C  CG2 . THR F  1 55  ? 136.270 52.356  60.014 1.00   20.46 ? 54   THR F CG2 1 
ATOM   5983  N  N   . ALA F  1 56  ? 139.829 53.248  62.922 1.00   21.89 ? 55   ALA F N   1 
ATOM   5984  C  CA  . ALA F  1 56  ? 140.691 53.152  64.094 1.00   22.30 ? 55   ALA F CA  1 
ATOM   5985  C  C   . ALA F  1 56  ? 141.442 54.450  64.274 1.00   22.39 ? 55   ALA F C   1 
ATOM   5986  O  O   . ALA F  1 56  ? 142.652 54.443  64.400 1.00   24.44 ? 55   ALA F O   1 
ATOM   5987  C  CB  . ALA F  1 56  ? 141.666 51.995  63.935 1.00   22.56 ? 55   ALA F CB  1 
ATOM   5988  N  N   . GLY F  1 57  ? 140.742 55.569  64.276 1.00   22.00 ? 56   GLY F N   1 
ATOM   5989  C  CA  . GLY F  1 57  ? 141.401 56.867  64.371 1.00   21.63 ? 56   GLY F CA  1 
ATOM   5990  C  C   . GLY F  1 57  ? 142.283 57.124  63.150 1.00   21.00 ? 56   GLY F C   1 
ATOM   5991  O  O   . GLY F  1 57  ? 142.015 56.604  62.059 1.00   21.82 ? 56   GLY F O   1 
ATOM   5992  N  N   . CYS F  1 58  ? 143.350 57.883  63.335 1.00   19.88 ? 57   CYS F N   1 
ATOM   5993  C  CA  . CYS F  1 58  ? 144.231 58.257  62.227 1.00   19.02 ? 57   CYS F CA  1 
ATOM   5994  C  C   . CYS F  1 58  ? 145.097 57.094  61.722 1.00   18.72 ? 57   CYS F C   1 
ATOM   5995  O  O   . CYS F  1 58  ? 145.642 57.148  60.638 1.00   18.04 ? 57   CYS F O   1 
ATOM   5996  C  CB  . CYS F  1 58  ? 145.116 59.430  62.648 1.00   18.60 ? 57   CYS F CB  1 
ATOM   5997  S  SG  . CYS F  1 58  ? 144.189 60.899  63.134 1.00   18.66 ? 57   CYS F SG  1 
ATOM   5998  N  N   . THR F  1 59  ? 145.233 56.047  62.517 1.00   19.03 ? 58   THR F N   1 
ATOM   5999  C  CA  . THR F  1 59  ? 146.046 54.894  62.132 1.00   19.33 ? 58   THR F CA  1 
ATOM   6000  C  C   . THR F  1 59  ? 145.531 54.190  60.885 1.00   18.72 ? 58   THR F C   1 
ATOM   6001  O  O   . THR F  1 59  ? 146.314 53.706  60.075 1.00   18.87 ? 58   THR F O   1 
ATOM   6002  C  CB  . THR F  1 59  ? 146.129 53.865  63.261 1.00   20.23 ? 58   THR F CB  1 
ATOM   6003  O  OG1 . THR F  1 59  ? 146.507 54.537  64.468 1.00   21.68 ? 58   THR F OG1 1 
ATOM   6004  C  CG2 . THR F  1 59  ? 147.182 52.833  62.958 1.00   20.67 ? 58   THR F CG2 1 
ATOM   6005  N  N   . SER F  1 60  ? 144.224 54.172  60.695 1.00   18.18 ? 59   SER F N   1 
ATOM   6006  C  CA  . SER F  1 60  ? 143.685 53.433  59.586 1.00   18.02 ? 59   SER F CA  1 
ATOM   6007  C  C   . SER F  1 60  ? 143.747 54.235  58.274 1.00   17.32 ? 59   SER F C   1 
ATOM   6008  O  O   . SER F  1 60  ? 143.284 53.764  57.243 1.00   17.50 ? 59   SER F O   1 
ATOM   6009  C  CB  . SER F  1 60  ? 142.284 52.943  59.923 1.00   18.28 ? 59   SER F CB  1 
ATOM   6010  O  OG  . SER F  1 60  ? 141.487 53.976  60.423 1.00   18.42 ? 59   SER F OG  1 
ATOM   6011  N  N   . ALA F  1 61  ? 144.332 55.431  58.295 1.00   16.61 ? 60   ALA F N   1 
ATOM   6012  C  CA  . ALA F  1 61  ? 144.460 56.230  57.046 1.00   16.18 ? 60   ALA F CA  1 
ATOM   6013  C  C   . ALA F  1 61  ? 145.512 55.653  56.106 1.00   16.07 ? 60   ALA F C   1 
ATOM   6014  O  O   . ALA F  1 61  ? 145.637 56.069  54.961 1.00   15.94 ? 60   ALA F O   1 
ATOM   6015  C  CB  . ALA F  1 61  ? 144.778 57.677  57.368 1.00   15.74 ? 60   ALA F CB  1 
ATOM   6016  N  N   . GLY F  1 62  ? 146.290 54.695  56.585 1.00   16.15 ? 61   GLY F N   1 
ATOM   6017  C  CA  . GLY F  1 62  ? 147.310 54.082  55.740 1.00   16.18 ? 61   GLY F CA  1 
ATOM   6018  C  C   . GLY F  1 62  ? 148.504 54.995  55.544 1.00   15.91 ? 61   GLY F C   1 
ATOM   6019  O  O   . GLY F  1 62  ? 148.644 56.018  56.234 1.00   16.00 ? 61   GLY F O   1 
ATOM   6020  N  N   . PRO F  1 63  ? 149.380 54.647  54.607 1.00   15.86 ? 62   PRO F N   1 
ATOM   6021  C  CA  . PRO F  1 63  ? 150.574 55.448  54.323 1.00   15.76 ? 62   PRO F CA  1 
ATOM   6022  C  C   . PRO F  1 63  ? 150.276 56.704  53.461 1.00   15.37 ? 62   PRO F C   1 
ATOM   6023  O  O   . PRO F  1 63  ? 149.110 57.001  53.200 1.00   14.97 ? 62   PRO F O   1 
ATOM   6024  C  CB  . PRO F  1 63  ? 151.467 54.466  53.558 1.00   15.99 ? 62   PRO F CB  1 
ATOM   6025  C  CG  . PRO F  1 63  ? 150.508 53.594  52.832 1.00   16.27 ? 62   PRO F CG  1 
ATOM   6026  C  CD  . PRO F  1 63  ? 149.255 53.496  53.700 1.00   16.26 ? 62   PRO F CD  1 
ATOM   6027  N  N   . HIS F  1 64  ? 151.316 57.413  53.030 1.00   15.24 ? 63   HIS F N   1 
ATOM   6028  C  CA  . HIS F  1 64  ? 151.122 58.609  52.207 1.00   15.14 ? 63   HIS F CA  1 
ATOM   6029  C  C   . HIS F  1 64  ? 150.518 58.225  50.894 1.00   15.31 ? 63   HIS F C   1 
ATOM   6030  O  O   . HIS F  1 64  ? 150.822 57.182  50.362 1.00   15.63 ? 63   HIS F O   1 
ATOM   6031  C  CB  . HIS F  1 64  ? 152.427 59.354  51.979 1.00   15.02 ? 63   HIS F CB  1 
ATOM   6032  C  CG  . HIS F  1 64  ? 153.044 59.896  53.225 1.00   15.02 ? 63   HIS F CG  1 
ATOM   6033  N  ND1 . HIS F  1 64  ? 154.231 60.524  53.237 1.00   14.94 ? 63   HIS F ND1 1 
ATOM   6034  C  CD2 . HIS F  1 64  ? 152.578 59.907  54.549 1.00   15.03 ? 63   HIS F CD2 1 
ATOM   6035  C  CE1 . HIS F  1 64  ? 154.527 60.880  54.510 1.00   14.87 ? 63   HIS F CE1 1 
ATOM   6036  N  NE2 . HIS F  1 64  ? 153.516 60.501  55.303 1.00   14.92 ? 63   HIS F NE2 1 
ATOM   6037  N  N   . PHE F  1 65  ? 149.612 59.045  50.385 1.00   15.39 ? 64   PHE F N   1 
ATOM   6038  C  CA  . PHE F  1 65  ? 149.063 58.865  49.043 1.00   15.65 ? 64   PHE F CA  1 
ATOM   6039  C  C   . PHE F  1 65  ? 150.203 58.953  48.047 1.00   15.89 ? 64   PHE F C   1 
ATOM   6040  O  O   . PHE F  1 65  ? 150.879 59.989  47.932 1.00   15.41 ? 64   PHE F O   1 
ATOM   6041  C  CB  . PHE F  1 65  ? 147.985 59.928  48.771 1.00   15.65 ? 64   PHE F CB  1 
ATOM   6042  C  CG  . PHE F  1 65  ? 147.292 59.796  47.436 1.00   15.90 ? 64   PHE F CG  1 
ATOM   6043  C  CD1 . PHE F  1 65  ? 146.918 58.564  46.932 1.00   16.13 ? 64   PHE F CD1 1 
ATOM   6044  C  CD2 . PHE F  1 65  ? 147.005 60.939  46.690 1.00   15.92 ? 64   PHE F CD2 1 
ATOM   6045  C  CE1 . PHE F  1 65  ? 146.280 58.469  45.717 1.00   16.39 ? 64   PHE F CE1 1 
ATOM   6046  C  CE2 . PHE F  1 65  ? 146.365 60.851  45.471 1.00   16.08 ? 64   PHE F CE2 1 
ATOM   6047  C  CZ  . PHE F  1 65  ? 146.006 59.617  44.981 1.00   16.35 ? 64   PHE F CZ  1 
ATOM   6048  N  N   . ASN F  1 66  ? 150.413 57.837  47.345 1.00   16.46 ? 65   ASN F N   1 
ATOM   6049  C  CA  . ASN F  1 66  ? 151.587 57.620  46.520 1.00   16.95 ? 65   ASN F CA  1 
ATOM   6050  C  C   . ASN F  1 66  ? 151.260 56.786  45.291 1.00   17.72 ? 65   ASN F C   1 
ATOM   6051  O  O   . ASN F  1 66  ? 151.815 55.717  45.115 1.00   18.43 ? 65   ASN F O   1 
ATOM   6052  C  CB  . ASN F  1 66  ? 152.644 56.896  47.343 1.00   16.96 ? 65   ASN F CB  1 
ATOM   6053  C  CG  . ASN F  1 66  ? 153.990 56.792  46.643 1.00   17.10 ? 65   ASN F CG  1 
ATOM   6054  O  OD1 . ASN F  1 66  ? 154.329 57.584  45.742 1.00   16.79 ? 65   ASN F OD1 1 
ATOM   6055  N  ND2 . ASN F  1 66  ? 154.791 55.817  47.088 1.00   17.09 ? 65   ASN F ND2 1 
ATOM   6056  N  N   . PRO F  1 67  ? 150.378 57.290  44.422 1.00   18.17 ? 66   PRO F N   1 
ATOM   6057  C  CA  . PRO F  1 67  ? 149.984 56.500  43.264 1.00   18.88 ? 66   PRO F CA  1 
ATOM   6058  C  C   . PRO F  1 67  ? 151.097 56.284  42.213 1.00   19.86 ? 66   PRO F C   1 
ATOM   6059  O  O   . PRO F  1 67  ? 150.963 55.396  41.398 1.00   20.35 ? 66   PRO F O   1 
ATOM   6060  C  CB  . PRO F  1 67  ? 148.860 57.316  42.645 1.00   18.59 ? 66   PRO F CB  1 
ATOM   6061  C  CG  . PRO F  1 67  ? 149.150 58.723  43.039 1.00   18.21 ? 66   PRO F CG  1 
ATOM   6062  C  CD  . PRO F  1 67  ? 149.756 58.631  44.422 1.00   17.93 ? 66   PRO F CD  1 
ATOM   6063  N  N   . LEU F  1 68  ? 152.150 57.103  42.203 1.00   20.27 ? 67   LEU F N   1 
ATOM   6064  C  CA  . LEU F  1 68  ? 153.262 56.895  41.262 1.00   20.87 ? 67   LEU F CA  1 
ATOM   6065  C  C   . LEU F  1 68  ? 154.387 56.104  41.899 1.00   21.16 ? 67   LEU F C   1 
ATOM   6066  O  O   . LEU F  1 68  ? 155.480 56.037  41.353 1.00   21.83 ? 67   LEU F O   1 
ATOM   6067  C  CB  . LEU F  1 68  ? 153.792 58.242  40.734 1.00   20.96 ? 67   LEU F CB  1 
ATOM   6068  C  CG  . LEU F  1 68  ? 152.755 59.107  40.013 1.00   21.25 ? 67   LEU F CG  1 
ATOM   6069  C  CD1 . LEU F  1 68  ? 153.327 60.407  39.459 1.00   21.22 ? 67   LEU F CD1 1 
ATOM   6070  C  CD2 . LEU F  1 68  ? 152.141 58.301  38.896 1.00   21.94 ? 67   LEU F CD2 1 
ATOM   6071  N  N   . SER F  1 69  ? 154.141 55.527  43.069 1.00   21.44 ? 68   SER F N   1 
ATOM   6072  C  CA  . SER F  1 69  ? 155.131 54.713  43.749 1.00   22.20 ? 68   SER F CA  1 
ATOM   6073  C  C   . SER F  1 69  ? 156.529 55.346  43.801 1.00   22.97 ? 68   SER F C   1 
ATOM   6074  O  O   . SER F  1 69  ? 157.521 54.737  43.416 1.00   23.54 ? 68   SER F O   1 
ATOM   6075  C  CB  . SER F  1 69  ? 155.185 53.317  43.096 1.00   22.73 ? 68   SER F CB  1 
ATOM   6076  O  OG  . SER F  1 69  ? 153.910 52.714  43.171 1.00   22.49 ? 68   SER F OG  1 
ATOM   6077  N  N   . ARG F  1 70  ? 156.590 56.574  44.304 1.00   23.73 ? 69   ARG F N   1 
ATOM   6078  C  CA  . ARG F  1 70  ? 157.841 57.269  44.504 1.00   24.20 ? 69   ARG F CA  1 
ATOM   6079  C  C   . ARG F  1 70  ? 158.271 57.193  45.967 1.00   23.09 ? 69   ARG F C   1 
ATOM   6080  O  O   . ARG F  1 70  ? 157.514 56.727  46.848 1.00   21.48 ? 69   ARG F O   1 
ATOM   6081  C  CB  . ARG F  1 70  ? 157.668 58.715  44.076 1.00   26.14 ? 69   ARG F CB  1 
ATOM   6082  C  CG  . ARG F  1 70  ? 157.126 58.872  42.654 1.00   29.62 ? 69   ARG F CG  1 
ATOM   6083  C  CD  . ARG F  1 70  ? 158.238 58.932  41.644 1.00   33.24 ? 69   ARG F CD  1 
ATOM   6084  N  NE  . ARG F  1 70  ? 157.800 59.260  40.276 1.00   38.64 ? 69   ARG F NE  1 
ATOM   6085  C  CZ  . ARG F  1 70  ? 157.483 60.475  39.806 1.00   41.04 ? 69   ARG F CZ  1 
ATOM   6086  N  NH1 . ARG F  1 70  ? 157.505 61.556  40.579 1.00   43.27 ? 69   ARG F NH1 1 
ATOM   6087  N  NH2 . ARG F  1 70  ? 157.122 60.607  38.530 1.00   42.95 ? 69   ARG F NH2 1 
ATOM   6088  N  N   . LYS F  1 71  ? 159.491 57.650  46.231 1.00   22.50 ? 70   LYS F N   1 
ATOM   6089  C  CA  . LYS F  1 71  ? 159.936 57.862  47.610 1.00   22.55 ? 70   LYS F CA  1 
ATOM   6090  C  C   . LYS F  1 71  ? 159.411 59.191  48.150 1.00   20.37 ? 70   LYS F C   1 
ATOM   6091  O  O   . LYS F  1 71  ? 159.020 60.082  47.379 1.00   19.35 ? 70   LYS F O   1 
ATOM   6092  C  CB  . LYS F  1 71  ? 161.466 57.787  47.724 1.00   24.87 ? 70   LYS F CB  1 
ATOM   6093  C  CG  . LYS F  1 71  ? 162.024 56.429  47.257 1.00   27.77 ? 70   LYS F CG  1 
ATOM   6094  C  CD  . LYS F  1 71  ? 163.500 56.243  47.619 1.00   30.74 ? 70   LYS F CD  1 
ATOM   6095  C  CE  . LYS F  1 71  ? 164.043 54.877  47.178 1.00   34.07 ? 70   LYS F CE  1 
ATOM   6096  N  NZ  . LYS F  1 71  ? 165.526 54.925  46.878 1.00   37.30 ? 70   LYS F NZ  1 
ATOM   6097  N  N   . HIS F  1 72  ? 159.413 59.292  49.476 1.00   18.60 ? 71   HIS F N   1 
ATOM   6098  C  CA  . HIS F  1 72  ? 158.991 60.486  50.200 1.00   17.58 ? 71   HIS F CA  1 
ATOM   6099  C  C   . HIS F  1 72  ? 159.927 61.642  49.956 1.00   17.26 ? 71   HIS F C   1 
ATOM   6100  O  O   . HIS F  1 72  ? 161.149 61.462  49.989 1.00   17.63 ? 71   HIS F O   1 
ATOM   6101  C  CB  . HIS F  1 72  ? 158.973 60.215  51.708 1.00   17.06 ? 71   HIS F CB  1 
ATOM   6102  C  CG  . HIS F  1 72  ? 158.469 61.379  52.529 1.00   16.60 ? 71   HIS F CG  1 
ATOM   6103  N  ND1 . HIS F  1 72  ? 157.144 61.679  52.647 1.00   15.98 ? 71   HIS F ND1 1 
ATOM   6104  C  CD2 . HIS F  1 72  ? 159.166 62.335  53.281 1.00   16.26 ? 71   HIS F CD2 1 
ATOM   6105  C  CE1 . HIS F  1 72  ? 157.016 62.774  53.432 1.00   15.90 ? 71   HIS F CE1 1 
ATOM   6106  N  NE2 . HIS F  1 72  ? 158.255 63.164  53.826 1.00   15.95 ? 71   HIS F NE2 1 
ATOM   6107  N  N   . GLY F  1 73  ? 159.352 62.825  49.745 1.00   16.40 ? 72   GLY F N   1 
ATOM   6108  C  CA  . GLY F  1 73  ? 160.100 64.051  49.614 1.00   16.18 ? 72   GLY F CA  1 
ATOM   6109  C  C   . GLY F  1 73  ? 159.347 65.228  50.184 1.00   15.92 ? 72   GLY F C   1 
ATOM   6110  O  O   . GLY F  1 73  ? 158.292 65.089  50.861 1.00   15.93 ? 72   GLY F O   1 
ATOM   6111  N  N   . GLY F  1 74  ? 159.907 66.400  49.948 1.00   15.87 ? 73   GLY F N   1 
ATOM   6112  C  CA  . GLY F  1 74  ? 159.220 67.645  50.168 1.00   15.66 ? 73   GLY F CA  1 
ATOM   6113  C  C   . GLY F  1 74  ? 158.383 68.005  48.952 1.00   15.61 ? 73   GLY F C   1 
ATOM   6114  O  O   . GLY F  1 74  ? 158.604 67.488  47.862 1.00   15.61 ? 73   GLY F O   1 
ATOM   6115  N  N   . PRO F  1 75  ? 157.433 68.935  49.119 1.00   15.62 ? 74   PRO F N   1 
ATOM   6116  C  CA  . PRO F  1 75  ? 156.526 69.283  48.016 1.00   15.84 ? 74   PRO F CA  1 
ATOM   6117  C  C   . PRO F  1 75  ? 157.234 69.927  46.824 1.00   16.20 ? 74   PRO F C   1 
ATOM   6118  O  O   . PRO F  1 75  ? 156.729 69.841  45.708 1.00   16.81 ? 74   PRO F O   1 
ATOM   6119  C  CB  . PRO F  1 75  ? 155.508 70.235  48.683 1.00   15.57 ? 74   PRO F CB  1 
ATOM   6120  C  CG  . PRO F  1 75  ? 156.230 70.779  49.876 1.00   15.43 ? 74   PRO F CG  1 
ATOM   6121  C  CD  . PRO F  1 75  ? 157.084 69.647  50.357 1.00   15.41 ? 74   PRO F CD  1 
ATOM   6122  N  N   . LYS F  1 76  ? 158.404 70.514  47.040 1.00   16.57 ? 75   LYS F N   1 
ATOM   6123  C  CA  . LYS F  1 76  ? 159.184 71.098  45.959 1.00   17.31 ? 75   LYS F CA  1 
ATOM   6124  C  C   . LYS F  1 76  ? 159.959 70.058  45.153 1.00   17.57 ? 75   LYS F C   1 
ATOM   6125  O  O   . LYS F  1 76  ? 160.445 70.395  44.117 1.00   17.57 ? 75   LYS F O   1 
ATOM   6126  C  CB  . LYS F  1 76  ? 160.158 72.161  46.476 1.00   17.77 ? 75   LYS F CB  1 
ATOM   6127  C  CG  . LYS F  1 76  ? 159.483 73.365  47.108 1.00   18.33 ? 75   LYS F CG  1 
ATOM   6128  C  CD  . LYS F  1 76  ? 160.481 74.208  47.911 1.00   18.95 ? 75   LYS F CD  1 
ATOM   6129  C  CE  . LYS F  1 76  ? 161.349 75.144  47.070 1.00   19.25 ? 75   LYS F CE  1 
ATOM   6130  N  NZ  . LYS F  1 76  ? 162.350 75.893  47.902 1.00   18.95 ? 75   LYS F NZ  1 
ATOM   6131  N  N   . ASP F  1 77  ? 160.066 68.813  45.609 1.00   17.89 ? 76   ASP F N   1 
ATOM   6132  C  CA  . ASP F  1 77  ? 160.833 67.800  44.882 1.00   18.74 ? 76   ASP F CA  1 
ATOM   6133  C  C   . ASP F  1 77  ? 160.017 67.110  43.786 1.00   19.55 ? 76   ASP F C   1 
ATOM   6134  O  O   . ASP F  1 77  ? 158.834 66.869  43.957 1.00   18.64 ? 76   ASP F O   1 
ATOM   6135  C  CB  . ASP F  1 77  ? 161.340 66.697  45.808 1.00   18.72 ? 76   ASP F CB  1 
ATOM   6136  C  CG  . ASP F  1 77  ? 162.207 67.217  46.942 1.00   18.99 ? 76   ASP F CG  1 
ATOM   6137  O  OD1 . ASP F  1 77  ? 163.054 68.106  46.685 1.00   18.86 ? 76   ASP F OD1 1 
ATOM   6138  O  OD2 . ASP F  1 77  ? 162.032 66.718  48.092 1.00   18.74 ? 76   ASP F OD2 1 
ATOM   6139  N  N   . GLU F  1 78  ? 160.684 66.766  42.681 1.00   20.98 ? 77   GLU F N   1 
ATOM   6140  C  CA  . GLU F  1 78  ? 160.124 65.839  41.693 1.00   22.06 ? 77   GLU F CA  1 
ATOM   6141  C  C   . GLU F  1 78  ? 159.869 64.471  42.323 1.00   20.84 ? 77   GLU F C   1 
ATOM   6142  O  O   . GLU F  1 78  ? 158.796 63.883  42.121 1.00   20.90 ? 77   GLU F O   1 
ATOM   6143  C  CB  . GLU F  1 78  ? 161.030 65.682  40.469 1.00   25.10 ? 77   GLU F CB  1 
ATOM   6144  C  CG  . GLU F  1 78  ? 160.246 65.038  39.325 1.00   28.76 ? 77   GLU F CG  1 
ATOM   6145  C  CD  . GLU F  1 78  ? 161.049 64.705  38.070 1.00   32.74 ? 77   GLU F CD  1 
ATOM   6146  O  OE1 . GLU F  1 78  ? 162.202 65.187  37.908 1.00   35.82 ? 77   GLU F OE1 1 
ATOM   6147  O  OE2 . GLU F  1 78  ? 160.488 63.944  37.231 1.00   37.34 ? 77   GLU F OE2 1 
ATOM   6148  N  N   . GLU F  1 79  ? 160.846 63.976  43.083 1.00   19.49 ? 78   GLU F N   1 
ATOM   6149  C  CA  . GLU F  1 79  ? 160.733 62.697  43.790 1.00   18.90 ? 78   GLU F CA  1 
ATOM   6150  C  C   . GLU F  1 79  ? 160.000 62.963  45.116 1.00   17.39 ? 78   GLU F C   1 
ATOM   6151  O  O   . GLU F  1 79  ? 160.593 63.384  46.127 1.00   17.13 ? 78   GLU F O   1 
ATOM   6152  C  CB  . GLU F  1 79  ? 162.121 62.052  44.017 1.00   19.67 ? 78   GLU F CB  1 
ATOM   6153  C  CG  . GLU F  1 79  ? 162.103 60.647  44.618 1.00   20.56 ? 78   GLU F CG  1 
ATOM   6154  C  CD  . GLU F  1 79  ? 161.532 59.588  43.667 1.00   21.80 ? 78   GLU F CD  1 
ATOM   6155  O  OE1 . GLU F  1 79  ? 161.424 59.879  42.452 1.00   22.81 ? 78   GLU F OE1 1 
ATOM   6156  O  OE2 . GLU F  1 79  ? 161.198 58.457  44.125 1.00   22.31 ? 78   GLU F OE2 1 
ATOM   6157  N  N   . ARG F  1 80  ? 158.701 62.728  45.084 1.00   16.29 ? 79   ARG F N   1 
ATOM   6158  C  CA  . ARG F  1 80  ? 157.836 62.883  46.234 1.00   15.58 ? 79   ARG F CA  1 
ATOM   6159  C  C   . ARG F  1 80  ? 156.617 62.014  46.050 1.00   15.29 ? 79   ARG F C   1 
ATOM   6160  O  O   . ARG F  1 80  ? 156.325 61.569  44.948 1.00   15.74 ? 79   ARG F O   1 
ATOM   6161  C  CB  . ARG F  1 80  ? 157.412 64.357  46.415 1.00   15.03 ? 79   ARG F CB  1 
ATOM   6162  C  CG  . ARG F  1 80  ? 156.619 64.901  45.228 1.00   14.88 ? 79   ARG F CG  1 
ATOM   6163  C  CD  . ARG F  1 80  ? 156.053 66.292  45.474 1.00   14.54 ? 79   ARG F CD  1 
ATOM   6164  N  NE  . ARG F  1 80  ? 154.674 66.235  45.982 1.00   14.27 ? 79   ARG F NE  1 
ATOM   6165  C  CZ  . ARG F  1 80  ? 153.863 67.283  46.062 1.00   14.06 ? 79   ARG F CZ  1 
ATOM   6166  N  NH1 . ARG F  1 80  ? 154.278 68.496  45.705 1.00   13.98 ? 79   ARG F NH1 1 
ATOM   6167  N  NH2 . ARG F  1 80  ? 152.627 67.114  46.499 1.00   13.96 ? 79   ARG F NH2 1 
ATOM   6168  N  N   . HIS F  1 81  ? 155.917 61.771  47.154 1.00   14.79 ? 80   HIS F N   1 
ATOM   6169  C  CA  . HIS F  1 81  ? 154.582 61.197  47.115 1.00   14.42 ? 80   HIS F CA  1 
ATOM   6170  C  C   . HIS F  1 81  ? 153.632 62.273  46.699 1.00   14.00 ? 80   HIS F C   1 
ATOM   6171  O  O   . HIS F  1 81  ? 153.825 63.442  47.062 1.00   13.71 ? 80   HIS F O   1 
ATOM   6172  C  CB  . HIS F  1 81  ? 154.191 60.692  48.491 1.00   14.34 ? 80   HIS F CB  1 
ATOM   6173  C  CG  . HIS F  1 81  ? 155.127 59.640  49.075 1.00   14.56 ? 80   HIS F CG  1 
ATOM   6174  N  ND1 . HIS F  1 81  ? 155.360 59.520  50.419 1.00   14.51 ? 80   HIS F ND1 1 
ATOM   6175  C  CD2 . HIS F  1 81  ? 155.833 58.613  48.464 1.00   14.88 ? 80   HIS F CD2 1 
ATOM   6176  C  CE1 . HIS F  1 81  ? 156.165 58.472  50.632 1.00   14.73 ? 80   HIS F CE1 1 
ATOM   6177  N  NE2 . HIS F  1 81  ? 156.460 57.916  49.433 1.00   14.98 ? 80   HIS F NE2 1 
ATOM   6178  N  N   . VAL F  1 82  ? 152.566 61.928  45.967 1.00   13.81 ? 81   VAL F N   1 
ATOM   6179  C  CA  . VAL F  1 82  ? 151.532 62.944  45.697 1.00   13.54 ? 81   VAL F CA  1 
ATOM   6180  C  C   . VAL F  1 82  ? 151.084 63.620  47.013 1.00   13.15 ? 81   VAL F C   1 
ATOM   6181  O  O   . VAL F  1 82  ? 150.937 64.844  47.082 1.00   12.97 ? 81   VAL F O   1 
ATOM   6182  C  CB  . VAL F  1 82  ? 150.334 62.365  44.918 1.00   13.69 ? 81   VAL F CB  1 
ATOM   6183  C  CG1 . VAL F  1 82  ? 149.137 63.313  44.971 1.00   13.62 ? 81   VAL F CG1 1 
ATOM   6184  C  CG2 . VAL F  1 82  ? 150.743 62.050  43.468 1.00   13.87 ? 81   VAL F CG2 1 
ATOM   6185  N  N   . GLY F  1 83  ? 150.936 62.841  48.087 1.00   12.92 ? 82   GLY F N   1 
ATOM   6186  C  CA  . GLY F  1 83  ? 150.460 63.403  49.354 1.00   12.62 ? 82   GLY F CA  1 
ATOM   6187  C  C   . GLY F  1 83  ? 151.434 64.235  50.178 1.00   12.38 ? 82   GLY F C   1 
ATOM   6188  O  O   . GLY F  1 83  ? 151.049 64.681  51.265 1.00   12.18 ? 82   GLY F O   1 
ATOM   6189  N  N   . ASP F  1 84  ? 152.657 64.490  49.687 1.00   12.29 ? 83   ASP F N   1 
ATOM   6190  C  CA  . ASP F  1 84  ? 153.664 65.166  50.484 1.00   12.23 ? 83   ASP F CA  1 
ATOM   6191  C  C   . ASP F  1 84  ? 153.538 66.675  50.415 1.00   12.11 ? 83   ASP F C   1 
ATOM   6192  O  O   . ASP F  1 84  ? 154.089 67.327  49.526 1.00   12.17 ? 83   ASP F O   1 
ATOM   6193  C  CB  . ASP F  1 84  ? 155.078 64.753  50.080 1.00   12.42 ? 83   ASP F CB  1 
ATOM   6194  C  CG  . ASP F  1 84  ? 155.387 63.285  50.396 1.00   12.61 ? 83   ASP F CG  1 
ATOM   6195  O  OD1 . ASP F  1 84  ? 154.669 62.651  51.165 1.00   12.41 ? 83   ASP F OD1 1 
ATOM   6196  O  OD2 . ASP F  1 84  ? 156.368 62.756  49.825 1.00   12.87 ? 83   ASP F OD2 1 
ATOM   6197  N  N   . LEU F  1 85  ? 152.835 67.246  51.382 1.00   11.93 ? 84   LEU F N   1 
ATOM   6198  C  CA  . LEU F  1 85  ? 152.682 68.670  51.435 1.00   11.85 ? 84   LEU F CA  1 
ATOM   6199  C  C   . LEU F  1 85  ? 153.690 69.343  52.366 1.00   11.91 ? 84   LEU F C   1 
ATOM   6200  O  O   . LEU F  1 85  ? 153.605 70.542  52.613 1.00   12.05 ? 84   LEU F O   1 
ATOM   6201  C  CB  . LEU F  1 85  ? 151.229 69.012  51.798 1.00   11.76 ? 84   LEU F CB  1 
ATOM   6202  C  CG  . LEU F  1 85  ? 150.163 68.513  50.808 1.00   11.81 ? 84   LEU F CG  1 
ATOM   6203  C  CD1 . LEU F  1 85  ? 148.739 68.793  51.289 1.00   11.73 ? 84   LEU F CD1 1 
ATOM   6204  C  CD2 . LEU F  1 85  ? 150.357 69.097  49.414 1.00   11.83 ? 84   LEU F CD2 1 
ATOM   6205  N  N   . GLY F  1 86  ? 154.659 68.599  52.872 1.00   12.03 ? 85   GLY F N   1 
ATOM   6206  C  CA  . GLY F  1 86  ? 155.747 69.183  53.665 1.00   12.19 ? 85   GLY F CA  1 
ATOM   6207  C  C   . GLY F  1 86  ? 155.401 69.478  55.110 1.00   12.25 ? 85   GLY F C   1 
ATOM   6208  O  O   . GLY F  1 86  ? 154.771 68.645  55.809 1.00   12.36 ? 85   GLY F O   1 
ATOM   6209  N  N   . ASN F  1 87  ? 155.800 70.658  55.582 1.00   12.36 ? 86   ASN F N   1 
ATOM   6210  C  CA  . ASN F  1 87  ? 155.484 71.087  56.942 1.00   12.45 ? 86   ASN F CA  1 
ATOM   6211  C  C   . ASN F  1 87  ? 154.482 72.244  57.019 1.00   12.54 ? 86   ASN F C   1 
ATOM   6212  O  O   . ASN F  1 87  ? 154.417 73.093  56.122 1.00   12.63 ? 86   ASN F O   1 
ATOM   6213  C  CB  . ASN F  1 87  ? 156.769 71.493  57.664 1.00   12.57 ? 86   ASN F CB  1 
ATOM   6214  C  CG  . ASN F  1 87  ? 157.654 70.315  57.962 1.00   12.65 ? 86   ASN F CG  1 
ATOM   6215  O  OD1 . ASN F  1 87  ? 157.227 69.376  58.635 1.00   12.71 ? 86   ASN F OD1 1 
ATOM   6216  N  ND2 . ASN F  1 87  ? 158.892 70.347  57.464 1.00   12.64 ? 86   ASN F ND2 1 
ATOM   6217  N  N   . VAL F  1 88  ? 153.737 72.290  58.126 1.00   12.62 ? 87   VAL F N   1 
ATOM   6218  C  CA  . VAL F  1 88  ? 153.063 73.530  58.582 1.00   12.79 ? 87   VAL F CA  1 
ATOM   6219  C  C   . VAL F  1 88  ? 153.694 74.028  59.895 1.00   13.07 ? 87   VAL F C   1 
ATOM   6220  O  O   . VAL F  1 88  ? 154.203 73.234  60.668 1.00   13.11 ? 87   VAL F O   1 
ATOM   6221  C  CB  . VAL F  1 88  ? 151.553 73.318  58.798 1.00   12.73 ? 87   VAL F CB  1 
ATOM   6222  C  CG1 . VAL F  1 88  ? 150.866 73.033  57.456 1.00   12.62 ? 87   VAL F CG1 1 
ATOM   6223  C  CG2 . VAL F  1 88  ? 151.284 72.222  59.806 1.00   12.75 ? 87   VAL F CG2 1 
ATOM   6224  N  N   . THR F  1 89  ? 153.645 75.329  60.143 1.00   13.37 ? 88   THR F N   1 
ATOM   6225  C  CA  . THR F  1 89  ? 154.297 75.932  61.312 1.00   13.75 ? 88   THR F CA  1 
ATOM   6226  C  C   . THR F  1 89  ? 153.264 76.485  62.288 1.00   14.21 ? 88   THR F C   1 
ATOM   6227  O  O   . THR F  1 89  ? 152.420 77.309  61.937 1.00   14.44 ? 88   THR F O   1 
ATOM   6228  C  CB  . THR F  1 89  ? 155.280 77.046  60.896 1.00   13.82 ? 88   THR F CB  1 
ATOM   6229  O  OG1 . THR F  1 89  ? 156.341 76.475  60.110 1.00   13.55 ? 88   THR F OG1 1 
ATOM   6230  C  CG2 . THR F  1 89  ? 155.888 77.799  62.133 1.00   14.04 ? 88   THR F CG2 1 
ATOM   6231  N  N   . ALA F  1 90  ? 153.343 76.025  63.526 1.00   14.68 ? 89   ALA F N   1 
ATOM   6232  C  CA  . ALA F  1 90  ? 152.513 76.571  64.594 1.00   15.29 ? 89   ALA F CA  1 
ATOM   6233  C  C   . ALA F  1 90  ? 153.286 77.683  65.304 1.00   16.07 ? 89   ALA F C   1 
ATOM   6234  O  O   . ALA F  1 90  ? 154.505 77.564  65.511 1.00   15.94 ? 89   ALA F O   1 
ATOM   6235  C  CB  . ALA F  1 90  ? 152.124 75.485  65.571 1.00   15.09 ? 89   ALA F CB  1 
ATOM   6236  N  N   . ASP F  1 91  ? 152.573 78.752  65.665 1.00   16.89 ? 90   ASP F N   1 
ATOM   6237  C  CA  . ASP F  1 91  ? 153.174 79.882  66.383 1.00   17.90 ? 90   ASP F CA  1 
ATOM   6238  C  C   . ASP F  1 91  ? 153.261 79.602  67.886 1.00   18.68 ? 90   ASP F C   1 
ATOM   6239  O  O   . ASP F  1 91  ? 152.929 78.512  68.338 1.00   18.17 ? 90   ASP F O   1 
ATOM   6240  C  CB  . ASP F  1 91  ? 152.417 81.200  66.085 1.00   18.26 ? 90   ASP F CB  1 
ATOM   6241  C  CG  . ASP F  1 91  ? 150.979 81.186  66.548 1.00   18.40 ? 90   ASP F CG  1 
ATOM   6242  O  OD1 . ASP F  1 91  ? 150.639 80.391  67.441 1.00   18.28 ? 90   ASP F OD1 1 
ATOM   6243  O  OD2 . ASP F  1 91  ? 150.170 81.980  66.001 1.00   19.23 ? 90   ASP F OD2 1 
ATOM   6244  N  N   . LYS F  1 92  ? 153.696 80.605  68.645 1.00   20.03 ? 91   LYS F N   1 
ATOM   6245  C  CA  . LYS F  1 92  ? 153.880 80.487  70.092 1.00   21.39 ? 91   LYS F CA  1 
ATOM   6246  C  C   . LYS F  1 92  ? 152.586 80.238  70.828 1.00   21.14 ? 91   LYS F C   1 
ATOM   6247  O  O   . LYS F  1 92  ? 152.618 79.822  71.958 1.00   21.23 ? 91   LYS F O   1 
ATOM   6248  C  CB  . LYS F  1 92  ? 154.574 81.743  70.666 1.00   22.92 ? 91   LYS F CB  1 
ATOM   6249  C  CG  . LYS F  1 92  ? 153.683 82.972  70.609 1.00   24.63 ? 91   LYS F CG  1 
ATOM   6250  C  CD  . LYS F  1 92  ? 154.392 84.269  70.960 1.00   26.62 ? 91   LYS F CD  1 
ATOM   6251  C  CE  . LYS F  1 92  ? 153.370 85.395  71.080 1.00   27.98 ? 91   LYS F CE  1 
ATOM   6252  N  NZ  . LYS F  1 92  ? 153.998 86.570  71.732 1.00   30.85 ? 91   LYS F NZ  1 
ATOM   6253  N  N   . ASP F  1 93  ? 151.438 80.469  70.194 1.00   21.09 ? 92   ASP F N   1 
ATOM   6254  C  CA  . ASP F  1 93  ? 150.161 80.122  70.820 1.00   21.20 ? 92   ASP F CA  1 
ATOM   6255  C  C   . ASP F  1 93  ? 149.642 78.791  70.338 1.00   20.03 ? 92   ASP F C   1 
ATOM   6256  O  O   . ASP F  1 93  ? 148.509 78.444  70.633 1.00   19.73 ? 92   ASP F O   1 
ATOM   6257  C  CB  . ASP F  1 93  ? 149.119 81.202  70.552 1.00   22.19 ? 92   ASP F CB  1 
ATOM   6258  C  CG  . ASP F  1 93  ? 149.541 82.543  71.101 1.00   23.69 ? 92   ASP F CG  1 
ATOM   6259  O  OD1 . ASP F  1 93  ? 150.115 82.576  72.203 1.00   24.22 ? 92   ASP F OD1 1 
ATOM   6260  O  OD2 . ASP F  1 93  ? 149.323 83.562  70.422 1.00   25.25 ? 92   ASP F OD2 1 
ATOM   6261  N  N   . GLY F  1 94  ? 150.454 78.063  69.575 1.00   18.95 ? 93   GLY F N   1 
ATOM   6262  C  CA  . GLY F  1 94  ? 150.070 76.735  69.112 1.00   18.18 ? 93   GLY F CA  1 
ATOM   6263  C  C   . GLY F  1 94  ? 149.117 76.710  67.932 1.00   17.62 ? 93   GLY F C   1 
ATOM   6264  O  O   . GLY F  1 94  ? 148.454 75.687  67.683 1.00   17.12 ? 93   GLY F O   1 
ATOM   6265  N  N   . VAL F  1 95  ? 149.068 77.824  67.189 1.00   17.39 ? 94   VAL F N   1 
ATOM   6266  C  CA  . VAL F  1 95  ? 148.229 77.952  65.993 1.00   16.98 ? 94   VAL F CA  1 
ATOM   6267  C  C   . VAL F  1 95  ? 149.045 77.963  64.699 1.00   16.68 ? 94   VAL F C   1 
ATOM   6268  O  O   . VAL F  1 95  ? 149.973 78.778  64.544 1.00   16.71 ? 94   VAL F O   1 
ATOM   6269  C  CB  . VAL F  1 95  ? 147.401 79.257  65.991 1.00   17.29 ? 94   VAL F CB  1 
ATOM   6270  C  CG1 . VAL F  1 95  ? 146.530 79.307  64.726 1.00   16.99 ? 94   VAL F CG1 1 
ATOM   6271  C  CG2 . VAL F  1 95  ? 146.534 79.377  67.264 1.00   17.56 ? 94   VAL F CG2 1 
ATOM   6272  N  N   . ALA F  1 96  ? 148.663 77.090  63.761 1.00   16.31 ? 95   ALA F N   1 
ATOM   6273  C  CA  . ALA F  1 96  ? 149.206 77.080  62.408 1.00   15.96 ? 95   ALA F CA  1 
ATOM   6274  C  C   . ALA F  1 96  ? 148.182 77.686  61.470 1.00   16.02 ? 95   ALA F C   1 
ATOM   6275  O  O   . ALA F  1 96  ? 147.091 77.094  61.285 1.00   15.87 ? 95   ALA F O   1 
ATOM   6276  C  CB  . ALA F  1 96  ? 149.525 75.651  61.960 1.00   15.64 ? 95   ALA F CB  1 
ATOM   6277  N  N   . ASP F  1 97  ? 148.491 78.867  60.917 1.00   15.88 ? 96   ASP F N   1 
ATOM   6278  C  CA  . ASP F  1 97  ? 147.637 79.489  59.916 1.00   16.07 ? 96   ASP F CA  1 
ATOM   6279  C  C   . ASP F  1 97  ? 148.179 79.004  58.565 1.00   15.49 ? 96   ASP F C   1 
ATOM   6280  O  O   . ASP F  1 97  ? 149.054 79.616  57.977 1.00   15.09 ? 96   ASP F O   1 
ATOM   6281  C  CB  . ASP F  1 97  ? 147.643 81.030  60.026 1.00   16.84 ? 96   ASP F CB  1 
ATOM   6282  C  CG  . ASP F  1 97  ? 146.931 81.538  61.287 1.00   17.59 ? 96   ASP F CG  1 
ATOM   6283  O  OD1 . ASP F  1 97  ? 145.758 81.202  61.511 1.00   18.10 ? 96   ASP F OD1 1 
ATOM   6284  O  OD2 . ASP F  1 97  ? 147.540 82.290  62.076 1.00   18.91 ? 96   ASP F OD2 1 
ATOM   6285  N  N   . VAL F  1 98  ? 147.671 77.859  58.132 1.00   15.11 ? 97   VAL F N   1 
ATOM   6286  C  CA  . VAL F  1 98  ? 148.202 77.125  56.997 1.00   14.86 ? 97   VAL F CA  1 
ATOM   6287  C  C   . VAL F  1 98  ? 147.951 77.899  55.698 1.00   15.15 ? 97   VAL F C   1 
ATOM   6288  O  O   . VAL F  1 98  ? 146.873 78.436  55.485 1.00   15.17 ? 97   VAL F O   1 
ATOM   6289  C  CB  . VAL F  1 98  ? 147.572 75.715  56.882 1.00   14.50 ? 97   VAL F CB  1 
ATOM   6290  C  CG1 . VAL F  1 98  ? 148.062 75.001  55.621 1.00   14.16 ? 97   VAL F CG1 1 
ATOM   6291  C  CG2 . VAL F  1 98  ? 147.832 74.880  58.146 1.00   14.29 ? 97   VAL F CG2 1 
ATOM   6292  N  N   . SER F  1 99  ? 148.967 77.954  54.842 1.00   15.43 ? 98   SER F N   1 
ATOM   6293  C  CA  . SER F  1 99  ? 148.838 78.593  53.546 1.00   16.11 ? 98   SER F CA  1 
ATOM   6294  C  C   . SER F  1 99  ? 149.842 77.982  52.588 1.00   16.11 ? 98   SER F C   1 
ATOM   6295  O  O   . SER F  1 99  ? 151.037 78.266  52.670 1.00   15.92 ? 98   SER F O   1 
ATOM   6296  C  CB  . SER F  1 99  ? 149.084 80.099  53.664 1.00   16.78 ? 98   SER F CB  1 
ATOM   6297  O  OG  . SER F  1 99  ? 149.047 80.705  52.385 1.00   17.81 ? 98   SER F OG  1 
ATOM   6298  N  N   . ILE F  1 100 ? 149.339 77.100  51.724 1.00   16.09 ? 99   ILE F N   1 
ATOM   6299  C  CA  . ILE F  1 100 ? 150.162 76.243  50.883 1.00   16.06 ? 99   ILE F CA  1 
ATOM   6300  C  C   . ILE F  1 100 ? 149.528 76.305  49.516 1.00   16.55 ? 99   ILE F C   1 
ATOM   6301  O  O   . ILE F  1 100 ? 148.304 76.411  49.392 1.00   16.43 ? 99   ILE F O   1 
ATOM   6302  C  CB  . ILE F  1 100 ? 150.188 74.781  51.402 1.00   15.75 ? 99   ILE F CB  1 
ATOM   6303  C  CG1 . ILE F  1 100 ? 151.160 74.632  52.569 1.00   15.65 ? 99   ILE F CG1 1 
ATOM   6304  C  CG2 . ILE F  1 100 ? 150.577 73.768  50.314 1.00   15.67 ? 99   ILE F CG2 1 
ATOM   6305  C  CD1 . ILE F  1 100 ? 150.979 73.333  53.327 1.00   15.43 ? 99   ILE F CD1 1 
ATOM   6306  N  N   . GLU F  1 101 ? 150.360 76.276  48.490 1.00   17.04 ? 100  GLU F N   1 
ATOM   6307  C  CA  . GLU F  1 101 ? 149.866 76.048  47.160 1.00   17.94 ? 100  GLU F CA  1 
ATOM   6308  C  C   . GLU F  1 101 ? 150.623 74.894  46.549 1.00   17.04 ? 100  GLU F C   1 
ATOM   6309  O  O   . GLU F  1 101 ? 151.845 74.846  46.622 1.00   17.04 ? 100  GLU F O   1 
ATOM   6310  C  CB  . GLU F  1 101 ? 150.009 77.305  46.324 1.00   19.89 ? 100  GLU F CB  1 
ATOM   6311  C  CG  . GLU F  1 101 ? 149.675 77.053  44.865 1.00   21.58 ? 100  GLU F CG  1 
ATOM   6312  C  CD  . GLU F  1 101 ? 149.920 78.281  44.024 1.00   23.64 ? 100  GLU F CD  1 
ATOM   6313  O  OE1 . GLU F  1 101 ? 149.215 79.273  44.257 1.00   24.89 ? 100  GLU F OE1 1 
ATOM   6314  O  OE2 . GLU F  1 101 ? 150.835 78.243  43.161 1.00   26.64 ? 100  GLU F OE2 1 
ATOM   6315  N  N   . ASP F  1 102 ? 149.911 73.948  45.971 1.00   16.17 ? 101  ASP F N   1 
ATOM   6316  C  CA  . ASP F  1 102 ? 150.566 72.728  45.471 1.00   15.78 ? 101  ASP F CA  1 
ATOM   6317  C  C   . ASP F  1 102 ? 149.967 72.309  44.157 1.00   15.69 ? 101  ASP F C   1 
ATOM   6318  O  O   . ASP F  1 102 ? 148.736 72.336  44.025 1.00   15.40 ? 101  ASP F O   1 
ATOM   6319  C  CB  . ASP F  1 102 ? 150.455 71.578  46.468 1.00   15.50 ? 101  ASP F CB  1 
ATOM   6320  C  CG  . ASP F  1 102 ? 151.395 70.434  46.123 1.00   15.53 ? 101  ASP F CG  1 
ATOM   6321  O  OD1 . ASP F  1 102 ? 152.622 70.554  46.349 1.00   15.60 ? 101  ASP F OD1 1 
ATOM   6322  O  OD2 . ASP F  1 102 ? 150.927 69.414  45.603 1.00   15.48 ? 101  ASP F OD2 1 
ATOM   6323  N  N   . SER F  1 103 ? 150.840 71.933  43.200 1.00   15.71 ? 102  SER F N   1 
ATOM   6324  C  CA  A SER F  1 103 ? 150.391 71.603  41.847 0.50   16.01 ? 102  SER F CA  1 
ATOM   6325  C  CA  B SER F  1 103 ? 150.456 71.607  41.831 0.50   15.84 ? 102  SER F CA  1 
ATOM   6326  C  C   . SER F  1 103 ? 150.437 70.107  41.547 1.00   15.86 ? 102  SER F C   1 
ATOM   6327  O  O   . SER F  1 103 ? 150.157 69.703  40.424 1.00   16.12 ? 102  SER F O   1 
ATOM   6328  C  CB  A SER F  1 103 ? 151.205 72.370  40.791 0.50   16.53 ? 102  SER F CB  1 
ATOM   6329  C  CB  B SER F  1 103 ? 151.430 72.273  40.845 0.50   16.13 ? 102  SER F CB  1 
ATOM   6330  O  OG  A SER F  1 103 ? 150.965 73.767  40.874 0.50   16.97 ? 102  SER F OG  1 
ATOM   6331  O  OG  B SER F  1 103 ? 152.771 71.837  41.065 0.50   16.03 ? 102  SER F OG  1 
ATOM   6332  N  N   . VAL F  1 104 ? 150.744 69.284  42.553 1.00   15.29 ? 103  VAL F N   1 
ATOM   6333  C  CA  . VAL F  1 104 ? 150.794 67.831  42.367 1.00   14.94 ? 103  VAL F CA  1 
ATOM   6334  C  C   . VAL F  1 104 ? 149.510 67.185  42.880 1.00   14.84 ? 103  VAL F C   1 
ATOM   6335  O  O   . VAL F  1 104 ? 148.959 66.299  42.227 1.00   14.78 ? 103  VAL F O   1 
ATOM   6336  C  CB  . VAL F  1 104 ? 152.029 67.211  43.053 1.00   14.75 ? 103  VAL F CB  1 
ATOM   6337  C  CG1 . VAL F  1 104 ? 152.010 65.680  42.943 1.00   14.62 ? 103  VAL F CG1 1 
ATOM   6338  C  CG2 . VAL F  1 104 ? 153.324 67.785  42.448 1.00   14.74 ? 103  VAL F CG2 1 
ATOM   6339  N  N   . ILE F  1 105 ? 149.028 67.616  44.051 1.00   14.56 ? 104  ILE F N   1 
ATOM   6340  C  CA  . ILE F  1 105 ? 147.678 67.192  44.499 1.00   14.44 ? 104  ILE F CA  1 
ATOM   6341  C  C   . ILE F  1 105 ? 146.636 67.765  43.542 1.00   14.78 ? 104  ILE F C   1 
ATOM   6342  O  O   . ILE F  1 105 ? 146.894 68.774  42.890 1.00   15.12 ? 104  ILE F O   1 
ATOM   6343  C  CB  . ILE F  1 105 ? 147.366 67.615  45.939 1.00   14.04 ? 104  ILE F CB  1 
ATOM   6344  C  CG1 . ILE F  1 105 ? 147.486 69.134  46.127 1.00   13.96 ? 104  ILE F CG1 1 
ATOM   6345  C  CG2 . ILE F  1 105 ? 148.241 66.842  46.944 1.00   13.73 ? 104  ILE F CG2 1 
ATOM   6346  C  CD1 . ILE F  1 105 ? 146.768 69.633  47.371 1.00   13.78 ? 104  ILE F CD1 1 
ATOM   6347  N  N   . SER F  1 106 ? 145.478 67.140  43.455 1.00   15.05 ? 105  SER F N   1 
ATOM   6348  C  CA  . SER F  1 106 ? 144.357 67.680  42.659 1.00   15.55 ? 105  SER F CA  1 
ATOM   6349  C  C   . SER F  1 106 ? 143.029 67.364  43.366 1.00   15.89 ? 105  SER F C   1 
ATOM   6350  O  O   . SER F  1 106 ? 142.966 66.490  44.221 1.00   15.24 ? 105  SER F O   1 
ATOM   6351  C  CB  . SER F  1 106 ? 144.372 67.084  41.242 1.00   15.98 ? 105  SER F CB  1 
ATOM   6352  O  OG  . SER F  1 106 ? 143.534 67.788  40.327 1.00   16.43 ? 105  SER F OG  1 
ATOM   6353  N  N   . LEU F  1 107 ? 141.995 68.139  43.038 1.00   16.67 ? 106  LEU F N   1 
ATOM   6354  C  CA  . LEU F  1 107 ? 140.626 67.836  43.437 1.00   17.11 ? 106  LEU F CA  1 
ATOM   6355  C  C   . LEU F  1 107 ? 139.867 67.076  42.325 1.00   18.04 ? 106  LEU F C   1 
ATOM   6356  O  O   . LEU F  1 107 ? 138.661 66.903  42.418 1.00   18.54 ? 106  LEU F O   1 
ATOM   6357  C  CB  . LEU F  1 107 ? 139.864 69.108  43.851 1.00   17.05 ? 106  LEU F CB  1 
ATOM   6358  C  CG  . LEU F  1 107 ? 140.513 69.991  44.937 1.00   16.74 ? 106  LEU F CG  1 
ATOM   6359  C  CD1 . LEU F  1 107 ? 139.556 71.111  45.383 1.00   16.55 ? 106  LEU F CD1 1 
ATOM   6360  C  CD2 . LEU F  1 107 ? 140.979 69.170  46.145 1.00   16.33 ? 106  LEU F CD2 1 
ATOM   6361  N  N   . SER F  1 108 ? 140.573 66.568  41.316 1.00   18.80 ? 107  SER F N   1 
ATOM   6362  C  CA  . SER F  1 108 ? 139.979 65.610  40.364 1.00   19.84 ? 107  SER F CA  1 
ATOM   6363  C  C   . SER F  1 108 ? 141.059 64.734  39.746 1.00   20.25 ? 107  SER F C   1 
ATOM   6364  O  O   . SER F  1 108 ? 142.259 64.989  39.927 1.00   20.36 ? 107  SER F O   1 
ATOM   6365  C  CB  . SER F  1 108 ? 139.210 66.335  39.248 1.00   20.40 ? 107  SER F CB  1 
ATOM   6366  O  OG  . SER F  1 108 ? 140.066 67.193  38.542 1.00   20.65 ? 107  SER F OG  1 
ATOM   6367  N  N   . GLY F  1 109 ? 140.632 63.685  39.047 1.00   20.83 ? 108  GLY F N   1 
ATOM   6368  C  CA  . GLY F  1 109 ? 141.551 62.829  38.286 1.00   21.19 ? 108  GLY F CA  1 
ATOM   6369  C  C   . GLY F  1 109 ? 142.369 61.881  39.149 1.00   20.91 ? 108  GLY F C   1 
ATOM   6370  O  O   . GLY F  1 109 ? 142.040 61.656  40.284 1.00   20.48 ? 108  GLY F O   1 
ATOM   6371  N  N   . ASP F  1 110 ? 143.468 61.369  38.603 1.00   21.40 ? 109  ASP F N   1 
ATOM   6372  C  CA  . ASP F  1 110 ? 144.267 60.328  39.254 1.00   21.77 ? 109  ASP F CA  1 
ATOM   6373  C  C   . ASP F  1 110 ? 144.855 60.756  40.605 1.00   20.74 ? 109  ASP F C   1 
ATOM   6374  O  O   . ASP F  1 110 ? 144.965 59.936  41.527 1.00   20.64 ? 109  ASP F O   1 
ATOM   6375  C  CB  . ASP F  1 110 ? 145.427 59.883  38.334 1.00   22.89 ? 109  ASP F CB  1 
ATOM   6376  C  CG  . ASP F  1 110 ? 144.962 59.076  37.142 1.00   24.25 ? 109  ASP F CG  1 
ATOM   6377  O  OD1 . ASP F  1 110 ? 143.827 58.570  37.121 1.00   25.46 ? 109  ASP F OD1 1 
ATOM   6378  O  OD2 . ASP F  1 110 ? 145.743 58.939  36.200 1.00   26.67 ? 109  ASP F OD2 1 
ATOM   6379  N  N   . HIS F  1 111 ? 145.253 62.024  40.697 1.00   19.81 ? 110  HIS F N   1 
ATOM   6380  C  CA  . HIS F  1 111 ? 145.822 62.590  41.929 1.00   19.22 ? 110  HIS F CA  1 
ATOM   6381  C  C   . HIS F  1 111 ? 144.805 63.198  42.853 1.00   18.46 ? 110  HIS F C   1 
ATOM   6382  O  O   . HIS F  1 111 ? 145.168 63.956  43.767 1.00   17.72 ? 110  HIS F O   1 
ATOM   6383  C  CB  . HIS F  1 111 ? 146.869 63.637  41.564 1.00   19.26 ? 110  HIS F CB  1 
ATOM   6384  C  CG  . HIS F  1 111 ? 148.065 63.053  40.898 1.00   19.73 ? 110  HIS F CG  1 
ATOM   6385  N  ND1 . HIS F  1 111 ? 149.180 63.767  40.647 1.00   19.98 ? 110  HIS F ND1 1 
ATOM   6386  C  CD2 . HIS F  1 111 ? 148.321 61.757  40.472 1.00   20.22 ? 110  HIS F CD2 1 
ATOM   6387  C  CE1 . HIS F  1 111 ? 150.077 62.965  40.055 1.00   20.34 ? 110  HIS F CE1 1 
ATOM   6388  N  NE2 . HIS F  1 111 ? 149.548 61.743  39.948 1.00   20.51 ? 110  HIS F NE2 1 
ATOM   6389  N  N   . CYS F  1 112 ? 143.532 62.876  42.627 1.00   18.25 ? 111  CYS F N   1 
ATOM   6390  C  CA  . CYS F  1 112 ? 142.441 63.357  43.479 1.00   18.00 ? 111  CYS F CA  1 
ATOM   6391  C  C   . CYS F  1 112 ? 142.650 62.973  44.938 1.00   16.68 ? 111  CYS F C   1 
ATOM   6392  O  O   . CYS F  1 112 ? 142.878 61.803  45.268 1.00   16.54 ? 111  CYS F O   1 
ATOM   6393  C  CB  . CYS F  1 112 ? 141.069 62.853  43.011 1.00   18.81 ? 111  CYS F CB  1 
ATOM   6394  S  SG  . CYS F  1 112 ? 139.698 63.806  43.721 1.00   21.32 ? 111  CYS F SG  1 
ATOM   6395  N  N   . ILE F  1 113 ? 142.519 63.961  45.806 1.00   15.46 ? 112  ILE F N   1 
ATOM   6396  C  CA  . ILE F  1 113 ? 142.660 63.740  47.233 1.00   14.82 ? 112  ILE F CA  1 
ATOM   6397  C  C   . ILE F  1 113 ? 141.313 63.727  47.998 1.00   14.55 ? 112  ILE F C   1 
ATOM   6398  O  O   . ILE F  1 113 ? 141.283 63.441  49.203 1.00   14.09 ? 112  ILE F O   1 
ATOM   6399  C  CB  . ILE F  1 113 ? 143.625 64.759  47.849 1.00   14.49 ? 112  ILE F CB  1 
ATOM   6400  C  CG1 . ILE F  1 113 ? 143.084 66.185  47.694 1.00   14.40 ? 112  ILE F CG1 1 
ATOM   6401  C  CG2 . ILE F  1 113 ? 144.995 64.625  47.206 1.00   14.48 ? 112  ILE F CG2 1 
ATOM   6402  C  CD1 . ILE F  1 113 ? 143.810 67.209  48.553 1.00   14.20 ? 112  ILE F CD1 1 
ATOM   6403  N  N   . ILE F  1 114 ? 140.201 63.978  47.290 1.00   14.53 ? 113  ILE F N   1 
ATOM   6404  C  CA  . ILE F  1 114 ? 138.877 63.881  47.892 1.00   14.42 ? 113  ILE F CA  1 
ATOM   6405  C  C   . ILE F  1 114 ? 138.643 62.429  48.305 1.00   14.37 ? 113  ILE F C   1 
ATOM   6406  O  O   . ILE F  1 114 ? 139.037 61.518  47.629 1.00   14.73 ? 113  ILE F O   1 
ATOM   6407  C  CB  . ILE F  1 114 ? 137.791 64.443  46.960 1.00   14.77 ? 113  ILE F CB  1 
ATOM   6408  C  CG1 . ILE F  1 114 ? 137.984 65.982  46.887 1.00   14.79 ? 113  ILE F CG1 1 
ATOM   6409  C  CG2 . ILE F  1 114 ? 136.384 64.058  47.470 1.00   14.73 ? 113  ILE F CG2 1 
ATOM   6410  C  CD1 . ILE F  1 114 ? 137.099 66.707  45.916 1.00   15.28 ? 113  ILE F CD1 1 
ATOM   6411  N  N   . GLY F  1 115 ? 138.102 62.224  49.489 1.00   14.16 ? 114  GLY F N   1 
ATOM   6412  C  CA  . GLY F  1 115 ? 137.882 60.890  50.000 1.00   14.14 ? 114  GLY F CA  1 
ATOM   6413  C  C   . GLY F  1 115 ? 139.111 60.284  50.677 1.00   13.95 ? 114  GLY F C   1 
ATOM   6414  O  O   . GLY F  1 115 ? 139.047 59.153  51.115 1.00   14.09 ? 114  GLY F O   1 
ATOM   6415  N  N   . ARG F  1 116 ? 140.219 61.018  50.746 1.00   13.51 ? 115  ARG F N   1 
ATOM   6416  C  CA  . ARG F  1 116 ? 141.419 60.554  51.430 1.00   13.38 ? 115  ARG F CA  1 
ATOM   6417  C  C   . ARG F  1 116 ? 141.580 61.333  52.734 1.00   13.06 ? 115  ARG F C   1 
ATOM   6418  O  O   . ARG F  1 116 ? 140.685 62.109  53.118 1.00   12.96 ? 115  ARG F O   1 
ATOM   6419  C  CB  . ARG F  1 116 ? 142.644 60.675  50.497 1.00   13.44 ? 115  ARG F CB  1 
ATOM   6420  C  CG  . ARG F  1 116 ? 142.406 59.898  49.190 1.00   13.77 ? 115  ARG F CG  1 
ATOM   6421  C  CD  . ARG F  1 116 ? 143.617 59.794  48.277 1.00   13.92 ? 115  ARG F CD  1 
ATOM   6422  N  NE  . ARG F  1 116 ? 143.258 59.232  46.982 1.00   14.13 ? 115  ARG F NE  1 
ATOM   6423  C  CZ  . ARG F  1 116 ? 143.207 57.942  46.678 1.00   14.52 ? 115  ARG F CZ  1 
ATOM   6424  N  NH1 . ARG F  1 116 ? 143.503 56.998  47.571 1.00   14.58 ? 115  ARG F NH1 1 
ATOM   6425  N  NH2 . ARG F  1 116 ? 142.874 57.587  45.439 1.00   14.79 ? 115  ARG F NH2 1 
ATOM   6426  N  N   . THR F  1 117 ? 142.668 61.100  53.454 1.00   12.84 ? 116  THR F N   1 
ATOM   6427  C  CA  . THR F  1 117 ? 142.796 61.662  54.785 1.00   12.69 ? 116  THR F CA  1 
ATOM   6428  C  C   . THR F  1 117 ? 143.927 62.658  54.861 1.00   12.42 ? 116  THR F C   1 
ATOM   6429  O  O   . THR F  1 117 ? 145.036 62.348  54.453 1.00   12.49 ? 116  THR F O   1 
ATOM   6430  C  CB  . THR F  1 117 ? 143.003 60.543  55.823 1.00   12.89 ? 116  THR F CB  1 
ATOM   6431  O  OG1 . THR F  1 117 ? 141.806 59.744  55.901 1.00   13.17 ? 116  THR F OG1 1 
ATOM   6432  C  CG2 . THR F  1 117 ? 143.281 61.125  57.181 1.00   12.83 ? 116  THR F CG2 1 
ATOM   6433  N  N   . LEU F  1 118 ? 143.640 63.856  55.376 1.00   12.24 ? 117  LEU F N   1 
ATOM   6434  C  CA  . LEU F  1 118 ? 144.665 64.830  55.723 1.00   12.04 ? 117  LEU F CA  1 
ATOM   6435  C  C   . LEU F  1 118 ? 145.142 64.545  57.131 1.00   12.11 ? 117  LEU F C   1 
ATOM   6436  O  O   . LEU F  1 118 ? 144.312 64.403  58.056 1.00   12.25 ? 117  LEU F O   1 
ATOM   6437  C  CB  . LEU F  1 118 ? 144.127 66.254  55.667 1.00   11.93 ? 117  LEU F CB  1 
ATOM   6438  C  CG  . LEU F  1 118 ? 145.127 67.401  55.769 1.00   11.80 ? 117  LEU F CG  1 
ATOM   6439  C  CD1 . LEU F  1 118 ? 146.183 67.345  54.638 1.00   11.66 ? 117  LEU F CD1 1 
ATOM   6440  C  CD2 . LEU F  1 118 ? 144.406 68.751  55.777 1.00   11.76 ? 117  LEU F CD2 1 
ATOM   6441  N  N   . VAL F  1 119 ? 146.452 64.536  57.313 1.00   12.07 ? 118  VAL F N   1 
ATOM   6442  C  CA  . VAL F  1 119 ? 147.051 64.250  58.618 1.00   12.25 ? 118  VAL F CA  1 
ATOM   6443  C  C   . VAL F  1 119 ? 148.053 65.336  58.998 1.00   12.34 ? 118  VAL F C   1 
ATOM   6444  O  O   . VAL F  1 119 ? 148.855 65.756  58.170 1.00   12.24 ? 118  VAL F O   1 
ATOM   6445  C  CB  . VAL F  1 119 ? 147.781 62.882  58.597 1.00   12.30 ? 118  VAL F CB  1 
ATOM   6446  C  CG1 . VAL F  1 119 ? 148.470 62.634  59.933 1.00   12.38 ? 118  VAL F CG1 1 
ATOM   6447  C  CG2 . VAL F  1 119 ? 146.806 61.752  58.257 1.00   12.35 ? 118  VAL F CG2 1 
ATOM   6448  N  N   . VAL F  1 120 ? 147.977 65.822  60.232 1.00   12.63 ? 119  VAL F N   1 
ATOM   6449  C  CA  . VAL F  1 120 ? 149.015 66.678  60.781 1.00   12.81 ? 119  VAL F CA  1 
ATOM   6450  C  C   . VAL F  1 120 ? 149.768 65.906  61.874 1.00   13.29 ? 119  VAL F C   1 
ATOM   6451  O  O   . VAL F  1 120 ? 149.167 65.247  62.724 1.00   13.33 ? 119  VAL F O   1 
ATOM   6452  C  CB  . VAL F  1 120 ? 148.461 68.028  61.271 1.00   12.76 ? 119  VAL F CB  1 
ATOM   6453  C  CG1 . VAL F  1 120 ? 147.519 67.861  62.461 1.00   12.90 ? 119  VAL F CG1 1 
ATOM   6454  C  CG2 . VAL F  1 120 ? 149.613 68.978  61.613 1.00   12.71 ? 119  VAL F CG2 1 
ATOM   6455  N  N   . HIS F  1 121 ? 151.086 66.008  61.847 1.00   13.83 ? 120  HIS F N   1 
ATOM   6456  C  CA  . HIS F  1 121 ? 151.981 65.144  62.620 1.00   14.60 ? 120  HIS F CA  1 
ATOM   6457  C  C   . HIS F  1 121 ? 152.620 65.770  63.822 1.00   15.32 ? 120  HIS F C   1 
ATOM   6458  O  O   . HIS F  1 121 ? 152.711 66.974  63.963 1.00   15.18 ? 120  HIS F O   1 
ATOM   6459  C  CB  . HIS F  1 121 ? 153.101 64.616  61.735 1.00   14.73 ? 120  HIS F CB  1 
ATOM   6460  C  CG  . HIS F  1 121 ? 152.690 63.456  60.859 1.00   14.89 ? 120  HIS F CG  1 
ATOM   6461  N  ND1 . HIS F  1 121 ? 152.765 62.174  61.271 1.00   15.14 ? 120  HIS F ND1 1 
ATOM   6462  C  CD2 . HIS F  1 121 ? 152.215 63.425  59.569 1.00   14.89 ? 120  HIS F CD2 1 
ATOM   6463  C  CE1 . HIS F  1 121 ? 152.336 61.377  60.312 1.00   15.32 ? 120  HIS F CE1 1 
ATOM   6464  N  NE2 . HIS F  1 121 ? 151.986 62.139  59.266 1.00   15.18 ? 120  HIS F NE2 1 
ATOM   6465  N  N   . GLU F  1 122 ? 153.128 64.880  64.656 1.00   16.45 ? 121  GLU F N   1 
ATOM   6466  C  CA  . GLU F  1 122 ? 153.859 65.185  65.873 1.00   17.55 ? 121  GLU F CA  1 
ATOM   6467  C  C   . GLU F  1 122 ? 155.100 66.035  65.666 1.00   17.83 ? 121  GLU F C   1 
ATOM   6468  O  O   . GLU F  1 122 ? 155.346 66.961  66.440 1.00   17.82 ? 121  GLU F O   1 
ATOM   6469  C  CB  . GLU F  1 122 ? 154.282 63.861  66.510 1.00   18.32 ? 121  GLU F CB  1 
ATOM   6470  C  CG  . GLU F  1 122 ? 154.938 63.937  67.878 1.00   19.40 ? 121  GLU F CG  1 
ATOM   6471  C  CD  . GLU F  1 122 ? 155.650 62.634  68.250 1.00   20.47 ? 121  GLU F CD  1 
ATOM   6472  O  OE1 . GLU F  1 122 ? 155.551 61.598  67.535 1.00   20.82 ? 121  GLU F OE1 1 
ATOM   6473  O  OE2 . GLU F  1 122 ? 156.391 62.665  69.240 1.00   22.50 ? 121  GLU F OE2 1 
ATOM   6474  N  N   . LYS F  1 123 ? 155.901 65.650  64.676 1.00   18.27 ? 122  LYS F N   1 
ATOM   6475  C  CA  . LYS F  1 123 ? 157.230 66.204  64.485 1.00   19.08 ? 122  LYS F CA  1 
ATOM   6476  C  C   . LYS F  1 123 ? 157.322 66.815  63.109 1.00   18.13 ? 122  LYS F C   1 
ATOM   6477  O  O   . LYS F  1 123 ? 156.408 66.630  62.282 1.00   17.61 ? 122  LYS F O   1 
ATOM   6478  C  CB  . LYS F  1 123 ? 158.308 65.110  64.578 1.00   21.07 ? 122  LYS F CB  1 
ATOM   6479  C  CG  . LYS F  1 123 ? 158.332 64.313  65.877 1.00   22.91 ? 122  LYS F CG  1 
ATOM   6480  C  CD  . LYS F  1 123 ? 159.625 63.534  65.998 1.00   25.20 ? 122  LYS F CD  1 
ATOM   6481  C  CE  . LYS F  1 123 ? 159.498 62.113  65.497 1.00   27.08 ? 122  LYS F CE  1 
ATOM   6482  N  NZ  . LYS F  1 123 ? 160.823 61.380  65.461 1.00   29.70 ? 122  LYS F NZ  1 
ATOM   6483  N  N   . ALA F  1 124 ? 158.440 67.502  62.880 1.00   17.29 ? 123  ALA F N   1 
ATOM   6484  C  CA  . ALA F  1 124 ? 158.820 68.029  61.575 1.00   16.99 ? 123  ALA F CA  1 
ATOM   6485  C  C   . ALA F  1 124 ? 159.022 66.902  60.574 1.00   16.72 ? 123  ALA F C   1 
ATOM   6486  O  O   . ALA F  1 124 ? 159.590 65.832  60.904 1.00   16.91 ? 123  ALA F O   1 
ATOM   6487  C  CB  . ALA F  1 124 ? 160.102 68.879  61.680 1.00   16.88 ? 123  ALA F CB  1 
ATOM   6488  N  N   . ASP F  1 125 ? 158.543 67.135  59.354 1.00   16.16 ? 124  ASP F N   1 
ATOM   6489  C  CA  . ASP F  1 125 ? 158.891 66.313  58.195 1.00   16.01 ? 124  ASP F CA  1 
ATOM   6490  C  C   . ASP F  1 125 ? 160.303 66.694  57.761 1.00   15.85 ? 124  ASP F C   1 
ATOM   6491  O  O   . ASP F  1 125 ? 160.577 67.861  57.530 1.00   16.17 ? 124  ASP F O   1 
ATOM   6492  C  CB  . ASP F  1 125 ? 157.904 66.598  57.055 1.00   15.79 ? 124  ASP F CB  1 
ATOM   6493  C  CG  . ASP F  1 125 ? 157.973 65.598  55.919 1.00   15.74 ? 124  ASP F CG  1 
ATOM   6494  O  OD1 . ASP F  1 125 ? 159.061 65.055  55.596 1.00   15.91 ? 124  ASP F OD1 1 
ATOM   6495  O  OD2 . ASP F  1 125 ? 156.911 65.391  55.302 1.00   15.58 ? 124  ASP F OD2 1 
ATOM   6496  N  N   . ASP F  1 126 ? 161.207 65.721  57.664 1.00   15.93 ? 125  ASP F N   1 
ATOM   6497  C  CA  . ASP F  1 126 ? 162.604 66.011  57.214 1.00   15.80 ? 125  ASP F CA  1 
ATOM   6498  C  C   . ASP F  1 126 ? 162.712 66.092  55.684 1.00   15.36 ? 125  ASP F C   1 
ATOM   6499  O  O   . ASP F  1 126 ? 163.784 66.291  55.139 1.00   15.48 ? 125  ASP F O   1 
ATOM   6500  C  CB  . ASP F  1 126 ? 163.642 65.050  57.843 1.00   16.10 ? 125  ASP F CB  1 
ATOM   6501  C  CG  . ASP F  1 126 ? 163.561 63.593  57.312 1.00   16.37 ? 125  ASP F CG  1 
ATOM   6502  O  OD1 . ASP F  1 126 ? 162.991 63.319  56.233 1.00   16.41 ? 125  ASP F OD1 1 
ATOM   6503  O  OD2 . ASP F  1 126 ? 164.085 62.689  57.996 1.00   16.79 ? 125  ASP F OD2 1 
ATOM   6504  N  N   . LEU F  1 127 ? 161.587 65.927  54.997 1.00   14.99 ? 126  LEU F N   1 
ATOM   6505  C  CA  . LEU F  1 127 ? 161.476 66.175  53.542 1.00   14.76 ? 126  LEU F CA  1 
ATOM   6506  C  C   . LEU F  1 127 ? 162.356 65.217  52.714 1.00   14.87 ? 126  LEU F C   1 
ATOM   6507  O  O   . LEU F  1 127 ? 162.762 65.520  51.590 1.00   14.93 ? 126  LEU F O   1 
ATOM   6508  C  CB  . LEU F  1 127 ? 161.762 67.639  53.213 1.00   14.56 ? 126  LEU F CB  1 
ATOM   6509  C  CG  . LEU F  1 127 ? 161.050 68.732  54.021 1.00   14.52 ? 126  LEU F CG  1 
ATOM   6510  C  CD1 . LEU F  1 127 ? 161.482 70.118  53.505 1.00   14.46 ? 126  LEU F CD1 1 
ATOM   6511  C  CD2 . LEU F  1 127 ? 159.518 68.578  53.950 1.00   14.22 ? 126  LEU F CD2 1 
ATOM   6512  N  N   . GLY F  1 128 ? 162.632 64.050  53.284 1.00   15.00 ? 127  GLY F N   1 
ATOM   6513  C  CA  . GLY F  1 128 ? 163.380 63.017  52.591 1.00   15.35 ? 127  GLY F CA  1 
ATOM   6514  C  C   . GLY F  1 128 ? 164.864 63.140  52.707 1.00   15.64 ? 127  GLY F C   1 
ATOM   6515  O  O   . GLY F  1 128 ? 165.564 62.404  52.060 1.00   15.51 ? 127  GLY F O   1 
ATOM   6516  N  N   . LYS F  1 129 ? 165.330 64.026  53.592 1.00   15.99 ? 128  LYS F N   1 
ATOM   6517  C  CA  . LYS F  1 129 ? 166.758 64.390  53.689 1.00   16.65 ? 128  LYS F CA  1 
ATOM   6518  C  C   . LYS F  1 129 ? 167.417 63.924  54.996 1.00   16.88 ? 128  LYS F C   1 
ATOM   6519  O  O   . LYS F  1 129 ? 168.461 64.433  55.373 1.00   17.32 ? 128  LYS F O   1 
ATOM   6520  C  CB  . LYS F  1 129 ? 166.909 65.921  53.528 1.00   16.81 ? 128  LYS F CB  1 
ATOM   6521  C  CG  . LYS F  1 129 ? 166.382 66.447  52.196 1.00   17.01 ? 128  LYS F CG  1 
ATOM   6522  C  CD  . LYS F  1 129 ? 166.221 67.959  52.136 1.00   17.45 ? 128  LYS F CD  1 
ATOM   6523  C  CE  . LYS F  1 129 ? 167.517 68.719  52.162 1.00   18.14 ? 128  LYS F CE  1 
ATOM   6524  N  NZ  . LYS F  1 129 ? 167.318 70.165  51.767 1.00   19.15 ? 128  LYS F NZ  1 
ATOM   6525  N  N   . GLY F  1 130 ? 166.829 62.936  55.662 1.00   16.92 ? 129  GLY F N   1 
ATOM   6526  C  CA  . GLY F  1 130 ? 167.314 62.468  56.970 1.00   17.16 ? 129  GLY F CA  1 
ATOM   6527  C  C   . GLY F  1 130 ? 168.295 61.292  56.961 1.00   17.74 ? 129  GLY F C   1 
ATOM   6528  O  O   . GLY F  1 130 ? 168.811 60.905  58.015 1.00   17.82 ? 129  GLY F O   1 
ATOM   6529  N  N   . GLY F  1 131 ? 168.538 60.705  55.794 1.00   18.10 ? 130  GLY F N   1 
ATOM   6530  C  CA  . GLY F  1 131 ? 169.606 59.728  55.635 1.00   18.84 ? 130  GLY F CA  1 
ATOM   6531  C  C   . GLY F  1 131 ? 169.293 58.327  56.113 1.00   19.51 ? 130  GLY F C   1 
ATOM   6532  O  O   . GLY F  1 131 ? 170.165 57.458  56.111 1.00   19.81 ? 130  GLY F O   1 
ATOM   6533  N  N   . ASN F  1 132 ? 168.044 58.084  56.490 1.00   20.24 ? 131  ASN F N   1 
ATOM   6534  C  CA  . ASN F  1 132 ? 167.607 56.731  56.821 1.00   21.24 ? 131  ASN F CA  1 
ATOM   6535  C  C   . ASN F  1 132 ? 166.409 56.319  55.999 1.00   21.81 ? 131  ASN F C   1 
ATOM   6536  O  O   . ASN F  1 132 ? 165.842 57.133  55.251 1.00   21.02 ? 131  ASN F O   1 
ATOM   6537  C  CB  . ASN F  1 132 ? 167.364 56.575  58.319 1.00   21.50 ? 131  ASN F CB  1 
ATOM   6538  C  CG  . ASN F  1 132 ? 166.313 57.510  58.850 1.00   21.20 ? 131  ASN F CG  1 
ATOM   6539  O  OD1 . ASN F  1 132 ? 165.558 58.100  58.085 1.00   20.99 ? 131  ASN F OD1 1 
ATOM   6540  N  ND2 . ASN F  1 132 ? 166.262 57.655  60.179 1.00   20.97 ? 131  ASN F ND2 1 
ATOM   6541  N  N   . GLU F  1 133 ? 166.058 55.038  56.101 1.00   23.11 ? 132  GLU F N   1 
ATOM   6542  C  CA  . GLU F  1 133 ? 164.984 54.454  55.325 1.00   24.36 ? 132  GLU F CA  1 
ATOM   6543  C  C   . GLU F  1 133 ? 163.642 55.063  55.703 1.00   23.28 ? 132  GLU F C   1 
ATOM   6544  O  O   . GLU F  1 133 ? 162.743 55.220  54.859 1.00   22.86 ? 132  GLU F O   1 
ATOM   6545  C  CB  . GLU F  1 133 ? 164.962 52.922  55.539 1.00   27.36 ? 132  GLU F CB  1 
ATOM   6546  C  CG  . GLU F  1 133 ? 163.787 52.203  54.908 1.00   29.34 ? 132  GLU F CG  1 
ATOM   6547  C  CD  . GLU F  1 133 ? 163.808 50.678  55.113 1.00   32.87 ? 132  GLU F CD  1 
ATOM   6548  O  OE1 . GLU F  1 133 ? 164.917 50.083  55.161 1.00   35.15 ? 132  GLU F OE1 1 
ATOM   6549  O  OE2 . GLU F  1 133 ? 162.702 50.078  55.213 1.00   34.92 ? 132  GLU F OE2 1 
ATOM   6550  N  N   . GLU F  1 134 ? 163.499 55.407  56.973 1.00   22.50 ? 133  GLU F N   1 
ATOM   6551  C  CA  . GLU F  1 134 ? 162.260 56.010  57.432 1.00   22.11 ? 133  GLU F CA  1 
ATOM   6552  C  C   . GLU F  1 134 ? 162.079 57.408  56.813 1.00   20.65 ? 133  GLU F C   1 
ATOM   6553  O  O   . GLU F  1 134 ? 160.964 57.797  56.572 1.00   20.12 ? 133  GLU F O   1 
ATOM   6554  C  CB  . GLU F  1 134 ? 162.211 56.078  58.959 1.00   22.90 ? 133  GLU F CB  1 
ATOM   6555  C  CG  . GLU F  1 134 ? 160.875 56.546  59.523 1.00   23.55 ? 133  GLU F CG  1 
ATOM   6556  C  CD  . GLU F  1 134 ? 159.730 55.625  59.173 1.00   24.40 ? 133  GLU F CD  1 
ATOM   6557  O  OE1 . GLU F  1 134 ? 159.927 54.409  59.053 1.00   28.15 ? 133  GLU F OE1 1 
ATOM   6558  O  OE2 . GLU F  1 134 ? 158.615 56.106  59.012 1.00   24.61 ? 133  GLU F OE2 1 
ATOM   6559  N  N   . SER F  1 135 ? 163.163 58.140  56.540 1.00   20.02 ? 134  SER F N   1 
ATOM   6560  C  CA  . SER F  1 135 ? 163.054 59.475  55.896 1.00   19.23 ? 134  SER F CA  1 
ATOM   6561  C  C   . SER F  1 135 ? 162.401 59.401  54.511 1.00   19.09 ? 134  SER F C   1 
ATOM   6562  O  O   . SER F  1 135 ? 161.646 60.286  54.128 1.00   18.11 ? 134  SER F O   1 
ATOM   6563  C  CB  . SER F  1 135 ? 164.423 60.153  55.778 1.00   19.03 ? 134  SER F CB  1 
ATOM   6564  O  OG  . SER F  1 135 ? 164.366 61.368  55.019 1.00   18.24 ? 134  SER F OG  1 
ATOM   6565  N  N   . THR F  1 136 ? 162.700 58.320  53.795 1.00   19.82 ? 135  THR F N   1 
ATOM   6566  C  CA  . THR F  1 136 ? 162.202 58.056  52.449 1.00   20.19 ? 135  THR F CA  1 
ATOM   6567  C  C   . THR F  1 136 ? 160.822 57.447  52.436 1.00   20.01 ? 135  THR F C   1 
ATOM   6568  O  O   . THR F  1 136 ? 160.306 57.173  51.368 1.00   19.59 ? 135  THR F O   1 
ATOM   6569  C  CB  . THR F  1 136 ? 163.103 57.042  51.702 1.00   21.36 ? 135  THR F CB  1 
ATOM   6570  O  OG1 . THR F  1 136 ? 162.843 55.696  52.171 1.00   22.95 ? 135  THR F OG1 1 
ATOM   6571  C  CG2 . THR F  1 136 ? 164.521 57.365  51.901 1.00   22.16 ? 135  THR F CG2 1 
ATOM   6572  N  N   . LYS F  1 137 ? 160.228 57.205  53.607 1.00   20.59 ? 136  LYS F N   1 
ATOM   6573  C  CA  . LYS F  1 137 ? 158.846 56.732  53.674 1.00   21.25 ? 136  LYS F CA  1 
ATOM   6574  C  C   . LYS F  1 137 ? 157.919 57.766  54.281 1.00   20.08 ? 136  LYS F C   1 
ATOM   6575  O  O   . LYS F  1 137 ? 156.838 58.025  53.770 1.00   19.98 ? 136  LYS F O   1 
ATOM   6576  C  CB  . LYS F  1 137 ? 158.726 55.478  54.524 1.00   23.25 ? 136  LYS F CB  1 
ATOM   6577  C  CG  . LYS F  1 137 ? 159.715 54.392  54.230 1.00   25.64 ? 136  LYS F CG  1 
ATOM   6578  C  CD  . LYS F  1 137 ? 159.259 53.091  54.897 1.00   28.09 ? 136  LYS F CD  1 
ATOM   6579  C  CE  . LYS F  1 137 ? 160.442 52.231  55.267 1.00   30.66 ? 136  LYS F CE  1 
ATOM   6580  N  NZ  . LYS F  1 137 ? 160.044 50.917  55.871 1.00   33.63 ? 136  LYS F NZ  1 
ATOM   6581  N  N   . THR F  1 138 ? 158.316 58.323  55.404 1.00   19.00 ? 137  THR F N   1 
ATOM   6582  C  CA  . THR F  1 138 ? 157.417 59.185  56.156 1.00   18.23 ? 137  THR F CA  1 
ATOM   6583  C  C   . THR F  1 138 ? 158.015 60.538  56.431 1.00   17.62 ? 137  THR F C   1 
ATOM   6584  O  O   . THR F  1 138 ? 157.323 61.417  56.945 1.00   17.86 ? 137  THR F O   1 
ATOM   6585  C  CB  . THR F  1 138 ? 157.018 58.562  57.522 1.00   18.27 ? 137  THR F CB  1 
ATOM   6586  O  OG1 . THR F  1 138 ? 158.183 58.446  58.359 1.00   18.39 ? 137  THR F OG1 1 
ATOM   6587  C  CG2 . THR F  1 138 ? 156.338 57.208  57.348 1.00   18.23 ? 137  THR F CG2 1 
ATOM   6588  N  N   . GLY F  1 139 ? 159.291 60.729  56.125 1.00   17.38 ? 138  GLY F N   1 
ATOM   6589  C  CA  . GLY F  1 139 ? 159.963 61.937  56.562 1.00   17.18 ? 138  GLY F CA  1 
ATOM   6590  C  C   . GLY F  1 139 ? 160.258 62.064  58.058 1.00   17.25 ? 138  GLY F C   1 
ATOM   6591  O  O   . GLY F  1 139 ? 160.621 63.148  58.498 1.00   17.21 ? 138  GLY F O   1 
ATOM   6592  N  N   . ASN F  1 140 ? 160.150 60.968  58.823 1.00   17.61 ? 139  ASN F N   1 
ATOM   6593  C  CA  . ASN F  1 140 ? 160.372 60.960  60.300 1.00   17.80 ? 139  ASN F CA  1 
ATOM   6594  C  C   . ASN F  1 140 ? 159.464 61.934  61.076 1.00   17.35 ? 139  ASN F C   1 
ATOM   6595  O  O   . ASN F  1 140 ? 159.868 62.484  62.110 1.00   16.97 ? 139  ASN F O   1 
ATOM   6596  C  CB  . ASN F  1 140 ? 161.852 61.235  60.646 1.00   18.03 ? 139  ASN F CB  1 
ATOM   6597  C  CG  . ASN F  1 140 ? 162.759 60.071  60.273 1.00   18.89 ? 139  ASN F CG  1 
ATOM   6598  O  OD1 . ASN F  1 140 ? 162.661 59.007  60.877 1.00   20.24 ? 139  ASN F OD1 1 
ATOM   6599  N  ND2 . ASN F  1 140 ? 163.615 60.251  59.269 1.00   18.43 ? 139  ASN F ND2 1 
ATOM   6600  N  N   . ALA F  1 141 ? 158.240 62.132  60.580 1.00   16.80 ? 140  ALA F N   1 
ATOM   6601  C  CA  . ALA F  1 141 ? 157.332 63.116  61.170 1.00   16.57 ? 140  ALA F CA  1 
ATOM   6602  C  C   . ALA F  1 141 ? 156.640 62.623  62.435 1.00   16.73 ? 140  ALA F C   1 
ATOM   6603  O  O   . ALA F  1 141 ? 155.911 63.378  63.074 1.00   16.60 ? 140  ALA F O   1 
ATOM   6604  C  CB  . ALA F  1 141 ? 156.281 63.574  60.146 1.00   16.09 ? 140  ALA F CB  1 
ATOM   6605  N  N   . GLY F  1 142 ? 156.802 61.349  62.766 1.00   17.14 ? 141  GLY F N   1 
ATOM   6606  C  CA  . GLY F  1 142 ? 156.278 60.824  64.035 1.00   17.35 ? 141  GLY F CA  1 
ATOM   6607  C  C   . GLY F  1 142 ? 154.792 60.591  63.992 1.00   17.45 ? 141  GLY F C   1 
ATOM   6608  O  O   . GLY F  1 142 ? 154.206 60.347  62.926 1.00   17.38 ? 141  GLY F O   1 
ATOM   6609  N  N   . SER F  1 143 ? 154.157 60.652  65.153 1.00   17.78 ? 142  SER F N   1 
ATOM   6610  C  CA  . SER F  1 143 ? 152.788 60.201  65.258 1.00   17.91 ? 142  SER F CA  1 
ATOM   6611  C  C   . SER F  1 143 ? 151.763 61.168  64.617 1.00   17.48 ? 142  SER F C   1 
ATOM   6612  O  O   . SER F  1 143 ? 152.066 62.318  64.234 1.00   17.42 ? 142  SER F O   1 
ATOM   6613  C  CB  . SER F  1 143 ? 152.452 59.904  66.725 1.00   18.66 ? 142  SER F CB  1 
ATOM   6614  O  OG  . SER F  1 143 ? 152.309 61.125  67.419 1.00   19.55 ? 142  SER F OG  1 
ATOM   6615  N  N   . ARG F  1 144 ? 150.550 60.666  64.465 1.00   17.18 ? 143  ARG F N   1 
ATOM   6616  C  CA  . ARG F  1 144 ? 149.478 61.360  63.776 1.00   16.96 ? 143  ARG F CA  1 
ATOM   6617  C  C   . ARG F  1 144 ? 148.635 62.072  64.820 1.00   17.11 ? 143  ARG F C   1 
ATOM   6618  O  O   . ARG F  1 144 ? 147.869 61.422  65.516 1.00   17.27 ? 143  ARG F O   1 
ATOM   6619  C  CB  . ARG F  1 144 ? 148.634 60.335  63.045 1.00   16.90 ? 143  ARG F CB  1 
ATOM   6620  C  CG  . ARG F  1 144 ? 149.502 59.515  62.107 1.00   17.09 ? 143  ARG F CG  1 
ATOM   6621  C  CD  . ARG F  1 144 ? 148.717 58.527  61.282 1.00   17.19 ? 143  ARG F CD  1 
ATOM   6622  N  NE  . ARG F  1 144 ? 149.645 57.779  60.481 1.00   17.33 ? 143  ARG F NE  1 
ATOM   6623  C  CZ  . ARG F  1 144 ? 149.329 56.868  59.584 1.00   17.85 ? 143  ARG F CZ  1 
ATOM   6624  N  NH1 . ARG F  1 144 ? 148.057 56.573  59.310 1.00   18.10 ? 143  ARG F NH1 1 
ATOM   6625  N  NH2 . ARG F  1 144 ? 150.309 56.261  58.936 1.00   18.15 ? 143  ARG F NH2 1 
ATOM   6626  N  N   . LEU F  1 145 ? 148.799 63.383  64.969 1.00   16.83 ? 144  LEU F N   1 
ATOM   6627  C  CA  . LEU F  1 145 ? 148.104 64.084  66.056 1.00   16.97 ? 144  LEU F CA  1 
ATOM   6628  C  C   . LEU F  1 145 ? 146.632 64.289  65.774 1.00   16.90 ? 144  LEU F C   1 
ATOM   6629  O  O   . LEU F  1 145 ? 145.784 64.184  66.666 1.00   17.63 ? 144  LEU F O   1 
ATOM   6630  C  CB  . LEU F  1 145 ? 148.769 65.421  66.357 1.00   16.86 ? 144  LEU F CB  1 
ATOM   6631  C  CG  . LEU F  1 145 ? 150.241 65.382  66.770 1.00   17.04 ? 144  LEU F CG  1 
ATOM   6632  C  CD1 . LEU F  1 145 ? 150.719 66.791  67.121 1.00   17.21 ? 144  LEU F CD1 1 
ATOM   6633  C  CD2 . LEU F  1 145 ? 150.455 64.429  67.930 1.00   17.36 ? 144  LEU F CD2 1 
ATOM   6634  N  N   . ALA F  1 146 ? 146.308 64.573  64.529 1.00   16.49 ? 145  ALA F N   1 
ATOM   6635  C  CA  . ALA F  1 146 ? 144.917 64.798  64.150 1.00   16.16 ? 145  ALA F CA  1 
ATOM   6636  C  C   . ALA F  1 146 ? 144.740 64.511  62.681 1.00   15.83 ? 145  ALA F C   1 
ATOM   6637  O  O   . ALA F  1 146 ? 145.691 64.568  61.895 1.00   15.51 ? 145  ALA F O   1 
ATOM   6638  C  CB  . ALA F  1 146 ? 144.514 66.241  64.462 1.00   16.25 ? 145  ALA F CB  1 
ATOM   6639  N  N   . CYS F  1 147 ? 143.507 64.238  62.288 1.00   15.86 ? 146  CYS F N   1 
ATOM   6640  C  CA  . CYS F  1 147 ? 143.229 63.926  60.897 1.00   15.63 ? 146  CYS F CA  1 
ATOM   6641  C  C   . CYS F  1 147 ? 141.763 64.090  60.564 1.00   15.33 ? 146  CYS F C   1 
ATOM   6642  O  O   . CYS F  1 147 ? 140.929 64.287  61.443 1.00   15.40 ? 146  CYS F O   1 
ATOM   6643  C  CB  . CYS F  1 147 ? 143.635 62.484  60.595 1.00   16.16 ? 146  CYS F CB  1 
ATOM   6644  S  SG  . CYS F  1 147 ? 142.791 61.231  61.587 1.00   17.04 ? 146  CYS F SG  1 
ATOM   6645  N  N   . GLY F  1 148 ? 141.459 63.984  59.275 1.00   14.82 ? 147  GLY F N   1 
ATOM   6646  C  CA  . GLY F  1 148 ? 140.086 64.043  58.800 1.00   14.50 ? 147  GLY F CA  1 
ATOM   6647  C  C   . GLY F  1 148 ? 140.015 63.636  57.351 1.00   14.07 ? 147  GLY F C   1 
ATOM   6648  O  O   . GLY F  1 148 ? 141.025 63.669  56.626 1.00   13.86 ? 147  GLY F O   1 
ATOM   6649  N  N   . VAL F  1 149 ? 138.829 63.213  56.942 1.00   13.82 ? 148  VAL F N   1 
ATOM   6650  C  CA  . VAL F  1 149 ? 138.585 62.816  55.583 1.00   13.67 ? 148  VAL F CA  1 
ATOM   6651  C  C   . VAL F  1 149 ? 138.300 64.061  54.761 1.00   13.54 ? 148  VAL F C   1 
ATOM   6652  O  O   . VAL F  1 149 ? 137.499 64.909  55.157 1.00   13.72 ? 148  VAL F O   1 
ATOM   6653  C  CB  . VAL F  1 149 ? 137.393 61.848  55.465 1.00   13.81 ? 148  VAL F CB  1 
ATOM   6654  C  CG1 . VAL F  1 149 ? 137.189 61.440  54.028 1.00   13.66 ? 148  VAL F CG1 1 
ATOM   6655  C  CG2 . VAL F  1 149 ? 137.603 60.608  56.354 1.00   13.91 ? 148  VAL F CG2 1 
ATOM   6656  N  N   . ILE F  1 150 ? 138.949 64.167  53.610 1.00   13.41 ? 149  ILE F N   1 
ATOM   6657  C  CA  . ILE F  1 150 ? 138.802 65.341  52.758 1.00   13.38 ? 149  ILE F CA  1 
ATOM   6658  C  C   . ILE F  1 150 ? 137.494 65.212  51.983 1.00   13.67 ? 149  ILE F C   1 
ATOM   6659  O  O   . ILE F  1 150 ? 137.306 64.246  51.260 1.00   13.76 ? 149  ILE F O   1 
ATOM   6660  C  CB  . ILE F  1 150 ? 139.978 65.482  51.788 1.00   13.16 ? 149  ILE F CB  1 
ATOM   6661  C  CG1 . ILE F  1 150 ? 141.272 65.689  52.562 1.00   12.99 ? 149  ILE F CG1 1 
ATOM   6662  C  CG2 . ILE F  1 150 ? 139.735 66.643  50.828 1.00   13.15 ? 149  ILE F CG2 1 
ATOM   6663  C  CD1 . ILE F  1 150 ? 142.544 65.502  51.751 1.00   12.90 ? 149  ILE F CD1 1 
ATOM   6664  N  N   . GLY F  1 151 ? 136.600 66.182  52.136 1.00   13.92 ? 150  GLY F N   1 
ATOM   6665  C  CA  . GLY F  1 151 ? 135.283 66.124  51.505 1.00   14.36 ? 150  GLY F CA  1 
ATOM   6666  C  C   . GLY F  1 151 ? 135.035 67.221  50.483 1.00   14.67 ? 150  GLY F C   1 
ATOM   6667  O  O   . GLY F  1 151 ? 135.637 68.291  50.552 1.00   14.55 ? 150  GLY F O   1 
ATOM   6668  N  N   . ILE F  1 152 ? 134.117 66.965  49.556 1.00   15.14 ? 151  ILE F N   1 
ATOM   6669  C  CA  A ILE F  1 152 ? 133.689 67.931  48.545 0.50   15.45 ? 151  ILE F CA  1 
ATOM   6670  C  CA  B ILE F  1 152 ? 133.794 67.988  48.578 0.50   15.55 ? 151  ILE F CA  1 
ATOM   6671  C  C   . ILE F  1 152 ? 132.966 69.088  49.241 1.00   15.81 ? 151  ILE F C   1 
ATOM   6672  O  O   . ILE F  1 152 ? 132.061 68.834  50.030 1.00   15.69 ? 151  ILE F O   1 
ATOM   6673  C  CB  A ILE F  1 152 ? 132.721 67.277  47.508 0.50   15.59 ? 151  ILE F CB  1 
ATOM   6674  C  CB  B ILE F  1 152 ? 133.121 67.447  47.299 0.50   15.84 ? 151  ILE F CB  1 
ATOM   6675  C  CG1 A ILE F  1 152 ? 133.381 66.064  46.845 0.50   15.53 ? 151  ILE F CG1 1 
ATOM   6676  C  CG1 B ILE F  1 152 ? 131.757 66.869  47.565 0.50   16.07 ? 151  ILE F CG1 1 
ATOM   6677  C  CG2 A ILE F  1 152 ? 132.321 68.274  46.425 0.50   15.76 ? 151  ILE F CG2 1 
ATOM   6678  C  CG2 B ILE F  1 152 ? 133.984 66.370  46.655 0.50   15.80 ? 151  ILE F CG2 1 
ATOM   6679  C  CD1 A ILE F  1 152 ? 132.502 65.276  45.902 0.50   15.75 ? 151  ILE F CD1 1 
ATOM   6680  C  CD1 B ILE F  1 152 ? 131.504 65.726  46.610 0.50   16.41 ? 151  ILE F CD1 1 
ATOM   6681  N  N   . ALA F  1 153 ? 133.332 70.327  48.924 1.00   16.38 ? 152  ALA F N   1 
ATOM   6682  C  CA  . ALA F  1 153 ? 132.714 71.513  49.520 1.00   17.51 ? 152  ALA F CA  1 
ATOM   6683  C  C   . ALA F  1 153 ? 132.079 72.389  48.431 1.00   19.00 ? 152  ALA F C   1 
ATOM   6684  O  O   . ALA F  1 153 ? 132.281 72.152  47.240 1.00   19.24 ? 152  ALA F O   1 
ATOM   6685  C  CB  . ALA F  1 153 ? 133.763 72.304  50.303 1.00   17.16 ? 152  ALA F CB  1 
ATOM   6686  N  N   . GLN F  1 154 ? 131.302 73.379  48.839 1.00   21.09 ? 153  GLN F N   1 
ATOM   6687  C  CA  . GLN F  1 154 ? 130.848 74.437  47.928 1.00   23.29 ? 153  GLN F CA  1 
ATOM   6688  C  C   . GLN F  1 154 ? 131.323 75.827  48.389 1.00   24.46 ? 153  GLN F C   1 
ATOM   6689  O  O   . GLN F  1 154 ? 131.875 76.010  49.486 1.00   25.34 ? 153  GLN F O   1 
ATOM   6690  C  CB  . GLN F  1 154 ? 129.329 74.460  47.860 1.00   24.80 ? 153  GLN F CB  1 
ATOM   6691  C  CG  . GLN F  1 154 ? 128.696 74.599  49.232 1.00   25.80 ? 153  GLN F CG  1 
ATOM   6692  C  CD  . GLN F  1 154 ? 127.237 74.977  49.192 1.00   26.90 ? 153  GLN F CD  1 
ATOM   6693  O  OE1 . GLN F  1 154 ? 126.767 75.613  48.235 1.00   28.52 ? 153  GLN F OE1 1 
ATOM   6694  N  NE2 . GLN F  1 154 ? 126.505 74.601  50.242 1.00   26.24 ? 153  GLN F NE2 1 
ATOM   6695  O  OXT . GLN F  1 154 ? 131.117 76.836  47.700 1.00   26.16 ? 153  GLN F OXT 1 
ATOM   6696  N  N   . ALA G  1 2   ? 178.031 101.624 40.624 1.00   37.88 ? 1    ALA G N   1 
ATOM   6697  C  CA  . ALA G  1 2   ? 178.647 101.319 41.964 1.00   37.13 ? 1    ALA G CA  1 
ATOM   6698  C  C   . ALA G  1 2   ? 179.142 99.865  42.071 1.00   34.34 ? 1    ALA G C   1 
ATOM   6699  O  O   . ALA G  1 2   ? 178.467 98.933  41.685 1.00   33.95 ? 1    ALA G O   1 
ATOM   6700  C  CB  . ALA G  1 2   ? 177.673 101.630 43.099 1.00   37.39 ? 1    ALA G CB  1 
ATOM   6701  N  N   . THR G  1 3   ? 180.322 99.705  42.640 1.00   32.51 ? 2    THR G N   1 
ATOM   6702  C  CA  . THR G  1 3   ? 181.015 98.442  42.683 1.00   31.03 ? 2    THR G CA  1 
ATOM   6703  C  C   . THR G  1 3   ? 181.181 97.950  44.150 1.00   28.10 ? 2    THR G C   1 
ATOM   6704  O  O   . THR G  1 3   ? 181.389 96.761  44.407 1.00   26.67 ? 2    THR G O   1 
ATOM   6705  C  CB  . THR G  1 3   ? 182.365 98.632  41.942 1.00   32.52 ? 2    THR G CB  1 
ATOM   6706  O  OG1 . THR G  1 3   ? 182.744 97.416  41.297 1.00   36.60 ? 2    THR G OG1 1 
ATOM   6707  C  CG2 . THR G  1 3   ? 183.467 99.090  42.871 1.00   31.92 ? 2    THR G CG2 1 
ATOM   6708  N  N   . LYS G  1 4   ? 181.065 98.864  45.111 1.00   26.46 ? 3    LYS G N   1 
ATOM   6709  C  CA  . LYS G  1 4   ? 181.211 98.531  46.522 1.00   25.29 ? 3    LYS G CA  1 
ATOM   6710  C  C   . LYS G  1 4   ? 180.174 99.236  47.394 1.00   22.98 ? 3    LYS G C   1 
ATOM   6711  O  O   . LYS G  1 4   ? 179.780 100.372 47.117 1.00   21.92 ? 3    LYS G O   1 
ATOM   6712  C  CB  . LYS G  1 4   ? 182.608 98.887  47.000 1.00   27.43 ? 3    LYS G CB  1 
ATOM   6713  C  CG  . LYS G  1 4   ? 183.688 97.921  46.527 1.00   29.62 ? 3    LYS G CG  1 
ATOM   6714  C  CD  . LYS G  1 4   ? 185.061 98.536  46.740 1.00   32.14 ? 3    LYS G CD  1 
ATOM   6715  C  CE  . LYS G  1 4   ? 186.186 97.510  46.886 1.00   34.41 ? 3    LYS G CE  1 
ATOM   6716  N  NZ  . LYS G  1 4   ? 186.711 96.998  45.588 1.00   36.10 ? 3    LYS G NZ  1 
ATOM   6717  N  N   . ALA G  1 5   ? 179.734 98.550  48.443 1.00   20.55 ? 4    ALA G N   1 
ATOM   6718  C  CA  . ALA G  1 5   ? 178.783 99.114  49.395 1.00   19.67 ? 4    ALA G CA  1 
ATOM   6719  C  C   . ALA G  1 5   ? 179.089 98.578  50.797 1.00   18.88 ? 4    ALA G C   1 
ATOM   6720  O  O   . ALA G  1 5   ? 179.849 97.611  50.944 1.00   18.98 ? 4    ALA G O   1 
ATOM   6721  C  CB  . ALA G  1 5   ? 177.339 98.789  48.979 1.00   19.16 ? 4    ALA G CB  1 
ATOM   6722  N  N   . VAL G  1 6   ? 178.512 99.212  51.817 1.00   17.99 ? 5    VAL G N   1 
ATOM   6723  C  CA  . VAL G  1 6   ? 178.791 98.876  53.219 1.00   17.39 ? 5    VAL G CA  1 
ATOM   6724  C  C   . VAL G  1 6   ? 177.583 99.219  54.069 1.00   16.87 ? 5    VAL G C   1 
ATOM   6725  O  O   . VAL G  1 6   ? 176.806 100.119 53.731 1.00   16.65 ? 5    VAL G O   1 
ATOM   6726  C  CB  . VAL G  1 6   ? 180.054 99.589  53.746 1.00   17.67 ? 5    VAL G CB  1 
ATOM   6727  C  CG1 . VAL G  1 6   ? 179.798 101.079 53.952 1.00   17.66 ? 5    VAL G CG1 1 
ATOM   6728  C  CG2 . VAL G  1 6   ? 180.559 98.901  55.010 1.00   17.61 ? 5    VAL G CG2 1 
ATOM   6729  N  N   . CYS G  1 7   ? 177.405 98.462  55.136 1.00   16.62 ? 6    CYS G N   1 
ATOM   6730  C  CA  . CYS G  1 7   ? 176.287 98.645  56.057 1.00   16.65 ? 6    CYS G CA  1 
ATOM   6731  C  C   . CYS G  1 7   ? 176.728 98.435  57.491 1.00   16.54 ? 6    CYS G C   1 
ATOM   6732  O  O   . CYS G  1 7   ? 177.329 97.413  57.820 1.00   15.97 ? 6    CYS G O   1 
ATOM   6733  C  CB  . CYS G  1 7   ? 175.200 97.646  55.738 1.00   16.51 ? 6    CYS G CB  1 
ATOM   6734  S  SG  . CYS G  1 7   ? 173.697 97.880  56.708 1.00   17.11 ? 6    CYS G SG  1 
ATOM   6735  N  N   . VAL G  1 8   ? 176.468 99.421  58.341 1.00   16.83 ? 7    VAL G N   1 
ATOM   6736  C  CA  . VAL G  1 8   ? 176.706 99.264  59.770 1.00   16.96 ? 7    VAL G CA  1 
ATOM   6737  C  C   . VAL G  1 8   ? 175.403 98.808  60.423 1.00   17.17 ? 7    VAL G C   1 
ATOM   6738  O  O   . VAL G  1 8   ? 174.422 99.501  60.387 1.00   17.25 ? 7    VAL G O   1 
ATOM   6739  C  CB  . VAL G  1 8   ? 177.191 100.577 60.422 1.00   17.10 ? 7    VAL G CB  1 
ATOM   6740  C  CG1 . VAL G  1 8   ? 177.442 100.359 61.919 1.00   17.09 ? 7    VAL G CG1 1 
ATOM   6741  C  CG2 . VAL G  1 8   ? 178.455 101.077 59.719 1.00   16.90 ? 7    VAL G CG2 1 
ATOM   6742  N  N   . LEU G  1 9   ? 175.395 97.641  61.042 1.00   17.79 ? 8    LEU G N   1 
ATOM   6743  C  CA  . LEU G  1 9   ? 174.193 97.170  61.715 1.00   18.28 ? 8    LEU G CA  1 
ATOM   6744  C  C   . LEU G  1 9   ? 174.220 97.530  63.184 1.00   19.41 ? 8    LEU G C   1 
ATOM   6745  O  O   . LEU G  1 9   ? 175.208 97.294  63.869 1.00   19.15 ? 8    LEU G O   1 
ATOM   6746  C  CB  . LEU G  1 9   ? 174.092 95.668  61.593 1.00   18.07 ? 8    LEU G CB  1 
ATOM   6747  C  CG  . LEU G  1 9   ? 173.961 95.032  60.213 1.00   17.81 ? 8    LEU G CG  1 
ATOM   6748  C  CD1 . LEU G  1 9   ? 174.202 93.521  60.350 1.00   17.97 ? 8    LEU G CD1 1 
ATOM   6749  C  CD2 . LEU G  1 9   ? 172.580 95.251  59.651 1.00   17.80 ? 8    LEU G CD2 1 
ATOM   6750  N  N   . LYS G  1 10  ? 173.120 98.095  63.662 1.00   21.27 ? 9    LYS G N   1 
ATOM   6751  C  CA  . LYS G  1 10  ? 172.966 98.478  65.066 1.00   22.99 ? 9    LYS G CA  1 
ATOM   6752  C  C   . LYS G  1 10  ? 171.561 98.169  65.513 1.00   23.06 ? 9    LYS G C   1 
ATOM   6753  O  O   . LYS G  1 10  ? 170.632 98.224  64.707 1.00   21.94 ? 9    LYS G O   1 
ATOM   6754  C  CB  . LYS G  1 10  ? 173.234 99.969  65.257 1.00   25.21 ? 9    LYS G CB  1 
ATOM   6755  C  CG  . LYS G  1 10  ? 174.705 100.327 65.403 1.00   27.57 ? 9    LYS G CG  1 
ATOM   6756  C  CD  . LYS G  1 10  ? 174.926 101.828 65.179 1.00   30.21 ? 9    LYS G CD  1 
ATOM   6757  C  CE  . LYS G  1 10  ? 176.268 102.326 65.744 1.00   32.07 ? 9    LYS G CE  1 
ATOM   6758  N  NZ  . LYS G  1 10  ? 177.448 101.557 65.250 1.00   32.43 ? 9    LYS G NZ  1 
ATOM   6759  N  N   . GLY G  1 11  ? 171.401 97.834  66.797 1.00   24.48 ? 10   GLY G N   1 
ATOM   6760  C  CA  . GLY G  1 11  ? 170.055 97.662  67.391 1.00   25.68 ? 10   GLY G CA  1 
ATOM   6761  C  C   . GLY G  1 11  ? 169.948 98.151  68.830 1.00   27.04 ? 10   GLY G C   1 
ATOM   6762  O  O   . GLY G  1 11  ? 170.885 98.736  69.363 1.00   27.50 ? 10   GLY G O   1 
ATOM   6763  N  N   . ASP G  1 12  ? 168.812 97.873  69.464 1.00   28.41 ? 11   ASP G N   1 
ATOM   6764  C  CA  . ASP G  1 12  ? 168.594 98.243  70.871 1.00   29.48 ? 11   ASP G CA  1 
ATOM   6765  C  C   . ASP G  1 12  ? 169.315 97.297  71.843 1.00   29.68 ? 11   ASP G C   1 
ATOM   6766  O  O   . ASP G  1 12  ? 169.623 97.676  72.965 1.00   30.67 ? 11   ASP G O   1 
ATOM   6767  C  CB  . ASP G  1 12  ? 167.105 98.223  71.191 1.00   30.88 ? 11   ASP G CB  1 
ATOM   6768  C  CG  . ASP G  1 12  ? 166.330 99.240  70.394 1.00   32.32 ? 11   ASP G CG  1 
ATOM   6769  O  OD1 . ASP G  1 12  ? 166.841 100.365 70.213 1.00   32.08 ? 11   ASP G OD1 1 
ATOM   6770  O  OD2 . ASP G  1 12  ? 165.215 98.896  69.932 1.00   35.34 ? 11   ASP G OD2 1 
ATOM   6771  N  N   . GLY G  1 13  ? 169.581 96.069  71.405 1.00   27.98 ? 12   GLY G N   1 
ATOM   6772  C  CA  . GLY G  1 13  ? 170.278 95.098  72.228 1.00   26.30 ? 12   GLY G CA  1 
ATOM   6773  C  C   . GLY G  1 13  ? 171.728 94.975  71.818 1.00   25.02 ? 12   GLY G C   1 
ATOM   6774  O  O   . GLY G  1 13  ? 172.336 95.952  71.368 1.00   23.98 ? 12   GLY G O   1 
ATOM   6775  N  N   . PRO G  1 14  ? 172.289 93.761  71.943 1.00   23.57 ? 13   PRO G N   1 
ATOM   6776  C  CA  . PRO G  1 14  ? 173.724 93.638  71.802 1.00   23.00 ? 13   PRO G CA  1 
ATOM   6777  C  C   . PRO G  1 14  ? 174.194 93.331  70.389 1.00   22.03 ? 13   PRO G C   1 
ATOM   6778  O  O   . PRO G  1 14  ? 175.389 93.201  70.173 1.00   22.08 ? 13   PRO G O   1 
ATOM   6779  C  CB  . PRO G  1 14  ? 174.049 92.475  72.744 1.00   23.53 ? 13   PRO G CB  1 
ATOM   6780  C  CG  . PRO G  1 14  ? 172.841 91.594  72.682 1.00   23.47 ? 13   PRO G CG  1 
ATOM   6781  C  CD  . PRO G  1 14  ? 171.670 92.500  72.381 1.00   23.62 ? 13   PRO G CD  1 
ATOM   6782  N  N   . VAL G  1 15  ? 173.285 93.236  69.414 1.00   21.61 ? 14   VAL G N   1 
ATOM   6783  C  CA  . VAL G  1 15  ? 173.671 92.812  68.080 1.00   20.41 ? 14   VAL G CA  1 
ATOM   6784  C  C   . VAL G  1 15  ? 174.249 93.973  67.327 1.00   20.42 ? 14   VAL G C   1 
ATOM   6785  O  O   . VAL G  1 15  ? 173.623 94.998  67.211 1.00   20.26 ? 14   VAL G O   1 
ATOM   6786  C  CB  . VAL G  1 15  ? 172.488 92.255  67.254 1.00   20.24 ? 14   VAL G CB  1 
ATOM   6787  C  CG1 . VAL G  1 15  ? 172.953 91.902  65.837 1.00   19.20 ? 14   VAL G CG1 1 
ATOM   6788  C  CG2 . VAL G  1 15  ? 171.841 91.049  67.938 1.00   20.00 ? 14   VAL G CG2 1 
ATOM   6789  N  N   . GLN G  1 16  ? 175.450 93.809  66.793 1.00   20.68 ? 15   GLN G N   1 
ATOM   6790  C  CA  . GLN G  1 16  ? 176.033 94.845  65.985 1.00   21.39 ? 15   GLN G CA  1 
ATOM   6791  C  C   . GLN G  1 16  ? 177.105 94.268  65.072 1.00   20.35 ? 15   GLN G C   1 
ATOM   6792  O  O   . GLN G  1 16  ? 177.714 93.231  65.361 1.00   19.77 ? 15   GLN G O   1 
ATOM   6793  C  CB  . GLN G  1 16  ? 176.594 95.980  66.859 1.00   23.62 ? 15   GLN G CB  1 
ATOM   6794  C  CG  . GLN G  1 16  ? 177.829 95.617  67.642 1.00   25.83 ? 15   GLN G CG  1 
ATOM   6795  C  CD  . GLN G  1 16  ? 178.195 96.655  68.709 1.00   28.54 ? 15   GLN G CD  1 
ATOM   6796  O  OE1 . GLN G  1 16  ? 179.272 97.252  68.673 1.00   31.15 ? 15   GLN G OE1 1 
ATOM   6797  N  NE2 . GLN G  1 16  ? 177.300 96.864  69.661 1.00   30.52 ? 15   GLN G NE2 1 
ATOM   6798  N  N   . GLY G  1 17  ? 177.274 94.908  63.931 1.00   19.20 ? 16   GLY G N   1 
ATOM   6799  C  CA  . GLY G  1 17  ? 178.317 94.493  63.006 1.00   18.67 ? 16   GLY G CA  1 
ATOM   6800  C  C   . GLY G  1 17  ? 178.460 95.342  61.770 1.00   17.70 ? 16   GLY G C   1 
ATOM   6801  O  O   . GLY G  1 17  ? 177.785 96.344  61.602 1.00   17.34 ? 16   GLY G O   1 
ATOM   6802  N  N   . ILE G  1 18  ? 179.356 94.901  60.904 1.00   17.21 ? 17   ILE G N   1 
ATOM   6803  C  CA  . ILE G  1 18  ? 179.651 95.578  59.670 1.00   16.87 ? 17   ILE G CA  1 
ATOM   6804  C  C   . ILE G  1 18  ? 179.615 94.567  58.537 1.00   16.51 ? 17   ILE G C   1 
ATOM   6805  O  O   . ILE G  1 18  ? 180.267 93.526  58.617 1.00   16.57 ? 17   ILE G O   1 
ATOM   6806  C  CB  . ILE G  1 18  ? 181.016 96.266  59.732 1.00   17.19 ? 17   ILE G CB  1 
ATOM   6807  C  CG1 . ILE G  1 18  ? 180.999 97.410  60.773 1.00   17.41 ? 17   ILE G CG1 1 
ATOM   6808  C  CG2 . ILE G  1 18  ? 181.405 96.842  58.363 1.00   16.99 ? 17   ILE G CG2 1 
ATOM   6809  C  CD1 . ILE G  1 18  ? 182.392 98.005  61.015 1.00   17.86 ? 17   ILE G CD1 1 
ATOM   6810  N  N   . ILE G  1 19  ? 178.843 94.887  57.491 1.00   15.98 ? 18   ILE G N   1 
ATOM   6811  C  CA  . ILE G  1 19  ? 178.667 94.027  56.349 1.00   15.79 ? 18   ILE G CA  1 
ATOM   6812  C  C   . ILE G  1 19  ? 179.089 94.750  55.045 1.00   16.17 ? 18   ILE G C   1 
ATOM   6813  O  O   . ILE G  1 19  ? 178.612 95.844  54.751 1.00   15.85 ? 18   ILE G O   1 
ATOM   6814  C  CB  . ILE G  1 19  ? 177.204 93.547  56.248 1.00   15.27 ? 18   ILE G CB  1 
ATOM   6815  C  CG1 . ILE G  1 19  ? 176.848 92.623  57.433 1.00   15.10 ? 18   ILE G CG1 1 
ATOM   6816  C  CG2 . ILE G  1 19  ? 176.982 92.839  54.908 1.00   15.12 ? 18   ILE G CG2 1 
ATOM   6817  C  CD1 . ILE G  1 19  ? 177.663 91.332  57.467 1.00   14.97 ? 18   ILE G CD1 1 
ATOM   6818  N  N   . ASN G  1 20  ? 179.971 94.099  54.283 1.00   16.72 ? 19   ASN G N   1 
ATOM   6819  C  CA  . ASN G  1 20  ? 180.514 94.625  53.044 1.00   17.26 ? 19   ASN G CA  1 
ATOM   6820  C  C   . ASN G  1 20  ? 179.830 93.974  51.843 1.00   17.24 ? 19   ASN G C   1 
ATOM   6821  O  O   . ASN G  1 20  ? 179.436 92.814  51.892 1.00   16.99 ? 19   ASN G O   1 
ATOM   6822  C  CB  . ASN G  1 20  ? 182.029 94.383  52.982 1.00   17.93 ? 19   ASN G CB  1 
ATOM   6823  C  CG  . ASN G  1 20  ? 182.783 94.898  54.216 1.00   18.58 ? 19   ASN G CG  1 
ATOM   6824  O  OD1 . ASN G  1 20  ? 183.252 94.113  55.068 1.00   19.21 ? 19   ASN G OD1 1 
ATOM   6825  N  ND2 . ASN G  1 20  ? 182.905 96.210  54.322 1.00   19.19 ? 19   ASN G ND2 1 
ATOM   6826  N  N   . PHE G  1 21  ? 179.664 94.742  50.777 1.00   17.69 ? 20   PHE G N   1 
ATOM   6827  C  CA  . PHE G  1 21  ? 179.181 94.244  49.494 1.00   18.13 ? 20   PHE G CA  1 
ATOM   6828  C  C   . PHE G  1 21  ? 180.126 94.674  48.400 1.00   19.14 ? 20   PHE G C   1 
ATOM   6829  O  O   . PHE G  1 21  ? 180.566 95.840  48.364 1.00   19.07 ? 20   PHE G O   1 
ATOM   6830  C  CB  . PHE G  1 21  ? 177.846 94.846  49.100 1.00   17.70 ? 20   PHE G CB  1 
ATOM   6831  C  CG  . PHE G  1 21  ? 176.770 94.656  50.097 1.00   17.30 ? 20   PHE G CG  1 
ATOM   6832  C  CD1 . PHE G  1 21  ? 176.663 95.505  51.180 1.00   17.11 ? 20   PHE G CD1 1 
ATOM   6833  C  CD2 . PHE G  1 21  ? 175.832 93.670  49.929 1.00   16.88 ? 20   PHE G CD2 1 
ATOM   6834  C  CE1 . PHE G  1 21  ? 175.643 95.360  52.085 1.00   16.89 ? 20   PHE G CE1 1 
ATOM   6835  C  CE2 . PHE G  1 21  ? 174.814 93.521  50.838 1.00   16.81 ? 20   PHE G CE2 1 
ATOM   6836  C  CZ  . PHE G  1 21  ? 174.720 94.365  51.927 1.00   16.60 ? 20   PHE G CZ  1 
ATOM   6837  N  N   . GLU G  1 22  ? 180.371 93.755  47.482 1.00   20.17 ? 21   GLU G N   1 
ATOM   6838  C  CA  . GLU G  1 22  ? 181.180 94.026  46.315 1.00   22.12 ? 21   GLU G CA  1 
ATOM   6839  C  C   . GLU G  1 22  ? 180.621 93.342  45.084 1.00   22.44 ? 21   GLU G C   1 
ATOM   6840  O  O   . GLU G  1 22  ? 180.277 92.164  45.112 1.00   21.22 ? 21   GLU G O   1 
ATOM   6841  C  CB  . GLU G  1 22  ? 182.618 93.575  46.526 1.00   23.69 ? 21   GLU G CB  1 
ATOM   6842  C  CG  . GLU G  1 22  ? 183.536 93.987  45.390 1.00   25.96 ? 21   GLU G CG  1 
ATOM   6843  C  CD  . GLU G  1 22  ? 184.958 93.562  45.643 1.00   28.10 ? 21   GLU G CD  1 
ATOM   6844  O  OE1 . GLU G  1 22  ? 185.158 92.419  46.091 1.00   30.47 ? 21   GLU G OE1 1 
ATOM   6845  O  OE2 . GLU G  1 22  ? 185.868 94.371  45.399 1.00   31.40 ? 21   GLU G OE2 1 
ATOM   6846  N  N   . GLN G  1 23  ? 180.557 94.109  43.998 1.00   23.63 ? 22   GLN G N   1 
ATOM   6847  C  CA  . GLN G  1 23  ? 180.068 93.631  42.716 1.00   24.95 ? 22   GLN G CA  1 
ATOM   6848  C  C   . GLN G  1 23  ? 181.058 94.154  41.663 1.00   28.49 ? 22   GLN G C   1 
ATOM   6849  O  O   . GLN G  1 23  ? 181.020 95.328  41.277 1.00   28.96 ? 22   GLN G O   1 
ATOM   6850  C  CB  . GLN G  1 23  ? 178.654 94.164  42.471 1.00   23.72 ? 22   GLN G CB  1 
ATOM   6851  C  CG  . GLN G  1 23  ? 177.965 93.597  41.228 1.00   22.99 ? 22   GLN G CG  1 
ATOM   6852  C  CD  . GLN G  1 23  ? 176.573 94.138  41.024 1.00   22.05 ? 22   GLN G CD  1 
ATOM   6853  O  OE1 . GLN G  1 23  ? 176.277 95.283  41.373 1.00   21.42 ? 22   GLN G OE1 1 
ATOM   6854  N  NE2 . GLN G  1 23  ? 175.693 93.304  40.498 1.00   21.18 ? 22   GLN G NE2 1 
ATOM   6855  N  N   . LYS G  1 24  ? 181.955 93.280  41.225 1.00   32.55 ? 23   LYS G N   1 
ATOM   6856  C  CA  . LYS G  1 24  ? 183.005 93.651  40.276 1.00   36.92 ? 23   LYS G CA  1 
ATOM   6857  C  C   . LYS G  1 24  ? 182.446 93.992  38.903 1.00   38.71 ? 23   LYS G C   1 
ATOM   6858  O  O   . LYS G  1 24  ? 182.941 94.882  38.235 1.00   40.38 ? 23   LYS G O   1 
ATOM   6859  C  CB  . LYS G  1 24  ? 184.028 92.519  40.162 1.00   40.20 ? 23   LYS G CB  1 
ATOM   6860  C  CG  . LYS G  1 24  ? 184.962 92.429  41.378 1.00   43.77 ? 23   LYS G CG  1 
ATOM   6861  C  CD  . LYS G  1 24  ? 185.659 91.074  41.459 1.00   46.19 ? 23   LYS G CD  1 
ATOM   6862  C  CE  . LYS G  1 24  ? 186.500 90.911  42.728 1.00   49.10 ? 23   LYS G CE  1 
ATOM   6863  N  NZ  . LYS G  1 24  ? 187.954 91.217  42.525 1.00   50.76 ? 23   LYS G NZ  1 
ATOM   6864  N  N   . GLU G  1 25  ? 181.395 93.292  38.503 1.00   40.12 ? 24   GLU G N   1 
ATOM   6865  C  CA  . GLU G  1 25  ? 180.830 93.417  37.167 1.00   42.49 ? 24   GLU G CA  1 
ATOM   6866  C  C   . GLU G  1 25  ? 179.366 93.802  37.269 1.00   40.97 ? 24   GLU G C   1 
ATOM   6867  O  O   . GLU G  1 25  ? 178.636 93.321  38.138 1.00   36.69 ? 24   GLU G O   1 
ATOM   6868  C  CB  . GLU G  1 25  ? 180.974 92.087  36.427 1.00   44.99 ? 24   GLU G CB  1 
ATOM   6869  C  CG  . GLU G  1 25  ? 182.429 91.649  36.249 1.00   48.91 ? 24   GLU G CG  1 
ATOM   6870  C  CD  . GLU G  1 25  ? 182.683 90.180  36.597 1.00   54.09 ? 24   GLU G CD  1 
ATOM   6871  O  OE1 . GLU G  1 25  ? 181.705 89.392  36.722 1.00   55.91 ? 24   GLU G OE1 1 
ATOM   6872  O  OE2 . GLU G  1 25  ? 183.878 89.805  36.751 1.00   57.38 ? 24   GLU G OE2 1 
ATOM   6873  N  N   . SER G  1 26  ? 178.952 94.671  36.364 1.00   40.83 ? 25   SER G N   1 
ATOM   6874  C  CA  . SER G  1 26  ? 177.598 95.211  36.342 1.00   42.66 ? 25   SER G CA  1 
ATOM   6875  C  C   . SER G  1 26  ? 176.492 94.152  36.424 1.00   41.77 ? 25   SER G C   1 
ATOM   6876  O  O   . SER G  1 26  ? 175.475 94.356  37.082 1.00   42.05 ? 25   SER G O   1 
ATOM   6877  C  CB  . SER G  1 26  ? 177.404 96.075  35.078 1.00   43.69 ? 25   SER G CB  1 
ATOM   6878  O  OG  . SER G  1 26  ? 176.033 96.162  34.728 1.00   43.21 ? 25   SER G OG  1 
ATOM   6879  N  N   . ASN G  1 27  ? 176.653 93.029  35.753 1.00   41.40 ? 26   ASN G N   1 
ATOM   6880  C  CA  . ASN G  1 27  ? 175.601 92.028  35.839 1.00   45.08 ? 26   ASN G CA  1 
ATOM   6881  C  C   . ASN G  1 27  ? 176.137 90.736  36.395 1.00   42.69 ? 26   ASN G C   1 
ATOM   6882  O  O   . ASN G  1 27  ? 175.959 89.642  35.820 1.00   44.11 ? 26   ASN G O   1 
ATOM   6883  C  CB  . ASN G  1 27  ? 174.904 91.851  34.499 1.00   48.45 ? 26   ASN G CB  1 
ATOM   6884  C  CG  . ASN G  1 27  ? 173.692 92.759  34.375 1.00   52.95 ? 26   ASN G CG  1 
ATOM   6885  O  OD1 . ASN G  1 27  ? 173.785 93.993  34.557 1.00   52.92 ? 26   ASN G OD1 1 
ATOM   6886  N  ND2 . ASN G  1 27  ? 172.537 92.152  34.077 1.00   52.40 ? 26   ASN G ND2 1 
ATOM   6887  N  N   . GLY G  1 28  ? 176.801 90.903  37.534 1.00   36.81 ? 27   GLY G N   1 
ATOM   6888  C  CA  . GLY G  1 28  ? 177.521 89.826  38.172 1.00   33.15 ? 27   GLY G CA  1 
ATOM   6889  C  C   . GLY G  1 28  ? 177.052 89.632  39.593 1.00   28.32 ? 27   GLY G C   1 
ATOM   6890  O  O   . GLY G  1 28  ? 176.248 90.412  40.110 1.00   27.03 ? 27   GLY G O   1 
ATOM   6891  N  N   . PRO G  1 29  ? 177.543 88.573  40.231 1.00   25.78 ? 28   PRO G N   1 
ATOM   6892  C  CA  . PRO G  1 29  ? 177.165 88.286  41.598 1.00   23.95 ? 28   PRO G CA  1 
ATOM   6893  C  C   . PRO G  1 29  ? 177.691 89.371  42.533 1.00   22.15 ? 28   PRO G C   1 
ATOM   6894  O  O   . PRO G  1 29  ? 178.701 90.017  42.234 1.00   21.69 ? 28   PRO G O   1 
ATOM   6895  C  CB  . PRO G  1 29  ? 177.866 86.956  41.889 1.00   25.06 ? 28   PRO G CB  1 
ATOM   6896  C  CG  . PRO G  1 29  ? 178.351 86.448  40.574 1.00   25.91 ? 28   PRO G CG  1 
ATOM   6897  C  CD  . PRO G  1 29  ? 178.565 87.647  39.732 1.00   26.34 ? 28   PRO G CD  1 
ATOM   6898  N  N   . VAL G  1 30  ? 176.992 89.565  43.643 1.00   20.09 ? 29   VAL G N   1 
ATOM   6899  C  CA  . VAL G  1 30  ? 177.424 90.447  44.708 1.00   18.94 ? 29   VAL G CA  1 
ATOM   6900  C  C   . VAL G  1 30  ? 177.941 89.556  45.831 1.00   18.39 ? 29   VAL G C   1 
ATOM   6901  O  O   . VAL G  1 30  ? 177.266 88.620  46.252 1.00   17.94 ? 29   VAL G O   1 
ATOM   6902  C  CB  . VAL G  1 30  ? 176.260 91.309  45.221 1.00   18.40 ? 29   VAL G CB  1 
ATOM   6903  C  CG1 . VAL G  1 30  ? 176.694 92.185  46.393 1.00   18.00 ? 29   VAL G CG1 1 
ATOM   6904  C  CG2 . VAL G  1 30  ? 175.660 92.127  44.074 1.00   18.41 ? 29   VAL G CG2 1 
ATOM   6905  N  N   . LYS G  1 31  ? 179.161 89.834  46.267 1.00   18.12 ? 30   LYS G N   1 
ATOM   6906  C  CA  . LYS G  1 31  ? 179.761 89.193  47.410 1.00   18.01 ? 30   LYS G CA  1 
ATOM   6907  C  C   . LYS G  1 31  ? 179.385 89.991  48.644 1.00   17.18 ? 30   LYS G C   1 
ATOM   6908  O  O   . LYS G  1 31  ? 179.420 91.227  48.626 1.00   17.19 ? 30   LYS G O   1 
ATOM   6909  C  CB  . LYS G  1 31  ? 181.278 89.138  47.238 1.00   18.75 ? 30   LYS G CB  1 
ATOM   6910  C  CG  . LYS G  1 31  ? 181.701 88.113  46.191 1.00   19.56 ? 30   LYS G CG  1 
ATOM   6911  C  CD  . LYS G  1 31  ? 183.217 87.893  46.139 0.50   20.01 ? 30   LYS G CD  1 
ATOM   6912  C  CE  . LYS G  1 31  ? 183.559 86.666  45.295 0.50   20.42 ? 30   LYS G CE  1 
ATOM   6913  N  NZ  . LYS G  1 31  ? 184.976 86.219  45.469 0.50   20.94 ? 30   LYS G NZ  1 
ATOM   6914  N  N   . VAL G  1 32  ? 178.994 89.281  49.697 1.00   16.56 ? 31   VAL G N   1 
ATOM   6915  C  CA  . VAL G  1 32  ? 178.480 89.880  50.928 1.00   16.10 ? 31   VAL G CA  1 
ATOM   6916  C  C   . VAL G  1 32  ? 179.252 89.237  52.056 1.00   16.28 ? 31   VAL G C   1 
ATOM   6917  O  O   . VAL G  1 32  ? 179.243 88.008  52.179 1.00   16.48 ? 31   VAL G O   1 
ATOM   6918  C  CB  . VAL G  1 32  ? 176.970 89.600  51.090 1.00   15.58 ? 31   VAL G CB  1 
ATOM   6919  C  CG1 . VAL G  1 32  ? 176.398 90.267  52.335 1.00   15.08 ? 31   VAL G CG1 1 
ATOM   6920  C  CG2 . VAL G  1 32  ? 176.212 90.018  49.834 1.00   15.47 ? 31   VAL G CG2 1 
ATOM   6921  N  N   . TRP G  1 33  ? 179.921 90.032  52.881 1.00   16.41 ? 32   TRP G N   1 
ATOM   6922  C  CA  . TRP G  1 33  ? 180.730 89.467  53.971 1.00   16.79 ? 32   TRP G CA  1 
ATOM   6923  C  C   . TRP G  1 33  ? 180.993 90.452  55.079 1.00   16.84 ? 32   TRP G C   1 
ATOM   6924  O  O   . TRP G  1 33  ? 180.874 91.671  54.909 1.00   16.76 ? 32   TRP G O   1 
ATOM   6925  C  CB  . TRP G  1 33  ? 182.048 88.917  53.421 1.00   17.38 ? 32   TRP G CB  1 
ATOM   6926  C  CG  . TRP G  1 33  ? 183.090 89.981  53.166 1.00   18.03 ? 32   TRP G CG  1 
ATOM   6927  C  CD1 . TRP G  1 33  ? 184.168 90.331  53.997 1.00   18.41 ? 32   TRP G CD1 1 
ATOM   6928  C  CD2 . TRP G  1 33  ? 183.177 90.891  52.031 1.00   18.33 ? 32   TRP G CD2 1 
ATOM   6929  N  NE1 . TRP G  1 33  ? 184.886 91.358  53.462 1.00   18.90 ? 32   TRP G NE1 1 
ATOM   6930  C  CE2 . TRP G  1 33  ? 184.357 91.732  52.268 1.00   18.94 ? 32   TRP G CE2 1 
ATOM   6931  C  CE3 . TRP G  1 33  ? 182.433 91.091  50.890 1.00   18.58 ? 32   TRP G CE3 1 
ATOM   6932  C  CZ2 . TRP G  1 33  ? 184.746 92.728  51.381 1.00   19.28 ? 32   TRP G CZ2 1 
ATOM   6933  C  CZ3 . TRP G  1 33  ? 182.850 92.086  49.989 1.00   18.94 ? 32   TRP G CZ3 1 
ATOM   6934  C  CH2 . TRP G  1 33  ? 183.978 92.892  50.245 1.00   19.17 ? 32   TRP G CH2 1 
ATOM   6935  N  N   . GLY G  1 34  ? 181.387 89.936  56.228 1.00   17.27 ? 33   GLY G N   1 
ATOM   6936  C  CA  . GLY G  1 34  ? 181.659 90.780  57.400 1.00   17.65 ? 33   GLY G CA  1 
ATOM   6937  C  C   . GLY G  1 34  ? 181.298 90.017  58.650 1.00   18.26 ? 33   GLY G C   1 
ATOM   6938  O  O   . GLY G  1 34  ? 181.066 88.813  58.609 1.00   18.60 ? 33   GLY G O   1 
ATOM   6939  N  N   . SER G  1 35  ? 181.220 90.725  59.761 1.00   18.88 ? 34   SER G N   1 
ATOM   6940  C  CA  . SER G  1 35  ? 181.079 90.126  61.055 1.00   19.15 ? 34   SER G CA  1 
ATOM   6941  C  C   . SER G  1 35  ? 179.954 90.807  61.819 1.00   18.53 ? 34   SER G C   1 
ATOM   6942  O  O   . SER G  1 35  ? 179.870 92.040  61.799 1.00   18.36 ? 34   SER G O   1 
ATOM   6943  C  CB  . SER G  1 35  ? 182.377 90.325  61.817 1.00   20.37 ? 34   SER G CB  1 
ATOM   6944  O  OG  . SER G  1 35  ? 182.444 89.338  62.809 1.00   22.66 ? 34   SER G OG  1 
ATOM   6945  N  N   . ILE G  1 36  ? 179.080 90.010  62.444 1.00   17.79 ? 35   ILE G N   1 
ATOM   6946  C  CA  . ILE G  1 36  ? 178.016 90.503  63.315 1.00   17.46 ? 35   ILE G CA  1 
ATOM   6947  C  C   . ILE G  1 36  ? 178.202 89.800  64.652 1.00   17.52 ? 35   ILE G C   1 
ATOM   6948  O  O   . ILE G  1 36  ? 178.346 88.569  64.684 1.00   17.72 ? 35   ILE G O   1 
ATOM   6949  C  CB  . ILE G  1 36  ? 176.610 90.186  62.762 1.00   17.17 ? 35   ILE G CB  1 
ATOM   6950  C  CG1 . ILE G  1 36  ? 176.469 90.584  61.289 1.00   17.12 ? 35   ILE G CG1 1 
ATOM   6951  C  CG2 . ILE G  1 36  ? 175.522 90.881  63.588 1.00   17.01 ? 35   ILE G CG2 1 
ATOM   6952  C  CD1 . ILE G  1 36  ? 175.209 90.057  60.603 1.00   16.82 ? 35   ILE G CD1 1 
ATOM   6953  N  N   . LYS G  1 37  ? 178.232 90.548  65.755 1.00   17.43 ? 36   LYS G N   1 
ATOM   6954  C  CA  . LYS G  1 37  ? 178.400 89.934  67.080 1.00   17.60 ? 36   LYS G CA  1 
ATOM   6955  C  C   . LYS G  1 37  ? 177.114 90.065  67.885 1.00   17.35 ? 36   LYS G C   1 
ATOM   6956  O  O   . LYS G  1 37  ? 176.208 90.836  67.541 1.00   17.08 ? 36   LYS G O   1 
ATOM   6957  C  CB  . LYS G  1 37  ? 179.606 90.534  67.826 1.00   18.24 ? 36   LYS G CB  1 
ATOM   6958  C  CG  . LYS G  1 37  ? 179.358 91.910  68.450 1.00   18.69 ? 36   LYS G CG  1 
ATOM   6959  C  CD  . LYS G  1 37  ? 180.656 92.476  69.026 0.50   19.29 ? 36   LYS G CD  1 
ATOM   6960  C  CE  . LYS G  1 37  ? 180.387 93.634  69.975 0.50   19.75 ? 36   LYS G CE  1 
ATOM   6961  N  NZ  . LYS G  1 37  ? 181.637 94.141  70.628 0.50   20.66 ? 36   LYS G NZ  1 
ATOM   6962  N  N   . GLY G  1 38  ? 177.007 89.287  68.945 1.00   17.27 ? 37   GLY G N   1 
ATOM   6963  C  CA  . GLY G  1 38  ? 175.857 89.417  69.857 1.00   17.26 ? 37   GLY G CA  1 
ATOM   6964  C  C   . GLY G  1 38  ? 174.643 88.594  69.521 1.00   16.81 ? 37   GLY G C   1 
ATOM   6965  O  O   . GLY G  1 38  ? 173.578 88.867  70.023 1.00   16.97 ? 37   GLY G O   1 
ATOM   6966  N  N   . LEU G  1 39  ? 174.798 87.595  68.649 1.00   16.75 ? 38   LEU G N   1 
ATOM   6967  C  CA  . LEU G  1 39  ? 173.668 86.796  68.121 1.00   16.39 ? 38   LEU G CA  1 
ATOM   6968  C  C   . LEU G  1 39  ? 173.617 85.438  68.804 1.00   16.54 ? 38   LEU G C   1 
ATOM   6969  O  O   . LEU G  1 39  ? 174.649 84.884  69.100 1.00   16.41 ? 38   LEU G O   1 
ATOM   6970  C  CB  . LEU G  1 39  ? 173.840 86.554  66.622 1.00   16.08 ? 38   LEU G CB  1 
ATOM   6971  C  CG  . LEU G  1 39  ? 173.611 87.750  65.696 1.00   15.83 ? 38   LEU G CG  1 
ATOM   6972  C  CD1 . LEU G  1 39  ? 174.287 87.439  64.372 1.00   15.40 ? 38   LEU G CD1 1 
ATOM   6973  C  CD2 . LEU G  1 39  ? 172.121 88.043  65.543 1.00   15.47 ? 38   LEU G CD2 1 
ATOM   6974  N  N   . THR G  1 40  ? 172.423 84.903  69.030 1.00   16.80 ? 39   THR G N   1 
ATOM   6975  C  CA  . THR G  1 40  ? 172.323 83.581  69.605 1.00   17.32 ? 39   THR G CA  1 
ATOM   6976  C  C   . THR G  1 40  ? 172.901 82.583  68.616 1.00   17.23 ? 39   THR G C   1 
ATOM   6977  O  O   . THR G  1 40  ? 172.743 82.741  67.387 1.00   16.73 ? 39   THR G O   1 
ATOM   6978  C  CB  . THR G  1 40  ? 170.875 83.187  69.981 1.00   17.63 ? 39   THR G CB  1 
ATOM   6979  O  OG1 . THR G  1 40  ? 170.028 83.264  68.824 1.00   17.86 ? 39   THR G OG1 1 
ATOM   6980  C  CG2 . THR G  1 40  ? 170.331 84.104  71.071 1.00   17.81 ? 39   THR G CG2 1 
ATOM   6981  N  N   . GLU G  1 41  ? 173.589 81.574  69.155 1.00   17.64 ? 40   GLU G N   1 
ATOM   6982  C  CA  . GLU G  1 41  ? 174.179 80.525  68.336 1.00   17.86 ? 40   GLU G CA  1 
ATOM   6983  C  C   . GLU G  1 41  ? 173.130 79.959  67.382 1.00   17.09 ? 40   GLU G C   1 
ATOM   6984  O  O   . GLU G  1 41  ? 171.994 79.723  67.750 1.00   17.04 ? 40   GLU G O   1 
ATOM   6985  C  CB  . GLU G  1 41  ? 174.779 79.409  69.211 1.00   18.96 ? 40   GLU G CB  1 
ATOM   6986  C  CG  . GLU G  1 41  ? 175.542 78.367  68.407 1.00   19.75 ? 40   GLU G CG  1 
ATOM   6987  C  CD  . GLU G  1 41  ? 176.208 77.287  69.275 1.00   20.89 ? 40   GLU G CD  1 
ATOM   6988  O  OE1 . GLU G  1 41  ? 175.939 77.264  70.472 1.00   21.56 ? 40   GLU G OE1 1 
ATOM   6989  O  OE2 . GLU G  1 41  ? 176.986 76.459  68.735 1.00   21.61 ? 40   GLU G OE2 1 
ATOM   6990  N  N   . GLY G  1 42  ? 173.521 79.770  66.140 1.00   16.56 ? 41   GLY G N   1 
ATOM   6991  C  CA  . GLY G  1 42  ? 172.633 79.183  65.150 1.00   16.13 ? 41   GLY G CA  1 
ATOM   6992  C  C   . GLY G  1 42  ? 172.154 80.178  64.118 1.00   15.57 ? 41   GLY G C   1 
ATOM   6993  O  O   . GLY G  1 42  ? 172.779 81.207  63.886 1.00   15.60 ? 41   GLY G O   1 
ATOM   6994  N  N   . LEU G  1 43  ? 171.018 79.866  63.519 1.00   15.33 ? 42   LEU G N   1 
ATOM   6995  C  CA  . LEU G  1 43  ? 170.563 80.504  62.281 1.00   14.93 ? 42   LEU G CA  1 
ATOM   6996  C  C   . LEU G  1 43  ? 169.787 81.778  62.537 1.00   14.72 ? 42   LEU G C   1 
ATOM   6997  O  O   . LEU G  1 43  ? 168.904 81.783  63.380 1.00   15.08 ? 42   LEU G O   1 
ATOM   6998  C  CB  . LEU G  1 43  ? 169.637 79.537  61.532 1.00   14.86 ? 42   LEU G CB  1 
ATOM   6999  C  CG  . LEU G  1 43  ? 170.256 78.267  60.921 1.00   14.91 ? 42   LEU G CG  1 
ATOM   7000  C  CD1 . LEU G  1 43  ? 169.139 77.281  60.529 1.00   14.87 ? 42   LEU G CD1 1 
ATOM   7001  C  CD2 . LEU G  1 43  ? 171.149 78.598  59.738 1.00   14.65 ? 42   LEU G CD2 1 
ATOM   7002  N  N   . HIS G  1 44  ? 170.083 82.831  61.770 1.00   14.40 ? 43   HIS G N   1 
ATOM   7003  C  CA  . HIS G  1 44  ? 169.351 84.106  61.804 1.00   14.11 ? 43   HIS G CA  1 
ATOM   7004  C  C   . HIS G  1 44  ? 169.008 84.604  60.429 1.00   13.63 ? 43   HIS G C   1 
ATOM   7005  O  O   . HIS G  1 44  ? 169.903 84.747  59.565 1.00   13.27 ? 43   HIS G O   1 
ATOM   7006  C  CB  . HIS G  1 44  ? 170.201 85.162  62.507 1.00   14.33 ? 43   HIS G CB  1 
ATOM   7007  C  CG  . HIS G  1 44  ? 170.416 84.843  63.944 1.00   14.87 ? 43   HIS G CG  1 
ATOM   7008  N  ND1 . HIS G  1 44  ? 169.566 85.243  64.898 1.00   15.08 ? 43   HIS G ND1 1 
ATOM   7009  C  CD2 . HIS G  1 44  ? 171.354 84.027  64.561 1.00   15.09 ? 43   HIS G CD2 1 
ATOM   7010  C  CE1 . HIS G  1 44  ? 169.961 84.739  66.080 1.00   15.56 ? 43   HIS G CE1 1 
ATOM   7011  N  NE2 . HIS G  1 44  ? 171.060 84.002  65.876 1.00   15.50 ? 43   HIS G NE2 1 
ATOM   7012  N  N   . GLY G  1 45  ? 167.732 84.914  60.224 1.00   13.39 ? 44   GLY G N   1 
ATOM   7013  C  CA  . GLY G  1 45  ? 167.262 85.522  58.962 1.00   13.24 ? 44   GLY G CA  1 
ATOM   7014  C  C   . GLY G  1 45  ? 168.039 86.800  58.632 1.00   13.01 ? 44   GLY G C   1 
ATOM   7015  O  O   . GLY G  1 45  ? 168.367 87.584  59.533 1.00   13.16 ? 44   GLY G O   1 
ATOM   7016  N  N   . PHE G  1 46  ? 168.283 87.027  57.357 1.00   12.82 ? 45   PHE G N   1 
ATOM   7017  C  CA  . PHE G  1 46  ? 169.199 88.060  56.885 1.00   12.85 ? 45   PHE G CA  1 
ATOM   7018  C  C   . PHE G  1 46  ? 168.686 88.572  55.557 1.00   12.94 ? 45   PHE G C   1 
ATOM   7019  O  O   . PHE G  1 46  ? 168.705 87.845  54.563 1.00   12.89 ? 45   PHE G O   1 
ATOM   7020  C  CB  . PHE G  1 46  ? 170.587 87.427  56.746 1.00   12.82 ? 45   PHE G CB  1 
ATOM   7021  C  CG  . PHE G  1 46  ? 171.692 88.390  56.468 1.00   12.78 ? 45   PHE G CG  1 
ATOM   7022  C  CD1 . PHE G  1 46  ? 172.107 89.288  57.441 1.00   12.86 ? 45   PHE G CD1 1 
ATOM   7023  C  CD2 . PHE G  1 46  ? 172.378 88.334  55.272 1.00   12.75 ? 45   PHE G CD2 1 
ATOM   7024  C  CE1 . PHE G  1 46  ? 173.179 90.131  57.207 1.00   12.96 ? 45   PHE G CE1 1 
ATOM   7025  C  CE2 . PHE G  1 46  ? 173.436 89.183  55.016 1.00   12.87 ? 45   PHE G CE2 1 
ATOM   7026  C  CZ  . PHE G  1 46  ? 173.842 90.091  55.984 1.00   12.97 ? 45   PHE G CZ  1 
ATOM   7027  N  N   . HIS G  1 47  ? 168.118 89.784  55.547 1.00   13.07 ? 46   HIS G N   1 
ATOM   7028  C  CA  . HIS G  1 47  ? 167.353 90.236  54.386 1.00   13.20 ? 46   HIS G CA  1 
ATOM   7029  C  C   . HIS G  1 47  ? 167.571 91.680  54.114 1.00   13.48 ? 46   HIS G C   1 
ATOM   7030  O  O   . HIS G  1 47  ? 167.853 92.478  55.038 1.00   13.44 ? 46   HIS G O   1 
ATOM   7031  C  CB  . HIS G  1 47  ? 165.851 90.102  54.614 1.00   13.38 ? 46   HIS G CB  1 
ATOM   7032  C  CG  . HIS G  1 47  ? 165.414 88.792  55.213 1.00   13.29 ? 46   HIS G CG  1 
ATOM   7033  N  ND1 . HIS G  1 47  ? 164.712 88.731  56.336 1.00   13.32 ? 46   HIS G ND1 1 
ATOM   7034  C  CD2 . HIS G  1 47  ? 165.603 87.495  54.798 1.00   13.19 ? 46   HIS G CD2 1 
ATOM   7035  C  CE1 . HIS G  1 47  ? 164.461 87.466  56.647 1.00   13.33 ? 46   HIS G CE1 1 
ATOM   7036  N  NE2 . HIS G  1 47  ? 165.007 86.696  55.696 1.00   13.29 ? 46   HIS G NE2 1 
ATOM   7037  N  N   . VAL G  1 48  ? 167.371 92.051  52.859 1.00   13.64 ? 47   VAL G N   1 
ATOM   7038  C  CA  . VAL G  1 48  ? 167.290 93.467  52.501 1.00   13.95 ? 47   VAL G CA  1 
ATOM   7039  C  C   . VAL G  1 48  ? 165.835 93.869  52.527 1.00   14.42 ? 47   VAL G C   1 
ATOM   7040  O  O   . VAL G  1 48  ? 165.008 93.298  51.786 1.00   14.61 ? 47   VAL G O   1 
ATOM   7041  C  CB  . VAL G  1 48  ? 167.851 93.793  51.096 1.00   13.87 ? 47   VAL G CB  1 
ATOM   7042  C  CG1 . VAL G  1 48  ? 167.795 95.304  50.839 1.00   13.98 ? 47   VAL G CG1 1 
ATOM   7043  C  CG2 . VAL G  1 48  ? 169.281 93.317  50.948 1.00   13.78 ? 47   VAL G CG2 1 
ATOM   7044  N  N   . HIS G  1 49  ? 165.523 94.843  53.373 1.00   14.75 ? 48   HIS G N   1 
ATOM   7045  C  CA  . HIS G  1 49  ? 164.174 95.402  53.446 1.00   15.30 ? 48   HIS G CA  1 
ATOM   7046  C  C   . HIS G  1 49  ? 164.025 96.630  52.587 1.00   15.89 ? 48   HIS G C   1 
ATOM   7047  O  O   . HIS G  1 49  ? 165.002 97.267  52.239 1.00   15.50 ? 48   HIS G O   1 
ATOM   7048  C  CB  . HIS G  1 49  ? 163.832 95.720  54.884 1.00   15.24 ? 48   HIS G CB  1 
ATOM   7049  C  CG  . HIS G  1 49  ? 163.554 94.524  55.684 1.00   15.08 ? 48   HIS G CG  1 
ATOM   7050  N  ND1 . HIS G  1 49  ? 162.383 94.341  56.323 1.00   15.31 ? 48   HIS G ND1 1 
ATOM   7051  C  CD2 . HIS G  1 49  ? 164.313 93.384  55.906 1.00   14.79 ? 48   HIS G CD2 1 
ATOM   7052  C  CE1 . HIS G  1 49  ? 162.408 93.152  56.953 1.00   15.13 ? 48   HIS G CE1 1 
ATOM   7053  N  NE2 . HIS G  1 49  ? 163.596 92.581  56.711 1.00   14.92 ? 48   HIS G NE2 1 
ATOM   7054  N  N   . GLU G  1 50  ? 162.781 96.965  52.255 1.00   16.92 ? 49   GLU G N   1 
ATOM   7055  C  CA  . GLU G  1 50  ? 162.515 97.897  51.176 1.00   17.99 ? 49   GLU G CA  1 
ATOM   7056  C  C   . GLU G  1 50  ? 163.018 99.319  51.415 1.00   18.29 ? 49   GLU G C   1 
ATOM   7057  O  O   . GLU G  1 50  ? 163.632 99.914  50.539 1.00   18.75 ? 49   GLU G O   1 
ATOM   7058  C  CB  . GLU G  1 50  ? 161.017 97.923  50.885 1.00   19.20 ? 49   GLU G CB  1 
ATOM   7059  C  CG  . GLU G  1 50  ? 160.703 98.662  49.611 1.00   20.04 ? 49   GLU G CG  1 
ATOM   7060  C  CD  . GLU G  1 50  ? 159.239 98.670  49.258 1.00   21.38 ? 49   GLU G CD  1 
ATOM   7061  O  OE1 . GLU G  1 50  ? 158.425 98.060  49.989 1.00   22.00 ? 49   GLU G OE1 1 
ATOM   7062  O  OE2 . GLU G  1 50  ? 158.925 99.318  48.229 1.00   22.74 ? 49   GLU G OE2 1 
ATOM   7063  N  N   . PHE G  1 51  ? 162.813 99.862  52.603 1.00   18.49 ? 50   PHE G N   1 
ATOM   7064  C  CA  . PHE G  1 51  ? 163.116 101.268 52.819 1.00   18.94 ? 50   PHE G CA  1 
ATOM   7065  C  C   . PHE G  1 51  ? 164.352 101.500 53.684 1.00   18.82 ? 50   PHE G C   1 
ATOM   7066  O  O   . PHE G  1 51  ? 164.579 100.805 54.675 1.00   18.85 ? 50   PHE G O   1 
ATOM   7067  C  CB  . PHE G  1 51  ? 161.884 101.945 53.411 1.00   19.25 ? 50   PHE G CB  1 
ATOM   7068  C  CG  . PHE G  1 51  ? 160.648 101.749 52.578 1.00   19.62 ? 50   PHE G CG  1 
ATOM   7069  C  CD1 . PHE G  1 51  ? 160.591 102.253 51.278 1.00   20.02 ? 50   PHE G CD1 1 
ATOM   7070  C  CD2 . PHE G  1 51  ? 159.561 101.035 53.062 1.00   19.68 ? 50   PHE G CD2 1 
ATOM   7071  C  CE1 . PHE G  1 51  ? 159.473 102.055 50.488 1.00   20.44 ? 50   PHE G CE1 1 
ATOM   7072  C  CE2 . PHE G  1 51  ? 158.434 100.849 52.284 1.00   20.11 ? 50   PHE G CE2 1 
ATOM   7073  C  CZ  . PHE G  1 51  ? 158.379 101.376 50.997 1.00   20.43 ? 50   PHE G CZ  1 
ATOM   7074  N  N   . GLY G  1 52  ? 165.157 102.489 53.298 1.00   19.12 ? 51   GLY G N   1 
ATOM   7075  C  CA  . GLY G  1 52  ? 166.310 102.909 54.086 1.00   19.31 ? 51   GLY G CA  1 
ATOM   7076  C  C   . GLY G  1 52  ? 165.883 103.970 55.100 1.00   20.00 ? 51   GLY G C   1 
ATOM   7077  O  O   . GLY G  1 52  ? 166.457 105.057 55.169 1.00   19.67 ? 51   GLY G O   1 
ATOM   7078  N  N   . ASP G  1 53  ? 164.845 103.640 55.854 1.00   20.66 ? 52   ASP G N   1 
ATOM   7079  C  CA  . ASP G  1 53  ? 164.198 104.546 56.774 1.00   22.13 ? 52   ASP G CA  1 
ATOM   7080  C  C   . ASP G  1 53  ? 164.403 103.992 58.172 1.00   22.91 ? 52   ASP G C   1 
ATOM   7081  O  O   . ASP G  1 53  ? 163.811 102.989 58.546 1.00   22.22 ? 52   ASP G O   1 
ATOM   7082  C  CB  . ASP G  1 53  ? 162.722 104.640 56.462 1.00   22.49 ? 52   ASP G CB  1 
ATOM   7083  C  CG  . ASP G  1 53  ? 161.980 105.589 57.378 1.00   23.42 ? 52   ASP G CG  1 
ATOM   7084  O  OD1 . ASP G  1 53  ? 162.500 105.940 58.473 1.00   23.97 ? 52   ASP G OD1 1 
ATOM   7085  O  OD2 . ASP G  1 53  ? 160.849 105.961 57.010 1.00   24.08 ? 52   ASP G OD2 1 
ATOM   7086  N  N   . ASN G  1 54  ? 165.254 104.664 58.934 1.00   24.81 ? 53   ASN G N   1 
ATOM   7087  C  CA  . ASN G  1 54  ? 165.520 104.254 60.287 1.00   26.39 ? 53   ASN G CA  1 
ATOM   7088  C  C   . ASN G  1 54  ? 164.882 105.187 61.303 1.00   26.75 ? 53   ASN G C   1 
ATOM   7089  O  O   . ASN G  1 54  ? 165.319 105.213 62.459 1.00   26.60 ? 53   ASN G O   1 
ATOM   7090  C  CB  . ASN G  1 54  ? 167.022 104.215 60.531 1.00   28.11 ? 53   ASN G CB  1 
ATOM   7091  C  CG  . ASN G  1 54  ? 167.370 103.433 61.773 1.00   30.45 ? 53   ASN G CG  1 
ATOM   7092  O  OD1 . ASN G  1 54  ? 166.883 102.308 61.962 1.00   33.29 ? 53   ASN G OD1 1 
ATOM   7093  N  ND2 . ASN G  1 54  ? 168.183 104.025 62.648 1.00   31.10 ? 53   ASN G ND2 1 
ATOM   7094  N  N   . THR G  1 55  ? 163.867 105.941 60.878 1.00   26.52 ? 54   THR G N   1 
ATOM   7095  C  CA  . THR G  1 55  ? 163.252 106.954 61.744 1.00   26.63 ? 54   THR G CA  1 
ATOM   7096  C  C   . THR G  1 55  ? 162.604 106.332 62.951 1.00   27.07 ? 54   THR G C   1 
ATOM   7097  O  O   . THR G  1 55  ? 162.581 106.949 63.997 1.00   28.64 ? 54   THR G O   1 
ATOM   7098  C  CB  . THR G  1 55  ? 162.208 107.844 61.024 1.00   26.45 ? 54   THR G CB  1 
ATOM   7099  O  OG1 . THR G  1 55  ? 161.125 107.045 60.541 1.00   26.13 ? 54   THR G OG1 1 
ATOM   7100  C  CG2 . THR G  1 55  ? 162.838 108.620 59.873 1.00   26.12 ? 54   THR G CG2 1 
ATOM   7101  N  N   . ALA G  1 56  ? 162.092 105.110 62.829 1.00   26.85 ? 55   ALA G N   1 
ATOM   7102  C  CA  . ALA G  1 56  ? 161.509 104.412 63.981 1.00   26.53 ? 55   ALA G CA  1 
ATOM   7103  C  C   . ALA G  1 56  ? 162.257 103.114 64.220 1.00   25.85 ? 55   ALA G C   1 
ATOM   7104  O  O   . ALA G  1 56  ? 161.658 102.077 64.393 1.00   28.25 ? 55   ALA G O   1 
ATOM   7105  C  CB  . ALA G  1 56  ? 160.015 104.153 63.743 1.00   26.71 ? 55   ALA G CB  1 
ATOM   7106  N  N   . GLY G  1 57  ? 163.578 103.157 64.217 1.00   25.02 ? 56   GLY G N   1 
ATOM   7107  C  CA  . GLY G  1 57  ? 164.367 101.929 64.293 1.00   24.30 ? 56   GLY G CA  1 
ATOM   7108  C  C   . GLY G  1 57  ? 164.206 101.024 63.068 1.00   23.61 ? 56   GLY G C   1 
ATOM   7109  O  O   . GLY G  1 57  ? 163.953 101.507 61.947 1.00   23.66 ? 56   GLY G O   1 
ATOM   7110  N  N   . CYS G  1 58  ? 164.359 99.713  63.272 1.00   22.12 ? 57   CYS G N   1 
ATOM   7111  C  CA  . CYS G  1 58  ? 164.280 98.755  62.166 1.00   20.93 ? 57   CYS G CA  1 
ATOM   7112  C  C   . CYS G  1 58  ? 162.861 98.593  61.627 1.00   20.88 ? 57   CYS G C   1 
ATOM   7113  O  O   . CYS G  1 58  ? 162.661 98.182  60.467 1.00   20.40 ? 57   CYS G O   1 
ATOM   7114  C  CB  . CYS G  1 58  ? 164.853 97.407  62.582 1.00   20.09 ? 57   CYS G CB  1 
ATOM   7115  S  SG  . CYS G  1 58  ? 166.572 97.519  63.136 1.00   19.86 ? 57   CYS G SG  1 
ATOM   7116  N  N   . THR G  1 59  ? 161.874 98.910  62.459 1.00   21.21 ? 58   THR G N   1 
ATOM   7117  C  CA  . THR G  1 59  ? 160.472 98.786  62.066 1.00   21.84 ? 58   THR G CA  1 
ATOM   7118  C  C   . THR G  1 59  ? 160.104 99.593  60.828 1.00   21.16 ? 58   THR G C   1 
ATOM   7119  O  O   . THR G  1 59  ? 159.242 99.194  60.064 1.00   21.22 ? 58   THR G O   1 
ATOM   7120  C  CB  . THR G  1 59  ? 159.523 99.265  63.173 1.00   23.25 ? 58   THR G CB  1 
ATOM   7121  O  OG1 . THR G  1 59  ? 159.901 98.624  64.399 1.00   24.68 ? 58   THR G OG1 1 
ATOM   7122  C  CG2 . THR G  1 59  ? 158.074 98.901  62.795 1.00   23.19 ? 58   THR G CG2 1 
ATOM   7123  N  N   . SER G  1 60  ? 160.750 100.732 60.638 1.00   20.61 ? 59   SER G N   1 
ATOM   7124  C  CA  . SER G  1 60  ? 160.343 101.620 59.566 1.00   20.53 ? 59   SER G CA  1 
ATOM   7125  C  C   . SER G  1 60  ? 161.029 101.243 58.224 1.00   19.76 ? 59   SER G C   1 
ATOM   7126  O  O   . SER G  1 60  ? 160.772 101.855 57.218 1.00   20.11 ? 59   SER G O   1 
ATOM   7127  C  CB  . SER G  1 60  ? 160.554 103.072 59.982 1.00   20.82 ? 59   SER G CB  1 
ATOM   7128  O  OG  . SER G  1 60  ? 161.869 103.298 60.430 1.00   20.96 ? 59   SER G OG  1 
ATOM   7129  N  N   . ALA G  1 61  ? 161.827 100.182 58.208 1.00   19.04 ? 60   ALA G N   1 
ATOM   7130  C  CA  . ALA G  1 61  ? 162.406 99.665  56.953 1.00   18.59 ? 60   ALA G CA  1 
ATOM   7131  C  C   . ALA G  1 61  ? 161.376 98.976  56.045 1.00   18.32 ? 60   ALA G C   1 
ATOM   7132  O  O   . ALA G  1 61  ? 161.678 98.655  54.903 1.00   18.44 ? 60   ALA G O   1 
ATOM   7133  C  CB  . ALA G  1 61  ? 163.575 98.726  57.246 1.00   17.80 ? 60   ALA G CB  1 
ATOM   7134  N  N   . GLY G  1 62  ? 160.177 98.739  56.547 1.00   18.32 ? 61   GLY G N   1 
ATOM   7135  C  CA  . GLY G  1 62  ? 159.124 98.074  55.785 1.00   18.21 ? 61   GLY G CA  1 
ATOM   7136  C  C   . GLY G  1 62  ? 159.421 96.597  55.565 1.00   17.86 ? 61   GLY G C   1 
ATOM   7137  O  O   . GLY G  1 62  ? 160.253 96.007  56.271 1.00   17.49 ? 61   GLY G O   1 
ATOM   7138  N  N   . PRO G  1 63  ? 158.765 95.993  54.570 1.00   17.72 ? 62   PRO G N   1 
ATOM   7139  C  CA  . PRO G  1 63  ? 158.920 94.564  54.336 1.00   17.32 ? 62   PRO G CA  1 
ATOM   7140  C  C   . PRO G  1 63  ? 160.133 94.265  53.450 1.00   16.91 ? 62   PRO G C   1 
ATOM   7141  O  O   . PRO G  1 63  ? 160.933 95.152  53.183 1.00   16.54 ? 62   PRO G O   1 
ATOM   7142  C  CB  . PRO G  1 63  ? 157.606 94.201  53.634 1.00   17.69 ? 62   PRO G CB  1 
ATOM   7143  C  CG  . PRO G  1 63  ? 157.307 95.434  52.821 1.00   18.00 ? 62   PRO G CG  1 
ATOM   7144  C  CD  . PRO G  1 63  ? 157.773 96.601  53.657 1.00   17.98 ? 62   PRO G CD  1 
ATOM   7145  N  N   . HIS G  1 64  ? 160.273 93.009  53.004 1.00   16.49 ? 63   HIS G N   1 
ATOM   7146  C  CA  . HIS G  1 64  ? 161.407 92.636  52.175 1.00   16.05 ? 63   HIS G CA  1 
ATOM   7147  C  C   . HIS G  1 64  ? 161.351 93.347  50.855 1.00   16.24 ? 63   HIS G C   1 
ATOM   7148  O  O   . HIS G  1 64  ? 160.296 93.578  50.324 1.00   16.26 ? 63   HIS G O   1 
ATOM   7149  C  CB  . HIS G  1 64  ? 161.447 91.129  51.985 1.00   15.81 ? 63   HIS G CB  1 
ATOM   7150  C  CG  . HIS G  1 64  ? 161.662 90.381  53.263 1.00   15.59 ? 63   HIS G CG  1 
ATOM   7151  N  ND1 . HIS G  1 64  ? 161.651 89.045  53.339 1.00   15.51 ? 63   HIS G ND1 1 
ATOM   7152  C  CD2 . HIS G  1 64  ? 161.870 90.848  54.556 1.00   15.75 ? 63   HIS G CD2 1 
ATOM   7153  C  CE1 . HIS G  1 64  ? 161.861 88.668  54.626 1.00   15.31 ? 63   HIS G CE1 1 
ATOM   7154  N  NE2 . HIS G  1 64  ? 162.026 89.778  55.361 1.00   15.52 ? 63   HIS G NE2 1 
ATOM   7155  N  N   . PHE G  1 65  ? 162.501 93.750  50.351 1.00   16.28 ? 64   PHE G N   1 
ATOM   7156  C  CA  . PHE G  1 65  ? 162.599 94.350  49.045 1.00   16.63 ? 64   PHE G CA  1 
ATOM   7157  C  C   . PHE G  1 65  ? 162.118 93.331  48.015 1.00   16.91 ? 64   PHE G C   1 
ATOM   7158  O  O   . PHE G  1 65  ? 162.670 92.231  47.887 1.00   16.86 ? 64   PHE G O   1 
ATOM   7159  C  CB  . PHE G  1 65  ? 164.039 94.795  48.804 1.00   16.50 ? 64   PHE G CB  1 
ATOM   7160  C  CG  . PHE G  1 65  ? 164.271 95.441  47.476 1.00   16.76 ? 64   PHE G CG  1 
ATOM   7161  C  CD1 . PHE G  1 65  ? 163.340 96.310  46.930 1.00   17.22 ? 64   PHE G CD1 1 
ATOM   7162  C  CD2 . PHE G  1 65  ? 165.434 95.160  46.758 1.00   16.70 ? 64   PHE G CD2 1 
ATOM   7163  C  CE1 . PHE G  1 65  ? 163.568 96.884  45.682 1.00   17.56 ? 64   PHE G CE1 1 
ATOM   7164  C  CE2 . PHE G  1 65  ? 165.661 95.724  45.528 1.00   16.99 ? 64   PHE G CE2 1 
ATOM   7165  C  CZ  . PHE G  1 65  ? 164.736 96.598  44.992 1.00   17.41 ? 64   PHE G CZ  1 
ATOM   7166  N  N   . ASN G  1 66  ? 161.053 93.687  47.307 1.00   17.62 ? 65   ASN G N   1 
ATOM   7167  C  CA  . ASN G  1 66  ? 160.304 92.748  46.491 1.00   18.21 ? 65   ASN G CA  1 
ATOM   7168  C  C   . ASN G  1 66  ? 159.724 93.398  45.243 1.00   19.46 ? 65   ASN G C   1 
ATOM   7169  O  O   . ASN G  1 66  ? 158.504 93.447  45.070 1.00   19.92 ? 65   ASN G O   1 
ATOM   7170  C  CB  . ASN G  1 66  ? 159.178 92.165  47.340 1.00   18.04 ? 65   ASN G CB  1 
ATOM   7171  C  CG  . ASN G  1 66  ? 158.454 91.022  46.658 1.00   17.99 ? 65   ASN G CG  1 
ATOM   7172  O  OD1 . ASN G  1 66  ? 158.983 90.370  45.746 1.00   17.77 ? 65   ASN G OD1 1 
ATOM   7173  N  ND2 . ASN G  1 66  ? 157.244 90.755  47.112 1.00   17.82 ? 65   ASN G ND2 1 
ATOM   7174  N  N   . PRO G  1 67  ? 160.592 93.897  44.352 1.00   20.30 ? 66   PRO G N   1 
ATOM   7175  C  CA  . PRO G  1 67  ? 160.048 94.630  43.223 1.00   21.51 ? 66   PRO G CA  1 
ATOM   7176  C  C   . PRO G  1 67  ? 159.270 93.769  42.233 1.00   23.16 ? 66   PRO G C   1 
ATOM   7177  O  O   . PRO G  1 67  ? 158.429 94.311  41.518 1.00   24.33 ? 66   PRO G O   1 
ATOM   7178  C  CB  . PRO G  1 67  ? 161.276 95.249  42.560 1.00   21.20 ? 66   PRO G CB  1 
ATOM   7179  C  CG  . PRO G  1 67  ? 162.436 94.464  43.047 1.00   20.64 ? 66   PRO G CG  1 
ATOM   7180  C  CD  . PRO G  1 67  ? 162.058 93.855  44.356 1.00   20.04 ? 66   PRO G CD  1 
ATOM   7181  N  N   . LEU G  1 68  ? 159.510 92.450  42.194 1.00   24.10 ? 67   LEU G N   1 
ATOM   7182  C  CA  . LEU G  1 68  ? 158.764 91.578  41.278 1.00   25.29 ? 67   LEU G CA  1 
ATOM   7183  C  C   . LEU G  1 68  ? 157.524 90.963  41.919 1.00   25.87 ? 67   LEU G C   1 
ATOM   7184  O  O   . LEU G  1 68  ? 156.936 90.044  41.358 1.00   26.65 ? 67   LEU G O   1 
ATOM   7185  C  CB  . LEU G  1 68  ? 159.665 90.461  40.711 1.00   25.66 ? 67   LEU G CB  1 
ATOM   7186  C  CG  . LEU G  1 68  ? 161.092 90.816  40.306 1.00   25.98 ? 67   LEU G CG  1 
ATOM   7187  C  CD1 . LEU G  1 68  ? 161.791 89.734  39.505 1.00   26.39 ? 67   LEU G CD1 1 
ATOM   7188  C  CD2 . LEU G  1 68  ? 161.110 92.106  39.526 1.00   27.57 ? 67   LEU G CD2 1 
ATOM   7189  N  N   . SER G  1 69  ? 157.140 91.447  43.096 1.00   26.05 ? 68   SER G N   1 
ATOM   7190  C  CA  . SER G  1 69  ? 155.948 90.950  43.799 1.00   26.50 ? 68   SER G CA  1 
ATOM   7191  C  C   . SER G  1 69  ? 155.860 89.419  43.854 1.00   26.16 ? 68   SER G C   1 
ATOM   7192  O  O   . SER G  1 69  ? 154.882 88.844  43.424 1.00   25.31 ? 68   SER G O   1 
ATOM   7193  C  CB  . SER G  1 69  ? 154.669 91.499  43.156 1.00   27.43 ? 68   SER G CB  1 
ATOM   7194  O  OG  . SER G  1 69  ? 154.760 92.883  42.972 1.00   28.80 ? 68   SER G OG  1 
ATOM   7195  N  N   . ARG G  1 70  ? 156.888 88.778  44.405 1.00   25.82 ? 69   ARG G N   1 
ATOM   7196  C  CA  . ARG G  1 70  ? 156.869 87.343  44.608 1.00   25.76 ? 69   ARG G CA  1 
ATOM   7197  C  C   . ARG G  1 70  ? 156.626 87.006  46.066 1.00   24.07 ? 69   ARG G C   1 
ATOM   7198  O  O   . ARG G  1 70  ? 156.623 87.874  46.930 1.00   22.78 ? 69   ARG G O   1 
ATOM   7199  C  CB  . ARG G  1 70  ? 158.207 86.731  44.223 1.00   27.33 ? 69   ARG G CB  1 
ATOM   7200  C  CG  . ARG G  1 70  ? 158.762 87.127  42.881 1.00   30.48 ? 69   ARG G CG  1 
ATOM   7201  C  CD  . ARG G  1 70  ? 158.029 86.559  41.689 1.00   34.56 ? 69   ARG G CD  1 
ATOM   7202  N  NE  . ARG G  1 70  ? 158.938 86.685  40.549 1.00   39.26 ? 69   ARG G NE  1 
ATOM   7203  C  CZ  . ARG G  1 70  ? 159.625 85.685  39.987 1.00   42.51 ? 69   ARG G CZ  1 
ATOM   7204  N  NH1 . ARG G  1 70  ? 159.467 84.419  40.396 1.00   44.50 ? 69   ARG G NH1 1 
ATOM   7205  N  NH2 . ARG G  1 70  ? 160.461 85.952  38.980 1.00   42.58 ? 69   ARG G NH2 1 
ATOM   7206  N  N   . LYS G  1 71  ? 156.469 85.723  46.332 1.00   23.20 ? 70   LYS G N   1 
ATOM   7207  C  CA  . LYS G  1 71  ? 156.435 85.208  47.694 1.00   22.67 ? 70   LYS G CA  1 
ATOM   7208  C  C   . LYS G  1 71  ? 157.853 85.050  48.249 1.00   20.33 ? 70   LYS G C   1 
ATOM   7209  O  O   . LYS G  1 71  ? 158.814 84.994  47.492 1.00   19.45 ? 70   LYS G O   1 
ATOM   7210  C  CB  . LYS G  1 71  ? 155.700 83.874  47.721 1.00   24.27 ? 70   LYS G CB  1 
ATOM   7211  C  CG  . LYS G  1 71  ? 154.232 83.981  47.315 1.00   26.42 ? 70   LYS G CG  1 
ATOM   7212  C  CD  . LYS G  1 71  ? 153.661 82.603  46.941 1.00   28.74 ? 70   LYS G CD  1 
ATOM   7213  C  CE  . LYS G  1 71  ? 152.267 82.710  46.301 1.00   31.29 ? 70   LYS G CE  1 
ATOM   7214  N  NZ  . LYS G  1 71  ? 151.680 81.381  45.918 1.00   32.78 ? 70   LYS G NZ  1 
ATOM   7215  N  N   . HIS G  1 72  ? 157.967 84.998  49.582 1.00   18.68 ? 71   HIS G N   1 
ATOM   7216  C  CA  . HIS G  1 72  ? 159.249 84.781  50.268 1.00   17.02 ? 71   HIS G CA  1 
ATOM   7217  C  C   . HIS G  1 72  ? 159.867 83.443  49.930 1.00   16.72 ? 71   HIS G C   1 
ATOM   7218  O  O   . HIS G  1 72  ? 159.166 82.434  49.799 1.00   16.86 ? 71   HIS G O   1 
ATOM   7219  C  CB  . HIS G  1 72  ? 159.069 84.901  51.785 1.00   16.49 ? 71   HIS G CB  1 
ATOM   7220  C  CG  . HIS G  1 72  ? 160.365 84.819  52.570 1.00   15.85 ? 71   HIS G CG  1 
ATOM   7221  N  ND1 . HIS G  1 72  ? 161.219 85.855  52.681 1.00   15.46 ? 71   HIS G ND1 1 
ATOM   7222  C  CD2 . HIS G  1 72  ? 160.955 83.749  53.231 1.00   15.49 ? 71   HIS G CD2 1 
ATOM   7223  C  CE1 . HIS G  1 72  ? 162.267 85.478  53.432 1.00   15.21 ? 71   HIS G CE1 1 
ATOM   7224  N  NE2 . HIS G  1 72  ? 162.098 84.182  53.768 1.00   15.21 ? 71   HIS G NE2 1 
ATOM   7225  N  N   . GLY G  1 73  ? 161.192 83.415  49.801 1.00   16.04 ? 72   GLY G N   1 
ATOM   7226  C  CA  . GLY G  1 73  ? 161.899 82.168  49.516 1.00   15.87 ? 72   GLY G CA  1 
ATOM   7227  C  C   . GLY G  1 73  ? 163.298 82.207  50.094 1.00   15.78 ? 72   GLY G C   1 
ATOM   7228  O  O   . GLY G  1 73  ? 163.667 83.151  50.831 1.00   15.24 ? 72   GLY G O   1 
ATOM   7229  N  N   . GLY G  1 74  ? 164.075 81.172  49.788 1.00   15.58 ? 73   GLY G N   1 
ATOM   7230  C  CA  . GLY G  1 74  ? 165.496 81.228  50.027 1.00   15.71 ? 73   GLY G CA  1 
ATOM   7231  C  C   . GLY G  1 74  ? 166.250 81.802  48.843 1.00   15.91 ? 73   GLY G C   1 
ATOM   7232  O  O   . GLY G  1 74  ? 165.707 81.923  47.750 1.00   15.90 ? 73   GLY G O   1 
ATOM   7233  N  N   . PRO G  1 75  ? 167.522 82.161  49.053 1.00   16.10 ? 74   PRO G N   1 
ATOM   7234  C  CA  . PRO G  1 75  ? 168.250 82.788  47.952 1.00   16.58 ? 74   PRO G CA  1 
ATOM   7235  C  C   . PRO G  1 75  ? 168.401 81.891  46.708 1.00   17.43 ? 74   PRO G C   1 
ATOM   7236  O  O   . PRO G  1 75  ? 168.472 82.408  45.588 1.00   17.41 ? 74   PRO G O   1 
ATOM   7237  C  CB  . PRO G  1 75  ? 169.619 83.129  48.571 1.00   16.36 ? 74   PRO G CB  1 
ATOM   7238  C  CG  . PRO G  1 75  ? 169.708 82.327  49.838 1.00   16.07 ? 74   PRO G CG  1 
ATOM   7239  C  CD  . PRO G  1 75  ? 168.302 82.131  50.302 1.00   15.80 ? 74   PRO G CD  1 
ATOM   7240  N  N   . LYS G  1 76  ? 168.396 80.570  46.894 1.00   18.36 ? 75   LYS G N   1 
ATOM   7241  C  CA  . LYS G  1 76  ? 168.538 79.638  45.781 1.00   19.49 ? 75   LYS G CA  1 
ATOM   7242  C  C   . LYS G  1 76  ? 167.226 79.462  45.013 1.00   19.80 ? 75   LYS G C   1 
ATOM   7243  O  O   . LYS G  1 76  ? 167.240 78.888  43.935 1.00   19.88 ? 75   LYS G O   1 
ATOM   7244  C  CB  . LYS G  1 76  ? 169.026 78.257  46.257 1.00   20.63 ? 75   LYS G CB  1 
ATOM   7245  C  CG  . LYS G  1 76  ? 170.430 78.239  46.865 1.00   21.79 ? 75   LYS G CG  1 
ATOM   7246  C  CD  . LYS G  1 76  ? 170.657 76.994  47.766 1.00   23.07 ? 75   LYS G CD  1 
ATOM   7247  C  CE  . LYS G  1 76  ? 171.050 75.750  46.980 1.00   24.06 ? 75   LYS G CE  1 
ATOM   7248  N  NZ  . LYS G  1 76  ? 170.996 74.490  47.803 1.00   25.31 ? 75   LYS G NZ  1 
ATOM   7249  N  N   . ASP G  1 77  ? 166.100 79.919  45.559 1.00   19.86 ? 76   ASP G N   1 
ATOM   7250  C  CA  . ASP G  1 77  ? 164.790 79.763  44.896 1.00   20.81 ? 76   ASP G CA  1 
ATOM   7251  C  C   . ASP G  1 77  ? 164.538 80.796  43.776 1.00   21.65 ? 76   ASP G C   1 
ATOM   7252  O  O   . ASP G  1 77  ? 164.930 81.971  43.877 1.00   20.73 ? 76   ASP G O   1 
ATOM   7253  C  CB  . ASP G  1 77  ? 163.659 79.893  45.945 1.00   21.06 ? 76   ASP G CB  1 
ATOM   7254  C  CG  . ASP G  1 77  ? 163.654 78.747  46.959 1.00   21.36 ? 76   ASP G CG  1 
ATOM   7255  O  OD1 . ASP G  1 77  ? 163.917 77.585  46.564 1.00   22.35 ? 76   ASP G OD1 1 
ATOM   7256  O  OD2 . ASP G  1 77  ? 163.377 79.007  48.147 1.00   20.69 ? 76   ASP G OD2 1 
ATOM   7257  N  N   . GLU G  1 78  ? 163.839 80.372  42.734 1.00   23.08 ? 77   GLU G N   1 
ATOM   7258  C  CA  . GLU G  1 78  ? 163.350 81.295  41.714 1.00   24.42 ? 77   GLU G CA  1 
ATOM   7259  C  C   . GLU G  1 78  ? 162.234 82.153  42.330 1.00   22.79 ? 77   GLU G C   1 
ATOM   7260  O  O   . GLU G  1 78  ? 162.159 83.358  42.111 1.00   21.88 ? 77   GLU G O   1 
ATOM   7261  C  CB  . GLU G  1 78  ? 162.861 80.504  40.487 1.00   27.84 ? 77   GLU G CB  1 
ATOM   7262  C  CG  . GLU G  1 78  ? 162.354 81.341  39.306 1.00   31.65 ? 77   GLU G CG  1 
ATOM   7263  C  CD  . GLU G  1 78  ? 163.409 82.292  38.746 1.00   36.94 ? 77   GLU G CD  1 
ATOM   7264  O  OE1 . GLU G  1 78  ? 164.637 81.946  38.808 1.00   42.20 ? 77   GLU G OE1 1 
ATOM   7265  O  OE2 . GLU G  1 78  ? 163.018 83.398  38.253 1.00   40.52 ? 77   GLU G OE2 1 
ATOM   7266  N  N   . GLU G  1 79  ? 161.363 81.524  43.102 1.00   21.65 ? 78   GLU G N   1 
ATOM   7267  C  CA  . GLU G  1 79  ? 160.319 82.249  43.819 1.00   20.98 ? 78   GLU G CA  1 
ATOM   7268  C  C   . GLU G  1 79  ? 160.939 82.771  45.120 1.00   18.78 ? 78   GLU G C   1 
ATOM   7269  O  O   . GLU G  1 79  ? 161.022 82.065  46.123 1.00   18.71 ? 78   GLU G O   1 
ATOM   7270  C  CB  . GLU G  1 79  ? 159.105 81.340  44.067 1.00   22.34 ? 78   GLU G CB  1 
ATOM   7271  C  CG  . GLU G  1 79  ? 157.851 82.014  44.626 1.00   24.10 ? 78   GLU G CG  1 
ATOM   7272  C  CD  . GLU G  1 79  ? 157.175 82.981  43.656 1.00   25.24 ? 78   GLU G CD  1 
ATOM   7273  O  OE1 . GLU G  1 79  ? 157.479 82.881  42.456 1.00   27.47 ? 78   GLU G OE1 1 
ATOM   7274  O  OE2 . GLU G  1 79  ? 156.354 83.853  44.079 1.00   26.12 ? 78   GLU G OE2 1 
ATOM   7275  N  N   . ARG G  1 80  ? 161.391 84.014  45.063 1.00   17.37 ? 79   ARG G N   1 
ATOM   7276  C  CA  . ARG G  1 80  ? 161.906 84.754  46.201 1.00   16.24 ? 79   ARG G CA  1 
ATOM   7277  C  C   . ARG G  1 80  ? 161.736 86.246  45.989 1.00   15.92 ? 79   ARG G C   1 
ATOM   7278  O  O   . ARG G  1 80  ? 161.513 86.709  44.847 1.00   16.28 ? 79   ARG G O   1 
ATOM   7279  C  CB  . ARG G  1 80  ? 163.387 84.501  46.371 1.00   15.66 ? 79   ARG G CB  1 
ATOM   7280  C  CG  . ARG G  1 80  ? 164.203 84.897  45.152 1.00   15.61 ? 79   ARG G CG  1 
ATOM   7281  C  CD  . ARG G  1 80  ? 165.693 84.704  45.317 1.00   15.32 ? 79   ARG G CD  1 
ATOM   7282  N  NE  . ARG G  1 80  ? 166.328 85.884  45.908 1.00   15.23 ? 79   ARG G NE  1 
ATOM   7283  C  CZ  . ARG G  1 80  ? 167.642 86.073  46.020 1.00   14.98 ? 79   ARG G CZ  1 
ATOM   7284  N  NH1 . ARG G  1 80  ? 168.499 85.149  45.626 1.00   14.96 ? 79   ARG G NH1 1 
ATOM   7285  N  NH2 . ARG G  1 80  ? 168.094 87.207  46.528 1.00   14.97 ? 79   ARG G NH2 1 
ATOM   7286  N  N   . HIS G  1 81  ? 161.886 86.976  47.096 1.00   15.17 ? 80   HIS G N   1 
ATOM   7287  C  CA  . HIS G  1 81  ? 161.997 88.417  47.098 1.00   15.05 ? 80   HIS G CA  1 
ATOM   7288  C  C   . HIS G  1 81  ? 163.422 88.736  46.738 1.00   14.54 ? 80   HIS G C   1 
ATOM   7289  O  O   . HIS G  1 81  ? 164.333 88.001  47.128 1.00   14.49 ? 80   HIS G O   1 
ATOM   7290  C  CB  . HIS G  1 81  ? 161.710 89.020  48.486 1.00   14.93 ? 80   HIS G CB  1 
ATOM   7291  C  CG  . HIS G  1 81  ? 160.363 88.662  49.080 1.00   15.24 ? 80   HIS G CG  1 
ATOM   7292  N  ND1 . HIS G  1 81  ? 160.194 88.413  50.406 1.00   15.16 ? 80   HIS G ND1 1 
ATOM   7293  C  CD2 . HIS G  1 81  ? 159.096 88.592  48.502 1.00   15.63 ? 80   HIS G CD2 1 
ATOM   7294  C  CE1 . HIS G  1 81  ? 158.889 88.160  50.642 1.00   15.53 ? 80   HIS G CE1 1 
ATOM   7295  N  NE2 . HIS G  1 81  ? 158.216 88.285  49.475 1.00   15.75 ? 80   HIS G NE2 1 
ATOM   7296  N  N   . VAL G  1 82  ? 163.649 89.837  46.038 1.00   14.31 ? 81   VAL G N   1 
ATOM   7297  C  CA  . VAL G  1 82  ? 165.026 90.237  45.718 1.00   14.08 ? 81   VAL G CA  1 
ATOM   7298  C  C   . VAL G  1 82  ? 165.867 90.298  46.980 1.00   13.67 ? 81   VAL G C   1 
ATOM   7299  O  O   . VAL G  1 82  ? 167.005 89.869  46.987 1.00   13.51 ? 81   VAL G O   1 
ATOM   7300  C  CB  . VAL G  1 82  ? 165.103 91.580  44.943 1.00   14.22 ? 81   VAL G CB  1 
ATOM   7301  C  CG1 . VAL G  1 82  ? 166.517 92.133  44.960 1.00   14.04 ? 81   VAL G CG1 1 
ATOM   7302  C  CG2 . VAL G  1 82  ? 164.586 91.401  43.506 1.00   14.44 ? 81   VAL G CG2 1 
ATOM   7303  N  N   . GLY G  1 83  ? 165.308 90.820  48.064 1.00   13.60 ? 82   GLY G N   1 
ATOM   7304  C  CA  . GLY G  1 83  ? 166.055 90.920  49.313 1.00   13.35 ? 82   GLY G CA  1 
ATOM   7305  C  C   . GLY G  1 83  ? 166.229 89.664  50.139 1.00   13.18 ? 82   GLY G C   1 
ATOM   7306  O  O   . GLY G  1 83  ? 166.797 89.714  51.258 1.00   13.01 ? 82   GLY G O   1 
ATOM   7307  N  N   . ASP G  1 84  ? 165.765 88.521  49.645 1.00   13.18 ? 83   ASP G N   1 
ATOM   7308  C  CA  . ASP G  1 84  ? 165.941 87.298  50.418 1.00   13.10 ? 83   ASP G CA  1 
ATOM   7309  C  C   . ASP G  1 84  ? 167.344 86.654  50.348 1.00   13.11 ? 83   ASP G C   1 
ATOM   7310  O  O   . ASP G  1 84  ? 167.635 85.843  49.470 1.00   13.26 ? 83   ASP G O   1 
ATOM   7311  C  CB  . ASP G  1 84  ? 164.910 86.264  50.005 1.00   13.29 ? 83   ASP G CB  1 
ATOM   7312  C  CG  . ASP G  1 84  ? 163.502 86.647  50.351 1.00   13.37 ? 83   ASP G CG  1 
ATOM   7313  O  OD1 . ASP G  1 84  ? 163.261 87.575  51.150 1.00   13.17 ? 83   ASP G OD1 1 
ATOM   7314  O  OD2 . ASP G  1 84  ? 162.606 85.987  49.774 1.00   13.62 ? 83   ASP G OD2 1 
ATOM   7315  N  N   . LEU G  1 85  ? 168.171 86.917  51.358 1.00   13.08 ? 84   LEU G N   1 
ATOM   7316  C  CA  . LEU G  1 85  ? 169.525 86.395  51.418 1.00   13.06 ? 84   LEU G CA  1 
ATOM   7317  C  C   . LEU G  1 85  ? 169.664 85.175  52.308 1.00   13.18 ? 84   LEU G C   1 
ATOM   7318  O  O   . LEU G  1 85  ? 170.757 84.655  52.481 1.00   13.34 ? 84   LEU G O   1 
ATOM   7319  C  CB  . LEU G  1 85  ? 170.488 87.502  51.837 1.00   12.99 ? 84   LEU G CB  1 
ATOM   7320  C  CG  . LEU G  1 85  ? 170.569 88.653  50.794 1.00   13.02 ? 84   LEU G CG  1 
ATOM   7321  C  CD1 . LEU G  1 85  ? 171.451 89.783  51.319 1.00   12.93 ? 84   LEU G CD1 1 
ATOM   7322  C  CD2 . LEU G  1 85  ? 171.094 88.158  49.436 1.00   13.02 ? 84   LEU G CD2 1 
ATOM   7323  N  N   . GLY G  1 86  ? 168.542 84.675  52.814 1.00   13.38 ? 85   GLY G N   1 
ATOM   7324  C  CA  . GLY G  1 86  ? 168.521 83.420  53.595 1.00   13.32 ? 85   GLY G CA  1 
ATOM   7325  C  C   . GLY G  1 86  ? 168.934 83.666  55.026 1.00   13.20 ? 85   GLY G C   1 
ATOM   7326  O  O   . GLY G  1 86  ? 168.479 84.635  55.659 1.00   13.14 ? 85   GLY G O   1 
ATOM   7327  N  N   . ASN G  1 87  ? 169.792 82.787  55.530 1.00   13.18 ? 86   ASN G N   1 
ATOM   7328  C  CA  . ASN G  1 87  ? 170.270 82.833  56.897 1.00   13.42 ? 86   ASN G CA  1 
ATOM   7329  C  C   . ASN G  1 87  ? 171.772 83.140  56.971 1.00   13.50 ? 86   ASN G C   1 
ATOM   7330  O  O   . ASN G  1 87  ? 172.544 82.865  56.033 1.00   13.51 ? 86   ASN G O   1 
ATOM   7331  C  CB  . ASN G  1 87  ? 170.032 81.482  57.589 1.00   13.52 ? 86   ASN G CB  1 
ATOM   7332  C  CG  . ASN G  1 87  ? 168.575 81.223  57.882 1.00   13.69 ? 86   ASN G CG  1 
ATOM   7333  O  OD1 . ASN G  1 87  ? 167.950 81.952  58.676 1.00   13.63 ? 86   ASN G OD1 1 
ATOM   7334  N  ND2 . ASN G  1 87  ? 168.020 80.145  57.269 1.00   13.65 ? 86   ASN G ND2 1 
ATOM   7335  N  N   . VAL G  1 88  ? 172.168 83.700  58.108 1.00   13.65 ? 87   VAL G N   1 
ATOM   7336  C  CA  . VAL G  1 88  ? 173.580 83.720  58.528 1.00   13.78 ? 87   VAL G CA  1 
ATOM   7337  C  C   . VAL G  1 88  ? 173.646 82.925  59.845 1.00   14.05 ? 87   VAL G C   1 
ATOM   7338  O  O   . VAL G  1 88  ? 172.627 82.784  60.531 1.00   14.34 ? 87   VAL G O   1 
ATOM   7339  C  CB  . VAL G  1 88  ? 174.096 85.168  58.664 1.00   13.80 ? 87   VAL G CB  1 
ATOM   7340  C  CG1 . VAL G  1 88  ? 174.013 85.883  57.295 1.00   13.48 ? 87   VAL G CG1 1 
ATOM   7341  C  CG2 . VAL G  1 88  ? 173.354 85.922  59.778 1.00   13.64 ? 87   VAL G CG2 1 
ATOM   7342  N  N   . THR G  1 89  ? 174.807 82.377  60.168 1.00   14.29 ? 88   THR G N   1 
ATOM   7343  C  CA  . THR G  1 89  ? 174.987 81.478  61.293 1.00   14.62 ? 88   THR G CA  1 
ATOM   7344  C  C   . THR G  1 89  ? 175.945 82.094  62.296 1.00   15.16 ? 88   THR G C   1 
ATOM   7345  O  O   . THR G  1 89  ? 177.058 82.478  61.949 1.00   15.49 ? 88   THR G O   1 
ATOM   7346  C  CB  . THR G  1 89  ? 175.571 80.115  60.839 1.00   14.67 ? 88   THR G CB  1 
ATOM   7347  O  OG1 . THR G  1 89  ? 174.620 79.473  59.982 1.00   14.41 ? 88   THR G OG1 1 
ATOM   7348  C  CG2 . THR G  1 89  ? 175.916 79.187  62.040 1.00   14.62 ? 88   THR G CG2 1 
ATOM   7349  N  N   . ALA G  1 90  ? 175.515 82.173  63.547 1.00   15.70 ? 89   ALA G N   1 
ATOM   7350  C  CA  . ALA G  1 90  ? 176.366 82.685  64.615 1.00   16.47 ? 89   ALA G CA  1 
ATOM   7351  C  C   . ALA G  1 90  ? 176.959 81.462  65.297 1.00   17.31 ? 89   ALA G C   1 
ATOM   7352  O  O   . ALA G  1 90  ? 176.256 80.471  65.507 1.00   17.14 ? 89   ALA G O   1 
ATOM   7353  C  CB  . ALA G  1 90  ? 175.556 83.513  65.608 1.00   16.32 ? 89   ALA G CB  1 
ATOM   7354  N  N   . ASP G  1 91  ? 178.241 81.547  65.646 1.00   18.52 ? 90   ASP G N   1 
ATOM   7355  C  CA  . ASP G  1 91  ? 178.939 80.472  66.358 1.00   19.52 ? 90   ASP G CA  1 
ATOM   7356  C  C   . ASP G  1 91  ? 178.623 80.522  67.846 1.00   20.66 ? 90   ASP G C   1 
ATOM   7357  O  O   . ASP G  1 91  ? 177.800 81.336  68.282 1.00   20.39 ? 90   ASP G O   1 
ATOM   7358  C  CB  . ASP G  1 91  ? 180.458 80.538  66.095 1.00   19.94 ? 90   ASP G CB  1 
ATOM   7359  C  CG  . ASP G  1 91  ? 181.106 81.836  66.599 1.00   20.20 ? 90   ASP G CG  1 
ATOM   7360  O  OD1 . ASP G  1 91  ? 180.534 82.553  67.455 1.00   19.77 ? 90   ASP G OD1 1 
ATOM   7361  O  OD2 . ASP G  1 91  ? 182.223 82.125  66.127 1.00   21.17 ? 90   ASP G OD2 1 
ATOM   7362  N  N   . LYS G  1 92  ? 179.287 79.665  68.614 1.00   22.04 ? 91   LYS G N   1 
ATOM   7363  C  CA  . LYS G  1 92  ? 179.037 79.537  70.041 1.00   23.96 ? 91   LYS G CA  1 
ATOM   7364  C  C   . LYS G  1 92  ? 179.442 80.766  70.826 1.00   23.29 ? 91   LYS G C   1 
ATOM   7365  O  O   . LYS G  1 92  ? 178.977 80.946  71.923 1.00   23.80 ? 91   LYS G O   1 
ATOM   7366  C  CB  . LYS G  1 92  ? 179.746 78.296  70.615 1.00   26.09 ? 91   LYS G CB  1 
ATOM   7367  C  CG  . LYS G  1 92  ? 181.266 78.402  70.673 1.00   28.51 ? 91   LYS G CG  1 
ATOM   7368  C  CD  . LYS G  1 92  ? 181.893 77.016  70.893 1.00   31.12 ? 91   LYS G CD  1 
ATOM   7369  C  CE  . LYS G  1 92  ? 183.323 77.124  71.413 1.00   33.24 ? 91   LYS G CE  1 
ATOM   7370  N  NZ  . LYS G  1 92  ? 184.185 78.010  70.556 1.00   34.79 ? 91   LYS G NZ  1 
ATOM   7371  N  N   . ASP G  1 93  ? 180.290 81.614  70.256 1.00   22.76 ? 92   ASP G N   1 
ATOM   7372  C  CA  . ASP G  1 93  ? 180.587 82.919  70.847 1.00   22.92 ? 92   ASP G CA  1 
ATOM   7373  C  C   . ASP G  1 93  ? 179.604 83.993  70.429 1.00   21.79 ? 92   ASP G C   1 
ATOM   7374  O  O   . ASP G  1 93  ? 179.720 85.141  70.859 1.00   22.41 ? 92   ASP G O   1 
ATOM   7375  C  CB  . ASP G  1 93  ? 182.004 83.350  70.465 1.00   23.83 ? 92   ASP G CB  1 
ATOM   7376  C  CG  . ASP G  1 93  ? 183.045 82.446  71.055 1.00   25.32 ? 92   ASP G CG  1 
ATOM   7377  O  OD1 . ASP G  1 93  ? 182.834 82.000  72.202 1.00   26.23 ? 92   ASP G OD1 1 
ATOM   7378  O  OD2 . ASP G  1 93  ? 184.067 82.158  70.388 1.00   27.21 ? 92   ASP G OD2 1 
ATOM   7379  N  N   . GLY G  1 94  ? 178.640 83.637  69.595 1.00   20.21 ? 93   GLY G N   1 
ATOM   7380  C  CA  . GLY G  1 94  ? 177.638 84.587  69.142 1.00   19.22 ? 93   GLY G CA  1 
ATOM   7381  C  C   . GLY G  1 94  ? 178.080 85.468  67.991 1.00   18.48 ? 93   GLY G C   1 
ATOM   7382  O  O   . GLY G  1 94  ? 177.472 86.512  67.757 1.00   18.01 ? 93   GLY G O   1 
ATOM   7383  N  N   . VAL G  1 95  ? 179.137 85.051  67.283 1.00   18.14 ? 94   VAL G N   1 
ATOM   7384  C  CA  . VAL G  1 95  ? 179.663 85.787  66.133 1.00   17.83 ? 94   VAL G CA  1 
ATOM   7385  C  C   . VAL G  1 95  ? 179.266 85.093  64.797 1.00   17.35 ? 94   VAL G C   1 
ATOM   7386  O  O   . VAL G  1 95  ? 179.501 83.866  64.632 1.00   17.17 ? 94   VAL G O   1 
ATOM   7387  C  CB  . VAL G  1 95  ? 181.198 85.920  66.203 1.00   18.38 ? 94   VAL G CB  1 
ATOM   7388  C  CG1 . VAL G  1 95  ? 181.747 86.626  64.936 1.00   18.33 ? 94   VAL G CG1 1 
ATOM   7389  C  CG2 . VAL G  1 95  ? 181.619 86.669  67.457 1.00   18.58 ? 94   VAL G CG2 1 
ATOM   7390  N  N   . ALA G  1 96  ? 178.654 85.871  63.887 1.00   16.68 ? 95   ALA G N   1 
ATOM   7391  C  CA  . ALA G  1 96  ? 178.358 85.429  62.511 1.00   16.57 ? 95   ALA G CA  1 
ATOM   7392  C  C   . ALA G  1 96  ? 179.402 86.017  61.565 1.00   16.84 ? 95   ALA G C   1 
ATOM   7393  O  O   . ALA G  1 96  ? 179.451 87.239  61.325 1.00   16.23 ? 95   ALA G O   1 
ATOM   7394  C  CB  . ALA G  1 96  ? 176.957 85.835  62.071 1.00   15.85 ? 95   ALA G CB  1 
ATOM   7395  N  N   . ASP G  1 97  ? 180.251 85.141  61.049 1.00   17.37 ? 96   ASP G N   1 
ATOM   7396  C  CA  . ASP G  1 97  ? 181.209 85.534  60.013 1.00   17.97 ? 96   ASP G CA  1 
ATOM   7397  C  C   . ASP G  1 97  ? 180.532 85.325  58.667 1.00   17.34 ? 96   ASP G C   1 
ATOM   7398  O  O   . ASP G  1 97  ? 180.663 84.264  58.034 1.00   17.25 ? 96   ASP G O   1 
ATOM   7399  C  CB  . ASP G  1 97  ? 182.471 84.712  60.128 1.00   18.95 ? 96   ASP G CB  1 
ATOM   7400  C  CG  . ASP G  1 97  ? 183.280 85.070  61.367 1.00   20.44 ? 96   ASP G CG  1 
ATOM   7401  O  OD1 . ASP G  1 97  ? 183.488 86.279  61.652 1.00   21.43 ? 96   ASP G OD1 1 
ATOM   7402  O  OD2 . ASP G  1 97  ? 183.714 84.138  62.063 1.00   22.09 ? 96   ASP G OD2 1 
ATOM   7403  N  N   . VAL G  1 98  ? 179.819 86.356  58.228 1.00   16.85 ? 97   VAL G N   1 
ATOM   7404  C  CA  . VAL G  1 98  ? 178.924 86.248  57.082 1.00   16.51 ? 97   VAL G CA  1 
ATOM   7405  C  C   . VAL G  1 98  ? 179.747 86.093  55.795 1.00   16.94 ? 97   VAL G C   1 
ATOM   7406  O  O   . VAL G  1 98  ? 180.759 86.769  55.620 1.00   17.33 ? 97   VAL G O   1 
ATOM   7407  C  CB  . VAL G  1 98  ? 178.015 87.481  56.983 1.00   16.14 ? 97   VAL G CB  1 
ATOM   7408  C  CG1 . VAL G  1 98  ? 177.168 87.437  55.702 1.00   15.69 ? 97   VAL G CG1 1 
ATOM   7409  C  CG2 . VAL G  1 98  ? 177.162 87.620  58.240 1.00   15.64 ? 97   VAL G CG2 1 
ATOM   7410  N  N   . SER G  1 99  ? 179.326 85.197  54.916 1.00   17.13 ? 98   SER G N   1 
ATOM   7411  C  CA  . SER G  1 99  ? 179.990 85.004  53.626 1.00   17.99 ? 98   SER G CA  1 
ATOM   7412  C  C   . SER G  1 99  ? 178.994 84.429  52.661 1.00   17.87 ? 98   SER G C   1 
ATOM   7413  O  O   . SER G  1 99  ? 178.697 83.235  52.712 1.00   18.02 ? 98   SER G O   1 
ATOM   7414  C  CB  . SER G  1 99  ? 181.159 84.034  53.722 1.00   19.03 ? 98   SER G CB  1 
ATOM   7415  O  OG  . SER G  1 99  ? 181.975 84.139  52.537 1.00   20.47 ? 98   SER G OG  1 
ATOM   7416  N  N   . ILE G  1 100 ? 178.459 85.297  51.810 1.00   17.29 ? 99   ILE G N   1 
ATOM   7417  C  CA  . ILE G  1 100 ? 177.369 84.970  50.908 1.00   17.05 ? 99   ILE G CA  1 
ATOM   7418  C  C   . ILE G  1 100 ? 177.733 85.540  49.557 1.00   17.30 ? 99   ILE G C   1 
ATOM   7419  O  O   . ILE G  1 100 ? 178.428 86.550  49.466 1.00   16.75 ? 99   ILE G O   1 
ATOM   7420  C  CB  . ILE G  1 100 ? 176.043 85.616  51.418 1.00   16.60 ? 99   ILE G CB  1 
ATOM   7421  C  CG1 . ILE G  1 100 ? 175.522 84.885  52.670 1.00   16.33 ? 99   ILE G CG1 1 
ATOM   7422  C  CG2 . ILE G  1 100 ? 174.948 85.679  50.352 1.00   16.64 ? 99   ILE G CG2 1 
ATOM   7423  C  CD1 . ILE G  1 100 ? 174.423 85.632  53.413 1.00   15.92 ? 99   ILE G CD1 1 
ATOM   7424  N  N   . GLU G  1 101 ? 177.282 84.861  48.509 1.00   18.11 ? 100  GLU G N   1 
ATOM   7425  C  CA  . GLU G  1 101 ? 177.303 85.409  47.172 1.00   19.13 ? 100  GLU G CA  1 
ATOM   7426  C  C   . GLU G  1 101 ? 175.905 85.253  46.564 1.00   18.39 ? 100  GLU G C   1 
ATOM   7427  O  O   . GLU G  1 101 ? 175.283 84.170  46.609 1.00   18.12 ? 100  GLU G O   1 
ATOM   7428  C  CB  . GLU G  1 101 ? 178.389 84.730  46.304 1.00   21.07 ? 100  GLU G CB  1 
ATOM   7429  C  CG  . GLU G  1 101 ? 178.355 85.187  44.853 1.00   22.93 ? 100  GLU G CG  1 
ATOM   7430  C  CD  . GLU G  1 101 ? 179.281 84.405  43.916 1.00   25.18 ? 100  GLU G CD  1 
ATOM   7431  O  OE1 . GLU G  1 101 ? 180.503 84.539  44.061 1.00   27.50 ? 100  GLU G OE1 1 
ATOM   7432  O  OE2 . GLU G  1 101 ? 178.784 83.690  43.003 1.00   27.91 ? 100  GLU G OE2 1 
ATOM   7433  N  N   . ASP G  1 102 ? 175.420 86.335  45.976 1.00   17.50 ? 101  ASP G N   1 
ATOM   7434  C  CA  . ASP G  1 102 ? 174.081 86.358  45.427 1.00   16.89 ? 101  ASP G CA  1 
ATOM   7435  C  C   . ASP G  1 102 ? 174.038 87.148  44.126 1.00   16.89 ? 101  ASP G C   1 
ATOM   7436  O  O   . ASP G  1 102 ? 174.623 88.240  44.022 1.00   16.63 ? 101  ASP G O   1 
ATOM   7437  C  CB  . ASP G  1 102 ? 173.133 87.000  46.432 1.00   16.54 ? 101  ASP G CB  1 
ATOM   7438  C  CG  . ASP G  1 102 ? 171.689 86.760  46.092 1.00   16.50 ? 101  ASP G CG  1 
ATOM   7439  O  OD1 . ASP G  1 102 ? 171.207 85.648  46.414 1.00   16.60 ? 101  ASP G OD1 1 
ATOM   7440  O  OD2 . ASP G  1 102 ? 171.027 87.677  45.552 1.00   16.08 ? 101  ASP G OD2 1 
ATOM   7441  N  N   . SER G  1 103 ? 173.281 86.602  43.176 1.00   16.78 ? 102  SER G N   1 
ATOM   7442  C  CA  . SER G  1 103 ? 173.172 87.106  41.817 1.00   17.14 ? 102  SER G CA  1 
ATOM   7443  C  C   . SER G  1 103 ? 171.826 87.742  41.530 1.00   16.91 ? 102  SER G C   1 
ATOM   7444  O  O   . SER G  1 103 ? 171.600 88.154  40.410 1.00   17.02 ? 102  SER G O   1 
ATOM   7445  C  CB  . SER G  1 103 ? 173.421 85.964  40.810 1.00   17.52 ? 102  SER G CB  1 
ATOM   7446  O  OG  . SER G  1 103 ? 174.748 85.490  40.965 0.50   17.76 ? 102  SER G OG  1 
ATOM   7447  N  N   . VAL G  1 104 ? 170.957 87.843  42.549 1.00   16.42 ? 103  VAL G N   1 
ATOM   7448  C  CA  . VAL G  1 104 ? 169.667 88.532  42.421 1.00   16.24 ? 103  VAL G CA  1 
ATOM   7449  C  C   . VAL G  1 104 ? 169.745 89.969  42.991 1.00   16.22 ? 103  VAL G C   1 
ATOM   7450  O  O   . VAL G  1 104 ? 169.252 90.904  42.362 1.00   16.33 ? 103  VAL G O   1 
ATOM   7451  C  CB  . VAL G  1 104 ? 168.528 87.725  43.069 1.00   16.04 ? 103  VAL G CB  1 
ATOM   7452  C  CG1 . VAL G  1 104 ? 167.221 88.531  43.101 1.00   16.07 ? 103  VAL G CG1 1 
ATOM   7453  C  CG2 . VAL G  1 104 ? 168.344 86.394  42.343 1.00   16.05 ? 103  VAL G CG2 1 
ATOM   7454  N  N   . ILE G  1 105 ? 170.354 90.175  44.152 1.00   16.05 ? 104  ILE G N   1 
ATOM   7455  C  CA  . ILE G  1 105 ? 170.618 91.561  44.596 1.00   16.28 ? 104  ILE G CA  1 
ATOM   7456  C  C   . ILE G  1 105 ? 171.616 92.198  43.613 1.00   17.08 ? 104  ILE G C   1 
ATOM   7457  O  O   . ILE G  1 105 ? 172.304 91.496  42.858 1.00   17.41 ? 104  ILE G O   1 
ATOM   7458  C  CB  . ILE G  1 105 ? 171.146 91.664  46.050 1.00   16.07 ? 104  ILE G CB  1 
ATOM   7459  C  CG1 . ILE G  1 105 ? 172.385 90.779  46.272 1.00   15.94 ? 104  ILE G CG1 1 
ATOM   7460  C  CG2 . ILE G  1 105 ? 170.053 91.303  47.060 1.00   15.56 ? 104  ILE G CG2 1 
ATOM   7461  C  CD1 . ILE G  1 105 ? 173.249 91.202  47.451 1.00   15.78 ? 104  ILE G CD1 1 
ATOM   7462  N  N   . SER G  1 106 ? 171.684 93.528  43.596 1.00   17.43 ? 105  SER G N   1 
ATOM   7463  C  CA  . SER G  1 106 ? 172.652 94.214  42.771 1.00   17.70 ? 105  SER G CA  1 
ATOM   7464  C  C   . SER G  1 106 ? 173.015 95.559  43.394 1.00   17.91 ? 105  SER G C   1 
ATOM   7465  O  O   . SER G  1 106 ? 172.300 96.051  44.259 1.00   17.18 ? 105  SER G O   1 
ATOM   7466  C  CB  . SER G  1 106 ? 172.070 94.431  41.377 1.00   18.13 ? 105  SER G CB  1 
ATOM   7467  O  OG  . SER G  1 106 ? 173.068 94.901  40.488 1.00   18.65 ? 105  SER G OG  1 
ATOM   7468  N  N   . LEU G  1 107 ? 174.115 96.155  42.935 1.00   18.63 ? 106  LEU G N   1 
ATOM   7469  C  CA  . LEU G  1 107 ? 174.499 97.513  43.375 1.00   19.37 ? 106  LEU G CA  1 
ATOM   7470  C  C   . LEU G  1 107 ? 174.198 98.516  42.279 1.00   20.41 ? 106  LEU G C   1 
ATOM   7471  O  O   . LEU G  1 107 ? 174.598 99.670  42.355 1.00   21.27 ? 106  LEU G O   1 
ATOM   7472  C  CB  . LEU G  1 107 ? 175.972 97.593  43.801 1.00   19.25 ? 106  LEU G CB  1 
ATOM   7473  C  CG  . LEU G  1 107 ? 176.393 96.587  44.874 1.00   18.97 ? 106  LEU G CG  1 
ATOM   7474  C  CD1 . LEU G  1 107 ? 177.851 96.830  45.266 1.00   19.22 ? 106  LEU G CD1 1 
ATOM   7475  C  CD2 . LEU G  1 107 ? 175.472 96.649  46.085 1.00   18.27 ? 106  LEU G CD2 1 
ATOM   7476  N  N   . SER G  1 108 ? 173.444 98.089  41.282 1.00   21.21 ? 107  SER G N   1 
ATOM   7477  C  CA  . SER G  1 108 ? 172.861 99.030  40.340 1.00   22.27 ? 107  SER G CA  1 
ATOM   7478  C  C   . SER G  1 108 ? 171.576 98.480  39.725 1.00   22.44 ? 107  SER G C   1 
ATOM   7479  O  O   . SER G  1 108 ? 171.233 97.290  39.879 1.00   22.12 ? 107  SER G O   1 
ATOM   7480  C  CB  . SER G  1 108 ? 173.865 99.404  39.250 1.00   23.04 ? 107  SER G CB  1 
ATOM   7481  O  OG  . SER G  1 108 ? 174.074 98.309  38.390 1.00   24.32 ? 107  SER G OG  1 
ATOM   7482  N  N   . GLY G  1 109 ? 170.857 99.374  39.058 1.00   22.80 ? 108  GLY G N   1 
ATOM   7483  C  CA  . GLY G  1 109 ? 169.696 98.995  38.280 1.00   23.40 ? 108  GLY G CA  1 
ATOM   7484  C  C   . GLY G  1 109 ? 168.470 98.778  39.135 1.00   23.13 ? 108  GLY G C   1 
ATOM   7485  O  O   . GLY G  1 109 ? 168.403 99.222  40.269 1.00   23.02 ? 108  GLY G O   1 
ATOM   7486  N  N   . ASP G  1 110 ? 167.511 98.077  38.564 1.00   23.11 ? 109  ASP G N   1 
ATOM   7487  C  CA  . ASP G  1 110 ? 166.233 97.813  39.207 1.00   23.30 ? 109  ASP G CA  1 
ATOM   7488  C  C   . ASP G  1 110 ? 166.329 97.029  40.528 1.00   22.49 ? 109  ASP G C   1 
ATOM   7489  O  O   . ASP G  1 110 ? 165.516 97.246  41.404 1.00   23.05 ? 109  ASP G O   1 
ATOM   7490  C  CB  . ASP G  1 110 ? 165.336 97.026  38.249 1.00   23.48 ? 109  ASP G CB  1 
ATOM   7491  C  CG  . ASP G  1 110 ? 164.682 97.891  37.222 1.00   24.40 ? 109  ASP G CG  1 
ATOM   7492  O  OD1 . ASP G  1 110 ? 164.814 99.137  37.259 1.00   24.55 ? 109  ASP G OD1 1 
ATOM   7493  O  OD2 . ASP G  1 110 ? 164.004 97.304  36.366 1.00   25.59 ? 109  ASP G OD2 1 
ATOM   7494  N  N   . HIS G  1 111 ? 167.296 96.128  40.663 1.00   21.54 ? 110  HIS G N   1 
ATOM   7495  C  CA  . HIS G  1 111 ? 167.447 95.360  41.906 1.00   21.02 ? 110  HIS G CA  1 
ATOM   7496  C  C   . HIS G  1 111 ? 168.474 95.951  42.872 1.00   20.03 ? 110  HIS G C   1 
ATOM   7497  O  O   . HIS G  1 111 ? 168.961 95.272  43.784 1.00   18.91 ? 110  HIS G O   1 
ATOM   7498  C  CB  . HIS G  1 111 ? 167.812 93.925  41.569 1.00   21.17 ? 110  HIS G CB  1 
ATOM   7499  C  CG  . HIS G  1 111 ? 166.703 93.161  40.902 1.00   21.55 ? 110  HIS G CG  1 
ATOM   7500  N  ND1 . HIS G  1 111 ? 166.805 91.839  40.608 1.00   22.44 ? 110  HIS G ND1 1 
ATOM   7501  C  CD2 . HIS G  1 111 ? 165.429 93.553  40.511 1.00   22.31 ? 110  HIS G CD2 1 
ATOM   7502  C  CE1 . HIS G  1 111 ? 165.656 91.432  40.018 1.00   22.50 ? 110  HIS G CE1 1 
ATOM   7503  N  NE2 . HIS G  1 111 ? 164.821 92.480  39.963 1.00   22.27 ? 110  HIS G NE2 1 
ATOM   7504  N  N   . CYS G  1 112 ? 168.810 97.222  42.674 1.00   19.83 ? 111  CYS G N   1 
ATOM   7505  C  CA  . CYS G  1 112 ? 169.802 97.909  43.501 1.00   19.65 ? 111  CYS G CA  1 
ATOM   7506  C  C   . CYS G  1 112 ? 169.351 97.918  44.950 1.00   18.44 ? 111  CYS G C   1 
ATOM   7507  O  O   . CYS G  1 112 ? 168.207 98.219  45.238 1.00   18.05 ? 111  CYS G O   1 
ATOM   7508  C  CB  . CYS G  1 112 ? 169.948 99.355  43.043 1.00   20.78 ? 111  CYS G CB  1 
ATOM   7509  S  SG  . CYS G  1 112 ? 171.372 100.160 43.778 1.00   22.54 ? 111  CYS G SG  1 
ATOM   7510  N  N   . ILE G  1 113 ? 170.250 97.576  45.854 1.00   17.58 ? 112  ILE G N   1 
ATOM   7511  C  CA  . ILE G  1 113 ? 169.936 97.551  47.287 1.00   17.01 ? 112  ILE G CA  1 
ATOM   7512  C  C   . ILE G  1 113 ? 170.552 98.760  48.039 1.00   17.03 ? 112  ILE G C   1 
ATOM   7513  O  O   . ILE G  1 113 ? 170.333 98.951  49.227 1.00   16.78 ? 112  ILE G O   1 
ATOM   7514  C  CB  . ILE G  1 113 ? 170.365 96.206  47.921 1.00   16.41 ? 112  ILE G CB  1 
ATOM   7515  C  CG1 . ILE G  1 113 ? 171.886 96.027  47.829 1.00   16.32 ? 112  ILE G CG1 1 
ATOM   7516  C  CG2 . ILE G  1 113 ? 169.628 95.040  47.244 1.00   15.98 ? 112  ILE G CG2 1 
ATOM   7517  C  CD1 . ILE G  1 113 ? 172.444 94.842  48.624 1.00   15.92 ? 112  ILE G CD1 1 
ATOM   7518  N  N   . ILE G  1 114 ? 171.315 99.584  47.339 1.00   17.24 ? 113  ILE G N   1 
ATOM   7519  C  CA  . ILE G  1 114 ? 171.850 100.793 47.953 1.00   17.44 ? 113  ILE G CA  1 
ATOM   7520  C  C   . ILE G  1 114 ? 170.696 101.715 48.374 1.00   17.27 ? 113  ILE G C   1 
ATOM   7521  O  O   . ILE G  1 114 ? 169.733 101.867 47.677 1.00   17.23 ? 113  ILE G O   1 
ATOM   7522  C  CB  . ILE G  1 114 ? 172.862 101.497 47.020 1.00   17.88 ? 113  ILE G CB  1 
ATOM   7523  C  CG1 . ILE G  1 114 ? 174.130 100.634 46.927 1.00   17.93 ? 113  ILE G CG1 1 
ATOM   7524  C  CG2 . ILE G  1 114 ? 173.204 102.901 47.542 1.00   17.92 ? 113  ILE G CG2 1 
ATOM   7525  C  CD1 . ILE G  1 114 ? 175.040 100.998 45.752 1.00   18.73 ? 113  ILE G CD1 1 
ATOM   7526  N  N   . GLY G  1 115 ? 170.775 102.274 49.563 1.00   17.24 ? 114  GLY G N   1 
ATOM   7527  C  CA  . GLY G  1 115 ? 169.696 103.108 50.059 1.00   17.49 ? 114  GLY G CA  1 
ATOM   7528  C  C   . GLY G  1 115 ? 168.559 102.346 50.702 1.00   17.39 ? 114  GLY G C   1 
ATOM   7529  O  O   . GLY G  1 115 ? 167.583 102.964 51.135 1.00   17.70 ? 114  GLY G O   1 
ATOM   7530  N  N   . ARG G  1 116 ? 168.683 101.016 50.789 1.00   16.97 ? 115  ARG G N   1 
ATOM   7531  C  CA  . ARG G  1 116 ? 167.696 100.184 51.466 1.00   16.71 ? 115  ARG G CA  1 
ATOM   7532  C  C   . ARG G  1 116 ? 168.279 99.647  52.768 1.00   16.24 ? 115  ARG G C   1 
ATOM   7533  O  O   . ARG G  1 116 ? 169.404 99.987  53.133 1.00   16.23 ? 115  ARG G O   1 
ATOM   7534  C  CB  . ARG G  1 116 ? 167.254 99.065  50.511 1.00   17.19 ? 115  ARG G CB  1 
ATOM   7535  C  CG  . ARG G  1 116 ? 166.682 99.641  49.218 1.00   18.02 ? 115  ARG G CG  1 
ATOM   7536  C  CD  . ARG G  1 116 ? 165.999 98.594  48.383 1.00   18.55 ? 115  ARG G CD  1 
ATOM   7537  N  NE  . ARG G  1 116 ? 165.700 99.098  47.062 1.00   19.16 ? 115  ARG G NE  1 
ATOM   7538  C  CZ  . ARG G  1 116 ? 164.600 99.769  46.729 1.00   19.72 ? 115  ARG G CZ  1 
ATOM   7539  N  NH1 . ARG G  1 116 ? 163.638 100.001 47.617 1.00   19.83 ? 115  ARG G NH1 1 
ATOM   7540  N  NH2 . ARG G  1 116 ? 164.456 100.168 45.473 1.00   19.94 ? 115  ARG G NH2 1 
ATOM   7541  N  N   . THR G  1 117 ? 167.530 98.844  53.519 1.00   15.71 ? 116  THR G N   1 
ATOM   7542  C  CA  . THR G  1 117 ? 167.983 98.473  54.860 1.00   15.11 ? 116  THR G CA  1 
ATOM   7543  C  C   . THR G  1 117 ? 168.293 96.998  54.912 1.00   14.47 ? 116  THR G C   1 
ATOM   7544  O  O   . THR G  1 117 ? 167.463 96.161  54.566 1.00   14.23 ? 116  THR G O   1 
ATOM   7545  C  CB  . THR G  1 117 ? 166.948 98.828  55.953 1.00   15.45 ? 116  THR G CB  1 
ATOM   7546  O  OG1 . THR G  1 117 ? 166.801 100.255 56.065 1.00   15.84 ? 116  THR G OG1 1 
ATOM   7547  C  CG2 . THR G  1 117 ? 167.354 98.258  57.322 1.00   15.23 ? 116  THR G CG2 1 
ATOM   7548  N  N   . LEU G  1 118 ? 169.504 96.684  55.370 1.00   13.98 ? 117  LEU G N   1 
ATOM   7549  C  CA  . LEU G  1 118 ? 169.872 95.313  55.702 1.00   13.47 ? 117  LEU G CA  1 
ATOM   7550  C  C   . LEU G  1 118 ? 169.433 95.016  57.139 1.00   13.39 ? 117  LEU G C   1 
ATOM   7551  O  O   . LEU G  1 118 ? 169.707 95.806  58.071 1.00   13.46 ? 117  LEU G O   1 
ATOM   7552  C  CB  . LEU G  1 118 ? 171.369 95.116  55.539 1.00   13.27 ? 117  LEU G CB  1 
ATOM   7553  C  CG  . LEU G  1 118 ? 171.927 93.716  55.718 1.00   13.17 ? 117  LEU G CG  1 
ATOM   7554  C  CD1 . LEU G  1 118 ? 171.364 92.793  54.639 1.00   12.93 ? 117  LEU G CD1 1 
ATOM   7555  C  CD2 . LEU G  1 118 ? 173.469 93.740  55.704 1.00   13.11 ? 117  LEU G CD2 1 
ATOM   7556  N  N   . VAL G  1 119 ? 168.786 93.868  57.324 1.00   13.16 ? 118  VAL G N   1 
ATOM   7557  C  CA  . VAL G  1 119 ? 168.235 93.473  58.634 1.00   13.30 ? 118  VAL G CA  1 
ATOM   7558  C  C   . VAL G  1 119 ? 168.690 92.074  59.026 1.00   13.22 ? 118  VAL G C   1 
ATOM   7559  O  O   . VAL G  1 119 ? 168.540 91.151  58.246 1.00   13.06 ? 118  VAL G O   1 
ATOM   7560  C  CB  . VAL G  1 119 ? 166.687 93.433  58.611 1.00   13.34 ? 118  VAL G CB  1 
ATOM   7561  C  CG1 . VAL G  1 119 ? 166.122 93.002  59.984 1.00   13.36 ? 118  VAL G CG1 1 
ATOM   7562  C  CG2 . VAL G  1 119 ? 166.117 94.786  58.173 1.00   13.48 ? 118  VAL G CG2 1 
ATOM   7563  N  N   . VAL G  1 120 ? 169.250 91.924  60.225 1.00   13.47 ? 119  VAL G N   1 
ATOM   7564  C  CA  . VAL G  1 120 ? 169.430 90.601  60.831 1.00   13.62 ? 119  VAL G CA  1 
ATOM   7565  C  C   . VAL G  1 120 ? 168.344 90.331  61.876 1.00   14.09 ? 119  VAL G C   1 
ATOM   7566  O  O   . VAL G  1 120 ? 167.966 91.228  62.660 1.00   14.31 ? 119  VAL G O   1 
ATOM   7567  C  CB  . VAL G  1 120 ? 170.875 90.415  61.371 1.00   13.59 ? 119  VAL G CB  1 
ATOM   7568  C  CG1 . VAL G  1 120 ? 171.205 91.407  62.496 1.00   13.64 ? 119  VAL G CG1 1 
ATOM   7569  C  CG2 . VAL G  1 120 ? 171.151 88.949  61.743 1.00   13.27 ? 119  VAL G CG2 1 
ATOM   7570  N  N   . HIS G  1 121 ? 167.839 89.101  61.869 1.00   14.58 ? 120  HIS G N   1 
ATOM   7571  C  CA  . HIS G  1 121 ? 166.625 88.714  62.581 1.00   15.35 ? 120  HIS G CA  1 
ATOM   7572  C  C   . HIS G  1 121 ? 166.825 87.840  63.788 1.00   16.07 ? 120  HIS G C   1 
ATOM   7573  O  O   . HIS G  1 121 ? 167.876 87.244  63.980 1.00   16.18 ? 120  HIS G O   1 
ATOM   7574  C  CB  . HIS G  1 121 ? 165.663 87.999  61.631 1.00   15.35 ? 120  HIS G CB  1 
ATOM   7575  C  CG  . HIS G  1 121 ? 164.875 88.930  60.754 1.00   15.41 ? 120  HIS G CG  1 
ATOM   7576  N  ND1 . HIS G  1 121 ? 163.732 89.520  61.168 1.00   15.70 ? 120  HIS G ND1 1 
ATOM   7577  C  CD2 . HIS G  1 121 ? 165.098 89.357  59.449 1.00   15.21 ? 120  HIS G CD2 1 
ATOM   7578  C  CE1 . HIS G  1 121 ? 163.252 90.290  60.184 1.00   15.81 ? 120  HIS G CE1 1 
ATOM   7579  N  NE2 . HIS G  1 121 ? 164.114 90.214  59.136 1.00   15.66 ? 120  HIS G NE2 1 
ATOM   7580  N  N   . GLU G  1 122 ? 165.781 87.765  64.615 1.00   17.24 ? 121  GLU G N   1 
ATOM   7581  C  CA  . GLU G  1 122 ? 165.775 87.014  65.876 1.00   18.21 ? 121  GLU G CA  1 
ATOM   7582  C  C   . GLU G  1 122 ? 165.872 85.501  65.647 1.00   17.82 ? 121  GLU G C   1 
ATOM   7583  O  O   . GLU G  1 122 ? 166.605 84.790  66.355 1.00   17.45 ? 121  GLU G O   1 
ATOM   7584  C  CB  . GLU G  1 122 ? 164.467 87.350  66.591 1.00   20.21 ? 121  GLU G CB  1 
ATOM   7585  C  CG  . GLU G  1 122 ? 164.140 86.643  67.913 1.00   22.05 ? 121  GLU G CG  1 
ATOM   7586  C  CD  . GLU G  1 122 ? 162.623 86.664  68.236 1.00   24.71 ? 121  GLU G CD  1 
ATOM   7587  O  OE1 . GLU G  1 122 ? 161.753 87.103  67.403 1.00   25.45 ? 121  GLU G OE1 1 
ATOM   7588  O  OE2 . GLU G  1 122 ? 162.271 86.185  69.344 1.00   29.19 ? 121  GLU G OE2 1 
ATOM   7589  N  N   . LYS G  1 123 ? 165.130 85.021  64.658 1.00   17.42 ? 122  LYS G N   1 
ATOM   7590  C  CA  . LYS G  1 123 ? 164.973 83.575  64.418 1.00   17.44 ? 122  LYS G CA  1 
ATOM   7591  C  C   . LYS G  1 123 ? 165.499 83.158  63.045 1.00   16.62 ? 122  LYS G C   1 
ATOM   7592  O  O   . LYS G  1 123 ? 165.833 83.997  62.201 1.00   15.86 ? 122  LYS G O   1 
ATOM   7593  C  CB  . LYS G  1 123 ? 163.490 83.190  64.511 1.00   18.24 ? 122  LYS G CB  1 
ATOM   7594  C  CG  . LYS G  1 123 ? 162.821 83.623  65.808 1.00   19.25 ? 122  LYS G CG  1 
ATOM   7595  C  CD  . LYS G  1 123 ? 161.464 82.963  66.021 1.00   20.40 ? 122  LYS G CD  1 
ATOM   7596  C  CE  . LYS G  1 123 ? 160.330 83.768  65.433 1.00   21.39 ? 122  LYS G CE  1 
ATOM   7597  N  NZ  . LYS G  1 123 ? 158.982 83.182  65.800 1.00   22.90 ? 122  LYS G NZ  1 
ATOM   7598  N  N   . ALA G  1 124 ? 165.524 81.844  62.837 1.00   16.09 ? 123  ALA G N   1 
ATOM   7599  C  CA  . ALA G  1 124 ? 165.867 81.248  61.554 1.00   15.40 ? 123  ALA G CA  1 
ATOM   7600  C  C   . ALA G  1 124 ? 164.805 81.597  60.498 1.00   15.00 ? 123  ALA G C   1 
ATOM   7601  O  O   . ALA G  1 124 ? 163.609 81.639  60.791 1.00   15.16 ? 123  ALA G O   1 
ATOM   7602  C  CB  . ALA G  1 124 ? 166.005 79.730  61.708 1.00   15.10 ? 123  ALA G CB  1 
ATOM   7603  N  N   . ASP G  1 125 ? 165.261 81.917  59.290 1.00   14.50 ? 124  ASP G N   1 
ATOM   7604  C  CA  . ASP G  1 125 ? 164.402 82.033  58.127 1.00   14.33 ? 124  ASP G CA  1 
ATOM   7605  C  C   . ASP G  1 125 ? 164.104 80.594  57.640 1.00   14.26 ? 124  ASP G C   1 
ATOM   7606  O  O   . ASP G  1 125 ? 165.033 79.838  57.338 1.00   14.25 ? 124  ASP G O   1 
ATOM   7607  C  CB  . ASP G  1 125 ? 165.172 82.818  57.044 1.00   14.19 ? 124  ASP G CB  1 
ATOM   7608  C  CG  . ASP G  1 125 ? 164.333 83.183  55.831 1.00   14.21 ? 124  ASP G CG  1 
ATOM   7609  O  OD1 . ASP G  1 125 ? 163.364 82.461  55.495 1.00   14.08 ? 124  ASP G OD1 1 
ATOM   7610  O  OD2 . ASP G  1 125 ? 164.683 84.210  55.190 1.00   14.18 ? 124  ASP G OD2 1 
ATOM   7611  N  N   . ASP G  1 126 ? 162.837 80.229  57.527 1.00   14.33 ? 125  ASP G N   1 
ATOM   7612  C  CA  . ASP G  1 126 ? 162.459 78.890  57.045 1.00   14.40 ? 125  ASP G CA  1 
ATOM   7613  C  C   . ASP G  1 126 ? 162.452 78.790  55.495 1.00   14.19 ? 125  ASP G C   1 
ATOM   7614  O  O   . ASP G  1 126 ? 162.057 77.768  54.912 1.00   14.15 ? 125  ASP G O   1 
ATOM   7615  C  CB  . ASP G  1 126 ? 161.136 78.429  57.662 1.00   14.73 ? 125  ASP G CB  1 
ATOM   7616  C  CG  . ASP G  1 126 ? 159.919 79.225  57.168 1.00   14.97 ? 125  ASP G CG  1 
ATOM   7617  O  OD1 . ASP G  1 126 ? 159.985 79.940  56.143 1.00   14.69 ? 125  ASP G OD1 1 
ATOM   7618  O  OD2 . ASP G  1 126 ? 158.861 79.123  57.852 1.00   15.54 ? 125  ASP G OD2 1 
ATOM   7619  N  N   . LEU G  1 127 ? 162.909 79.855  54.838 1.00   13.92 ? 126  LEU G N   1 
ATOM   7620  C  CA  . LEU G  1 127 ? 163.172 79.846  53.399 1.00   13.88 ? 126  LEU G CA  1 
ATOM   7621  C  C   . LEU G  1 127 ? 161.885 79.593  52.600 1.00   14.10 ? 126  LEU G C   1 
ATOM   7622  O  O   . LEU G  1 127 ? 161.913 79.105  51.480 1.00   14.04 ? 126  LEU G O   1 
ATOM   7623  C  CB  . LEU G  1 127 ? 164.303 78.858  53.019 1.00   13.84 ? 126  LEU G CB  1 
ATOM   7624  C  CG  . LEU G  1 127 ? 165.612 79.003  53.841 1.00   13.89 ? 126  LEU G CG  1 
ATOM   7625  C  CD1 . LEU G  1 127 ? 166.622 77.915  53.481 1.00   14.15 ? 126  LEU G CD1 1 
ATOM   7626  C  CD2 . LEU G  1 127 ? 166.226 80.417  53.694 1.00   13.49 ? 126  LEU G CD2 1 
ATOM   7627  N  N   . GLY G  1 128 ? 160.749 79.975  53.183 1.00   14.32 ? 127  GLY G N   1 
ATOM   7628  C  CA  . GLY G  1 128 ? 159.463 79.783  52.511 1.00   14.61 ? 127  GLY G CA  1 
ATOM   7629  C  C   . GLY G  1 128 ? 158.894 78.394  52.552 1.00   14.78 ? 127  GLY G C   1 
ATOM   7630  O  O   . GLY G  1 128 ? 157.895 78.119  51.890 1.00   15.27 ? 127  GLY G O   1 
ATOM   7631  N  N   . LYS G  1 129 ? 159.479 77.522  53.351 1.00   14.77 ? 128  LYS G N   1 
ATOM   7632  C  CA  . LYS G  1 129 ? 159.046 76.121  53.427 1.00   15.11 ? 128  LYS G CA  1 
ATOM   7633  C  C   . LYS G  1 129 ? 158.278 75.811  54.725 1.00   14.99 ? 128  LYS G C   1 
ATOM   7634  O  O   . LYS G  1 129 ? 158.171 74.658  55.139 1.00   15.22 ? 128  LYS G O   1 
ATOM   7635  C  CB  . LYS G  1 129 ? 160.270 75.211  53.310 1.00   15.38 ? 128  LYS G CB  1 
ATOM   7636  C  CG  . LYS G  1 129 ? 161.172 75.552  52.114 1.00   15.68 ? 128  LYS G CG  1 
ATOM   7637  C  CD  . LYS G  1 129 ? 162.507 74.800  52.151 1.00   15.97 ? 128  LYS G CD  1 
ATOM   7638  C  CE  . LYS G  1 129 ? 162.328 73.315  51.906 1.00   16.83 ? 128  LYS G CE  1 
ATOM   7639  N  NZ  . LYS G  1 129 ? 163.642 72.606  51.806 1.00   17.06 ? 128  LYS G NZ  1 
ATOM   7640  N  N   . GLY G  1 130 ? 157.773 76.839  55.384 1.00   14.75 ? 129  GLY G N   1 
ATOM   7641  C  CA  . GLY G  1 130 ? 157.126 76.653  56.699 1.00   14.87 ? 129  GLY G CA  1 
ATOM   7642  C  C   . GLY G  1 130 ? 155.644 76.349  56.665 1.00   15.08 ? 129  GLY G C   1 
ATOM   7643  O  O   . GLY G  1 130 ? 155.061 75.997  57.694 1.00   15.31 ? 129  GLY G O   1 
ATOM   7644  N  N   . GLY G  1 131 ? 155.014 76.550  55.517 1.00   15.08 ? 130  GLY G N   1 
ATOM   7645  C  CA  . GLY G  1 131 ? 153.606 76.164  55.321 1.00   15.51 ? 130  GLY G CA  1 
ATOM   7646  C  C   . GLY G  1 131 ? 152.518 77.024  55.946 1.00   15.84 ? 130  GLY G C   1 
ATOM   7647  O  O   . GLY G  1 131 ? 151.332 76.693  55.842 1.00   16.10 ? 130  GLY G O   1 
ATOM   7648  N  N   . ASN G  1 132 ? 152.909 78.111  56.602 1.00   15.83 ? 131  ASN G N   1 
ATOM   7649  C  CA  . ASN G  1 132 ? 151.967 79.081  57.120 1.00   16.44 ? 131  ASN G CA  1 
ATOM   7650  C  C   . ASN G  1 132 ? 152.056 80.402  56.353 1.00   16.76 ? 131  ASN G C   1 
ATOM   7651  O  O   . ASN G  1 132 ? 152.947 80.592  55.490 1.00   16.58 ? 131  ASN G O   1 
ATOM   7652  C  CB  . ASN G  1 132 ? 152.095 79.290  58.651 1.00   16.47 ? 131  ASN G CB  1 
ATOM   7653  C  CG  . ASN G  1 132 ? 153.411 79.925  59.072 1.00   15.96 ? 131  ASN G CG  1 
ATOM   7654  O  OD1 . ASN G  1 132 ? 154.351 79.987  58.308 1.00   15.60 ? 131  ASN G OD1 1 
ATOM   7655  N  ND2 . ASN G  1 132 ? 153.477 80.378  60.322 1.00   16.13 ? 131  ASN G ND2 1 
ATOM   7656  N  N   . GLU G  1 133 ? 151.112 81.297  56.629 1.00   17.48 ? 132  GLU G N   1 
ATOM   7657  C  CA  . GLU G  1 133 ? 151.059 82.576  55.927 1.00   17.86 ? 132  GLU G CA  1 
ATOM   7658  C  C   . GLU G  1 133 ? 152.357 83.301  56.087 1.00   17.36 ? 132  GLU G C   1 
ATOM   7659  O  O   . GLU G  1 133 ? 152.889 83.856  55.135 1.00   16.99 ? 132  GLU G O   1 
ATOM   7660  C  CB  . GLU G  1 133 ? 149.932 83.468  56.447 1.00   18.72 ? 132  GLU G CB  1 
ATOM   7661  C  CG  . GLU G  1 133 ? 148.599 82.790  56.380 1.00   19.91 ? 132  GLU G CG  1 
ATOM   7662  C  CD  . GLU G  1 133 ? 147.431 83.689  56.738 1.00   21.07 ? 132  GLU G CD  1 
ATOM   7663  O  OE1 . GLU G  1 133 ? 147.643 84.816  57.179 1.00   22.23 ? 132  GLU G OE1 1 
ATOM   7664  O  OE2 . GLU G  1 133 ? 146.299 83.259  56.572 1.00   22.44 ? 132  GLU G OE2 1 
ATOM   7665  N  N   . GLU G  1 134 ? 152.876 83.288  57.306 1.00   17.57 ? 133  GLU G N   1 
ATOM   7666  C  CA  . GLU G  1 134 ? 154.044 84.074  57.634 1.00   17.58 ? 133  GLU G CA  1 
ATOM   7667  C  C   . GLU G  1 134 ? 155.288 83.596  56.858 1.00   17.09 ? 133  GLU G C   1 
ATOM   7668  O  O   . GLU G  1 134 ? 156.131 84.395  56.485 1.00   16.84 ? 133  GLU G O   1 
ATOM   7669  C  CB  . GLU G  1 134 ? 154.248 84.044  59.140 1.00   18.11 ? 133  GLU G CB  1 
ATOM   7670  C  CG  . GLU G  1 134 ? 155.287 84.985  59.704 1.00   18.21 ? 133  GLU G CG  1 
ATOM   7671  C  CD  . GLU G  1 134 ? 154.962 86.438  59.465 1.00   18.75 ? 133  GLU G CD  1 
ATOM   7672  O  OE1 . GLU G  1 134 ? 153.783 86.848  59.507 1.00   19.48 ? 133  GLU G OE1 1 
ATOM   7673  O  OE2 . GLU G  1 134 ? 155.927 87.176  59.239 1.00   19.09 ? 133  GLU G OE2 1 
ATOM   7674  N  N   . SER G  1 135 ? 155.386 82.302  56.587 1.00   16.90 ? 134  SER G N   1 
ATOM   7675  C  CA  . SER G  1 135 ? 156.509 81.783  55.826 1.00   16.52 ? 134  SER G CA  1 
ATOM   7676  C  C   . SER G  1 135 ? 156.633 82.438  54.458 1.00   16.69 ? 134  SER G C   1 
ATOM   7677  O  O   . SER G  1 135 ? 157.754 82.665  53.991 1.00   16.20 ? 134  SER G O   1 
ATOM   7678  C  CB  . SER G  1 135 ? 156.367 80.262  55.645 1.00   16.42 ? 134  SER G CB  1 
ATOM   7679  O  OG  . SER G  1 135 ? 157.492 79.712  54.973 1.00   15.81 ? 134  SER G OG  1 
ATOM   7680  N  N   . THR G  1 136 ? 155.483 82.733  53.831 1.00   17.24 ? 135  THR G N   1 
ATOM   7681  C  CA  . THR G  1 136 ? 155.438 83.348  52.487 1.00   17.68 ? 135  THR G CA  1 
ATOM   7682  C  C   . THR G  1 136 ? 155.740 84.835  52.503 1.00   17.75 ? 135  THR G C   1 
ATOM   7683  O  O   . THR G  1 136 ? 155.898 85.433  51.445 1.00   17.85 ? 135  THR G O   1 
ATOM   7684  C  CB  . THR G  1 136 ? 154.045 83.168  51.816 1.00   18.19 ? 135  THR G CB  1 
ATOM   7685  O  OG1 . THR G  1 136 ? 153.093 84.043  52.439 1.00   18.86 ? 135  THR G OG1 1 
ATOM   7686  C  CG2 . THR G  1 136 ? 153.527 81.757  51.967 1.00   18.82 ? 135  THR G CG2 1 
ATOM   7687  N  N   . LYS G  1 137 ? 155.848 85.415  53.701 1.00   17.94 ? 136  LYS G N   1 
ATOM   7688  C  CA  . LYS G  1 137 ? 156.171 86.828  53.883 1.00   18.18 ? 136  LYS G CA  1 
ATOM   7689  C  C   . LYS G  1 137 ? 157.561 87.062  54.448 1.00   17.33 ? 136  LYS G C   1 
ATOM   7690  O  O   . LYS G  1 137 ? 158.323 87.843  53.890 1.00   17.02 ? 136  LYS G O   1 
ATOM   7691  C  CB  . LYS G  1 137 ? 155.173 87.485  54.833 1.00   18.99 ? 136  LYS G CB  1 
ATOM   7692  C  CG  . LYS G  1 137 ? 153.726 87.366  54.404 1.00   20.36 ? 136  LYS G CG  1 
ATOM   7693  C  CD  . LYS G  1 137 ? 152.834 88.083  55.410 1.00   21.67 ? 136  LYS G CD  1 
ATOM   7694  C  CE  . LYS G  1 137 ? 151.363 87.920  55.081 1.00   23.35 ? 136  LYS G CE  1 
ATOM   7695  N  NZ  . LYS G  1 137 ? 150.509 88.301  56.267 1.00   24.69 ? 136  LYS G NZ  1 
ATOM   7696  N  N   . THR G  1 138 ? 157.864 86.430  55.582 1.00   16.75 ? 137  THR G N   1 
ATOM   7697  C  CA  . THR G  1 138 ? 159.095 86.705  56.303 1.00   16.25 ? 137  THR G CA  1 
ATOM   7698  C  C   . THR G  1 138 ? 159.972 85.489  56.561 1.00   15.69 ? 137  THR G C   1 
ATOM   7699  O  O   . THR G  1 138 ? 161.008 85.595  57.183 1.00   15.42 ? 137  THR G O   1 
ATOM   7700  C  CB  . THR G  1 138 ? 158.762 87.330  57.672 1.00   16.68 ? 137  THR G CB  1 
ATOM   7701  O  OG1 . THR G  1 138 ? 158.099 86.365  58.491 1.00   16.92 ? 137  THR G OG1 1 
ATOM   7702  C  CG2 . THR G  1 138 ? 157.862 88.584  57.513 1.00   17.06 ? 137  THR G CG2 1 
ATOM   7703  N  N   . GLY G  1 139 ? 159.519 84.312  56.147 1.00   15.52 ? 138  GLY G N   1 
ATOM   7704  C  CA  . GLY G  1 139 ? 160.115 83.070  56.573 1.00   15.26 ? 138  GLY G CA  1 
ATOM   7705  C  C   . GLY G  1 139 ? 160.064 82.774  58.068 1.00   15.30 ? 138  GLY G C   1 
ATOM   7706  O  O   . GLY G  1 139 ? 160.840 81.935  58.528 1.00   15.02 ? 138  GLY G O   1 
ATOM   7707  N  N   . ASN G  1 140 ? 159.143 83.411  58.813 1.00   15.48 ? 139  ASN G N   1 
ATOM   7708  C  CA  . ASN G  1 140 ? 159.036 83.254  60.283 1.00   15.71 ? 139  ASN G CA  1 
ATOM   7709  C  C   . ASN G  1 140 ? 160.334 83.643  61.020 1.00   15.60 ? 139  ASN G C   1 
ATOM   7710  O  O   . ASN G  1 140 ? 160.672 83.042  62.038 1.00   15.74 ? 139  ASN G O   1 
ATOM   7711  C  CB  . ASN G  1 140 ? 158.596 81.812  60.672 1.00   15.86 ? 139  ASN G CB  1 
ATOM   7712  C  CG  . ASN G  1 140 ? 157.169 81.500  60.231 1.00   16.23 ? 139  ASN G CG  1 
ATOM   7713  O  OD1 . ASN G  1 140 ? 156.217 81.982  60.830 1.00   16.69 ? 139  ASN G OD1 1 
ATOM   7714  N  ND2 . ASN G  1 140 ? 157.015 80.703  59.148 1.00   16.25 ? 139  ASN G ND2 1 
ATOM   7715  N  N   . ALA G  1 141 ? 161.064 84.623  60.475 1.00   15.31 ? 140  ALA G N   1 
ATOM   7716  C  CA  . ALA G  1 141 ? 162.342 85.080  61.040 1.00   15.33 ? 140  ALA G CA  1 
ATOM   7717  C  C   . ALA G  1 141 ? 162.176 85.960  62.287 1.00   15.71 ? 140  ALA G C   1 
ATOM   7718  O  O   . ALA G  1 141 ? 163.142 86.235  62.997 1.00   15.65 ? 140  ALA G O   1 
ATOM   7719  C  CB  . ALA G  1 141 ? 163.203 85.795  59.974 1.00   14.81 ? 140  ALA G CB  1 
ATOM   7720  N  N   . GLY G  1 142 ? 160.954 86.374  62.570 1.00   16.52 ? 141  GLY G N   1 
ATOM   7721  C  CA  . GLY G  1 142 ? 160.656 87.111  63.788 1.00   17.04 ? 141  GLY G CA  1 
ATOM   7722  C  C   . GLY G  1 142 ? 161.257 88.499  63.802 1.00   17.34 ? 141  GLY G C   1 
ATOM   7723  O  O   . GLY G  1 142 ? 161.439 89.149  62.747 1.00   16.75 ? 141  GLY G O   1 
ATOM   7724  N  N   . SER G  1 143 ? 161.578 88.953  65.013 1.00   17.96 ? 142  SER G N   1 
ATOM   7725  C  CA  . SER G  1 143 ? 161.872 90.353  65.220 1.00   18.33 ? 142  SER G CA  1 
ATOM   7726  C  C   . SER G  1 143 ? 163.208 90.772  64.586 1.00   17.72 ? 142  SER G C   1 
ATOM   7727  O  O   . SER G  1 143 ? 164.042 89.939  64.209 1.00   17.51 ? 142  SER G O   1 
ATOM   7728  C  CB  . SER G  1 143 ? 161.772 90.697  66.716 1.00   19.17 ? 142  SER G CB  1 
ATOM   7729  O  OG  . SER G  1 143 ? 163.010 90.461  67.337 1.00   20.17 ? 142  SER G OG  1 
ATOM   7730  N  N   . ARG G  1 144 ? 163.373 92.080  64.443 1.00   17.71 ? 143  ARG G N   1 
ATOM   7731  C  CA  . ARG G  1 144 ? 164.532 92.704  63.816 1.00   17.19 ? 143  ARG G CA  1 
ATOM   7732  C  C   . ARG G  1 144 ? 165.519 93.132  64.898 1.00   17.20 ? 143  ARG G C   1 
ATOM   7733  O  O   . ARG G  1 144 ? 165.279 94.086  65.608 1.00   17.98 ? 143  ARG G O   1 
ATOM   7734  C  CB  . ARG G  1 144 ? 164.079 93.911  62.991 1.00   17.04 ? 143  ARG G CB  1 
ATOM   7735  C  CG  . ARG G  1 144 ? 162.841 93.621  62.180 1.00   17.15 ? 143  ARG G CG  1 
ATOM   7736  C  CD  . ARG G  1 144 ? 162.412 94.758  61.279 1.00   17.34 ? 143  ARG G CD  1 
ATOM   7737  N  NE  . ARG G  1 144 ? 161.285 94.304  60.491 1.00   17.44 ? 143  ARG G NE  1 
ATOM   7738  C  CZ  . ARG G  1 144 ? 160.701 94.970  59.507 1.00   17.62 ? 143  ARG G CZ  1 
ATOM   7739  N  NH1 . ARG G  1 144 ? 161.104 96.192  59.145 1.00   17.71 ? 143  ARG G NH1 1 
ATOM   7740  N  NH2 . ARG G  1 144 ? 159.690 94.395  58.885 1.00   17.78 ? 143  ARG G NH2 1 
ATOM   7741  N  N   . LEU G  1 145 ? 166.625 92.424  65.024 1.00   16.90 ? 144  LEU G N   1 
ATOM   7742  C  CA  . LEU G  1 145 ? 167.560 92.636  66.104 1.00   17.10 ? 144  LEU G CA  1 
ATOM   7743  C  C   . LEU G  1 145 ? 168.550 93.751  65.839 1.00   17.33 ? 144  LEU G C   1 
ATOM   7744  O  O   . LEU G  1 145 ? 168.929 94.429  66.758 1.00   17.82 ? 144  LEU G O   1 
ATOM   7745  C  CB  . LEU G  1 145 ? 168.320 91.359  66.409 1.00   17.02 ? 144  LEU G CB  1 
ATOM   7746  C  CG  . LEU G  1 145 ? 167.450 90.191  66.912 1.00   17.15 ? 144  LEU G CG  1 
ATOM   7747  C  CD1 . LEU G  1 145 ? 168.358 89.109  67.426 1.00   17.21 ? 144  LEU G CD1 1 
ATOM   7748  C  CD2 . LEU G  1 145 ? 166.456 90.622  67.997 1.00   17.33 ? 144  LEU G CD2 1 
ATOM   7749  N  N   . ALA G  1 146 ? 168.987 93.920  64.593 1.00   17.18 ? 145  ALA G N   1 
ATOM   7750  C  CA  . ALA G  1 146 ? 169.819 95.067  64.213 1.00   17.25 ? 145  ALA G CA  1 
ATOM   7751  C  C   . ALA G  1 146 ? 169.616 95.340  62.731 1.00   17.08 ? 145  ALA G C   1 
ATOM   7752  O  O   . ALA G  1 146 ? 169.201 94.464  61.995 1.00   16.99 ? 145  ALA G O   1 
ATOM   7753  C  CB  . ALA G  1 146 ? 171.287 94.818  64.517 1.00   16.96 ? 145  ALA G CB  1 
ATOM   7754  N  N   . CYS G  1 147 ? 169.935 96.548  62.305 1.00   17.28 ? 146  CYS G N   1 
ATOM   7755  C  CA  . CYS G  1 147 ? 169.768 96.946  60.930 1.00   17.29 ? 146  CYS G CA  1 
ATOM   7756  C  C   . CYS G  1 147 ? 170.600 98.189  60.621 1.00   17.36 ? 146  CYS G C   1 
ATOM   7757  O  O   . CYS G  1 147 ? 171.178 98.812  61.505 1.00   17.77 ? 146  CYS G O   1 
ATOM   7758  C  CB  . CYS G  1 147 ? 168.294 97.208  60.640 1.00   17.75 ? 146  CYS G CB  1 
ATOM   7759  S  SG  . CYS G  1 147 ? 167.555 98.562  61.592 1.00   18.63 ? 146  CYS G SG  1 
ATOM   7760  N  N   . GLY G  1 148 ? 170.686 98.527  59.357 1.00   17.14 ? 147  GLY G N   1 
ATOM   7761  C  CA  . GLY G  1 148 ? 171.436 99.724  58.930 1.00   17.19 ? 147  GLY G CA  1 
ATOM   7762  C  C   . GLY G  1 148 ? 171.069 99.985  57.499 1.00   16.87 ? 147  GLY G C   1 
ATOM   7763  O  O   . GLY G  1 148 ? 170.609 99.068  56.799 1.00   16.40 ? 147  GLY G O   1 
ATOM   7764  N  N   . VAL G  1 149 ? 171.268 101.224 57.072 1.00   16.89 ? 148  VAL G N   1 
ATOM   7765  C  CA  . VAL G  1 149 ? 171.053 101.610 55.688 1.00   16.72 ? 148  VAL G CA  1 
ATOM   7766  C  C   . VAL G  1 149 ? 172.281 101.271 54.866 1.00   16.51 ? 148  VAL G C   1 
ATOM   7767  O  O   . VAL G  1 149 ? 173.395 101.499 55.298 1.00   16.73 ? 148  VAL G O   1 
ATOM   7768  C  CB  . VAL G  1 149 ? 170.707 103.114 55.559 1.00   17.02 ? 148  VAL G CB  1 
ATOM   7769  C  CG1 . VAL G  1 149 ? 170.443 103.467 54.100 1.00   16.85 ? 148  VAL G CG1 1 
ATOM   7770  C  CG2 . VAL G  1 149 ? 169.501 103.457 56.424 1.00   16.98 ? 148  VAL G CG2 1 
ATOM   7771  N  N   . ILE G  1 150 ? 172.075 100.672 53.698 1.00   16.32 ? 149  ILE G N   1 
ATOM   7772  C  CA  . ILE G  1 150 ? 173.183 100.259 52.843 1.00   16.41 ? 149  ILE G CA  1 
ATOM   7773  C  C   . ILE G  1 150 ? 173.686 101.450 52.027 1.00   16.98 ? 149  ILE G C   1 
ATOM   7774  O  O   . ILE G  1 150 ? 172.930 102.064 51.269 1.00   16.66 ? 149  ILE G O   1 
ATOM   7775  C  CB  . ILE G  1 150 ? 172.761 99.130  51.897 1.00   16.07 ? 149  ILE G CB  1 
ATOM   7776  C  CG1 . ILE G  1 150 ? 172.305 97.900  52.697 1.00   15.77 ? 149  ILE G CG1 1 
ATOM   7777  C  CG2 . ILE G  1 150 ? 173.909 98.784  50.948 1.00   16.10 ? 149  ILE G CG2 1 
ATOM   7778  C  CD1 . ILE G  1 150 ? 171.507 96.887  51.894 1.00   15.56 ? 149  ILE G CD1 1 
ATOM   7779  N  N   . GLY G  1 151 ? 174.965 101.777 52.199 1.00   17.78 ? 150  GLY G N   1 
ATOM   7780  C  CA  . GLY G  1 151 ? 175.539 102.958 51.564 1.00   18.78 ? 150  GLY G CA  1 
ATOM   7781  C  C   . GLY G  1 151 ? 176.664 102.633 50.597 1.00   19.41 ? 150  GLY G C   1 
ATOM   7782  O  O   . GLY G  1 151 ? 177.365 101.623 50.752 1.00   18.86 ? 150  GLY G O   1 
ATOM   7783  N  N   . ILE G  1 152 ? 176.847 103.525 49.619 1.00   20.43 ? 151  ILE G N   1 
ATOM   7784  C  CA  . ILE G  1 152 ? 177.934 103.432 48.646 1.00   21.37 ? 151  ILE G CA  1 
ATOM   7785  C  C   . ILE G  1 152 ? 179.282 103.503 49.371 1.00   21.82 ? 151  ILE G C   1 
ATOM   7786  O  O   . ILE G  1 152 ? 179.509 104.394 50.181 1.00   21.88 ? 151  ILE G O   1 
ATOM   7787  C  CB  . ILE G  1 152 ? 177.864 104.575 47.596 1.00   22.20 ? 151  ILE G CB  1 
ATOM   7788  C  CG1 . ILE G  1 152 ? 176.546 104.532 46.819 1.00   22.88 ? 151  ILE G CG1 1 
ATOM   7789  C  CG2 . ILE G  1 152 ? 179.009 104.452 46.612 1.00   22.76 ? 151  ILE G CG2 1 
ATOM   7790  C  CD1 . ILE G  1 152 ? 176.088 105.887 46.259 1.00   23.48 ? 151  ILE G CD1 1 
ATOM   7791  N  N   . ALA G  1 153 ? 180.185 102.585 49.053 1.00   22.58 ? 152  ALA G N   1 
ATOM   7792  C  CA  . ALA G  1 153 ? 181.487 102.537 49.693 1.00   24.14 ? 152  ALA G CA  1 
ATOM   7793  C  C   . ALA G  1 153 ? 182.579 102.799 48.669 1.00   26.28 ? 152  ALA G C   1 
ATOM   7794  O  O   . ALA G  1 153 ? 182.348 102.689 47.454 1.00   26.43 ? 152  ALA G O   1 
ATOM   7795  C  CB  . ALA G  1 153 ? 181.693 101.178 50.366 1.00   23.12 ? 152  ALA G CB  1 
ATOM   7796  N  N   . GLN G  1 154 ? 183.771 103.124 49.164 1.00   28.74 ? 153  GLN G N   1 
ATOM   7797  C  CA  . GLN G  1 154 ? 184.907 103.469 48.311 1.00   31.64 ? 153  GLN G CA  1 
ATOM   7798  C  C   . GLN G  1 154 ? 185.575 102.218 47.803 1.00   33.82 ? 153  GLN G C   1 
ATOM   7799  O  O   . GLN G  1 154 ? 186.008 102.120 46.640 1.00   36.37 ? 153  GLN G O   1 
ATOM   7800  C  CB  . GLN G  1 154 ? 185.945 104.269 49.093 1.00   33.06 ? 153  GLN G CB  1 
ATOM   7801  C  CG  . GLN G  1 154 ? 187.136 104.729 48.275 1.00   33.97 ? 153  GLN G CG  1 
ATOM   7802  C  CD  . GLN G  1 154 ? 188.056 105.615 49.099 1.00   35.54 ? 153  GLN G CD  1 
ATOM   7803  O  OE1 . GLN G  1 154 ? 188.811 105.131 49.948 1.00   36.42 ? 153  GLN G OE1 1 
ATOM   7804  N  NE2 . GLN G  1 154 ? 187.973 106.913 48.877 1.00   35.33 ? 153  GLN G NE2 1 
ATOM   7805  O  OXT . GLN G  1 154 ? 185.719 101.295 48.598 1.00   36.10 ? 153  GLN G OXT 1 
ATOM   7806  N  N   . ALA H  1 2   ? 185.177 47.626  43.892 1.00   41.73 ? 1    ALA H N   1 
ATOM   7807  C  CA  . ALA H  1 2   ? 184.784 48.022  42.490 1.00   39.91 ? 1    ALA H CA  1 
ATOM   7808  C  C   . ALA H  1 2   ? 183.269 47.938  42.275 1.00   35.07 ? 1    ALA H C   1 
ATOM   7809  O  O   . ALA H  1 2   ? 182.694 48.772  41.603 1.00   37.31 ? 1    ALA H O   1 
ATOM   7810  C  CB  . ALA H  1 2   ? 185.530 47.170  41.469 1.00   40.06 ? 1    ALA H CB  1 
ATOM   7811  N  N   . THR H  1 3   ? 182.618 46.919  42.813 1.00   32.26 ? 2    THR H N   1 
ATOM   7812  C  CA  . THR H  1 3   ? 181.159 46.962  42.923 1.00   29.37 ? 2    THR H CA  1 
ATOM   7813  C  C   . THR H  1 3   ? 180.709 46.999  44.382 1.00   25.97 ? 2    THR H C   1 
ATOM   7814  O  O   . THR H  1 3   ? 179.559 47.332  44.650 1.00   24.38 ? 2    THR H O   1 
ATOM   7815  C  CB  . THR H  1 3   ? 180.464 45.812  42.185 1.00   30.52 ? 2    THR H CB  1 
ATOM   7816  O  OG1 . THR H  1 3   ? 180.591 44.589  42.928 1.00   30.40 ? 2    THR H OG1 1 
ATOM   7817  C  CG2 . THR H  1 3   ? 181.054 45.637  40.797 1.00   32.96 ? 2    THR H CG2 1 
ATOM   7818  N  N   . LYS H  1 4   ? 181.601 46.641  45.306 1.00   22.99 ? 3    LYS H N   1 
ATOM   7819  C  CA  . LYS H  1 4   ? 181.306 46.691  46.730 1.00   21.46 ? 3    LYS H CA  1 
ATOM   7820  C  C   . LYS H  1 4   ? 182.456 47.261  47.540 1.00   19.36 ? 3    LYS H C   1 
ATOM   7821  O  O   . LYS H  1 4   ? 183.626 47.024  47.253 1.00   18.50 ? 3    LYS H O   1 
ATOM   7822  C  CB  . LYS H  1 4   ? 180.953 45.312  47.253 1.00   22.59 ? 3    LYS H CB  1 
ATOM   7823  C  CG  . LYS H  1 4   ? 179.573 44.847  46.786 1.00   24.50 ? 3    LYS H CG  1 
ATOM   7824  C  CD  . LYS H  1 4   ? 179.305 43.405  47.134 1.00   25.79 ? 3    LYS H CD  1 
ATOM   7825  C  CE  . LYS H  1 4   ? 177.921 43.019  46.625 1.00   27.57 ? 3    LYS H CE  1 
ATOM   7826  N  NZ  . LYS H  1 4   ? 177.574 41.596  46.891 1.00   28.82 ? 3    LYS H NZ  1 
ATOM   7827  N  N   . ALA H  1 5   ? 182.098 48.009  48.567 1.00   17.64 ? 4    ALA H N   1 
ATOM   7828  C  CA  . ALA H  1 5   ? 183.058 48.568  49.502 1.00   16.66 ? 4    ALA H CA  1 
ATOM   7829  C  C   . ALA H  1 5   ? 182.433 48.576  50.908 1.00   15.99 ? 4    ALA H C   1 
ATOM   7830  O  O   . ALA H  1 5   ? 181.222 48.356  51.075 1.00   15.76 ? 4    ALA H O   1 
ATOM   7831  C  CB  . ALA H  1 5   ? 183.463 49.976  49.066 1.00   16.22 ? 4    ALA H CB  1 
ATOM   7832  N  N   . VAL H  1 6   ? 183.280 48.791  51.909 1.00   15.32 ? 5    VAL H N   1 
ATOM   7833  C  CA  . VAL H  1 6   ? 182.865 48.753  53.281 1.00   15.11 ? 5    VAL H CA  1 
ATOM   7834  C  C   . VAL H  1 6   ? 183.727 49.702  54.133 1.00   14.97 ? 5    VAL H C   1 
ATOM   7835  O  O   . VAL H  1 6   ? 184.860 50.040  53.790 1.00   14.61 ? 5    VAL H O   1 
ATOM   7836  C  CB  . VAL H  1 6   ? 182.894 47.299  53.846 1.00   15.25 ? 5    VAL H CB  1 
ATOM   7837  C  CG1 . VAL H  1 6   ? 184.320 46.821  54.097 1.00   14.87 ? 5    VAL H CG1 1 
ATOM   7838  C  CG2 . VAL H  1 6   ? 182.076 47.216  55.131 1.00   15.12 ? 5    VAL H CG2 1 
ATOM   7839  N  N   . CYS H  1 7   ? 183.176 50.135  55.255 1.00   15.15 ? 6    CYS H N   1 
ATOM   7840  C  CA  . CYS H  1 7   ? 183.890 51.037  56.133 1.00   15.31 ? 6    CYS H CA  1 
ATOM   7841  C  C   . CYS H  1 7   ? 183.473 50.786  57.568 1.00   15.55 ? 6    CYS H C   1 
ATOM   7842  O  O   . CYS H  1 7   ? 182.281 50.737  57.875 1.00   15.27 ? 6    CYS H O   1 
ATOM   7843  C  CB  . CYS H  1 7   ? 183.606 52.484  55.743 1.00   15.36 ? 6    CYS H CB  1 
ATOM   7844  S  SG  . CYS H  1 7   ? 184.412 53.707  56.806 1.00   15.69 ? 6    CYS H SG  1 
ATOM   7845  N  N   . VAL H  1 8   ? 184.480 50.608  58.428 1.00   15.79 ? 7    VAL H N   1 
ATOM   7846  C  CA  . VAL H  1 8   ? 184.286 50.458  59.855 1.00   16.28 ? 7    VAL H CA  1 
ATOM   7847  C  C   . VAL H  1 8   ? 184.584 51.824  60.484 1.00   16.65 ? 7    VAL H C   1 
ATOM   7848  O  O   . VAL H  1 8   ? 185.699 52.337  60.381 1.00   16.47 ? 7    VAL H O   1 
ATOM   7849  C  CB  . VAL H  1 8   ? 185.217 49.355  60.440 1.00   16.40 ? 7    VAL H CB  1 
ATOM   7850  C  CG1 . VAL H  1 8   ? 185.093 49.277  61.962 1.00   16.60 ? 7    VAL H CG1 1 
ATOM   7851  C  CG2 . VAL H  1 8   ? 184.891 48.002  59.803 1.00   16.35 ? 7    VAL H CG2 1 
ATOM   7852  N  N   . LEU H  1 9   ? 183.582 52.412  61.128 1.00   17.45 ? 8    LEU H N   1 
ATOM   7853  C  CA  . LEU H  1 9   ? 183.739 53.720  61.762 1.00   18.20 ? 8    LEU H CA  1 
ATOM   7854  C  C   . LEU H  1 9   ? 184.121 53.515  63.216 1.00   18.86 ? 8    LEU H C   1 
ATOM   7855  O  O   . LEU H  1 9   ? 183.445 52.770  63.922 1.00   19.05 ? 8    LEU H O   1 
ATOM   7856  C  CB  . LEU H  1 9   ? 182.425 54.501  61.710 1.00   18.16 ? 8    LEU H CB  1 
ATOM   7857  C  CG  . LEU H  1 9   ? 181.922 54.918  60.341 1.00   18.44 ? 8    LEU H CG  1 
ATOM   7858  C  CD1 . LEU H  1 9   ? 180.458 55.317  60.342 1.00   18.65 ? 8    LEU H CD1 1 
ATOM   7859  C  CD2 . LEU H  1 9   ? 182.737 56.094  59.866 1.00   18.17 ? 8    LEU H CD2 1 
ATOM   7860  N  N   . LYS H  1 10  ? 185.166 54.194  63.659 1.00   19.94 ? 9    LYS H N   1 
ATOM   7861  C  CA  . LYS H  1 10  ? 185.545 54.234  65.076 1.00   21.72 ? 9    LYS H CA  1 
ATOM   7862  C  C   . LYS H  1 10  ? 186.026 55.628  65.432 1.00   21.89 ? 9    LYS H C   1 
ATOM   7863  O  O   . LYS H  1 10  ? 186.455 56.362  64.543 1.00   20.05 ? 9    LYS H O   1 
ATOM   7864  C  CB  . LYS H  1 10  ? 186.701 53.281  65.363 1.00   23.57 ? 9    LYS H CB  1 
ATOM   7865  C  CG  . LYS H  1 10  ? 186.373 51.817  65.123 1.00   25.75 ? 9    LYS H CG  1 
ATOM   7866  C  CD  . LYS H  1 10  ? 185.747 51.182  66.370 1.00   28.50 ? 9    LYS H CD  1 
ATOM   7867  C  CE  . LYS H  1 10  ? 185.049 49.855  66.067 1.00   29.58 ? 9    LYS H CE  1 
ATOM   7868  N  NZ  . LYS H  1 10  ? 183.824 50.140  65.257 1.00   30.07 ? 9    LYS H NZ  1 
ATOM   7869  N  N   . GLY H  1 11  ? 186.035 55.943  66.736 1.00   22.56 ? 10   GLY H N   1 
ATOM   7870  C  CA  . GLY H  1 11  ? 186.567 57.224  67.218 1.00   23.96 ? 10   GLY H CA  1 
ATOM   7871  C  C   . GLY H  1 11  ? 187.115 57.162  68.630 1.00   25.39 ? 10   GLY H C   1 
ATOM   7872  O  O   . GLY H  1 11  ? 187.295 56.071  69.168 1.00   25.77 ? 10   GLY H O   1 
ATOM   7873  N  N   . ASP H  1 12  ? 187.345 58.322  69.247 1.00   26.67 ? 11   ASP H N   1 
ATOM   7874  C  CA  . ASP H  1 12  ? 187.820 58.361  70.650 1.00   28.53 ? 11   ASP H CA  1 
ATOM   7875  C  C   . ASP H  1 12  ? 186.700 58.164  71.670 1.00   28.26 ? 11   ASP H C   1 
ATOM   7876  O  O   . ASP H  1 12  ? 186.970 57.831  72.822 1.00   29.79 ? 11   ASP H O   1 
ATOM   7877  C  CB  . ASP H  1 12  ? 188.567 59.664  70.955 1.00   30.29 ? 11   ASP H CB  1 
ATOM   7878  C  CG  . ASP H  1 12  ? 189.702 59.933  69.959 1.00   32.82 ? 11   ASP H CG  1 
ATOM   7879  O  OD1 . ASP H  1 12  ? 190.474 58.986  69.648 1.00   31.86 ? 11   ASP H OD1 1 
ATOM   7880  O  OD2 . ASP H  1 12  ? 189.796 61.089  69.470 1.00   35.80 ? 11   ASP H OD2 1 
ATOM   7881  N  N   . GLY H  1 13  ? 185.451 58.364  71.249 1.00   26.60 ? 12   GLY H N   1 
ATOM   7882  C  CA  . GLY H  1 13  ? 184.295 58.141  72.098 1.00   25.27 ? 12   GLY H CA  1 
ATOM   7883  C  C   . GLY H  1 13  ? 183.585 56.845  71.756 1.00   24.25 ? 12   GLY H C   1 
ATOM   7884  O  O   . GLY H  1 13  ? 184.197 55.912  71.208 1.00   25.00 ? 12   GLY H O   1 
ATOM   7885  N  N   . PRO H  1 14  ? 182.272 56.792  72.020 1.00   23.13 ? 13   PRO H N   1 
ATOM   7886  C  CA  . PRO H  1 14  ? 181.455 55.596  71.804 1.00   22.37 ? 13   PRO H CA  1 
ATOM   7887  C  C   . PRO H  1 14  ? 180.863 55.385  70.397 1.00   21.45 ? 13   PRO H C   1 
ATOM   7888  O  O   . PRO H  1 14  ? 180.146 54.420  70.192 1.00   21.00 ? 13   PRO H O   1 
ATOM   7889  C  CB  . PRO H  1 14  ? 180.314 55.813  72.796 1.00   22.85 ? 13   PRO H CB  1 
ATOM   7890  C  CG  . PRO H  1 14  ? 180.103 57.285  72.748 1.00   23.00 ? 13   PRO H CG  1 
ATOM   7891  C  CD  . PRO H  1 14  ? 181.491 57.869  72.670 1.00   23.08 ? 13   PRO H CD  1 
ATOM   7892  N  N   . VAL H  1 15  ? 181.137 56.273  69.440 1.00   20.57 ? 14   VAL H N   1 
ATOM   7893  C  CA  . VAL H  1 15  ? 180.506 56.169  68.142 1.00   19.87 ? 14   VAL H CA  1 
ATOM   7894  C  C   . VAL H  1 15  ? 181.170 55.107  67.270 1.00   19.68 ? 14   VAL H C   1 
ATOM   7895  O  O   . VAL H  1 15  ? 182.369 55.127  67.059 1.00   19.56 ? 14   VAL H O   1 
ATOM   7896  C  CB  . VAL H  1 15  ? 180.470 57.512  67.385 1.00   19.34 ? 14   VAL H CB  1 
ATOM   7897  C  CG1 . VAL H  1 15  ? 179.909 57.303  65.992 1.00   18.33 ? 14   VAL H CG1 1 
ATOM   7898  C  CG2 . VAL H  1 15  ? 179.636 58.518  68.169 1.00   18.97 ? 14   VAL H CG2 1 
ATOM   7899  N  N   . GLN H  1 16  ? 180.371 54.188  66.761 1.00   19.65 ? 15   GLN H N   1 
ATOM   7900  C  CA  . GLN H  1 16  ? 180.912 53.120  65.960 1.00   19.87 ? 15   GLN H CA  1 
ATOM   7901  C  C   . GLN H  1 16  ? 179.858 52.520  65.062 1.00   18.75 ? 15   GLN H C   1 
ATOM   7902  O  O   . GLN H  1 16  ? 178.681 52.538  65.361 1.00   18.51 ? 15   GLN H O   1 
ATOM   7903  C  CB  . GLN H  1 16  ? 181.552 52.051  66.848 1.00   21.61 ? 15   GLN H CB  1 
ATOM   7904  C  CG  . GLN H  1 16  ? 180.613 51.406  67.840 1.00   23.27 ? 15   GLN H CG  1 
ATOM   7905  C  CD  . GLN H  1 16  ? 181.292 50.276  68.597 1.00   25.92 ? 15   GLN H CD  1 
ATOM   7906  O  OE1 . GLN H  1 16  ? 182.195 49.618  68.069 1.00   29.17 ? 15   GLN H OE1 1 
ATOM   7907  N  NE2 . GLN H  1 16  ? 180.871 50.045  69.825 1.00   27.72 ? 15   GLN H NE2 1 
ATOM   7908  N  N   . GLY H  1 17  ? 180.297 52.033  63.917 1.00   17.80 ? 16   GLY H N   1 
ATOM   7909  C  CA  . GLY H  1 17  ? 179.387 51.439  62.975 1.00   17.41 ? 16   GLY H CA  1 
ATOM   7910  C  C   . GLY H  1 17  ? 180.103 50.845  61.806 1.00   16.75 ? 16   GLY H C   1 
ATOM   7911  O  O   . GLY H  1 17  ? 181.331 50.930  61.711 1.00   16.44 ? 16   GLY H O   1 
ATOM   7912  N  N   . ILE H  1 18  ? 179.303 50.236  60.937 1.00   16.44 ? 17   ILE H N   1 
ATOM   7913  C  CA  . ILE H  1 18  ? 179.736 49.606  59.712 1.00   16.03 ? 17   ILE H CA  1 
ATOM   7914  C  C   . ILE H  1 18  ? 178.831 50.140  58.615 1.00   15.74 ? 17   ILE H C   1 
ATOM   7915  O  O   . ILE H  1 18  ? 177.585 50.089  58.737 1.00   15.79 ? 17   ILE H O   1 
ATOM   7916  C  CB  . ILE H  1 18  ? 179.596 48.066  59.764 1.00   16.49 ? 17   ILE H CB  1 
ATOM   7917  C  CG1 . ILE H  1 18  ? 180.534 47.431  60.818 1.00   16.72 ? 17   ILE H CG1 1 
ATOM   7918  C  CG2 . ILE H  1 18  ? 179.859 47.428  58.388 1.00   16.29 ? 17   ILE H CG2 1 
ATOM   7919  C  CD1 . ILE H  1 18  ? 180.148 45.985  61.191 1.00   17.14 ? 17   ILE H CD1 1 
ATOM   7920  N  N   . ILE H  1 19  ? 179.455 50.686  57.563 1.00   15.23 ? 18   ILE H N   1 
ATOM   7921  C  CA  . ILE H  1 19  ? 178.751 51.188  56.397 1.00   15.01 ? 18   ILE H CA  1 
ATOM   7922  C  C   . ILE H  1 19  ? 179.224 50.450  55.140 1.00   15.28 ? 18   ILE H C   1 
ATOM   7923  O  O   . ILE H  1 19  ? 180.435 50.339  54.864 1.00   14.98 ? 18   ILE H O   1 
ATOM   7924  C  CB  . ILE H  1 19  ? 178.980 52.695  56.209 1.00   14.61 ? 18   ILE H CB  1 
ATOM   7925  C  CG1 . ILE H  1 19  ? 178.472 53.475  57.441 1.00   14.57 ? 18   ILE H CG1 1 
ATOM   7926  C  CG2 . ILE H  1 19  ? 178.269 53.165  54.962 1.00   14.41 ? 18   ILE H CG2 1 
ATOM   7927  C  CD1 . ILE H  1 19  ? 176.938 53.476  57.556 1.00   14.70 ? 18   ILE H CD1 1 
ATOM   7928  N  N   . ASN H  1 20  ? 178.232 49.985  54.392 1.00   15.61 ? 19   ASN H N   1 
ATOM   7929  C  CA  . ASN H  1 20  ? 178.376 49.267  53.155 1.00   16.11 ? 19   ASN H CA  1 
ATOM   7930  C  C   . ASN H  1 20  ? 178.079 50.185  51.968 1.00   16.28 ? 19   ASN H C   1 
ATOM   7931  O  O   . ASN H  1 20  ? 177.228 51.088  52.059 1.00   15.96 ? 19   ASN H O   1 
ATOM   7932  C  CB  . ASN H  1 20  ? 177.373 48.106  53.133 1.00   16.55 ? 19   ASN H CB  1 
ATOM   7933  C  CG  . ASN H  1 20  ? 177.539 47.168  54.321 1.00   16.77 ? 19   ASN H CG  1 
ATOM   7934  O  OD1 . ASN H  1 20  ? 178.506 46.443  54.406 1.00   17.19 ? 19   ASN H OD1 1 
ATOM   7935  N  ND2 . ASN H  1 20  ? 176.607 47.203  55.238 1.00   17.01 ? 19   ASN H ND2 1 
ATOM   7936  N  N   . PHE H  1 21  ? 178.795 49.931  50.874 1.00   16.81 ? 20   PHE H N   1 
ATOM   7937  C  CA  . PHE H  1 21  ? 178.608 50.614  49.603 1.00   17.41 ? 20   PHE H CA  1 
ATOM   7938  C  C   . PHE H  1 21  ? 178.461 49.537  48.546 1.00   18.72 ? 20   PHE H C   1 
ATOM   7939  O  O   . PHE H  1 21  ? 179.169 48.527  48.591 1.00   18.73 ? 20   PHE H O   1 
ATOM   7940  C  CB  . PHE H  1 21  ? 179.807 51.478  49.244 1.00   16.99 ? 20   PHE H CB  1 
ATOM   7941  C  CG  . PHE H  1 21  ? 180.171 52.525  50.284 1.00   16.49 ? 20   PHE H CG  1 
ATOM   7942  C  CD1 . PHE H  1 21  ? 180.956 52.197  51.373 1.00   16.33 ? 20   PHE H CD1 1 
ATOM   7943  C  CD2 . PHE H  1 21  ? 179.771 53.850  50.131 1.00   16.40 ? 20   PHE H CD2 1 
ATOM   7944  C  CE1 . PHE H  1 21  ? 181.306 53.165  52.316 1.00   16.15 ? 20   PHE H CE1 1 
ATOM   7945  C  CE2 . PHE H  1 21  ? 180.093 54.818  51.083 1.00   16.04 ? 20   PHE H CE2 1 
ATOM   7946  C  CZ  . PHE H  1 21  ? 180.870 54.478  52.162 1.00   15.94 ? 20   PHE H CZ  1 
ATOM   7947  N  N   . GLU H  1 22  ? 177.577 49.780  47.587 1.00   20.19 ? 21   GLU H N   1 
ATOM   7948  C  CA  . GLU H  1 22  ? 177.370 48.899  46.465 1.00   21.81 ? 21   GLU H CA  1 
ATOM   7949  C  C   . GLU H  1 22  ? 177.023 49.701  45.229 1.00   21.95 ? 21   GLU H C   1 
ATOM   7950  O  O   . GLU H  1 22  ? 176.115 50.540  45.245 1.00   20.76 ? 21   GLU H O   1 
ATOM   7951  C  CB  . GLU H  1 22  ? 176.228 47.950  46.752 1.00   23.74 ? 21   GLU H CB  1 
ATOM   7952  C  CG  . GLU H  1 22  ? 175.953 46.912  45.696 1.00   26.11 ? 21   GLU H CG  1 
ATOM   7953  C  CD  . GLU H  1 22  ? 174.750 46.049  46.098 1.00   28.82 ? 21   GLU H CD  1 
ATOM   7954  O  OE1 . GLU H  1 22  ? 173.606 46.579  46.194 1.00   31.79 ? 21   GLU H OE1 1 
ATOM   7955  O  OE2 . GLU H  1 22  ? 174.951 44.854  46.342 1.00   31.39 ? 21   GLU H OE2 1 
ATOM   7956  N  N   . GLN H  1 23  ? 177.733 49.404  44.152 1.00   22.54 ? 22   GLN H N   1 
ATOM   7957  C  CA  . GLN H  1 23  ? 177.493 50.030  42.876 1.00   24.18 ? 22   GLN H CA  1 
ATOM   7958  C  C   . GLN H  1 23  ? 177.456 48.957  41.793 1.00   26.59 ? 22   GLN H C   1 
ATOM   7959  O  O   . GLN H  1 23  ? 178.479 48.456  41.416 1.00   26.29 ? 22   GLN H O   1 
ATOM   7960  C  CB  . GLN H  1 23  ? 178.602 51.027  42.605 1.00   23.24 ? 22   GLN H CB  1 
ATOM   7961  C  CG  . GLN H  1 23  ? 178.446 51.796  41.316 1.00   23.23 ? 22   GLN H CG  1 
ATOM   7962  C  CD  . GLN H  1 23  ? 179.542 52.822  41.128 1.00   22.69 ? 22   GLN H CD  1 
ATOM   7963  O  OE1 . GLN H  1 23  ? 180.684 52.591  41.517 1.00   22.16 ? 22   GLN H OE1 1 
ATOM   7964  N  NE2 . GLN H  1 23  ? 179.192 53.976  40.564 1.00   22.16 ? 22   GLN H NE2 1 
ATOM   7965  N  N   . LYS H  1 24  ? 176.269 48.635  41.296 1.00   31.21 ? 23   LYS H N   1 
ATOM   7966  C  CA  . LYS H  1 24  ? 176.092 47.564  40.298 1.00   35.62 ? 23   LYS H CA  1 
ATOM   7967  C  C   . LYS H  1 24  ? 176.743 47.885  38.960 1.00   37.06 ? 23   LYS H C   1 
ATOM   7968  O  O   . LYS H  1 24  ? 177.351 47.020  38.351 1.00   38.72 ? 23   LYS H O   1 
ATOM   7969  C  CB  . LYS H  1 24  ? 174.610 47.311  40.049 1.00   38.84 ? 23   LYS H CB  1 
ATOM   7970  C  CG  . LYS H  1 24  ? 173.876 46.574  41.154 1.00   41.75 ? 23   LYS H CG  1 
ATOM   7971  C  CD  . LYS H  1 24  ? 172.390 46.929  41.086 1.00   44.21 ? 23   LYS H CD  1 
ATOM   7972  C  CE  . LYS H  1 24  ? 171.521 46.047  41.975 1.00   45.60 ? 23   LYS H CE  1 
ATOM   7973  N  NZ  . LYS H  1 24  ? 170.101 46.491  41.896 1.00   46.67 ? 23   LYS H NZ  1 
ATOM   7974  N  N   . GLU H  1 25  ? 176.608 49.129  38.514 1.00   38.39 ? 24   GLU H N   1 
ATOM   7975  C  CA  . GLU H  1 25  ? 177.156 49.582  37.233 1.00   40.53 ? 24   GLU H CA  1 
ATOM   7976  C  C   . GLU H  1 25  ? 178.064 50.768  37.482 1.00   39.91 ? 24   GLU H C   1 
ATOM   7977  O  O   . GLU H  1 25  ? 177.757 51.595  38.342 1.00   38.56 ? 24   GLU H O   1 
ATOM   7978  C  CB  . GLU H  1 25  ? 176.010 50.042  36.311 1.00   43.53 ? 24   GLU H CB  1 
ATOM   7979  C  CG  . GLU H  1 25  ? 174.767 49.154  36.308 1.00   46.38 ? 24   GLU H CG  1 
ATOM   7980  C  CD  . GLU H  1 25  ? 175.010 47.749  35.735 1.00   50.56 ? 24   GLU H CD  1 
ATOM   7981  O  OE1 . GLU H  1 25  ? 176.113 47.482  35.181 1.00   50.30 ? 24   GLU H OE1 1 
ATOM   7982  O  OE2 . GLU H  1 25  ? 174.079 46.905  35.834 1.00   54.23 ? 24   GLU H OE2 1 
ATOM   7983  N  N   . SER H  1 26  ? 179.149 50.896  36.720 1.00   40.88 ? 25   SER H N   1 
ATOM   7984  C  CA  . SER H  1 26  ? 180.070 52.038  36.909 1.00   42.00 ? 25   SER H CA  1 
ATOM   7985  C  C   . SER H  1 26  ? 179.460 53.384  36.507 1.00   42.24 ? 25   SER H C   1 
ATOM   7986  O  O   . SER H  1 26  ? 179.920 54.439  36.943 1.00   41.84 ? 25   SER H O   1 
ATOM   7987  C  CB  . SER H  1 26  ? 181.391 51.818  36.159 1.00   44.10 ? 25   SER H CB  1 
ATOM   7988  O  OG  . SER H  1 26  ? 181.192 51.726  34.757 1.00   44.64 ? 25   SER H OG  1 
ATOM   7989  N  N   . ASN H  1 27  ? 178.423 53.359  35.678 1.00   43.01 ? 26   ASN H N   1 
ATOM   7990  C  CA  . ASN H  1 27  ? 177.743 54.595  35.295 1.00   44.58 ? 26   ASN H CA  1 
ATOM   7991  C  C   . ASN H  1 27  ? 176.562 54.927  36.229 1.00   42.64 ? 26   ASN H C   1 
ATOM   7992  O  O   . ASN H  1 27  ? 175.637 55.670  35.837 1.00   44.90 ? 26   ASN H O   1 
ATOM   7993  C  CB  . ASN H  1 27  ? 177.254 54.495  33.836 1.00   47.81 ? 26   ASN H CB  1 
ATOM   7994  C  CG  . ASN H  1 27  ? 176.082 53.533  33.663 1.00   49.81 ? 26   ASN H CG  1 
ATOM   7995  O  OD1 . ASN H  1 27  ? 176.256 52.314  33.639 1.00   54.46 ? 26   ASN H OD1 1 
ATOM   7996  N  ND2 . ASN H  1 27  ? 174.886 54.081  33.527 1.00   51.14 ? 26   ASN H ND2 1 
ATOM   7997  N  N   . GLY H  1 28  ? 176.589 54.399  37.457 1.00   37.58 ? 27   GLY H N   1 
ATOM   7998  C  CA  . GLY H  1 28  ? 175.356 54.283  38.234 1.00   33.10 ? 27   GLY H CA  1 
ATOM   7999  C  C   . GLY H  1 28  ? 175.429 54.714  39.672 1.00   29.00 ? 27   GLY H C   1 
ATOM   8000  O  O   . GLY H  1 28  ? 176.488 55.019  40.191 1.00   28.11 ? 27   GLY H O   1 
ATOM   8001  N  N   . PRO H  1 29  ? 174.284 54.708  40.337 1.00   26.26 ? 28   PRO H N   1 
ATOM   8002  C  CA  . PRO H  1 29  ? 174.238 55.097  41.741 1.00   24.36 ? 28   PRO H CA  1 
ATOM   8003  C  C   . PRO H  1 29  ? 174.974 54.131  42.671 1.00   22.09 ? 28   PRO H C   1 
ATOM   8004  O  O   . PRO H  1 29  ? 175.076 52.938  42.389 1.00   21.36 ? 28   PRO H O   1 
ATOM   8005  C  CB  . PRO H  1 29  ? 172.738 55.124  42.072 1.00   25.19 ? 28   PRO H CB  1 
ATOM   8006  C  CG  . PRO H  1 29  ? 172.034 54.442  40.939 1.00   26.16 ? 28   PRO H CG  1 
ATOM   8007  C  CD  . PRO H  1 29  ? 172.949 54.489  39.752 1.00   26.97 ? 28   PRO H CD  1 
ATOM   8008  N  N   . VAL H  1 30  ? 175.501 54.690  43.747 1.00   19.80 ? 29   VAL H N   1 
ATOM   8009  C  CA  . VAL H  1 30  ? 176.049 53.927  44.841 1.00   18.92 ? 29   VAL H CA  1 
ATOM   8010  C  C   . VAL H  1 30  ? 175.027 53.881  45.966 1.00   18.35 ? 29   VAL H C   1 
ATOM   8011  O  O   . VAL H  1 30  ? 174.563 54.942  46.417 1.00   18.05 ? 29   VAL H O   1 
ATOM   8012  C  CB  . VAL H  1 30  ? 177.367 54.565  45.339 1.00   18.21 ? 29   VAL H CB  1 
ATOM   8013  C  CG1 . VAL H  1 30  ? 178.030 53.703  46.410 1.00   17.49 ? 29   VAL H CG1 1 
ATOM   8014  C  CG2 . VAL H  1 30  ? 178.286 54.779  44.146 1.00   18.07 ? 29   VAL H CG2 1 
ATOM   8015  N  N   . LYS H  1 31  ? 174.670 52.670  46.406 1.00   18.07 ? 30   LYS H N   1 
ATOM   8016  C  CA  . LYS H  1 31  ? 173.869 52.479  47.609 1.00   18.01 ? 30   LYS H CA  1 
ATOM   8017  C  C   . LYS H  1 31  ? 174.795 52.445  48.820 1.00   17.27 ? 30   LYS H C   1 
ATOM   8018  O  O   . LYS H  1 31  ? 175.826 51.768  48.787 1.00   17.14 ? 30   LYS H O   1 
ATOM   8019  C  CB  . LYS H  1 31  ? 173.063 51.173  47.543 1.00   18.97 ? 30   LYS H CB  1 
ATOM   8020  C  CG  . LYS H  1 31  ? 172.119 51.134  46.353 1.00   20.07 ? 30   LYS H CG  1 
ATOM   8021  C  CD  . LYS H  1 31  ? 171.147 49.935  46.366 1.00   20.99 ? 30   LYS H CD  1 
ATOM   8022  C  CE  . LYS H  1 31  ? 170.251 49.952  45.134 0.10   21.23 ? 30   LYS H CE  1 
ATOM   8023  N  NZ  . LYS H  1 31  ? 169.359 48.764  45.058 0.10   21.78 ? 30   LYS H NZ  1 
ATOM   8024  N  N   . VAL H  1 32  ? 174.415 53.182  49.861 1.00   16.71 ? 31   VAL H N   1 
ATOM   8025  C  CA  . VAL H  1 32  ? 175.171 53.345  51.096 1.00   16.41 ? 31   VAL H CA  1 
ATOM   8026  C  C   . VAL H  1 32  ? 174.228 52.987  52.241 1.00   16.73 ? 31   VAL H C   1 
ATOM   8027  O  O   . VAL H  1 32  ? 173.204 53.645  52.414 1.00   16.92 ? 31   VAL H O   1 
ATOM   8028  C  CB  . VAL H  1 32  ? 175.662 54.787  51.264 1.00   16.05 ? 31   VAL H CB  1 
ATOM   8029  C  CG1 . VAL H  1 32  ? 176.621 54.913  52.462 1.00   15.64 ? 31   VAL H CG1 1 
ATOM   8030  C  CG2 . VAL H  1 32  ? 176.309 55.280  49.969 1.00   15.82 ? 31   VAL H CG2 1 
ATOM   8031  N  N   . TRP H  1 33  ? 174.541 51.933  52.991 1.00   16.78 ? 32   TRP H N   1 
ATOM   8032  C  CA  . TRP H  1 33  ? 173.687 51.513  54.084 1.00   17.39 ? 32   TRP H CA  1 
ATOM   8033  C  C   . TRP H  1 33  ? 174.423 50.845  55.205 1.00   17.38 ? 32   TRP H C   1 
ATOM   8034  O  O   . TRP H  1 33  ? 175.541 50.339  55.063 1.00   16.77 ? 32   TRP H O   1 
ATOM   8035  C  CB  . TRP H  1 33  ? 172.570 50.593  53.577 1.00   17.94 ? 32   TRP H CB  1 
ATOM   8036  C  CG  . TRP H  1 33  ? 173.015 49.174  53.299 1.00   18.47 ? 32   TRP H CG  1 
ATOM   8037  C  CD1 . TRP H  1 33  ? 172.768 48.049  54.072 1.00   19.05 ? 32   TRP H CD1 1 
ATOM   8038  C  CD2 . TRP H  1 33  ? 173.790 48.676  52.154 1.00   18.68 ? 32   TRP H CD2 1 
ATOM   8039  N  NE1 . TRP H  1 33  ? 173.316 46.931  53.492 1.00   19.42 ? 32   TRP H NE1 1 
ATOM   8040  C  CE2 . TRP H  1 33  ? 173.934 47.240  52.346 1.00   19.07 ? 32   TRP H CE2 1 
ATOM   8041  C  CE3 . TRP H  1 33  ? 174.340 49.253  51.031 1.00   18.66 ? 32   TRP H CE3 1 
ATOM   8042  C  CZ2 . TRP H  1 33  ? 174.620 46.443  51.450 1.00   19.42 ? 32   TRP H CZ2 1 
ATOM   8043  C  CZ3 . TRP H  1 33  ? 175.031 48.441  50.133 1.00   18.98 ? 32   TRP H CZ3 1 
ATOM   8044  C  CH2 . TRP H  1 33  ? 175.155 47.065  50.329 1.00   19.26 ? 32   TRP H CH2 1 
ATOM   8045  N  N   . GLY H  1 34  ? 173.773 50.836  56.355 1.00   18.10 ? 33   GLY H N   1 
ATOM   8046  C  CA  . GLY H  1 34  ? 174.347 50.222  57.537 1.00   18.61 ? 33   GLY H CA  1 
ATOM   8047  C  C   . GLY H  1 34  ? 173.885 50.924  58.767 1.00   19.40 ? 33   GLY H C   1 
ATOM   8048  O  O   . GLY H  1 34  ? 172.872 51.620  58.760 1.00   19.90 ? 33   GLY H O   1 
ATOM   8049  N  N   . SER H  1 35  ? 174.627 50.732  59.842 1.00   20.20 ? 34   SER H N   1 
ATOM   8050  C  CA  . SER H  1 35  ? 174.173 51.142  61.132 1.00   21.12 ? 34   SER H CA  1 
ATOM   8051  C  C   . SER H  1 35  ? 175.305 51.822  61.864 1.00   20.82 ? 34   SER H C   1 
ATOM   8052  O  O   . SER H  1 35  ? 176.443 51.335  61.812 1.00   21.20 ? 34   SER H O   1 
ATOM   8053  C  CB  . SER H  1 35  ? 173.744 49.901  61.880 1.00   22.52 ? 34   SER H CB  1 
ATOM   8054  O  OG  . SER H  1 35  ? 173.163 50.297  63.085 1.00   24.97 ? 34   SER H OG  1 
ATOM   8055  N  N   . ILE H  1 36  ? 175.011 52.947  62.514 1.00   20.35 ? 35   ILE H N   1 
ATOM   8056  C  CA  . ILE H  1 36  ? 175.979 53.628  63.363 1.00   20.12 ? 35   ILE H CA  1 
ATOM   8057  C  C   . ILE H  1 36  ? 175.338 53.829  64.734 1.00   20.68 ? 35   ILE H C   1 
ATOM   8058  O  O   . ILE H  1 36  ? 174.218 54.320  64.806 1.00   20.62 ? 35   ILE H O   1 
ATOM   8059  C  CB  . ILE H  1 36  ? 176.407 54.988  62.791 1.00   19.41 ? 35   ILE H CB  1 
ATOM   8060  C  CG1 . ILE H  1 36  ? 176.742 54.873  61.293 1.00   19.34 ? 35   ILE H CG1 1 
ATOM   8061  C  CG2 . ILE H  1 36  ? 177.568 55.529  63.608 1.00   19.31 ? 35   ILE H CG2 1 
ATOM   8062  C  CD1 . ILE H  1 36  ? 177.066 56.203  60.608 1.00   18.76 ? 35   ILE H CD1 1 
ATOM   8063  N  N   . LYS H  1 37  ? 176.052 53.465  65.806 1.00   21.15 ? 36   LYS H N   1 
ATOM   8064  C  CA  . LYS H  1 37  ? 175.521 53.561  67.165 1.00   21.93 ? 36   LYS H CA  1 
ATOM   8065  C  C   . LYS H  1 37  ? 176.364 54.476  68.009 1.00   21.23 ? 36   LYS H C   1 
ATOM   8066  O  O   . LYS H  1 37  ? 177.426 54.920  67.579 1.00   20.50 ? 36   LYS H O   1 
ATOM   8067  C  CB  . LYS H  1 37  ? 175.402 52.168  67.821 1.00   23.54 ? 36   LYS H CB  1 
ATOM   8068  C  CG  . LYS H  1 37  ? 176.719 51.513  68.195 1.00   24.56 ? 36   LYS H CG  1 
ATOM   8069  C  CD  . LYS H  1 37  ? 176.518 50.205  68.987 1.00   25.84 ? 36   LYS H CD  1 
ATOM   8070  C  CE  . LYS H  1 37  ? 176.821 48.970  68.152 1.00   27.10 ? 36   LYS H CE  1 
ATOM   8071  N  NZ  . LYS H  1 37  ? 177.361 47.788  68.918 1.00   28.12 ? 36   LYS H NZ  1 
ATOM   8072  N  N   . GLY H  1 38  ? 175.889 54.770  69.214 1.00   20.87 ? 37   GLY H N   1 
ATOM   8073  C  CA  . GLY H  1 38  ? 176.601 55.675  70.119 1.00   20.48 ? 37   GLY H CA  1 
ATOM   8074  C  C   . GLY H  1 38  ? 176.375 57.144  69.807 1.00   19.81 ? 37   GLY H C   1 
ATOM   8075  O  O   . GLY H  1 38  ? 177.118 57.989  70.252 1.00   19.58 ? 37   GLY H O   1 
ATOM   8076  N  N   . LEU H  1 39  ? 175.340 57.451  69.042 1.00   19.85 ? 38   LEU H N   1 
ATOM   8077  C  CA  . LEU H  1 39  ? 175.091 58.830  68.587 1.00   19.86 ? 38   LEU H CA  1 
ATOM   8078  C  C   . LEU H  1 39  ? 173.990 59.480  69.420 1.00   20.74 ? 38   LEU H C   1 
ATOM   8079  O  O   . LEU H  1 39  ? 173.088 58.800  69.880 1.00   21.04 ? 38   LEU H O   1 
ATOM   8080  C  CB  . LEU H  1 39  ? 174.656 58.851  67.119 1.00   19.39 ? 38   LEU H CB  1 
ATOM   8081  C  CG  . LEU H  1 39  ? 175.733 58.627  66.041 1.00   18.96 ? 38   LEU H CG  1 
ATOM   8082  C  CD1 . LEU H  1 39  ? 175.114 58.360  64.661 1.00   18.32 ? 38   LEU H CD1 1 
ATOM   8083  C  CD2 . LEU H  1 39  ? 176.686 59.820  66.014 1.00   18.41 ? 38   LEU H CD2 1 
ATOM   8084  N  N   . THR H  1 40  ? 174.072 60.798  69.584 1.00   21.31 ? 39   THR H N   1 
ATOM   8085  C  CA  . THR H  1 40  ? 172.969 61.573  70.153 1.00   22.03 ? 39   THR H CA  1 
ATOM   8086  C  C   . THR H  1 40  ? 171.869 61.655  69.101 1.00   21.98 ? 39   THR H C   1 
ATOM   8087  O  O   . THR H  1 40  ? 172.138 61.661  67.905 1.00   20.92 ? 39   THR H O   1 
ATOM   8088  C  CB  . THR H  1 40  ? 173.405 62.980  70.589 1.00   22.02 ? 39   THR H CB  1 
ATOM   8089  O  OG1 . THR H  1 40  ? 173.874 63.711  69.451 1.00   22.33 ? 39   THR H OG1 1 
ATOM   8090  C  CG2 . THR H  1 40  ? 174.511 62.889  71.584 1.00   22.12 ? 39   THR H CG2 1 
ATOM   8091  N  N   . GLU H  1 41  ? 170.626 61.688  69.572 1.00   22.71 ? 40   GLU H N   1 
ATOM   8092  C  CA  . GLU H  1 41  ? 169.461 61.665  68.718 1.00   22.75 ? 40   GLU H CA  1 
ATOM   8093  C  C   . GLU H  1 41  ? 169.452 62.902  67.835 1.00   21.72 ? 40   GLU H C   1 
ATOM   8094  O  O   . GLU H  1 41  ? 169.795 63.989  68.284 1.00   21.93 ? 40   GLU H O   1 
ATOM   8095  C  CB  . GLU H  1 41  ? 168.196 61.638  69.592 1.00   24.68 ? 40   GLU H CB  1 
ATOM   8096  C  CG  . GLU H  1 41  ? 166.902 61.552  68.796 1.00   25.62 ? 40   GLU H CG  1 
ATOM   8097  C  CD  . GLU H  1 41  ? 165.665 61.592  69.667 1.00   27.17 ? 40   GLU H CD  1 
ATOM   8098  O  OE1 . GLU H  1 41  ? 165.792 61.642  70.900 1.00   28.67 ? 40   GLU H OE1 1 
ATOM   8099  O  OE2 . GLU H  1 41  ? 164.563 61.581  69.097 1.00   28.19 ? 40   GLU H OE2 1 
ATOM   8100  N  N   . GLY H  1 42  ? 169.049 62.732  66.586 1.00   20.34 ? 41   GLY H N   1 
ATOM   8101  C  CA  . GLY H  1 42  ? 169.024 63.833  65.637 1.00   19.57 ? 41   GLY H CA  1 
ATOM   8102  C  C   . GLY H  1 42  ? 169.993 63.696  64.459 1.00   18.61 ? 41   GLY H C   1 
ATOM   8103  O  O   . GLY H  1 42  ? 170.518 62.611  64.172 1.00   18.05 ? 41   GLY H O   1 
ATOM   8104  N  N   . LEU H  1 43  ? 170.209 64.828  63.794 1.00   17.89 ? 42   LEU H N   1 
ATOM   8105  C  CA  . LEU H  1 43  ? 170.954 64.893  62.572 1.00   17.16 ? 42   LEU H CA  1 
ATOM   8106  C  C   . LEU H  1 43  ? 172.430 64.906  62.841 1.00   16.79 ? 42   LEU H C   1 
ATOM   8107  O  O   . LEU H  1 43  ? 172.901 65.646  63.721 1.00   17.40 ? 42   LEU H O   1 
ATOM   8108  C  CB  . LEU H  1 43  ? 170.566 66.147  61.792 1.00   17.07 ? 42   LEU H CB  1 
ATOM   8109  C  CG  . LEU H  1 43  ? 169.152 66.179  61.205 1.00   17.16 ? 42   LEU H CG  1 
ATOM   8110  C  CD1 . LEU H  1 43  ? 168.878 67.522  60.517 1.00   16.91 ? 42   LEU H CD1 1 
ATOM   8111  C  CD2 . LEU H  1 43  ? 168.888 65.009  60.268 1.00   17.01 ? 42   LEU H CD2 1 
ATOM   8112  N  N   . HIS H  1 44  ? 173.173 64.109  62.069 1.00   16.06 ? 43   HIS H N   1 
ATOM   8113  C  CA  . HIS H  1 44  ? 174.631 64.153  62.030 1.00   15.46 ? 43   HIS H CA  1 
ATOM   8114  C  C   . HIS H  1 44  ? 175.219 64.246  60.626 1.00   14.74 ? 43   HIS H C   1 
ATOM   8115  O  O   . HIS H  1 44  ? 174.861 63.487  59.726 1.00   14.39 ? 43   HIS H O   1 
ATOM   8116  C  CB  . HIS H  1 44  ? 175.158 62.924  62.740 1.00   15.74 ? 43   HIS H CB  1 
ATOM   8117  C  CG  . HIS H  1 44  ? 174.839 62.914  64.211 1.00   16.24 ? 43   HIS H CG  1 
ATOM   8118  N  ND1 . HIS H  1 44  ? 175.656 63.459  65.135 1.00   16.44 ? 43   HIS H ND1 1 
ATOM   8119  C  CD2 . HIS H  1 44  ? 173.731 62.436  64.898 1.00   16.53 ? 43   HIS H CD2 1 
ATOM   8120  C  CE1 . HIS H  1 44  ? 175.089 63.335  66.344 1.00   16.87 ? 43   HIS H CE1 1 
ATOM   8121  N  NE2 . HIS H  1 44  ? 173.914 62.708  66.194 1.00   16.85 ? 43   HIS H NE2 1 
ATOM   8122  N  N   . GLY H  1 45  ? 176.105 65.215  60.412 1.00   14.23 ? 44   GLY H N   1 
ATOM   8123  C  CA  . GLY H  1 45  ? 176.833 65.318  59.140 1.00   13.81 ? 44   GLY H CA  1 
ATOM   8124  C  C   . GLY H  1 45  ? 177.567 64.017  58.805 1.00   13.40 ? 44   GLY H C   1 
ATOM   8125  O  O   . GLY H  1 45  ? 178.094 63.336  59.694 1.00   13.35 ? 44   GLY H O   1 
ATOM   8126  N  N   . PHE H  1 46  ? 177.604 63.695  57.516 1.00   13.12 ? 45   PHE H N   1 
ATOM   8127  C  CA  . PHE H  1 46  ? 178.071 62.421  56.986 1.00   12.86 ? 45   PHE H CA  1 
ATOM   8128  C  C   . PHE H  1 46  ? 178.746 62.677  55.630 1.00   12.75 ? 45   PHE H C   1 
ATOM   8129  O  O   . PHE H  1 46  ? 178.085 62.991  54.607 1.00   12.70 ? 45   PHE H O   1 
ATOM   8130  C  CB  . PHE H  1 46  ? 176.856 61.527  56.840 1.00   12.97 ? 45   PHE H CB  1 
ATOM   8131  C  CG  . PHE H  1 46  ? 177.158 60.070  56.598 1.00   13.01 ? 45   PHE H CG  1 
ATOM   8132  C  CD1 . PHE H  1 46  ? 177.763 59.289  57.575 1.00   13.03 ? 45   PHE H CD1 1 
ATOM   8133  C  CD2 . PHE H  1 46  ? 176.712 59.453  55.449 1.00   13.02 ? 45   PHE H CD2 1 
ATOM   8134  C  CE1 . PHE H  1 46  ? 177.986 57.928  57.371 1.00   13.04 ? 45   PHE H CE1 1 
ATOM   8135  C  CE2 . PHE H  1 46  ? 176.934 58.090  55.236 1.00   13.08 ? 45   PHE H CE2 1 
ATOM   8136  C  CZ  . PHE H  1 46  ? 177.582 57.334  56.187 1.00   13.05 ? 45   PHE H CZ  1 
ATOM   8137  N  N   . HIS H  1 47  ? 180.068 62.572  55.616 1.00   12.57 ? 46   HIS H N   1 
ATOM   8138  C  CA  . HIS H  1 47  ? 180.837 62.959  54.464 1.00   12.62 ? 46   HIS H CA  1 
ATOM   8139  C  C   . HIS H  1 47  ? 181.992 62.057  54.180 1.00   12.48 ? 46   HIS H C   1 
ATOM   8140  O  O   . HIS H  1 47  ? 182.563 61.444  55.079 1.00   12.31 ? 46   HIS H O   1 
ATOM   8141  C  CB  . HIS H  1 47  ? 181.457 64.344  54.664 1.00   12.79 ? 46   HIS H CB  1 
ATOM   8142  C  CG  . HIS H  1 47  ? 180.543 65.360  55.297 1.00   12.88 ? 46   HIS H CG  1 
ATOM   8143  N  ND1 . HIS H  1 47  ? 180.879 66.027  56.407 1.00   12.92 ? 46   HIS H ND1 1 
ATOM   8144  C  CD2 . HIS H  1 47  ? 179.298 65.835  54.906 1.00   12.84 ? 46   HIS H CD2 1 
ATOM   8145  C  CE1 . HIS H  1 47  ? 179.879 66.859  56.734 1.00   13.09 ? 46   HIS H CE1 1 
ATOM   8146  N  NE2 . HIS H  1 47  ? 178.908 66.730  55.808 1.00   12.95 ? 46   HIS H NE2 1 
ATOM   8147  N  N   . VAL H  1 48  ? 182.426 62.079  52.927 1.00   12.49 ? 47   VAL H N   1 
ATOM   8148  C  CA  . VAL H  1 48  ? 183.677 61.456  52.543 1.00   12.50 ? 47   VAL H CA  1 
ATOM   8149  C  C   . VAL H  1 48  ? 184.704 62.546  52.513 1.00   12.72 ? 47   VAL H C   1 
ATOM   8150  O  O   . VAL H  1 48  ? 184.563 63.562  51.799 1.00   12.86 ? 47   VAL H O   1 
ATOM   8151  C  CB  . VAL H  1 48  ? 183.619 60.741  51.188 1.00   12.52 ? 47   VAL H CB  1 
ATOM   8152  C  CG1 . VAL H  1 48  ? 184.977 60.118  50.873 1.00   12.54 ? 47   VAL H CG1 1 
ATOM   8153  C  CG2 . VAL H  1 48  ? 182.522 59.694  51.176 1.00   12.46 ? 47   VAL H CG2 1 
ATOM   8154  N  N   . HIS H  1 49  ? 185.730 62.349  53.308 1.00   12.90 ? 48   HIS H N   1 
ATOM   8155  C  CA  . HIS H  1 49  ? 186.845 63.264  53.382 1.00   13.29 ? 48   HIS H CA  1 
ATOM   8156  C  C   . HIS H  1 49  ? 187.953 62.773  52.501 1.00   13.58 ? 48   HIS H C   1 
ATOM   8157  O  O   . HIS H  1 49  ? 188.019 61.601  52.161 1.00   13.60 ? 48   HIS H O   1 
ATOM   8158  C  CB  . HIS H  1 49  ? 187.316 63.421  54.824 1.00   13.31 ? 48   HIS H CB  1 
ATOM   8159  C  CG  . HIS H  1 49  ? 186.430 64.279  55.672 1.00   13.39 ? 48   HIS H CG  1 
ATOM   8160  N  ND1 . HIS H  1 49  ? 186.884 65.360  56.330 1.00   13.59 ? 48   HIS H ND1 1 
ATOM   8161  C  CD2 . HIS H  1 49  ? 185.081 64.210  55.943 1.00   13.37 ? 48   HIS H CD2 1 
ATOM   8162  C  CE1 . HIS H  1 49  ? 185.885 65.934  56.993 1.00   13.64 ? 48   HIS H CE1 1 
ATOM   8163  N  NE2 . HIS H  1 49  ? 184.788 65.234  56.771 1.00   13.40 ? 48   HIS H NE2 1 
ATOM   8164  N  N   . GLU H  1 50  ? 188.844 63.666  52.130 1.00   14.04 ? 49   GLU H N   1 
ATOM   8165  C  CA  . GLU H  1 50  ? 189.787 63.426  51.039 1.00   14.52 ? 49   GLU H CA  1 
ATOM   8166  C  C   . GLU H  1 50  ? 190.806 62.299  51.266 1.00   14.53 ? 49   GLU H C   1 
ATOM   8167  O  O   . GLU H  1 50  ? 191.054 61.505  50.357 1.00   14.56 ? 49   GLU H O   1 
ATOM   8168  C  CB  . GLU H  1 50  ? 190.556 64.708  50.769 1.00   15.09 ? 49   GLU H CB  1 
ATOM   8169  C  CG  . GLU H  1 50  ? 191.435 64.605  49.549 1.00   15.63 ? 49   GLU H CG  1 
ATOM   8170  C  CD  . GLU H  1 50  ? 192.066 65.924  49.147 1.00   16.39 ? 49   GLU H CD  1 
ATOM   8171  O  OE1 . GLU H  1 50  ? 191.863 66.952  49.799 1.00   16.62 ? 49   GLU H OE1 1 
ATOM   8172  O  OE2 . GLU H  1 50  ? 192.815 65.898  48.162 1.00   17.25 ? 49   GLU H OE2 1 
ATOM   8173  N  N   . PHE H  1 51  ? 191.411 62.249  52.455 1.00   14.52 ? 50   PHE H N   1 
ATOM   8174  C  CA  . PHE H  1 51  ? 192.526 61.327  52.710 1.00   14.60 ? 50   PHE H CA  1 
ATOM   8175  C  C   . PHE H  1 51  ? 192.148 60.143  53.566 1.00   14.38 ? 50   PHE H C   1 
ATOM   8176  O  O   . PHE H  1 51  ? 191.475 60.288  54.595 1.00   14.14 ? 50   PHE H O   1 
ATOM   8177  C  CB  . PHE H  1 51  ? 193.689 62.084  53.339 1.00   14.94 ? 50   PHE H CB  1 
ATOM   8178  C  CG  . PHE H  1 51  ? 194.147 63.238  52.498 1.00   15.36 ? 50   PHE H CG  1 
ATOM   8179  C  CD1 . PHE H  1 51  ? 194.594 63.018  51.209 1.00   15.63 ? 50   PHE H CD1 1 
ATOM   8180  C  CD2 . PHE H  1 51  ? 194.067 64.539  52.962 1.00   15.65 ? 50   PHE H CD2 1 
ATOM   8181  C  CE1 . PHE H  1 51  ? 194.994 64.084  50.397 1.00   16.08 ? 50   PHE H CE1 1 
ATOM   8182  C  CE2 . PHE H  1 51  ? 194.458 65.613  52.155 1.00   16.02 ? 50   PHE H CE2 1 
ATOM   8183  C  CZ  . PHE H  1 51  ? 194.922 65.379  50.873 1.00   16.17 ? 50   PHE H CZ  1 
ATOM   8184  N  N   . GLY H  1 52  ? 192.575 58.956  53.146 1.00   14.36 ? 51   GLY H N   1 
ATOM   8185  C  CA  . GLY H  1 52  ? 192.420 57.772  53.997 1.00   14.36 ? 51   GLY H CA  1 
ATOM   8186  C  C   . GLY H  1 52  ? 193.572 57.683  54.998 1.00   14.66 ? 51   GLY H C   1 
ATOM   8187  O  O   . GLY H  1 52  ? 194.238 56.670  55.095 1.00   14.51 ? 51   GLY H O   1 
ATOM   8188  N  N   . ASP H  1 53  ? 193.788 58.760  55.731 1.00   15.17 ? 52   ASP H N   1 
ATOM   8189  C  CA  . ASP H  1 53  ? 194.917 58.901  56.651 1.00   15.91 ? 52   ASP H CA  1 
ATOM   8190  C  C   . ASP H  1 53  ? 194.339 59.040  58.040 1.00   16.50 ? 52   ASP H C   1 
ATOM   8191  O  O   . ASP H  1 53  ? 193.727 60.082  58.370 1.00   16.23 ? 52   ASP H O   1 
ATOM   8192  C  CB  . ASP H  1 53  ? 195.684 60.145  56.257 1.00   16.25 ? 52   ASP H CB  1 
ATOM   8193  C  CG  . ASP H  1 53  ? 196.943 60.356  57.038 1.00   16.58 ? 52   ASP H CG  1 
ATOM   8194  O  OD1 . ASP H  1 53  ? 197.056 59.866  58.199 1.00   16.63 ? 52   ASP H OD1 1 
ATOM   8195  O  OD2 . ASP H  1 53  ? 197.835 61.035  56.461 1.00   17.08 ? 52   ASP H OD2 1 
ATOM   8196  N  N   . ASN H  1 54  ? 194.525 57.984  58.834 1.00   17.37 ? 53   ASN H N   1 
ATOM   8197  C  CA  . ASN H  1 54  ? 194.135 57.948  60.236 1.00   18.58 ? 53   ASN H CA  1 
ATOM   8198  C  C   . ASN H  1 54  ? 195.316 58.128  61.218 1.00   18.80 ? 53   ASN H C   1 
ATOM   8199  O  O   . ASN H  1 54  ? 195.175 57.825  62.382 1.00   18.56 ? 53   ASN H O   1 
ATOM   8200  C  CB  . ASN H  1 54  ? 193.449 56.603  60.536 1.00   19.71 ? 53   ASN H CB  1 
ATOM   8201  C  CG  . ASN H  1 54  ? 192.660 56.617  61.849 1.00   21.08 ? 53   ASN H CG  1 
ATOM   8202  O  OD1 . ASN H  1 54  ? 192.846 55.753  62.718 1.00   23.83 ? 53   ASN H OD1 1 
ATOM   8203  N  ND2 . ASN H  1 54  ? 191.791 57.588  61.999 1.00   21.65 ? 53   ASN H ND2 1 
ATOM   8204  N  N   . THR H  1 55  ? 196.464 58.608  60.747 1.00   18.81 ? 54   THR H N   1 
ATOM   8205  C  CA  . THR H  1 55  ? 197.649 58.701  61.598 1.00   19.26 ? 54   THR H CA  1 
ATOM   8206  C  C   . THR H  1 55  ? 197.463 59.608  62.807 1.00   20.11 ? 54   THR H C   1 
ATOM   8207  O  O   . THR H  1 55  ? 198.014 59.322  63.847 1.00   20.30 ? 54   THR H O   1 
ATOM   8208  C  CB  . THR H  1 55  ? 198.918 59.131  60.834 1.00   19.13 ? 54   THR H CB  1 
ATOM   8209  O  OG1 . THR H  1 55  ? 198.697 60.379  60.196 1.00   18.91 ? 54   THR H OG1 1 
ATOM   8210  C  CG2 . THR H  1 55  ? 199.286 58.109  59.799 1.00   18.56 ? 54   THR H CG2 1 
ATOM   8211  N  N   . ALA H  1 56  ? 196.650 60.658  62.696 1.00   20.72 ? 55   ALA H N   1 
ATOM   8212  C  CA  . ALA H  1 56  ? 196.289 61.468  63.883 1.00   21.48 ? 55   ALA H CA  1 
ATOM   8213  C  C   . ALA H  1 56  ? 194.785 61.385  64.145 1.00   21.58 ? 55   ALA H C   1 
ATOM   8214  O  O   . ALA H  1 56  ? 194.149 62.395  64.401 1.00   23.09 ? 55   ALA H O   1 
ATOM   8215  C  CB  . ALA H  1 56  ? 196.734 62.925  63.729 1.00   21.49 ? 55   ALA H CB  1 
ATOM   8216  N  N   . GLY H  1 57  ? 194.210 60.196  64.090 1.00   20.71 ? 56   GLY H N   1 
ATOM   8217  C  CA  . GLY H  1 57  ? 192.769 60.070  64.268 1.00   20.63 ? 56   GLY H CA  1 
ATOM   8218  C  C   . GLY H  1 57  ? 192.048 60.672  63.061 1.00   20.17 ? 56   GLY H C   1 
ATOM   8219  O  O   . GLY H  1 57  ? 192.621 60.745  61.956 1.00   21.61 ? 56   GLY H O   1 
ATOM   8220  N  N   . CYS H  1 58  ? 190.819 61.131  63.259 1.00   19.27 ? 57   CYS H N   1 
ATOM   8221  C  CA  . CYS H  1 58  ? 190.002 61.636  62.162 1.00   18.59 ? 57   CYS H CA  1 
ATOM   8222  C  C   . CYS H  1 58  ? 190.488 62.970  61.565 1.00   18.46 ? 57   CYS H C   1 
ATOM   8223  O  O   . CYS H  1 58  ? 190.146 63.284  60.420 1.00   17.79 ? 57   CYS H O   1 
ATOM   8224  C  CB  . CYS H  1 58  ? 188.522 61.730  62.569 1.00   18.09 ? 57   CYS H CB  1 
ATOM   8225  S  SG  . CYS H  1 58  ? 187.788 60.167  63.096 1.00   17.90 ? 57   CYS H SG  1 
ATOM   8226  N  N   . THR H  1 59  ? 191.268 63.743  62.324 1.00   18.54 ? 58   THR H N   1 
ATOM   8227  C  CA  . THR H  1 59  ? 191.771 65.030  61.852 1.00   18.88 ? 58   THR H CA  1 
ATOM   8228  C  C   . THR H  1 59  ? 192.633 64.900  60.614 1.00   18.25 ? 58   THR H C   1 
ATOM   8229  O  O   . THR H  1 59  ? 192.605 65.746  59.732 1.00   18.24 ? 58   THR H O   1 
ATOM   8230  C  CB  . THR H  1 59  ? 192.605 65.756  62.943 1.00   20.41 ? 58   THR H CB  1 
ATOM   8231  O  OG1 . THR H  1 59  ? 191.888 65.713  64.193 1.00   20.87 ? 58   THR H OG1 1 
ATOM   8232  C  CG2 . THR H  1 59  ? 192.845 67.226  62.532 1.00   20.47 ? 58   THR H CG2 1 
ATOM   8233  N  N   . SER H  1 60  ? 193.397 63.823  60.529 1.00   17.79 ? 59   SER H N   1 
ATOM   8234  C  CA  . SER H  1 60  ? 194.288 63.666  59.414 1.00   17.58 ? 59   SER H CA  1 
ATOM   8235  C  C   . SER H  1 60  ? 193.578 63.253  58.118 1.00   16.84 ? 59   SER H C   1 
ATOM   8236  O  O   . SER H  1 60  ? 194.222 63.196  57.070 1.00   17.14 ? 59   SER H O   1 
ATOM   8237  C  CB  . SER H  1 60  ? 195.466 62.770  59.777 1.00   17.96 ? 59   SER H CB  1 
ATOM   8238  O  OG  . SER H  1 60  ? 195.015 61.569  60.310 1.00   18.38 ? 59   SER H OG  1 
ATOM   8239  N  N   . ALA H  1 61  ? 192.260 63.045  58.142 1.00   16.01 ? 60   ALA H N   1 
ATOM   8240  C  CA  . ALA H  1 61  ? 191.518 62.759  56.883 1.00   15.66 ? 60   ALA H CA  1 
ATOM   8241  C  C   . ALA H  1 61  ? 191.385 63.978  55.966 1.00   15.63 ? 60   ALA H C   1 
ATOM   8242  O  O   . ALA H  1 61  ? 190.960 63.852  54.816 1.00   15.39 ? 60   ALA H O   1 
ATOM   8243  C  CB  . ALA H  1 61  ? 190.127 62.185  57.177 1.00   15.22 ? 60   ALA H CB  1 
ATOM   8244  N  N   . GLY H  1 62  ? 191.741 65.154  56.473 1.00   15.62 ? 61   GLY H N   1 
ATOM   8245  C  CA  . GLY H  1 62  ? 191.700 66.386  55.686 1.00   15.66 ? 61   GLY H CA  1 
ATOM   8246  C  C   . GLY H  1 62  ? 190.271 66.843  55.440 1.00   15.41 ? 61   GLY H C   1 
ATOM   8247  O  O   . GLY H  1 62  ? 189.371 66.442  56.144 1.00   15.07 ? 61   GLY H O   1 
ATOM   8248  N  N   . PRO H  1 63  ? 190.060 67.683  54.418 1.00   15.38 ? 62   PRO H N   1 
ATOM   8249  C  CA  . PRO H  1 63  ? 188.760 68.274  54.181 1.00   15.09 ? 62   PRO H CA  1 
ATOM   8250  C  C   . PRO H  1 63  ? 187.876 67.355  53.379 1.00   14.65 ? 62   PRO H C   1 
ATOM   8251  O  O   . PRO H  1 63  ? 188.237 66.190  53.108 1.00   14.29 ? 62   PRO H O   1 
ATOM   8252  C  CB  . PRO H  1 63  ? 189.098 69.570  53.435 1.00   15.50 ? 62   PRO H CB  1 
ATOM   8253  C  CG  . PRO H  1 63  ? 190.372 69.278  52.731 1.00   15.77 ? 62   PRO H CG  1 
ATOM   8254  C  CD  . PRO H  1 63  ? 191.092 68.217  53.514 1.00   15.67 ? 62   PRO H CD  1 
ATOM   8255  N  N   . HIS H  1 64  ? 186.717 67.849  52.975 1.00   14.53 ? 63   HIS H N   1 
ATOM   8256  C  CA  . HIS H  1 64  ? 185.842 67.007  52.142 1.00   14.33 ? 63   HIS H CA  1 
ATOM   8257  C  C   . HIS H  1 64  ? 186.471 66.689  50.840 1.00   14.58 ? 63   HIS H C   1 
ATOM   8258  O  O   . HIS H  1 64  ? 187.192 67.518  50.291 1.00   14.82 ? 63   HIS H O   1 
ATOM   8259  C  CB  . HIS H  1 64  ? 184.519 67.666  51.912 1.00   14.24 ? 63   HIS H CB  1 
ATOM   8260  C  CG  . HIS H  1 64  ? 183.749 67.873  53.154 1.00   14.17 ? 63   HIS H CG  1 
ATOM   8261  N  ND1 . HIS H  1 64  ? 182.588 68.537  53.187 1.00   14.15 ? 63   HIS H ND1 1 
ATOM   8262  C  CD2 . HIS H  1 64  ? 184.023 67.482  54.456 1.00   14.14 ? 63   HIS H CD2 1 
ATOM   8263  C  CE1 . HIS H  1 64  ? 182.130 68.536  54.462 1.00   14.12 ? 63   HIS H CE1 1 
ATOM   8264  N  NE2 . HIS H  1 64  ? 183.010 67.887  55.219 1.00   14.11 ? 63   HIS H NE2 1 
ATOM   8265  N  N   . PHE H  1 65  ? 186.179 65.497  50.314 1.00   14.59 ? 64   PHE H N   1 
ATOM   8266  C  CA  . PHE H  1 65  ? 186.645 65.083  48.997 1.00   14.90 ? 64   PHE H CA  1 
ATOM   8267  C  C   . PHE H  1 65  ? 185.963 65.972  47.975 1.00   15.37 ? 64   PHE H C   1 
ATOM   8268  O  O   . PHE H  1 65  ? 184.733 66.055  47.918 1.00   15.08 ? 64   PHE H O   1 
ATOM   8269  C  CB  . PHE H  1 65  ? 186.299 63.592  48.778 1.00   14.74 ? 64   PHE H CB  1 
ATOM   8270  C  CG  . PHE H  1 65  ? 186.689 63.041  47.434 1.00   14.97 ? 64   PHE H CG  1 
ATOM   8271  C  CD1 . PHE H  1 65  ? 187.883 63.378  46.838 1.00   15.30 ? 64   PHE H CD1 1 
ATOM   8272  C  CD2 . PHE H  1 65  ? 185.868 62.133  46.792 1.00   14.96 ? 64   PHE H CD2 1 
ATOM   8273  C  CE1 . PHE H  1 65  ? 188.241 62.858  45.609 1.00   15.52 ? 64   PHE H CE1 1 
ATOM   8274  C  CE2 . PHE H  1 65  ? 186.222 61.592  45.574 1.00   15.28 ? 64   PHE H CE2 1 
ATOM   8275  C  CZ  . PHE H  1 65  ? 187.417 61.960  44.972 1.00   15.53 ? 64   PHE H CZ  1 
ATOM   8276  N  N   . ASN H  1 66  ? 186.777 66.657  47.176 1.00   16.11 ? 65   ASN H N   1 
ATOM   8277  C  CA  . ASN H  1 66  ? 186.314 67.792  46.384 1.00   16.54 ? 65   ASN H CA  1 
ATOM   8278  C  C   . ASN H  1 66  ? 187.162 67.939  45.120 1.00   17.66 ? 65   ASN H C   1 
ATOM   8279  O  O   . ASN H  1 66  ? 187.765 68.979  44.878 1.00   17.88 ? 65   ASN H O   1 
ATOM   8280  C  CB  . ASN H  1 66  ? 186.401 69.069  47.224 1.00   16.31 ? 65   ASN H CB  1 
ATOM   8281  C  CG  . ASN H  1 66  ? 185.722 70.271  46.563 1.00   16.45 ? 65   ASN H CG  1 
ATOM   8282  O  OD1 . ASN H  1 66  ? 184.834 70.119  45.694 1.00   16.31 ? 65   ASN H OD1 1 
ATOM   8283  N  ND2 . ASN H  1 66  ? 186.128 71.464  46.965 1.00   16.26 ? 65   ASN H ND2 1 
ATOM   8284  N  N   . PRO H  1 67  ? 187.195 66.898  44.283 1.00   18.53 ? 66   PRO H N   1 
ATOM   8285  C  CA  . PRO H  1 67  ? 188.048 67.004  43.113 1.00   19.71 ? 66   PRO H CA  1 
ATOM   8286  C  C   . PRO H  1 67  ? 187.628 68.116  42.171 1.00   20.91 ? 66   PRO H C   1 
ATOM   8287  O  O   . PRO H  1 67  ? 188.476 68.612  41.450 1.00   22.43 ? 66   PRO H O   1 
ATOM   8288  C  CB  . PRO H  1 67  ? 187.863 65.658  42.424 1.00   19.56 ? 66   PRO H CB  1 
ATOM   8289  C  CG  . PRO H  1 67  ? 186.463 65.264  42.807 1.00   19.03 ? 66   PRO H CG  1 
ATOM   8290  C  CD  . PRO H  1 67  ? 186.388 65.670  44.259 1.00   18.46 ? 66   PRO H CD  1 
ATOM   8291  N  N   . LEU H  1 68  ? 186.354 68.512  42.167 1.00   21.34 ? 67   LEU H N   1 
ATOM   8292  C  CA  . LEU H  1 68  ? 185.919 69.614  41.282 1.00   22.22 ? 67   LEU H CA  1 
ATOM   8293  C  C   . LEU H  1 68  ? 186.010 71.007  41.924 1.00   22.67 ? 67   LEU H C   1 
ATOM   8294  O  O   . LEU H  1 68  ? 185.519 71.989  41.371 1.00   23.24 ? 67   LEU H O   1 
ATOM   8295  C  CB  . LEU H  1 68  ? 184.514 69.334  40.753 1.00   22.28 ? 67   LEU H CB  1 
ATOM   8296  C  CG  . LEU H  1 68  ? 184.429 68.090  39.864 1.00   22.63 ? 67   LEU H CG  1 
ATOM   8297  C  CD1 . LEU H  1 68  ? 182.984 67.682  39.584 1.00   22.51 ? 67   LEU H CD1 1 
ATOM   8298  C  CD2 . LEU H  1 68  ? 185.167 68.356  38.549 1.00   23.60 ? 67   LEU H CD2 1 
ATOM   8299  N  N   . SER H  1 69  ? 186.655 71.103  43.084 1.00   22.84 ? 68   SER H N   1 
ATOM   8300  C  CA  . SER H  1 69  ? 186.875 72.396  43.746 1.00   23.17 ? 68   SER H CA  1 
ATOM   8301  C  C   . SER H  1 69  ? 185.606 73.230  43.813 1.00   23.16 ? 68   SER H C   1 
ATOM   8302  O  O   . SER H  1 69  ? 185.606 74.373  43.399 1.00   22.92 ? 68   SER H O   1 
ATOM   8303  C  CB  . SER H  1 69  ? 187.984 73.202  43.044 1.00   23.84 ? 68   SER H CB  1 
ATOM   8304  O  OG  . SER H  1 69  ? 189.157 72.430  42.895 1.00   24.48 ? 68   SER H OG  1 
ATOM   8305  N  N   . ARG H  1 70  ? 184.533 72.664  44.361 1.00   23.37 ? 69   ARG H N   1 
ATOM   8306  C  CA  . ARG H  1 70  ? 183.283 73.406  44.509 1.00   24.13 ? 69   ARG H CA  1 
ATOM   8307  C  C   . ARG H  1 70  ? 183.080 73.755  45.969 1.00   22.90 ? 69   ARG H C   1 
ATOM   8308  O  O   . ARG H  1 70  ? 183.861 73.324  46.837 1.00   22.12 ? 69   ARG H O   1 
ATOM   8309  C  CB  . ARG H  1 70  ? 182.084 72.595  44.018 1.00   26.06 ? 69   ARG H CB  1 
ATOM   8310  C  CG  . ARG H  1 70  ? 182.233 71.992  42.636 1.00   29.22 ? 69   ARG H CG  1 
ATOM   8311  C  CD  . ARG H  1 70  ? 181.866 72.926  41.507 1.00   33.27 ? 69   ARG H CD  1 
ATOM   8312  N  NE  . ARG H  1 70  ? 181.932 72.238  40.204 1.00   38.04 ? 69   ARG H NE  1 
ATOM   8313  C  CZ  . ARG H  1 70  ? 180.929 71.556  39.628 1.00   42.02 ? 69   ARG H CZ  1 
ATOM   8314  N  NH1 . ARG H  1 70  ? 179.734 71.451  40.212 1.00   42.64 ? 69   ARG H NH1 1 
ATOM   8315  N  NH2 . ARG H  1 70  ? 181.126 70.973  38.440 1.00   42.83 ? 69   ARG H NH2 1 
ATOM   8316  N  N   . LYS H  1 71  ? 182.048 74.546  46.241 1.00   21.64 ? 70   LYS H N   1 
ATOM   8317  C  CA  . LYS H  1 71  ? 181.653 74.834  47.601 1.00   20.94 ? 70   LYS H CA  1 
ATOM   8318  C  C   . LYS H  1 71  ? 180.795 73.693  48.163 1.00   19.47 ? 70   LYS H C   1 
ATOM   8319  O  O   . LYS H  1 71  ? 180.162 72.946  47.404 1.00   18.68 ? 70   LYS H O   1 
ATOM   8320  C  CB  . LYS H  1 71  ? 180.882 76.148  47.672 1.00   22.17 ? 70   LYS H CB  1 
ATOM   8321  C  CG  . LYS H  1 71  ? 181.704 77.402  47.301 1.00   23.57 ? 70   LYS H CG  1 
ATOM   8322  C  CD  . LYS H  1 71  ? 180.779 78.556  46.943 1.00   24.73 ? 70   LYS H CD  1 
ATOM   8323  C  CE  . LYS H  1 71  ? 181.553 79.878  46.828 1.00   26.68 ? 70   LYS H CE  1 
ATOM   8324  N  NZ  . LYS H  1 71  ? 181.997 81.362  47.380 0.0000 51.47 ? 70   LYS H NZ  1 
ATOM   8325  N  N   . HIS H  1 72  ? 180.787 73.585  49.497 1.00   17.89 ? 71   HIS H N   1 
ATOM   8326  C  CA  . HIS H  1 72  ? 179.970 72.612  50.216 1.00   17.02 ? 71   HIS H CA  1 
ATOM   8327  C  C   . HIS H  1 72  ? 178.490 72.780  49.916 1.00   17.02 ? 71   HIS H C   1 
ATOM   8328  O  O   . HIS H  1 72  ? 177.973 73.899  49.775 1.00   17.49 ? 71   HIS H O   1 
ATOM   8329  C  CB  . HIS H  1 72  ? 180.241 72.713  51.728 1.00   16.44 ? 71   HIS H CB  1 
ATOM   8330  C  CG  . HIS H  1 72  ? 179.482 71.696  52.566 1.00   15.86 ? 71   HIS H CG  1 
ATOM   8331  N  ND1 . HIS H  1 72  ? 179.920 70.431  52.768 1.00   15.46 ? 71   HIS H ND1 1 
ATOM   8332  C  CD2 . HIS H  1 72  ? 178.274 71.802  53.236 1.00   15.40 ? 71   HIS H CD2 1 
ATOM   8333  C  CE1 . HIS H  1 72  ? 179.032 69.784  53.530 1.00   15.15 ? 71   HIS H CE1 1 
ATOM   8334  N  NE2 . HIS H  1 72  ? 178.026 70.626  53.808 1.00   15.10 ? 71   HIS H NE2 1 
ATOM   8335  N  N   . GLY H  1 73  ? 177.808 71.650  49.807 1.00   16.60 ? 72   GLY H N   1 
ATOM   8336  C  CA  . GLY H  1 73  ? 176.383 71.612  49.623 1.00   16.57 ? 72   GLY H CA  1 
ATOM   8337  C  C   . GLY H  1 73  ? 175.790 70.356  50.207 1.00   16.30 ? 72   GLY H C   1 
ATOM   8338  O  O   . GLY H  1 73  ? 176.448 69.616  50.975 1.00   16.14 ? 72   GLY H O   1 
ATOM   8339  N  N   . GLY H  1 74  ? 174.527 70.154  49.887 1.00   16.21 ? 73   GLY H N   1 
ATOM   8340  C  CA  . GLY H  1 74  ? 173.834 68.923  50.197 1.00   16.18 ? 73   GLY H CA  1 
ATOM   8341  C  C   . GLY H  1 74  ? 173.937 67.984  48.999 1.00   16.18 ? 73   GLY H C   1 
ATOM   8342  O  O   . GLY H  1 74  ? 174.307 68.415  47.889 1.00   16.20 ? 73   GLY H O   1 
ATOM   8343  N  N   . PRO H  1 75  ? 173.635 66.701  49.211 1.00   16.02 ? 74   PRO H N   1 
ATOM   8344  C  CA  . PRO H  1 75  ? 173.818 65.769  48.115 1.00   16.50 ? 74   PRO H CA  1 
ATOM   8345  C  C   . PRO H  1 75  ? 172.903 66.047  46.917 1.00   17.16 ? 74   PRO H C   1 
ATOM   8346  O  O   . PRO H  1 75  ? 173.221 65.618  45.816 1.00   16.81 ? 74   PRO H O   1 
ATOM   8347  C  CB  . PRO H  1 75  ? 173.503 64.405  48.742 1.00   16.31 ? 74   PRO H CB  1 
ATOM   8348  C  CG  . PRO H  1 75  ? 172.659 64.729  49.939 1.00   16.18 ? 74   PRO H CG  1 
ATOM   8349  C  CD  . PRO H  1 75  ? 173.207 66.031  50.442 1.00   15.90 ? 74   PRO H CD  1 
ATOM   8350  N  N   . LYS H  1 76  ? 171.802 66.766  47.129 1.00   18.04 ? 75   LYS H N   1 
ATOM   8351  C  CA  . LYS H  1 76  ? 170.880 67.073  46.033 1.00   19.34 ? 75   LYS H CA  1 
ATOM   8352  C  C   . LYS H  1 76  ? 171.334 68.264  45.209 1.00   20.32 ? 75   LYS H C   1 
ATOM   8353  O  O   . LYS H  1 76  ? 170.765 68.506  44.152 1.00   20.56 ? 75   LYS H O   1 
ATOM   8354  C  CB  . LYS H  1 76  ? 169.461 67.324  46.547 1.00   19.48 ? 75   LYS H CB  1 
ATOM   8355  C  CG  . LYS H  1 76  ? 168.785 66.107  47.173 1.00   19.64 ? 75   LYS H CG  1 
ATOM   8356  C  CD  . LYS H  1 76  ? 167.602 66.550  48.063 1.00   19.95 ? 75   LYS H CD  1 
ATOM   8357  C  CE  . LYS H  1 76  ? 166.389 66.995  47.233 1.00   20.43 ? 75   LYS H CE  1 
ATOM   8358  N  NZ  . LYS H  1 76  ? 165.242 67.544  48.027 1.00   20.98 ? 75   LYS H NZ  1 
ATOM   8359  N  N   . ASP H  1 77  ? 172.343 69.008  45.681 1.00   20.92 ? 76   ASP H N   1 
ATOM   8360  C  CA  . ASP H  1 77  ? 172.810 70.195  44.967 1.00   22.12 ? 76   ASP H CA  1 
ATOM   8361  C  C   . ASP H  1 77  ? 173.822 69.885  43.867 1.00   22.82 ? 76   ASP H C   1 
ATOM   8362  O  O   . ASP H  1 77  ? 174.632 68.953  43.969 1.00   21.34 ? 76   ASP H O   1 
ATOM   8363  C  CB  . ASP H  1 77  ? 173.465 71.207  45.929 1.00   22.53 ? 76   ASP H CB  1 
ATOM   8364  C  CG  . ASP H  1 77  ? 172.570 71.599  47.051 1.00   22.87 ? 76   ASP H CG  1 
ATOM   8365  O  OD1 . ASP H  1 77  ? 171.380 71.775  46.769 1.00   26.36 ? 76   ASP H OD1 1 
ATOM   8366  O  OD2 . ASP H  1 77  ? 173.021 71.735  48.209 1.00   21.98 ? 76   ASP H OD2 1 
ATOM   8367  N  N   . GLU H  1 78  ? 173.808 70.728  42.841 1.00   24.16 ? 77   GLU H N   1 
ATOM   8368  C  CA  . GLU H  1 78  ? 174.836 70.689  41.812 1.00   26.04 ? 77   GLU H CA  1 
ATOM   8369  C  C   . GLU H  1 78  ? 176.129 71.251  42.401 1.00   24.10 ? 77   GLU H C   1 
ATOM   8370  O  O   . GLU H  1 78  ? 177.212 70.701  42.184 1.00   24.07 ? 77   GLU H O   1 
ATOM   8371  C  CB  . GLU H  1 78  ? 174.388 71.488  40.574 1.00   29.96 ? 77   GLU H CB  1 
ATOM   8372  C  CG  . GLU H  1 78  ? 174.881 70.933  39.244 1.00   34.32 ? 77   GLU H CG  1 
ATOM   8373  C  CD  . GLU H  1 78  ? 176.089 71.671  38.690 1.00   39.50 ? 77   GLU H CD  1 
ATOM   8374  O  OE1 . GLU H  1 78  ? 176.216 72.882  38.982 1.00   44.69 ? 77   GLU H OE1 1 
ATOM   8375  O  OE2 . GLU H  1 78  ? 176.909 71.052  37.942 1.00   44.42 ? 77   GLU H OE2 1 
ATOM   8376  N  N   . GLU H  1 79  ? 176.010 72.335  43.160 1.00   22.34 ? 78   GLU H N   1 
ATOM   8377  C  CA  . GLU H  1 79  ? 177.155 72.898  43.865 1.00   21.76 ? 78   GLU H CA  1 
ATOM   8378  C  C   . GLU H  1 79  ? 177.348 72.116  45.172 1.00   19.87 ? 78   GLU H C   1 
ATOM   8379  O  O   . GLU H  1 79  ? 176.705 72.382  46.172 1.00   19.50 ? 78   GLU H O   1 
ATOM   8380  C  CB  . GLU H  1 79  ? 176.995 74.414  44.133 1.00   22.37 ? 78   GLU H CB  1 
ATOM   8381  C  CG  . GLU H  1 79  ? 178.255 75.079  44.717 1.00   23.38 ? 78   GLU H CG  1 
ATOM   8382  C  CD  . GLU H  1 79  ? 179.402 75.243  43.711 1.00   24.87 ? 78   GLU H CD  1 
ATOM   8383  O  OE1 . GLU H  1 79  ? 179.191 75.007  42.487 1.00   26.84 ? 78   GLU H OE1 1 
ATOM   8384  O  OE2 . GLU H  1 79  ? 180.524 75.626  44.118 1.00   24.82 ? 78   GLU H OE2 1 
ATOM   8385  N  N   . ARG H  1 80  ? 178.227 71.127  45.128 1.00   18.45 ? 79   ARG H N   1 
ATOM   8386  C  CA  . ARG H  1 80  ? 178.543 70.308  46.299 1.00   17.19 ? 79   ARG H CA  1 
ATOM   8387  C  C   . ARG H  1 80  ? 179.917 69.717  46.113 1.00   16.66 ? 79   ARG H C   1 
ATOM   8388  O  O   . ARG H  1 80  ? 180.420 69.636  44.991 1.00   17.12 ? 79   ARG H O   1 
ATOM   8389  C  CB  . ARG H  1 80  ? 177.551 69.165  46.453 1.00   16.65 ? 79   ARG H CB  1 
ATOM   8390  C  CG  . ARG H  1 80  ? 177.489 68.232  45.254 1.00   16.56 ? 79   ARG H CG  1 
ATOM   8391  C  CD  . ARG H  1 80  ? 176.626 67.020  45.529 1.00   16.18 ? 79   ARG H CD  1 
ATOM   8392  N  NE  . ARG H  1 80  ? 177.402 65.886  46.055 1.00   15.75 ? 79   ARG H NE  1 
ATOM   8393  C  CZ  . ARG H  1 80  ? 176.955 64.631  46.113 1.00   15.51 ? 79   ARG H CZ  1 
ATOM   8394  N  NH1 . ARG H  1 80  ? 175.735 64.314  45.712 1.00   15.59 ? 79   ARG H NH1 1 
ATOM   8395  N  NH2 . ARG H  1 80  ? 177.728 63.684  46.585 1.00   15.27 ? 79   ARG H NH2 1 
ATOM   8396  N  N   . HIS H  1 81  ? 180.526 69.311  47.215 1.00   15.69 ? 80   HIS H N   1 
ATOM   8397  C  CA  . HIS H  1 81  ? 181.696 68.486  47.131 1.00   15.08 ? 80   HIS H CA  1 
ATOM   8398  C  C   . HIS H  1 81  ? 181.263 67.104  46.735 1.00   14.53 ? 80   HIS H C   1 
ATOM   8399  O  O   . HIS H  1 81  ? 180.175 66.692  47.080 1.00   14.14 ? 80   HIS H O   1 
ATOM   8400  C  CB  . HIS H  1 81  ? 182.392 68.426  48.469 1.00   14.88 ? 80   HIS H CB  1 
ATOM   8401  C  CG  . HIS H  1 81  ? 182.781 69.770  49.033 1.00   15.01 ? 80   HIS H CG  1 
ATOM   8402  N  ND1 . HIS H  1 81  ? 182.687 70.065  50.356 1.00   14.66 ? 80   HIS H ND1 1 
ATOM   8403  C  CD2 . HIS H  1 81  ? 183.313 70.891  48.414 1.00   15.29 ? 80   HIS H CD2 1 
ATOM   8404  C  CE1 . HIS H  1 81  ? 183.135 71.317  50.545 1.00   14.94 ? 80   HIS H CE1 1 
ATOM   8405  N  NE2 . HIS H  1 81  ? 183.553 71.803  49.364 1.00   15.22 ? 80   HIS H NE2 1 
ATOM   8406  N  N   . VAL H  1 82  ? 182.103 66.356  46.022 1.00   14.25 ? 81   VAL H N   1 
ATOM   8407  C  CA  . VAL H  1 82  ? 181.786 64.934  45.770 1.00   13.99 ? 81   VAL H CA  1 
ATOM   8408  C  C   . VAL H  1 82  ? 181.495 64.186  47.079 1.00   13.54 ? 81   VAL H C   1 
ATOM   8409  O  O   . VAL H  1 82  ? 180.595 63.367  47.150 1.00   13.40 ? 81   VAL H O   1 
ATOM   8410  C  CB  . VAL H  1 82  ? 182.906 64.201  44.993 1.00   14.11 ? 81   VAL H CB  1 
ATOM   8411  C  CG1 . VAL H  1 82  ? 182.662 62.699  44.991 1.00   13.96 ? 81   VAL H CG1 1 
ATOM   8412  C  CG2 . VAL H  1 82  ? 183.004 64.727  43.567 1.00   14.51 ? 81   VAL H CG2 1 
ATOM   8413  N  N   . GLY H  1 83  ? 182.253 64.467  48.128 1.00   13.38 ? 82   GLY H N   1 
ATOM   8414  C  CA  . GLY H  1 83  ? 182.053 63.793  49.404 1.00   13.19 ? 82   GLY H CA  1 
ATOM   8415  C  C   . GLY H  1 83  ? 180.809 64.153  50.218 1.00   13.11 ? 82   GLY H C   1 
ATOM   8416  O  O   . GLY H  1 83  ? 180.596 63.583  51.317 1.00   12.94 ? 82   GLY H O   1 
ATOM   8417  N  N   . ASP H  1 84  ? 179.953 65.041  49.695 1.00   13.13 ? 83   ASP H N   1 
ATOM   8418  C  CA  . ASP H  1 84  ? 178.848 65.581  50.483 1.00   13.09 ? 83   ASP H CA  1 
ATOM   8419  C  C   . ASP H  1 84  ? 177.625 64.695  50.473 1.00   13.13 ? 83   ASP H C   1 
ATOM   8420  O  O   . ASP H  1 84  ? 176.791 64.821  49.600 1.00   13.39 ? 83   ASP H O   1 
ATOM   8421  C  CB  . ASP H  1 84  ? 178.460 66.988  49.978 1.00   13.23 ? 83   ASP H CB  1 
ATOM   8422  C  CG  . ASP H  1 84  ? 179.484 68.067  50.342 1.00   13.30 ? 83   ASP H CG  1 
ATOM   8423  O  OD1 . ASP H  1 84  ? 180.423 67.842  51.139 1.00   13.12 ? 83   ASP H OD1 1 
ATOM   8424  O  OD2 . ASP H  1 84  ? 179.347 69.186  49.807 1.00   13.59 ? 83   ASP H OD2 1 
ATOM   8425  N  N   . LEU H  1 85  ? 177.481 63.823  51.463 1.00   13.03 ? 84   LEU H N   1 
ATOM   8426  C  CA  . LEU H  1 85  ? 176.354 62.919  51.546 1.00   13.09 ? 84   LEU H CA  1 
ATOM   8427  C  C   . LEU H  1 85  ? 175.286 63.394  52.540 1.00   13.29 ? 84   LEU H C   1 
ATOM   8428  O  O   . LEU H  1 85  ? 174.341 62.672  52.844 1.00   13.61 ? 84   LEU H O   1 
ATOM   8429  C  CB  . LEU H  1 85  ? 176.829 61.500  51.879 1.00   12.98 ? 84   LEU H CB  1 
ATOM   8430  C  CG  . LEU H  1 85  ? 177.781 60.856  50.846 1.00   12.98 ? 84   LEU H CG  1 
ATOM   8431  C  CD1 . LEU H  1 85  ? 178.219 59.499  51.362 1.00   12.84 ? 84   LEU H CD1 1 
ATOM   8432  C  CD2 . LEU H  1 85  ? 177.147 60.742  49.462 1.00   13.08 ? 84   LEU H CD2 1 
ATOM   8433  N  N   . GLY H  1 86  ? 175.387 64.632  52.990 1.00   13.38 ? 85   GLY H N   1 
ATOM   8434  C  CA  . GLY H  1 86  ? 174.347 65.232  53.810 1.00   13.50 ? 85   GLY H CA  1 
ATOM   8435  C  C   . GLY H  1 86  ? 174.311 64.766  55.243 1.00   13.55 ? 85   GLY H C   1 
ATOM   8436  O  O   . GLY H  1 86  ? 175.343 64.650  55.915 1.00   13.64 ? 85   GLY H O   1 
ATOM   8437  N  N   . ASN H  1 87  ? 173.114 64.501  55.723 1.00   13.68 ? 86   ASN H N   1 
ATOM   8438  C  CA  . ASN H  1 87  ? 172.919 64.097  57.092 1.00   13.91 ? 86   ASN H CA  1 
ATOM   8439  C  C   . ASN H  1 87  ? 172.447 62.657  57.239 1.00   14.15 ? 86   ASN H C   1 
ATOM   8440  O  O   . ASN H  1 87  ? 171.751 62.133  56.378 1.00   14.43 ? 86   ASN H O   1 
ATOM   8441  C  CB  . ASN H  1 87  ? 171.877 65.018  57.746 1.00   13.97 ? 86   ASN H CB  1 
ATOM   8442  C  CG  . ASN H  1 87  ? 172.437 66.375  58.079 1.00   13.93 ? 86   ASN H CG  1 
ATOM   8443  O  OD1 . ASN H  1 87  ? 173.400 66.479  58.853 1.00   14.08 ? 86   ASN H OD1 1 
ATOM   8444  N  ND2 . ASN H  1 87  ? 171.820 67.420  57.558 1.00   13.70 ? 86   ASN H ND2 1 
ATOM   8445  N  N   . VAL H  1 88  ? 172.819 62.045  58.345 1.00   14.41 ? 87   VAL H N   1 
ATOM   8446  C  CA  . VAL H  1 88  ? 172.159 60.826  58.824 1.00   14.96 ? 87   VAL H CA  1 
ATOM   8447  C  C   . VAL H  1 88  ? 171.410 61.156  60.121 1.00   15.54 ? 87   VAL H C   1 
ATOM   8448  O  O   . VAL H  1 88  ? 171.735 62.139  60.810 1.00   15.57 ? 87   VAL H O   1 
ATOM   8449  C  CB  . VAL H  1 88  ? 173.169 59.671  59.003 1.00   14.86 ? 87   VAL H CB  1 
ATOM   8450  C  CG1 . VAL H  1 88  ? 173.798 59.322  57.659 1.00   14.50 ? 87   VAL H CG1 1 
ATOM   8451  C  CG2 . VAL H  1 88  ? 174.228 60.009  60.028 1.00   14.73 ? 87   VAL H CG2 1 
ATOM   8452  N  N   . THR H  1 89  ? 170.392 60.363  60.438 1.00   16.21 ? 88   THR H N   1 
ATOM   8453  C  CA  . THR H  1 89  ? 169.528 60.620  61.602 1.00   16.81 ? 88   THR H CA  1 
ATOM   8454  C  C   . THR H  1 89  ? 169.613 59.486  62.609 1.00   17.51 ? 88   THR H C   1 
ATOM   8455  O  O   . THR H  1 89  ? 169.347 58.316  62.282 1.00   17.80 ? 88   THR H O   1 
ATOM   8456  C  CB  . THR H  1 89  ? 168.062 60.789  61.155 1.00   16.97 ? 88   THR H CB  1 
ATOM   8457  O  OG1 . THR H  1 89  ? 167.977 61.880  60.216 1.00   16.46 ? 88   THR H OG1 1 
ATOM   8458  C  CG2 . THR H  1 89  ? 167.119 61.032  62.366 1.00   17.15 ? 88   THR H CG2 1 
ATOM   8459  N  N   . ALA H  1 90  ? 170.010 59.838  63.832 1.00   18.36 ? 89   ALA H N   1 
ATOM   8460  C  CA  . ALA H  1 90  ? 170.090 58.883  64.936 1.00   19.48 ? 89   ALA H CA  1 
ATOM   8461  C  C   . ALA H  1 90  ? 168.766 58.910  65.682 1.00   20.83 ? 89   ALA H C   1 
ATOM   8462  O  O   . ALA H  1 90  ? 168.272 59.975  66.016 1.00   20.33 ? 89   ALA H O   1 
ATOM   8463  C  CB  . ALA H  1 90  ? 171.235 59.235  65.882 1.00   19.25 ? 89   ALA H CB  1 
ATOM   8464  N  N   . ASP H  1 91  ? 168.209 57.732  65.942 1.00   22.44 ? 90   ASP H N   1 
ATOM   8465  C  CA  . ASP H  1 91  ? 166.961 57.627  66.675 1.00   24.21 ? 90   ASP H CA  1 
ATOM   8466  C  C   . ASP H  1 91  ? 167.209 57.816  68.165 1.00   25.43 ? 90   ASP H C   1 
ATOM   8467  O  O   . ASP H  1 91  ? 168.345 58.073  68.587 1.00   24.72 ? 90   ASP H O   1 
ATOM   8468  C  CB  . ASP H  1 91  ? 166.240 56.306  66.363 1.00   25.06 ? 90   ASP H CB  1 
ATOM   8469  C  CG  . ASP H  1 91  ? 167.022 55.057  66.802 1.00   25.97 ? 90   ASP H CG  1 
ATOM   8470  O  OD1 . ASP H  1 91  ? 167.802 55.094  67.800 1.00   25.47 ? 90   ASP H OD1 1 
ATOM   8471  O  OD2 . ASP H  1 91  ? 166.822 54.003  66.130 1.00   27.24 ? 90   ASP H OD2 1 
ATOM   8472  N  N   . LYS H  1 92  ? 166.138 57.686  68.951 1.00   27.35 ? 91   LYS H N   1 
ATOM   8473  C  CA  . LYS H  1 92  ? 166.168 57.909  70.396 1.00   28.88 ? 91   LYS H CA  1 
ATOM   8474  C  C   . LYS H  1 92  ? 167.050 56.917  71.167 1.00   28.98 ? 91   LYS H C   1 
ATOM   8475  O  O   . LYS H  1 92  ? 167.490 57.214  72.266 1.00   29.32 ? 91   LYS H O   1 
ATOM   8476  C  CB  . LYS H  1 92  ? 164.730 57.883  70.951 1.00   31.01 ? 91   LYS H CB  1 
ATOM   8477  C  CG  . LYS H  1 92  ? 164.095 56.488  71.001 1.00   33.03 ? 91   LYS H CG  1 
ATOM   8478  C  CD  . LYS H  1 92  ? 162.567 56.523  71.167 1.00   35.07 ? 91   LYS H CD  1 
ATOM   8479  C  CE  . LYS H  1 92  ? 161.991 55.109  71.165 1.00   36.24 ? 91   LYS H CE  1 
ATOM   8480  N  NZ  . LYS H  1 92  ? 160.499 55.086  71.039 1.00   38.87 ? 91   LYS H NZ  1 
ATOM   8481  N  N   . ASP H  1 93  ? 167.306 55.748  70.598 1.00   28.62 ? 92   ASP H N   1 
ATOM   8482  C  CA  . ASP H  1 93  ? 168.224 54.787  71.208 1.00   29.57 ? 92   ASP H CA  1 
ATOM   8483  C  C   . ASP H  1 93  ? 169.688 54.953  70.760 1.00   28.50 ? 92   ASP H C   1 
ATOM   8484  O  O   . ASP H  1 93  ? 170.526 54.106  71.065 1.00   27.93 ? 92   ASP H O   1 
ATOM   8485  C  CB  . ASP H  1 93  ? 167.754 53.380  70.882 1.00   31.35 ? 92   ASP H CB  1 
ATOM   8486  C  CG  . ASP H  1 93  ? 166.361 53.112  71.406 1.00   34.52 ? 92   ASP H CG  1 
ATOM   8487  O  OD1 . ASP H  1 93  ? 166.046 53.559  72.541 1.00   36.93 ? 92   ASP H OD1 1 
ATOM   8488  O  OD2 . ASP H  1 93  ? 165.565 52.482  70.676 1.00   37.56 ? 92   ASP H OD2 1 
ATOM   8489  N  N   . GLY H  1 94  ? 169.975 56.017  70.004 1.00   26.59 ? 93   GLY H N   1 
ATOM   8490  C  CA  . GLY H  1 94  ? 171.340 56.335  69.610 1.00   25.38 ? 93   GLY H CA  1 
ATOM   8491  C  C   . GLY H  1 94  ? 171.834 55.732  68.306 1.00   23.91 ? 93   GLY H C   1 
ATOM   8492  O  O   . GLY H  1 94  ? 173.032 55.820  67.998 1.00   23.23 ? 93   GLY H O   1 
ATOM   8493  N  N   . VAL H  1 95  ? 170.935 55.131  67.537 1.00   23.12 ? 94   VAL H N   1 
ATOM   8494  C  CA  . VAL H  1 95  ? 171.325 54.412  66.341 1.00   22.41 ? 94   VAL H CA  1 
ATOM   8495  C  C   . VAL H  1 95  ? 170.839 55.156  65.100 1.00   21.92 ? 94   VAL H C   1 
ATOM   8496  O  O   . VAL H  1 95  ? 169.653 55.529  65.004 1.00   21.87 ? 94   VAL H O   1 
ATOM   8497  C  CB  . VAL H  1 95  ? 170.731 53.003  66.290 1.00   22.97 ? 94   VAL H CB  1 
ATOM   8498  C  CG1 . VAL H  1 95  ? 171.188 52.288  65.011 1.00   22.44 ? 94   VAL H CG1 1 
ATOM   8499  C  CG2 . VAL H  1 95  ? 171.111 52.194  67.542 1.00   23.25 ? 94   VAL H CG2 1 
ATOM   8500  N  N   . ALA H  1 96  ? 171.756 55.353  64.156 1.00   20.78 ? 95   ALA H N   1 
ATOM   8501  C  CA  . ALA H  1 96  ? 171.419 55.871  62.846 1.00   20.62 ? 95   ALA H CA  1 
ATOM   8502  C  C   . ALA H  1 96  ? 171.432 54.689  61.906 1.00   20.79 ? 95   ALA H C   1 
ATOM   8503  O  O   . ALA H  1 96  ? 172.513 54.129  61.642 1.00   20.32 ? 95   ALA H O   1 
ATOM   8504  C  CB  . ALA H  1 96  ? 172.445 56.925  62.394 1.00   19.68 ? 95   ALA H CB  1 
ATOM   8505  N  N   . ASP H  1 97  ? 170.250 54.286  61.428 1.00   21.61 ? 96   ASP H N   1 
ATOM   8506  C  CA  . ASP H  1 97  ? 170.141 53.266  60.380 1.00   22.03 ? 96   ASP H CA  1 
ATOM   8507  C  C   . ASP H  1 97  ? 170.232 53.924  59.019 1.00   21.46 ? 96   ASP H C   1 
ATOM   8508  O  O   . ASP H  1 97  ? 169.220 54.361  58.456 1.00   22.62 ? 96   ASP H O   1 
ATOM   8509  C  CB  . ASP H  1 97  ? 168.835 52.499  60.486 1.00   23.27 ? 96   ASP H CB  1 
ATOM   8510  C  CG  . ASP H  1 97  ? 168.821 51.568  61.684 1.00   24.44 ? 96   ASP H CG  1 
ATOM   8511  O  OD1 . ASP H  1 97  ? 169.754 50.733  61.793 1.00   24.88 ? 96   ASP H OD1 1 
ATOM   8512  O  OD2 . ASP H  1 97  ? 167.897 51.711  62.506 1.00   25.01 ? 96   ASP H OD2 1 
ATOM   8513  N  N   . VAL H  1 98  ? 171.440 53.963  58.485 1.00   20.27 ? 97   VAL H N   1 
ATOM   8514  C  CA  . VAL H  1 98  ? 171.739 54.703  57.281 1.00   19.48 ? 97   VAL H CA  1 
ATOM   8515  C  C   . VAL H  1 98  ? 171.218 53.984  56.028 1.00   19.86 ? 97   VAL H C   1 
ATOM   8516  O  O   . VAL H  1 98  ? 171.373 52.779  55.900 1.00   20.23 ? 97   VAL H O   1 
ATOM   8517  C  CB  . VAL H  1 98  ? 173.253 54.913  57.188 1.00   18.75 ? 97   VAL H CB  1 
ATOM   8518  C  CG1 . VAL H  1 98  ? 173.604 55.683  55.932 1.00   18.06 ? 97   VAL H CG1 1 
ATOM   8519  C  CG2 . VAL H  1 98  ? 173.735 55.614  58.466 1.00   18.36 ? 97   VAL H CG2 1 
ATOM   8520  N  N   . SER H  1 99  ? 170.615 54.741  55.122 1.00   20.01 ? 98   SER H N   1 
ATOM   8521  C  CA  . SER H  1 99  ? 170.167 54.250  53.829 1.00   20.74 ? 98   SER H CA  1 
ATOM   8522  C  C   . SER H  1 99  ? 170.063 55.458  52.893 1.00   20.65 ? 98   SER H C   1 
ATOM   8523  O  O   . SER H  1 99  ? 169.132 56.267  52.979 1.00   21.13 ? 98   SER H O   1 
ATOM   8524  C  CB  . SER H  1 99  ? 168.820 53.545  53.943 1.00   21.69 ? 98   SER H CB  1 
ATOM   8525  O  OG  . SER H  1 99  ? 168.468 52.873  52.730 1.00   22.77 ? 98   SER H OG  1 
ATOM   8526  N  N   . ILE H  1 100 ? 171.048 55.551  52.016 1.00   20.10 ? 99   ILE H N   1 
ATOM   8527  C  CA  . ILE H  1 100 ? 171.306 56.661  51.137 1.00   20.00 ? 99   ILE H CA  1 
ATOM   8528  C  C   . ILE H  1 100 ? 171.634 56.042  49.770 1.00   20.24 ? 99   ILE H C   1 
ATOM   8529  O  O   . ILE H  1 100 ? 172.188 54.921  49.685 1.00   19.76 ? 99   ILE H O   1 
ATOM   8530  C  CB  . ILE H  1 100 ? 172.533 57.443  51.651 1.00   19.96 ? 99   ILE H CB  1 
ATOM   8531  C  CG1 . ILE H  1 100 ? 172.126 58.430  52.758 1.00   20.08 ? 99   ILE H CG1 1 
ATOM   8532  C  CG2 . ILE H  1 100 ? 173.224 58.219  50.539 1.00   20.05 ? 99   ILE H CG2 1 
ATOM   8533  C  CD1 . ILE H  1 100 ? 173.342 59.160  53.331 1.00   19.61 ? 99   ILE H CD1 1 
ATOM   8534  N  N   . GLU H  1 101 ? 171.239 56.736  48.710 1.00   20.25 ? 100  GLU H N   1 
ATOM   8535  C  CA  . GLU H  1 101 ? 171.722 56.438  47.393 1.00   20.66 ? 100  GLU H CA  1 
ATOM   8536  C  C   . GLU H  1 101 ? 172.274 57.737  46.821 1.00   19.70 ? 100  GLU H C   1 
ATOM   8537  O  O   . GLU H  1 101 ? 171.640 58.783  46.943 1.00   19.36 ? 100  GLU H O   1 
ATOM   8538  C  CB  . GLU H  1 101 ? 170.567 55.908  46.539 1.00   22.87 ? 100  GLU H CB  1 
ATOM   8539  C  CG  . GLU H  1 101 ? 170.933 55.637  45.096 1.00   24.49 ? 100  GLU H CG  1 
ATOM   8540  C  CD  . GLU H  1 101 ? 169.744 55.140  44.280 1.00   26.74 ? 100  GLU H CD  1 
ATOM   8541  O  OE1 . GLU H  1 101 ? 169.362 53.968  44.465 1.00   26.84 ? 100  GLU H OE1 1 
ATOM   8542  O  OE2 . GLU H  1 101 ? 169.210 55.943  43.469 1.00   29.16 ? 100  GLU H OE2 1 
ATOM   8543  N  N   . ASP H  1 102 ? 173.430 57.675  46.163 1.00   18.66 ? 101  ASP H N   1 
ATOM   8544  C  CA  . ASP H  1 102 ? 174.045 58.876  45.617 1.00   18.08 ? 101  ASP H CA  1 
ATOM   8545  C  C   . ASP H  1 102 ? 174.729 58.570  44.287 1.00   18.21 ? 101  ASP H C   1 
ATOM   8546  O  O   . ASP H  1 102 ? 175.338 57.513  44.131 1.00   18.12 ? 101  ASP H O   1 
ATOM   8547  C  CB  . ASP H  1 102 ? 175.069 59.414  46.619 1.00   17.53 ? 101  ASP H CB  1 
ATOM   8548  C  CG  . ASP H  1 102 ? 175.520 60.799  46.279 1.00   17.56 ? 101  ASP H CG  1 
ATOM   8549  O  OD1 . ASP H  1 102 ? 174.765 61.760  46.575 1.00   17.07 ? 101  ASP H OD1 1 
ATOM   8550  O  OD2 . ASP H  1 102 ? 176.637 60.912  45.696 1.00   17.69 ? 101  ASP H OD2 1 
ATOM   8551  N  N   . SER H  1 103 ? 174.636 59.497  43.338 1.00   18.23 ? 102  SER H N   1 
ATOM   8552  C  CA  . SER H  1 103 ? 175.123 59.277  41.972 1.00   18.38 ? 102  SER H CA  1 
ATOM   8553  C  C   . SER H  1 103 ? 176.338 60.118  41.648 1.00   17.83 ? 102  SER H C   1 
ATOM   8554  O  O   . SER H  1 103 ? 176.778 60.133  40.519 1.00   18.51 ? 102  SER H O   1 
ATOM   8555  C  CB  . SER H  1 103 ? 173.990 59.567  40.953 1.00   19.11 ? 102  SER H CB  1 
ATOM   8556  O  OG  . SER H  1 103 ? 173.136 58.437  40.876 0.50   19.31 ? 102  SER H OG  1 
ATOM   8557  N  N   . VAL H  1 104 ? 176.879 60.818  42.632 1.00   17.03 ? 103  VAL H N   1 
ATOM   8558  C  CA  . VAL H  1 104 ? 178.062 61.664  42.439 1.00   16.60 ? 103  VAL H CA  1 
ATOM   8559  C  C   . VAL H  1 104 ? 179.328 60.937  42.959 1.00   16.42 ? 103  VAL H C   1 
ATOM   8560  O  O   . VAL H  1 104 ? 180.365 60.915  42.283 1.00   16.54 ? 103  VAL H O   1 
ATOM   8561  C  CB  . VAL H  1 104 ? 177.851 63.035  43.112 1.00   16.28 ? 103  VAL H CB  1 
ATOM   8562  C  CG1 . VAL H  1 104 ? 179.131 63.861  43.125 1.00   15.90 ? 103  VAL H CG1 1 
ATOM   8563  C  CG2 . VAL H  1 104 ? 176.685 63.789  42.439 1.00   16.30 ? 103  VAL H CG2 1 
ATOM   8564  N  N   . ILE H  1 105 ? 179.237 60.330  44.142 1.00   16.07 ? 104  ILE H N   1 
ATOM   8565  C  CA  . ILE H  1 105 ? 180.272 59.393  44.573 1.00   15.92 ? 104  ILE H CA  1 
ATOM   8566  C  C   . ILE H  1 105 ? 180.298 58.196  43.596 1.00   16.24 ? 104  ILE H C   1 
ATOM   8567  O  O   . ILE H  1 105 ? 179.308 57.909  42.909 1.00   16.71 ? 104  ILE H O   1 
ATOM   8568  C  CB  . ILE H  1 105 ? 180.124 58.890  46.045 1.00   15.51 ? 104  ILE H CB  1 
ATOM   8569  C  CG1 . ILE H  1 105 ? 178.826 58.133  46.277 1.00   15.54 ? 104  ILE H CG1 1 
ATOM   8570  C  CG2 . ILE H  1 105 ? 180.298 60.009  47.074 1.00   15.14 ? 104  ILE H CG2 1 
ATOM   8571  C  CD1 . ILE H  1 105 ? 178.771 57.387  47.611 1.00   15.35 ? 104  ILE H CD1 1 
ATOM   8572  N  N   . SER H  1 106 ? 181.440 57.520  43.525 1.00   16.13 ? 105  SER H N   1 
ATOM   8573  C  CA  . SER H  1 106 ? 181.577 56.320  42.705 1.00   16.48 ? 105  SER H CA  1 
ATOM   8574  C  C   . SER H  1 106 ? 182.520 55.365  43.384 1.00   16.43 ? 105  SER H C   1 
ATOM   8575  O  O   . SER H  1 106 ? 183.296 55.772  44.265 1.00   15.75 ? 105  SER H O   1 
ATOM   8576  C  CB  . SER H  1 106 ? 182.164 56.697  41.357 1.00   16.82 ? 105  SER H CB  1 
ATOM   8577  O  OG  . SER H  1 106 ? 182.053 55.637  40.457 1.00   17.40 ? 105  SER H OG  1 
ATOM   8578  N  N   . LEU H  1 107 ? 182.493 54.108  42.948 1.00   16.82 ? 106  LEU H N   1 
ATOM   8579  C  CA  . LEU H  1 107 ? 183.448 53.141  43.454 1.00   17.12 ? 106  LEU H CA  1 
ATOM   8580  C  C   . LEU H  1 107 ? 184.539 52.895  42.394 1.00   18.05 ? 106  LEU H C   1 
ATOM   8581  O  O   . LEU H  1 107 ? 185.280 51.941  42.493 1.00   18.26 ? 106  LEU H O   1 
ATOM   8582  C  CB  . LEU H  1 107 ? 182.770 51.847  43.905 1.00   16.94 ? 106  LEU H CB  1 
ATOM   8583  C  CG  . LEU H  1 107 ? 181.779 51.951  45.076 1.00   16.69 ? 106  LEU H CG  1 
ATOM   8584  C  CD1 . LEU H  1 107 ? 181.273 50.556  45.433 1.00   16.51 ? 106  LEU H CD1 1 
ATOM   8585  C  CD2 . LEU H  1 107 ? 182.403 52.651  46.283 1.00   16.04 ? 106  LEU H CD2 1 
ATOM   8586  N  N   . SER H  1 108 ? 184.638 53.792  41.409 1.00   18.99 ? 107  SER H N   1 
ATOM   8587  C  CA  . SER H  1 108 ? 185.733 53.771  40.440 1.00   20.08 ? 107  SER H CA  1 
ATOM   8588  C  C   . SER H  1 108 ? 185.840 55.138  39.762 1.00   20.52 ? 107  SER H C   1 
ATOM   8589  O  O   . SER H  1 108 ? 184.982 55.975  39.946 1.00   20.51 ? 107  SER H O   1 
ATOM   8590  C  CB  . SER H  1 108 ? 185.518 52.675  39.388 1.00   20.77 ? 107  SER H CB  1 
ATOM   8591  O  OG  . SER H  1 108 ? 184.344 52.918  38.626 1.00   21.74 ? 107  SER H OG  1 
ATOM   8592  N  N   . GLY H  1 109 ? 186.933 55.365  39.043 1.00   21.20 ? 108  GLY H N   1 
ATOM   8593  C  CA  . GLY H  1 109 ? 187.160 56.615  38.338 1.00   21.88 ? 108  GLY H CA  1 
ATOM   8594  C  C   . GLY H  1 109 ? 187.585 57.798  39.190 1.00   21.93 ? 108  GLY H C   1 
ATOM   8595  O  O   . GLY H  1 109 ? 188.025 57.647  40.325 1.00   21.62 ? 108  GLY H O   1 
ATOM   8596  N  N   . ASP H  1 110 ? 187.413 58.993  38.632 1.00   22.27 ? 109  ASP H N   1 
ATOM   8597  C  CA  . ASP H  1 110 ? 187.810 60.241  39.297 1.00   22.34 ? 109  ASP H CA  1 
ATOM   8598  C  C   . ASP H  1 110 ? 187.089 60.476  40.607 1.00   21.46 ? 109  ASP H C   1 
ATOM   8599  O  O   . ASP H  1 110 ? 187.678 61.024  41.519 1.00   21.41 ? 109  ASP H O   1 
ATOM   8600  C  CB  . ASP H  1 110 ? 187.536 61.451  38.378 1.00   23.52 ? 109  ASP H CB  1 
ATOM   8601  C  CG  . ASP H  1 110 ? 188.450 61.473  37.175 1.00   24.75 ? 109  ASP H CG  1 
ATOM   8602  O  OD1 . ASP H  1 110 ? 189.486 60.778  37.200 1.00   25.44 ? 109  ASP H OD1 1 
ATOM   8603  O  OD2 . ASP H  1 110 ? 188.132 62.172  36.205 1.00   26.67 ? 109  ASP H OD2 1 
ATOM   8604  N  N   . HIS H  1 111 ? 185.819 60.083  40.695 1.00   20.41 ? 110  HIS H N   1 
ATOM   8605  C  CA  . HIS H  1 111 ? 185.059 60.304  41.929 1.00   19.53 ? 110  HIS H CA  1 
ATOM   8606  C  C   . HIS H  1 111 ? 185.117 59.133  42.878 1.00   18.66 ? 110  HIS H C   1 
ATOM   8607  O  O   . HIS H  1 111 ? 184.352 59.060  43.849 1.00   18.02 ? 110  HIS H O   1 
ATOM   8608  C  CB  . HIS H  1 111 ? 183.605 60.642  41.597 1.00   19.69 ? 110  HIS H CB  1 
ATOM   8609  C  CG  . HIS H  1 111 ? 183.432 61.982  40.933 1.00   19.88 ? 110  HIS H CG  1 
ATOM   8610  N  ND1 . HIS H  1 111 ? 182.217 62.516  40.688 1.00   20.00 ? 110  HIS H ND1 1 
ATOM   8611  C  CD2 . HIS H  1 111 ? 184.371 62.901  40.465 1.00   20.02 ? 110  HIS H CD2 1 
ATOM   8612  C  CE1 . HIS H  1 111 ? 182.384 63.713  40.080 1.00   20.12 ? 110  HIS H CE1 1 
ATOM   8613  N  NE2 . HIS H  1 111 ? 183.694 63.946  39.959 1.00   20.00 ? 110  HIS H NE2 1 
ATOM   8614  N  N   . CYS H  1 112 ? 186.036 58.214  42.631 1.00   18.23 ? 111  CYS H N   1 
ATOM   8615  C  CA  . CYS H  1 112 ? 186.182 57.027  43.474 1.00   17.82 ? 111  CYS H CA  1 
ATOM   8616  C  C   . CYS H  1 112 ? 186.464 57.424  44.926 1.00   16.63 ? 111  CYS H C   1 
ATOM   8617  O  O   . CYS H  1 112 ? 187.300 58.267  45.186 1.00   16.40 ? 111  CYS H O   1 
ATOM   8618  C  CB  . CYS H  1 112 ? 187.324 56.140  42.956 1.00   18.63 ? 111  CYS H CB  1 
ATOM   8619  S  SG  . CYS H  1 112 ? 187.431 54.548  43.804 1.00   20.09 ? 111  CYS H SG  1 
ATOM   8620  N  N   . ILE H  1 113 ? 185.737 56.819  45.846 1.00   15.60 ? 112  ILE H N   1 
ATOM   8621  C  CA  . ILE H  1 113 ? 185.878 57.086  47.272 1.00   15.07 ? 112  ILE H CA  1 
ATOM   8622  C  C   . ILE H  1 113 ? 186.624 55.974  48.040 1.00   14.55 ? 112  ILE H C   1 
ATOM   8623  O  O   . ILE H  1 113 ? 186.887 56.092  49.232 1.00   13.94 ? 112  ILE H O   1 
ATOM   8624  C  CB  . ILE H  1 113 ? 184.493 57.363  47.925 1.00   14.78 ? 112  ILE H CB  1 
ATOM   8625  C  CG1 . ILE H  1 113 ? 183.622 56.112  47.923 1.00   14.75 ? 112  ILE H CG1 1 
ATOM   8626  C  CG2 . ILE H  1 113 ? 183.824 58.554  47.212 1.00   14.90 ? 112  ILE H CG2 1 
ATOM   8627  C  CD1 . ILE H  1 113 ? 182.295 56.287  48.666 1.00   14.71 ? 112  ILE H CD1 1 
ATOM   8628  N  N   . ILE H  1 114 ? 186.964 54.901  47.337 1.00   14.62 ? 113  ILE H N   1 
ATOM   8629  C  CA  . ILE H  1 114 ? 187.817 53.853  47.896 1.00   14.47 ? 113  ILE H CA  1 
ATOM   8630  C  C   . ILE H  1 114 ? 189.191 54.403  48.320 1.00   14.19 ? 113  ILE H C   1 
ATOM   8631  O  O   . ILE H  1 114 ? 189.849 55.110  47.574 1.00   14.17 ? 113  ILE H O   1 
ATOM   8632  C  CB  . ILE H  1 114 ? 187.933 52.657  46.917 1.00   14.88 ? 113  ILE H CB  1 
ATOM   8633  C  CG1 . ILE H  1 114 ? 186.547 51.983  46.830 1.00   15.04 ? 113  ILE H CG1 1 
ATOM   8634  C  CG2 . ILE H  1 114 ? 188.959 51.641  47.423 1.00   14.81 ? 113  ILE H CG2 1 
ATOM   8635  C  CD1 . ILE H  1 114 ? 186.427 50.935  45.757 1.00   15.57 ? 113  ILE H CD1 1 
ATOM   8636  N  N   . GLY H  1 115 ? 189.599 54.115  49.548 1.00   13.81 ? 114  GLY H N   1 
ATOM   8637  C  CA  . GLY H  1 115 ? 190.857 54.649  50.074 1.00   13.80 ? 114  GLY H CA  1 
ATOM   8638  C  C   . GLY H  1 115 ? 190.738 56.038  50.689 1.00   13.73 ? 114  GLY H C   1 
ATOM   8639  O  O   . GLY H  1 115 ? 191.739 56.618  51.108 1.00   13.83 ? 114  GLY H O   1 
ATOM   8640  N  N   . ARG H  1 116 ? 189.523 56.573  50.747 1.00   13.52 ? 115  ARG H N   1 
ATOM   8641  C  CA  . ARG H  1 116 ? 189.254 57.847  51.391 1.00   13.46 ? 115  ARG H CA  1 
ATOM   8642  C  C   . ARG H  1 116 ? 188.559 57.566  52.712 1.00   13.15 ? 115  ARG H C   1 
ATOM   8643  O  O   . ARG H  1 116 ? 188.401 56.409  53.069 1.00   13.03 ? 115  ARG H O   1 
ATOM   8644  C  CB  . ARG H  1 116 ? 188.435 58.734  50.452 1.00   13.66 ? 115  ARG H CB  1 
ATOM   8645  C  CG  . ARG H  1 116 ? 189.198 58.915  49.134 1.00   14.09 ? 115  ARG H CG  1 
ATOM   8646  C  CD  . ARG H  1 116 ? 188.698 60.064  48.280 1.00   14.42 ? 115  ARG H CD  1 
ATOM   8647  N  NE  . ARG H  1 116 ? 189.332 60.063  46.967 1.00   14.77 ? 115  ARG H NE  1 
ATOM   8648  C  CZ  . ARG H  1 116 ? 190.434 60.729  46.619 1.00   15.25 ? 115  ARG H CZ  1 
ATOM   8649  N  NH1 . ARG H  1 116 ? 191.081 61.500  47.480 1.00   15.34 ? 115  ARG H NH1 1 
ATOM   8650  N  NH2 . ARG H  1 116 ? 190.882 60.653  45.355 1.00   15.57 ? 115  ARG H NH2 1 
ATOM   8651  N  N   . THR H  1 117 ? 188.181 58.609  53.451 1.00   12.92 ? 116  THR H N   1 
ATOM   8652  C  CA  . THR H  1 117 ? 187.653 58.436  54.794 1.00   12.70 ? 116  THR H CA  1 
ATOM   8653  C  C   . THR H  1 117 ? 186.211 58.865  54.911 1.00   12.64 ? 116  THR H C   1 
ATOM   8654  O  O   . THR H  1 117 ? 185.853 59.989  54.546 1.00   12.70 ? 116  THR H O   1 
ATOM   8655  C  CB  . THR H  1 117 ? 188.495 59.225  55.809 1.00   12.73 ? 116  THR H CB  1 
ATOM   8656  O  OG1 . THR H  1 117 ? 189.801 58.647  55.874 1.00   12.69 ? 116  THR H OG1 1 
ATOM   8657  C  CG2 . THR H  1 117 ? 187.877 59.187  57.174 1.00   12.61 ? 116  THR H CG2 1 
ATOM   8658  N  N   . LEU H  1 118 ? 185.374 57.971  55.420 1.00   12.49 ? 117  LEU H N   1 
ATOM   8659  C  CA  . LEU H  1 118 ? 184.014 58.320  55.771 1.00   12.44 ? 117  LEU H CA  1 
ATOM   8660  C  C   . LEU H  1 118 ? 184.013 58.874  57.201 1.00   12.54 ? 117  LEU H C   1 
ATOM   8661  O  O   . LEU H  1 118 ? 184.543 58.235  58.126 1.00   12.65 ? 117  LEU H O   1 
ATOM   8662  C  CB  . LEU H  1 118 ? 183.119 57.102  55.709 1.00   12.37 ? 117  LEU H CB  1 
ATOM   8663  C  CG  . LEU H  1 118 ? 181.611 57.304  55.885 1.00   12.40 ? 117  LEU H CG  1 
ATOM   8664  C  CD1 . LEU H  1 118 ? 181.078 58.093  54.691 1.00   12.23 ? 117  LEU H CD1 1 
ATOM   8665  C  CD2 . LEU H  1 118 ? 180.897 55.941  56.030 1.00   12.44 ? 117  LEU H CD2 1 
ATOM   8666  N  N   . VAL H  1 119 ? 183.387 60.026  57.382 1.00   12.56 ? 118  VAL H N   1 
ATOM   8667  C  CA  . VAL H  1 119 ? 183.304 60.690  58.690 1.00   12.69 ? 118  VAL H CA  1 
ATOM   8668  C  C   . VAL H  1 119 ? 181.859 60.977  59.051 1.00   12.87 ? 118  VAL H C   1 
ATOM   8669  O  O   . VAL H  1 119 ? 181.099 61.517  58.227 1.00   12.71 ? 118  VAL H O   1 
ATOM   8670  C  CB  . VAL H  1 119 ? 184.083 62.028  58.672 1.00   12.73 ? 118  VAL H CB  1 
ATOM   8671  C  CG1 . VAL H  1 119 ? 184.037 62.725  60.040 1.00   12.84 ? 118  VAL H CG1 1 
ATOM   8672  C  CG2 . VAL H  1 119 ? 185.529 61.792  58.263 1.00   12.74 ? 118  VAL H CG2 1 
ATOM   8673  N  N   . VAL H  1 120 ? 181.487 60.614  60.279 1.00   13.28 ? 119  VAL H N   1 
ATOM   8674  C  CA  . VAL H  1 120 ? 180.238 61.062  60.922 1.00   13.67 ? 119  VAL H CA  1 
ATOM   8675  C  C   . VAL H  1 120 ? 180.530 62.116  62.008 1.00   14.21 ? 119  VAL H C   1 
ATOM   8676  O  O   . VAL H  1 120 ? 181.482 61.995  62.807 1.00   14.29 ? 119  VAL H O   1 
ATOM   8677  C  CB  . VAL H  1 120 ? 179.396 59.882  61.451 1.00   13.70 ? 119  VAL H CB  1 
ATOM   8678  C  CG1 . VAL H  1 120 ? 180.118 59.138  62.562 1.00   13.82 ? 119  VAL H CG1 1 
ATOM   8679  C  CG2 . VAL H  1 120 ? 177.990 60.345  61.878 1.00   13.73 ? 119  VAL H CG2 1 
ATOM   8680  N  N   . HIS H  1 121 ? 179.733 63.176  61.994 1.00   14.82 ? 120  HIS H N   1 
ATOM   8681  C  CA  . HIS H  1 121 ? 179.986 64.385  62.776 1.00   15.58 ? 120  HIS H CA  1 
ATOM   8682  C  C   . HIS H  1 121 ? 179.072 64.602  63.969 1.00   16.63 ? 120  HIS H C   1 
ATOM   8683  O  O   . HIS H  1 121 ? 177.964 64.089  64.057 1.00   16.51 ? 120  HIS H O   1 
ATOM   8684  C  CB  . HIS H  1 121 ? 179.840 65.598  61.884 1.00   15.41 ? 120  HIS H CB  1 
ATOM   8685  C  CG  . HIS H  1 121 ? 180.997 65.829  60.972 1.00   15.30 ? 120  HIS H CG  1 
ATOM   8686  N  ND1 . HIS H  1 121 ? 182.070 66.544  61.341 1.00   15.50 ? 120  HIS H ND1 1 
ATOM   8687  C  CD2 . HIS H  1 121 ? 181.235 65.409  59.681 1.00   15.21 ? 120  HIS H CD2 1 
ATOM   8688  C  CE1 . HIS H  1 121 ? 182.948 66.585  60.329 1.00   15.43 ? 120  HIS H CE1 1 
ATOM   8689  N  NE2 . HIS H  1 121 ? 182.440 65.894  59.319 1.00   15.40 ? 120  HIS H NE2 1 
ATOM   8690  N  N   . GLU H  1 122 ? 179.578 65.427  64.875 1.00   18.31 ? 121  GLU H N   1 
ATOM   8691  C  CA  . GLU H  1 122 ? 178.911 65.960  66.055 1.00   19.79 ? 121  GLU H CA  1 
ATOM   8692  C  C   . GLU H  1 122 ? 177.541 66.595  65.798 1.00   20.05 ? 121  GLU H C   1 
ATOM   8693  O  O   . GLU H  1 122 ? 176.575 66.261  66.448 1.00   20.36 ? 121  GLU H O   1 
ATOM   8694  C  CB  . GLU H  1 122 ? 179.859 67.026  66.607 1.00   21.41 ? 121  GLU H CB  1 
ATOM   8695  C  CG  . GLU H  1 122 ? 179.514 67.609  67.964 1.00   23.47 ? 121  GLU H CG  1 
ATOM   8696  C  CD  . GLU H  1 122 ? 180.309 68.891  68.283 1.00   25.29 ? 121  GLU H CD  1 
ATOM   8697  O  OE1 . GLU H  1 122 ? 181.023 69.488  67.418 1.00   25.74 ? 121  GLU H OE1 1 
ATOM   8698  O  OE2 . GLU H  1 122 ? 180.180 69.318  69.438 1.00   28.93 ? 121  GLU H OE2 1 
ATOM   8699  N  N   . LYS H  1 123 ? 177.473 67.505  64.834 1.00   20.49 ? 122  LYS H N   1 
ATOM   8700  C  CA  . LYS H  1 123 ? 176.288 68.323  64.592 1.00   20.66 ? 122  LYS H CA  1 
ATOM   8701  C  C   . LYS H  1 123 ? 175.692 68.062  63.225 1.00   18.94 ? 122  LYS H C   1 
ATOM   8702  O  O   . LYS H  1 123 ? 176.279 67.349  62.378 1.00   17.84 ? 122  LYS H O   1 
ATOM   8703  C  CB  . LYS H  1 123 ? 176.680 69.805  64.610 1.00   22.74 ? 122  LYS H CB  1 
ATOM   8704  C  CG  . LYS H  1 123 ? 177.285 70.309  65.891 1.00   25.87 ? 122  LYS H CG  1 
ATOM   8705  C  CD  . LYS H  1 123 ? 177.902 71.681  65.669 1.00   28.75 ? 122  LYS H CD  1 
ATOM   8706  C  CE  . LYS H  1 123 ? 178.125 72.377  66.989 1.00   32.22 ? 122  LYS H CE  1 
ATOM   8707  N  NZ  . LYS H  1 123 ? 178.751 73.730  66.862 1.00   34.91 ? 122  LYS H NZ  1 
ATOM   8708  N  N   . ALA H  1 124 ? 174.548 68.698  63.007 1.00   17.57 ? 123  ALA H N   1 
ATOM   8709  C  CA  . ALA H  1 124 ? 173.867 68.688  61.725 1.00   16.89 ? 123  ALA H CA  1 
ATOM   8710  C  C   . ALA H  1 124 ? 174.703 69.427  60.681 1.00   15.88 ? 123  ALA H C   1 
ATOM   8711  O  O   . ALA H  1 124 ? 175.327 70.417  60.970 1.00   15.98 ? 123  ALA H O   1 
ATOM   8712  C  CB  . ALA H  1 124 ? 172.485 69.330  61.837 1.00   16.47 ? 123  ALA H CB  1 
ATOM   8713  N  N   . ASP H  1 125 ? 174.715 68.890  59.482 1.00   15.32 ? 124  ASP H N   1 
ATOM   8714  C  CA  . ASP H  1 125 ? 175.214 69.573  58.270 1.00   14.80 ? 124  ASP H CA  1 
ATOM   8715  C  C   . ASP H  1 125 ? 174.107 70.520  57.810 1.00   14.78 ? 124  ASP H C   1 
ATOM   8716  O  O   . ASP H  1 125 ? 172.965 70.064  57.615 1.00   14.93 ? 124  ASP H O   1 
ATOM   8717  C  CB  . ASP H  1 125 ? 175.485 68.500  57.223 1.00   14.49 ? 124  ASP H CB  1 
ATOM   8718  C  CG  . ASP H  1 125 ? 176.195 69.009  55.958 1.00   14.40 ? 124  ASP H CG  1 
ATOM   8719  O  OD1 . ASP H  1 125 ? 176.070 70.209  55.603 1.00   14.32 ? 124  ASP H OD1 1 
ATOM   8720  O  OD2 . ASP H  1 125 ? 176.844 68.156  55.290 1.00   14.02 ? 124  ASP H OD2 1 
ATOM   8721  N  N   . ASP H  1 126 ? 174.436 71.818  57.657 1.00   14.61 ? 125  ASP H N   1 
ATOM   8722  C  CA  . ASP H  1 126 ? 173.490 72.851  57.168 1.00   14.55 ? 125  ASP H CA  1 
ATOM   8723  C  C   . ASP H  1 126 ? 173.367 72.880  55.625 1.00   14.42 ? 125  ASP H C   1 
ATOM   8724  O  O   . ASP H  1 126 ? 172.693 73.720  55.052 1.00   14.49 ? 125  ASP H O   1 
ATOM   8725  C  CB  . ASP H  1 126 ? 173.802 74.267  57.734 1.00   14.68 ? 125  ASP H CB  1 
ATOM   8726  C  CG  . ASP H  1 126 ? 175.083 74.893  57.181 1.00   14.75 ? 125  ASP H CG  1 
ATOM   8727  O  OD1 . ASP H  1 126 ? 175.617 74.478  56.112 1.00   14.77 ? 125  ASP H OD1 1 
ATOM   8728  O  OD2 . ASP H  1 126 ? 175.587 75.828  57.828 1.00   14.97 ? 125  ASP H OD2 1 
ATOM   8729  N  N   . LEU H  1 127 ? 174.031 71.942  54.974 1.00   14.31 ? 126  LEU H N   1 
ATOM   8730  C  CA  . LEU H  1 127 ? 173.904 71.720  53.532 1.00   14.27 ? 126  LEU H CA  1 
ATOM   8731  C  C   . LEU H  1 127 ? 174.321 72.947  52.711 1.00   14.45 ? 126  LEU H C   1 
ATOM   8732  O  O   . LEU H  1 127 ? 173.866 73.146  51.592 1.00   14.82 ? 126  LEU H O   1 
ATOM   8733  C  CB  . LEU H  1 127 ? 172.504 71.205  53.174 1.00   14.23 ? 126  LEU H CB  1 
ATOM   8734  C  CG  . LEU H  1 127 ? 171.908 70.028  53.997 1.00   14.18 ? 126  LEU H CG  1 
ATOM   8735  C  CD1 . LEU H  1 127 ? 170.511 69.620  53.517 1.00   14.12 ? 126  LEU H CD1 1 
ATOM   8736  C  CD2 . LEU H  1 127 ? 172.828 68.805  54.036 1.00   13.92 ? 126  LEU H CD2 1 
ATOM   8737  N  N   . GLY H  1 128 ? 175.211 73.752  53.273 1.00   14.57 ? 127  GLY H N   1 
ATOM   8738  C  CA  . GLY H  1 128 ? 175.799 74.882  52.584 1.00   14.96 ? 127  GLY H CA  1 
ATOM   8739  C  C   . GLY H  1 128 ? 174.932 76.127  52.619 1.00   15.27 ? 127  GLY H C   1 
ATOM   8740  O  O   . GLY H  1 128 ? 175.215 77.110  51.937 1.00   15.24 ? 127  GLY H O   1 
ATOM   8741  N  N   . LYS H  1 129 ? 173.888 76.088  53.431 1.00   15.41 ? 128  LYS H N   1 
ATOM   8742  C  CA  . LYS H  1 129 ? 172.895 77.181  53.458 1.00   15.99 ? 128  LYS H CA  1 
ATOM   8743  C  C   . LYS H  1 129 ? 172.970 78.024  54.714 1.00   15.97 ? 128  LYS H C   1 
ATOM   8744  O  O   . LYS H  1 129 ? 172.010 78.705  55.040 1.00   16.41 ? 128  LYS H O   1 
ATOM   8745  C  CB  . LYS H  1 129 ? 171.499 76.582  53.314 1.00   16.32 ? 128  LYS H CB  1 
ATOM   8746  C  CG  . LYS H  1 129 ? 171.334 75.891  51.962 1.00   16.74 ? 128  LYS H CG  1 
ATOM   8747  C  CD  . LYS H  1 129 ? 170.097 75.002  51.855 1.00   17.21 ? 128  LYS H CD  1 
ATOM   8748  C  CE  . LYS H  1 129 ? 168.797 75.757  51.893 1.00   17.81 ? 128  LYS H CE  1 
ATOM   8749  N  NZ  . LYS H  1 129 ? 167.639 74.843  51.559 1.00   18.66 ? 128  LYS H NZ  1 
ATOM   8750  N  N   . GLY H  1 130 ? 174.100 77.963  55.424 1.00   15.84 ? 129  GLY H N   1 
ATOM   8751  C  CA  . GLY H  1 130 ? 174.254 78.646  56.707 1.00   15.91 ? 129  GLY H CA  1 
ATOM   8752  C  C   . GLY H  1 130 ? 174.709 80.101  56.685 1.00   16.18 ? 129  GLY H C   1 
ATOM   8753  O  O   . GLY H  1 130 ? 174.657 80.788  57.729 1.00   16.22 ? 129  GLY H O   1 
ATOM   8754  N  N   . GLY H  1 131 ? 175.214 80.550  55.536 1.00   16.30 ? 130  GLY H N   1 
ATOM   8755  C  CA  . GLY H  1 131 ? 175.567 81.937  55.298 1.00   16.91 ? 130  GLY H CA  1 
ATOM   8756  C  C   . GLY H  1 131 ? 176.858 82.442  55.906 1.00   17.52 ? 130  GLY H C   1 
ATOM   8757  O  O   . GLY H  1 131 ? 177.154 83.617  55.794 1.00   17.63 ? 130  GLY H O   1 
ATOM   8758  N  N   . ASN H  1 132 ? 177.594 81.568  56.589 1.00   17.92 ? 131  ASN H N   1 
ATOM   8759  C  CA  . ASN H  1 132 ? 178.944 81.873  57.041 1.00   18.83 ? 131  ASN H CA  1 
ATOM   8760  C  C   . ASN H  1 132 ? 179.974 81.141  56.207 1.00   19.16 ? 131  ASN H C   1 
ATOM   8761  O  O   . ASN H  1 132 ? 179.637 80.262  55.407 1.00   19.07 ? 131  ASN H O   1 
ATOM   8762  C  CB  . ASN H  1 132 ? 179.142 81.605  58.563 1.00   18.81 ? 131  ASN H CB  1 
ATOM   8763  C  CG  . ASN H  1 132 ? 178.989 80.152  58.965 1.00   18.72 ? 131  ASN H CG  1 
ATOM   8764  O  OD1 . ASN H  1 132 ? 178.562 79.299  58.170 1.00   18.68 ? 131  ASN H OD1 1 
ATOM   8765  N  ND2 . ASN H  1 132 ? 179.323 79.853  60.240 1.00   18.73 ? 131  ASN H ND2 1 
ATOM   8766  N  N   . GLU H  1 133 ? 181.236 81.482  56.404 1.00   20.02 ? 132  GLU H N   1 
ATOM   8767  C  CA  . GLU H  1 133 ? 182.311 80.838  55.650 1.00   20.58 ? 132  GLU H CA  1 
ATOM   8768  C  C   . GLU H  1 133 ? 182.395 79.333  55.945 1.00   20.09 ? 132  GLU H C   1 
ATOM   8769  O  O   . GLU H  1 133 ? 182.639 78.508  55.070 1.00   19.74 ? 132  GLU H O   1 
ATOM   8770  C  CB  . GLU H  1 133 ? 183.655 81.531  55.937 1.00   22.07 ? 132  GLU H CB  1 
ATOM   8771  C  CG  . GLU H  1 133 ? 184.702 81.207  54.858 1.00   22.78 ? 132  GLU H CG  1 
ATOM   8772  C  CD  . GLU H  1 133 ? 186.009 81.952  55.023 0.50   23.66 ? 132  GLU H CD  1 
ATOM   8773  O  OE1 . GLU H  1 133 ? 185.972 83.187  55.165 0.50   24.59 ? 132  GLU H OE1 1 
ATOM   8774  O  OE2 . GLU H  1 133 ? 187.069 81.295  54.993 0.50   24.06 ? 132  GLU H OE2 1 
ATOM   8775  N  N   . GLU H  1 134 ? 182.174 78.970  57.194 1.00   20.33 ? 133  GLU H N   1 
ATOM   8776  C  CA  . GLU H  1 134 ? 182.279 77.584  57.594 1.00   20.24 ? 133  GLU H CA  1 
ATOM   8777  C  C   . GLU H  1 134 ? 181.235 76.726  56.843 1.00   19.13 ? 133  GLU H C   1 
ATOM   8778  O  O   . GLU H  1 134 ? 181.515 75.586  56.501 1.00   18.05 ? 133  GLU H O   1 
ATOM   8779  C  CB  . GLU H  1 134 ? 182.111 77.467  59.102 1.00   21.21 ? 133  GLU H CB  1 
ATOM   8780  C  CG  . GLU H  1 134 ? 182.390 76.087  59.661 1.00   22.22 ? 133  GLU H CG  1 
ATOM   8781  C  CD  . GLU H  1 134 ? 183.839 75.652  59.470 1.00   23.34 ? 133  GLU H CD  1 
ATOM   8782  O  OE1 . GLU H  1 134 ? 184.763 76.471  59.604 1.00   25.40 ? 133  GLU H OE1 1 
ATOM   8783  O  OE2 . GLU H  1 134 ? 184.047 74.465  59.192 1.00   25.01 ? 133  GLU H OE2 1 
ATOM   8784  N  N   . SER H  1 135 ? 180.054 77.299  56.590 1.00   18.63 ? 134  SER H N   1 
ATOM   8785  C  CA  . SER H  1 135 ? 178.996 76.601  55.852 1.00   18.27 ? 134  SER H CA  1 
ATOM   8786  C  C   . SER H  1 135 ? 179.453 76.107  54.505 1.00   18.29 ? 134  SER H C   1 
ATOM   8787  O  O   . SER H  1 135 ? 179.155 74.987  54.155 1.00   17.77 ? 134  SER H O   1 
ATOM   8788  C  CB  . SER H  1 135 ? 177.750 77.465  55.664 1.00   18.09 ? 134  SER H CB  1 
ATOM   8789  O  OG  . SER H  1 135 ? 176.672 76.714  55.125 1.00   17.58 ? 134  SER H OG  1 
ATOM   8790  N  N   . THR H  1 136 ? 180.197 76.940  53.783 1.00   18.88 ? 135  THR H N   1 
ATOM   8791  C  CA  . THR H  1 136 ? 180.654 76.638  52.428 1.00   19.49 ? 135  THR H CA  1 
ATOM   8792  C  C   . THR H  1 136 ? 181.818 75.651  52.389 1.00   19.11 ? 135  THR H C   1 
ATOM   8793  O  O   . THR H  1 136 ? 182.257 75.267  51.312 1.00   18.86 ? 135  THR H O   1 
ATOM   8794  C  CB  . THR H  1 136 ? 181.219 77.900  51.748 1.00   20.33 ? 135  THR H CB  1 
ATOM   8795  O  OG1 . THR H  1 136 ? 182.352 78.355  52.523 1.00   21.46 ? 135  THR H OG1 1 
ATOM   8796  C  CG2 . THR H  1 136 ? 180.177 78.992  51.635 1.00   20.79 ? 135  THR H CG2 1 
ATOM   8797  N  N   . LYS H  1 137 ? 182.357 75.323  53.564 1.00   19.26 ? 136  LYS H N   1 
ATOM   8798  C  CA  . LYS H  1 137 ? 183.424 74.338  53.705 1.00   19.31 ? 136  LYS H CA  1 
ATOM   8799  C  C   . LYS H  1 137 ? 182.946 73.014  54.297 1.00   18.04 ? 136  LYS H C   1 
ATOM   8800  O  O   . LYS H  1 137 ? 183.254 71.946  53.758 1.00   17.42 ? 136  LYS H O   1 
ATOM   8801  C  CB  . LYS H  1 137 ? 184.512 74.875  54.627 1.00   20.76 ? 136  LYS H CB  1 
ATOM   8802  C  CG  . LYS H  1 137 ? 185.191 76.168  54.207 1.00   22.41 ? 136  LYS H CG  1 
ATOM   8803  C  CD  . LYS H  1 137 ? 186.093 76.647  55.338 1.00   23.83 ? 136  LYS H CD  1 
ATOM   8804  C  CE  . LYS H  1 137 ? 186.648 78.033  55.087 1.00   25.68 ? 136  LYS H CE  1 
ATOM   8805  N  NZ  . LYS H  1 137 ? 187.439 78.574  56.249 1.00   27.58 ? 136  LYS H NZ  1 
ATOM   8806  N  N   . THR H  1 138 ? 182.247 73.078  55.432 1.00   17.32 ? 137  THR H N   1 
ATOM   8807  C  CA  . THR H  1 138 ? 181.915 71.877  56.212 1.00   16.77 ? 137  THR H CA  1 
ATOM   8808  C  C   . THR H  1 138 ? 180.439 71.687  56.529 1.00   16.38 ? 137  THR H C   1 
ATOM   8809  O  O   . THR H  1 138 ? 180.054 70.688  57.130 1.00   16.38 ? 137  THR H O   1 
ATOM   8810  C  CB  . THR H  1 138 ? 182.638 71.881  57.581 1.00   16.99 ? 137  THR H CB  1 
ATOM   8811  O  OG1 . THR H  1 138 ? 182.144 72.949  58.400 1.00   17.53 ? 137  THR H OG1 1 
ATOM   8812  C  CG2 . THR H  1 138 ? 184.138 72.028  57.415 1.00   17.18 ? 137  THR H CG2 1 
ATOM   8813  N  N   . GLY H  1 139 ? 179.613 72.656  56.194 1.00   16.01 ? 138  GLY H N   1 
ATOM   8814  C  CA  . GLY H  1 139 ? 178.239 72.660  56.641 1.00   15.79 ? 138  GLY H CA  1 
ATOM   8815  C  C   . GLY H  1 139 ? 178.024 72.946  58.122 1.00   15.84 ? 138  GLY H C   1 
ATOM   8816  O  O   . GLY H  1 139 ? 176.926 72.737  58.633 1.00   15.58 ? 138  GLY H O   1 
ATOM   8817  N  N   . ASN H  1 140 ? 179.060 73.445  58.804 1.00   16.02 ? 139  ASN H N   1 
ATOM   8818  C  CA  . ASN H  1 140 ? 179.016 73.629  60.254 1.00   16.20 ? 139  ASN H CA  1 
ATOM   8819  C  C   . ASN H  1 140 ? 178.706 72.325  60.993 1.00   15.75 ? 139  ASN H C   1 
ATOM   8820  O  O   . ASN H  1 140 ? 177.997 72.348  62.008 1.00   15.73 ? 139  ASN H O   1 
ATOM   8821  C  CB  . ASN H  1 140 ? 177.997 74.733  60.642 1.00   16.54 ? 139  ASN H CB  1 
ATOM   8822  C  CG  . ASN H  1 140 ? 178.476 76.122  60.266 1.00   17.24 ? 139  ASN H CG  1 
ATOM   8823  O  OD1 . ASN H  1 140 ? 179.386 76.674  60.895 1.00   18.18 ? 139  ASN H OD1 1 
ATOM   8824  N  ND2 . ASN H  1 140 ? 177.873 76.697  59.211 1.00   17.44 ? 139  ASN H ND2 1 
ATOM   8825  N  N   . ALA H  1 141 ? 179.220 71.198  60.483 1.00   15.17 ? 140  ALA H N   1 
ATOM   8826  C  CA  . ALA H  1 141 ? 178.910 69.887  61.061 1.00   15.10 ? 140  ALA H CA  1 
ATOM   8827  C  C   . ALA H  1 141 ? 179.714 69.573  62.347 1.00   15.15 ? 140  ALA H C   1 
ATOM   8828  O  O   . ALA H  1 141 ? 179.517 68.541  62.985 1.00   14.85 ? 140  ALA H O   1 
ATOM   8829  C  CB  . ALA H  1 141 ? 179.095 68.770  60.008 1.00   14.69 ? 140  ALA H CB  1 
ATOM   8830  N  N   . GLY H  1 142 ? 180.656 70.436  62.679 1.00   15.37 ? 141  GLY H N   1 
ATOM   8831  C  CA  . GLY H  1 142 ? 181.467 70.252  63.871 1.00   15.79 ? 141  GLY H CA  1 
ATOM   8832  C  C   . GLY H  1 142 ? 182.456 69.101  63.852 1.00   15.77 ? 141  GLY H C   1 
ATOM   8833  O  O   . GLY H  1 142 ? 182.949 68.669  62.806 1.00   16.01 ? 141  GLY H O   1 
ATOM   8834  N  N   . SER H  1 143 ? 182.720 68.595  65.038 1.00   16.12 ? 142  SER H N   1 
ATOM   8835  C  CA  A SER H  1 143 ? 183.805 67.647  65.238 0.50   16.15 ? 142  SER H CA  1 
ATOM   8836  C  CA  B SER H  1 143 ? 183.777 67.621  65.275 0.50   16.24 ? 142  SER H CA  1 
ATOM   8837  C  C   . SER H  1 143 ? 183.482 66.306  64.591 1.00   15.91 ? 142  SER H C   1 
ATOM   8838  O  O   . SER H  1 143 ? 182.336 66.017  64.270 1.00   15.84 ? 142  SER H O   1 
ATOM   8839  C  CB  A SER H  1 143 ? 184.091 67.445  66.725 0.50   16.43 ? 142  SER H CB  1 
ATOM   8840  C  CB  B SER H  1 143 ? 183.926 67.363  66.771 0.50   16.62 ? 142  SER H CB  1 
ATOM   8841  O  OG  A SER H  1 143 ? 183.085 66.666  67.333 0.50   16.28 ? 142  SER H OG  1 
ATOM   8842  O  OG  B SER H  1 143 ? 184.479 68.499  67.393 0.50   17.10 ? 142  SER H OG  1 
ATOM   8843  N  N   . ARG H  1 144 ? 184.527 65.525  64.411 1.00   15.91 ? 143  ARG H N   1 
ATOM   8844  C  CA  . ARG H  1 144 ? 184.484 64.259  63.733 1.00   15.73 ? 143  ARG H CA  1 
ATOM   8845  C  C   . ARG H  1 144 ? 184.367 63.215  64.795 1.00   15.89 ? 143  ARG H C   1 
ATOM   8846  O  O   . ARG H  1 144 ? 185.336 62.931  65.463 1.00   16.24 ? 143  ARG H O   1 
ATOM   8847  C  CB  . ARG H  1 144 ? 185.784 64.100  62.959 1.00   15.62 ? 143  ARG H CB  1 
ATOM   8848  C  CG  . ARG H  1 144 ? 186.068 65.323  62.103 1.00   15.70 ? 143  ARG H CG  1 
ATOM   8849  C  CD  . ARG H  1 144 ? 187.253 65.163  61.169 1.00   15.80 ? 143  ARG H CD  1 
ATOM   8850  N  NE  . ARG H  1 144 ? 187.389 66.362  60.367 1.00   15.91 ? 143  ARG H NE  1 
ATOM   8851  C  CZ  . ARG H  1 144 ? 188.252 66.552  59.392 1.00   16.23 ? 143  ARG H CZ  1 
ATOM   8852  N  NH1 . ARG H  1 144 ? 189.104 65.604  59.039 1.00   16.46 ? 143  ARG H NH1 1 
ATOM   8853  N  NH2 . ARG H  1 144 ? 188.262 67.710  58.749 1.00   16.56 ? 143  ARG H NH2 1 
ATOM   8854  N  N   . LEU H  1 145 ? 183.181 62.679  65.014 1.00   15.98 ? 144  LEU H N   1 
ATOM   8855  C  CA  . LEU H  1 145 ? 182.994 61.714  66.117 1.00   16.32 ? 144  LEU H CA  1 
ATOM   8856  C  C   . LEU H  1 145 ? 183.613 60.336  65.837 1.00   16.27 ? 144  LEU H C   1 
ATOM   8857  O  O   . LEU H  1 145 ? 184.099 59.652  66.757 1.00   17.15 ? 144  LEU H O   1 
ATOM   8858  C  CB  . LEU H  1 145 ? 181.514 61.587  66.471 1.00   16.41 ? 144  LEU H CB  1 
ATOM   8859  C  CG  . LEU H  1 145 ? 180.848 62.892  66.952 1.00   16.80 ? 144  LEU H CG  1 
ATOM   8860  C  CD1 . LEU H  1 145 ? 179.400 62.585  67.309 1.00   17.09 ? 144  LEU H CD1 1 
ATOM   8861  C  CD2 . LEU H  1 145 ? 181.584 63.524  68.148 1.00   17.10 ? 144  LEU H CD2 1 
ATOM   8862  N  N   . ALA H  1 146 ? 183.578 59.916  64.588 1.00   15.81 ? 145  ALA H N   1 
ATOM   8863  C  CA  . ALA H  1 146 ? 184.119 58.617  64.199 1.00   15.70 ? 145  ALA H CA  1 
ATOM   8864  C  C   . ALA H  1 146 ? 184.407 58.622  62.725 1.00   15.37 ? 145  ALA H C   1 
ATOM   8865  O  O   . ALA H  1 146 ? 183.807 59.383  61.971 1.00   15.26 ? 145  ALA H O   1 
ATOM   8866  C  CB  . ALA H  1 146 ? 183.151 57.476  64.544 1.00   15.63 ? 145  ALA H CB  1 
ATOM   8867  N  N   . CYS H  1 147 ? 185.312 57.758  62.310 1.00   15.31 ? 146  CYS H N   1 
ATOM   8868  C  CA  . CYS H  1 147 ? 185.717 57.677  60.898 1.00   15.18 ? 146  CYS H CA  1 
ATOM   8869  C  C   . CYS H  1 147 ? 186.362 56.315  60.585 1.00   14.80 ? 146  CYS H C   1 
ATOM   8870  O  O   . CYS H  1 147 ? 186.674 55.558  61.480 1.00   14.85 ? 146  CYS H O   1 
ATOM   8871  C  CB  . CYS H  1 147 ? 186.714 58.781  60.576 1.00   15.52 ? 146  CYS H CB  1 
ATOM   8872  S  SG  . CYS H  1 147 ? 188.239 58.754  61.570 1.00   16.42 ? 146  CYS H SG  1 
ATOM   8873  N  N   . GLY H  1 148 ? 186.545 56.037  59.306 1.00   14.25 ? 147  GLY H N   1 
ATOM   8874  C  CA  . GLY H  1 148 ? 187.225 54.833  58.847 1.00   14.00 ? 147  GLY H CA  1 
ATOM   8875  C  C   . GLY H  1 148 ? 187.625 55.012  57.404 1.00   13.73 ? 147  GLY H C   1 
ATOM   8876  O  O   . GLY H  1 148 ? 187.052 55.866  56.701 1.00   13.31 ? 147  GLY H O   1 
ATOM   8877  N  N   . VAL H  1 149 ? 188.612 54.230  56.971 1.00   13.43 ? 148  VAL H N   1 
ATOM   8878  C  CA  . VAL H  1 149 ? 189.017 54.209  55.582 1.00   13.34 ? 148  VAL H CA  1 
ATOM   8879  C  C   . VAL H  1 149 ? 188.099 53.277  54.792 1.00   13.31 ? 148  VAL H C   1 
ATOM   8880  O  O   . VAL H  1 149 ? 187.823 52.153  55.212 1.00   13.31 ? 148  VAL H O   1 
ATOM   8881  C  CB  . VAL H  1 149 ? 190.495 53.776  55.452 1.00   13.46 ? 148  VAL H CB  1 
ATOM   8882  C  CG1 . VAL H  1 149 ? 190.954 53.793  53.996 1.00   13.34 ? 148  VAL H CG1 1 
ATOM   8883  C  CG2 . VAL H  1 149 ? 191.374 54.693  56.298 1.00   13.37 ? 148  VAL H CG2 1 
ATOM   8884  N  N   . ILE H  1 150 ? 187.613 53.752  53.646 1.00   13.28 ? 149  ILE H N   1 
ATOM   8885  C  CA  . ILE H  1 150 ? 186.707 52.977  52.827 1.00   13.39 ? 149  ILE H CA  1 
ATOM   8886  C  C   . ILE H  1 150 ? 187.530 51.927  52.058 1.00   13.74 ? 149  ILE H C   1 
ATOM   8887  O  O   . ILE H  1 150 ? 188.475 52.266  51.367 1.00   13.55 ? 149  ILE H O   1 
ATOM   8888  C  CB  . ILE H  1 150 ? 185.900 53.889  51.885 1.00   13.27 ? 149  ILE H CB  1 
ATOM   8889  C  CG1 . ILE H  1 150 ? 185.062 54.896  52.680 1.00   13.10 ? 149  ILE H CG1 1 
ATOM   8890  C  CG2 . ILE H  1 150 ? 184.982 53.070  50.969 1.00   13.41 ? 149  ILE H CG2 1 
ATOM   8891  C  CD1 . ILE H  1 150 ? 184.569 56.074  51.841 1.00   13.05 ? 149  ILE H CD1 1 
ATOM   8892  N  N   . GLY H  1 151 ? 187.192 50.649  52.235 1.00   14.19 ? 150  GLY H N   1 
ATOM   8893  C  CA  . GLY H  1 151 ? 187.954 49.566  51.636 1.00   14.85 ? 150  GLY H CA  1 
ATOM   8894  C  C   . GLY H  1 151 ? 187.148 48.744  50.659 1.00   15.48 ? 150  GLY H C   1 
ATOM   8895  O  O   . GLY H  1 151 ? 185.932 48.704  50.739 1.00   15.91 ? 150  GLY H O   1 
ATOM   8896  N  N   . ILE H  1 152 ? 187.830 48.084  49.739 1.00   16.34 ? 151  ILE H N   1 
ATOM   8897  C  CA  . ILE H  1 152 ? 187.197 47.182  48.756 1.00   17.19 ? 151  ILE H CA  1 
ATOM   8898  C  C   . ILE H  1 152 ? 186.648 45.987  49.524 1.00   17.79 ? 151  ILE H C   1 
ATOM   8899  O  O   . ILE H  1 152 ? 187.334 45.453  50.410 1.00   17.31 ? 151  ILE H O   1 
ATOM   8900  C  CB  . ILE H  1 152 ? 188.211 46.688  47.700 1.00   17.58 ? 151  ILE H CB  1 
ATOM   8901  C  CG1 . ILE H  1 152 ? 188.768 47.868  46.908 1.00   17.93 ? 151  ILE H CG1 1 
ATOM   8902  C  CG2 . ILE H  1 152 ? 187.570 45.696  46.728 1.00   17.93 ? 151  ILE H CG2 1 
ATOM   8903  C  CD1 . ILE H  1 152 ? 190.084 47.576  46.184 1.00   18.00 ? 151  ILE H CD1 1 
ATOM   8904  N  N   . ALA H  1 153 ? 185.403 45.607  49.239 1.00   18.78 ? 152  ALA H N   1 
ATOM   8905  C  CA  . ALA H  1 153 ? 184.770 44.487  49.949 1.00   20.23 ? 152  ALA H CA  1 
ATOM   8906  C  C   . ALA H  1 153 ? 184.415 43.376  48.991 1.00   21.85 ? 152  ALA H C   1 
ATOM   8907  O  O   . ALA H  1 153 ? 184.252 43.601  47.797 1.00   22.24 ? 152  ALA H O   1 
ATOM   8908  C  CB  . ALA H  1 153 ? 183.511 44.944  50.708 1.00   20.01 ? 152  ALA H CB  1 
ATOM   8909  N  N   . GLN H  1 154 ? 184.247 42.181  49.532 1.00   24.40 ? 153  GLN H N   1 
ATOM   8910  C  CA  . GLN H  1 154 ? 183.910 41.028  48.702 1.00   27.68 ? 153  GLN H CA  1 
ATOM   8911  C  C   . GLN H  1 154 ? 182.473 41.107  48.268 1.00   29.36 ? 153  GLN H C   1 
ATOM   8912  O  O   . GLN H  1 154 ? 181.571 41.347  49.088 1.00   31.12 ? 153  GLN H O   1 
ATOM   8913  C  CB  . GLN H  1 154 ? 184.131 39.712  49.439 1.00   28.54 ? 153  GLN H CB  1 
ATOM   8914  C  CG  . GLN H  1 154 ? 183.953 38.491  48.546 1.00   30.25 ? 153  GLN H CG  1 
ATOM   8915  C  CD  . GLN H  1 154 ? 184.330 37.212  49.270 1.00   31.39 ? 153  GLN H CD  1 
ATOM   8916  O  OE1 . GLN H  1 154 ? 183.973 37.012  50.434 1.00   32.76 ? 153  GLN H OE1 1 
ATOM   8917  N  NE2 . GLN H  1 154 ? 185.068 36.366  48.605 1.00   32.33 ? 153  GLN H NE2 1 
ATOM   8918  O  OXT . GLN H  1 154 ? 182.235 40.907  47.083 1.00   32.63 ? 153  GLN H OXT 1 
ATOM   8919  N  N   . ALA I  1 2   ? 163.639 140.935 39.082 1.00   47.11 ? 1    ALA I N   1 
ATOM   8920  C  CA  . ALA I  1 2   ? 163.979 139.690 39.852 1.00   44.77 ? 1    ALA I CA  1 
ATOM   8921  C  C   . ALA I  1 2   ? 162.894 138.607 39.709 1.00   41.59 ? 1    ALA I C   1 
ATOM   8922  O  O   . ALA I  1 2   ? 161.772 138.899 39.333 1.00   40.15 ? 1    ALA I O   1 
ATOM   8923  C  CB  . ALA I  1 2   ? 164.227 140.017 41.327 1.00   45.29 ? 1    ALA I CB  1 
ATOM   8924  N  N   . THR I  1 3   ? 163.271 137.363 39.996 1.00   38.82 ? 2    THR I N   1 
ATOM   8925  C  CA  . THR I  1 3   ? 162.407 136.210 39.824 1.00   37.47 ? 2    THR I CA  1 
ATOM   8926  C  C   . THR I  1 3   ? 162.203 135.428 41.121 1.00   34.87 ? 2    THR I C   1 
ATOM   8927  O  O   . THR I  1 3   ? 161.299 134.605 41.192 1.00   32.12 ? 2    THR I O   1 
ATOM   8928  C  CB  . THR I  1 3   ? 162.970 135.246 38.766 1.00   39.00 ? 2    THR I CB  1 
ATOM   8929  O  OG1 . THR I  1 3   ? 164.046 134.462 39.321 1.00   38.53 ? 2    THR I OG1 1 
ATOM   8930  C  CG2 . THR I  1 3   ? 163.462 136.018 37.560 1.00   40.26 ? 2    THR I CG2 1 
ATOM   8931  N  N   . LYS I  1 4   ? 163.057 135.661 42.122 1.00   32.72 ? 3    LYS I N   1 
ATOM   8932  C  CA  . LYS I  1 4   ? 162.832 135.163 43.476 1.00   30.85 ? 3    LYS I CA  1 
ATOM   8933  C  C   . LYS I  1 4   ? 162.902 136.287 44.499 1.00   29.10 ? 3    LYS I C   1 
ATOM   8934  O  O   . LYS I  1 4   ? 163.688 137.211 44.373 1.00   29.55 ? 3    LYS I O   1 
ATOM   8935  C  CB  . LYS I  1 4   ? 163.851 134.096 43.841 1.00   31.74 ? 3    LYS I CB  1 
ATOM   8936  C  CG  . LYS I  1 4   ? 163.647 132.741 43.194 1.00   32.50 ? 3    LYS I CG  1 
ATOM   8937  C  CD  . LYS I  1 4   ? 164.775 131.800 43.570 0.50   33.01 ? 3    LYS I CD  1 
ATOM   8938  C  CE  . LYS I  1 4   ? 164.476 130.378 43.143 0.50   33.75 ? 3    LYS I CE  1 
ATOM   8939  N  NZ  . LYS I  1 4   ? 165.605 129.480 43.502 0.50   34.48 ? 3    LYS I NZ  1 
ATOM   8940  N  N   . ALA I  1 5   ? 162.046 136.205 45.508 1.00   27.01 ? 4    ALA I N   1 
ATOM   8941  C  CA  . ALA I  1 5   ? 162.093 137.095 46.647 1.00   25.19 ? 4    ALA I CA  1 
ATOM   8942  C  C   . ALA I  1 5   ? 161.873 136.253 47.908 1.00   23.89 ? 4    ALA I C   1 
ATOM   8943  O  O   . ALA I  1 5   ? 161.556 135.062 47.816 1.00   23.52 ? 4    ALA I O   1 
ATOM   8944  C  CB  . ALA I  1 5   ? 161.056 138.198 46.529 1.00   24.61 ? 4    ALA I CB  1 
ATOM   8945  N  N   . VAL I  1 6   ? 162.089 136.872 49.070 1.00   22.50 ? 5    VAL I N   1 
ATOM   8946  C  CA  . VAL I  1 6   ? 161.974 136.200 50.342 1.00   21.51 ? 5    VAL I CA  1 
ATOM   8947  C  C   . VAL I  1 6   ? 161.672 137.218 51.437 1.00   20.99 ? 5    VAL I C   1 
ATOM   8948  O  O   . VAL I  1 6   ? 162.017 138.392 51.322 1.00   20.71 ? 5    VAL I O   1 
ATOM   8949  C  CB  . VAL I  1 6   ? 163.248 135.377 50.669 1.00   21.79 ? 5    VAL I CB  1 
ATOM   8950  C  CG1 . VAL I  1 6   ? 164.435 136.297 50.981 1.00   21.69 ? 5    VAL I CG1 1 
ATOM   8951  C  CG2 . VAL I  1 6   ? 162.974 134.407 51.818 1.00   21.34 ? 5    VAL I CG2 1 
ATOM   8952  N  N   . CYS I  1 7   ? 161.001 136.768 52.490 1.00   20.52 ? 6    CYS I N   1 
ATOM   8953  C  CA  . CYS I  1 7   ? 160.618 137.643 53.576 1.00   20.66 ? 6    CYS I CA  1 
ATOM   8954  C  C   . CYS I  1 7   ? 160.689 136.905 54.919 1.00   20.36 ? 6    CYS I C   1 
ATOM   8955  O  O   . CYS I  1 7   ? 160.136 135.817 55.082 1.00   19.53 ? 6    CYS I O   1 
ATOM   8956  C  CB  . CYS I  1 7   ? 159.180 138.162 53.346 1.00   20.62 ? 6    CYS I CB  1 
ATOM   8957  S  SG  . CYS I  1 7   ? 158.605 139.308 54.622 1.00   21.01 ? 6    CYS I SG  1 
ATOM   8958  N  N   . VAL I  1 8   ? 161.360 137.518 55.884 1.00   20.61 ? 7    VAL I N   1 
ATOM   8959  C  CA  . VAL I  1 8   ? 161.409 136.980 57.215 1.00   20.58 ? 7    VAL I CA  1 
ATOM   8960  C  C   . VAL I  1 8   ? 160.399 137.775 58.014 1.00   20.77 ? 7    VAL I C   1 
ATOM   8961  O  O   . VAL I  1 8   ? 160.544 138.977 58.157 1.00   21.03 ? 7    VAL I O   1 
ATOM   8962  C  CB  . VAL I  1 8   ? 162.813 137.105 57.850 1.00   20.89 ? 7    VAL I CB  1 
ATOM   8963  C  CG1 . VAL I  1 8   ? 162.795 136.517 59.238 1.00   20.33 ? 7    VAL I CG1 1 
ATOM   8964  C  CG2 . VAL I  1 8   ? 163.878 136.413 57.004 1.00   21.38 ? 7    VAL I CG2 1 
ATOM   8965  N  N   . LEU I  1 9   ? 159.374 137.102 58.533 1.00   21.13 ? 8    LEU I N   1 
ATOM   8966  C  CA  . LEU I  1 9   ? 158.341 137.750 59.338 1.00   21.13 ? 8    LEU I CA  1 
ATOM   8967  C  C   . LEU I  1 9   ? 158.663 137.658 60.829 1.00   22.03 ? 8    LEU I C   1 
ATOM   8968  O  O   . LEU I  1 9   ? 158.894 136.578 61.369 1.00   21.65 ? 8    LEU I O   1 
ATOM   8969  C  CB  . LEU I  1 9   ? 157.001 137.072 59.100 1.00   21.24 ? 8    LEU I CB  1 
ATOM   8970  C  CG  . LEU I  1 9   ? 156.312 137.147 57.741 1.00   21.33 ? 8    LEU I CG  1 
ATOM   8971  C  CD1 . LEU I  1 9   ? 155.210 136.106 57.652 1.00   21.94 ? 8    LEU I CD1 1 
ATOM   8972  C  CD2 . LEU I  1 9   ? 155.703 138.513 57.529 1.00   21.92 ? 8    LEU I CD2 1 
ATOM   8973  N  N   . LYS I  1 10  ? 158.638 138.798 61.494 1.00   23.28 ? 9    LYS I N   1 
ATOM   8974  C  CA  . LYS I  1 10  ? 158.875 138.891 62.916 1.00   25.23 ? 9    LYS I CA  1 
ATOM   8975  C  C   . LYS I  1 10  ? 157.921 139.915 63.479 1.00   25.37 ? 9    LYS I C   1 
ATOM   8976  O  O   . LYS I  1 10  ? 157.499 140.816 62.764 1.00   25.03 ? 9    LYS I O   1 
ATOM   8977  C  CB  . LYS I  1 10  ? 160.305 139.338 63.196 1.00   27.33 ? 9    LYS I CB  1 
ATOM   8978  C  CG  . LYS I  1 10  ? 161.340 138.274 62.926 1.00   29.70 ? 9    LYS I CG  1 
ATOM   8979  C  CD  . LYS I  1 10  ? 162.764 138.829 62.879 1.00   32.07 ? 9    LYS I CD  1 
ATOM   8980  C  CE  . LYS I  1 10  ? 163.789 137.692 62.992 1.00   33.87 ? 9    LYS I CE  1 
ATOM   8981  N  NZ  . LYS I  1 10  ? 165.136 138.044 62.442 1.00   35.49 ? 9    LYS I NZ  1 
ATOM   8982  N  N   . GLY I  1 11  ? 157.578 139.781 64.756 1.00   26.42 ? 10   GLY I N   1 
ATOM   8983  C  CA  . GLY I  1 11  ? 156.819 140.827 65.446 1.00   27.62 ? 10   GLY I CA  1 
ATOM   8984  C  C   . GLY I  1 11  ? 157.144 140.953 66.921 1.00   28.55 ? 10   GLY I C   1 
ATOM   8985  O  O   . GLY I  1 11  ? 158.166 140.495 67.371 1.00   28.85 ? 10   GLY I O   1 
ATOM   8986  N  N   . ASP I  1 12  ? 156.240 141.565 67.667 1.00   29.83 ? 11   ASP I N   1 
ATOM   8987  C  CA  . ASP I  1 12  ? 156.422 141.755 69.095 1.00   31.15 ? 11   ASP I CA  1 
ATOM   8988  C  C   . ASP I  1 12  ? 156.154 140.493 69.916 1.00   31.16 ? 11   ASP I C   1 
ATOM   8989  O  O   . ASP I  1 12  ? 156.676 140.356 71.032 1.00   32.37 ? 11   ASP I O   1 
ATOM   8990  C  CB  . ASP I  1 12  ? 155.497 142.874 69.562 1.00   32.82 ? 11   ASP I CB  1 
ATOM   8991  C  CG  . ASP I  1 12  ? 155.934 144.227 69.060 1.00   35.31 ? 11   ASP I CG  1 
ATOM   8992  O  OD1 . ASP I  1 12  ? 157.148 144.394 68.764 1.00   36.99 ? 11   ASP I OD1 1 
ATOM   8993  O  OD2 . ASP I  1 12  ? 155.070 145.132 68.978 1.00   37.42 ? 11   ASP I OD2 1 
ATOM   8994  N  N   . GLY I  1 13  ? 155.348 139.579 69.372 1.00   27.81 ? 12   GLY I N   1 
ATOM   8995  C  CA  . GLY I  1 13  ? 154.935 138.381 70.089 1.00   26.68 ? 12   GLY I CA  1 
ATOM   8996  C  C   . GLY I  1 13  ? 155.603 137.174 69.490 1.00   25.66 ? 12   GLY I C   1 
ATOM   8997  O  O   . GLY I  1 13  ? 156.674 137.290 68.904 1.00   25.65 ? 12   GLY I O   1 
ATOM   8998  N  N   . PRO I  1 14  ? 154.967 136.003 69.606 1.00   24.16 ? 13   PRO I N   1 
ATOM   8999  C  CA  . PRO I  1 14  ? 155.612 134.797 69.115 1.00   23.90 ? 13   PRO I CA  1 
ATOM   9000  C  C   . PRO I  1 14  ? 155.483 134.528 67.610 1.00   22.84 ? 13   PRO I C   1 
ATOM   9001  O  O   . PRO I  1 14  ? 155.997 133.526 67.137 1.00   22.89 ? 13   PRO I O   1 
ATOM   9002  C  CB  . PRO I  1 14  ? 154.868 133.705 69.870 1.00   23.99 ? 13   PRO I CB  1 
ATOM   9003  C  CG  . PRO I  1 14  ? 153.482 134.240 69.958 1.00   24.12 ? 13   PRO I CG  1 
ATOM   9004  C  CD  . PRO I  1 14  ? 153.640 135.719 70.167 1.00   24.09 ? 13   PRO I CD  1 
ATOM   9005  N  N   . VAL I  1 15  ? 154.789 135.364 66.848 1.00   22.06 ? 14   VAL I N   1 
ATOM   9006  C  CA  . VAL I  1 15  ? 154.534 134.988 65.459 1.00   21.44 ? 14   VAL I CA  1 
ATOM   9007  C  C   . VAL I  1 15  ? 155.775 135.195 64.598 1.00   21.60 ? 14   VAL I C   1 
ATOM   9008  O  O   . VAL I  1 15  ? 156.355 136.270 64.598 1.00   21.61 ? 14   VAL I O   1 
ATOM   9009  C  CB  . VAL I  1 15  ? 153.311 135.700 64.845 1.00   20.65 ? 14   VAL I CB  1 
ATOM   9010  C  CG1 . VAL I  1 15  ? 153.153 135.308 63.385 1.00   19.79 ? 14   VAL I CG1 1 
ATOM   9011  C  CG2 . VAL I  1 15  ? 152.051 135.325 65.605 1.00   20.71 ? 14   VAL I CG2 1 
ATOM   9012  N  N   . GLN I  1 16  ? 156.178 134.170 63.856 1.00   21.89 ? 15   GLN I N   1 
ATOM   9013  C  CA  . GLN I  1 16  ? 157.364 134.290 62.998 1.00   22.05 ? 15   GLN I CA  1 
ATOM   9014  C  C   . GLN I  1 16  ? 157.375 133.270 61.884 1.00   21.08 ? 15   GLN I C   1 
ATOM   9015  O  O   . GLN I  1 16  ? 156.827 132.186 62.022 1.00   20.23 ? 15   GLN I O   1 
ATOM   9016  C  CB  . GLN I  1 16  ? 158.656 134.169 63.814 1.00   24.09 ? 15   GLN I CB  1 
ATOM   9017  C  CG  . GLN I  1 16  ? 158.943 132.783 64.388 1.00   25.45 ? 15   GLN I CG  1 
ATOM   9018  C  CD  . GLN I  1 16  ? 160.204 132.770 65.247 1.00   27.50 ? 15   GLN I CD  1 
ATOM   9019  O  OE1 . GLN I  1 16  ? 160.163 132.382 66.410 1.00   29.34 ? 15   GLN I OE1 1 
ATOM   9020  N  NE2 . GLN I  1 16  ? 161.329 133.200 64.676 1.00   28.36 ? 15   GLN I NE2 1 
ATOM   9021  N  N   . GLY I  1 17  ? 158.017 133.637 60.779 1.00   20.74 ? 16   GLY I N   1 
ATOM   9022  C  CA  . GLY I  1 17  ? 158.164 132.725 59.663 1.00   20.52 ? 16   GLY I CA  1 
ATOM   9023  C  C   . GLY I  1 17  ? 159.019 133.226 58.527 1.00   20.07 ? 16   GLY I C   1 
ATOM   9024  O  O   . GLY I  1 17  ? 159.586 134.328 58.560 1.00   20.00 ? 16   GLY I O   1 
ATOM   9025  N  N   . ILE I  1 18  ? 159.106 132.380 57.512 1.00   19.64 ? 17   ILE I N   1 
ATOM   9026  C  CA  . ILE I  1 18  ? 159.799 132.693 56.294 1.00   19.44 ? 17   ILE I CA  1 
ATOM   9027  C  C   . ILE I  1 18  ? 158.830 132.447 55.136 1.00   19.10 ? 17   ILE I C   1 
ATOM   9028  O  O   . ILE I  1 18  ? 158.253 131.356 55.029 1.00   19.30 ? 17   ILE I O   1 
ATOM   9029  C  CB  . ILE I  1 18  ? 161.063 131.815 56.130 1.00   19.53 ? 17   ILE I CB  1 
ATOM   9030  C  CG1 . ILE I  1 18  ? 162.080 132.118 57.215 1.00   19.61 ? 17   ILE I CG1 1 
ATOM   9031  C  CG2 . ILE I  1 18  ? 161.665 132.032 54.745 1.00   19.67 ? 17   ILE I CG2 1 
ATOM   9032  C  CD1 . ILE I  1 18  ? 163.254 131.140 57.282 1.00   20.07 ? 17   ILE I CD1 1 
ATOM   9033  N  N   . ILE I  1 19  ? 158.648 133.459 54.286 1.00   18.73 ? 18   ILE I N   1 
ATOM   9034  C  CA  . ILE I  1 19  ? 157.816 133.340 53.096 1.00   18.69 ? 18   ILE I CA  1 
ATOM   9035  C  C   . ILE I  1 19  ? 158.673 133.584 51.858 1.00   19.54 ? 18   ILE I C   1 
ATOM   9036  O  O   . ILE I  1 19  ? 159.419 134.574 51.784 1.00   19.67 ? 18   ILE I O   1 
ATOM   9037  C  CB  . ILE I  1 19  ? 156.612 134.305 53.136 1.00   17.99 ? 18   ILE I CB  1 
ATOM   9038  C  CG1 . ILE I  1 19  ? 155.706 133.976 54.345 1.00   17.49 ? 18   ILE I CG1 1 
ATOM   9039  C  CG2 . ILE I  1 19  ? 155.784 134.239 51.842 1.00   17.77 ? 18   ILE I CG2 1 
ATOM   9040  C  CD1 . ILE I  1 19  ? 154.989 132.646 54.252 1.00   17.07 ? 18   ILE I CD1 1 
ATOM   9041  N  N   . ASN I  1 20  ? 158.552 132.658 50.909 1.00   20.03 ? 19   ASN I N   1 
ATOM   9042  C  CA  . ASN I  1 20  ? 159.255 132.690 49.640 1.00   21.01 ? 19   ASN I CA  1 
ATOM   9043  C  C   . ASN I  1 20  ? 158.327 133.125 48.531 1.00   21.44 ? 19   ASN I C   1 
ATOM   9044  O  O   . ASN I  1 20  ? 157.130 132.861 48.591 1.00   21.86 ? 19   ASN I O   1 
ATOM   9045  C  CB  . ASN I  1 20  ? 159.794 131.292 49.306 1.00   21.17 ? 19   ASN I CB  1 
ATOM   9046  C  CG  . ASN I  1 20  ? 160.680 130.728 50.395 1.00   21.25 ? 19   ASN I CG  1 
ATOM   9047  O  OD1 . ASN I  1 20  ? 160.281 129.813 51.130 1.00   21.67 ? 19   ASN I OD1 1 
ATOM   9048  N  ND2 . ASN I  1 20  ? 161.861 131.280 50.528 1.00   21.38 ? 19   ASN I ND2 1 
ATOM   9049  N  N   . PHE I  1 21  ? 158.889 133.768 47.513 1.00   22.49 ? 20   PHE I N   1 
ATOM   9050  C  CA  . PHE I  1 21  ? 158.142 134.233 46.333 1.00   23.16 ? 20   PHE I CA  1 
ATOM   9051  C  C   . PHE I  1 21  ? 158.919 133.815 45.088 1.00   24.74 ? 20   PHE I C   1 
ATOM   9052  O  O   . PHE I  1 21  ? 160.158 133.967 45.019 1.00   23.82 ? 20   PHE I O   1 
ATOM   9053  C  CB  . PHE I  1 21  ? 158.051 135.762 46.303 1.00   23.12 ? 20   PHE I CB  1 
ATOM   9054  C  CG  . PHE I  1 21  ? 157.303 136.374 47.453 1.00   22.96 ? 20   PHE I CG  1 
ATOM   9055  C  CD1 . PHE I  1 21  ? 157.922 136.580 48.670 1.00   22.82 ? 20   PHE I CD1 1 
ATOM   9056  C  CD2 . PHE I  1 21  ? 155.985 136.781 47.304 1.00   23.20 ? 20   PHE I CD2 1 
ATOM   9057  C  CE1 . PHE I  1 21  ? 157.236 137.147 49.732 1.00   22.81 ? 20   PHE I CE1 1 
ATOM   9058  C  CE2 . PHE I  1 21  ? 155.296 137.359 48.368 1.00   23.02 ? 20   PHE I CE2 1 
ATOM   9059  C  CZ  . PHE I  1 21  ? 155.926 137.536 49.578 1.00   22.65 ? 20   PHE I CZ  1 
ATOM   9060  N  N   . GLU I  1 22  ? 158.203 133.322 44.084 1.00   26.33 ? 21   GLU I N   1 
ATOM   9061  C  CA  . GLU I  1 22  ? 158.829 132.983 42.813 1.00   27.98 ? 21   GLU I CA  1 
ATOM   9062  C  C   . GLU I  1 22  ? 157.943 133.365 41.654 1.00   28.34 ? 21   GLU I C   1 
ATOM   9063  O  O   . GLU I  1 22  ? 156.769 132.990 41.625 1.00   27.37 ? 21   GLU I O   1 
ATOM   9064  C  CB  . GLU I  1 22  ? 159.136 131.498 42.732 1.00   29.55 ? 21   GLU I CB  1 
ATOM   9065  C  CG  . GLU I  1 22  ? 159.999 131.150 41.537 1.00   31.60 ? 21   GLU I CG  1 
ATOM   9066  C  CD  . GLU I  1 22  ? 160.295 129.670 41.439 1.00   33.72 ? 21   GLU I CD  1 
ATOM   9067  O  OE1 . GLU I  1 22  ? 159.342 128.863 41.439 1.00   36.64 ? 21   GLU I OE1 1 
ATOM   9068  O  OE2 . GLU I  1 22  ? 161.480 129.319 41.346 1.00   36.75 ? 21   GLU I OE2 1 
ATOM   9069  N  N   . GLN I  1 23  ? 158.528 134.099 40.713 1.00   28.27 ? 22   GLN I N   1 
ATOM   9070  C  CA  . GLN I  1 23  ? 157.868 134.517 39.504 1.00   30.17 ? 22   GLN I CA  1 
ATOM   9071  C  C   . GLN I  1 23  ? 158.737 134.155 38.300 1.00   33.02 ? 22   GLN I C   1 
ATOM   9072  O  O   . GLN I  1 23  ? 159.718 134.835 38.003 1.00   33.32 ? 22   GLN I O   1 
ATOM   9073  C  CB  . GLN I  1 23  ? 157.620 136.015 39.546 1.00   28.83 ? 22   GLN I CB  1 
ATOM   9074  C  CG  . GLN I  1 23  ? 156.805 136.508 38.377 1.00   28.91 ? 22   GLN I CG  1 
ATOM   9075  C  CD  . GLN I  1 23  ? 156.422 137.956 38.519 1.00   28.48 ? 22   GLN I CD  1 
ATOM   9076  O  OE1 . GLN I  1 23  ? 157.113 138.726 39.177 1.00   28.49 ? 22   GLN I OE1 1 
ATOM   9077  N  NE2 . GLN I  1 23  ? 155.306 138.332 37.925 1.00   28.50 ? 22   GLN I NE2 1 
ATOM   9078  N  N   . LYS I  1 24  ? 158.381 133.086 37.601 1.00   35.83 ? 23   LYS I N   1 
ATOM   9079  C  CA  . LYS I  1 24  ? 159.181 132.653 36.448 1.00   39.02 ? 23   LYS I CA  1 
ATOM   9080  C  C   . LYS I  1 24  ? 158.990 133.505 35.175 1.00   38.28 ? 23   LYS I C   1 
ATOM   9081  O  O   . LYS I  1 24  ? 159.870 133.518 34.330 1.00   37.94 ? 23   LYS I O   1 
ATOM   9082  C  CB  . LYS I  1 24  ? 158.954 131.161 36.167 1.00   42.59 ? 23   LYS I CB  1 
ATOM   9083  C  CG  . LYS I  1 24  ? 159.700 130.257 37.153 1.00   45.40 ? 23   LYS I CG  1 
ATOM   9084  C  CD  . LYS I  1 24  ? 159.607 128.780 36.781 1.00   48.72 ? 23   LYS I CD  1 
ATOM   9085  C  CE  . LYS I  1 24  ? 160.917 128.012 36.978 1.00   51.09 ? 23   LYS I CE  1 
ATOM   9086  N  NZ  . LYS I  1 24  ? 160.857 126.677 36.291 1.00   53.17 ? 23   LYS I NZ  1 
ATOM   9087  N  N   . GLU I  1 25  ? 157.874 134.226 35.048 1.00   37.49 ? 24   GLU I N   1 
ATOM   9088  C  CA  . GLU I  1 25  ? 157.605 135.053 33.857 1.00   38.49 ? 24   GLU I CA  1 
ATOM   9089  C  C   . GLU I  1 25  ? 157.072 136.440 34.246 1.00   39.37 ? 24   GLU I C   1 
ATOM   9090  O  O   . GLU I  1 25  ? 156.240 136.566 35.162 1.00   38.16 ? 24   GLU I O   1 
ATOM   9091  C  CB  . GLU I  1 25  ? 156.561 134.370 32.978 1.00   39.23 ? 24   GLU I CB  1 
ATOM   9092  C  CG  . GLU I  1 25  ? 156.822 132.903 32.711 1.00   40.08 ? 24   GLU I CG  1 
ATOM   9093  C  CD  . GLU I  1 25  ? 155.668 132.239 32.007 1.00   42.18 ? 24   GLU I CD  1 
ATOM   9094  O  OE1 . GLU I  1 25  ? 154.659 131.915 32.673 1.00   43.97 ? 24   GLU I OE1 1 
ATOM   9095  O  OE2 . GLU I  1 25  ? 155.767 132.040 30.777 1.00   45.19 ? 24   GLU I OE2 1 
ATOM   9096  N  N   . SER I  1 26  ? 157.495 137.470 33.522 1.00   39.99 ? 25   SER I N   1 
ATOM   9097  C  CA  . SER I  1 26  ? 157.253 138.852 33.951 1.00   40.88 ? 25   SER I CA  1 
ATOM   9098  C  C   . SER I  1 26  ? 155.772 139.278 33.920 1.00   41.05 ? 25   SER I C   1 
ATOM   9099  O  O   . SER I  1 26  ? 155.363 140.222 34.598 1.00   42.27 ? 25   SER I O   1 
ATOM   9100  C  CB  . SER I  1 26  ? 158.099 139.814 33.111 1.00   42.28 ? 25   SER I CB  1 
ATOM   9101  O  OG  . SER I  1 26  ? 157.622 139.908 31.782 1.00   41.01 ? 25   SER I OG  1 
ATOM   9102  N  N   . ASN I  1 27  ? 154.971 138.592 33.128 1.00   41.38 ? 26   ASN I N   1 
ATOM   9103  C  CA  . ASN I  1 27  ? 153.535 138.850 33.096 1.00   41.33 ? 26   ASN I CA  1 
ATOM   9104  C  C   . ASN I  1 27  ? 152.795 137.653 33.687 1.00   38.64 ? 26   ASN I C   1 
ATOM   9105  O  O   . ASN I  1 27  ? 151.655 137.391 33.320 1.00   40.55 ? 26   ASN I O   1 
ATOM   9106  C  CB  . ASN I  1 27  ? 153.090 139.088 31.648 1.00   43.38 ? 26   ASN I CB  1 
ATOM   9107  C  CG  . ASN I  1 27  ? 153.221 137.839 30.783 1.00   45.09 ? 26   ASN I CG  1 
ATOM   9108  O  OD1 . ASN I  1 27  ? 153.911 136.878 31.166 1.00   46.45 ? 26   ASN I OD1 1 
ATOM   9109  N  ND2 . ASN I  1 27  ? 152.560 137.837 29.621 1.00   44.38 ? 26   ASN I ND2 1 
ATOM   9110  N  N   . GLY I  1 28  ? 153.456 136.916 34.575 1.00   36.50 ? 27   GLY I N   1 
ATOM   9111  C  CA  . GLY I  1 28  ? 152.949 135.627 35.050 1.00   34.35 ? 27   GLY I CA  1 
ATOM   9112  C  C   . GLY I  1 28  ? 152.784 135.530 36.558 1.00   32.14 ? 27   GLY I C   1 
ATOM   9113  O  O   . GLY I  1 28  ? 153.154 136.451 37.287 1.00   31.83 ? 27   GLY I O   1 
ATOM   9114  N  N   . PRO I  1 29  ? 152.255 134.392 37.044 1.00   30.53 ? 28   PRO I N   1 
ATOM   9115  C  CA  . PRO I  1 29  ? 151.908 134.277 38.460 1.00   29.15 ? 28   PRO I CA  1 
ATOM   9116  C  C   . PRO I  1 29  ? 153.107 134.210 39.387 1.00   27.41 ? 28   PRO I C   1 
ATOM   9117  O  O   . PRO I  1 29  ? 154.164 133.711 39.006 1.00   27.86 ? 28   PRO I O   1 
ATOM   9118  C  CB  . PRO I  1 29  ? 151.120 132.948 38.542 1.00   29.49 ? 28   PRO I CB  1 
ATOM   9119  C  CG  . PRO I  1 29  ? 150.867 132.523 37.137 1.00   30.37 ? 28   PRO I CG  1 
ATOM   9120  C  CD  . PRO I  1 29  ? 151.976 133.139 36.325 1.00   31.09 ? 28   PRO I CD  1 
ATOM   9121  N  N   . VAL I  1 30  ? 152.919 134.717 40.601 1.00   25.90 ? 29   VAL I N   1 
ATOM   9122  C  CA  . VAL I  1 30  ? 153.881 134.552 41.673 1.00   24.52 ? 29   VAL I CA  1 
ATOM   9123  C  C   . VAL I  1 30  ? 153.414 133.437 42.592 1.00   23.91 ? 29   VAL I C   1 
ATOM   9124  O  O   . VAL I  1 30  ? 152.309 133.477 43.119 1.00   24.11 ? 29   VAL I O   1 
ATOM   9125  C  CB  . VAL I  1 30  ? 154.031 135.847 42.475 1.00   23.92 ? 29   VAL I CB  1 
ATOM   9126  C  CG1 . VAL I  1 30  ? 155.112 135.701 43.529 1.00   23.29 ? 29   VAL I CG1 1 
ATOM   9127  C  CG2 . VAL I  1 30  ? 154.329 137.004 41.528 1.00   23.90 ? 29   VAL I CG2 1 
ATOM   9128  N  N   . LYS I  1 31  ? 154.268 132.452 42.800 1.00   23.91 ? 30   LYS I N   1 
ATOM   9129  C  CA  . LYS I  1 31  ? 154.065 131.419 43.809 1.00   24.07 ? 30   LYS I CA  1 
ATOM   9130  C  C   . LYS I  1 31  ? 154.502 132.010 45.159 1.00   23.47 ? 30   LYS I C   1 
ATOM   9131  O  O   . LYS I  1 31  ? 155.560 132.645 45.242 1.00   23.14 ? 30   LYS I O   1 
ATOM   9132  C  CB  . LYS I  1 31  ? 154.941 130.232 43.447 1.00   25.88 ? 30   LYS I CB  1 
ATOM   9133  C  CG  . LYS I  1 31  ? 154.469 128.877 43.934 1.00   27.37 ? 30   LYS I CG  1 
ATOM   9134  C  CD  . LYS I  1 31  ? 155.080 127.753 43.102 0.10   27.79 ? 30   LYS I CD  1 
ATOM   9135  C  CE  . LYS I  1 31  ? 154.422 126.413 43.390 0.10   28.24 ? 30   LYS I CE  1 
ATOM   9136  N  NZ  . LYS I  1 31  ? 154.855 125.353 42.436 0.10   28.78 ? 30   LYS I NZ  1 
ATOM   9137  N  N   . VAL I  1 32  ? 153.701 131.814 46.212 1.00   22.09 ? 31   VAL I N   1 
ATOM   9138  C  CA  . VAL I  1 32  ? 154.032 132.337 47.545 1.00   21.05 ? 31   VAL I CA  1 
ATOM   9139  C  C   . VAL I  1 32  ? 153.917 131.173 48.497 1.00   21.03 ? 31   VAL I C   1 
ATOM   9140  O  O   . VAL I  1 32  ? 152.846 130.585 48.614 1.00   20.29 ? 31   VAL I O   1 
ATOM   9141  C  CB  . VAL I  1 32  ? 153.085 133.468 47.990 1.00   20.40 ? 31   VAL I CB  1 
ATOM   9142  C  CG1 . VAL I  1 32  ? 153.435 133.965 49.387 1.00   19.85 ? 31   VAL I CG1 1 
ATOM   9143  C  CG2 . VAL I  1 32  ? 153.113 134.630 47.008 1.00   20.33 ? 31   VAL I CG2 1 
ATOM   9144  N  N   . TRP I  1 33  ? 155.020 130.802 49.149 1.00   21.35 ? 32   TRP I N   1 
ATOM   9145  C  CA  . TRP I  1 33  ? 154.991 129.675 50.078 1.00   21.49 ? 32   TRP I CA  1 
ATOM   9146  C  C   . TRP I  1 33  ? 155.961 129.799 51.210 1.00   21.55 ? 32   TRP I C   1 
ATOM   9147  O  O   . TRP I  1 33  ? 156.953 130.545 51.142 1.00   21.08 ? 32   TRP I O   1 
ATOM   9148  C  CB  . TRP I  1 33  ? 155.235 128.353 49.350 1.00   22.72 ? 32   TRP I CB  1 
ATOM   9149  C  CG  . TRP I  1 33  ? 156.665 128.124 48.950 1.00   23.87 ? 32   TRP I CG  1 
ATOM   9150  C  CD1 . TRP I  1 33  ? 157.601 127.281 49.559 1.00   24.51 ? 32   TRP I CD1 1 
ATOM   9151  C  CD2 . TRP I  1 33  ? 157.386 128.768 47.852 1.00   24.53 ? 32   TRP I CD2 1 
ATOM   9152  N  NE1 . TRP I  1 33  ? 158.805 127.356 48.908 1.00   25.44 ? 32   TRP I NE1 1 
ATOM   9153  C  CE2 . TRP I  1 33  ? 158.736 128.232 47.877 1.00   24.99 ? 32   TRP I CE2 1 
ATOM   9154  C  CE3 . TRP I  1 33  ? 157.059 129.724 46.898 1.00   25.18 ? 32   TRP I CE3 1 
ATOM   9155  C  CZ2 . TRP I  1 33  ? 159.707 128.639 46.969 1.00   26.23 ? 32   TRP I CZ2 1 
ATOM   9156  C  CZ3 . TRP I  1 33  ? 158.042 130.123 45.980 1.00   25.77 ? 32   TRP I CZ3 1 
ATOM   9157  C  CH2 . TRP I  1 33  ? 159.340 129.596 46.026 1.00   26.33 ? 32   TRP I CH2 1 
ATOM   9158  N  N   . GLY I  1 34  ? 155.676 129.043 52.259 1.00   20.79 ? 33   GLY I N   1 
ATOM   9159  C  CA  . GLY I  1 34  ? 156.539 128.992 53.402 1.00   21.24 ? 33   GLY I CA  1 
ATOM   9160  C  C   . GLY I  1 34  ? 155.740 128.663 54.636 1.00   21.04 ? 33   GLY I C   1 
ATOM   9161  O  O   . GLY I  1 34  ? 154.638 128.181 54.539 1.00   21.33 ? 33   GLY I O   1 
ATOM   9162  N  N   . SER I  1 35  ? 156.317 128.906 55.790 1.00   21.33 ? 34   SER I N   1 
ATOM   9163  C  CA  . SER I  1 35  ? 155.740 128.473 57.049 1.00   21.70 ? 34   SER I CA  1 
ATOM   9164  C  C   . SER I  1 35  ? 155.751 129.618 58.039 1.00   20.79 ? 34   SER I C   1 
ATOM   9165  O  O   . SER I  1 35  ? 156.779 130.281 58.182 1.00   20.90 ? 34   SER I O   1 
ATOM   9166  C  CB  . SER I  1 35  ? 156.562 127.332 57.606 1.00   22.93 ? 34   SER I CB  1 
ATOM   9167  O  OG  . SER I  1 35  ? 155.764 126.611 58.510 1.00   25.50 ? 34   SER I OG  1 
ATOM   9168  N  N   . ILE I  1 36  ? 154.620 129.856 58.695 1.00   19.77 ? 35   ILE I N   1 
ATOM   9169  C  CA  . ILE I  1 36  ? 154.518 130.828 59.771 1.00   19.51 ? 35   ILE I CA  1 
ATOM   9170  C  C   . ILE I  1 36  ? 154.051 130.053 60.997 1.00   19.57 ? 35   ILE I C   1 
ATOM   9171  O  O   . ILE I  1 36  ? 153.141 129.236 60.893 1.00   19.49 ? 35   ILE I O   1 
ATOM   9172  C  CB  . ILE I  1 36  ? 153.501 131.952 59.428 1.00   19.14 ? 35   ILE I CB  1 
ATOM   9173  C  CG1 . ILE I  1 36  ? 153.823 132.579 58.068 1.00   18.84 ? 35   ILE I CG1 1 
ATOM   9174  C  CG2 . ILE I  1 36  ? 153.485 133.006 60.520 1.00   18.61 ? 35   ILE I CG2 1 
ATOM   9175  C  CD1 . ILE I  1 36  ? 152.775 133.547 57.543 1.00   18.43 ? 35   ILE I CD1 1 
ATOM   9176  N  N   . LYS I  1 37  ? 154.693 130.282 62.140 1.00   19.69 ? 36   LYS I N   1 
ATOM   9177  C  CA  . LYS I  1 37  ? 154.348 129.592 63.399 1.00   20.22 ? 36   LYS I CA  1 
ATOM   9178  C  C   . LYS I  1 37  ? 153.966 130.592 64.488 1.00   19.89 ? 36   LYS I C   1 
ATOM   9179  O  O   . LYS I  1 37  ? 154.147 131.797 64.319 1.00   19.38 ? 36   LYS I O   1 
ATOM   9180  C  CB  . LYS I  1 37  ? 155.485 128.660 63.871 1.00   21.12 ? 36   LYS I CB  1 
ATOM   9181  C  CG  . LYS I  1 37  ? 156.778 129.347 64.286 1.00   21.47 ? 36   LYS I CG  1 
ATOM   9182  C  CD  . LYS I  1 37  ? 157.873 128.324 64.602 1.00   22.40 ? 36   LYS I CD  1 
ATOM   9183  C  CE  . LYS I  1 37  ? 159.133 129.002 65.165 1.00   22.78 ? 36   LYS I CE  1 
ATOM   9184  N  NZ  . LYS I  1 37  ? 160.145 128.041 65.684 1.00   23.46 ? 36   LYS I NZ  1 
ATOM   9185  N  N   . GLY I  1 38  ? 153.397 130.090 65.573 1.00   19.85 ? 37   GLY I N   1 
ATOM   9186  C  CA  . GLY I  1 38  ? 152.987 130.936 66.686 1.00   19.87 ? 37   GLY I CA  1 
ATOM   9187  C  C   . GLY I  1 38  ? 151.654 131.646 66.500 1.00   19.74 ? 37   GLY I C   1 
ATOM   9188  O  O   . GLY I  1 38  ? 151.320 132.565 67.278 1.00   19.47 ? 37   GLY I O   1 
ATOM   9189  N  N   . LEU I  1 39  ? 150.881 131.204 65.498 1.00   19.40 ? 38   LEU I N   1 
ATOM   9190  C  CA  . LEU I  1 39  ? 149.572 131.788 65.168 1.00   19.20 ? 38   LEU I CA  1 
ATOM   9191  C  C   . LEU I  1 39  ? 148.477 131.048 65.903 1.00   19.76 ? 38   LEU I C   1 
ATOM   9192  O  O   . LEU I  1 39  ? 148.619 129.865 66.169 1.00   20.45 ? 38   LEU I O   1 
ATOM   9193  C  CB  . LEU I  1 39  ? 149.280 131.685 63.659 1.00   18.80 ? 38   LEU I CB  1 
ATOM   9194  C  CG  . LEU I  1 39  ? 150.078 132.569 62.697 1.00   18.59 ? 38   LEU I CG  1 
ATOM   9195  C  CD1 . LEU I  1 39  ? 149.933 132.095 61.259 1.00   18.50 ? 38   LEU I CD1 1 
ATOM   9196  C  CD2 . LEU I  1 39  ? 149.609 134.019 62.846 1.00   18.74 ? 38   LEU I CD2 1 
ATOM   9197  N  N   . THR I  1 40  ? 147.383 131.730 66.228 1.00   19.71 ? 39   THR I N   1 
ATOM   9198  C  CA  . THR I  1 40  ? 146.193 131.030 66.673 1.00   20.33 ? 39   THR I CA  1 
ATOM   9199  C  C   . THR I  1 40  ? 145.599 130.247 65.489 1.00   20.49 ? 39   THR I C   1 
ATOM   9200  O  O   . THR I  1 40  ? 145.574 130.715 64.359 1.00   19.65 ? 39   THR I O   1 
ATOM   9201  C  CB  . THR I  1 40  ? 145.106 131.979 67.216 1.00   20.08 ? 39   THR I CB  1 
ATOM   9202  O  OG1 . THR I  1 40  ? 144.696 132.863 66.174 1.00   20.05 ? 39   THR I OG1 1 
ATOM   9203  C  CG2 . THR I  1 40  ? 145.608 132.786 68.405 1.00   20.00 ? 39   THR I CG2 1 
ATOM   9204  N  N   . GLU I  1 41  ? 145.103 129.058 65.773 1.00   21.57 ? 40   GLU I N   1 
ATOM   9205  C  CA  . GLU I  1 41  ? 144.431 128.236 64.776 1.00   21.82 ? 40   GLU I CA  1 
ATOM   9206  C  C   . GLU I  1 41  ? 143.344 129.008 64.056 1.00   21.35 ? 40   GLU I C   1 
ATOM   9207  O  O   . GLU I  1 41  ? 142.569 129.718 64.680 1.00   21.84 ? 40   GLU I O   1 
ATOM   9208  C  CB  . GLU I  1 41  ? 143.807 127.015 65.454 1.00   22.86 ? 40   GLU I CB  1 
ATOM   9209  C  CG  . GLU I  1 41  ? 143.085 126.100 64.484 1.00   23.32 ? 40   GLU I CG  1 
ATOM   9210  C  CD  . GLU I  1 41  ? 142.477 124.882 65.145 1.00   24.65 ? 40   GLU I CD  1 
ATOM   9211  O  OE1 . GLU I  1 41  ? 142.501 124.747 66.390 1.00   25.50 ? 40   GLU I OE1 1 
ATOM   9212  O  OE2 . GLU I  1 41  ? 141.970 124.044 64.392 1.00   25.60 ? 40   GLU I OE2 1 
ATOM   9213  N  N   . GLY I  1 42  ? 143.285 128.866 62.734 1.00   20.93 ? 41   GLY I N   1 
ATOM   9214  C  CA  . GLY I  1 42  ? 142.238 129.523 61.932 1.00   20.13 ? 41   GLY I CA  1 
ATOM   9215  C  C   . GLY I  1 42  ? 142.801 130.522 60.936 1.00   19.41 ? 41   GLY I C   1 
ATOM   9216  O  O   . GLY I  1 42  ? 143.992 130.503 60.609 1.00   19.02 ? 41   GLY I O   1 
ATOM   9217  N  N   . LEU I  1 43  ? 141.927 131.399 60.467 1.00   18.92 ? 42   LEU I N   1 
ATOM   9218  C  CA  . LEU I  1 43  ? 142.214 132.268 59.341 1.00   18.58 ? 42   LEU I CA  1 
ATOM   9219  C  C   . LEU I  1 43  ? 142.957 133.520 59.771 1.00   18.09 ? 42   LEU I C   1 
ATOM   9220  O  O   . LEU I  1 43  ? 142.589 134.123 60.762 1.00   19.13 ? 42   LEU I O   1 
ATOM   9221  C  CB  . LEU I  1 43  ? 140.908 132.675 58.657 1.00   18.78 ? 42   LEU I CB  1 
ATOM   9222  C  CG  . LEU I  1 43  ? 140.125 131.590 57.921 1.00   19.08 ? 42   LEU I CG  1 
ATOM   9223  C  CD1 . LEU I  1 43  ? 138.687 132.082 57.637 1.00   19.27 ? 42   LEU I CD1 1 
ATOM   9224  C  CD2 . LEU I  1 43  ? 140.839 131.215 56.628 1.00   19.17 ? 42   LEU I CD2 1 
ATOM   9225  N  N   . HIS I  1 44  ? 143.985 133.922 59.024 1.00   17.03 ? 43   HIS I N   1 
ATOM   9226  C  CA  . HIS I  1 44  ? 144.685 135.179 59.294 1.00   16.28 ? 43   HIS I CA  1 
ATOM   9227  C  C   . HIS I  1 44  ? 144.895 135.972 58.025 1.00   16.00 ? 43   HIS I C   1 
ATOM   9228  O  O   . HIS I  1 44  ? 145.365 135.434 57.031 1.00   15.68 ? 43   HIS I O   1 
ATOM   9229  C  CB  . HIS I  1 44  ? 146.033 134.890 59.948 1.00   16.08 ? 43   HIS I CB  1 
ATOM   9230  C  CG  . HIS I  1 44  ? 145.921 134.327 61.336 1.00   16.28 ? 43   HIS I CG  1 
ATOM   9231  N  ND1 . HIS I  1 44  ? 145.846 135.108 62.439 1.00   16.30 ? 43   HIS I ND1 1 
ATOM   9232  C  CD2 . HIS I  1 44  ? 145.840 133.010 61.774 1.00   16.32 ? 43   HIS I CD2 1 
ATOM   9233  C  CE1 . HIS I  1 44  ? 145.743 134.315 63.515 1.00   17.01 ? 43   HIS I CE1 1 
ATOM   9234  N  NE2 . HIS I  1 44  ? 145.744 133.031 63.102 1.00   16.68 ? 43   HIS I NE2 1 
ATOM   9235  N  N   . GLY I  1 45  ? 144.554 137.264 58.064 1.00   16.00 ? 44   GLY I N   1 
ATOM   9236  C  CA  . GLY I  1 45  ? 144.807 138.199 56.959 1.00   15.95 ? 44   GLY I CA  1 
ATOM   9237  C  C   . GLY I  1 45  ? 146.284 138.274 56.592 1.00   15.81 ? 44   GLY I C   1 
ATOM   9238  O  O   . GLY I  1 45  ? 147.152 138.206 57.467 1.00   15.67 ? 44   GLY I O   1 
ATOM   9239  N  N   . PHE I  1 46  ? 146.549 138.447 55.301 1.00   15.66 ? 45   PHE I N   1 
ATOM   9240  C  CA  . PHE I  1 46  ? 147.864 138.261 54.703 1.00   15.67 ? 45   PHE I CA  1 
ATOM   9241  C  C   . PHE I  1 46  ? 147.985 139.238 53.521 1.00   15.76 ? 45   PHE I C   1 
ATOM   9242  O  O   . PHE I  1 46  ? 147.363 139.036 52.453 1.00   15.60 ? 45   PHE I O   1 
ATOM   9243  C  CB  . PHE I  1 46  ? 147.981 136.796 54.243 1.00   15.68 ? 45   PHE I CB  1 
ATOM   9244  C  CG  . PHE I  1 46  ? 149.395 136.328 53.955 1.00   16.07 ? 45   PHE I CG  1 
ATOM   9245  C  CD1 . PHE I  1 46  ? 150.381 136.310 54.963 1.00   16.04 ? 45   PHE I CD1 1 
ATOM   9246  C  CD2 . PHE I  1 46  ? 149.726 135.822 52.700 1.00   16.01 ? 45   PHE I CD2 1 
ATOM   9247  C  CE1 . PHE I  1 46  ? 151.667 135.848 54.697 1.00   16.10 ? 45   PHE I CE1 1 
ATOM   9248  C  CE2 . PHE I  1 46  ? 151.013 135.339 52.438 1.00   16.22 ? 45   PHE I CE2 1 
ATOM   9249  C  CZ  . PHE I  1 46  ? 151.983 135.353 53.430 1.00   16.26 ? 45   PHE I CZ  1 
ATOM   9250  N  N   . HIS I  1 47  ? 148.741 140.316 53.713 1.00   15.86 ? 46   HIS I N   1 
ATOM   9251  C  CA  . HIS I  1 47  ? 148.776 141.396 52.739 1.00   16.30 ? 46   HIS I CA  1 
ATOM   9252  C  C   . HIS I  1 47  ? 150.132 141.939 52.497 1.00   16.43 ? 46   HIS I C   1 
ATOM   9253  O  O   . HIS I  1 47  ? 150.984 141.866 53.365 1.00   16.23 ? 46   HIS I O   1 
ATOM   9254  C  CB  . HIS I  1 47  ? 147.965 142.556 53.248 1.00   16.73 ? 46   HIS I CB  1 
ATOM   9255  C  CG  . HIS I  1 47  ? 146.647 142.185 53.825 1.00   16.89 ? 46   HIS I CG  1 
ATOM   9256  N  ND1 . HIS I  1 47  ? 146.246 142.631 55.032 1.00   17.29 ? 46   HIS I ND1 1 
ATOM   9257  C  CD2 . HIS I  1 47  ? 145.604 141.441 53.315 1.00   16.93 ? 46   HIS I CD2 1 
ATOM   9258  C  CE1 . HIS I  1 47  ? 145.012 142.169 55.295 1.00   17.21 ? 46   HIS I CE1 1 
ATOM   9259  N  NE2 . HIS I  1 47  ? 144.616 141.440 54.251 1.00   17.23 ? 46   HIS I NE2 1 
ATOM   9260  N  N   . VAL I  1 48  ? 150.340 142.529 51.324 1.00   16.92 ? 47   VAL I N   1 
ATOM   9261  C  CA  . VAL I  1 48  ? 151.498 143.386 51.088 1.00   17.16 ? 47   VAL I CA  1 
ATOM   9262  C  C   . VAL I  1 48  ? 151.091 144.814 51.390 1.00   17.87 ? 47   VAL I C   1 
ATOM   9263  O  O   . VAL I  1 48  ? 150.083 145.325 50.862 1.00   18.16 ? 47   VAL I O   1 
ATOM   9264  C  CB  . VAL I  1 48  ? 152.059 143.307 49.665 1.00   17.33 ? 47   VAL I CB  1 
ATOM   9265  C  CG1 . VAL I  1 48  ? 153.269 144.250 49.532 1.00   17.03 ? 47   VAL I CG1 1 
ATOM   9266  C  CG2 . VAL I  1 48  ? 152.412 141.870 49.308 1.00   16.75 ? 47   VAL I CG2 1 
ATOM   9267  N  N   . HIS I  1 49  ? 151.830 145.426 52.309 1.00   18.45 ? 48   HIS I N   1 
ATOM   9268  C  CA  . HIS I  1 49  ? 151.598 146.809 52.689 1.00   19.57 ? 48   HIS I CA  1 
ATOM   9269  C  C   . HIS I  1 49  ? 152.577 147.677 51.965 1.00   21.05 ? 48   HIS I C   1 
ATOM   9270  O  O   . HIS I  1 49  ? 153.607 147.211 51.475 1.00   21.45 ? 48   HIS I O   1 
ATOM   9271  C  CB  . HIS I  1 49  ? 151.713 146.989 54.190 1.00   19.48 ? 48   HIS I CB  1 
ATOM   9272  C  CG  . HIS I  1 49  ? 150.510 146.511 54.953 1.00   19.14 ? 48   HIS I CG  1 
ATOM   9273  N  ND1 . HIS I  1 49  ? 149.809 147.320 55.757 1.00   19.51 ? 48   HIS I ND1 1 
ATOM   9274  C  CD2 . HIS I  1 49  ? 149.887 145.261 55.015 1.00   18.90 ? 48   HIS I CD2 1 
ATOM   9275  C  CE1 . HIS I  1 49  ? 148.779 146.627 56.315 1.00   19.41 ? 48   HIS I CE1 1 
ATOM   9276  N  NE2 . HIS I  1 49  ? 148.833 145.372 55.871 1.00   18.78 ? 48   HIS I NE2 1 
ATOM   9277  N  N   . GLU I  1 50  ? 152.257 148.958 51.888 1.00   22.48 ? 49   GLU I N   1 
ATOM   9278  C  CA  . GLU I  1 50  ? 152.943 149.865 50.998 1.00   23.12 ? 49   GLU I CA  1 
ATOM   9279  C  C   . GLU I  1 50  ? 154.415 150.129 51.294 1.00   23.43 ? 49   GLU I C   1 
ATOM   9280  O  O   . GLU I  1 50  ? 155.228 150.163 50.387 1.00   23.85 ? 49   GLU I O   1 
ATOM   9281  C  CB  . GLU I  1 50  ? 152.185 151.181 50.969 1.00   24.31 ? 49   GLU I CB  1 
ATOM   9282  C  CG  . GLU I  1 50  ? 152.774 152.178 50.006 1.00   25.29 ? 49   GLU I CG  1 
ATOM   9283  C  CD  . GLU I  1 50  ? 151.936 153.419 49.877 1.00   26.43 ? 49   GLU I CD  1 
ATOM   9284  O  OE1 . GLU I  1 50  ? 150.974 153.600 50.658 1.00   26.95 ? 49   GLU I OE1 1 
ATOM   9285  O  OE2 . GLU I  1 50  ? 152.274 154.216 48.989 1.00   27.81 ? 49   GLU I OE2 1 
ATOM   9286  N  N   . PHE I  1 51  ? 154.769 150.353 52.546 1.00   24.17 ? 50   PHE I N   1 
ATOM   9287  C  CA  . PHE I  1 51  ? 156.144 150.733 52.879 1.00   24.16 ? 50   PHE I CA  1 
ATOM   9288  C  C   . PHE I  1 51  ? 156.966 149.623 53.522 1.00   23.30 ? 50   PHE I C   1 
ATOM   9289  O  O   . PHE I  1 51  ? 156.488 148.899 54.364 1.00   23.38 ? 50   PHE I O   1 
ATOM   9290  C  CB  . PHE I  1 51  ? 156.102 151.969 53.766 1.00   25.09 ? 50   PHE I CB  1 
ATOM   9291  C  CG  . PHE I  1 51  ? 155.292 153.081 53.170 1.00   25.82 ? 50   PHE I CG  1 
ATOM   9292  C  CD1 . PHE I  1 51  ? 155.679 153.658 51.975 1.00   26.41 ? 50   PHE I CD1 1 
ATOM   9293  C  CD2 . PHE I  1 51  ? 154.141 153.522 53.780 1.00   26.14 ? 50   PHE I CD2 1 
ATOM   9294  C  CE1 . PHE I  1 51  ? 154.931 154.662 51.394 1.00   27.34 ? 50   PHE I CE1 1 
ATOM   9295  C  CE2 . PHE I  1 51  ? 153.394 154.536 53.212 1.00   27.19 ? 50   PHE I CE2 1 
ATOM   9296  C  CZ  . PHE I  1 51  ? 153.781 155.102 52.014 1.00   27.42 ? 50   PHE I CZ  1 
ATOM   9297  N  N   . GLY I  1 52  ? 158.208 149.484 53.081 1.00   23.32 ? 51   GLY I N   1 
ATOM   9298  C  CA  . GLY I  1 52  ? 159.179 148.599 53.719 1.00   22.87 ? 51   GLY I CA  1 
ATOM   9299  C  C   . GLY I  1 52  ? 159.885 149.356 54.829 1.00   23.10 ? 51   GLY I C   1 
ATOM   9300  O  O   . GLY I  1 52  ? 161.102 149.440 54.865 1.00   23.84 ? 51   GLY I O   1 
ATOM   9301  N  N   . ASP I  1 53  ? 159.089 149.910 55.730 1.00   23.43 ? 52   ASP I N   1 
ATOM   9302  C  CA  . ASP I  1 53  ? 159.551 150.761 56.791 1.00   23.91 ? 52   ASP I CA  1 
ATOM   9303  C  C   . ASP I  1 53  ? 159.162 150.087 58.114 1.00   24.33 ? 52   ASP I C   1 
ATOM   9304  O  O   . ASP I  1 53  ? 157.982 150.034 58.487 1.00   23.32 ? 52   ASP I O   1 
ATOM   9305  C  CB  . ASP I  1 53  ? 158.922 152.141 56.638 1.00   24.21 ? 52   ASP I CB  1 
ATOM   9306  C  CG  . ASP I  1 53  ? 159.406 153.128 57.678 1.00   24.44 ? 52   ASP I CG  1 
ATOM   9307  O  OD1 . ASP I  1 53  ? 159.854 152.712 58.758 1.00   23.94 ? 52   ASP I OD1 1 
ATOM   9308  O  OD2 . ASP I  1 53  ? 159.356 154.338 57.403 1.00   25.67 ? 52   ASP I OD2 1 
ATOM   9309  N  N   . ASN I  1 54  ? 160.168 149.531 58.781 1.00   25.20 ? 53   ASN I N   1 
ATOM   9310  C  CA  . ASN I  1 54  ? 159.982 148.853 60.048 1.00   26.58 ? 53   ASN I CA  1 
ATOM   9311  C  C   . ASN I  1 54  ? 160.555 149.680 61.190 1.00   26.63 ? 53   ASN I C   1 
ATOM   9312  O  O   . ASN I  1 54  ? 160.800 149.149 62.247 1.00   26.51 ? 53   ASN I O   1 
ATOM   9313  C  CB  . ASN I  1 54  ? 160.669 147.492 60.033 1.00   27.60 ? 53   ASN I CB  1 
ATOM   9314  C  CG  . ASN I  1 54  ? 160.291 146.636 61.230 1.00   29.37 ? 53   ASN I CG  1 
ATOM   9315  O  OD1 . ASN I  1 54  ? 159.101 146.537 61.581 1.00   31.37 ? 53   ASN I OD1 1 
ATOM   9316  N  ND2 . ASN I  1 54  ? 161.292 146.009 61.868 1.00   28.33 ? 53   ASN I ND2 1 
ATOM   9317  N  N   . THR I  1 55  ? 160.749 150.978 60.986 1.00   26.44 ? 54   THR I N   1 
ATOM   9318  C  CA  . THR I  1 55  ? 161.301 151.811 62.054 1.00   26.66 ? 54   THR I CA  1 
ATOM   9319  C  C   . THR I  1 55  ? 160.391 151.844 63.265 1.00   27.07 ? 54   THR I C   1 
ATOM   9320  O  O   . THR I  1 55  ? 160.877 151.932 64.359 1.00   28.01 ? 54   THR I O   1 
ATOM   9321  C  CB  . THR I  1 55  ? 161.574 153.253 61.597 1.00   26.22 ? 54   THR I CB  1 
ATOM   9322  O  OG1 . THR I  1 55  ? 160.358 153.855 61.133 1.00   26.27 ? 54   THR I OG1 1 
ATOM   9323  C  CG2 . THR I  1 55  ? 162.596 153.255 60.499 1.00   25.79 ? 54   THR I CG2 1 
ATOM   9324  N  N   . ALA I  1 56  ? 159.078 151.766 63.092 1.00   26.96 ? 55   ALA I N   1 
ATOM   9325  C  CA  . ALA I  1 56  ? 158.194 151.691 64.261 1.00   27.39 ? 55   ALA I CA  1 
ATOM   9326  C  C   . ALA I  1 56  ? 157.514 150.332 64.313 1.00   27.23 ? 55   ALA I C   1 
ATOM   9327  O  O   . ALA I  1 56  ? 156.329 150.252 64.567 1.00   29.94 ? 55   ALA I O   1 
ATOM   9328  C  CB  . ALA I  1 56  ? 157.152 152.815 64.218 1.00   27.30 ? 55   ALA I CB  1 
ATOM   9329  N  N   . GLY I  1 57  ? 158.238 149.258 64.036 1.00   26.60 ? 56   GLY I N   1 
ATOM   9330  C  CA  . GLY I  1 57  ? 157.595 147.945 63.910 1.00   26.10 ? 56   GLY I CA  1 
ATOM   9331  C  C   . GLY I  1 57  ? 156.694 147.864 62.679 1.00   25.64 ? 56   GLY I C   1 
ATOM   9332  O  O   . GLY I  1 57  ? 156.949 148.542 61.669 1.00   26.00 ? 56   GLY I O   1 
ATOM   9333  N  N   . CYS I  1 58  ? 155.641 147.046 62.759 1.00   24.37 ? 57   CYS I N   1 
ATOM   9334  C  CA  . CYS I  1 58  ? 154.736 146.833 61.639 1.00   23.79 ? 57   CYS I CA  1 
ATOM   9335  C  C   . CYS I  1 58  ? 153.836 148.031 61.355 1.00   23.96 ? 57   CYS I C   1 
ATOM   9336  O  O   . CYS I  1 58  ? 153.344 148.172 60.259 1.00   23.68 ? 57   CYS I O   1 
ATOM   9337  C  CB  . CYS I  1 58  ? 153.898 145.588 61.869 1.00   23.30 ? 57   CYS I CB  1 
ATOM   9338  S  SG  . CYS I  1 58  ? 154.884 144.085 62.023 1.00   23.39 ? 57   CYS I SG  1 
ATOM   9339  N  N   . THR I  1 59  ? 153.663 148.923 62.319 1.00   24.95 ? 58   THR I N   1 
ATOM   9340  C  CA  . THR I  1 59  ? 152.806 150.105 62.140 1.00   25.94 ? 58   THR I CA  1 
ATOM   9341  C  C   . THR I  1 59  ? 153.281 151.036 61.039 1.00   25.81 ? 58   THR I C   1 
ATOM   9342  O  O   . THR I  1 59  ? 152.467 151.645 60.342 1.00   25.56 ? 58   THR I O   1 
ATOM   9343  C  CB  . THR I  1 59  ? 152.744 150.928 63.435 1.00   27.89 ? 58   THR I CB  1 
ATOM   9344  O  OG1 . THR I  1 59  ? 152.417 150.054 64.519 1.00   29.72 ? 58   THR I OG1 1 
ATOM   9345  C  CG2 . THR I  1 59  ? 151.679 152.045 63.337 1.00   28.49 ? 58   THR I CG2 1 
ATOM   9346  N  N   . SER I  1 60  ? 154.599 151.145 60.871 1.00   24.99 ? 59   SER I N   1 
ATOM   9347  C  CA  . SER I  1 60  ? 155.151 152.102 59.909 1.00   25.11 ? 59   SER I CA  1 
ATOM   9348  C  C   . SER I  1 60  ? 155.148 151.569 58.483 1.00   24.43 ? 59   SER I C   1 
ATOM   9349  O  O   . SER I  1 60  ? 155.553 152.269 57.557 1.00   24.85 ? 59   SER I O   1 
ATOM   9350  C  CB  . SER I  1 60  ? 156.557 152.563 60.326 1.00   25.13 ? 59   SER I CB  1 
ATOM   9351  O  OG  . SER I  1 60  ? 157.335 151.487 60.796 1.00   25.60 ? 59   SER I OG  1 
ATOM   9352  N  N   . ALA I  1 61  ? 154.671 150.339 58.301 1.00   23.93 ? 60   ALA I N   1 
ATOM   9353  C  CA  . ALA I  1 61  ? 154.514 149.747 56.972 1.00   23.34 ? 60   ALA I CA  1 
ATOM   9354  C  C   . ALA I  1 61  ? 153.389 150.392 56.134 1.00   23.24 ? 60   ALA I C   1 
ATOM   9355  O  O   . ALA I  1 61  ? 153.304 150.176 54.920 1.00   23.39 ? 60   ALA I O   1 
ATOM   9356  C  CB  . ALA I  1 61  ? 154.285 148.250 57.096 1.00   22.84 ? 60   ALA I CB  1 
ATOM   9357  N  N   . GLY I  1 62  ? 152.520 151.159 56.781 1.00   23.31 ? 61   GLY I N   1 
ATOM   9358  C  CA  . GLY I  1 62  ? 151.488 151.914 56.093 1.00   23.48 ? 61   GLY I CA  1 
ATOM   9359  C  C   . GLY I  1 62  ? 150.346 151.033 55.670 1.00   23.56 ? 61   GLY I C   1 
ATOM   9360  O  O   . GLY I  1 62  ? 150.169 149.927 56.220 1.00   23.70 ? 61   GLY I O   1 
ATOM   9361  N  N   . PRO I  1 63  ? 149.542 151.509 54.705 1.00   23.39 ? 62   PRO I N   1 
ATOM   9362  C  CA  . PRO I  1 63  ? 148.365 150.749 54.321 1.00   23.10 ? 62   PRO I CA  1 
ATOM   9363  C  C   . PRO I  1 63  ? 148.651 149.669 53.284 1.00   22.34 ? 62   PRO I C   1 
ATOM   9364  O  O   . PRO I  1 63  ? 149.794 149.467 52.879 1.00   22.24 ? 62   PRO I O   1 
ATOM   9365  C  CB  . PRO I  1 63  ? 147.443 151.835 53.742 1.00   23.75 ? 62   PRO I CB  1 
ATOM   9366  C  CG  . PRO I  1 63  ? 148.407 152.808 53.120 1.00   24.19 ? 62   PRO I CG  1 
ATOM   9367  C  CD  . PRO I  1 63  ? 149.597 152.823 54.033 1.00   23.99 ? 62   PRO I CD  1 
ATOM   9368  N  N   . HIS I  1 64  ? 147.605 148.982 52.857 1.00   22.10 ? 63   HIS I N   1 
ATOM   9369  C  CA  . HIS I  1 64  ? 147.721 147.989 51.802 1.00   22.01 ? 63   HIS I CA  1 
ATOM   9370  C  C   . HIS I  1 64  ? 148.310 148.612 50.559 1.00   22.65 ? 63   HIS I C   1 
ATOM   9371  O  O   . HIS I  1 64  ? 147.964 149.729 50.209 1.00   22.80 ? 63   HIS I O   1 
ATOM   9372  C  CB  . HIS I  1 64  ? 146.362 147.402 51.492 1.00   21.71 ? 63   HIS I CB  1 
ATOM   9373  C  CG  . HIS I  1 64  ? 145.826 146.538 52.576 1.00   21.34 ? 63   HIS I CG  1 
ATOM   9374  N  ND1 . HIS I  1 64  ? 144.766 145.753 52.413 1.00   20.88 ? 63   HIS I ND1 1 
ATOM   9375  C  CD2 . HIS I  1 64  ? 146.277 146.321 53.866 1.00   21.45 ? 63   HIS I CD2 1 
ATOM   9376  C  CE1 . HIS I  1 64  ? 144.533 145.080 53.556 1.00   20.72 ? 63   HIS I CE1 1 
ATOM   9377  N  NE2 . HIS I  1 64  ? 145.445 145.440 54.439 1.00   20.76 ? 63   HIS I NE2 1 
ATOM   9378  N  N   . PHE I  1 65  ? 149.231 147.908 49.904 1.00   23.03 ? 64   PHE I N   1 
ATOM   9379  C  CA  . PHE I  1 65  ? 149.802 148.391 48.646 1.00   23.97 ? 64   PHE I CA  1 
ATOM   9380  C  C   . PHE I  1 65  ? 148.696 148.412 47.575 1.00   24.12 ? 64   PHE I C   1 
ATOM   9381  O  O   . PHE I  1 65  ? 148.109 147.387 47.237 1.00   22.85 ? 64   PHE I O   1 
ATOM   9382  C  CB  . PHE I  1 65  ? 150.961 147.498 48.223 1.00   24.59 ? 64   PHE I CB  1 
ATOM   9383  C  CG  . PHE I  1 65  ? 151.582 147.880 46.919 1.00   25.93 ? 64   PHE I CG  1 
ATOM   9384  C  CD1 . PHE I  1 65  ? 151.967 149.188 46.672 1.00   26.67 ? 64   PHE I CD1 1 
ATOM   9385  C  CD2 . PHE I  1 65  ? 151.808 146.922 45.945 1.00   26.38 ? 64   PHE I CD2 1 
ATOM   9386  C  CE1 . PHE I  1 65  ? 152.546 149.537 45.472 1.00   27.68 ? 64   PHE I CE1 1 
ATOM   9387  C  CE2 . PHE I  1 65  ? 152.393 147.260 44.745 1.00   26.90 ? 64   PHE I CE2 1 
ATOM   9388  C  CZ  . PHE I  1 65  ? 152.759 148.567 44.506 1.00   27.92 ? 64   PHE I CZ  1 
ATOM   9389  N  N   . ASN I  1 66  ? 148.442 149.610 47.060 1.00   24.80 ? 65   ASN I N   1 
ATOM   9390  C  CA  . ASN I  1 66  ? 147.244 149.942 46.303 1.00   25.03 ? 65   ASN I CA  1 
ATOM   9391  C  C   . ASN I  1 66  ? 147.573 150.996 45.235 1.00   25.87 ? 65   ASN I C   1 
ATOM   9392  O  O   . ASN I  1 66  ? 147.008 152.093 45.254 1.00   26.38 ? 65   ASN I O   1 
ATOM   9393  C  CB  . ASN I  1 66  ? 146.201 150.515 47.280 1.00   24.88 ? 65   ASN I CB  1 
ATOM   9394  C  CG  . ASN I  1 66  ? 144.834 150.723 46.644 1.00   25.29 ? 65   ASN I CG  1 
ATOM   9395  O  OD1 . ASN I  1 66  ? 144.523 150.129 45.595 1.00   25.52 ? 65   ASN I OD1 1 
ATOM   9396  N  ND2 . ASN I  1 66  ? 144.001 151.546 47.282 1.00   24.51 ? 65   ASN I ND2 1 
ATOM   9397  N  N   . PRO I  1 67  ? 148.495 150.676 44.310 1.00   26.08 ? 66   PRO I N   1 
ATOM   9398  C  CA  . PRO I  1 67  ? 148.840 151.677 43.294 1.00   27.39 ? 66   PRO I CA  1 
ATOM   9399  C  C   . PRO I  1 67  ? 147.679 151.994 42.334 1.00   28.37 ? 66   PRO I C   1 
ATOM   9400  O  O   . PRO I  1 67  ? 147.656 153.079 41.802 1.00   28.81 ? 66   PRO I O   1 
ATOM   9401  C  CB  . PRO I  1 67  ? 150.015 151.033 42.551 1.00   27.01 ? 66   PRO I CB  1 
ATOM   9402  C  CG  . PRO I  1 67  ? 149.758 149.573 42.689 1.00   26.36 ? 66   PRO I CG  1 
ATOM   9403  C  CD  . PRO I  1 67  ? 149.133 149.379 44.035 1.00   25.73 ? 66   PRO I CD  1 
ATOM   9404  N  N   . LEU I  1 68  ? 146.725 151.073 42.132 1.00   28.89 ? 67   LEU I N   1 
ATOM   9405  C  CA  . LEU I  1 68  ? 145.564 151.340 41.259 1.00   29.71 ? 67   LEU I CA  1 
ATOM   9406  C  C   . LEU I  1 68  ? 144.365 151.978 41.990 1.00   30.08 ? 67   LEU I C   1 
ATOM   9407  O  O   . LEU I  1 68  ? 143.281 152.086 41.422 1.00   30.39 ? 67   LEU I O   1 
ATOM   9408  C  CB  . LEU I  1 68  ? 145.091 150.060 40.565 1.00   29.80 ? 67   LEU I CB  1 
ATOM   9409  C  CG  . LEU I  1 68  ? 146.102 149.287 39.719 1.00   30.31 ? 67   LEU I CG  1 
ATOM   9410  C  CD1 . LEU I  1 68  ? 145.383 148.212 38.925 1.00   30.49 ? 67   LEU I CD1 1 
ATOM   9411  C  CD2 . LEU I  1 68  ? 146.878 150.182 38.764 1.00   31.29 ? 67   LEU I CD2 1 
ATOM   9412  N  N   . SER I  1 69  ? 144.548 152.372 43.248 1.00   30.08 ? 68   SER I N   1 
ATOM   9413  C  CA  . SER I  1 69  ? 143.523 153.085 43.997 1.00   30.49 ? 68   SER I CA  1 
ATOM   9414  C  C   . SER I  1 69  ? 142.162 152.391 44.004 1.00   30.67 ? 68   SER I C   1 
ATOM   9415  O  O   . SER I  1 69  ? 141.135 153.005 43.757 1.00   31.92 ? 68   SER I O   1 
ATOM   9416  C  CB  . SER I  1 69  ? 143.404 154.516 43.476 1.00   31.64 ? 68   SER I CB  1 
ATOM   9417  O  OG  . SER I  1 69  ? 144.598 155.224 43.772 1.00   31.82 ? 68   SER I OG  1 
ATOM   9418  N  N   . ARG I  1 70  ? 142.163 151.102 44.311 1.00   30.55 ? 69   ARG I N   1 
ATOM   9419  C  CA  . ARG I  1 70  ? 140.934 150.337 44.389 1.00   30.65 ? 69   ARG I CA  1 
ATOM   9420  C  C   . ARG I  1 70  ? 140.517 150.090 45.832 1.00   28.93 ? 69   ARG I C   1 
ATOM   9421  O  O   . ARG I  1 70  ? 141.216 150.485 46.769 1.00   27.51 ? 69   ARG I O   1 
ATOM   9422  C  CB  . ARG I  1 70  ? 141.112 149.040 43.607 1.00   32.08 ? 69   ARG I CB  1 
ATOM   9423  C  CG  . ARG I  1 70  ? 141.453 149.343 42.156 1.00   34.90 ? 69   ARG I CG  1 
ATOM   9424  C  CD  . ARG I  1 70  ? 141.190 148.169 41.239 1.00   37.97 ? 69   ARG I CD  1 
ATOM   9425  N  NE  . ARG I  1 70  ? 141.294 148.556 39.837 1.00   41.36 ? 69   ARG I NE  1 
ATOM   9426  C  CZ  . ARG I  1 70  ? 141.474 147.708 38.824 1.00   44.79 ? 69   ARG I CZ  1 
ATOM   9427  N  NH1 . ARG I  1 70  ? 141.600 146.396 39.035 1.00   46.34 ? 69   ARG I NH1 1 
ATOM   9428  N  NH2 . ARG I  1 70  ? 141.553 148.179 37.583 1.00   46.43 ? 69   ARG I NH2 1 
ATOM   9429  N  N   . LYS I  1 71  ? 139.351 149.481 46.001 1.00   27.75 ? 70   LYS I N   1 
ATOM   9430  C  CA  . LYS I  1 71  ? 138.898 149.050 47.311 1.00   27.33 ? 70   LYS I CA  1 
ATOM   9431  C  C   . LYS I  1 71  ? 139.471 147.672 47.652 1.00   25.18 ? 70   LYS I C   1 
ATOM   9432  O  O   . LYS I  1 71  ? 139.867 146.911 46.771 1.00   23.72 ? 70   LYS I O   1 
ATOM   9433  C  CB  . LYS I  1 71  ? 137.375 149.055 47.388 1.00   28.93 ? 70   LYS I CB  1 
ATOM   9434  C  CG  . LYS I  1 71  ? 136.824 150.472 47.226 1.00   31.36 ? 70   LYS I CG  1 
ATOM   9435  C  CD  . LYS I  1 71  ? 135.343 150.567 47.530 1.00   33.67 ? 70   LYS I CD  1 
ATOM   9436  C  CE  . LYS I  1 71  ? 134.910 152.040 47.631 1.00   36.53 ? 70   LYS I CE  1 
ATOM   9437  N  NZ  . LYS I  1 71  ? 135.913 152.962 48.288 1.00   37.34 ? 70   LYS I NZ  1 
ATOM   9438  N  N   . HIS I  1 72  ? 139.488 147.377 48.945 1.00   23.20 ? 71   HIS I N   1 
ATOM   9439  C  CA  . HIS I  1 72  ? 139.975 146.113 49.441 1.00   22.06 ? 71   HIS I CA  1 
ATOM   9440  C  C   . HIS I  1 72  ? 139.082 145.005 48.962 1.00   22.09 ? 71   HIS I C   1 
ATOM   9441  O  O   . HIS I  1 72  ? 137.842 145.145 49.013 1.00   22.41 ? 71   HIS I O   1 
ATOM   9442  C  CB  . HIS I  1 72  ? 140.011 146.125 50.976 1.00   21.23 ? 71   HIS I CB  1 
ATOM   9443  C  CG  . HIS I  1 72  ? 140.553 144.864 51.564 1.00   20.21 ? 71   HIS I CG  1 
ATOM   9444  N  ND1 . HIS I  1 72  ? 141.875 144.589 51.610 1.00   19.23 ? 71   HIS I ND1 1 
ATOM   9445  C  CD2 . HIS I  1 72  ? 139.899 143.766 52.105 1.00   19.50 ? 71   HIS I CD2 1 
ATOM   9446  C  CE1 . HIS I  1 72  ? 142.047 143.369 52.127 1.00   19.05 ? 71   HIS I CE1 1 
ATOM   9447  N  NE2 . HIS I  1 72  ? 140.840 142.873 52.452 1.00   19.09 ? 71   HIS I NE2 1 
ATOM   9448  N  N   . GLY I  1 73  ? 139.688 143.901 48.515 1.00   21.01 ? 72   GLY I N   1 
ATOM   9449  C  CA  . GLY I  1 73  ? 138.951 142.669 48.236 1.00   20.58 ? 72   GLY I CA  1 
ATOM   9450  C  C   . GLY I  1 73  ? 139.728 141.400 48.579 1.00   20.18 ? 72   GLY I C   1 
ATOM   9451  O  O   . GLY I  1 73  ? 140.745 141.452 49.257 1.00   19.89 ? 72   GLY I O   1 
ATOM   9452  N  N   . GLY I  1 74  ? 139.219 140.253 48.136 1.00   19.97 ? 73   GLY I N   1 
ATOM   9453  C  CA  . GLY I  1 74  ? 139.970 139.009 48.141 1.00   20.02 ? 73   GLY I CA  1 
ATOM   9454  C  C   . GLY I  1 74  ? 140.856 138.923 46.908 1.00   20.48 ? 73   GLY I C   1 
ATOM   9455  O  O   . GLY I  1 74  ? 140.647 139.648 45.938 1.00   20.21 ? 73   GLY I O   1 
ATOM   9456  N  N   . PRO I  1 75  ? 141.842 138.019 46.927 1.00   20.93 ? 74   PRO I N   1 
ATOM   9457  C  CA  . PRO I  1 75  ? 142.737 137.844 45.791 1.00   21.59 ? 74   PRO I CA  1 
ATOM   9458  C  C   . PRO I  1 75  ? 142.004 137.410 44.499 1.00   22.44 ? 74   PRO I C   1 
ATOM   9459  O  O   . PRO I  1 75  ? 142.467 137.725 43.405 1.00   23.57 ? 74   PRO I O   1 
ATOM   9460  C  CB  . PRO I  1 75  ? 143.684 136.752 46.267 1.00   21.28 ? 74   PRO I CB  1 
ATOM   9461  C  CG  . PRO I  1 75  ? 142.898 135.997 47.289 1.00   20.91 ? 74   PRO I CG  1 
ATOM   9462  C  CD  . PRO I  1 75  ? 142.129 137.056 48.000 1.00   20.88 ? 74   PRO I CD  1 
ATOM   9463  N  N   . LYS I  1 76  ? 140.882 136.711 44.633 1.00   22.76 ? 75   LYS I N   1 
ATOM   9464  C  CA  . LYS I  1 76  ? 140.077 136.301 43.489 1.00   23.49 ? 75   LYS I CA  1 
ATOM   9465  C  C   . LYS I  1 76  ? 139.317 137.446 42.813 1.00   24.24 ? 75   LYS I C   1 
ATOM   9466  O  O   . LYS I  1 76  ? 138.818 137.248 41.740 1.00   25.03 ? 75   LYS I O   1 
ATOM   9467  C  CB  . LYS I  1 76  ? 139.072 135.204 43.901 1.00   23.43 ? 75   LYS I CB  1 
ATOM   9468  C  CG  . LYS I  1 76  ? 139.718 133.874 44.243 1.00   23.33 ? 75   LYS I CG  1 
ATOM   9469  C  CD  . LYS I  1 76  ? 138.706 132.845 44.757 0.50   23.05 ? 75   LYS I CD  1 
ATOM   9470  C  CE  . LYS I  1 76  ? 138.062 132.072 43.617 0.50   23.22 ? 75   LYS I CE  1 
ATOM   9471  N  NZ  . LYS I  1 76  ? 137.097 131.046 44.096 0.50   23.33 ? 75   LYS I NZ  1 
ATOM   9472  N  N   . ASP I  1 77  ? 139.212 138.620 43.435 1.00   25.23 ? 76   ASP I N   1 
ATOM   9473  C  CA  . ASP I  1 77  ? 138.415 139.728 42.891 1.00   25.92 ? 76   ASP I CA  1 
ATOM   9474  C  C   . ASP I  1 77  ? 139.192 140.645 41.947 1.00   27.20 ? 76   ASP I C   1 
ATOM   9475  O  O   . ASP I  1 77  ? 140.387 140.847 42.104 1.00   25.95 ? 76   ASP I O   1 
ATOM   9476  C  CB  . ASP I  1 77  ? 137.867 140.629 44.016 1.00   26.37 ? 76   ASP I CB  1 
ATOM   9477  C  CG  . ASP I  1 77  ? 136.971 139.885 45.008 1.00   26.26 ? 76   ASP I CG  1 
ATOM   9478  O  OD1 . ASP I  1 77  ? 136.094 139.120 44.566 1.00   27.70 ? 76   ASP I OD1 1 
ATOM   9479  O  OD2 . ASP I  1 77  ? 137.121 140.079 46.230 1.00   25.22 ? 76   ASP I OD2 1 
ATOM   9480  N  N   . GLU I  1 78  ? 138.465 141.243 41.002 1.00   28.90 ? 77   GLU I N   1 
ATOM   9481  C  CA  . GLU I  1 78  ? 138.956 142.342 40.173 1.00   30.59 ? 77   GLU I CA  1 
ATOM   9482  C  C   . GLU I  1 78  ? 139.130 143.617 41.008 1.00   29.07 ? 77   GLU I C   1 
ATOM   9483  O  O   . GLU I  1 78  ? 140.135 144.334 40.896 1.00   29.54 ? 77   GLU I O   1 
ATOM   9484  C  CB  . GLU I  1 78  ? 137.961 142.564 39.002 1.00   34.93 ? 77   GLU I CB  1 
ATOM   9485  C  CG  . GLU I  1 78  ? 137.965 143.951 38.355 1.00   38.80 ? 77   GLU I CG  1 
ATOM   9486  C  CD  . GLU I  1 78  ? 139.329 144.370 37.837 1.00   43.18 ? 77   GLU I CD  1 
ATOM   9487  O  OE1 . GLU I  1 78  ? 140.222 143.492 37.703 1.00   46.81 ? 77   GLU I OE1 1 
ATOM   9488  O  OE2 . GLU I  1 78  ? 139.510 145.588 37.566 1.00   48.67 ? 77   GLU I OE2 1 
ATOM   9489  N  N   . GLU I  1 79  ? 138.147 143.900 41.851 1.00   27.29 ? 78   GLU I N   1 
ATOM   9490  C  CA  . GLU I  1 79  ? 138.241 145.024 42.776 1.00   26.72 ? 78   GLU I CA  1 
ATOM   9491  C  C   . GLU I  1 79  ? 139.002 144.566 44.032 1.00   24.54 ? 78   GLU I C   1 
ATOM   9492  O  O   . GLU I  1 79  ? 138.453 143.947 44.933 1.00   24.06 ? 78   GLU I O   1 
ATOM   9493  C  CB  . GLU I  1 79  ? 136.845 145.552 43.138 1.00   27.32 ? 78   GLU I CB  1 
ATOM   9494  C  CG  . GLU I  1 79  ? 136.848 146.901 43.875 1.00   28.45 ? 78   GLU I CG  1 
ATOM   9495  C  CD  . GLU I  1 79  ? 137.378 148.066 43.031 1.00   29.75 ? 78   GLU I CD  1 
ATOM   9496  O  OE1 . GLU I  1 79  ? 137.454 147.922 41.779 1.00   31.26 ? 78   GLU I OE1 1 
ATOM   9497  O  OE2 . GLU I  1 79  ? 137.701 149.137 43.612 1.00   29.69 ? 78   GLU I OE2 1 
ATOM   9498  N  N   . ARG I  1 80  ? 140.275 144.893 44.074 1.00   23.27 ? 79   ARG I N   1 
ATOM   9499  C  CA  . ARG I  1 80  ? 141.148 144.494 45.164 1.00   22.19 ? 79   ARG I CA  1 
ATOM   9500  C  C   . ARG I  1 80  ? 142.346 145.383 45.124 1.00   21.98 ? 79   ARG I C   1 
ATOM   9501  O  O   . ARG I  1 80  ? 142.653 145.937 44.077 1.00   22.28 ? 79   ARG I O   1 
ATOM   9502  C  CB  . ARG I  1 80  ? 141.598 143.031 45.029 1.00   21.31 ? 79   ARG I CB  1 
ATOM   9503  C  CG  . ARG I  1 80  ? 142.458 142.727 43.807 1.00   21.25 ? 79   ARG I CG  1 
ATOM   9504  C  CD  . ARG I  1 80  ? 143.072 141.329 43.869 1.00   20.55 ? 79   ARG I CD  1 
ATOM   9505  N  NE  . ARG I  1 80  ? 144.448 141.395 44.367 1.00   20.10 ? 79   ARG I NE  1 
ATOM   9506  C  CZ  . ARG I  1 80  ? 145.333 140.415 44.283 1.00   19.53 ? 79   ARG I CZ  1 
ATOM   9507  N  NH1 . ARG I  1 80  ? 144.995 139.259 43.742 1.00   19.66 ? 79   ARG I NH1 1 
ATOM   9508  N  NH2 . ARG I  1 80  ? 146.554 140.582 44.782 1.00   19.43 ? 79   ARG I NH2 1 
ATOM   9509  N  N   . HIS I  1 81  ? 143.036 145.497 46.261 1.00   21.40 ? 80   HIS I N   1 
ATOM   9510  C  CA  . HIS I  1 81  ? 144.345 146.128 46.295 1.00   20.94 ? 80   HIS I CA  1 
ATOM   9511  C  C   . HIS I  1 81  ? 145.331 145.155 45.750 1.00   20.54 ? 80   HIS I C   1 
ATOM   9512  O  O   . HIS I  1 81  ? 145.142 143.942 45.899 1.00   19.91 ? 80   HIS I O   1 
ATOM   9513  C  CB  . HIS I  1 81  ? 144.771 146.442 47.722 1.00   20.97 ? 80   HIS I CB  1 
ATOM   9514  C  CG  . HIS I  1 81  ? 143.800 147.288 48.503 1.00   21.12 ? 80   HIS I CG  1 
ATOM   9515  N  ND1 . HIS I  1 81  ? 143.613 147.132 49.843 1.00   20.50 ? 80   HIS I ND1 1 
ATOM   9516  C  CD2 . HIS I  1 81  ? 143.026 148.377 48.111 1.00   21.33 ? 80   HIS I CD2 1 
ATOM   9517  C  CE1 . HIS I  1 81  ? 142.726 148.049 50.264 1.00   21.09 ? 80   HIS I CE1 1 
ATOM   9518  N  NE2 . HIS I  1 81  ? 142.380 148.827 49.202 1.00   21.58 ? 80   HIS I NE2 1 
ATOM   9519  N  N   . VAL I  1 82  ? 146.417 145.660 45.153 1.00   20.68 ? 81   VAL I N   1 
ATOM   9520  C  CA  . VAL I  1 82  ? 147.479 144.790 44.665 1.00   20.42 ? 81   VAL I CA  1 
ATOM   9521  C  C   . VAL I  1 82  ? 148.000 143.915 45.797 1.00   19.71 ? 81   VAL I C   1 
ATOM   9522  O  O   . VAL I  1 82  ? 148.208 142.716 45.622 1.00   19.70 ? 81   VAL I O   1 
ATOM   9523  C  CB  . VAL I  1 82  ? 148.650 145.578 44.045 1.00   21.35 ? 81   VAL I CB  1 
ATOM   9524  C  CG1 . VAL I  1 82  ? 149.879 144.675 43.878 1.00   21.34 ? 81   VAL I CG1 1 
ATOM   9525  C  CG2 . VAL I  1 82  ? 148.232 146.174 42.700 1.00   22.03 ? 81   VAL I CG2 1 
ATOM   9526  N  N   . GLY I  1 83  ? 148.173 144.498 46.971 1.00   19.25 ? 82   GLY I N   1 
ATOM   9527  C  CA  . GLY I  1 83  ? 148.635 143.737 48.135 1.00   18.66 ? 82   GLY I CA  1 
ATOM   9528  C  C   . GLY I  1 83  ? 147.673 142.721 48.737 1.00   18.00 ? 82   GLY I C   1 
ATOM   9529  O  O   . GLY I  1 83  ? 148.026 142.072 49.695 1.00   17.60 ? 82   GLY I O   1 
ATOM   9530  N  N   . ASP I  1 84  ? 146.473 142.552 48.182 1.00   17.87 ? 83   ASP I N   1 
ATOM   9531  C  CA  . ASP I  1 84  ? 145.451 141.718 48.825 1.00   17.70 ? 83   ASP I CA  1 
ATOM   9532  C  C   . ASP I  1 84  ? 145.572 140.231 48.525 1.00   17.58 ? 83   ASP I C   1 
ATOM   9533  O  O   . ASP I  1 84  ? 144.962 139.707 47.573 1.00   17.80 ? 83   ASP I O   1 
ATOM   9534  C  CB  . ASP I  1 84  ? 144.023 142.183 48.457 1.00   17.88 ? 83   ASP I CB  1 
ATOM   9535  C  CG  . ASP I  1 84  ? 143.650 143.510 49.091 1.00   17.98 ? 83   ASP I CG  1 
ATOM   9536  O  OD1 . ASP I  1 84  ? 144.357 143.979 50.016 1.00   17.13 ? 83   ASP I OD1 1 
ATOM   9537  O  OD2 . ASP I  1 84  ? 142.623 144.082 48.653 1.00   18.30 ? 83   ASP I OD2 1 
ATOM   9538  N  N   . LEU I  1 85  ? 146.296 139.534 49.387 1.00   17.23 ? 84   LEU I N   1 
ATOM   9539  C  CA  . LEU I  1 85  ? 146.542 138.123 49.210 1.00   16.82 ? 84   LEU I CA  1 
ATOM   9540  C  C   . LEU I  1 85  ? 145.618 137.240 49.988 1.00   16.73 ? 84   LEU I C   1 
ATOM   9541  O  O   . LEU I  1 85  ? 145.815 136.031 50.018 1.00   17.77 ? 84   LEU I O   1 
ATOM   9542  C  CB  . LEU I  1 85  ? 147.982 137.811 49.603 1.00   16.79 ? 84   LEU I CB  1 
ATOM   9543  C  CG  . LEU I  1 85  ? 149.008 138.510 48.701 1.00   16.90 ? 84   LEU I CG  1 
ATOM   9544  C  CD1 . LEU I  1 85  ? 150.428 138.134 49.121 1.00   16.74 ? 84   LEU I CD1 1 
ATOM   9545  C  CD2 . LEU I  1 85  ? 148.746 138.164 47.229 1.00   16.91 ? 84   LEU I CD2 1 
ATOM   9546  N  N   . GLY I  1 86  ? 144.611 137.798 50.641 1.00   16.57 ? 85   GLY I N   1 
ATOM   9547  C  CA  . GLY I  1 86  ? 143.587 136.965 51.259 1.00   16.32 ? 85   GLY I CA  1 
ATOM   9548  C  C   . GLY I  1 86  ? 143.937 136.497 52.652 1.00   16.09 ? 85   GLY I C   1 
ATOM   9549  O  O   . GLY I  1 86  ? 144.479 137.252 53.476 1.00   16.20 ? 85   GLY I O   1 
ATOM   9550  N  N   . ASN I  1 87  ? 143.618 135.247 52.934 1.00   15.62 ? 86   ASN I N   1 
ATOM   9551  C  CA  . ASN I  1 87  ? 143.896 134.662 54.241 1.00   15.40 ? 86   ASN I CA  1 
ATOM   9552  C  C   . ASN I  1 87  ? 144.932 133.551 54.133 1.00   15.48 ? 86   ASN I C   1 
ATOM   9553  O  O   . ASN I  1 87  ? 145.033 132.896 53.091 1.00   15.87 ? 86   ASN I O   1 
ATOM   9554  C  CB  . ASN I  1 87  ? 142.614 134.073 54.836 1.00   15.22 ? 86   ASN I CB  1 
ATOM   9555  C  CG  . ASN I  1 87  ? 141.663 135.128 55.354 1.00   15.29 ? 86   ASN I CG  1 
ATOM   9556  O  OD1 . ASN I  1 87  ? 142.018 135.923 56.250 1.00   15.25 ? 86   ASN I OD1 1 
ATOM   9557  N  ND2 . ASN I  1 87  ? 140.432 135.108 54.856 1.00   15.06 ? 86   ASN I ND2 1 
ATOM   9558  N  N   . VAL I  1 88  ? 145.643 133.302 55.233 1.00   15.56 ? 87   VAL I N   1 
ATOM   9559  C  CA  . VAL I  1 88  ? 146.363 132.047 55.439 1.00   15.60 ? 87   VAL I CA  1 
ATOM   9560  C  C   . VAL I  1 88  ? 145.762 131.334 56.642 1.00   16.07 ? 87   VAL I C   1 
ATOM   9561  O  O   . VAL I  1 88  ? 145.142 131.983 57.486 1.00   16.65 ? 87   VAL I O   1 
ATOM   9562  C  CB  . VAL I  1 88  ? 147.868 132.270 55.639 1.00   15.47 ? 87   VAL I CB  1 
ATOM   9563  C  CG1 . VAL I  1 88  ? 148.489 132.796 54.359 1.00   15.32 ? 87   VAL I CG1 1 
ATOM   9564  C  CG2 . VAL I  1 88  ? 148.141 133.210 56.800 1.00   15.34 ? 87   VAL I CG2 1 
ATOM   9565  N  N   . THR I  1 89  ? 145.949 130.018 56.737 1.00   16.29 ? 88   THR I N   1 
ATOM   9566  C  CA  . THR I  1 89  ? 145.287 129.188 57.754 1.00   16.73 ? 88   THR I CA  1 
ATOM   9567  C  C   . THR I  1 89  ? 146.309 128.475 58.626 1.00   17.11 ? 88   THR I C   1 
ATOM   9568  O  O   . THR I  1 89  ? 147.160 127.731 58.122 1.00   17.31 ? 88   THR I O   1 
ATOM   9569  C  CB  . THR I  1 89  ? 144.347 128.135 57.125 1.00   16.92 ? 88   THR I CB  1 
ATOM   9570  O  OG1 . THR I  1 89  ? 143.345 128.785 56.329 1.00   16.73 ? 88   THR I OG1 1 
ATOM   9571  C  CG2 . THR I  1 89  ? 143.637 127.262 58.207 1.00   17.04 ? 88   THR I CG2 1 
ATOM   9572  N  N   . ALA I  1 90  ? 146.233 128.727 59.930 1.00   17.34 ? 89   ALA I N   1 
ATOM   9573  C  CA  . ALA I  1 90  ? 147.076 128.059 60.900 1.00   17.87 ? 89   ALA I CA  1 
ATOM   9574  C  C   . ALA I  1 90  ? 146.355 126.800 61.362 1.00   18.65 ? 89   ALA I C   1 
ATOM   9575  O  O   . ALA I  1 90  ? 145.156 126.822 61.593 1.00   18.64 ? 89   ALA I O   1 
ATOM   9576  C  CB  . ALA I  1 90  ? 147.362 128.978 62.074 1.00   17.73 ? 89   ALA I CB  1 
ATOM   9577  N  N   . ASP I  1 91  ? 147.083 125.699 61.483 1.00   19.78 ? 90   ASP I N   1 
ATOM   9578  C  CA  . ASP I  1 91  ? 146.515 124.439 61.989 1.00   20.91 ? 90   ASP I CA  1 
ATOM   9579  C  C   . ASP I  1 91  ? 146.439 124.470 63.528 1.00   21.78 ? 90   ASP I C   1 
ATOM   9580  O  O   . ASP I  1 91  ? 146.728 125.509 64.147 1.00   21.37 ? 90   ASP I O   1 
ATOM   9581  C  CB  . ASP I  1 91  ? 147.344 123.249 61.484 1.00   21.48 ? 90   ASP I CB  1 
ATOM   9582  C  CG  . ASP I  1 91  ? 148.756 123.256 62.006 1.00   21.68 ? 90   ASP I CG  1 
ATOM   9583  O  OD1 . ASP I  1 91  ? 149.028 123.969 62.982 1.00   21.59 ? 90   ASP I OD1 1 
ATOM   9584  O  OD2 . ASP I  1 91  ? 149.603 122.573 61.416 1.00   21.98 ? 90   ASP I OD2 1 
ATOM   9585  N  N   . LYS I  1 92  ? 146.055 123.348 64.144 1.00   23.30 ? 91   LYS I N   1 
ATOM   9586  C  CA  . LYS I  1 92  ? 145.911 123.282 65.614 1.00   24.52 ? 91   LYS I CA  1 
ATOM   9587  C  C   . LYS I  1 92  ? 147.206 123.471 66.412 1.00   24.05 ? 91   LYS I C   1 
ATOM   9588  O  O   . LYS I  1 92  ? 147.168 123.731 67.623 1.00   24.22 ? 91   LYS I O   1 
ATOM   9589  C  CB  . LYS I  1 92  ? 145.169 122.000 66.051 1.00   26.64 ? 91   LYS I CB  1 
ATOM   9590  C  CG  . LYS I  1 92  ? 145.897 120.668 65.881 1.00   28.71 ? 91   LYS I CG  1 
ATOM   9591  C  CD  . LYS I  1 92  ? 145.011 119.508 66.395 1.00   30.60 ? 91   LYS I CD  1 
ATOM   9592  C  CE  . LYS I  1 92  ? 145.837 118.283 66.798 1.00   33.13 ? 91   LYS I CE  1 
ATOM   9593  N  NZ  . LYS I  1 92  ? 145.090 117.185 67.530 1.00   34.79 ? 91   LYS I NZ  1 
ATOM   9594  N  N   . ASP I  1 93  ? 148.350 123.367 65.753 1.00   23.31 ? 92   ASP I N   1 
ATOM   9595  C  CA  . ASP I  1 93  ? 149.615 123.629 66.419 1.00   23.26 ? 92   ASP I CA  1 
ATOM   9596  C  C   . ASP I  1 93  ? 150.097 125.041 66.161 1.00   21.74 ? 92   ASP I C   1 
ATOM   9597  O  O   . ASP I  1 93  ? 151.200 125.379 66.548 1.00   21.28 ? 92   ASP I O   1 
ATOM   9598  C  CB  . ASP I  1 93  ? 150.645 122.619 65.949 1.00   24.25 ? 92   ASP I CB  1 
ATOM   9599  C  CG  . ASP I  1 93  ? 150.287 121.191 66.373 1.00   25.90 ? 92   ASP I CG  1 
ATOM   9600  O  OD1 . ASP I  1 93  ? 149.597 120.990 67.399 1.00   26.58 ? 92   ASP I OD1 1 
ATOM   9601  O  OD2 . ASP I  1 93  ? 150.712 120.263 65.676 1.00   27.43 ? 92   ASP I OD2 1 
ATOM   9602  N  N   . GLY I  1 94  ? 149.274 125.852 65.494 1.00   20.44 ? 93   GLY I N   1 
ATOM   9603  C  CA  . GLY I  1 94  ? 149.598 127.252 65.245 1.00   19.73 ? 93   GLY I CA  1 
ATOM   9604  C  C   . GLY I  1 94  ? 150.509 127.526 64.051 1.00   19.15 ? 93   GLY I C   1 
ATOM   9605  O  O   . GLY I  1 94  ? 151.081 128.634 63.929 1.00   18.29 ? 93   GLY I O   1 
ATOM   9606  N  N   . VAL I  1 95  ? 150.627 126.520 63.177 1.00   19.07 ? 94   VAL I N   1 
ATOM   9607  C  CA  . VAL I  1 95  ? 151.460 126.589 61.983 1.00   18.89 ? 94   VAL I CA  1 
ATOM   9608  C  C   . VAL I  1 95  ? 150.615 126.813 60.708 1.00   18.47 ? 94   VAL I C   1 
ATOM   9609  O  O   . VAL I  1 95  ? 149.663 126.079 60.434 1.00   18.40 ? 94   VAL I O   1 
ATOM   9610  C  CB  . VAL I  1 95  ? 152.349 125.308 61.835 1.00   19.66 ? 94   VAL I CB  1 
ATOM   9611  C  CG1 . VAL I  1 95  ? 153.210 125.380 60.570 1.00   19.50 ? 94   VAL I CG1 1 
ATOM   9612  C  CG2 . VAL I  1 95  ? 153.249 125.102 63.064 1.00   19.72 ? 94   VAL I CG2 1 
ATOM   9613  N  N   . ALA I  1 96  ? 150.992 127.832 59.929 1.00   18.24 ? 95   ALA I N   1 
ATOM   9614  C  CA  . ALA I  1 96  ? 150.417 128.103 58.626 1.00   18.05 ? 95   ALA I CA  1 
ATOM   9615  C  C   . ALA I  1 96  ? 151.427 127.696 57.570 1.00   18.51 ? 95   ALA I C   1 
ATOM   9616  O  O   . ALA I  1 96  ? 152.440 128.380 57.375 1.00   18.36 ? 95   ALA I O   1 
ATOM   9617  C  CB  . ALA I  1 96  ? 150.066 129.578 58.482 1.00   17.37 ? 95   ALA I CB  1 
ATOM   9618  N  N   . ASP I  1 97  ? 151.172 126.576 56.897 1.00   19.13 ? 96   ASP I N   1 
ATOM   9619  C  CA  . ASP I  1 97  ? 151.998 126.187 55.756 1.00   19.84 ? 96   ASP I CA  1 
ATOM   9620  C  C   . ASP I  1 97  ? 151.411 126.881 54.540 1.00   19.19 ? 96   ASP I C   1 
ATOM   9621  O  O   . ASP I  1 97  ? 150.540 126.354 53.839 1.00   19.20 ? 96   ASP I O   1 
ATOM   9622  C  CB  . ASP I  1 97  ? 152.045 124.670 55.606 1.00   21.06 ? 96   ASP I CB  1 
ATOM   9623  C  CG  . ASP I  1 97  ? 152.816 124.015 56.749 1.00   22.06 ? 96   ASP I CG  1 
ATOM   9624  O  OD1 . ASP I  1 97  ? 153.951 124.456 57.009 1.00   23.35 ? 96   ASP I OD1 1 
ATOM   9625  O  OD2 . ASP I  1 97  ? 152.282 123.115 57.416 1.00   23.17 ? 96   ASP I OD2 1 
ATOM   9626  N  N   . VAL I  1 98  ? 151.880 128.096 54.319 1.00   18.74 ? 97   VAL I N   1 
ATOM   9627  C  CA  . VAL I  1 98  ? 151.318 128.952 53.290 1.00   18.50 ? 97   VAL I CA  1 
ATOM   9628  C  C   . VAL I  1 98  ? 151.546 128.381 51.887 1.00   19.30 ? 97   VAL I C   1 
ATOM   9629  O  O   . VAL I  1 98  ? 152.631 127.881 51.556 1.00   19.51 ? 97   VAL I O   1 
ATOM   9630  C  CB  . VAL I  1 98  ? 151.922 130.361 53.394 1.00   17.91 ? 97   VAL I CB  1 
ATOM   9631  C  CG1 . VAL I  1 98  ? 151.464 131.216 52.218 1.00   17.15 ? 97   VAL I CG1 1 
ATOM   9632  C  CG2 . VAL I  1 98  ? 151.554 130.979 54.761 1.00   17.52 ? 97   VAL I CG2 1 
ATOM   9633  N  N   . SER I  1 99  ? 150.516 128.452 51.056 1.00   20.37 ? 98   SER I N   1 
ATOM   9634  C  CA  . SER I  1 99  ? 150.669 128.071 49.657 1.00   21.48 ? 98   SER I CA  1 
ATOM   9635  C  C   . SER I  1 99  ? 149.629 128.818 48.860 1.00   21.48 ? 98   SER I C   1 
ATOM   9636  O  O   . SER I  1 99  ? 148.434 128.544 48.977 1.00   21.77 ? 98   SER I O   1 
ATOM   9637  C  CB  . SER I  1 99  ? 150.503 126.570 49.480 1.00   22.57 ? 98   SER I CB  1 
ATOM   9638  O  OG  . SER I  1 99  ? 150.649 126.235 48.110 1.00   23.60 ? 98   SER I OG  1 
ATOM   9639  N  N   . ILE I  1 100 ? 150.102 129.792 48.089 1.00   21.06 ? 99   ILE I N   1 
ATOM   9640  C  CA  . ILE I  1 100 ? 149.263 130.745 47.405 1.00   21.24 ? 99   ILE I CA  1 
ATOM   9641  C  C   . ILE I  1 100 ? 149.919 130.990 46.075 1.00   21.81 ? 99   ILE I C   1 
ATOM   9642  O  O   . ILE I  1 100 ? 151.148 130.990 45.985 1.00   22.03 ? 99   ILE I O   1 
ATOM   9643  C  CB  . ILE I  1 100 ? 149.196 132.080 48.196 1.00   20.95 ? 99   ILE I CB  1 
ATOM   9644  C  CG1 . ILE I  1 100 ? 148.279 131.931 49.413 1.00   20.66 ? 99   ILE I CG1 1 
ATOM   9645  C  CG2 . ILE I  1 100 ? 148.721 133.247 47.338 1.00   20.60 ? 99   ILE I CG2 1 
ATOM   9646  C  CD1 . ILE I  1 100 ? 148.218 133.187 50.252 1.00   20.00 ? 99   ILE I CD1 1 
ATOM   9647  N  N   . GLU I  1 101 ? 149.098 131.182 45.051 1.00   22.13 ? 100  GLU I N   1 
ATOM   9648  C  CA  . GLU I  1 101 ? 149.559 131.633 43.754 1.00   22.68 ? 100  GLU I CA  1 
ATOM   9649  C  C   . GLU I  1 101 ? 148.732 132.851 43.370 1.00   22.82 ? 100  GLU I C   1 
ATOM   9650  O  O   . GLU I  1 101 ? 147.521 132.841 43.516 1.00   22.06 ? 100  GLU I O   1 
ATOM   9651  C  CB  . GLU I  1 101 ? 149.378 130.515 42.732 1.00   23.53 ? 100  GLU I CB  1 
ATOM   9652  C  CG  . GLU I  1 101 ? 150.064 130.784 41.409 1.00   24.40 ? 100  GLU I CG  1 
ATOM   9653  C  CD  . GLU I  1 101 ? 149.930 129.624 40.454 0.50   24.65 ? 100  GLU I CD  1 
ATOM   9654  O  OE1 . GLU I  1 101 ? 150.603 128.600 40.700 0.50   25.13 ? 100  GLU I OE1 1 
ATOM   9655  O  OE2 . GLU I  1 101 ? 149.142 129.738 39.491 0.50   24.50 ? 100  GLU I OE2 1 
ATOM   9656  N  N   . ASP I  1 102 ? 149.377 133.903 42.887 1.00   23.08 ? 101  ASP I N   1 
ATOM   9657  C  CA  . ASP I  1 102 ? 148.684 135.157 42.650 1.00   23.54 ? 101  ASP I CA  1 
ATOM   9658  C  C   . ASP I  1 102 ? 149.195 135.869 41.419 1.00   24.71 ? 101  ASP I C   1 
ATOM   9659  O  O   . ASP I  1 102 ? 150.402 136.073 41.274 1.00   26.20 ? 101  ASP I O   1 
ATOM   9660  C  CB  . ASP I  1 102 ? 148.859 136.082 43.847 1.00   23.29 ? 101  ASP I CB  1 
ATOM   9661  C  CG  . ASP I  1 102 ? 147.918 137.266 43.798 1.00   23.25 ? 101  ASP I CG  1 
ATOM   9662  O  OD1 . ASP I  1 102 ? 146.752 137.091 44.207 1.00   24.44 ? 101  ASP I OD1 1 
ATOM   9663  O  OD2 . ASP I  1 102 ? 148.335 138.363 43.365 1.00   22.80 ? 101  ASP I OD2 1 
ATOM   9664  N  N   . SER I  1 103 ? 148.264 136.306 40.574 1.00   25.67 ? 102  SER I N   1 
ATOM   9665  C  CA  . SER I  1 103 ? 148.575 136.871 39.273 1.00   27.38 ? 102  SER I CA  1 
ATOM   9666  C  C   . SER I  1 103 ? 148.605 138.399 39.240 1.00   27.08 ? 102  SER I C   1 
ATOM   9667  O  O   . SER I  1 103 ? 148.883 138.974 38.199 1.00   28.48 ? 102  SER I O   1 
ATOM   9668  C  CB  . SER I  1 103 ? 147.540 136.380 38.262 1.00   29.40 ? 102  SER I CB  1 
ATOM   9669  O  OG  . SER I  1 103 ? 146.225 136.656 38.758 1.00   31.95 ? 102  SER I OG  1 
ATOM   9670  N  N   . VAL I  1 104 ? 148.357 139.050 40.372 1.00   25.93 ? 103  VAL I N   1 
ATOM   9671  C  CA  . VAL I  1 104 ? 148.241 140.511 40.445 1.00   25.03 ? 103  VAL I CA  1 
ATOM   9672  C  C   . VAL I  1 104 ? 149.514 141.131 41.018 1.00   25.38 ? 103  VAL I C   1 
ATOM   9673  O  O   . VAL I  1 104 ? 149.951 142.178 40.553 1.00   25.96 ? 103  VAL I O   1 
ATOM   9674  C  CB  . VAL I  1 104 ? 147.018 140.917 41.307 1.00   23.91 ? 103  VAL I CB  1 
ATOM   9675  C  CG1 . VAL I  1 104 ? 146.989 142.411 41.590 1.00   23.54 ? 103  VAL I CG1 1 
ATOM   9676  C  CG2 . VAL I  1 104 ? 145.728 140.470 40.635 1.00   23.94 ? 103  VAL I CG2 1 
ATOM   9677  N  N   . ILE I  1 105 ? 150.089 140.521 42.054 1.00   24.61 ? 104  ILE I N   1 
ATOM   9678  C  CA  . ILE I  1 105 ? 151.397 140.968 42.546 1.00   24.59 ? 104  ILE I CA  1 
ATOM   9679  C  C   . ILE I  1 105 ? 152.475 140.620 41.524 1.00   25.90 ? 104  ILE I C   1 
ATOM   9680  O  O   . ILE I  1 105 ? 152.292 139.705 40.709 1.00   26.16 ? 104  ILE I O   1 
ATOM   9681  C  CB  . ILE I  1 105 ? 151.782 140.387 43.939 1.00   23.41 ? 104  ILE I CB  1 
ATOM   9682  C  CG1 . ILE I  1 105 ? 151.828 138.844 43.956 1.00   22.84 ? 104  ILE I CG1 1 
ATOM   9683  C  CG2 . ILE I  1 105 ? 150.859 140.940 45.011 1.00   22.83 ? 104  ILE I CG2 1 
ATOM   9684  C  CD1 . ILE I  1 105 ? 152.424 138.234 45.209 1.00   22.58 ? 104  ILE I CD1 1 
ATOM   9685  N  N   . SER I  1 106 ? 153.583 141.357 41.564 1.00   26.69 ? 105  SER I N   1 
ATOM   9686  C  CA  . SER I  1 106 ? 154.732 141.087 40.704 1.00   28.39 ? 105  SER I CA  1 
ATOM   9687  C  C   . SER I  1 106 ? 156.050 141.332 41.422 1.00   28.92 ? 105  SER I C   1 
ATOM   9688  O  O   . SER I  1 106 ? 156.115 142.107 42.377 1.00   28.67 ? 105  SER I O   1 
ATOM   9689  C  CB  . SER I  1 106 ? 154.681 141.979 39.462 1.00   29.99 ? 105  SER I CB  1 
ATOM   9690  O  OG  . SER I  1 106 ? 155.655 141.547 38.534 1.00   32.02 ? 105  SER I OG  1 
ATOM   9691  N  N   . LEU I  1 107 ? 157.106 140.680 40.952 1.00   29.57 ? 106  LEU I N   1 
ATOM   9692  C  CA  . LEU I  1 107 ? 158.433 140.883 41.519 1.00   29.90 ? 106  LEU I CA  1 
ATOM   9693  C  C   . LEU I  1 107 ? 159.263 141.832 40.646 1.00   32.43 ? 106  LEU I C   1 
ATOM   9694  O  O   . LEU I  1 107 ? 160.465 141.980 40.872 1.00   32.38 ? 106  LEU I O   1 
ATOM   9695  C  CB  . LEU I  1 107 ? 159.154 139.549 41.731 1.00   29.26 ? 106  LEU I CB  1 
ATOM   9696  C  CG  . LEU I  1 107 ? 158.407 138.525 42.621 1.00   28.38 ? 106  LEU I CG  1 
ATOM   9697  C  CD1 . LEU I  1 107 ? 159.253 137.269 42.813 1.00   27.31 ? 106  LEU I CD1 1 
ATOM   9698  C  CD2 . LEU I  1 107 ? 157.993 139.096 43.967 1.00   27.26 ? 106  LEU I CD2 1 
ATOM   9699  N  N   . SER I  1 108 ? 158.621 142.484 39.666 1.00   33.86 ? 107  SER I N   1 
ATOM   9700  C  CA  . SER I  1 108 ? 159.248 143.593 38.934 1.00   35.42 ? 107  SER I CA  1 
ATOM   9701  C  C   . SER I  1 108 ? 158.189 144.535 38.324 1.00   37.06 ? 107  SER I C   1 
ATOM   9702  O  O   . SER I  1 108 ? 157.011 144.180 38.250 1.00   35.76 ? 107  SER I O   1 
ATOM   9703  C  CB  . SER I  1 108 ? 160.174 143.055 37.836 1.00   36.03 ? 107  SER I CB  1 
ATOM   9704  O  OG  . SER I  1 108 ? 159.422 142.643 36.700 1.00   36.69 ? 107  SER I OG  1 
ATOM   9705  N  N   . GLY I  1 109 ? 158.624 145.721 37.890 1.00   39.22 ? 108  GLY I N   1 
ATOM   9706  C  CA  . GLY I  1 109 ? 157.721 146.765 37.380 1.00   42.90 ? 108  GLY I CA  1 
ATOM   9707  C  C   . GLY I  1 109 ? 157.164 147.712 38.443 1.00   45.54 ? 108  GLY I C   1 
ATOM   9708  O  O   . GLY I  1 109 ? 157.563 147.660 39.591 1.00   45.11 ? 108  GLY I O   1 
ATOM   9709  N  N   . ASP I  1 110 ? 156.243 148.592 38.057 1.00   49.92 ? 109  ASP I N   1 
ATOM   9710  C  CA  . ASP I  1 110 ? 155.565 149.494 39.022 1.00   51.18 ? 109  ASP I CA  1 
ATOM   9711  C  C   . ASP I  1 110 ? 154.669 148.799 40.073 1.00   50.58 ? 109  ASP I C   1 
ATOM   9712  O  O   . ASP I  1 110 ? 154.419 149.376 41.125 1.00   52.28 ? 109  ASP I O   1 
ATOM   9713  C  CB  . ASP I  1 110 ? 154.730 150.557 38.285 0.50   51.33 ? 109  ASP I CB  1 
ATOM   9714  C  CG  . ASP I  1 110 ? 155.579 151.550 37.511 0.50   50.72 ? 109  ASP I CG  1 
ATOM   9715  O  OD1 . ASP I  1 110 ? 156.784 151.683 37.792 0.50   51.11 ? 109  ASP I OD1 1 
ATOM   9716  O  OD2 . ASP I  1 110 ? 155.028 152.210 36.614 0.50   52.01 ? 109  ASP I OD2 1 
ATOM   9717  N  N   . HIS I  1 111 ? 154.188 147.580 39.806 1.00   49.66 ? 110  HIS I N   1 
ATOM   9718  C  CA  . HIS I  1 111 ? 153.389 146.824 40.802 1.00   47.09 ? 110  HIS I CA  1 
ATOM   9719  C  C   . HIS I  1 111 ? 154.279 145.899 41.596 1.00   45.00 ? 110  HIS I C   1 
ATOM   9720  O  O   . HIS I  1 111 ? 153.809 144.877 42.170 1.00   43.06 ? 110  HIS I O   1 
ATOM   9721  C  CB  . HIS I  1 111 ? 152.265 146.009 40.144 1.00   48.19 ? 110  HIS I CB  1 
ATOM   9722  C  CG  . HIS I  1 111 ? 151.194 146.850 39.483 1.00   50.75 ? 110  HIS I CG  1 
ATOM   9723  N  ND1 . HIS I  1 111 ? 150.014 146.328 39.069 1.00   48.77 ? 110  HIS I ND1 1 
ATOM   9724  C  CD2 . HIS I  1 111 ? 151.154 148.220 39.171 1.00   50.87 ? 110  HIS I CD2 1 
ATOM   9725  C  CE1 . HIS I  1 111 ? 149.266 147.301 38.510 1.00   51.58 ? 110  HIS I CE1 1 
ATOM   9726  N  NE2 . HIS I  1 111 ? 149.967 148.460 38.571 1.00   52.48 ? 110  HIS I NE2 1 
ATOM   9727  N  N   . CYS I  1 112 ? 155.567 146.251 41.644 1.00   41.17 ? 111  CYS I N   1 
ATOM   9728  C  CA  . CYS I  1 112 ? 156.582 145.424 42.261 1.00   38.16 ? 111  CYS I CA  1 
ATOM   9729  C  C   . CYS I  1 112 ? 156.412 145.491 43.765 1.00   33.28 ? 111  CYS I C   1 
ATOM   9730  O  O   . CYS I  1 112 ? 156.158 146.559 44.303 1.00   32.07 ? 111  CYS I O   1 
ATOM   9731  C  CB  . CYS I  1 112 ? 157.980 145.913 41.881 1.00   40.59 ? 111  CYS I CB  1 
ATOM   9732  S  SG  . CYS I  1 112 ? 159.277 144.906 42.603 1.00   47.96 ? 111  CYS I SG  1 
ATOM   9733  N  N   . ILE I  1 113 ? 156.551 144.349 44.432 1.00   29.57 ? 112  ILE I N   1 
ATOM   9734  C  CA  . ILE I  1 113 ? 156.363 144.278 45.882 1.00   27.61 ? 112  ILE I CA  1 
ATOM   9735  C  C   . ILE I  1 113 ? 157.697 144.153 46.630 1.00   26.40 ? 112  ILE I C   1 
ATOM   9736  O  O   . ILE I  1 113 ? 157.712 144.049 47.854 1.00   25.65 ? 112  ILE I O   1 
ATOM   9737  C  CB  . ILE I  1 113 ? 155.433 143.107 46.282 1.00   26.75 ? 112  ILE I CB  1 
ATOM   9738  C  CG1 . ILE I  1 113 ? 156.025 141.770 45.829 1.00   26.30 ? 112  ILE I CG1 1 
ATOM   9739  C  CG2 . ILE I  1 113 ? 154.023 143.337 45.744 1.00   26.06 ? 112  ILE I CG2 1 
ATOM   9740  C  CD1 . ILE I  1 113 ? 155.322 140.563 46.391 1.00   26.23 ? 112  ILE I CD1 1 
ATOM   9741  N  N   . ILE I  1 114 ? 158.809 144.129 45.888 1.00   25.42 ? 113  ILE I N   1 
ATOM   9742  C  CA  . ILE I  1 114 ? 160.120 144.083 46.475 1.00   24.27 ? 113  ILE I CA  1 
ATOM   9743  C  C   . ILE I  1 114 ? 160.364 145.403 47.181 1.00   23.28 ? 113  ILE I C   1 
ATOM   9744  O  O   . ILE I  1 114 ? 160.022 146.457 46.682 1.00   23.15 ? 113  ILE I O   1 
ATOM   9745  C  CB  . ILE I  1 114 ? 161.197 143.750 45.421 1.00   25.31 ? 113  ILE I CB  1 
ATOM   9746  C  CG1 . ILE I  1 114 ? 161.119 142.240 45.090 1.00   25.12 ? 113  ILE I CG1 1 
ATOM   9747  C  CG2 . ILE I  1 114 ? 162.600 144.134 45.897 1.00   24.54 ? 113  ILE I CG2 1 
ATOM   9748  C  CD1 . ILE I  1 114 ? 161.725 141.910 43.740 1.00   25.82 ? 113  ILE I CD1 1 
ATOM   9749  N  N   . GLY I  1 115 ? 160.902 145.327 48.382 1.00   21.99 ? 114  GLY I N   1 
ATOM   9750  C  CA  . GLY I  1 115 ? 161.125 146.509 49.184 1.00   22.14 ? 114  GLY I CA  1 
ATOM   9751  C  C   . GLY I  1 115 ? 159.885 147.038 49.878 1.00   21.56 ? 114  GLY I C   1 
ATOM   9752  O  O   . GLY I  1 115 ? 159.913 148.127 50.434 1.00   21.89 ? 114  GLY I O   1 
ATOM   9753  N  N   . ARG I  1 116 ? 158.797 146.272 49.822 1.00   20.79 ? 115  ARG I N   1 
ATOM   9754  C  CA  . ARG I  1 116 ? 157.582 146.564 50.573 1.00   20.32 ? 115  ARG I CA  1 
ATOM   9755  C  C   . ARG I  1 116 ? 157.457 145.525 51.685 1.00   19.31 ? 115  ARG I C   1 
ATOM   9756  O  O   . ARG I  1 116 ? 158.340 144.673 51.827 1.00   19.38 ? 115  ARG I O   1 
ATOM   9757  C  CB  . ARG I  1 116 ? 156.390 146.595 49.617 1.00   20.71 ? 115  ARG I CB  1 
ATOM   9758  C  CG  . ARG I  1 116 ? 156.621 147.627 48.493 1.00   21.71 ? 115  ARG I CG  1 
ATOM   9759  C  CD  . ARG I  1 116 ? 155.388 147.855 47.642 1.00   22.24 ? 115  ARG I CD  1 
ATOM   9760  N  NE  . ARG I  1 116 ? 155.666 148.731 46.506 1.00   22.79 ? 115  ARG I NE  1 
ATOM   9761  C  CZ  . ARG I  1 116 ? 155.581 150.060 46.516 1.00   23.63 ? 115  ARG I CZ  1 
ATOM   9762  N  NH1 . ARG I  1 116 ? 155.209 150.737 47.608 1.00   23.80 ? 115  ARG I NH1 1 
ATOM   9763  N  NH2 . ARG I  1 116 ? 155.873 150.729 45.407 1.00   24.27 ? 115  ARG I NH2 1 
ATOM   9764  N  N   . THR I  1 117 ? 156.387 145.592 52.470 1.00   18.49 ? 116  THR I N   1 
ATOM   9765  C  CA  . THR I  1 117 ? 156.259 144.792 53.684 1.00   17.81 ? 116  THR I CA  1 
ATOM   9766  C  C   . THR I  1 117 ? 155.133 143.771 53.629 1.00   17.30 ? 116  THR I C   1 
ATOM   9767  O  O   . THR I  1 117 ? 153.997 144.128 53.383 1.00   17.69 ? 116  THR I O   1 
ATOM   9768  C  CB  . THR I  1 117 ? 156.010 145.704 54.916 1.00   17.92 ? 116  THR I CB  1 
ATOM   9769  O  OG1 . THR I  1 117 ? 157.127 146.591 55.099 1.00   18.03 ? 116  THR I OG1 1 
ATOM   9770  C  CG2 . THR I  1 117 ? 155.776 144.862 56.214 1.00   17.30 ? 116  THR I CG2 1 
ATOM   9771  N  N   . LEU I  1 118 ? 155.443 142.509 53.911 1.00   16.68 ? 117  LEU I N   1 
ATOM   9772  C  CA  . LEU I  1 118 ? 154.425 141.481 54.078 1.00   16.16 ? 117  LEU I CA  1 
ATOM   9773  C  C   . LEU I  1 118 ? 153.962 141.468 55.526 1.00   15.92 ? 117  LEU I C   1 
ATOM   9774  O  O   . LEU I  1 118 ? 154.784 141.483 56.444 1.00   15.64 ? 117  LEU I O   1 
ATOM   9775  C  CB  . LEU I  1 118 ? 155.018 140.125 53.745 1.00   16.05 ? 117  LEU I CB  1 
ATOM   9776  C  CG  . LEU I  1 118 ? 154.089 138.916 53.726 1.00   15.73 ? 117  LEU I CG  1 
ATOM   9777  C  CD1 . LEU I  1 118 ? 153.060 139.032 52.600 1.00   15.55 ? 117  LEU I CD1 1 
ATOM   9778  C  CD2 . LEU I  1 118 ? 154.982 137.691 53.567 1.00   15.78 ? 117  LEU I CD2 1 
ATOM   9779  N  N   . VAL I  1 119 ? 152.652 141.384 55.733 1.00   15.59 ? 118  VAL I N   1 
ATOM   9780  C  CA  . VAL I  1 119 ? 152.070 141.416 57.094 1.00   15.57 ? 118  VAL I CA  1 
ATOM   9781  C  C   . VAL I  1 119 ? 151.110 140.263 57.284 1.00   15.50 ? 118  VAL I C   1 
ATOM   9782  O  O   . VAL I  1 119 ? 150.256 140.020 56.420 1.00   15.28 ? 118  VAL I O   1 
ATOM   9783  C  CB  . VAL I  1 119 ? 151.287 142.746 57.336 1.00   15.62 ? 118  VAL I CB  1 
ATOM   9784  C  CG1 . VAL I  1 119 ? 150.567 142.753 58.682 1.00   15.63 ? 118  VAL I CG1 1 
ATOM   9785  C  CG2 . VAL I  1 119 ? 152.217 143.940 57.214 1.00   15.69 ? 118  VAL I CG2 1 
ATOM   9786  N  N   . VAL I  1 120 ? 151.241 139.546 58.406 1.00   15.62 ? 119  VAL I N   1 
ATOM   9787  C  CA  . VAL I  1 120 ? 150.223 138.563 58.795 1.00   15.54 ? 119  VAL I CA  1 
ATOM   9788  C  C   . VAL I  1 120 ? 149.471 139.138 59.998 1.00   15.93 ? 119  VAL I C   1 
ATOM   9789  O  O   . VAL I  1 120 ? 150.093 139.702 60.915 1.00   15.90 ? 119  VAL I O   1 
ATOM   9790  C  CB  . VAL I  1 120 ? 150.800 137.151 59.049 1.00   15.45 ? 119  VAL I CB  1 
ATOM   9791  C  CG1 . VAL I  1 120 ? 151.851 137.130 60.154 1.00   15.25 ? 119  VAL I CG1 1 
ATOM   9792  C  CG2 . VAL I  1 120 ? 149.673 136.170 59.344 1.00   15.27 ? 119  VAL I CG2 1 
ATOM   9793  N  N   . HIS I  1 121 ? 148.146 138.992 59.968 1.00   16.12 ? 120  HIS I N   1 
ATOM   9794  C  CA  . HIS I  1 121 ? 147.236 139.683 60.866 1.00   16.85 ? 120  HIS I CA  1 
ATOM   9795  C  C   . HIS I  1 121 ? 146.631 138.831 61.920 1.00   17.63 ? 120  HIS I C   1 
ATOM   9796  O  O   . HIS I  1 121 ? 146.557 137.617 61.802 1.00   17.58 ? 120  HIS I O   1 
ATOM   9797  C  CB  . HIS I  1 121 ? 146.089 140.305 60.079 1.00   16.81 ? 120  HIS I CB  1 
ATOM   9798  C  CG  . HIS I  1 121 ? 146.461 141.573 59.378 1.00   16.95 ? 120  HIS I CG  1 
ATOM   9799  N  ND1 . HIS I  1 121 ? 146.314 142.780 59.947 1.00   17.13 ? 120  HIS I ND1 1 
ATOM   9800  C  CD2 . HIS I  1 121 ? 146.990 141.793 58.111 1.00   17.11 ? 120  HIS I CD2 1 
ATOM   9801  C  CE1 . HIS I  1 121 ? 146.729 143.728 59.099 1.00   17.40 ? 120  HIS I CE1 1 
ATOM   9802  N  NE2 . HIS I  1 121 ? 147.154 143.122 57.974 1.00   17.43 ? 120  HIS I NE2 1 
ATOM   9803  N  N   . GLU I  1 122 ? 146.148 139.519 62.947 1.00   18.83 ? 121  GLU I N   1 
ATOM   9804  C  CA  . GLU I  1 122 ? 145.455 138.952 64.099 1.00   19.87 ? 121  GLU I CA  1 
ATOM   9805  C  C   . GLU I  1 122 ? 144.203 138.145 63.773 1.00   19.92 ? 121  GLU I C   1 
ATOM   9806  O  O   . GLU I  1 122 ? 143.994 137.095 64.349 1.00   19.24 ? 121  GLU I O   1 
ATOM   9807  C  CB  . GLU I  1 122 ? 145.079 140.122 65.005 1.00   21.30 ? 121  GLU I CB  1 
ATOM   9808  C  CG  . GLU I  1 122 ? 144.181 139.801 66.177 1.00   22.86 ? 121  GLU I CG  1 
ATOM   9809  C  CD  . GLU I  1 122 ? 143.629 141.067 66.827 1.00   24.57 ? 121  GLU I CD  1 
ATOM   9810  O  OE1 . GLU I  1 122 ? 143.394 142.114 66.149 1.00   24.56 ? 121  GLU I OE1 1 
ATOM   9811  O  OE2 . GLU I  1 122 ? 143.434 141.003 68.049 1.00   27.32 ? 121  GLU I OE2 1 
ATOM   9812  N  N   . LYS I  1 123 ? 143.372 138.671 62.864 1.00   20.41 ? 122  LYS I N   1 
ATOM   9813  C  CA  . LYS I  1 123 ? 142.067 138.091 62.536 1.00   20.76 ? 122  LYS I CA  1 
ATOM   9814  C  C   . LYS I  1 123 ? 141.952 137.715 61.073 1.00   19.62 ? 122  LYS I C   1 
ATOM   9815  O  O   . LYS I  1 123 ? 142.762 138.120 60.253 1.00   19.20 ? 122  LYS I O   1 
ATOM   9816  C  CB  . LYS I  1 123 ? 140.950 139.122 62.805 1.00   22.20 ? 122  LYS I CB  1 
ATOM   9817  C  CG  . LYS I  1 123 ? 140.935 139.723 64.208 1.00   23.74 ? 122  LYS I CG  1 
ATOM   9818  C  CD  . LYS I  1 123 ? 139.681 140.549 64.407 1.00   25.22 ? 122  LYS I CD  1 
ATOM   9819  C  CE  . LYS I  1 123 ? 139.814 141.516 65.568 1.00   27.64 ? 122  LYS I CE  1 
ATOM   9820  N  NZ  . LYS I  1 123 ? 138.533 142.241 65.836 1.00   30.04 ? 122  LYS I NZ  1 
ATOM   9821  N  N   . ALA I  1 124 ? 140.885 137.002 60.739 1.00   19.50 ? 123  ALA I N   1 
ATOM   9822  C  CA  . ALA I  1 124 ? 140.515 136.745 59.331 1.00   19.00 ? 123  ALA I CA  1 
ATOM   9823  C  C   . ALA I  1 124 ? 140.265 138.041 58.563 1.00   18.92 ? 123  ALA I C   1 
ATOM   9824  O  O   . ALA I  1 124 ? 139.796 139.043 59.128 1.00   19.12 ? 123  ALA I O   1 
ATOM   9825  C  CB  . ALA I  1 124 ? 139.284 135.858 59.261 1.00   18.83 ? 123  ALA I CB  1 
ATOM   9826  N  N   . ASP I  1 125 ? 140.624 138.012 57.277 1.00   18.69 ? 124  ASP I N   1 
ATOM   9827  C  CA  . ASP I  1 125 ? 140.320 139.063 56.298 1.00   18.58 ? 124  ASP I CA  1 
ATOM   9828  C  C   . ASP I  1 125 ? 138.952 138.693 55.750 1.00   18.42 ? 124  ASP I C   1 
ATOM   9829  O  O   . ASP I  1 125 ? 138.773 137.572 55.275 1.00   17.93 ? 124  ASP I O   1 
ATOM   9830  C  CB  . ASP I  1 125 ? 141.370 139.016 55.190 1.00   18.21 ? 124  ASP I CB  1 
ATOM   9831  C  CG  . ASP I  1 125 ? 141.218 140.112 54.147 1.00   18.15 ? 124  ASP I CG  1 
ATOM   9832  O  OD1 . ASP I  1 125 ? 140.099 140.627 53.889 1.00   18.72 ? 124  ASP I OD1 1 
ATOM   9833  O  OD2 . ASP I  1 125 ? 142.251 140.453 53.542 1.00   18.03 ? 124  ASP I OD2 1 
ATOM   9834  N  N   . ASP I  1 126 ? 137.987 139.618 55.831 1.00   18.95 ? 125  ASP I N   1 
ATOM   9835  C  CA  . ASP I  1 126 ? 136.620 139.353 55.335 1.00   18.86 ? 125  ASP I CA  1 
ATOM   9836  C  C   . ASP I  1 126 ? 136.492 139.515 53.825 1.00   18.93 ? 125  ASP I C   1 
ATOM   9837  O  O   . ASP I  1 126 ? 135.394 139.424 53.275 1.00   19.15 ? 125  ASP I O   1 
ATOM   9838  C  CB  . ASP I  1 126 ? 135.536 140.144 56.105 1.00   19.47 ? 125  ASP I CB  1 
ATOM   9839  C  CG  . ASP I  1 126 ? 135.560 141.661 55.845 1.00   19.68 ? 125  ASP I CG  1 
ATOM   9840  O  OD1 . ASP I  1 126 ? 136.133 142.131 54.833 1.00   19.57 ? 125  ASP I OD1 1 
ATOM   9841  O  OD2 . ASP I  1 126 ? 134.997 142.378 56.699 1.00   20.09 ? 125  ASP I OD2 1 
ATOM   9842  N  N   . LEU I  1 127 ? 137.629 139.725 53.155 1.00   18.80 ? 126  LEU I N   1 
ATOM   9843  C  CA  . LEU I  1 127 ? 137.714 139.812 51.701 1.00   18.70 ? 126  LEU I CA  1 
ATOM   9844  C  C   . LEU I  1 127 ? 136.811 140.908 51.123 1.00   19.03 ? 126  LEU I C   1 
ATOM   9845  O  O   . LEU I  1 127 ? 136.379 140.826 49.980 1.00   18.89 ? 126  LEU I O   1 
ATOM   9846  C  CB  . LEU I  1 127 ? 137.455 138.437 51.051 1.00   18.69 ? 126  LEU I CB  1 
ATOM   9847  C  CG  . LEU I  1 127 ? 138.234 137.250 51.686 1.00   18.71 ? 126  LEU I CG  1 
ATOM   9848  C  CD1 . LEU I  1 127 ? 137.839 135.941 51.023 1.00   18.53 ? 126  LEU I CD1 1 
ATOM   9849  C  CD2 . LEU I  1 127 ? 139.738 137.439 51.586 1.00   18.34 ? 126  LEU I CD2 1 
ATOM   9850  N  N   . GLY I  1 128 ? 136.551 141.944 51.920 1.00   19.38 ? 127  GLY I N   1 
ATOM   9851  C  CA  . GLY I  1 128 ? 135.797 143.093 51.458 1.00   20.22 ? 127  GLY I CA  1 
ATOM   9852  C  C   . GLY I  1 128 ? 134.295 142.886 51.464 1.00   20.43 ? 127  GLY I C   1 
ATOM   9853  O  O   . GLY I  1 128 ? 133.577 143.699 50.927 1.00   20.18 ? 127  GLY I O   1 
ATOM   9854  N  N   . LYS I  1 129 ? 133.842 141.818 52.117 1.00   20.68 ? 128  LYS I N   1 
ATOM   9855  C  CA  . LYS I  1 129 ? 132.439 141.433 52.164 1.00   21.38 ? 128  LYS I CA  1 
ATOM   9856  C  C   . LYS I  1 129 ? 131.758 141.707 53.518 1.00   21.25 ? 128  LYS I C   1 
ATOM   9857  O  O   . LYS I  1 129 ? 130.688 141.170 53.807 1.00   21.38 ? 128  LYS I O   1 
ATOM   9858  C  CB  . LYS I  1 129 ? 132.338 139.947 51.802 1.00   22.15 ? 128  LYS I CB  1 
ATOM   9859  C  CG  . LYS I  1 129 ? 132.851 139.668 50.405 1.00   23.29 ? 128  LYS I CG  1 
ATOM   9860  C  CD  . LYS I  1 129 ? 133.068 138.194 50.108 1.00   24.34 ? 128  LYS I CD  1 
ATOM   9861  C  CE  . LYS I  1 129 ? 131.789 137.464 49.827 1.00   25.41 ? 128  LYS I CE  1 
ATOM   9862  N  NZ  . LYS I  1 129 ? 132.156 136.087 49.371 1.00   27.98 ? 128  LYS I NZ  1 
ATOM   9863  N  N   . GLY I  1 130 ? 132.376 142.560 54.334 1.00   20.91 ? 129  GLY I N   1 
ATOM   9864  C  CA  . GLY I  1 130 ? 131.895 142.841 55.662 1.00   21.10 ? 129  GLY I CA  1 
ATOM   9865  C  C   . GLY I  1 130 ? 130.812 143.915 55.772 1.00   21.56 ? 129  GLY I C   1 
ATOM   9866  O  O   . GLY I  1 130 ? 130.172 144.036 56.820 1.00   21.43 ? 129  GLY I O   1 
ATOM   9867  N  N   . GLY I  1 131 ? 130.629 144.715 54.725 1.00   21.69 ? 130  GLY I N   1 
ATOM   9868  C  CA  . GLY I  1 131 ? 129.528 145.696 54.697 1.00   22.59 ? 130  GLY I CA  1 
ATOM   9869  C  C   . GLY I  1 131 ? 129.739 146.954 55.518 1.00   23.21 ? 130  GLY I C   1 
ATOM   9870  O  O   . GLY I  1 131 ? 128.810 147.752 55.669 1.00   23.32 ? 130  GLY I O   1 
ATOM   9871  N  N   . ASN I  1 132 ? 130.934 147.120 56.084 1.00   23.81 ? 131  ASN I N   1 
ATOM   9872  C  CA  . ASN I  1 132 ? 131.331 148.392 56.723 1.00   25.03 ? 131  ASN I CA  1 
ATOM   9873  C  C   . ASN I  1 132 ? 132.520 149.025 56.000 1.00   25.82 ? 131  ASN I C   1 
ATOM   9874  O  O   . ASN I  1 132 ? 133.115 148.407 55.129 1.00   25.21 ? 131  ASN I O   1 
ATOM   9875  C  CB  . ASN I  1 132 ? 131.608 148.226 58.219 1.00   25.28 ? 131  ASN I CB  1 
ATOM   9876  C  CG  . ASN I  1 132 ? 132.690 147.203 58.543 1.00   24.75 ? 131  ASN I CG  1 
ATOM   9877  O  OD1 . ASN I  1 132 ? 133.381 146.685 57.662 1.00   25.27 ? 131  ASN I OD1 1 
ATOM   9878  N  ND2 . ASN I  1 132 ? 132.849 146.922 59.821 1.00   24.28 ? 131  ASN I ND2 1 
ATOM   9879  N  N   . GLU I  1 133 ? 132.840 150.265 56.321 1.00   27.92 ? 132  GLU I N   1 
ATOM   9880  C  CA  . GLU I  1 133 ? 133.931 150.957 55.632 1.00   30.01 ? 132  GLU I CA  1 
ATOM   9881  C  C   . GLU I  1 133 ? 135.299 150.305 55.875 1.00   28.59 ? 132  GLU I C   1 
ATOM   9882  O  O   . GLU I  1 133 ? 136.164 150.324 55.003 1.00   28.71 ? 132  GLU I O   1 
ATOM   9883  C  CB  . GLU I  1 133 ? 134.008 152.448 56.042 1.00   33.18 ? 132  GLU I CB  1 
ATOM   9884  C  CG  . GLU I  1 133 ? 135.161 153.183 55.347 1.00   35.50 ? 132  GLU I CG  1 
ATOM   9885  C  CD  . GLU I  1 133 ? 134.990 154.702 55.280 1.00   39.54 ? 132  GLU I CD  1 
ATOM   9886  O  OE1 . GLU I  1 133 ? 133.886 155.163 54.909 1.00   43.41 ? 132  GLU I OE1 1 
ATOM   9887  O  OE2 . GLU I  1 133 ? 135.964 155.436 55.592 1.00   41.50 ? 132  GLU I OE2 1 
ATOM   9888  N  N   . GLU I  1 134 ? 135.492 149.778 57.076 1.00   27.98 ? 133  GLU I N   1 
ATOM   9889  C  CA  . GLU I  1 134 ? 136.728 149.103 57.459 1.00   27.79 ? 133  GLU I CA  1 
ATOM   9890  C  C   . GLU I  1 134 ? 136.968 147.867 56.582 1.00   25.80 ? 133  GLU I C   1 
ATOM   9891  O  O   . GLU I  1 134 ? 138.094 147.575 56.276 1.00   25.00 ? 133  GLU I O   1 
ATOM   9892  C  CB  . GLU I  1 134 ? 136.655 148.699 58.947 1.00   29.11 ? 133  GLU I CB  1 
ATOM   9893  C  CG  . GLU I  1 134 ? 137.946 148.149 59.541 1.00   30.15 ? 133  GLU I CG  1 
ATOM   9894  C  CD  . GLU I  1 134 ? 139.053 149.174 59.552 1.00   31.41 ? 133  GLU I CD  1 
ATOM   9895  O  OE1 . GLU I  1 134 ? 138.797 150.320 59.920 1.00   35.39 ? 133  GLU I OE1 1 
ATOM   9896  O  OE2 . GLU I  1 134 ? 140.189 148.844 59.204 1.00   34.57 ? 133  GLU I OE2 1 
ATOM   9897  N  N   . SER I  1 135 ? 135.905 147.158 56.185 1.00   24.85 ? 134  SER I N   1 
ATOM   9898  C  CA  . SER I  1 135 ? 136.024 145.969 55.330 1.00   24.38 ? 134  SER I CA  1 
ATOM   9899  C  C   . SER I  1 135 ? 136.638 146.362 54.000 1.00   25.06 ? 134  SER I C   1 
ATOM   9900  O  O   . SER I  1 135 ? 137.415 145.625 53.397 1.00   23.95 ? 134  SER I O   1 
ATOM   9901  C  CB  . SER I  1 135 ? 134.647 145.323 55.105 1.00   24.10 ? 134  SER I CB  1 
ATOM   9902  O  OG  . SER I  1 135 ? 134.655 144.300 54.119 1.00   23.03 ? 134  SER I OG  1 
ATOM   9903  N  N   . THR I  1 136 ? 136.291 147.567 53.585 1.00   26.70 ? 135  THR I N   1 
ATOM   9904  C  CA  . THR I  1 136 ? 136.652 148.137 52.301 1.00   27.52 ? 135  THR I CA  1 
ATOM   9905  C  C   . THR I  1 136 ? 138.093 148.684 52.261 1.00   27.13 ? 135  THR I C   1 
ATOM   9906  O  O   . THR I  1 136 ? 138.572 149.075 51.201 1.00   26.87 ? 135  THR I O   1 
ATOM   9907  C  CB  . THR I  1 136 ? 135.624 149.265 52.002 1.00   29.43 ? 135  THR I CB  1 
ATOM   9908  O  OG1 . THR I  1 136 ? 135.196 149.152 50.662 1.00   32.53 ? 135  THR I OG1 1 
ATOM   9909  C  CG2 . THR I  1 136 ? 136.183 150.713 52.285 1.00   29.45 ? 135  THR I CG2 1 
ATOM   9910  N  N   . LYS I  1 137 ? 138.753 148.738 53.421 1.00   27.04 ? 136  LYS I N   1 
ATOM   9911  C  CA  . LYS I  1 137 ? 140.154 149.178 53.531 1.00   27.89 ? 136  LYS I CA  1 
ATOM   9912  C  C   . LYS I  1 137 ? 141.107 148.051 53.937 1.00   25.77 ? 136  LYS I C   1 
ATOM   9913  O  O   . LYS I  1 137 ? 142.172 147.892 53.351 1.00   24.63 ? 136  LYS I O   1 
ATOM   9914  C  CB  . LYS I  1 137 ? 140.294 150.289 54.568 1.00   31.23 ? 136  LYS I CB  1 
ATOM   9915  C  CG  . LYS I  1 137 ? 139.543 151.560 54.236 1.00   35.21 ? 136  LYS I CG  1 
ATOM   9916  C  CD  . LYS I  1 137 ? 139.960 152.738 55.116 1.00   38.95 ? 136  LYS I CD  1 
ATOM   9917  C  CE  . LYS I  1 137 ? 139.250 152.723 56.468 1.00   41.35 ? 136  LYS I CE  1 
ATOM   9918  N  NZ  . LYS I  1 137 ? 139.274 154.078 57.104 1.00   43.45 ? 136  LYS I NZ  1 
ATOM   9919  N  N   . THR I  1 138 ? 140.731 147.288 54.961 1.00   23.91 ? 137  THR I N   1 
ATOM   9920  C  CA  . THR I  1 138 ? 141.637 146.313 55.569 1.00   23.13 ? 137  THR I CA  1 
ATOM   9921  C  C   . THR I  1 138 ? 141.039 144.924 55.669 1.00   21.93 ? 137  THR I C   1 
ATOM   9922  O  O   . THR I  1 138 ? 141.724 143.986 56.044 1.00   22.20 ? 137  THR I O   1 
ATOM   9923  C  CB  . THR I  1 138 ? 141.984 146.713 57.005 1.00   23.14 ? 137  THR I CB  1 
ATOM   9924  O  OG1 . THR I  1 138 ? 140.789 146.650 57.800 1.00   24.46 ? 137  THR I OG1 1 
ATOM   9925  C  CG2 . THR I  1 138 ? 142.585 148.115 57.065 1.00   23.46 ? 137  THR I CG2 1 
ATOM   9926  N  N   . GLY I  1 139 ? 139.758 144.783 55.367 1.00   20.99 ? 138  GLY I N   1 
ATOM   9927  C  CA  . GLY I  1 139 ? 139.083 143.531 55.548 1.00   20.21 ? 138  GLY I CA  1 
ATOM   9928  C  C   . GLY I  1 139 ? 138.817 143.141 56.990 1.00   20.26 ? 138  GLY I C   1 
ATOM   9929  O  O   . GLY I  1 139 ? 138.507 141.979 57.244 1.00   19.38 ? 138  GLY I O   1 
ATOM   9930  N  N   . ASN I  1 140 ? 138.902 144.104 57.924 1.00   20.74 ? 139  ASN I N   1 
ATOM   9931  C  CA  . ASN I  1 140 ? 138.659 143.850 59.342 1.00   21.03 ? 139  ASN I CA  1 
ATOM   9932  C  C   . ASN I  1 140 ? 139.640 142.790 59.920 1.00   20.37 ? 139  ASN I C   1 
ATOM   9933  O  O   . ASN I  1 140 ? 139.285 142.045 60.840 1.00   19.66 ? 139  ASN I O   1 
ATOM   9934  C  CB  . ASN I  1 140 ? 137.203 143.408 59.568 1.00   21.43 ? 139  ASN I CB  1 
ATOM   9935  C  CG  . ASN I  1 140 ? 136.213 144.540 59.373 1.00   23.02 ? 139  ASN I CG  1 
ATOM   9936  O  OD1 . ASN I  1 140 ? 136.318 145.583 60.034 1.00   24.84 ? 139  ASN I OD1 1 
ATOM   9937  N  ND2 . ASN I  1 140 ? 135.231 144.343 58.476 1.00   22.79 ? 139  ASN I ND2 1 
ATOM   9938  N  N   . ALA I  1 141 ? 140.854 142.729 59.357 1.00   19.54 ? 140  ALA I N   1 
ATOM   9939  C  CA  . ALA I  1 141 ? 141.861 141.719 59.745 1.00   19.45 ? 140  ALA I CA  1 
ATOM   9940  C  C   . ALA I  1 141 ? 142.528 142.041 61.092 1.00   19.31 ? 140  ALA I C   1 
ATOM   9941  O  O   . ALA I  1 141 ? 143.238 141.205 61.660 1.00   19.06 ? 140  ALA I O   1 
ATOM   9942  C  CB  . ALA I  1 141 ? 142.930 141.568 58.645 1.00   18.93 ? 140  ALA I CB  1 
ATOM   9943  N  N   . GLY I  1 142 ? 142.331 143.252 61.586 1.00   19.46 ? 141  GLY I N   1 
ATOM   9944  C  CA  . GLY I  1 142 ? 142.793 143.593 62.947 1.00   20.09 ? 141  GLY I CA  1 
ATOM   9945  C  C   . GLY I  1 142 ? 144.292 143.847 63.000 1.00   20.03 ? 141  GLY I C   1 
ATOM   9946  O  O   . GLY I  1 142 ? 144.898 144.254 62.017 1.00   20.02 ? 141  GLY I O   1 
ATOM   9947  N  N   . SER I  1 143 ? 144.913 143.579 64.134 1.00   20.45 ? 142  SER I N   1 
ATOM   9948  C  CA  . SER I  1 143 ? 146.275 144.064 64.329 1.00   20.74 ? 142  SER I CA  1 
ATOM   9949  C  C   . SER I  1 143 ? 147.321 143.278 63.516 1.00   20.15 ? 142  SER I C   1 
ATOM   9950  O  O   . SER I  1 143 ? 147.033 142.227 62.952 1.00   19.21 ? 142  SER I O   1 
ATOM   9951  C  CB  . SER I  1 143 ? 146.606 144.104 65.833 1.00   21.74 ? 142  SER I CB  1 
ATOM   9952  O  OG  . SER I  1 143 ? 147.029 142.842 66.220 1.00   23.06 ? 142  SER I OG  1 
ATOM   9953  N  N   . ARG I  1 144 ? 148.539 143.822 63.463 1.00   20.12 ? 143  ARG I N   1 
ATOM   9954  C  CA  . ARG I  1 144 ? 149.618 143.271 62.681 1.00   19.69 ? 143  ARG I CA  1 
ATOM   9955  C  C   . ARG I  1 144 ? 150.507 142.426 63.577 1.00   19.83 ? 143  ARG I C   1 
ATOM   9956  O  O   . ARG I  1 144 ? 151.246 142.972 64.386 1.00   19.56 ? 143  ARG I O   1 
ATOM   9957  C  CB  . ARG I  1 144 ? 150.418 144.428 62.040 1.00   19.92 ? 143  ARG I CB  1 
ATOM   9958  C  CG  . ARG I  1 144 ? 149.520 145.383 61.263 1.00   20.23 ? 143  ARG I CG  1 
ATOM   9959  C  CD  . ARG I  1 144 ? 150.219 146.583 60.666 1.00   20.70 ? 143  ARG I CD  1 
ATOM   9960  N  NE  . ARG I  1 144 ? 149.242 147.438 60.007 1.00   21.16 ? 143  ARG I NE  1 
ATOM   9961  C  CZ  . ARG I  1 144 ? 149.528 148.484 59.246 1.00   21.72 ? 143  ARG I CZ  1 
ATOM   9962  N  NH1 . ARG I  1 144 ? 150.783 148.840 59.004 1.00   22.12 ? 143  ARG I NH1 1 
ATOM   9963  N  NH2 . ARG I  1 144 ? 148.538 149.176 58.707 1.00   22.13 ? 143  ARG I NH2 1 
ATOM   9964  N  N   . LEU I  1 145 ? 150.445 141.099 63.440 1.00   19.63 ? 144  LEU I N   1 
ATOM   9965  C  CA  . LEU I  1 145 ? 151.165 140.213 64.366 1.00   19.85 ? 144  LEU I CA  1 
ATOM   9966  C  C   . LEU I  1 145 ? 152.632 140.093 64.013 1.00   19.86 ? 144  LEU I C   1 
ATOM   9967  O  O   . LEU I  1 145 ? 153.466 139.994 64.881 1.00   20.04 ? 144  LEU I O   1 
ATOM   9968  C  CB  . LEU I  1 145 ? 150.536 138.819 64.433 1.00   20.03 ? 144  LEU I CB  1 
ATOM   9969  C  CG  . LEU I  1 145 ? 149.100 138.791 64.985 1.00   20.59 ? 144  LEU I CG  1 
ATOM   9970  C  CD1 . LEU I  1 145 ? 148.587 137.360 65.033 1.00   20.43 ? 144  LEU I CD1 1 
ATOM   9971  C  CD2 . LEU I  1 145 ? 148.991 139.486 66.348 1.00   20.65 ? 144  LEU I CD2 1 
ATOM   9972  N  N   . ALA I  1 146 ? 152.949 140.103 62.724 1.00   19.40 ? 145  ALA I N   1 
ATOM   9973  C  CA  . ALA I  1 146 ? 154.331 139.975 62.321 1.00   19.31 ? 145  ALA I CA  1 
ATOM   9974  C  C   . ALA I  1 146 ? 154.465 140.566 60.945 1.00   18.93 ? 145  ALA I C   1 
ATOM   9975  O  O   . ALA I  1 146 ? 153.483 140.639 60.187 1.00   18.05 ? 145  ALA I O   1 
ATOM   9976  C  CB  . ALA I  1 146 ? 154.784 138.512 62.347 1.00   18.93 ? 145  ALA I CB  1 
ATOM   9977  N  N   . CYS I  1 147 ? 155.672 141.018 60.636 1.00   19.18 ? 146  CYS I N   1 
ATOM   9978  C  CA  . CYS I  1 147 ? 155.933 141.579 59.323 1.00   19.70 ? 146  CYS I CA  1 
ATOM   9979  C  C   . CYS I  1 147 ? 157.406 141.488 58.997 1.00   19.64 ? 146  CYS I C   1 
ATOM   9980  O  O   . CYS I  1 147 ? 158.212 141.119 59.843 1.00   19.78 ? 146  CYS I O   1 
ATOM   9981  C  CB  . CYS I  1 147 ? 155.455 143.031 59.233 1.00   20.37 ? 146  CYS I CB  1 
ATOM   9982  S  SG  . CYS I  1 147 ? 156.250 144.145 60.421 1.00   21.22 ? 146  CYS I SG  1 
ATOM   9983  N  N   . GLY I  1 148 ? 157.724 141.801 57.748 1.00   19.30 ? 147  GLY I N   1 
ATOM   9984  C  CA  . GLY I  1 148 ? 159.100 141.832 57.270 1.00   19.25 ? 147  GLY I CA  1 
ATOM   9985  C  C   . GLY I  1 148 ? 159.135 142.508 55.913 1.00   18.99 ? 147  GLY I C   1 
ATOM   9986  O  O   . GLY I  1 148 ? 158.110 142.590 55.225 1.00   18.97 ? 147  GLY I O   1 
ATOM   9987  N  N   . VAL I  1 149 ? 160.304 142.999 55.538 1.00   18.70 ? 148  VAL I N   1 
ATOM   9988  C  CA  . VAL I  1 149 ? 160.498 143.633 54.232 1.00   19.02 ? 148  VAL I CA  1 
ATOM   9989  C  C   . VAL I  1 149 ? 160.792 142.545 53.202 1.00   18.79 ? 148  VAL I C   1 
ATOM   9990  O  O   . VAL I  1 149 ? 161.538 141.597 53.468 1.00   18.41 ? 148  VAL I O   1 
ATOM   9991  C  CB  . VAL I  1 149 ? 161.647 144.673 54.277 1.00   19.20 ? 148  VAL I CB  1 
ATOM   9992  C  CG1 . VAL I  1 149 ? 161.781 145.414 52.962 1.00   19.55 ? 148  VAL I CG1 1 
ATOM   9993  C  CG2 . VAL I  1 149 ? 161.396 145.666 55.382 1.00   19.32 ? 148  VAL I CG2 1 
ATOM   9994  N  N   . ILE I  1 150 ? 160.165 142.658 52.042 1.00   18.86 ? 149  ILE I N   1 
ATOM   9995  C  CA  . ILE I  1 150 ? 160.316 141.652 51.001 1.00   19.09 ? 149  ILE I CA  1 
ATOM   9996  C  C   . ILE I  1 150 ? 161.599 141.946 50.213 1.00   19.69 ? 149  ILE I C   1 
ATOM   9997  O  O   . ILE I  1 150 ? 161.718 142.995 49.609 1.00   19.66 ? 149  ILE I O   1 
ATOM   9998  C  CB  . ILE I  1 150 ? 159.123 141.668 50.044 1.00   18.93 ? 149  ILE I CB  1 
ATOM   9999  C  CG1 . ILE I  1 150 ? 157.829 141.427 50.816 1.00   18.71 ? 149  ILE I CG1 1 
ATOM   10000 C  CG2 . ILE I  1 150 ? 159.320 140.624 48.955 1.00   18.95 ? 149  ILE I CG2 1 
ATOM   10001 C  CD1 . ILE I  1 150 ? 156.581 141.635 49.990 1.00   18.30 ? 149  ILE I CD1 1 
ATOM   10002 N  N   . GLY I  1 151 ? 162.559 141.031 50.247 1.00   20.36 ? 150  GLY I N   1 
ATOM   10003 C  CA  . GLY I  1 151 ? 163.866 141.260 49.625 1.00   21.32 ? 150  GLY I CA  1 
ATOM   10004 C  C   . GLY I  1 151 ? 164.132 140.313 48.468 1.00   22.04 ? 150  GLY I C   1 
ATOM   10005 O  O   . GLY I  1 151 ? 163.549 139.213 48.413 1.00   21.35 ? 150  GLY I O   1 
ATOM   10006 N  N   . ILE I  1 152 ? 165.010 140.756 47.556 1.00   23.08 ? 151  ILE I N   1 
ATOM   10007 C  CA  . ILE I  1 152 ? 165.378 140.010 46.364 1.00   24.21 ? 151  ILE I CA  1 
ATOM   10008 C  C   . ILE I  1 152 ? 166.145 138.812 46.832 1.00   24.40 ? 151  ILE I C   1 
ATOM   10009 O  O   . ILE I  1 152 ? 167.031 138.967 47.645 1.00   24.96 ? 151  ILE I O   1 
ATOM   10010 C  CB  . ILE I  1 152 ? 166.324 140.824 45.423 1.00   25.69 ? 151  ILE I CB  1 
ATOM   10011 C  CG1 . ILE I  1 152 ? 165.628 142.074 44.860 1.00   26.27 ? 151  ILE I CG1 1 
ATOM   10012 C  CG2 . ILE I  1 152 ? 166.821 139.948 44.277 1.00   25.25 ? 151  ILE I CG2 1 
ATOM   10013 C  CD1 . ILE I  1 152 ? 166.579 143.140 44.347 1.00   27.09 ? 151  ILE I CD1 1 
ATOM   10014 N  N   . ALA I  1 153 ? 165.815 137.629 46.333 1.00   25.00 ? 152  ALA I N   1 
ATOM   10015 C  CA  . ALA I  1 153 ? 166.499 136.403 46.746 1.00   26.55 ? 152  ALA I CA  1 
ATOM   10016 C  C   . ALA I  1 153 ? 167.215 135.769 45.562 1.00   28.55 ? 152  ALA I C   1 
ATOM   10017 O  O   . ALA I  1 153 ? 166.849 135.983 44.423 1.00   28.79 ? 152  ALA I O   1 
ATOM   10018 C  CB  . ALA I  1 153 ? 165.510 135.422 47.363 1.00   25.67 ? 152  ALA I CB  1 
ATOM   10019 N  N   . GLN I  1 154 ? 168.243 134.988 45.844 1.00   31.92 ? 153  GLN I N   1 
ATOM   10020 C  CA  . GLN I  1 154 ? 169.064 134.392 44.795 1.00   35.21 ? 153  GLN I CA  1 
ATOM   10021 C  C   . GLN I  1 154 ? 168.329 133.216 44.215 1.00   36.99 ? 153  GLN I C   1 
ATOM   10022 O  O   . GLN I  1 154 ? 168.344 133.068 43.004 1.00   41.38 ? 153  GLN I O   1 
ATOM   10023 C  CB  . GLN I  1 154 ? 170.411 133.939 45.346 1.00   36.38 ? 153  GLN I CB  1 
ATOM   10024 C  CG  . GLN I  1 154 ? 171.448 133.587 44.283 1.00   37.95 ? 153  GLN I CG  1 
ATOM   10025 C  CD  . GLN I  1 154 ? 172.814 133.326 44.892 1.00   39.20 ? 153  GLN I CD  1 
ATOM   10026 O  OE1 . GLN I  1 154 ? 172.931 133.121 46.104 1.00   39.31 ? 153  GLN I OE1 1 
ATOM   10027 N  NE2 . GLN I  1 154 ? 173.850 133.314 44.059 1.00   41.20 ? 153  GLN I NE2 1 
ATOM   10028 O  OXT . GLN I  1 154 ? 167.708 132.427 44.934 1.00   38.33 ? 153  GLN I OXT 1 
ATOM   10029 N  N   . ALA J  1 2   ? 121.462 104.789 35.604 1.00   53.24 ? 1    ALA J N   1 
ATOM   10030 C  CA  . ALA J  1 2   ? 120.787 105.108 36.900 1.00   53.02 ? 1    ALA J CA  1 
ATOM   10031 C  C   . ALA J  1 2   ? 120.416 106.596 36.977 1.00   50.85 ? 1    ALA J C   1 
ATOM   10032 O  O   . ALA J  1 2   ? 121.272 107.458 36.865 1.00   52.61 ? 1    ALA J O   1 
ATOM   10033 C  CB  . ALA J  1 2   ? 121.685 104.723 38.068 1.00   53.20 ? 1    ALA J CB  1 
ATOM   10034 N  N   . THR J  1 3   ? 119.131 106.883 37.148 1.00   48.97 ? 2    THR J N   1 
ATOM   10035 C  CA  . THR J  1 3   ? 118.651 108.238 37.302 1.00   45.00 ? 2    THR J CA  1 
ATOM   10036 C  C   . THR J  1 3   ? 118.439 108.571 38.784 1.00   41.38 ? 2    THR J C   1 
ATOM   10037 O  O   . THR J  1 3   ? 118.287 109.750 39.135 1.00   39.48 ? 2    THR J O   1 
ATOM   10038 C  CB  . THR J  1 3   ? 117.338 108.473 36.518 1.00   47.00 ? 2    THR J CB  1 
ATOM   10039 O  OG1 . THR J  1 3   ? 116.449 107.372 36.720 1.00   48.42 ? 2    THR J OG1 1 
ATOM   10040 C  CG2 . THR J  1 3   ? 117.611 108.617 35.027 1.00   48.44 ? 2    THR J CG2 1 
ATOM   10041 N  N   . LYS J  1 4   ? 118.426 107.560 39.653 1.00   37.34 ? 3    LYS J N   1 
ATOM   10042 C  CA  . LYS J  1 4   ? 118.316 107.814 41.094 1.00   36.07 ? 3    LYS J CA  1 
ATOM   10043 C  C   . LYS J  1 4   ? 119.354 107.071 41.922 1.00   34.12 ? 3    LYS J C   1 
ATOM   10044 O  O   . LYS J  1 4   ? 119.756 105.954 41.584 1.00   33.00 ? 3    LYS J O   1 
ATOM   10045 C  CB  . LYS J  1 4   ? 116.928 107.473 41.610 1.00   38.20 ? 3    LYS J CB  1 
ATOM   10046 C  CG  . LYS J  1 4   ? 115.830 108.419 41.144 1.00   40.63 ? 3    LYS J CG  1 
ATOM   10047 C  CD  . LYS J  1 4   ? 114.535 108.145 41.906 1.00   42.25 ? 3    LYS J CD  1 
ATOM   10048 C  CE  . LYS J  1 4   ? 113.314 108.588 41.117 1.00   45.14 ? 3    LYS J CE  1 
ATOM   10049 N  NZ  . LYS J  1 4   ? 112.240 109.161 41.983 1.00   46.20 ? 3    LYS J NZ  1 
ATOM   10050 N  N   . ALA J  1 5   ? 119.771 107.693 43.027 1.00   32.22 ? 4    ALA J N   1 
ATOM   10051 C  CA  . ALA J  1 5   ? 120.750 107.086 43.936 1.00   30.36 ? 4    ALA J CA  1 
ATOM   10052 C  C   . ALA J  1 5   ? 120.453 107.484 45.386 1.00   29.08 ? 4    ALA J C   1 
ATOM   10053 O  O   . ALA J  1 5   ? 119.691 108.423 45.640 1.00   28.17 ? 4    ALA J O   1 
ATOM   10054 C  CB  . ALA J  1 5   ? 122.172 107.482 43.533 1.00   29.19 ? 4    ALA J CB  1 
ATOM   10055 N  N   . VAL J  1 6   ? 121.039 106.748 46.327 1.00   27.86 ? 5    VAL J N   1 
ATOM   10056 C  CA  . VAL J  1 6   ? 120.790 106.972 47.746 1.00   27.57 ? 5    VAL J CA  1 
ATOM   10057 C  C   . VAL J  1 6   ? 122.031 106.626 48.575 1.00   27.16 ? 5    VAL J C   1 
ATOM   10058 O  O   . VAL J  1 6   ? 122.850 105.792 48.185 1.00   27.15 ? 5    VAL J O   1 
ATOM   10059 C  CB  . VAL J  1 6   ? 119.554 106.182 48.237 1.00   27.68 ? 5    VAL J CB  1 
ATOM   10060 C  CG1 . VAL J  1 6   ? 119.870 104.689 48.390 1.00   28.25 ? 5    VAL J CG1 1 
ATOM   10061 C  CG2 . VAL J  1 6   ? 119.034 106.771 49.536 1.00   27.84 ? 5    VAL J CG2 1 
ATOM   10062 N  N   . CYS J  1 7   ? 122.169 107.280 49.712 1.00   26.75 ? 6    CYS J N   1 
ATOM   10063 C  CA  . CYS J  1 7   ? 123.293 107.050 50.570 1.00   26.93 ? 6    CYS J CA  1 
ATOM   10064 C  C   . CYS J  1 7   ? 122.886 107.193 52.020 1.00   27.02 ? 6    CYS J C   1 
ATOM   10065 O  O   . CYS J  1 7   ? 122.277 108.197 52.407 1.00   27.96 ? 6    CYS J O   1 
ATOM   10066 C  CB  . CYS J  1 7   ? 124.402 108.046 50.243 1.00   27.12 ? 6    CYS J CB  1 
ATOM   10067 S  SG  . CYS J  1 7   ? 125.849 107.780 51.273 1.00   28.36 ? 6    CYS J SG  1 
ATOM   10068 N  N   . VAL J  1 8   ? 123.217 106.191 52.820 1.00   26.89 ? 7    VAL J N   1 
ATOM   10069 C  CA  . VAL J  1 8   ? 122.971 106.222 54.271 1.00   27.59 ? 7    VAL J CA  1 
ATOM   10070 C  C   . VAL J  1 8   ? 124.274 106.591 54.986 1.00   27.37 ? 7    VAL J C   1 
ATOM   10071 O  O   . VAL J  1 8   ? 125.275 105.883 54.873 1.00   26.89 ? 7    VAL J O   1 
ATOM   10072 C  CB  . VAL J  1 8   ? 122.458 104.864 54.823 1.00   27.92 ? 7    VAL J CB  1 
ATOM   10073 C  CG1 . VAL J  1 8   ? 122.330 104.944 56.328 1.00   28.34 ? 7    VAL J CG1 1 
ATOM   10074 C  CG2 . VAL J  1 8   ? 121.106 104.492 54.204 1.00   29.41 ? 7    VAL J CG2 1 
ATOM   10075 N  N   . LEU J  1 9   ? 124.238 107.685 55.734 1.00   28.12 ? 8    LEU J N   1 
ATOM   10076 C  CA  . LEU J  1 9   ? 125.420 108.238 56.363 1.00   29.46 ? 8    LEU J CA  1 
ATOM   10077 C  C   . LEU J  1 9   ? 125.494 107.745 57.792 1.00   29.92 ? 8    LEU J C   1 
ATOM   10078 O  O   . LEU J  1 9   ? 124.566 107.952 58.556 1.00   30.21 ? 8    LEU J O   1 
ATOM   10079 C  CB  . LEU J  1 9   ? 125.361 109.769 56.356 1.00   30.58 ? 8    LEU J CB  1 
ATOM   10080 C  CG  . LEU J  1 9   ? 126.125 110.545 55.285 1.00   31.75 ? 8    LEU J CG  1 
ATOM   10081 C  CD1 . LEU J  1 9   ? 126.222 109.772 53.996 1.00   33.47 ? 8    LEU J CD1 1 
ATOM   10082 C  CD2 . LEU J  1 9   ? 125.464 111.894 55.063 1.00   32.92 ? 8    LEU J CD2 1 
ATOM   10083 N  N   . LYS J  1 10  ? 126.601 107.112 58.154 1.00   30.12 ? 9    LYS J N   1 
ATOM   10084 C  CA  . LYS J  1 10  ? 126.790 106.606 59.518 1.00   32.39 ? 9    LYS J CA  1 
ATOM   10085 C  C   . LYS J  1 10  ? 128.240 106.739 59.951 1.00   31.48 ? 9    LYS J C   1 
ATOM   10086 O  O   . LYS J  1 10  ? 129.146 106.738 59.124 1.00   29.42 ? 9    LYS J O   1 
ATOM   10087 C  CB  . LYS J  1 10  ? 126.362 105.137 59.609 1.00   34.44 ? 9    LYS J CB  1 
ATOM   10088 C  CG  . LYS J  1 10  ? 124.859 104.929 59.489 1.00   37.11 ? 9    LYS J CG  1 
ATOM   10089 C  CD  . LYS J  1 10  ? 124.529 103.446 59.406 1.00   39.99 ? 9    LYS J CD  1 
ATOM   10090 C  CE  . LYS J  1 10  ? 123.033 103.190 59.207 1.00   42.04 ? 9    LYS J CE  1 
ATOM   10091 N  NZ  . LYS J  1 10  ? 122.808 101.776 58.767 1.00   43.20 ? 9    LYS J NZ  1 
ATOM   10092 N  N   . GLY J  1 11  ? 128.464 106.846 61.252 1.00   33.41 ? 10   GLY J N   1 
ATOM   10093 C  CA  . GLY J  1 11  ? 129.834 107.013 61.751 1.00   35.49 ? 10   GLY J CA  1 
ATOM   10094 C  C   . GLY J  1 11  ? 130.080 106.279 63.040 1.00   37.02 ? 10   GLY J C   1 
ATOM   10095 O  O   . GLY J  1 11  ? 129.269 105.455 63.440 1.00   38.34 ? 10   GLY J O   1 
ATOM   10096 N  N   . ASP J  1 12  ? 131.209 106.589 63.682 1.00   39.79 ? 11   ASP J N   1 
ATOM   10097 C  CA  . ASP J  1 12  ? 131.503 106.133 65.058 1.00   40.67 ? 11   ASP J CA  1 
ATOM   10098 C  C   . ASP J  1 12  ? 130.691 106.871 66.134 1.00   41.15 ? 11   ASP J C   1 
ATOM   10099 O  O   . ASP J  1 12  ? 130.314 106.272 67.137 1.00   43.51 ? 11   ASP J O   1 
ATOM   10100 C  CB  . ASP J  1 12  ? 132.998 106.267 65.357 1.00   40.22 ? 11   ASP J CB  1 
ATOM   10101 C  CG  . ASP J  1 12  ? 133.827 105.252 64.610 0.50   39.38 ? 11   ASP J CG  1 
ATOM   10102 O  OD1 . ASP J  1 12  ? 133.349 104.112 64.434 0.50   39.43 ? 11   ASP J OD1 1 
ATOM   10103 O  OD2 . ASP J  1 12  ? 134.953 105.589 64.201 0.50   38.45 ? 11   ASP J OD2 1 
ATOM   10104 N  N   . GLY J  1 13  ? 130.409 108.157 65.923 1.00   40.47 ? 12   GLY J N   1 
ATOM   10105 C  CA  . GLY J  1 13  ? 129.641 108.956 66.893 1.00   38.76 ? 12   GLY J CA  1 
ATOM   10106 C  C   . GLY J  1 13  ? 128.164 109.072 66.546 1.00   38.41 ? 12   GLY J C   1 
ATOM   10107 O  O   . GLY J  1 13  ? 127.591 108.179 65.908 1.00   37.69 ? 12   GLY J O   1 
ATOM   10108 N  N   . PRO J  1 14  ? 127.536 110.199 66.927 1.00   37.63 ? 13   PRO J N   1 
ATOM   10109 C  CA  . PRO J  1 14  ? 126.090 110.360 66.777 1.00   37.56 ? 13   PRO J CA  1 
ATOM   10110 C  C   . PRO J  1 14  ? 125.607 110.862 65.405 1.00   35.72 ? 13   PRO J C   1 
ATOM   10111 O  O   . PRO J  1 14  ? 124.392 110.958 65.194 1.00   35.24 ? 13   PRO J O   1 
ATOM   10112 C  CB  . PRO J  1 14  ? 125.762 111.400 67.851 1.00   38.69 ? 13   PRO J CB  1 
ATOM   10113 C  CG  . PRO J  1 14  ? 126.967 112.274 67.877 1.00   38.97 ? 13   PRO J CG  1 
ATOM   10114 C  CD  . PRO J  1 14  ? 128.144 111.366 67.593 1.00   38.31 ? 13   PRO J CD  1 
ATOM   10115 N  N   . VAL J  1 15  ? 126.524 111.177 64.484 1.00   33.33 ? 14   VAL J N   1 
ATOM   10116 C  CA  . VAL J  1 15  ? 126.126 111.781 63.218 1.00   31.62 ? 14   VAL J CA  1 
ATOM   10117 C  C   . VAL J  1 15  ? 125.567 110.708 62.282 1.00   31.95 ? 14   VAL J C   1 
ATOM   10118 O  O   . VAL J  1 15  ? 126.176 109.653 62.097 1.00   31.73 ? 14   VAL J O   1 
ATOM   10119 C  CB  . VAL J  1 15  ? 127.293 112.556 62.537 1.00   30.70 ? 14   VAL J CB  1 
ATOM   10120 C  CG1 . VAL J  1 15  ? 126.857 113.095 61.181 1.00   28.75 ? 14   VAL J CG1 1 
ATOM   10121 C  CG2 . VAL J  1 15  ? 127.776 113.690 63.437 1.00   30.57 ? 14   VAL J CG2 1 
ATOM   10122 N  N   . GLN J  1 16  ? 124.406 110.980 61.694 1.00   31.63 ? 15   GLN J N   1 
ATOM   10123 C  CA  . GLN J  1 16  ? 123.802 110.047 60.764 1.00   31.97 ? 15   GLN J CA  1 
ATOM   10124 C  C   . GLN J  1 16  ? 122.735 110.712 59.891 1.00   31.06 ? 15   GLN J C   1 
ATOM   10125 O  O   . GLN J  1 16  ? 122.166 111.740 60.253 1.00   30.68 ? 15   GLN J O   1 
ATOM   10126 C  CB  . GLN J  1 16  ? 123.202 108.845 61.515 1.00   34.55 ? 15   GLN J CB  1 
ATOM   10127 C  CG  . GLN J  1 16  ? 122.118 109.192 62.520 1.00   36.64 ? 15   GLN J CG  1 
ATOM   10128 C  CD  . GLN J  1 16  ? 121.511 107.954 63.195 1.00   39.62 ? 15   GLN J CD  1 
ATOM   10129 O  OE1 . GLN J  1 16  ? 121.638 106.828 62.708 1.00   41.20 ? 15   GLN J OE1 1 
ATOM   10130 N  NE2 . GLN J  1 16  ? 120.854 108.169 64.325 1.00   40.65 ? 15   GLN J NE2 1 
ATOM   10131 N  N   . GLY J  1 17  ? 122.472 110.118 58.734 1.00   29.87 ? 16   GLY J N   1 
ATOM   10132 C  CA  . GLY J  1 17  ? 121.432 110.637 57.850 1.00   29.06 ? 16   GLY J CA  1 
ATOM   10133 C  C   . GLY J  1 17  ? 121.264 109.888 56.549 1.00   27.62 ? 16   GLY J C   1 
ATOM   10134 O  O   . GLY J  1 17  ? 121.897 108.848 56.314 1.00   26.62 ? 16   GLY J O   1 
ATOM   10135 N  N   . ILE J  1 18  ? 120.413 110.449 55.697 1.00   26.82 ? 17   ILE J N   1 
ATOM   10136 C  CA  . ILE J  1 18  ? 120.061 109.869 54.414 1.00   26.54 ? 17   ILE J CA  1 
ATOM   10137 C  C   . ILE J  1 18  ? 120.121 110.954 53.350 1.00   26.55 ? 17   ILE J C   1 
ATOM   10138 O  O   . ILE J  1 18  ? 119.522 112.035 53.511 1.00   26.56 ? 17   ILE J O   1 
ATOM   10139 C  CB  . ILE J  1 18  ? 118.635 109.289 54.443 1.00   27.68 ? 17   ILE J CB  1 
ATOM   10140 C  CG1 . ILE J  1 18  ? 118.548 108.102 55.424 1.00   28.68 ? 17   ILE J CG1 1 
ATOM   10141 C  CG2 . ILE J  1 18  ? 118.222 108.864 53.044 1.00   27.69 ? 17   ILE J CG2 1 
ATOM   10142 C  CD1 . ILE J  1 18  ? 117.130 107.576 55.626 1.00   29.65 ? 17   ILE J CD1 1 
ATOM   10143 N  N   . ILE J  1 19  ? 120.866 110.694 52.280 1.00   25.99 ? 18   ILE J N   1 
ATOM   10144 C  CA  . ILE J  1 19  ? 120.971 111.642 51.172 1.00   26.12 ? 18   ILE J CA  1 
ATOM   10145 C  C   . ILE J  1 19  ? 120.513 110.954 49.872 1.00   26.57 ? 18   ILE J C   1 
ATOM   10146 O  O   . ILE J  1 19  ? 120.904 109.822 49.603 1.00   27.14 ? 18   ILE J O   1 
ATOM   10147 C  CB  . ILE J  1 19  ? 122.404 112.193 51.051 1.00   25.27 ? 18   ILE J CB  1 
ATOM   10148 C  CG1 . ILE J  1 19  ? 122.758 113.017 52.301 1.00   25.11 ? 18   ILE J CG1 1 
ATOM   10149 C  CG2 . ILE J  1 19  ? 122.580 113.020 49.780 1.00   24.62 ? 18   ILE J CG2 1 
ATOM   10150 C  CD1 . ILE J  1 19  ? 122.067 114.368 52.385 1.00   25.60 ? 18   ILE J CD1 1 
ATOM   10151 N  N   . ASN J  1 20  ? 119.647 111.631 49.119 1.00   26.98 ? 19   ASN J N   1 
ATOM   10152 C  CA  . ASN J  1 20  ? 119.130 111.162 47.825 1.00   27.95 ? 19   ASN J CA  1 
ATOM   10153 C  C   . ASN J  1 20  ? 119.735 111.928 46.661 1.00   27.61 ? 19   ASN J C   1 
ATOM   10154 O  O   . ASN J  1 20  ? 120.022 113.117 46.782 1.00   26.94 ? 19   ASN J O   1 
ATOM   10155 C  CB  . ASN J  1 20  ? 117.615 111.358 47.756 1.00   29.46 ? 19   ASN J CB  1 
ATOM   10156 C  CG  . ASN J  1 20  ? 116.888 110.686 48.908 1.00   30.09 ? 19   ASN J CG  1 
ATOM   10157 O  OD1 . ASN J  1 20  ? 116.395 111.355 49.814 1.00   32.43 ? 19   ASN J OD1 1 
ATOM   10158 N  ND2 . ASN J  1 20  ? 116.828 109.378 48.881 1.00   29.63 ? 19   ASN J ND2 1 
ATOM   10159 N  N   . PHE J  1 21  ? 119.925 111.235 45.542 1.00   27.56 ? 20   PHE J N   1 
ATOM   10160 C  CA  . PHE J  1 21  ? 120.407 111.839 44.315 1.00   28.41 ? 20   PHE J CA  1 
ATOM   10161 C  C   . PHE J  1 21  ? 119.419 111.538 43.198 1.00   30.13 ? 20   PHE J C   1 
ATOM   10162 O  O   . PHE J  1 21  ? 118.909 110.414 43.083 1.00   29.21 ? 20   PHE J O   1 
ATOM   10163 C  CB  . PHE J  1 21  ? 121.765 111.272 43.898 1.00   27.96 ? 20   PHE J CB  1 
ATOM   10164 C  CG  . PHE J  1 21  ? 122.840 111.404 44.941 1.00   27.07 ? 20   PHE J CG  1 
ATOM   10165 C  CD1 . PHE J  1 21  ? 122.860 110.565 46.047 1.00   26.79 ? 20   PHE J CD1 1 
ATOM   10166 C  CD2 . PHE J  1 21  ? 123.861 112.330 44.789 1.00   26.48 ? 20   PHE J CD2 1 
ATOM   10167 C  CE1 . PHE J  1 21  ? 123.867 110.674 46.997 1.00   26.32 ? 20   PHE J CE1 1 
ATOM   10168 C  CE2 . PHE J  1 21  ? 124.871 112.435 45.734 1.00   26.09 ? 20   PHE J CE2 1 
ATOM   10169 C  CZ  . PHE J  1 21  ? 124.872 111.604 46.842 1.00   25.39 ? 20   PHE J CZ  1 
ATOM   10170 N  N   . GLU J  1 22  ? 119.168 112.536 42.365 1.00   31.52 ? 21   GLU J N   1 
ATOM   10171 C  CA  . GLU J  1 22  ? 118.361 112.330 41.178 1.00   34.21 ? 21   GLU J CA  1 
ATOM   10172 C  C   . GLU J  1 22  ? 118.956 113.083 40.015 1.00   34.66 ? 21   GLU J C   1 
ATOM   10173 O  O   . GLU J  1 22  ? 119.254 114.271 40.140 1.00   33.80 ? 21   GLU J O   1 
ATOM   10174 C  CB  . GLU J  1 22  ? 116.927 112.781 41.403 1.00   36.43 ? 21   GLU J CB  1 
ATOM   10175 C  CG  . GLU J  1 22  ? 116.039 112.458 40.219 1.00   39.66 ? 21   GLU J CG  1 
ATOM   10176 C  CD  . GLU J  1 22  ? 114.572 112.683 40.506 1.00   42.74 ? 21   GLU J CD  1 
ATOM   10177 O  OE1 . GLU J  1 22  ? 114.165 113.850 40.686 1.00   45.88 ? 21   GLU J OE1 1 
ATOM   10178 O  OE2 . GLU J  1 22  ? 113.825 111.687 40.526 1.00   47.15 ? 21   GLU J OE2 1 
ATOM   10179 N  N   . GLN J  1 23  ? 119.111 112.380 38.895 1.00   35.29 ? 22   GLN J N   1 
ATOM   10180 C  CA  . GLN J  1 23  ? 119.556 112.952 37.639 1.00   36.67 ? 22   GLN J CA  1 
ATOM   10181 C  C   . GLN J  1 23  ? 118.566 112.524 36.566 1.00   40.17 ? 22   GLN J C   1 
ATOM   10182 O  O   . GLN J  1 23  ? 118.578 111.364 36.133 1.00   41.63 ? 22   GLN J O   1 
ATOM   10183 C  CB  . GLN J  1 23  ? 120.949 112.439 37.290 1.00   35.38 ? 22   GLN J CB  1 
ATOM   10184 C  CG  . GLN J  1 23  ? 121.582 113.130 36.091 1.00   35.43 ? 22   GLN J CG  1 
ATOM   10185 C  CD  . GLN J  1 23  ? 122.997 112.660 35.829 1.00   34.40 ? 22   GLN J CD  1 
ATOM   10186 O  OE1 . GLN J  1 23  ? 123.297 111.492 35.993 1.00   33.94 ? 22   GLN J OE1 1 
ATOM   10187 N  NE2 . GLN J  1 23  ? 123.879 113.577 35.444 1.00   34.19 ? 22   GLN J NE2 1 
ATOM   10188 N  N   . LYS J  1 24  ? 117.712 113.456 36.143 1.00   43.83 ? 23   LYS J N   1 
ATOM   10189 C  CA  . LYS J  1 24  ? 116.631 113.161 35.183 1.00   47.70 ? 23   LYS J CA  1 
ATOM   10190 C  C   . LYS J  1 24  ? 117.164 112.969 33.764 1.00   50.56 ? 23   LYS J C   1 
ATOM   10191 O  O   . LYS J  1 24  ? 116.668 112.130 33.015 1.00   54.08 ? 23   LYS J O   1 
ATOM   10192 C  CB  . LYS J  1 24  ? 115.583 114.285 35.187 1.00   48.22 ? 23   LYS J CB  1 
ATOM   10193 C  CG  . LYS J  1 24  ? 114.711 114.334 36.434 0.10   47.79 ? 23   LYS J CG  1 
ATOM   10194 C  CD  . LYS J  1 24  ? 113.602 113.294 36.395 0.10   48.47 ? 23   LYS J CD  1 
ATOM   10195 C  CE  . LYS J  1 24  ? 112.513 113.607 37.408 0.10   48.57 ? 23   LYS J CE  1 
ATOM   10196 N  NZ  . LYS J  1 24  ? 111.321 112.734 37.234 0.10   49.44 ? 23   LYS J NZ  1 
ATOM   10197 N  N   . GLU J  1 25  ? 118.178 113.747 33.406 1.00   52.47 ? 24   GLU J N   1 
ATOM   10198 C  CA  . GLU J  1 25  ? 118.753 113.714 32.073 1.00   54.89 ? 24   GLU J CA  1 
ATOM   10199 C  C   . GLU J  1 25  ? 120.221 113.330 32.173 1.00   54.64 ? 24   GLU J C   1 
ATOM   10200 O  O   . GLU J  1 25  ? 120.929 113.833 33.043 1.00   56.24 ? 24   GLU J O   1 
ATOM   10201 C  CB  . GLU J  1 25  ? 118.614 115.107 31.452 1.00   56.47 ? 24   GLU J CB  1 
ATOM   10202 C  CG  . GLU J  1 25  ? 118.408 115.126 29.943 1.00   59.42 ? 24   GLU J CG  1 
ATOM   10203 C  CD  . GLU J  1 25  ? 118.254 116.535 29.406 0.50   59.03 ? 24   GLU J CD  1 
ATOM   10204 O  OE1 . GLU J  1 25  ? 117.591 117.352 30.080 0.50   58.15 ? 24   GLU J OE1 1 
ATOM   10205 O  OE2 . GLU J  1 25  ? 118.794 116.825 28.316 0.50   59.21 ? 24   GLU J OE2 1 
ATOM   10206 N  N   . SER J  1 26  ? 120.695 112.450 31.296 1.00   55.59 ? 25   SER J N   1 
ATOM   10207 C  CA  . SER J  1 26  ? 122.119 112.083 31.293 1.00   57.11 ? 25   SER J CA  1 
ATOM   10208 C  C   . SER J  1 26  ? 122.934 113.335 31.040 1.00   57.01 ? 25   SER J C   1 
ATOM   10209 O  O   . SER J  1 26  ? 122.493 114.213 30.293 1.00   60.28 ? 25   SER J O   1 
ATOM   10210 C  CB  . SER J  1 26  ? 122.432 111.047 30.215 1.00   59.40 ? 25   SER J CB  1 
ATOM   10211 O  OG  . SER J  1 26  ? 121.817 109.802 30.500 1.00   62.85 ? 25   SER J OG  1 
ATOM   10212 N  N   . ASN J  1 27  ? 124.106 113.429 31.668 1.00   54.31 ? 26   ASN J N   1 
ATOM   10213 C  CA  . ASN J  1 27  ? 124.941 114.649 31.617 1.00   54.72 ? 26   ASN J CA  1 
ATOM   10214 C  C   . ASN J  1 27  ? 124.288 115.915 32.205 1.00   53.35 ? 26   ASN J C   1 
ATOM   10215 O  O   . ASN J  1 27  ? 124.914 116.978 32.203 1.00   52.73 ? 26   ASN J O   1 
ATOM   10216 C  CB  . ASN J  1 27  ? 125.423 114.958 30.176 1.00   56.40 ? 26   ASN J CB  1 
ATOM   10217 C  CG  . ASN J  1 27  ? 126.719 114.250 29.814 0.50   56.34 ? 26   ASN J CG  1 
ATOM   10218 O  OD1 . ASN J  1 27  ? 127.612 114.082 30.647 0.50   55.78 ? 26   ASN J OD1 1 
ATOM   10219 N  ND2 . ASN J  1 27  ? 126.835 113.853 28.551 0.50   56.73 ? 26   ASN J ND2 1 
ATOM   10220 N  N   . GLY J  1 28  ? 123.052 115.799 32.703 1.00   50.37 ? 27   GLY J N   1 
ATOM   10221 C  CA  . GLY J  1 28  ? 122.318 116.930 33.263 1.00   47.75 ? 27   GLY J CA  1 
ATOM   10222 C  C   . GLY J  1 28  ? 122.637 117.134 34.736 1.00   44.41 ? 27   GLY J C   1 
ATOM   10223 O  O   . GLY J  1 28  ? 123.432 116.394 35.306 1.00   44.10 ? 27   GLY J O   1 
ATOM   10224 N  N   . PRO J  1 29  ? 122.022 118.150 35.361 1.00   42.41 ? 28   PRO J N   1 
ATOM   10225 C  CA  . PRO J  1 29  ? 122.274 118.398 36.783 1.00   40.24 ? 28   PRO J CA  1 
ATOM   10226 C  C   . PRO J  1 29  ? 121.752 117.278 37.689 1.00   37.68 ? 28   PRO J C   1 
ATOM   10227 O  O   . PRO J  1 29  ? 120.862 116.515 37.303 1.00   37.93 ? 28   PRO J O   1 
ATOM   10228 C  CB  . PRO J  1 29  ? 121.548 119.723 37.058 1.00   41.02 ? 28   PRO J CB  1 
ATOM   10229 C  CG  . PRO J  1 29  ? 120.572 119.885 35.943 1.00   42.92 ? 28   PRO J CG  1 
ATOM   10230 C  CD  . PRO J  1 29  ? 121.129 119.156 34.759 1.00   43.14 ? 28   PRO J CD  1 
ATOM   10231 N  N   . VAL J  1 30  ? 122.340 117.170 38.875 1.00   34.03 ? 29   VAL J N   1 
ATOM   10232 C  CA  . VAL J  1 30  ? 121.926 116.186 39.861 1.00   32.10 ? 29   VAL J CA  1 
ATOM   10233 C  C   . VAL J  1 30  ? 121.437 116.911 41.103 1.00   31.27 ? 29   VAL J C   1 
ATOM   10234 O  O   . VAL J  1 30  ? 122.146 117.750 41.658 1.00   30.38 ? 29   VAL J O   1 
ATOM   10235 C  CB  . VAL J  1 30  ? 123.097 115.249 40.249 1.00   31.36 ? 29   VAL J CB  1 
ATOM   10236 C  CG1 . VAL J  1 30  ? 122.689 114.310 41.373 1.00   29.91 ? 29   VAL J CG1 1 
ATOM   10237 C  CG2 . VAL J  1 30  ? 123.568 114.458 39.044 1.00   31.09 ? 29   VAL J CG2 1 
ATOM   10238 N  N   . LYS J  1 31  ? 120.224 116.579 41.529 1.00   32.33 ? 30   LYS J N   1 
ATOM   10239 C  CA  . LYS J  1 31  ? 119.653 117.086 42.764 1.00   32.97 ? 30   LYS J CA  1 
ATOM   10240 C  C   . LYS J  1 31  ? 120.145 116.187 43.861 1.00   31.14 ? 30   LYS J C   1 
ATOM   10241 O  O   . LYS J  1 31  ? 120.123 114.967 43.714 1.00   31.43 ? 30   LYS J O   1 
ATOM   10242 C  CB  . LYS J  1 31  ? 118.121 117.057 42.746 1.00   35.94 ? 30   LYS J CB  1 
ATOM   10243 C  CG  . LYS J  1 31  ? 117.517 117.872 41.618 1.00   40.29 ? 30   LYS J CG  1 
ATOM   10244 C  CD  . LYS J  1 31  ? 115.989 117.913 41.658 1.00   42.99 ? 30   LYS J CD  1 
ATOM   10245 C  CE  . LYS J  1 31  ? 115.460 118.960 40.680 1.00   45.11 ? 30   LYS J CE  1 
ATOM   10246 N  NZ  . LYS J  1 31  ? 114.000 118.775 40.432 1.00   47.95 ? 30   LYS J NZ  1 
ATOM   10247 N  N   . VAL J  1 32  ? 120.602 116.804 44.947 1.00   28.90 ? 31   VAL J N   1 
ATOM   10248 C  CA  . VAL J  1 32  ? 121.113 116.101 46.098 1.00   27.83 ? 31   VAL J CA  1 
ATOM   10249 C  C   . VAL J  1 32  ? 120.366 116.659 47.285 1.00   28.07 ? 31   VAL J C   1 
ATOM   10250 O  O   . VAL J  1 32  ? 120.445 117.870 47.557 1.00   27.29 ? 31   VAL J O   1 
ATOM   10251 C  CB  . VAL J  1 32  ? 122.621 116.341 46.291 1.00   26.90 ? 31   VAL J CB  1 
ATOM   10252 C  CG1 . VAL J  1 32  ? 123.127 115.533 47.488 1.00   26.07 ? 31   VAL J CG1 1 
ATOM   10253 C  CG2 . VAL J  1 32  ? 123.382 116.029 45.007 1.00   26.10 ? 31   VAL J CG2 1 
ATOM   10254 N  N   . TRP J  1 33  ? 119.631 115.797 47.981 1.00   27.51 ? 32   TRP J N   1 
ATOM   10255 C  CA  . TRP J  1 33  ? 118.832 116.265 49.115 1.00   28.43 ? 32   TRP J CA  1 
ATOM   10256 C  C   . TRP J  1 33  ? 118.556 115.197 50.108 1.00   27.90 ? 32   TRP J C   1 
ATOM   10257 O  O   . TRP J  1 33  ? 118.637 114.002 49.807 1.00   28.04 ? 32   TRP J O   1 
ATOM   10258 C  CB  . TRP J  1 33  ? 117.493 116.860 48.659 1.00   29.21 ? 32   TRP J CB  1 
ATOM   10259 C  CG  . TRP J  1 33  ? 116.458 115.822 48.360 1.00   30.41 ? 32   TRP J CG  1 
ATOM   10260 C  CD1 . TRP J  1 33  ? 115.419 115.400 49.179 1.00   31.02 ? 32   TRP J CD1 1 
ATOM   10261 C  CD2 . TRP J  1 33  ? 116.356 114.992 47.156 1.00   31.23 ? 32   TRP J CD2 1 
ATOM   10262 N  NE1 . TRP J  1 33  ? 114.691 114.411 48.572 1.00   31.76 ? 32   TRP J NE1 1 
ATOM   10263 C  CE2 . TRP J  1 33  ? 115.194 114.126 47.355 1.00   31.88 ? 32   TRP J CE2 1 
ATOM   10264 C  CE3 . TRP J  1 33  ? 117.074 114.896 45.972 1.00   31.56 ? 32   TRP J CE3 1 
ATOM   10265 C  CZ2 . TRP J  1 33  ? 114.782 113.212 46.392 1.00   32.98 ? 32   TRP J CZ2 1 
ATOM   10266 C  CZ3 . TRP J  1 33  ? 116.655 113.965 45.006 1.00   32.36 ? 32   TRP J CZ3 1 
ATOM   10267 C  CH2 . TRP J  1 33  ? 115.538 113.136 45.218 1.00   32.90 ? 32   TRP J CH2 1 
ATOM   10268 N  N   . GLY J  1 34  ? 118.184 115.641 51.298 1.00   27.51 ? 33   GLY J N   1 
ATOM   10269 C  CA  . GLY J  1 34  ? 117.956 114.749 52.410 1.00   27.34 ? 33   GLY J CA  1 
ATOM   10270 C  C   . GLY J  1 34  ? 118.284 115.482 53.683 1.00   27.17 ? 33   GLY J C   1 
ATOM   10271 O  O   . GLY J  1 34  ? 118.197 116.710 53.740 1.00   25.63 ? 33   GLY J O   1 
ATOM   10272 N  N   . SER J  1 35  ? 118.669 114.718 54.698 1.00   27.65 ? 34   SER J N   1 
ATOM   10273 C  CA  . SER J  1 35  ? 118.787 115.235 56.043 1.00   28.70 ? 34   SER J CA  1 
ATOM   10274 C  C   . SER J  1 35  ? 119.845 114.460 56.822 1.00   28.55 ? 34   SER J C   1 
ATOM   10275 O  O   . SER J  1 35  ? 119.965 113.242 56.663 1.00   28.84 ? 34   SER J O   1 
ATOM   10276 C  CB  . SER J  1 35  ? 117.435 115.099 56.730 1.00   30.71 ? 34   SER J CB  1 
ATOM   10277 O  OG  . SER J  1 35  ? 117.538 115.442 58.099 1.00   33.14 ? 34   SER J OG  1 
ATOM   10278 N  N   . ILE J  1 36  ? 120.611 115.170 57.643 1.00   28.21 ? 35   ILE J N   1 
ATOM   10279 C  CA  . ILE J  1 36  ? 121.661 114.560 58.468 1.00   28.52 ? 35   ILE J CA  1 
ATOM   10280 C  C   . ILE J  1 36  ? 121.484 115.123 59.866 1.00   29.44 ? 35   ILE J C   1 
ATOM   10281 O  O   . ILE J  1 36  ? 121.242 116.321 60.008 1.00   29.97 ? 35   ILE J O   1 
ATOM   10282 C  CB  . ILE J  1 36  ? 123.077 114.931 57.954 1.00   27.30 ? 35   ILE J CB  1 
ATOM   10283 C  CG1 . ILE J  1 36  ? 123.283 114.412 56.522 1.00   26.93 ? 35   ILE J CG1 1 
ATOM   10284 C  CG2 . ILE J  1 36  ? 124.152 114.404 58.909 1.00   26.79 ? 35   ILE J CG2 1 
ATOM   10285 C  CD1 . ILE J  1 36  ? 124.406 115.076 55.738 1.00   25.49 ? 35   ILE J CD1 1 
ATOM   10286 N  N   . LYS J  1 37  ? 121.574 114.286 60.895 1.00   29.81 ? 36   LYS J N   1 
ATOM   10287 C  CA  . LYS J  1 37  ? 121.410 114.776 62.276 1.00   30.69 ? 36   LYS J CA  1 
ATOM   10288 C  C   . LYS J  1 37  ? 122.641 114.484 63.091 1.00   30.33 ? 36   LYS J C   1 
ATOM   10289 O  O   . LYS J  1 37  ? 123.562 113.809 62.604 1.00   29.69 ? 36   LYS J O   1 
ATOM   10290 C  CB  . LYS J  1 37  ? 120.153 114.198 62.954 1.00   31.67 ? 36   LYS J CB  1 
ATOM   10291 C  CG  . LYS J  1 37  ? 120.191 112.709 63.239 1.00   33.03 ? 36   LYS J CG  1 
ATOM   10292 C  CD  . LYS J  1 37  ? 118.815 112.204 63.685 1.00   34.71 ? 36   LYS J CD  1 
ATOM   10293 C  CE  . LYS J  1 37  ? 118.846 110.721 64.057 1.00   35.88 ? 36   LYS J CE  1 
ATOM   10294 N  NZ  . LYS J  1 37  ? 117.495 110.206 64.455 1.00   37.77 ? 36   LYS J NZ  1 
ATOM   10295 N  N   . GLY J  1 38  ? 122.662 115.006 64.321 1.00   30.81 ? 37   GLY J N   1 
ATOM   10296 C  CA  . GLY J  1 38  ? 123.759 114.765 65.259 1.00   31.07 ? 37   GLY J CA  1 
ATOM   10297 C  C   . GLY J  1 38  ? 125.001 115.606 65.013 1.00   31.10 ? 37   GLY J C   1 
ATOM   10298 O  O   . GLY J  1 38  ? 126.073 115.306 65.563 1.00   31.38 ? 37   GLY J O   1 
ATOM   10299 N  N   . LEU J  1 39  ? 124.860 116.650 64.191 1.00   30.28 ? 38   LEU J N   1 
ATOM   10300 C  CA  . LEU J  1 39  ? 125.944 117.593 63.874 1.00   30.35 ? 38   LEU J CA  1 
ATOM   10301 C  C   . LEU J  1 39  ? 125.959 118.780 64.843 1.00   31.66 ? 38   LEU J C   1 
ATOM   10302 O  O   . LEU J  1 39  ? 124.917 119.168 65.356 1.00   31.45 ? 38   LEU J O   1 
ATOM   10303 C  CB  . LEU J  1 39  ? 125.743 118.164 62.457 1.00   29.41 ? 38   LEU J CB  1 
ATOM   10304 C  CG  . LEU J  1 39  ? 125.787 117.141 61.307 1.00   28.42 ? 38   LEU J CG  1 
ATOM   10305 C  CD1 . LEU J  1 39  ? 125.198 117.720 60.030 1.00   27.26 ? 38   LEU J CD1 1 
ATOM   10306 C  CD2 . LEU J  1 39  ? 127.219 116.669 61.105 1.00   27.20 ? 38   LEU J CD2 1 
ATOM   10307 N  N   . THR J  1 40  ? 127.131 119.374 65.059 1.00   31.25 ? 39   THR J N   1 
ATOM   10308 C  CA  . THR J  1 40  ? 127.200 120.682 65.727 1.00   31.88 ? 39   THR J CA  1 
ATOM   10309 C  C   . THR J  1 40  ? 126.693 121.781 64.776 1.00   31.47 ? 39   THR J C   1 
ATOM   10310 O  O   . THR J  1 40  ? 126.884 121.705 63.548 1.00   31.17 ? 39   THR J O   1 
ATOM   10311 C  CB  . THR J  1 40  ? 128.640 121.027 66.129 1.00   32.15 ? 39   THR J CB  1 
ATOM   10312 O  OG1 . THR J  1 40  ? 129.463 121.043 64.943 1.00   32.57 ? 39   THR J OG1 1 
ATOM   10313 C  CG2 . THR J  1 40  ? 129.183 119.983 67.111 1.00   32.04 ? 39   THR J CG2 1 
ATOM   10314 N  N   . GLU J  1 41  ? 126.082 122.815 65.333 1.00   31.24 ? 40   GLU J N   1 
ATOM   10315 C  CA  . GLU J  1 41  ? 125.502 123.883 64.517 1.00   31.32 ? 40   GLU J CA  1 
ATOM   10316 C  C   . GLU J  1 41  ? 126.565 124.520 63.642 1.00   29.68 ? 40   GLU J C   1 
ATOM   10317 O  O   . GLU J  1 41  ? 127.692 124.687 64.069 1.00   29.69 ? 40   GLU J O   1 
ATOM   10318 C  CB  . GLU J  1 41  ? 124.874 124.966 65.398 1.00   32.43 ? 40   GLU J CB  1 
ATOM   10319 C  CG  . GLU J  1 41  ? 124.131 126.032 64.596 1.00   32.98 ? 40   GLU J CG  1 
ATOM   10320 C  CD  . GLU J  1 41  ? 123.418 127.058 65.462 1.00   34.38 ? 40   GLU J CD  1 
ATOM   10321 O  OE1 . GLU J  1 41  ? 123.552 126.980 66.702 1.00   34.72 ? 40   GLU J OE1 1 
ATOM   10322 O  OE2 . GLU J  1 41  ? 122.722 127.934 64.882 1.00   35.25 ? 40   GLU J OE2 1 
ATOM   10323 N  N   . GLY J  1 42  ? 126.182 124.884 62.425 1.00   29.15 ? 41   GLY J N   1 
ATOM   10324 C  CA  . GLY J  1 42  ? 127.074 125.565 61.497 1.00   28.03 ? 41   GLY J CA  1 
ATOM   10325 C  C   . GLY J  1 42  ? 127.474 124.685 60.322 1.00   27.28 ? 41   GLY J C   1 
ATOM   10326 O  O   . GLY J  1 42  ? 126.794 123.690 60.005 1.00   26.88 ? 41   GLY J O   1 
ATOM   10327 N  N   . LEU J  1 43  ? 128.590 125.051 59.697 1.00   26.03 ? 42   LEU J N   1 
ATOM   10328 C  CA  . LEU J  1 43  ? 128.962 124.539 58.383 1.00   25.45 ? 42   LEU J CA  1 
ATOM   10329 C  C   . LEU J  1 43  ? 129.762 123.247 58.504 1.00   24.56 ? 42   LEU J C   1 
ATOM   10330 O  O   . LEU J  1 43  ? 130.598 123.109 59.399 1.00   24.56 ? 42   LEU J O   1 
ATOM   10331 C  CB  . LEU J  1 43  ? 129.791 125.571 57.606 1.00   25.00 ? 42   LEU J CB  1 
ATOM   10332 C  CG  . LEU J  1 43  ? 129.089 126.835 57.078 1.00   25.74 ? 42   LEU J CG  1 
ATOM   10333 C  CD1 . LEU J  1 43  ? 130.086 127.817 56.459 1.00   24.41 ? 42   LEU J CD1 1 
ATOM   10334 C  CD2 . LEU J  1 43  ? 128.008 126.481 56.070 1.00   25.41 ? 42   LEU J CD2 1 
ATOM   10335 N  N   . HIS J  1 44  ? 129.523 122.319 57.577 1.00   23.36 ? 43   HIS J N   1 
ATOM   10336 C  CA  . HIS J  1 44  ? 130.286 121.076 57.539 1.00   22.77 ? 43   HIS J CA  1 
ATOM   10337 C  C   . HIS J  1 44  ? 130.600 120.706 56.134 1.00   22.07 ? 43   HIS J C   1 
ATOM   10338 O  O   . HIS J  1 44  ? 129.702 120.631 55.300 1.00   21.41 ? 43   HIS J O   1 
ATOM   10339 C  CB  . HIS J  1 44  ? 129.474 119.960 58.166 1.00   22.92 ? 43   HIS J CB  1 
ATOM   10340 C  CG  . HIS J  1 44  ? 129.270 120.115 59.647 1.00   24.27 ? 43   HIS J CG  1 
ATOM   10341 N  ND1 . HIS J  1 44  ? 130.135 119.613 60.563 1.00   25.10 ? 43   HIS J ND1 1 
ATOM   10342 C  CD2 . HIS J  1 44  ? 128.269 120.754 60.363 1.00   24.83 ? 43   HIS J CD2 1 
ATOM   10343 C  CE1 . HIS J  1 44  ? 129.698 119.900 61.792 1.00   25.46 ? 43   HIS J CE1 1 
ATOM   10344 N  NE2 . HIS J  1 44  ? 128.561 120.610 61.674 1.00   25.83 ? 43   HIS J NE2 1 
ATOM   10345 N  N   . GLY J  1 45  ? 131.868 120.426 55.859 1.00   21.64 ? 44   GLY J N   1 
ATOM   10346 C  CA  . GLY J  1 45  ? 132.260 119.941 54.540 1.00   21.26 ? 44   GLY J CA  1 
ATOM   10347 C  C   . GLY J  1 45  ? 131.502 118.670 54.139 1.00   20.91 ? 44   GLY J C   1 
ATOM   10348 O  O   . GLY J  1 45  ? 131.243 117.790 54.959 1.00   20.47 ? 44   GLY J O   1 
ATOM   10349 N  N   . PHE J  1 46  ? 131.214 118.580 52.849 1.00   20.38 ? 45   PHE J N   1 
ATOM   10350 C  CA  . PHE J  1 46  ? 130.323 117.584 52.261 1.00   20.19 ? 45   PHE J CA  1 
ATOM   10351 C  C   . PHE J  1 46  ? 130.894 117.256 50.891 1.00   19.83 ? 45   PHE J C   1 
ATOM   10352 O  O   . PHE J  1 46  ? 130.892 118.112 49.987 1.00   19.24 ? 45   PHE J O   1 
ATOM   10353 C  CB  . PHE J  1 46  ? 128.954 118.232 52.119 1.00   20.46 ? 45   PHE J CB  1 
ATOM   10354 C  CG  . PHE J  1 46  ? 127.835 117.304 51.729 1.00   20.39 ? 45   PHE J CG  1 
ATOM   10355 C  CD1 . PHE J  1 46  ? 127.486 116.228 52.526 1.00   20.51 ? 45   PHE J CD1 1 
ATOM   10356 C  CD2 . PHE J  1 46  ? 127.059 117.588 50.620 1.00   20.29 ? 45   PHE J CD2 1 
ATOM   10357 C  CE1 . PHE J  1 46  ? 126.408 115.420 52.187 1.00   20.73 ? 45   PHE J CE1 1 
ATOM   10358 C  CE2 . PHE J  1 46  ? 125.981 116.790 50.286 1.00   20.66 ? 45   PHE J CE2 1 
ATOM   10359 C  CZ  . PHE J  1 46  ? 125.651 115.709 51.072 1.00   20.58 ? 45   PHE J CZ  1 
ATOM   10360 N  N   . HIS J  1 47  ? 131.402 116.028 50.748 1.00   19.74 ? 46   HIS J N   1 
ATOM   10361 C  CA  . HIS J  1 47  ? 132.133 115.622 49.551 1.00   19.90 ? 46   HIS J CA  1 
ATOM   10362 C  C   . HIS J  1 47  ? 131.931 114.178 49.170 1.00   19.87 ? 46   HIS J C   1 
ATOM   10363 O  O   . HIS J  1 47  ? 131.685 113.322 50.032 1.00   19.36 ? 46   HIS J O   1 
ATOM   10364 C  CB  . HIS J  1 47  ? 133.634 115.756 49.769 1.00   20.54 ? 46   HIS J CB  1 
ATOM   10365 C  CG  . HIS J  1 47  ? 134.071 117.037 50.411 1.00   20.62 ? 46   HIS J CG  1 
ATOM   10366 N  ND1 . HIS J  1 47  ? 134.853 117.050 51.476 1.00   21.10 ? 46   HIS J ND1 1 
ATOM   10367 C  CD2 . HIS J  1 47  ? 133.836 118.354 50.080 1.00   21.08 ? 46   HIS J CD2 1 
ATOM   10368 C  CE1 . HIS J  1 47  ? 135.118 118.302 51.836 1.00   21.63 ? 46   HIS J CE1 1 
ATOM   10369 N  NE2 . HIS J  1 47  ? 134.491 119.114 50.981 1.00   21.64 ? 46   HIS J NE2 1 
ATOM   10370 N  N   . VAL J  1 48  ? 132.089 113.912 47.880 1.00   19.92 ? 47   VAL J N   1 
ATOM   10371 C  CA  . VAL J  1 48  ? 132.226 112.560 47.342 1.00   20.52 ? 47   VAL J CA  1 
ATOM   10372 C  C   . VAL J  1 48  ? 133.709 112.201 47.361 1.00   20.81 ? 47   VAL J C   1 
ATOM   10373 O  O   . VAL J  1 48  ? 134.526 112.878 46.730 1.00   21.80 ? 47   VAL J O   1 
ATOM   10374 C  CB  . VAL J  1 48  ? 131.732 112.427 45.876 1.00   20.97 ? 47   VAL J CB  1 
ATOM   10375 C  CG1 . VAL J  1 48  ? 131.843 110.976 45.404 1.00   21.14 ? 47   VAL J CG1 1 
ATOM   10376 C  CG2 . VAL J  1 48  ? 130.293 112.928 45.719 1.00   20.79 ? 47   VAL J CG2 1 
ATOM   10377 N  N   . HIS J  1 49  ? 134.042 111.157 48.103 1.00   20.61 ? 48   HIS J N   1 
ATOM   10378 C  CA  . HIS J  1 49  ? 135.390 110.592 48.128 1.00   21.18 ? 48   HIS J CA  1 
ATOM   10379 C  C   . HIS J  1 49  ? 135.470 109.415 47.184 1.00   21.68 ? 48   HIS J C   1 
ATOM   10380 O  O   . HIS J  1 49  ? 134.453 108.781 46.863 1.00   21.88 ? 48   HIS J O   1 
ATOM   10381 C  CB  . HIS J  1 49  ? 135.741 110.151 49.535 1.00   20.77 ? 48   HIS J CB  1 
ATOM   10382 C  CG  . HIS J  1 49  ? 136.065 111.277 50.448 1.00   20.78 ? 48   HIS J CG  1 
ATOM   10383 N  ND1 . HIS J  1 49  ? 137.260 111.395 51.069 1.00   21.14 ? 48   HIS J ND1 1 
ATOM   10384 C  CD2 . HIS J  1 49  ? 135.305 112.372 50.844 1.00   20.53 ? 48   HIS J CD2 1 
ATOM   10385 C  CE1 . HIS J  1 49  ? 137.252 112.505 51.822 1.00   20.88 ? 48   HIS J CE1 1 
ATOM   10386 N  NE2 . HIS J  1 49  ? 136.053 113.089 51.693 1.00   20.58 ? 48   HIS J NE2 1 
ATOM   10387 N  N   . GLU J  1 50  ? 136.683 109.117 46.744 1.00   22.24 ? 49   GLU J N   1 
ATOM   10388 C  CA  . GLU J  1 50  ? 136.922 108.264 45.575 1.00   23.35 ? 49   GLU J CA  1 
ATOM   10389 C  C   . GLU J  1 50  ? 136.416 106.816 45.688 1.00   23.57 ? 49   GLU J C   1 
ATOM   10390 O  O   . GLU J  1 50  ? 135.874 106.255 44.714 1.00   23.93 ? 49   GLU J O   1 
ATOM   10391 C  CB  . GLU J  1 50  ? 138.426 108.243 45.281 1.00   24.52 ? 49   GLU J CB  1 
ATOM   10392 C  CG  . GLU J  1 50  ? 138.779 107.533 44.000 1.00   25.68 ? 49   GLU J CG  1 
ATOM   10393 C  CD  . GLU J  1 50  ? 140.251 107.635 43.656 1.00   26.91 ? 49   GLU J CD  1 
ATOM   10394 O  OE1 . GLU J  1 50  ? 141.075 108.091 44.493 1.00   27.35 ? 49   GLU J OE1 1 
ATOM   10395 O  OE2 . GLU J  1 50  ? 140.572 107.215 42.536 1.00   28.34 ? 49   GLU J OE2 1 
ATOM   10396 N  N   . PHE J  1 51  ? 136.604 106.219 46.860 1.00   23.71 ? 50   PHE J N   1 
ATOM   10397 C  CA  . PHE J  1 51  ? 136.354 104.796 47.049 1.00   24.49 ? 50   PHE J CA  1 
ATOM   10398 C  C   . PHE J  1 51  ? 135.176 104.472 47.964 1.00   24.30 ? 50   PHE J C   1 
ATOM   10399 O  O   . PHE J  1 51  ? 135.012 105.065 49.045 1.00   23.65 ? 50   PHE J O   1 
ATOM   10400 C  CB  . PHE J  1 51  ? 137.601 104.130 47.596 1.00   25.12 ? 50   PHE J CB  1 
ATOM   10401 C  CG  . PHE J  1 51  ? 138.815 104.325 46.730 1.00   26.27 ? 50   PHE J CG  1 
ATOM   10402 C  CD1 . PHE J  1 51  ? 138.845 103.834 45.420 1.00   26.58 ? 50   PHE J CD1 1 
ATOM   10403 C  CD2 . PHE J  1 51  ? 139.939 104.987 47.224 1.00   26.90 ? 50   PHE J CD2 1 
ATOM   10404 C  CE1 . PHE J  1 51  ? 139.967 104.010 44.629 1.00   27.52 ? 50   PHE J CE1 1 
ATOM   10405 C  CE2 . PHE J  1 51  ? 141.069 105.157 46.438 1.00   27.45 ? 50   PHE J CE2 1 
ATOM   10406 C  CZ  . PHE J  1 51  ? 141.081 104.662 45.139 1.00   27.99 ? 50   PHE J CZ  1 
ATOM   10407 N  N   . GLY J  1 52  ? 134.364 103.511 47.526 1.00   24.29 ? 51   GLY J N   1 
ATOM   10408 C  CA  . GLY J  1 52  ? 133.257 103.001 48.323 1.00   24.59 ? 51   GLY J CA  1 
ATOM   10409 C  C   . GLY J  1 52  ? 133.752 101.905 49.244 1.00   25.03 ? 51   GLY J C   1 
ATOM   10410 O  O   . GLY J  1 52  ? 133.182 100.814 49.290 1.00   25.22 ? 51   GLY J O   1 
ATOM   10411 N  N   . ASP J  1 53  ? 134.811 102.224 49.983 1.00   25.43 ? 52   ASP J N   1 
ATOM   10412 C  CA  . ASP J  1 53  ? 135.496 101.294 50.876 1.00   26.12 ? 52   ASP J CA  1 
ATOM   10413 C  C   . ASP J  1 53  ? 135.338 101.785 52.312 1.00   26.36 ? 52   ASP J C   1 
ATOM   10414 O  O   . ASP J  1 53  ? 135.933 102.795 52.720 1.00   25.98 ? 52   ASP J O   1 
ATOM   10415 C  CB  . ASP J  1 53  ? 136.985 101.222 50.517 1.00   26.25 ? 52   ASP J CB  1 
ATOM   10416 C  CG  . ASP J  1 53  ? 137.732 100.189 51.340 1.00   26.74 ? 52   ASP J CG  1 
ATOM   10417 O  OD1 . ASP J  1 53  ? 137.249 99.855  52.459 1.00   25.56 ? 52   ASP J OD1 1 
ATOM   10418 O  OD2 . ASP J  1 53  ? 138.794 99.718  50.860 1.00   26.82 ? 52   ASP J OD2 1 
ATOM   10419 N  N   . ASN J  1 54  ? 134.504 101.084 53.061 1.00   27.40 ? 53   ASN J N   1 
ATOM   10420 C  CA  . ASN J  1 54  ? 134.254 101.403 54.460 1.00   28.54 ? 53   ASN J CA  1 
ATOM   10421 C  C   . ASN J  1 54  ? 134.851 100.361 55.418 1.00   28.01 ? 53   ASN J C   1 
ATOM   10422 O  O   . ASN J  1 54  ? 134.447 100.279 56.581 1.00   28.63 ? 53   ASN J O   1 
ATOM   10423 C  CB  . ASN J  1 54  ? 132.745 101.502 54.678 1.00   30.54 ? 53   ASN J CB  1 
ATOM   10424 C  CG  . ASN J  1 54  ? 132.389 101.960 56.078 1.00   33.50 ? 53   ASN J CG  1 
ATOM   10425 O  OD1 . ASN J  1 54  ? 131.695 101.246 56.835 1.00   36.79 ? 53   ASN J OD1 1 
ATOM   10426 N  ND2 . ASN J  1 54  ? 132.874 103.137 56.442 1.00   33.47 ? 53   ASN J ND2 1 
ATOM   10427 N  N   . THR J  1 55  ? 135.819 99.588  54.937 1.00   27.65 ? 54   THR J N   1 
ATOM   10428 C  CA  . THR J  1 55  ? 136.429 98.522  55.735 1.00   28.51 ? 54   THR J CA  1 
ATOM   10429 C  C   . THR J  1 55  ? 137.078 99.048  57.014 1.00   29.59 ? 54   THR J C   1 
ATOM   10430 O  O   . THR J  1 55  ? 136.951 98.423  58.066 1.00   30.01 ? 54   THR J O   1 
ATOM   10431 C  CB  . THR J  1 55  ? 137.424 97.642  54.911 1.00   27.62 ? 54   THR J CB  1 
ATOM   10432 O  OG1 . THR J  1 55  ? 138.441 98.453  54.317 1.00   27.34 ? 54   THR J OG1 1 
ATOM   10433 C  CG2 . THR J  1 55  ? 136.689 96.882  53.805 1.00   26.82 ? 54   THR J CG2 1 
ATOM   10434 N  N   . ALA J  1 56  ? 137.753 100.196 56.950 1.00   29.95 ? 55   ALA J N   1 
ATOM   10435 C  CA  . ALA J  1 56  ? 138.306 100.794 58.186 1.00   31.21 ? 55   ALA J CA  1 
ATOM   10436 C  C   . ALA J  1 56  ? 137.531 102.058 58.585 1.00   31.43 ? 55   ALA J C   1 
ATOM   10437 O  O   . ALA J  1 56  ? 138.110 103.002 59.105 1.00   33.64 ? 55   ALA J O   1 
ATOM   10438 C  CB  . ALA J  1 56  ? 139.803 101.102 58.027 1.00   30.88 ? 55   ALA J CB  1 
ATOM   10439 N  N   . GLY J  1 57  ? 136.221 102.075 58.357 1.00   30.33 ? 56   GLY J N   1 
ATOM   10440 C  CA  . GLY J  1 57  ? 135.444 103.300 58.538 1.00   29.42 ? 56   GLY J CA  1 
ATOM   10441 C  C   . GLY J  1 57  ? 135.662 104.272 57.387 1.00   28.82 ? 56   GLY J C   1 
ATOM   10442 O  O   . GLY J  1 57  ? 136.111 103.880 56.301 1.00   29.11 ? 56   GLY J O   1 
ATOM   10443 N  N   . CYS J  1 58  ? 135.371 105.551 57.622 1.00   27.56 ? 57   CYS J N   1 
ATOM   10444 C  CA  . CYS J  1 58  ? 135.435 106.559 56.559 1.00   26.34 ? 57   CYS J CA  1 
ATOM   10445 C  C   . CYS J  1 58  ? 136.849 106.822 56.013 1.00   26.26 ? 57   CYS J C   1 
ATOM   10446 O  O   . CYS J  1 58  ? 137.005 107.310 54.878 1.00   25.63 ? 57   CYS J O   1 
ATOM   10447 C  CB  . CYS J  1 58  ? 134.805 107.854 57.057 1.00   26.34 ? 57   CYS J CB  1 
ATOM   10448 S  SG  . CYS J  1 58  ? 133.106 107.653 57.670 1.00   26.74 ? 57   CYS J SG  1 
ATOM   10449 N  N   . THR J  1 59  ? 137.869 106.507 56.809 1.00   26.52 ? 58   THR J N   1 
ATOM   10450 C  CA  . THR J  1 59  ? 139.265 106.630 56.389 1.00   27.62 ? 58   THR J CA  1 
ATOM   10451 C  C   . THR J  1 59  ? 139.552 105.856 55.126 1.00   26.94 ? 58   THR J C   1 
ATOM   10452 O  O   . THR J  1 59  ? 140.356 106.283 54.319 1.00   26.67 ? 58   THR J O   1 
ATOM   10453 C  CB  . THR J  1 59  ? 140.250 106.105 57.466 1.00   29.69 ? 58   THR J CB  1 
ATOM   10454 O  OG1 . THR J  1 59  ? 139.971 106.764 58.705 1.00   31.37 ? 58   THR J OG1 1 
ATOM   10455 C  CG2 . THR J  1 59  ? 141.717 106.377 57.061 1.00   29.44 ? 58   THR J CG2 1 
ATOM   10456 N  N   . SER J  1 60  ? 138.889 104.719 54.952 1.00   26.68 ? 59   SER J N   1 
ATOM   10457 C  CA  . SER J  1 60  ? 139.133 103.869 53.792 1.00   26.73 ? 59   SER J CA  1 
ATOM   10458 C  C   . SER J  1 60  ? 138.630 104.445 52.482 1.00   25.14 ? 59   SER J C   1 
ATOM   10459 O  O   . SER J  1 60  ? 138.972 103.930 51.416 1.00   25.76 ? 59   SER J O   1 
ATOM   10460 C  CB  . SER J  1 60  ? 138.470 102.512 53.995 1.00   27.00 ? 59   SER J CB  1 
ATOM   10461 O  OG  . SER J  1 60  ? 138.797 102.008 55.260 1.00   29.66 ? 59   SER J OG  1 
ATOM   10462 N  N   . ALA J  1 61  ? 137.793 105.470 52.546 1.00   23.90 ? 60   ALA J N   1 
ATOM   10463 C  CA  . ALA J  1 61  ? 137.193 106.070 51.327 1.00   23.36 ? 60   ALA J CA  1 
ATOM   10464 C  C   . ALA J  1 61  ? 138.193 106.776 50.400 1.00   23.66 ? 60   ALA J C   1 
ATOM   10465 O  O   . ALA J  1 61  ? 137.868 107.111 49.239 1.00   23.67 ? 60   ALA J O   1 
ATOM   10466 C  CB  . ALA J  1 61  ? 136.088 107.030 51.708 1.00   22.44 ? 60   ALA J CB  1 
ATOM   10467 N  N   . GLY J  1 62  ? 139.394 107.028 50.908 1.00   23.58 ? 61   GLY J N   1 
ATOM   10468 C  CA  . GLY J  1 62  ? 140.420 107.703 50.131 1.00   23.65 ? 61   GLY J CA  1 
ATOM   10469 C  C   . GLY J  1 62  ? 140.133 109.194 50.054 1.00   23.32 ? 61   GLY J C   1 
ATOM   10470 O  O   . GLY J  1 62  ? 139.316 109.708 50.826 1.00   21.56 ? 61   GLY J O   1 
ATOM   10471 N  N   . PRO J  1 63  ? 140.792 109.889 49.105 1.00   23.47 ? 62   PRO J N   1 
ATOM   10472 C  CA  . PRO J  1 63  ? 140.726 111.343 48.945 1.00   23.47 ? 62   PRO J CA  1 
ATOM   10473 C  C   . PRO J  1 63  ? 139.482 111.777 48.171 1.00   23.36 ? 62   PRO J C   1 
ATOM   10474 O  O   . PRO J  1 63  ? 138.624 110.943 47.901 1.00   22.94 ? 62   PRO J O   1 
ATOM   10475 C  CB  . PRO J  1 63  ? 142.021 111.687 48.174 1.00   24.00 ? 62   PRO J CB  1 
ATOM   10476 C  CG  . PRO J  1 63  ? 142.547 110.391 47.643 1.00   24.98 ? 62   PRO J CG  1 
ATOM   10477 C  CD  . PRO J  1 63  ? 141.646 109.261 48.086 1.00   24.22 ? 62   PRO J CD  1 
ATOM   10478 N  N   . HIS J  1 64  ? 139.376 113.060 47.820 1.00   23.11 ? 63   HIS J N   1 
ATOM   10479 C  CA  . HIS J  1 64  ? 138.194 113.540 47.087 1.00   23.46 ? 63   HIS J CA  1 
ATOM   10480 C  C   . HIS J  1 64  ? 138.195 112.941 45.723 1.00   23.71 ? 63   HIS J C   1 
ATOM   10481 O  O   . HIS J  1 64  ? 139.244 112.781 45.140 1.00   24.78 ? 63   HIS J O   1 
ATOM   10482 C  CB  . HIS J  1 64  ? 138.144 115.069 46.996 1.00   23.36 ? 63   HIS J CB  1 
ATOM   10483 C  CG  . HIS J  1 64  ? 137.907 115.737 48.312 1.00   23.62 ? 63   HIS J CG  1 
ATOM   10484 N  ND1 . HIS J  1 64  ? 137.902 117.074 48.462 1.00   23.12 ? 63   HIS J ND1 1 
ATOM   10485 C  CD2 . HIS J  1 64  ? 137.697 115.190 49.585 1.00   23.59 ? 63   HIS J CD2 1 
ATOM   10486 C  CE1 . HIS J  1 64  ? 137.692 117.372 49.761 1.00   23.34 ? 63   HIS J CE1 1 
ATOM   10487 N  NE2 . HIS J  1 64  ? 137.561 116.217 50.446 1.00   23.61 ? 63   HIS J NE2 1 
ATOM   10488 N  N   . PHE J  1 65  ? 137.024 112.576 45.210 1.00   24.36 ? 64   PHE J N   1 
ATOM   10489 C  CA  . PHE J  1 65  ? 136.914 112.036 43.852 1.00   24.35 ? 64   PHE J CA  1 
ATOM   10490 C  C   . PHE J  1 65  ? 137.372 113.129 42.889 1.00   24.67 ? 64   PHE J C   1 
ATOM   10491 O  O   . PHE J  1 65  ? 136.794 114.229 42.854 1.00   24.74 ? 64   PHE J O   1 
ATOM   10492 C  CB  . PHE J  1 65  ? 135.473 111.596 43.603 1.00   24.33 ? 64   PHE J CB  1 
ATOM   10493 C  CG  . PHE J  1 65  ? 135.213 111.045 42.225 1.00   25.26 ? 64   PHE J CG  1 
ATOM   10494 C  CD1 . PHE J  1 65  ? 136.020 110.059 41.673 1.00   26.00 ? 64   PHE J CD1 1 
ATOM   10495 C  CD2 . PHE J  1 65  ? 134.113 111.472 41.499 1.00   25.85 ? 64   PHE J CD2 1 
ATOM   10496 C  CE1 . PHE J  1 65  ? 135.763 109.549 40.403 1.00   26.58 ? 64   PHE J CE1 1 
ATOM   10497 C  CE2 . PHE J  1 65  ? 133.844 110.952 40.235 1.00   26.29 ? 64   PHE J CE2 1 
ATOM   10498 C  CZ  . PHE J  1 65  ? 134.680 109.993 39.686 1.00   26.53 ? 64   PHE J CZ  1 
ATOM   10499 N  N   . ASN J  1 66  ? 138.426 112.842 42.130 1.00   25.22 ? 65   ASN J N   1 
ATOM   10500 C  CA  . ASN J  1 66  ? 139.115 113.851 41.318 1.00   25.81 ? 65   ASN J CA  1 
ATOM   10501 C  C   . ASN J  1 66  ? 139.650 113.327 39.963 1.00   26.94 ? 65   ASN J C   1 
ATOM   10502 O  O   . ASN J  1 66  ? 140.851 113.386 39.673 1.00   27.44 ? 65   ASN J O   1 
ATOM   10503 C  CB  . ASN J  1 66  ? 140.256 114.427 42.158 1.00   25.57 ? 65   ASN J CB  1 
ATOM   10504 C  CG  . ASN J  1 66  ? 140.955 115.599 41.499 1.00   25.78 ? 65   ASN J CG  1 
ATOM   10505 O  OD1 . ASN J  1 66  ? 140.389 116.310 40.628 1.00   25.27 ? 65   ASN J OD1 1 
ATOM   10506 N  ND2 . ASN J  1 66  ? 142.189 115.837 41.940 1.00   24.83 ? 65   ASN J ND2 1 
ATOM   10507 N  N   . PRO J  1 67  ? 138.754 112.840 39.108 1.00   27.45 ? 66   PRO J N   1 
ATOM   10508 C  CA  . PRO J  1 67  ? 139.216 112.228 37.869 1.00   28.64 ? 66   PRO J CA  1 
ATOM   10509 C  C   . PRO J  1 67  ? 139.931 113.197 36.921 1.00   29.98 ? 66   PRO J C   1 
ATOM   10510 O  O   . PRO J  1 67  ? 140.709 112.749 36.094 1.00   30.30 ? 66   PRO J O   1 
ATOM   10511 C  CB  . PRO J  1 67  ? 137.923 111.707 37.235 1.00   28.40 ? 66   PRO J CB  1 
ATOM   10512 C  CG  . PRO J  1 67  ? 136.871 112.634 37.755 1.00   27.69 ? 66   PRO J CG  1 
ATOM   10513 C  CD  . PRO J  1 67  ? 137.281 112.889 39.183 1.00   27.26 ? 66   PRO J CD  1 
ATOM   10514 N  N   . LEU J  1 68  ? 139.685 114.503 37.048 1.00   30.52 ? 67   LEU J N   1 
ATOM   10515 C  CA  . LEU J  1 68  ? 140.374 115.492 36.209 1.00   31.73 ? 67   LEU J CA  1 
ATOM   10516 C  C   . LEU J  1 68  ? 141.626 116.084 36.880 1.00   32.06 ? 67   LEU J C   1 
ATOM   10517 O  O   . LEU J  1 68  ? 142.177 117.052 36.389 1.00   33.67 ? 67   LEU J O   1 
ATOM   10518 C  CB  . LEU J  1 68  ? 139.415 116.614 35.787 1.00   31.80 ? 67   LEU J CB  1 
ATOM   10519 C  CG  . LEU J  1 68  ? 138.116 116.227 35.060 1.00   32.37 ? 67   LEU J CG  1 
ATOM   10520 C  CD1 . LEU J  1 68  ? 137.264 117.466 34.830 1.00   32.02 ? 67   LEU J CD1 1 
ATOM   10521 C  CD2 . LEU J  1 68  ? 138.361 115.525 33.720 1.00   33.85 ? 67   LEU J CD2 1 
ATOM   10522 N  N   . SER J  1 69  ? 142.079 115.521 37.993 1.00   32.33 ? 68   SER J N   1 
ATOM   10523 C  CA  . SER J  1 69  ? 143.308 116.005 38.645 1.00   33.19 ? 68   SER J CA  1 
ATOM   10524 C  C   . SER J  1 69  ? 143.364 117.525 38.858 1.00   34.06 ? 68   SER J C   1 
ATOM   10525 O  O   . SER J  1 69  ? 144.326 118.180 38.445 1.00   34.84 ? 68   SER J O   1 
ATOM   10526 C  CB  . SER J  1 69  ? 144.511 115.590 37.814 1.00   34.14 ? 68   SER J CB  1 
ATOM   10527 O  OG  . SER J  1 69  ? 144.395 114.231 37.496 1.00   35.22 ? 68   SER J OG  1 
ATOM   10528 N  N   . ARG J  1 70  ? 142.336 118.087 39.487 1.00   33.80 ? 69   ARG J N   1 
ATOM   10529 C  CA  . ARG J  1 70  ? 142.311 119.518 39.769 1.00   34.08 ? 69   ARG J CA  1 
ATOM   10530 C  C   . ARG J  1 70  ? 142.596 119.745 41.246 1.00   31.70 ? 69   ARG J C   1 
ATOM   10531 O  O   . ARG J  1 70  ? 142.689 118.794 42.015 1.00   29.55 ? 69   ARG J O   1 
ATOM   10532 C  CB  . ARG J  1 70  ? 140.939 120.091 39.432 1.00   36.64 ? 69   ARG J CB  1 
ATOM   10533 C  CG  . ARG J  1 70  ? 140.487 119.862 38.002 1.00   40.15 ? 69   ARG J CG  1 
ATOM   10534 C  CD  . ARG J  1 70  ? 140.791 121.038 37.089 1.00   44.20 ? 69   ARG J CD  1 
ATOM   10535 N  NE  . ARG J  1 70  ? 140.417 120.725 35.706 1.00   49.06 ? 69   ARG J NE  1 
ATOM   10536 C  CZ  . ARG J  1 70  ? 139.286 121.090 35.087 1.00   50.82 ? 69   ARG J CZ  1 
ATOM   10537 N  NH1 . ARG J  1 70  ? 138.357 121.823 35.697 1.00   50.67 ? 69   ARG J NH1 1 
ATOM   10538 N  NH2 . ARG J  1 70  ? 139.085 120.718 33.824 1.00   51.41 ? 69   ARG J NH2 1 
ATOM   10539 N  N   . LYS J  1 71  ? 142.705 121.008 41.646 1.00   30.83 ? 70   LYS J N   1 
ATOM   10540 C  CA  . LYS J  1 71  ? 142.823 121.355 43.066 1.00   29.84 ? 70   LYS J CA  1 
ATOM   10541 C  C   . LYS J  1 71  ? 141.435 121.444 43.692 1.00   27.37 ? 70   LYS J C   1 
ATOM   10542 O  O   . LYS J  1 71  ? 140.436 121.599 42.994 1.00   26.29 ? 70   LYS J O   1 
ATOM   10543 C  CB  . LYS J  1 71  ? 143.594 122.663 43.246 1.00   31.92 ? 70   LYS J CB  1 
ATOM   10544 C  CG  . LYS J  1 71  ? 145.071 122.536 42.875 1.00   34.21 ? 70   LYS J CG  1 
ATOM   10545 C  CD  . LYS J  1 71  ? 145.873 123.814 43.126 1.00   36.57 ? 70   LYS J CD  1 
ATOM   10546 C  CE  . LYS J  1 71  ? 145.275 125.032 42.435 1.00   38.23 ? 70   LYS J CE  1 
ATOM   10547 N  NZ  . LYS J  1 71  ? 146.217 126.196 42.365 1.00   41.18 ? 70   LYS J NZ  1 
ATOM   10548 N  N   . HIS J  1 72  ? 141.372 121.327 45.013 1.00   25.80 ? 71   HIS J N   1 
ATOM   10549 C  CA  . HIS J  1 72  ? 140.106 121.444 45.734 1.00   24.02 ? 71   HIS J CA  1 
ATOM   10550 C  C   . HIS J  1 72  ? 139.522 122.828 45.557 1.00   23.60 ? 71   HIS J C   1 
ATOM   10551 O  O   . HIS J  1 72  ? 140.246 123.807 45.551 1.00   23.36 ? 71   HIS J O   1 
ATOM   10552 C  CB  . HIS J  1 72  ? 140.340 121.186 47.220 1.00   23.49 ? 71   HIS J CB  1 
ATOM   10553 C  CG  . HIS J  1 72  ? 139.096 121.291 48.052 1.00   22.50 ? 71   HIS J CG  1 
ATOM   10554 N  ND1 . HIS J  1 72  ? 138.192 120.291 48.136 1.00   21.92 ? 71   HIS J ND1 1 
ATOM   10555 C  CD2 . HIS J  1 72  ? 138.608 122.337 48.830 1.00   21.95 ? 71   HIS J CD2 1 
ATOM   10556 C  CE1 . HIS J  1 72  ? 137.189 120.671 48.947 1.00   21.66 ? 71   HIS J CE1 1 
ATOM   10557 N  NE2 . HIS J  1 72  ? 137.436 121.931 49.360 1.00   21.67 ? 71   HIS J NE2 1 
ATOM   10558 N  N   . GLY J  1 73  ? 138.206 122.921 45.417 1.00   23.27 ? 72   GLY J N   1 
ATOM   10559 C  CA  . GLY J  1 73  ? 137.528 124.216 45.431 1.00   23.62 ? 72   GLY J CA  1 
ATOM   10560 C  C   . GLY J  1 73  ? 136.121 124.088 45.961 1.00   23.63 ? 72   GLY J C   1 
ATOM   10561 O  O   . GLY J  1 73  ? 135.743 123.041 46.516 1.00   22.96 ? 72   GLY J O   1 
ATOM   10562 N  N   . GLY J  1 74  ? 135.347 125.161 45.801 1.00   23.63 ? 73   GLY J N   1 
ATOM   10563 C  CA  . GLY J  1 74  ? 133.920 125.115 46.068 1.00   23.96 ? 73   GLY J CA  1 
ATOM   10564 C  C   . GLY J  1 74  ? 133.145 124.616 44.855 1.00   24.59 ? 73   GLY J C   1 
ATOM   10565 O  O   . GLY J  1 74  ? 133.654 124.627 43.737 1.00   24.37 ? 73   GLY J O   1 
ATOM   10566 N  N   . PRO J  1 75  ? 131.900 124.178 45.063 1.00   25.01 ? 74   PRO J N   1 
ATOM   10567 C  CA  . PRO J  1 75  ? 131.131 123.639 43.945 1.00   26.01 ? 74   PRO J CA  1 
ATOM   10568 C  C   . PRO J  1 75  ? 130.895 124.650 42.814 1.00   27.80 ? 74   PRO J C   1 
ATOM   10569 O  O   . PRO J  1 75  ? 130.698 124.248 41.674 1.00   28.39 ? 74   PRO J O   1 
ATOM   10570 C  CB  . PRO J  1 75  ? 129.814 123.218 44.590 1.00   25.78 ? 74   PRO J CB  1 
ATOM   10571 C  CG  . PRO J  1 75  ? 129.727 123.970 45.876 1.00   25.23 ? 74   PRO J CG  1 
ATOM   10572 C  CD  . PRO J  1 75  ? 131.139 124.188 46.321 1.00   25.00 ? 74   PRO J CD  1 
ATOM   10573 N  N   . LYS J  1 76  ? 130.927 125.945 43.125 1.00   28.98 ? 75   LYS J N   1 
ATOM   10574 C  CA  . LYS J  1 76  ? 130.733 126.990 42.116 1.00   31.03 ? 75   LYS J CA  1 
ATOM   10575 C  C   . LYS J  1 76  ? 132.004 127.268 41.304 1.00   30.72 ? 75   LYS J C   1 
ATOM   10576 O  O   . LYS J  1 76  ? 131.937 127.939 40.310 1.00   30.54 ? 75   LYS J O   1 
ATOM   10577 C  CB  . LYS J  1 76  ? 130.188 128.270 42.780 1.00   32.29 ? 75   LYS J CB  1 
ATOM   10578 C  CG  . LYS J  1 76  ? 128.797 128.047 43.374 1.00   34.26 ? 75   LYS J CG  1 
ATOM   10579 C  CD  . LYS J  1 76  ? 128.279 129.169 44.272 1.00   36.79 ? 75   LYS J CD  1 
ATOM   10580 C  CE  . LYS J  1 76  ? 126.796 128.926 44.621 1.00   38.61 ? 75   LYS J CE  1 
ATOM   10581 N  NZ  . LYS J  1 76  ? 126.093 128.768 44.424 0.0000 48.78 ? 75   LYS J NZ  1 
ATOM   10582 N  N   . ASP J  1 77  ? 133.148 126.731 41.719 1.00   30.10 ? 76   ASP J N   1 
ATOM   10583 C  CA  . ASP J  1 77  ? 134.411 127.018 41.070 1.00   31.07 ? 76   ASP J CA  1 
ATOM   10584 C  C   . ASP J  1 77  ? 134.679 126.126 39.847 1.00   32.86 ? 76   ASP J C   1 
ATOM   10585 O  O   . ASP J  1 77  ? 134.239 124.995 39.787 1.00   31.74 ? 76   ASP J O   1 
ATOM   10586 C  CB  . ASP J  1 77  ? 135.564 126.853 42.075 1.00   31.63 ? 76   ASP J CB  1 
ATOM   10587 C  CG  . ASP J  1 77  ? 135.470 127.823 43.251 1.00   31.24 ? 76   ASP J CG  1 
ATOM   10588 O  OD1 . ASP J  1 77  ? 134.924 128.912 43.060 1.00   32.22 ? 76   ASP J OD1 1 
ATOM   10589 O  OD2 . ASP J  1 77  ? 135.948 127.505 44.360 1.00   30.28 ? 76   ASP J OD2 1 
ATOM   10590 N  N   . GLU J  1 78  ? 135.424 126.656 38.880 1.00   34.28 ? 77   GLU J N   1 
ATOM   10591 C  CA  . GLU J  1 78  ? 135.921 125.858 37.770 1.00   36.24 ? 77   GLU J CA  1 
ATOM   10592 C  C   . GLU J  1 78  ? 137.043 124.945 38.260 1.00   33.59 ? 77   GLU J C   1 
ATOM   10593 O  O   . GLU J  1 78  ? 137.085 123.770 37.912 1.00   32.45 ? 77   GLU J O   1 
ATOM   10594 C  CB  . GLU J  1 78  ? 136.414 126.758 36.623 1.00   39.81 ? 77   GLU J CB  1 
ATOM   10595 C  CG  . GLU J  1 78  ? 136.729 126.006 35.329 1.00   43.73 ? 77   GLU J CG  1 
ATOM   10596 C  CD  . GLU J  1 78  ? 138.167 125.477 35.243 1.00   47.26 ? 77   GLU J CD  1 
ATOM   10597 O  OE1 . GLU J  1 78  ? 139.099 126.134 35.761 1.00   51.12 ? 77   GLU J OE1 1 
ATOM   10598 O  OE2 . GLU J  1 78  ? 138.387 124.405 34.628 1.00   50.76 ? 77   GLU J OE2 1 
ATOM   10599 N  N   . GLU J  1 79  ? 137.967 125.482 39.047 1.00   31.50 ? 78   GLU J N   1 
ATOM   10600 C  CA  . GLU J  1 79  ? 139.003 124.650 39.652 1.00   31.08 ? 78   GLU J CA  1 
ATOM   10601 C  C   . GLU J  1 79  ? 138.356 124.002 40.874 1.00   28.18 ? 78   GLU J C   1 
ATOM   10602 O  O   . GLU J  1 79  ? 138.186 124.634 41.907 1.00   27.89 ? 78   GLU J O   1 
ATOM   10603 C  CB  . GLU J  1 79  ? 140.263 125.461 40.012 1.00   33.03 ? 78   GLU J CB  1 
ATOM   10604 C  CG  . GLU J  1 79  ? 141.504 124.630 40.380 1.00   35.71 ? 78   GLU J CG  1 
ATOM   10605 C  CD  . GLU J  1 79  ? 142.139 123.857 39.199 1.00   38.65 ? 78   GLU J CD  1 
ATOM   10606 O  OE1 . GLU J  1 79  ? 141.666 123.992 38.037 1.00   43.59 ? 78   GLU J OE1 1 
ATOM   10607 O  OE2 . GLU J  1 79  ? 143.114 123.089 39.422 1.00   38.90 ? 78   GLU J OE2 1 
ATOM   10608 N  N   . ARG J  1 80  ? 137.932 122.754 40.716 1.00   26.43 ? 79   ARG J N   1 
ATOM   10609 C  CA  . ARG J  1 80  ? 137.402 121.960 41.826 1.00   24.93 ? 79   ARG J CA  1 
ATOM   10610 C  C   . ARG J  1 80  ? 137.622 120.496 41.537 1.00   24.43 ? 79   ARG J C   1 
ATOM   10611 O  O   . ARG J  1 80  ? 137.859 120.130 40.398 1.00   26.40 ? 79   ARG J O   1 
ATOM   10612 C  CB  . ARG J  1 80  ? 135.909 122.189 41.994 1.00   23.96 ? 79   ARG J CB  1 
ATOM   10613 C  CG  . ARG J  1 80  ? 135.102 121.880 40.744 1.00   24.08 ? 79   ARG J CG  1 
ATOM   10614 C  CD  . ARG J  1 80  ? 133.616 122.003 41.018 1.00   23.54 ? 79   ARG J CD  1 
ATOM   10615 N  NE  . ARG J  1 80  ? 133.049 120.744 41.478 1.00   23.00 ? 79   ARG J NE  1 
ATOM   10616 C  CZ  . ARG J  1 80  ? 131.747 120.497 41.594 1.00   22.48 ? 79   ARG J CZ  1 
ATOM   10617 N  NH1 . ARG J  1 80  ? 130.849 121.438 41.327 1.00   22.61 ? 79   ARG J NH1 1 
ATOM   10618 N  NH2 . ARG J  1 80  ? 131.345 119.296 41.976 1.00   22.17 ? 79   ARG J NH2 1 
ATOM   10619 N  N   . HIS J  1 81  ? 137.534 119.673 42.572 1.00   23.38 ? 80   HIS J N   1 
ATOM   10620 C  CA  . HIS J  1 81  ? 137.446 118.222 42.424 1.00   22.81 ? 80   HIS J CA  1 
ATOM   10621 C  C   . HIS J  1 81  ? 136.029 117.921 42.034 1.00   22.85 ? 80   HIS J C   1 
ATOM   10622 O  O   . HIS J  1 81  ? 135.105 118.630 42.498 1.00   23.20 ? 80   HIS J O   1 
ATOM   10623 C  CB  . HIS J  1 81  ? 137.717 117.522 43.755 1.00   21.99 ? 80   HIS J CB  1 
ATOM   10624 C  CG  . HIS J  1 81  ? 139.095 117.753 44.326 1.00   21.64 ? 80   HIS J CG  1 
ATOM   10625 N  ND1 . HIS J  1 81  ? 139.324 117.908 45.653 1.00   20.57 ? 80   HIS J ND1 1 
ATOM   10626 C  CD2 . HIS J  1 81  ? 140.336 117.803 43.710 1.00   22.19 ? 80   HIS J CD2 1 
ATOM   10627 C  CE1 . HIS J  1 81  ? 140.640 118.028 45.865 1.00   21.04 ? 80   HIS J CE1 1 
ATOM   10628 N  NE2 . HIS J  1 81  ? 141.263 117.982 44.681 1.00   21.95 ? 80   HIS J NE2 1 
ATOM   10629 N  N   . VAL J  1 82  ? 135.806 116.869 41.236 1.00   22.09 ? 81   VAL J N   1 
ATOM   10630 C  CA  . VAL J  1 82  ? 134.427 116.425 40.944 1.00   21.82 ? 81   VAL J CA  1 
ATOM   10631 C  C   . VAL J  1 82  ? 133.601 116.234 42.241 1.00   21.20 ? 81   VAL J C   1 
ATOM   10632 O  O   . VAL J  1 82  ? 132.455 116.650 42.313 1.00   21.42 ? 81   VAL J O   1 
ATOM   10633 C  CB  . VAL J  1 82  ? 134.400 115.140 40.083 1.00   22.22 ? 81   VAL J CB  1 
ATOM   10634 C  CG1 . VAL J  1 82  ? 133.025 114.472 40.139 1.00   21.94 ? 81   VAL J CG1 1 
ATOM   10635 C  CG2 . VAL J  1 82  ? 134.825 115.442 38.637 1.00   22.37 ? 81   VAL J CG2 1 
ATOM   10636 N  N   . GLY J  1 83  ? 134.188 115.644 43.273 1.00   20.64 ? 82   GLY J N   1 
ATOM   10637 C  CA  . GLY J  1 83  ? 133.468 115.418 44.522 1.00   20.65 ? 82   GLY J CA  1 
ATOM   10638 C  C   . GLY J  1 83  ? 133.203 116.602 45.450 1.00   20.33 ? 82   GLY J C   1 
ATOM   10639 O  O   . GLY J  1 83  ? 132.607 116.430 46.525 1.00   20.43 ? 82   GLY J O   1 
ATOM   10640 N  N   . ASP J  1 84  ? 133.634 117.797 45.061 1.00   20.49 ? 83   ASP J N   1 
ATOM   10641 C  CA  . ASP J  1 84  ? 133.513 118.978 45.909 1.00   20.24 ? 83   ASP J CA  1 
ATOM   10642 C  C   . ASP J  1 84  ? 132.095 119.529 45.908 1.00   20.63 ? 83   ASP J C   1 
ATOM   10643 O  O   . ASP J  1 84  ? 131.717 120.327 45.027 1.00   21.64 ? 83   ASP J O   1 
ATOM   10644 C  CB  . ASP J  1 84  ? 134.499 120.049 45.460 1.00   20.22 ? 83   ASP J CB  1 
ATOM   10645 C  CG  . ASP J  1 84  ? 135.944 119.676 45.775 1.00   20.57 ? 83   ASP J CG  1 
ATOM   10646 O  OD1 . ASP J  1 84  ? 136.166 118.676 46.493 1.00   20.22 ? 83   ASP J OD1 1 
ATOM   10647 O  OD2 . ASP J  1 84  ? 136.869 120.353 45.295 1.00   20.60 ? 83   ASP J OD2 1 
ATOM   10648 N  N   . LEU J  1 85  ? 131.299 119.124 46.887 1.00   20.11 ? 84   LEU J N   1 
ATOM   10649 C  CA  . LEU J  1 85  ? 129.947 119.661 46.976 1.00   20.48 ? 84   LEU J CA  1 
ATOM   10650 C  C   . LEU J  1 85  ? 129.802 120.763 47.998 1.00   20.30 ? 84   LEU J C   1 
ATOM   10651 O  O   . LEU J  1 85  ? 128.681 121.161 48.295 1.00   21.20 ? 84   LEU J O   1 
ATOM   10652 C  CB  . LEU J  1 85  ? 128.922 118.553 47.237 1.00   20.63 ? 84   LEU J CB  1 
ATOM   10653 C  CG  . LEU J  1 85  ? 128.857 117.486 46.139 1.00   20.89 ? 84   LEU J CG  1 
ATOM   10654 C  CD1 . LEU J  1 85  ? 127.976 116.324 46.580 1.00   20.70 ? 84   LEU J CD1 1 
ATOM   10655 C  CD2 . LEU J  1 85  ? 128.389 118.101 44.820 1.00   20.92 ? 84   LEU J CD2 1 
ATOM   10656 N  N   . GLY J  1 86  ? 130.920 121.274 48.504 1.00   19.83 ? 85   GLY J N   1 
ATOM   10657 C  CA  . GLY J  1 86  ? 130.909 122.429 49.384 1.00   20.25 ? 85   GLY J CA  1 
ATOM   10658 C  C   . GLY J  1 86  ? 130.547 122.094 50.827 1.00   20.38 ? 85   GLY J C   1 
ATOM   10659 O  O   . GLY J  1 86  ? 131.020 121.071 51.383 1.00   19.86 ? 85   GLY J O   1 
ATOM   10660 N  N   . ASN J  1 87  ? 129.723 122.965 51.430 1.00   20.09 ? 86   ASN J N   1 
ATOM   10661 C  CA  . ASN J  1 87  ? 129.249 122.782 52.787 1.00   20.19 ? 86   ASN J CA  1 
ATOM   10662 C  C   . ASN J  1 87  ? 127.762 122.483 52.876 1.00   20.68 ? 86   ASN J C   1 
ATOM   10663 O  O   . ASN J  1 87  ? 126.962 122.884 52.003 1.00   20.30 ? 86   ASN J O   1 
ATOM   10664 C  CB  . ASN J  1 87  ? 129.522 124.036 53.597 1.00   20.59 ? 86   ASN J CB  1 
ATOM   10665 C  CG  . ASN J  1 87  ? 130.996 124.230 53.894 1.00   20.87 ? 86   ASN J CG  1 
ATOM   10666 O  OD1 . ASN J  1 87  ? 131.604 123.417 54.593 1.00   21.49 ? 86   ASN J OD1 1 
ATOM   10667 N  ND2 . ASN J  1 87  ? 131.573 125.319 53.400 1.00   20.63 ? 86   ASN J ND2 1 
ATOM   10668 N  N   . VAL J  1 88  ? 127.400 121.797 53.961 1.00   20.79 ? 87   VAL J N   1 
ATOM   10669 C  CA  . VAL J  1 88  ? 126.018 121.723 54.423 1.00   21.43 ? 87   VAL J CA  1 
ATOM   10670 C  C   . VAL J  1 88  ? 125.937 122.421 55.787 1.00   21.92 ? 87   VAL J C   1 
ATOM   10671 O  O   . VAL J  1 88  ? 126.957 122.595 56.477 1.00   21.62 ? 87   VAL J O   1 
ATOM   10672 C  CB  . VAL J  1 88  ? 125.524 120.266 54.534 1.00   21.91 ? 87   VAL J CB  1 
ATOM   10673 C  CG1 . VAL J  1 88  ? 125.532 119.587 53.153 1.00   21.26 ? 87   VAL J CG1 1 
ATOM   10674 C  CG2 . VAL J  1 88  ? 126.366 119.508 55.554 1.00   20.80 ? 87   VAL J CG2 1 
ATOM   10675 N  N   . THR J  1 89  ? 124.724 122.814 56.178 1.00   22.55 ? 88   THR J N   1 
ATOM   10676 C  CA  . THR J  1 89  ? 124.524 123.646 57.353 1.00   23.41 ? 88   THR J CA  1 
ATOM   10677 C  C   . THR J  1 89  ? 123.601 122.968 58.368 1.00   24.86 ? 88   THR J C   1 
ATOM   10678 O  O   . THR J  1 89  ? 122.457 122.641 58.057 1.00   25.13 ? 88   THR J O   1 
ATOM   10679 C  CB  . THR J  1 89  ? 123.922 125.018 56.968 1.00   23.41 ? 88   THR J CB  1 
ATOM   10680 O  OG1 . THR J  1 89  ? 124.804 125.700 56.055 1.00   23.09 ? 88   THR J OG1 1 
ATOM   10681 C  CG2 . THR J  1 89  ? 123.704 125.890 58.224 1.00   23.73 ? 88   THR J CG2 1 
ATOM   10682 N  N   . ALA J  1 90  ? 124.102 122.787 59.585 1.00   26.11 ? 89   ALA J N   1 
ATOM   10683 C  CA  . ALA J  1 90  ? 123.318 122.219 60.664 1.00   28.10 ? 89   ALA J CA  1 
ATOM   10684 C  C   . ALA J  1 90  ? 122.662 123.335 61.472 1.00   30.23 ? 89   ALA J C   1 
ATOM   10685 O  O   . ALA J  1 90  ? 123.326 124.296 61.839 1.00   30.45 ? 89   ALA J O   1 
ATOM   10686 C  CB  . ALA J  1 90  ? 124.199 121.374 61.560 1.00   27.66 ? 89   ALA J CB  1 
ATOM   10687 N  N   . ASP J  1 91  ? 121.371 123.193 61.760 1.00   32.55 ? 90   ASP J N   1 
ATOM   10688 C  CA  . ASP J  1 91  ? 120.655 124.172 62.605 1.00   35.24 ? 90   ASP J CA  1 
ATOM   10689 C  C   . ASP J  1 91  ? 121.029 123.947 64.079 1.00   36.71 ? 90   ASP J C   1 
ATOM   10690 O  O   . ASP J  1 91  ? 121.856 123.080 64.400 1.00   34.50 ? 90   ASP J O   1 
ATOM   10691 C  CB  . ASP J  1 91  ? 119.127 124.101 62.381 1.00   36.25 ? 90   ASP J CB  1 
ATOM   10692 C  CG  . ASP J  1 91  ? 118.530 122.731 62.731 1.00   38.41 ? 90   ASP J CG  1 
ATOM   10693 O  OD1 . ASP J  1 91  ? 119.022 122.067 63.678 1.00   40.17 ? 90   ASP J OD1 1 
ATOM   10694 O  OD2 . ASP J  1 91  ? 117.572 122.304 62.049 1.00   39.57 ? 90   ASP J OD2 1 
ATOM   10695 N  N   . LYS J  1 92  ? 120.424 124.733 64.968 1.00   38.35 ? 91   LYS J N   1 
ATOM   10696 C  CA  . LYS J  1 92  ? 120.745 124.672 66.394 1.00   39.51 ? 91   LYS J CA  1 
ATOM   10697 C  C   . LYS J  1 92  ? 120.352 123.341 67.036 1.00   39.78 ? 91   LYS J C   1 
ATOM   10698 O  O   . LYS J  1 92  ? 120.841 123.017 68.113 1.00   40.88 ? 91   LYS J O   1 
ATOM   10699 C  CB  . LYS J  1 92  ? 120.110 125.851 67.155 1.00   41.34 ? 91   LYS J CB  1 
ATOM   10700 C  CG  . LYS J  1 92  ? 118.584 125.869 67.221 1.00   43.35 ? 91   LYS J CG  1 
ATOM   10701 C  CD  . LYS J  1 92  ? 118.077 127.131 67.943 1.00   45.97 ? 91   LYS J CD  1 
ATOM   10702 C  CE  . LYS J  1 92  ? 116.615 127.007 68.369 1.00   48.08 ? 91   LYS J CE  1 
ATOM   10703 N  NZ  . LYS J  1 92  ? 116.117 128.152 69.210 1.00   50.51 ? 91   LYS J NZ  1 
ATOM   10704 N  N   . ASP J  1 93  ? 119.486 122.572 66.376 1.00   39.73 ? 92   ASP J N   1 
ATOM   10705 C  CA  . ASP J  1 93  ? 119.135 121.212 66.823 1.00   40.04 ? 92   ASP J CA  1 
ATOM   10706 C  C   . ASP J  1 93  ? 120.084 120.123 66.287 1.00   37.90 ? 92   ASP J C   1 
ATOM   10707 O  O   . ASP J  1 93  ? 119.905 118.934 66.582 1.00   36.57 ? 92   ASP J O   1 
ATOM   10708 C  CB  . ASP J  1 93  ? 117.683 120.888 66.434 1.00   41.88 ? 92   ASP J CB  1 
ATOM   10709 C  CG  . ASP J  1 93  ? 116.665 121.768 67.175 1.00   45.64 ? 92   ASP J CG  1 
ATOM   10710 O  OD1 . ASP J  1 93  ? 116.932 122.185 68.324 1.00   46.86 ? 92   ASP J OD1 1 
ATOM   10711 O  OD2 . ASP J  1 93  ? 115.593 122.049 66.604 1.00   48.86 ? 92   ASP J OD2 1 
ATOM   10712 N  N   . GLY J  1 94  ? 121.087 120.523 65.509 1.00   35.18 ? 93   GLY J N   1 
ATOM   10713 C  CA  . GLY J  1 94  ? 122.041 119.570 64.932 1.00   33.49 ? 93   GLY J CA  1 
ATOM   10714 C  C   . GLY J  1 94  ? 121.589 118.893 63.649 1.00   32.18 ? 93   GLY J C   1 
ATOM   10715 O  O   . GLY J  1 94  ? 122.218 117.937 63.206 1.00   30.11 ? 93   GLY J O   1 
ATOM   10716 N  N   . VAL J  1 95  ? 120.501 119.387 63.053 1.00   32.58 ? 94   VAL J N   1 
ATOM   10717 C  CA  . VAL J  1 95  ? 119.965 118.829 61.814 1.00   32.25 ? 94   VAL J CA  1 
ATOM   10718 C  C   . VAL J  1 95  ? 120.386 119.692 60.619 1.00   31.89 ? 94   VAL J C   1 
ATOM   10719 O  O   . VAL J  1 95  ? 120.215 120.926 60.615 1.00   31.55 ? 94   VAL J O   1 
ATOM   10720 C  CB  . VAL J  1 95  ? 118.414 118.729 61.829 1.00   33.56 ? 94   VAL J CB  1 
ATOM   10721 C  CG1 . VAL J  1 95  ? 117.888 118.228 60.487 1.00   32.87 ? 94   VAL J CG1 1 
ATOM   10722 C  CG2 . VAL J  1 95  ? 117.931 117.812 62.949 1.00   34.66 ? 94   VAL J CG2 1 
ATOM   10723 N  N   . ALA J  1 96  ? 120.929 119.034 59.604 1.00   30.38 ? 95   ALA J N   1 
ATOM   10724 C  CA  . ALA J  1 96  ? 121.233 119.690 58.342 1.00   30.12 ? 95   ALA J CA  1 
ATOM   10725 C  C   . ALA J  1 96  ? 120.243 119.138 57.338 1.00   30.45 ? 95   ALA J C   1 
ATOM   10726 O  O   . ALA J  1 96  ? 120.306 117.958 56.999 1.00   30.84 ? 95   ALA J O   1 
ATOM   10727 C  CB  . ALA J  1 96  ? 122.666 119.408 57.903 1.00   27.93 ? 95   ALA J CB  1 
ATOM   10728 N  N   . ASP J  1 97  ? 119.302 119.974 56.909 1.00   30.72 ? 96   ASP J N   1 
ATOM   10729 C  CA  . ASP J  1 97  ? 118.491 119.671 55.742 1.00   31.43 ? 96   ASP J CA  1 
ATOM   10730 C  C   . ASP J  1 97  ? 119.373 120.028 54.587 1.00   31.04 ? 96   ASP J C   1 
ATOM   10731 O  O   . ASP J  1 97  ? 119.909 121.126 54.557 1.00   33.40 ? 96   ASP J O   1 
ATOM   10732 C  CB  . ASP J  1 97  ? 117.232 120.530 55.677 1.00   33.61 ? 96   ASP J CB  1 
ATOM   10733 C  CG  . ASP J  1 97  ? 116.285 120.262 56.829 1.00   35.95 ? 96   ASP J CG  1 
ATOM   10734 O  OD1 . ASP J  1 97  ? 115.957 119.080 57.099 1.00   36.51 ? 96   ASP J OD1 1 
ATOM   10735 O  OD2 . ASP J  1 97  ? 115.904 121.246 57.484 1.00   38.83 ? 96   ASP J OD2 1 
ATOM   10736 N  N   . VAL J  1 98  ? 119.552 119.101 53.651 1.00   29.64 ? 97   VAL J N   1 
ATOM   10737 C  CA  . VAL J  1 98  ? 120.461 119.298 52.533 1.00   27.88 ? 97   VAL J CA  1 
ATOM   10738 C  C   . VAL J  1 98  ? 119.629 119.421 51.275 1.00   28.19 ? 97   VAL J C   1 
ATOM   10739 O  O   . VAL J  1 98  ? 118.692 118.661 51.065 1.00   28.14 ? 97   VAL J O   1 
ATOM   10740 C  CB  . VAL J  1 98  ? 121.450 118.118 52.413 1.00   27.11 ? 97   VAL J CB  1 
ATOM   10741 C  CG1 . VAL J  1 98  ? 122.292 118.246 51.158 1.00   26.16 ? 97   VAL J CG1 1 
ATOM   10742 C  CG2 . VAL J  1 98  ? 122.326 118.016 53.664 1.00   25.81 ? 97   VAL J CG2 1 
ATOM   10743 N  N   . SER J  1 99  ? 119.969 120.394 50.441 1.00   28.49 ? 98   SER J N   1 
ATOM   10744 C  CA  . SER J  1 99  ? 119.335 120.547 49.151 1.00   29.32 ? 98   SER J CA  1 
ATOM   10745 C  C   . SER J  1 99  ? 120.321 121.283 48.267 1.00   28.93 ? 98   SER J C   1 
ATOM   10746 O  O   . SER J  1 99  ? 120.581 122.468 48.451 1.00   28.92 ? 98   SER J O   1 
ATOM   10747 C  CB  . SER J  1 99  ? 118.003 121.294 49.278 1.00   30.86 ? 98   SER J CB  1 
ATOM   10748 O  OG  . SER J  1 99  ? 117.218 121.160 48.102 1.00   32.21 ? 98   SER J OG  1 
ATOM   10749 N  N   . ILE J  1 100 ? 120.881 120.550 47.316 1.00   28.53 ? 99   ILE J N   1 
ATOM   10750 C  CA  . ILE J  1 100 ? 121.974 121.022 46.494 1.00   28.67 ? 99   ILE J CA  1 
ATOM   10751 C  C   . ILE J  1 100 ? 121.685 120.563 45.084 1.00   28.38 ? 99   ILE J C   1 
ATOM   10752 O  O   . ILE J  1 100 ? 121.123 119.487 44.872 1.00   27.38 ? 99   ILE J O   1 
ATOM   10753 C  CB  . ILE J  1 100 ? 123.321 120.398 46.964 1.00   29.24 ? 99   ILE J CB  1 
ATOM   10754 C  CG1 . ILE J  1 100 ? 123.886 121.157 48.170 1.00   29.03 ? 99   ILE J CG1 1 
ATOM   10755 C  CG2 . ILE J  1 100 ? 124.352 120.373 45.833 1.00   30.20 ? 99   ILE J CG2 1 
ATOM   10756 C  CD1 . ILE J  1 100 ? 124.963 120.383 48.926 1.00   28.46 ? 99   ILE J CD1 1 
ATOM   10757 N  N   . GLU J  1 101 ? 122.076 121.384 44.124 1.00   28.34 ? 100  GLU J N   1 
ATOM   10758 C  CA  . GLU J  1 101 ? 122.087 120.975 42.736 1.00   29.09 ? 100  GLU J CA  1 
ATOM   10759 C  C   . GLU J  1 101 ? 123.497 121.163 42.188 1.00   28.28 ? 100  GLU J C   1 
ATOM   10760 O  O   . GLU J  1 101 ? 124.132 122.200 42.428 1.00   27.51 ? 100  GLU J O   1 
ATOM   10761 C  CB  . GLU J  1 101 ? 121.062 121.774 41.920 1.00   30.28 ? 100  GLU J CB  1 
ATOM   10762 C  CG  . GLU J  1 101 ? 120.960 121.303 40.476 1.00   31.13 ? 100  GLU J CG  1 
ATOM   10763 C  CD  . GLU J  1 101 ? 119.871 121.998 39.704 0.50   31.28 ? 100  GLU J CD  1 
ATOM   10764 O  OE1 . GLU J  1 101 ? 118.700 121.804 40.075 0.50   31.06 ? 100  GLU J OE1 1 
ATOM   10765 O  OE2 . GLU J  1 101 ? 120.205 122.730 38.743 0.50   31.44 ? 100  GLU J OE2 1 
ATOM   10766 N  N   . ASP J  1 102 ? 123.984 120.154 41.464 1.00   28.29 ? 101  ASP J N   1 
ATOM   10767 C  CA  . ASP J  1 102 ? 125.340 120.190 40.913 1.00   27.81 ? 101  ASP J CA  1 
ATOM   10768 C  C   . ASP J  1 102 ? 125.407 119.556 39.525 1.00   28.71 ? 101  ASP J C   1 
ATOM   10769 O  O   . ASP J  1 102 ? 124.782 118.550 39.267 1.00   28.08 ? 101  ASP J O   1 
ATOM   10770 C  CB  . ASP J  1 102 ? 126.291 119.483 41.871 1.00   26.83 ? 101  ASP J CB  1 
ATOM   10771 C  CG  . ASP J  1 102 ? 127.730 119.723 41.543 1.00   26.02 ? 101  ASP J CG  1 
ATOM   10772 O  OD1 . ASP J  1 102 ? 128.220 120.840 41.778 1.00   26.30 ? 101  ASP J OD1 1 
ATOM   10773 O  OD2 . ASP J  1 102 ? 128.387 118.792 41.068 1.00   25.58 ? 101  ASP J OD2 1 
ATOM   10774 N  N   . SER J  1 103 ? 126.204 120.152 38.648 1.00   30.81 ? 102  SER J N   1 
ATOM   10775 C  CA  . SER J  1 103 ? 126.287 119.745 37.250 1.00   32.15 ? 102  SER J CA  1 
ATOM   10776 C  C   . SER J  1 103 ? 127.620 119.129 36.871 1.00   31.42 ? 102  SER J C   1 
ATOM   10777 O  O   . SER J  1 103 ? 127.868 118.885 35.697 1.00   30.94 ? 102  SER J O   1 
ATOM   10778 C  CB  . SER J  1 103 ? 126.023 120.963 36.373 1.00   34.50 ? 102  SER J CB  1 
ATOM   10779 O  OG  . SER J  1 103 ? 124.621 121.130 36.273 1.00   37.74 ? 102  SER J OG  1 
ATOM   10780 N  N   . VAL J  1 104 ? 128.469 118.896 37.871 1.00   30.37 ? 103  VAL J N   1 
ATOM   10781 C  CA  . VAL J  1 104 ? 129.782 118.293 37.685 1.00   29.24 ? 103  VAL J CA  1 
ATOM   10782 C  C   . VAL J  1 104 ? 129.725 116.818 38.102 1.00   29.16 ? 103  VAL J C   1 
ATOM   10783 O  O   . VAL J  1 104 ? 130.183 115.953 37.343 1.00   29.47 ? 103  VAL J O   1 
ATOM   10784 C  CB  . VAL J  1 104 ? 130.858 119.096 38.455 1.00   28.55 ? 103  VAL J CB  1 
ATOM   10785 C  CG1 . VAL J  1 104 ? 132.205 118.394 38.434 1.00   27.16 ? 103  VAL J CG1 1 
ATOM   10786 C  CG2 . VAL J  1 104 ? 130.966 120.514 37.855 1.00   28.70 ? 103  VAL J CG2 1 
ATOM   10787 N  N   . ILE J  1 105 ? 129.152 116.509 39.271 1.00   27.80 ? 104  ILE J N   1 
ATOM   10788 C  CA  . ILE J  1 105 ? 128.890 115.089 39.584 1.00   27.98 ? 104  ILE J CA  1 
ATOM   10789 C  C   . ILE J  1 105 ? 127.920 114.533 38.530 1.00   29.48 ? 104  ILE J C   1 
ATOM   10790 O  O   . ILE J  1 105 ? 127.208 115.304 37.870 1.00   29.44 ? 104  ILE J O   1 
ATOM   10791 C  CB  . ILE J  1 105 ? 128.363 114.805 41.022 1.00   26.46 ? 104  ILE J CB  1 
ATOM   10792 C  CG1 . ILE J  1 105 ? 127.050 115.523 41.341 1.00   26.15 ? 104  ILE J CG1 1 
ATOM   10793 C  CG2 . ILE J  1 105 ? 129.425 115.139 42.066 1.00   25.64 ? 104  ILE J CG2 1 
ATOM   10794 C  CD1 . ILE J  1 105 ? 126.419 115.099 42.666 1.00   25.31 ? 104  ILE J CD1 1 
ATOM   10795 N  N   . SER J  1 106 ? 127.938 113.214 38.352 1.00   30.32 ? 105  SER J N   1 
ATOM   10796 C  CA  . SER J  1 106 ? 126.974 112.519 37.503 1.00   32.49 ? 105  SER J CA  1 
ATOM   10797 C  C   . SER J  1 106 ? 126.598 111.167 38.116 1.00   32.41 ? 105  SER J C   1 
ATOM   10798 O  O   . SER J  1 106 ? 127.370 110.631 38.908 1.00   30.12 ? 105  SER J O   1 
ATOM   10799 C  CB  . SER J  1 106 ? 127.562 112.306 36.101 1.00   34.02 ? 105  SER J CB  1 
ATOM   10800 O  OG  . SER J  1 106 ? 126.547 111.890 35.194 1.00   36.38 ? 105  SER J OG  1 
ATOM   10801 N  N   . LEU J  1 107 ? 125.408 110.649 37.770 1.00   33.63 ? 106  LEU J N   1 
ATOM   10802 C  CA  . LEU J  1 107 ? 125.025 109.259 38.103 1.00   34.86 ? 106  LEU J CA  1 
ATOM   10803 C  C   . LEU J  1 107 ? 125.270 108.289 36.932 1.00   36.74 ? 106  LEU J C   1 
ATOM   10804 O  O   . LEU J  1 107 ? 124.841 107.140 36.985 1.00   37.41 ? 106  LEU J O   1 
ATOM   10805 C  CB  . LEU J  1 107 ? 123.564 109.155 38.586 1.00   34.83 ? 106  LEU J CB  1 
ATOM   10806 C  CG  . LEU J  1 107 ? 123.137 109.975 39.817 1.00   33.91 ? 106  LEU J CG  1 
ATOM   10807 C  CD1 . LEU J  1 107 ? 121.671 109.724 40.148 1.00   33.74 ? 106  LEU J CD1 1 
ATOM   10808 C  CD2 . LEU J  1 107 ? 123.995 109.681 41.040 1.00   33.80 ? 106  LEU J CD2 1 
ATOM   10809 N  N   . SER J  1 108 ? 125.962 108.756 35.891 1.00   38.87 ? 107  SER J N   1 
ATOM   10810 C  CA  . SER J  1 108 ? 126.578 107.876 34.877 1.00   40.48 ? 107  SER J CA  1 
ATOM   10811 C  C   . SER J  1 108 ? 127.786 108.557 34.196 1.00   41.70 ? 107  SER J C   1 
ATOM   10812 O  O   . SER J  1 108 ? 128.035 109.740 34.399 1.00   42.19 ? 107  SER J O   1 
ATOM   10813 C  CB  . SER J  1 108 ? 125.539 107.429 33.843 1.00   41.99 ? 107  SER J CB  1 
ATOM   10814 O  OG  . SER J  1 108 ? 124.830 108.525 33.301 1.00   43.15 ? 107  SER J OG  1 
ATOM   10815 N  N   . GLY J  1 109 ? 128.551 107.805 33.409 1.00   43.37 ? 108  GLY J N   1 
ATOM   10816 C  CA  . GLY J  1 109 ? 129.709 108.366 32.685 1.00   42.55 ? 108  GLY J CA  1 
ATOM   10817 C  C   . GLY J  1 109 ? 130.962 108.437 33.537 1.00   41.83 ? 108  GLY J C   1 
ATOM   10818 O  O   . GLY J  1 109 ? 131.052 107.784 34.568 1.00   41.25 ? 108  GLY J O   1 
ATOM   10819 N  N   . ASP J  1 110 ? 131.933 109.244 33.121 1.00   41.71 ? 109  ASP J N   1 
ATOM   10820 C  CA  . ASP J  1 110 ? 133.224 109.320 33.839 1.00   41.62 ? 109  ASP J CA  1 
ATOM   10821 C  C   . ASP J  1 110 ? 133.176 109.995 35.238 1.00   40.00 ? 109  ASP J C   1 
ATOM   10822 O  O   . ASP J  1 110 ? 133.958 109.635 36.120 1.00   39.90 ? 109  ASP J O   1 
ATOM   10823 C  CB  . ASP J  1 110 ? 134.299 109.980 32.958 1.00   41.83 ? 109  ASP J CB  1 
ATOM   10824 C  CG  . ASP J  1 110 ? 134.669 109.128 31.744 0.50   42.20 ? 109  ASP J CG  1 
ATOM   10825 O  OD1 . ASP J  1 110 ? 134.697 107.883 31.850 0.50   41.28 ? 109  ASP J OD1 1 
ATOM   10826 O  OD2 . ASP J  1 110 ? 134.939 109.712 30.681 0.50   42.47 ? 109  ASP J OD2 1 
ATOM   10827 N  N   . HIS J  1 111 ? 132.269 110.950 35.441 1.00   38.77 ? 110  HIS J N   1 
ATOM   10828 C  CA  . HIS J  1 111 ? 132.068 111.559 36.778 1.00   36.20 ? 110  HIS J CA  1 
ATOM   10829 C  C   . HIS J  1 111 ? 131.059 110.787 37.599 1.00   34.56 ? 110  HIS J C   1 
ATOM   10830 O  O   . HIS J  1 111 ? 130.509 111.321 38.574 1.00   32.41 ? 110  HIS J O   1 
ATOM   10831 C  CB  . HIS J  1 111 ? 131.603 112.997 36.648 1.00   36.46 ? 110  HIS J CB  1 
ATOM   10832 C  CG  . HIS J  1 111 ? 132.587 113.895 35.951 1.00   38.56 ? 110  HIS J CG  1 
ATOM   10833 N  ND1 . HIS J  1 111 ? 132.422 115.238 35.892 1.00   39.77 ? 110  HIS J ND1 1 
ATOM   10834 C  CD2 . HIS J  1 111 ? 133.779 113.612 35.285 1.00   39.26 ? 110  HIS J CD2 1 
ATOM   10835 C  CE1 . HIS J  1 111 ? 133.445 115.780 35.207 1.00   40.38 ? 110  HIS J CE1 1 
ATOM   10836 N  NE2 . HIS J  1 111 ? 134.276 114.780 34.836 1.00   40.87 ? 110  HIS J NE2 1 
ATOM   10837 N  N   . CYS J  1 112 ? 130.787 109.532 37.220 1.00   33.63 ? 111  CYS J N   1 
ATOM   10838 C  CA  . CYS J  1 112 ? 129.834 108.710 37.970 1.00   32.54 ? 111  CYS J CA  1 
ATOM   10839 C  C   . CYS J  1 112 ? 130.282 108.566 39.434 1.00   30.18 ? 111  CYS J C   1 
ATOM   10840 O  O   . CYS J  1 112 ? 131.435 108.230 39.708 1.00   28.63 ? 111  CYS J O   1 
ATOM   10841 C  CB  . CYS J  1 112 ? 129.677 107.326 37.335 1.00   34.40 ? 111  CYS J CB  1 
ATOM   10842 S  SG  . CYS J  1 112 ? 128.265 106.428 38.008 1.00   37.83 ? 111  CYS J SG  1 
ATOM   10843 N  N   . ILE J  1 113 ? 129.371 108.842 40.360 1.00   28.07 ? 112  ILE J N   1 
ATOM   10844 C  CA  . ILE J  1 113 ? 129.675 108.746 41.789 1.00   27.04 ? 112  ILE J CA  1 
ATOM   10845 C  C   . ILE J  1 113 ? 129.036 107.513 42.432 1.00   26.39 ? 112  ILE J C   1 
ATOM   10846 O  O   . ILE J  1 113 ? 129.230 107.276 43.615 1.00   25.30 ? 112  ILE J O   1 
ATOM   10847 C  CB  . ILE J  1 113 ? 129.259 110.016 42.568 1.00   26.09 ? 112  ILE J CB  1 
ATOM   10848 C  CG1 . ILE J  1 113 ? 127.730 110.221 42.527 1.00   26.36 ? 112  ILE J CG1 1 
ATOM   10849 C  CG2 . ILE J  1 113 ? 129.991 111.235 42.001 1.00   25.90 ? 112  ILE J CG2 1 
ATOM   10850 C  CD1 . ILE J  1 113 ? 127.240 111.413 43.336 1.00   25.86 ? 112  ILE J CD1 1 
ATOM   10851 N  N   . ILE J  1 114 ? 128.271 106.737 41.668 1.00   26.53 ? 113  ILE J N   1 
ATOM   10852 C  CA  . ILE J  1 114 ? 127.718 105.485 42.191 1.00   26.92 ? 113  ILE J CA  1 
ATOM   10853 C  C   . ILE J  1 114 ? 128.858 104.527 42.600 1.00   26.47 ? 113  ILE J C   1 
ATOM   10854 O  O   . ILE J  1 114 ? 129.857 104.398 41.897 1.00   25.91 ? 113  ILE J O   1 
ATOM   10855 C  CB  . ILE J  1 114 ? 126.713 104.855 41.208 1.00   28.26 ? 113  ILE J CB  1 
ATOM   10856 C  CG1 . ILE J  1 114 ? 125.470 105.748 41.168 1.00   28.69 ? 113  ILE J CG1 1 
ATOM   10857 C  CG2 . ILE J  1 114 ? 126.337 103.437 41.630 1.00   27.93 ? 113  ILE J CG2 1 
ATOM   10858 C  CD1 . ILE J  1 114 ? 124.367 105.260 40.264 1.00   30.21 ? 113  ILE J CD1 1 
ATOM   10859 N  N   . GLY J  1 115 ? 128.728 103.920 43.783 1.00   25.64 ? 114  GLY J N   1 
ATOM   10860 C  CA  . GLY J  1 115 ? 129.766 103.030 44.314 1.00   25.77 ? 114  GLY J CA  1 
ATOM   10861 C  C   . GLY J  1 115 ? 130.916 103.766 44.993 1.00   25.29 ? 114  GLY J C   1 
ATOM   10862 O  O   . GLY J  1 115 ? 131.889 103.147 45.403 1.00   24.09 ? 114  GLY J O   1 
ATOM   10863 N  N   . ARG J  1 116 ? 130.812 105.095 45.098 1.00   24.84 ? 115  ARG J N   1 
ATOM   10864 C  CA  . ARG J  1 116 ? 131.818 105.875 45.791 1.00   25.15 ? 115  ARG J CA  1 
ATOM   10865 C  C   . ARG J  1 116 ? 131.242 106.254 47.142 1.00   24.36 ? 115  ARG J C   1 
ATOM   10866 O  O   . ARG J  1 116 ? 130.175 105.754 47.512 1.00   24.75 ? 115  ARG J O   1 
ATOM   10867 C  CB  . ARG J  1 116 ? 132.228 107.083 44.943 1.00   26.12 ? 115  ARG J CB  1 
ATOM   10868 C  CG  . ARG J  1 116 ? 132.855 106.618 43.635 1.00   27.38 ? 115  ARG J CG  1 
ATOM   10869 C  CD  . ARG J  1 116 ? 133.432 107.763 42.822 1.00   28.23 ? 115  ARG J CD  1 
ATOM   10870 N  NE  . ARG J  1 116 ? 133.742 107.333 41.460 1.00   28.54 ? 115  ARG J NE  1 
ATOM   10871 C  CZ  . ARG J  1 116 ? 134.826 106.658 41.093 1.00   28.71 ? 115  ARG J CZ  1 
ATOM   10872 N  NH1 . ARG J  1 116 ? 135.752 106.316 41.970 1.00   29.00 ? 115  ARG J NH1 1 
ATOM   10873 N  NH2 . ARG J  1 116 ? 134.994 106.346 39.819 1.00   30.13 ? 115  ARG J NH2 1 
ATOM   10874 N  N   . THR J  1 117 ? 131.947 107.085 47.898 1.00   23.43 ? 116  THR J N   1 
ATOM   10875 C  CA  . THR J  1 117 ? 131.546 107.388 49.260 1.00   23.13 ? 116  THR J CA  1 
ATOM   10876 C  C   . THR J  1 117 ? 131.197 108.873 49.425 1.00   23.11 ? 116  THR J C   1 
ATOM   10877 O  O   . THR J  1 117 ? 131.931 109.755 48.950 1.00   23.83 ? 116  THR J O   1 
ATOM   10878 C  CB  . THR J  1 117 ? 132.650 106.982 50.258 1.00   23.22 ? 116  THR J CB  1 
ATOM   10879 O  OG1 . THR J  1 117 ? 132.824 105.554 50.248 1.00   22.76 ? 116  THR J OG1 1 
ATOM   10880 C  CG2 . THR J  1 117 ? 132.312 107.418 51.683 1.00   22.87 ? 116  THR J CG2 1 
ATOM   10881 N  N   . LEU J  1 118 ? 130.071 109.130 50.086 1.00   22.46 ? 117  LEU J N   1 
ATOM   10882 C  CA  . LEU J  1 118 ? 129.687 110.473 50.532 1.00   21.75 ? 117  LEU J CA  1 
ATOM   10883 C  C   . LEU J  1 118 ? 130.156 110.665 51.971 1.00   21.09 ? 117  LEU J C   1 
ATOM   10884 O  O   . LEU J  1 118 ? 129.947 109.796 52.823 1.00   20.79 ? 117  LEU J O   1 
ATOM   10885 C  CB  . LEU J  1 118 ? 128.173 110.640 50.457 1.00   21.61 ? 117  LEU J CB  1 
ATOM   10886 C  CG  . LEU J  1 118 ? 127.603 112.034 50.701 1.00   21.88 ? 117  LEU J CG  1 
ATOM   10887 C  CD1 . LEU J  1 118 ? 128.089 113.037 49.647 1.00   21.27 ? 117  LEU J CD1 1 
ATOM   10888 C  CD2 . LEU J  1 118 ? 126.064 111.930 50.732 1.00   21.75 ? 117  LEU J CD2 1 
ATOM   10889 N  N   . VAL J  1 119 ? 130.790 111.803 52.236 1.00   20.64 ? 118  VAL J N   1 
ATOM   10890 C  CA  . VAL J  1 119 ? 131.335 112.112 53.561 1.00   20.33 ? 118  VAL J CA  1 
ATOM   10891 C  C   . VAL J  1 119 ? 130.872 113.475 54.053 1.00   20.21 ? 118  VAL J C   1 
ATOM   10892 O  O   . VAL J  1 119 ? 130.891 114.459 53.304 1.00   20.23 ? 118  VAL J O   1 
ATOM   10893 C  CB  . VAL J  1 119 ? 132.869 112.121 53.538 1.00   20.58 ? 118  VAL J CB  1 
ATOM   10894 C  CG1 . VAL J  1 119 ? 133.438 112.484 54.932 1.00   20.40 ? 118  VAL J CG1 1 
ATOM   10895 C  CG2 . VAL J  1 119 ? 133.393 110.783 53.022 1.00   20.43 ? 118  VAL J CG2 1 
ATOM   10896 N  N   . VAL J  1 120 ? 130.447 113.530 55.309 1.00   20.17 ? 119  VAL J N   1 
ATOM   10897 C  CA  . VAL J  1 120 ? 130.180 114.784 55.972 1.00   20.53 ? 119  VAL J CA  1 
ATOM   10898 C  C   . VAL J  1 120 ? 131.269 114.976 57.032 1.00   21.05 ? 119  VAL J C   1 
ATOM   10899 O  O   . VAL J  1 120 ? 131.614 114.024 57.781 1.00   20.66 ? 119  VAL J O   1 
ATOM   10900 C  CB  . VAL J  1 120 ? 128.762 114.827 56.587 1.00   21.06 ? 119  VAL J CB  1 
ATOM   10901 C  CG1 . VAL J  1 120 ? 128.597 113.750 57.664 1.00   21.44 ? 119  VAL J CG1 1 
ATOM   10902 C  CG2 . VAL J  1 120 ? 128.471 116.224 57.126 1.00   21.37 ? 119  VAL J CG2 1 
ATOM   10903 N  N   . HIS J  1 121 ? 131.808 116.197 57.084 1.00   20.65 ? 120  HIS J N   1 
ATOM   10904 C  CA  . HIS J  1 121 ? 133.013 116.500 57.859 1.00   21.32 ? 120  HIS J CA  1 
ATOM   10905 C  C   . HIS J  1 121 ? 132.795 117.255 59.147 1.00   22.54 ? 120  HIS J C   1 
ATOM   10906 O  O   . HIS J  1 121 ? 131.764 117.898 59.377 1.00   22.79 ? 120  HIS J O   1 
ATOM   10907 C  CB  . HIS J  1 121 ? 134.011 117.287 57.010 1.00   20.82 ? 120  HIS J CB  1 
ATOM   10908 C  CG  . HIS J  1 121 ? 134.748 116.445 56.015 1.00   20.42 ? 120  HIS J CG  1 
ATOM   10909 N  ND1 . HIS J  1 121 ? 135.914 115.847 56.299 1.00   20.68 ? 120  HIS J ND1 1 
ATOM   10910 C  CD2 . HIS J  1 121 ? 134.435 116.105 54.707 1.00   20.12 ? 120  HIS J CD2 1 
ATOM   10911 C  CE1 . HIS J  1 121 ? 136.326 115.157 55.225 1.00   20.96 ? 120  HIS J CE1 1 
ATOM   10912 N  NE2 . HIS J  1 121 ? 135.408 115.308 54.256 1.00   20.08 ? 120  HIS J NE2 1 
ATOM   10913 N  N   . GLU J  1 122 ? 133.831 117.191 59.963 1.00   23.98 ? 121  GLU J N   1 
ATOM   10914 C  CA  . GLU J  1 122 ? 133.917 117.818 61.274 1.00   26.04 ? 121  GLU J CA  1 
ATOM   10915 C  C   . GLU J  1 122 ? 133.787 119.339 61.185 1.00   25.59 ? 121  GLU J C   1 
ATOM   10916 O  O   . GLU J  1 122 ? 133.033 119.927 61.936 1.00   25.99 ? 121  GLU J O   1 
ATOM   10917 C  CB  . GLU J  1 122 ? 135.272 117.436 61.868 1.00   27.66 ? 121  GLU J CB  1 
ATOM   10918 C  CG  . GLU J  1 122 ? 135.655 118.054 63.201 1.00   30.78 ? 121  GLU J CG  1 
ATOM   10919 C  CD  . GLU J  1 122 ? 137.159 117.956 63.477 1.00   33.18 ? 121  GLU J CD  1 
ATOM   10920 O  OE1 . GLU J  1 122 ? 137.958 117.523 62.602 1.00   34.06 ? 121  GLU J OE1 1 
ATOM   10921 O  OE2 . GLU J  1 122 ? 137.557 118.340 64.592 1.00   38.92 ? 121  GLU J OE2 1 
ATOM   10922 N  N   . LYS J  1 123 ? 134.521 119.944 60.250 1.00   25.56 ? 122  LYS J N   1 
ATOM   10923 C  CA  . LYS J  1 123 ? 134.631 121.405 60.118 1.00   25.49 ? 122  LYS J CA  1 
ATOM   10924 C  C   . LYS J  1 123 ? 134.089 121.930 58.781 1.00   24.20 ? 122  LYS J C   1 
ATOM   10925 O  O   . LYS J  1 123 ? 133.710 121.163 57.873 1.00   23.94 ? 122  LYS J O   1 
ATOM   10926 C  CB  . LYS J  1 123 ? 136.109 121.827 60.249 1.00   26.66 ? 122  LYS J CB  1 
ATOM   10927 C  CG  . LYS J  1 123 ? 136.809 121.386 61.535 1.00   27.74 ? 122  LYS J CG  1 
ATOM   10928 C  CD  . LYS J  1 123 ? 138.233 121.933 61.633 1.00   29.01 ? 122  LYS J CD  1 
ATOM   10929 C  CE  . LYS J  1 123 ? 139.253 120.945 61.074 1.00   30.54 ? 122  LYS J CE  1 
ATOM   10930 N  NZ  . LYS J  1 123 ? 140.645 121.474 60.849 1.00   31.07 ? 122  LYS J NZ  1 
ATOM   10931 N  N   . ALA J  1 124 ? 134.069 123.250 58.671 1.00   23.54 ? 123  ALA J N   1 
ATOM   10932 C  CA  . ALA J  1 124 ? 133.721 123.944 57.439 1.00   22.48 ? 123  ALA J CA  1 
ATOM   10933 C  C   . ALA J  1 124 ? 134.785 123.670 56.395 1.00   21.64 ? 123  ALA J C   1 
ATOM   10934 O  O   . ALA J  1 124 ? 135.971 123.619 56.713 1.00   21.76 ? 123  ALA J O   1 
ATOM   10935 C  CB  . ALA J  1 124 ? 133.597 125.462 57.695 1.00   22.38 ? 123  ALA J CB  1 
ATOM   10936 N  N   . ASP J  1 125 ? 134.339 123.444 55.161 1.00   20.31 ? 124  ASP J N   1 
ATOM   10937 C  CA  . ASP J  1 125 ? 135.192 123.424 53.988 1.00   19.73 ? 124  ASP J CA  1 
ATOM   10938 C  C   . ASP J  1 125 ? 135.414 124.902 53.642 1.00   19.45 ? 124  ASP J C   1 
ATOM   10939 O  O   . ASP J  1 125 ? 134.421 125.656 53.480 1.00   19.19 ? 124  ASP J O   1 
ATOM   10940 C  CB  . ASP J  1 125 ? 134.445 122.684 52.848 1.00   19.90 ? 124  ASP J CB  1 
ATOM   10941 C  CG  . ASP J  1 125 ? 135.255 122.548 51.554 1.00   19.80 ? 124  ASP J CG  1 
ATOM   10942 O  OD1 . ASP J  1 125 ? 136.216 123.326 51.332 1.00   19.78 ? 124  ASP J OD1 1 
ATOM   10943 O  OD2 . ASP J  1 125 ? 134.898 121.652 50.738 1.00   19.51 ? 124  ASP J OD2 1 
ATOM   10944 N  N   . ASP J  1 126 ? 136.684 125.311 53.538 1.00   18.81 ? 125  ASP J N   1 
ATOM   10945 C  CA  . ASP J  1 126 ? 137.025 126.701 53.200 1.00   18.90 ? 125  ASP J CA  1 
ATOM   10946 C  C   . ASP J  1 126 ? 136.994 127.006 51.703 1.00   18.58 ? 125  ASP J C   1 
ATOM   10947 O  O   . ASP J  1 126 ? 137.335 128.112 51.307 1.00   18.69 ? 125  ASP J O   1 
ATOM   10948 C  CB  . ASP J  1 126 ? 138.387 127.116 53.813 1.00   18.95 ? 125  ASP J CB  1 
ATOM   10949 C  CG  . ASP J  1 126 ? 139.584 126.413 53.188 1.00   18.95 ? 125  ASP J CG  1 
ATOM   10950 O  OD1 . ASP J  1 126 ? 139.486 125.858 52.082 1.00   18.98 ? 125  ASP J OD1 1 
ATOM   10951 O  OD2 . ASP J  1 126 ? 140.669 126.431 53.814 1.00   19.19 ? 125  ASP J OD2 1 
ATOM   10952 N  N   . LEU J  1 127 ? 136.624 126.010 50.887 1.00   18.30 ? 126  LEU J N   1 
ATOM   10953 C  CA  . LEU J  1 127 ? 136.367 126.178 49.438 1.00   18.41 ? 126  LEU J CA  1 
ATOM   10954 C  C   . LEU J  1 127 ? 137.625 126.551 48.645 1.00   18.77 ? 126  LEU J C   1 
ATOM   10955 O  O   . LEU J  1 127 ? 137.545 127.193 47.587 1.00   19.04 ? 126  LEU J O   1 
ATOM   10956 C  CB  . LEU J  1 127 ? 135.225 127.174 49.168 1.00   17.88 ? 126  LEU J CB  1 
ATOM   10957 C  CG  . LEU J  1 127 ? 133.970 126.961 50.024 1.00   17.78 ? 126  LEU J CG  1 
ATOM   10958 C  CD1 . LEU J  1 127 ? 132.907 128.009 49.694 1.00   17.37 ? 126  LEU J CD1 1 
ATOM   10959 C  CD2 . LEU J  1 127 ? 133.400 125.540 49.883 1.00   17.18 ? 126  LEU J CD2 1 
ATOM   10960 N  N   . GLY J  1 128 ? 138.775 126.125 49.160 1.00   18.84 ? 127  GLY J N   1 
ATOM   10961 C  CA  . GLY J  1 128 ? 140.063 126.397 48.526 1.00   19.53 ? 127  GLY J CA  1 
ATOM   10962 C  C   . GLY J  1 128 ? 140.629 127.771 48.802 1.00   19.77 ? 127  GLY J C   1 
ATOM   10963 O  O   . GLY J  1 128 ? 141.618 128.163 48.197 1.00   20.44 ? 127  GLY J O   1 
ATOM   10964 N  N   . LYS J  1 129 ? 140.029 128.501 49.738 1.00   19.81 ? 128  LYS J N   1 
ATOM   10965 C  CA  . LYS J  1 129 ? 140.422 129.886 49.977 1.00   20.18 ? 128  LYS J CA  1 
ATOM   10966 C  C   . LYS J  1 129 ? 141.188 130.067 51.300 1.00   20.18 ? 128  LYS J C   1 
ATOM   10967 O  O   . LYS J  1 129 ? 141.311 131.183 51.805 1.00   20.12 ? 128  LYS J O   1 
ATOM   10968 C  CB  . LYS J  1 129 ? 139.167 130.767 49.970 1.00   20.53 ? 128  LYS J CB  1 
ATOM   10969 C  CG  . LYS J  1 129 ? 138.377 130.745 48.657 1.00   20.52 ? 128  LYS J CG  1 
ATOM   10970 C  CD  . LYS J  1 129 ? 137.048 131.494 48.817 1.00   20.99 ? 128  LYS J CD  1 
ATOM   10971 C  CE  . LYS J  1 129 ? 137.216 133.002 49.029 1.00   21.77 ? 128  LYS J CE  1 
ATOM   10972 N  NZ  . LYS J  1 129 ? 135.888 133.710 48.953 1.00   23.25 ? 128  LYS J NZ  1 
ATOM   10973 N  N   . GLY J  1 130 ? 141.701 128.975 51.857 1.00   19.56 ? 129  GLY J N   1 
ATOM   10974 C  CA  . GLY J  1 130 ? 142.388 129.022 53.145 1.00   19.93 ? 129  GLY J CA  1 
ATOM   10975 C  C   . GLY J  1 130 ? 143.851 129.462 53.128 1.00   19.98 ? 129  GLY J C   1 
ATOM   10976 O  O   . GLY J  1 130 ? 144.423 129.748 54.184 1.00   19.95 ? 129  GLY J O   1 
ATOM   10977 N  N   . GLY J  1 131 ? 144.464 129.482 51.948 1.00   20.00 ? 130  GLY J N   1 
ATOM   10978 C  CA  . GLY J  1 131 ? 145.838 129.973 51.799 1.00   20.90 ? 130  GLY J CA  1 
ATOM   10979 C  C   . GLY J  1 131 ? 146.950 129.049 52.282 1.00   21.50 ? 130  GLY J C   1 
ATOM   10980 O  O   . GLY J  1 131 ? 148.114 129.416 52.214 1.00   21.71 ? 130  GLY J O   1 
ATOM   10981 N  N   . ASN J  1 132 ? 146.598 127.864 52.771 1.00   21.64 ? 131  ASN J N   1 
ATOM   10982 C  CA  . ASN J  1 132 ? 147.580 126.833 53.085 1.00   23.01 ? 131  ASN J CA  1 
ATOM   10983 C  C   . ASN J  1 132 ? 147.465 125.658 52.118 1.00   23.64 ? 131  ASN J C   1 
ATOM   10984 O  O   . ASN J  1 132 ? 146.513 125.562 51.354 1.00   23.15 ? 131  ASN J O   1 
ATOM   10985 C  CB  . ASN J  1 132 ? 147.494 126.361 54.561 1.00   22.81 ? 131  ASN J CB  1 
ATOM   10986 C  CG  . ASN J  1 132 ? 146.201 125.607 54.896 1.00   22.33 ? 131  ASN J CG  1 
ATOM   10987 O  OD1 . ASN J  1 132 ? 145.250 125.536 54.089 1.00   22.11 ? 131  ASN J OD1 1 
ATOM   10988 N  ND2 . ASN J  1 132 ? 146.158 125.039 56.108 1.00   22.03 ? 131  ASN J ND2 1 
ATOM   10989 N  N   . GLU J  1 133 ? 148.447 124.772 52.190 1.00   25.05 ? 132  GLU J N   1 
ATOM   10990 C  CA  . GLU J  1 133 ? 148.535 123.612 51.332 1.00   25.98 ? 132  GLU J CA  1 
ATOM   10991 C  C   . GLU J  1 133 ? 147.290 122.758 51.474 1.00   25.49 ? 132  GLU J C   1 
ATOM   10992 O  O   . GLU J  1 133 ? 146.755 122.273 50.487 1.00   25.36 ? 132  GLU J O   1 
ATOM   10993 C  CB  . GLU J  1 133 ? 149.767 122.782 51.698 1.00   27.58 ? 132  GLU J CB  1 
ATOM   10994 C  CG  . GLU J  1 133 ? 151.101 123.476 51.420 1.00   29.69 ? 132  GLU J CG  1 
ATOM   10995 C  CD  . GLU J  1 133 ? 152.308 122.586 51.737 1.00   31.58 ? 132  GLU J CD  1 
ATOM   10996 O  OE1 . GLU J  1 133 ? 152.121 121.463 52.236 1.00   32.80 ? 132  GLU J OE1 1 
ATOM   10997 O  OE2 . GLU J  1 133 ? 153.450 123.008 51.496 1.00   34.32 ? 132  GLU J OE2 1 
ATOM   10998 N  N   . GLU J  1 134 ? 146.820 122.595 52.708 1.00   25.42 ? 133  GLU J N   1 
ATOM   10999 C  CA  . GLU J  1 134 ? 145.674 121.729 52.988 1.00   25.01 ? 133  GLU J CA  1 
ATOM   11000 C  C   . GLU J  1 134 ? 144.366 122.233 52.357 1.00   23.38 ? 133  GLU J C   1 
ATOM   11001 O  O   . GLU J  1 134 ? 143.502 121.438 51.982 1.00   22.49 ? 133  GLU J O   1 
ATOM   11002 C  CB  . GLU J  1 134 ? 145.501 121.574 54.504 1.00   26.10 ? 133  GLU J CB  1 
ATOM   11003 C  CG  . GLU J  1 134 ? 144.431 120.570 54.886 1.00   26.38 ? 133  GLU J CG  1 
ATOM   11004 C  CD  . GLU J  1 134 ? 144.768 119.165 54.415 1.00   27.60 ? 133  GLU J CD  1 
ATOM   11005 O  OE1 . GLU J  1 134 ? 145.969 118.781 54.421 1.00   28.63 ? 133  GLU J OE1 1 
ATOM   11006 O  OE2 . GLU J  1 134 ? 143.825 118.441 54.054 1.00   28.18 ? 133  GLU J OE2 1 
ATOM   11007 N  N   . SER J  1 135 ? 144.225 123.548 52.234 1.00   22.70 ? 134  SER J N   1 
ATOM   11008 C  CA  . SER J  1 135 ? 143.034 124.140 51.616 1.00   21.69 ? 134  SER J CA  1 
ATOM   11009 C  C   . SER J  1 135 ? 142.794 123.663 50.173 1.00   21.80 ? 134  SER J C   1 
ATOM   11010 O  O   . SER J  1 135 ? 141.655 123.471 49.768 1.00   20.57 ? 134  SER J O   1 
ATOM   11011 C  CB  . SER J  1 135 ? 143.092 125.675 51.666 1.00   21.42 ? 134  SER J CB  1 
ATOM   11012 O  OG  . SER J  1 135 ? 142.003 126.254 50.972 1.00   20.39 ? 134  SER J OG  1 
ATOM   11013 N  N   . THR J  1 136 ? 143.864 123.455 49.412 1.00   23.10 ? 135  THR J N   1 
ATOM   11014 C  CA  . THR J  1 136 ? 143.754 123.007 48.028 1.00   24.10 ? 135  THR J CA  1 
ATOM   11015 C  C   . THR J  1 136 ? 143.648 121.479 47.899 1.00   24.41 ? 135  THR J C   1 
ATOM   11016 O  O   . THR J  1 136 ? 143.598 120.976 46.777 1.00   24.34 ? 135  THR J O   1 
ATOM   11017 C  CB  . THR J  1 136 ? 144.964 123.466 47.172 1.00   25.84 ? 135  THR J CB  1 
ATOM   11018 O  OG1 . THR J  1 136 ? 146.180 122.998 47.766 1.00   28.10 ? 135  THR J OG1 1 
ATOM   11019 C  CG2 . THR J  1 136 ? 145.037 124.945 47.096 1.00   27.02 ? 135  THR J CG2 1 
ATOM   11020 N  N   . LYS J  1 137 ? 143.624 120.753 49.020 1.00   24.26 ? 136  LYS J N   1 
ATOM   11021 C  CA  . LYS J  1 137 ? 143.423 119.295 49.010 1.00   25.24 ? 136  LYS J CA  1 
ATOM   11022 C  C   . LYS J  1 137 ? 142.057 118.924 49.623 1.00   24.15 ? 136  LYS J C   1 
ATOM   11023 O  O   . LYS J  1 137 ? 141.287 118.156 49.038 1.00   23.61 ? 136  LYS J O   1 
ATOM   11024 C  CB  . LYS J  1 137 ? 144.518 118.561 49.798 1.00   26.94 ? 136  LYS J CB  1 
ATOM   11025 C  CG  . LYS J  1 137 ? 145.940 119.027 49.570 1.00   28.91 ? 136  LYS J CG  1 
ATOM   11026 C  CD  . LYS J  1 137 ? 146.919 118.253 50.456 1.00   30.94 ? 136  LYS J CD  1 
ATOM   11027 C  CE  . LYS J  1 137 ? 148.335 118.351 49.917 1.00   32.93 ? 136  LYS J CE  1 
ATOM   11028 N  NZ  . LYS J  1 137 ? 149.353 117.787 50.862 1.00   35.71 ? 136  LYS J NZ  1 
ATOM   11029 N  N   . THR J  1 138 ? 141.759 119.473 50.801 1.00   23.18 ? 137  THR J N   1 
ATOM   11030 C  CA  . THR J  1 138 ? 140.551 119.090 51.535 1.00   22.38 ? 137  THR J CA  1 
ATOM   11031 C  C   . THR J  1 138 ? 139.656 120.251 51.975 1.00   21.90 ? 137  THR J C   1 
ATOM   11032 O  O   . THR J  1 138 ? 138.593 120.006 52.537 1.00   21.43 ? 137  THR J O   1 
ATOM   11033 C  CB  . THR J  1 138 ? 140.908 118.273 52.798 1.00   23.06 ? 137  THR J CB  1 
ATOM   11034 O  OG1 . THR J  1 138 ? 141.579 119.114 53.751 1.00   23.41 ? 137  THR J OG1 1 
ATOM   11035 C  CG2 . THR J  1 138 ? 141.779 117.023 52.467 1.00   22.93 ? 137  THR J CG2 1 
ATOM   11036 N  N   . GLY J  1 139 ? 140.073 121.502 51.742 1.00   21.66 ? 138  GLY J N   1 
ATOM   11037 C  CA  . GLY J  1 139 ? 139.336 122.671 52.257 1.00   21.28 ? 138  GLY J CA  1 
ATOM   11038 C  C   . GLY J  1 139 ? 139.480 122.861 53.778 1.00   21.71 ? 138  GLY J C   1 
ATOM   11039 O  O   . GLY J  1 139 ? 138.732 123.644 54.395 1.00   21.91 ? 138  GLY J O   1 
ATOM   11040 N  N   . ASN J  1 140 ? 140.435 122.158 54.387 1.00   21.59 ? 139  ASN J N   1 
ATOM   11041 C  CA  . ASN J  1 140 ? 140.593 122.152 55.853 1.00   21.73 ? 139  ASN J CA  1 
ATOM   11042 C  C   . ASN J  1 140 ? 139.309 121.687 56.589 1.00   21.68 ? 139  ASN J C   1 
ATOM   11043 O  O   . ASN J  1 140 ? 138.976 122.206 57.657 1.00   21.73 ? 139  ASN J O   1 
ATOM   11044 C  CB  . ASN J  1 140 ? 141.052 123.524 56.347 1.00   21.23 ? 139  ASN J CB  1 
ATOM   11045 C  CG  . ASN J  1 140 ? 142.469 123.851 55.928 1.00   21.42 ? 139  ASN J CG  1 
ATOM   11046 O  OD1 . ASN J  1 140 ? 143.418 123.318 56.492 1.00   22.20 ? 139  ASN J OD1 1 
ATOM   11047 N  ND2 . ASN J  1 140 ? 142.627 124.730 54.946 1.00   20.55 ? 139  ASN J ND2 1 
ATOM   11048 N  N   . ALA J  1 141 ? 138.598 120.709 56.010 1.00   21.17 ? 140  ALA J N   1 
ATOM   11049 C  CA  . ALA J  1 141 ? 137.301 120.264 56.562 1.00   21.05 ? 140  ALA J CA  1 
ATOM   11050 C  C   . ALA J  1 141 ? 137.474 119.302 57.713 1.00   21.67 ? 140  ALA J C   1 
ATOM   11051 O  O   . ALA J  1 141 ? 136.532 119.020 58.443 1.00   22.34 ? 140  ALA J O   1 
ATOM   11052 C  CB  . ALA J  1 141 ? 136.416 119.650 55.479 1.00   19.88 ? 140  ALA J CB  1 
ATOM   11053 N  N   . GLY J  1 142 ? 138.676 118.779 57.870 1.00   22.77 ? 141  GLY J N   1 
ATOM   11054 C  CA  . GLY J  1 142 ? 139.002 117.985 59.021 1.00   23.77 ? 141  GLY J CA  1 
ATOM   11055 C  C   . GLY J  1 142 ? 138.453 116.582 58.943 1.00   24.16 ? 141  GLY J C   1 
ATOM   11056 O  O   . GLY J  1 142 ? 138.374 115.993 57.859 1.00   23.45 ? 141  GLY J O   1 
ATOM   11057 N  N   . SER J  1 143 ? 138.087 116.033 60.100 1.00   24.54 ? 142  SER J N   1 
ATOM   11058 C  CA  . SER J  1 143 ? 137.812 114.600 60.171 1.00   25.23 ? 142  SER J CA  1 
ATOM   11059 C  C   . SER J  1 143 ? 136.462 114.238 59.542 1.00   24.50 ? 142  SER J C   1 
ATOM   11060 O  O   . SER J  1 143 ? 135.599 115.083 59.318 1.00   23.73 ? 142  SER J O   1 
ATOM   11061 C  CB  . SER J  1 143 ? 137.867 114.105 61.614 1.00   26.26 ? 142  SER J CB  1 
ATOM   11062 O  OG  . SER J  1 143 ? 136.757 114.619 62.310 1.00   27.30 ? 142  SER J OG  1 
ATOM   11063 N  N   . ARG J  1 144 ? 136.307 112.951 59.295 1.00   24.26 ? 143  ARG J N   1 
ATOM   11064 C  CA  . ARG J  1 144 ? 135.150 112.376 58.644 1.00   24.43 ? 143  ARG J CA  1 
ATOM   11065 C  C   . ARG J  1 144 ? 134.202 111.868 59.735 1.00   25.31 ? 143  ARG J C   1 
ATOM   11066 O  O   . ARG J  1 144 ? 134.481 110.851 60.355 1.00   25.85 ? 143  ARG J O   1 
ATOM   11067 C  CB  . ARG J  1 144 ? 135.633 111.225 57.747 1.00   23.95 ? 143  ARG J CB  1 
ATOM   11068 C  CG  . ARG J  1 144 ? 136.747 111.676 56.818 1.00   24.22 ? 143  ARG J CG  1 
ATOM   11069 C  CD  . ARG J  1 144 ? 137.263 110.611 55.857 1.00   24.19 ? 143  ARG J CD  1 
ATOM   11070 N  NE  . ARG J  1 144 ? 138.353 111.163 55.059 1.00   24.16 ? 143  ARG J NE  1 
ATOM   11071 C  CZ  . ARG J  1 144 ? 138.911 110.558 54.019 1.00   24.80 ? 143  ARG J CZ  1 
ATOM   11072 N  NH1 . ARG J  1 144 ? 138.510 109.343 53.648 1.00   24.59 ? 143  ARG J NH1 1 
ATOM   11073 N  NH2 . ARG J  1 144 ? 139.896 111.167 53.355 1.00   24.96 ? 143  ARG J NH2 1 
ATOM   11074 N  N   . LEU J  1 145 ? 133.109 112.595 59.982 1.00   25.80 ? 144  LEU J N   1 
ATOM   11075 C  CA  . LEU J  1 145 ? 132.161 112.258 61.052 1.00   26.19 ? 144  LEU J CA  1 
ATOM   11076 C  C   . LEU J  1 145 ? 131.198 111.160 60.639 1.00   26.28 ? 144  LEU J C   1 
ATOM   11077 O  O   . LEU J  1 145 ? 130.813 110.331 61.467 1.00   27.79 ? 144  LEU J O   1 
ATOM   11078 C  CB  . LEU J  1 145 ? 131.383 113.495 61.499 1.00   26.43 ? 144  LEU J CB  1 
ATOM   11079 C  CG  . LEU J  1 145 ? 132.225 114.660 62.069 1.00   26.81 ? 144  LEU J CG  1 
ATOM   11080 C  CD1 . LEU J  1 145 ? 131.305 115.705 62.685 1.00   27.08 ? 144  LEU J CD1 1 
ATOM   11081 C  CD2 . LEU J  1 145 ? 133.224 114.170 63.110 1.00   26.79 ? 144  LEU J CD2 1 
ATOM   11082 N  N   . ALA J  1 146 ? 130.801 111.139 59.372 1.00   24.86 ? 145  ALA J N   1 
ATOM   11083 C  CA  . ALA J  1 146 ? 129.973 110.051 58.881 1.00   25.09 ? 145  ALA J CA  1 
ATOM   11084 C  C   . ALA J  1 146 ? 130.074 109.923 57.372 1.00   24.76 ? 145  ALA J C   1 
ATOM   11085 O  O   . ALA J  1 146 ? 130.457 110.858 56.660 1.00   23.70 ? 145  ALA J O   1 
ATOM   11086 C  CB  . ALA J  1 146 ? 128.519 110.213 59.317 1.00   25.38 ? 145  ALA J CB  1 
ATOM   11087 N  N   . CYS J  1 147 ? 129.757 108.734 56.904 1.00   24.71 ? 146  CYS J N   1 
ATOM   11088 C  CA  . CYS J  1 147 ? 129.905 108.406 55.511 1.00   25.12 ? 146  CYS J CA  1 
ATOM   11089 C  C   . CYS J  1 147 ? 129.048 107.212 55.123 1.00   25.26 ? 146  CYS J C   1 
ATOM   11090 O  O   . CYS J  1 147 ? 128.470 106.529 55.980 1.00   26.34 ? 146  CYS J O   1 
ATOM   11091 C  CB  . CYS J  1 147 ? 131.368 108.107 55.191 1.00   25.35 ? 146  CYS J CB  1 
ATOM   11092 S  SG  . CYS J  1 147 ? 132.091 106.705 56.085 1.00   25.80 ? 146  CYS J SG  1 
ATOM   11093 N  N   . GLY J  1 148 ? 128.958 106.987 53.820 1.00   24.60 ? 147  GLY J N   1 
ATOM   11094 C  CA  . GLY J  1 148 ? 128.280 105.823 53.289 1.00   24.46 ? 147  GLY J CA  1 
ATOM   11095 C  C   . GLY J  1 148 ? 128.555 105.716 51.813 1.00   24.48 ? 147  GLY J C   1 
ATOM   11096 O  O   . GLY J  1 148 ? 128.972 106.702 51.173 1.00   24.03 ? 147  GLY J O   1 
ATOM   11097 N  N   . VAL J  1 149 ? 128.308 104.525 51.276 1.00   24.48 ? 148  VAL J N   1 
ATOM   11098 C  CA  . VAL J  1 149 ? 128.501 104.235 49.863 1.00   23.97 ? 148  VAL J CA  1 
ATOM   11099 C  C   . VAL J  1 149 ? 127.260 104.622 49.079 1.00   24.16 ? 148  VAL J C   1 
ATOM   11100 O  O   . VAL J  1 149 ? 126.144 104.289 49.468 1.00   24.68 ? 148  VAL J O   1 
ATOM   11101 C  CB  . VAL J  1 149 ? 128.812 102.750 49.633 1.00   24.02 ? 148  VAL J CB  1 
ATOM   11102 C  CG1 . VAL J  1 149 ? 129.108 102.484 48.153 1.00   23.92 ? 148  VAL J CG1 1 
ATOM   11103 C  CG2 . VAL J  1 149 ? 129.994 102.345 50.504 1.00   23.82 ? 148  VAL J CG2 1 
ATOM   11104 N  N   . ILE J  1 150 ? 127.462 105.333 47.975 1.00   24.18 ? 149  ILE J N   1 
ATOM   11105 C  CA  . ILE J  1 150 ? 126.359 105.814 47.158 1.00   24.56 ? 149  ILE J CA  1 
ATOM   11106 C  C   . ILE J  1 150 ? 125.824 104.638 46.344 1.00   25.64 ? 149  ILE J C   1 
ATOM   11107 O  O   . ILE J  1 150 ? 126.570 103.999 45.604 1.00   26.27 ? 149  ILE J O   1 
ATOM   11108 C  CB  . ILE J  1 150 ? 126.815 106.957 46.232 1.00   24.41 ? 149  ILE J CB  1 
ATOM   11109 C  CG1 . ILE J  1 150 ? 127.436 108.110 47.060 1.00   23.68 ? 149  ILE J CG1 1 
ATOM   11110 C  CG2 . ILE J  1 150 ? 125.645 107.451 45.394 1.00   24.70 ? 149  ILE J CG2 1 
ATOM   11111 C  CD1 . ILE J  1 150 ? 128.049 109.226 46.244 1.00   23.04 ? 149  ILE J CD1 1 
ATOM   11112 N  N   . GLY J  1 151 ? 124.547 104.323 46.509 1.00   26.28 ? 150  GLY J N   1 
ATOM   11113 C  CA  . GLY J  1 151 ? 123.986 103.126 45.907 1.00   27.41 ? 150  GLY J CA  1 
ATOM   11114 C  C   . GLY J  1 151 ? 122.889 103.429 44.911 1.00   28.47 ? 150  GLY J C   1 
ATOM   11115 O  O   . GLY J  1 151 ? 122.245 104.493 44.981 1.00   28.76 ? 150  GLY J O   1 
ATOM   11116 N  N   . ILE J  1 152 ? 122.663 102.503 43.984 1.00   29.09 ? 151  ILE J N   1 
ATOM   11117 C  CA  . ILE J  1 152 ? 121.594 102.666 42.990 1.00   30.71 ? 151  ILE J CA  1 
ATOM   11118 C  C   . ILE J  1 152 ? 120.234 102.538 43.694 1.00   31.81 ? 151  ILE J C   1 
ATOM   11119 O  O   . ILE J  1 152 ? 120.028 101.625 44.494 1.00   31.31 ? 151  ILE J O   1 
ATOM   11120 C  CB  . ILE J  1 152 ? 121.710 101.659 41.838 1.00   31.67 ? 151  ILE J CB  1 
ATOM   11121 C  CG1 . ILE J  1 152 ? 123.025 101.890 41.077 1.00   31.50 ? 151  ILE J CG1 1 
ATOM   11122 C  CG2 . ILE J  1 152 ? 120.505 101.789 40.900 1.00   32.03 ? 151  ILE J CG2 1 
ATOM   11123 C  CD1 . ILE J  1 152 ? 123.392 100.766 40.115 1.00   32.52 ? 151  ILE J CD1 1 
ATOM   11124 N  N   . ALA J  1 153 ? 119.335 103.485 43.415 1.00   32.48 ? 152  ALA J N   1 
ATOM   11125 C  CA  . ALA J  1 153 ? 118.050 103.604 44.105 1.00   34.19 ? 152  ALA J CA  1 
ATOM   11126 C  C   . ALA J  1 153 ? 116.870 103.411 43.124 1.00   36.89 ? 152  ALA J C   1 
ATOM   11127 O  O   . ALA J  1 153 ? 116.971 103.714 41.923 1.00   36.16 ? 152  ALA J O   1 
ATOM   11128 C  CB  . ALA J  1 153 ? 117.949 104.972 44.785 1.00   33.24 ? 152  ALA J CB  1 
ATOM   11129 N  N   . GLN J  1 154 ? 115.750 102.918 43.642 1.00   39.33 ? 153  GLN J N   1 
ATOM   11130 C  CA  . GLN J  1 154 ? 114.577 102.693 42.804 1.00   43.31 ? 153  GLN J CA  1 
ATOM   11131 C  C   . GLN J  1 154 ? 114.002 104.029 42.367 1.00   44.71 ? 153  GLN J C   1 
ATOM   11132 O  O   . GLN J  1 154 ? 113.772 104.190 41.163 1.00   46.32 ? 153  GLN J O   1 
ATOM   11133 C  CB  . GLN J  1 154 ? 113.507 101.894 43.533 1.00   45.45 ? 153  GLN J CB  1 
ATOM   11134 C  CG  . GLN J  1 154 ? 112.161 101.892 42.822 1.00   48.61 ? 153  GLN J CG  1 
ATOM   11135 C  CD  . GLN J  1 154 ? 111.549 100.517 42.753 1.00   52.02 ? 153  GLN J CD  1 
ATOM   11136 O  OE1 . GLN J  1 154 ? 111.128 99.964  43.768 1.00   55.12 ? 153  GLN J OE1 1 
ATOM   11137 N  NE2 . GLN J  1 154 ? 111.505 99.948  41.548 1.00   54.48 ? 153  GLN J NE2 1 
ATOM   11138 O  OXT . GLN J  1 154 ? 113.776 104.924 43.200 1.00   42.07 ? 153  GLN J OXT 1 
HETATM 11139 CU CU  . CU  K  2 .   ? 119.065 63.505  54.825 1.00   30.95 ? 154  CU  A CU  1 
HETATM 11140 ZN ZN  . ZN  L  3 .   ? 116.241 62.838  48.726 1.00   22.60 ? 155  ZN  A ZN  1 
HETATM 11141 C  C   . CO3 M  4 .   ? 117.425 66.459  55.325 1.00   33.34 ? 156  CO3 A C   1 
HETATM 11142 O  O1  . CO3 M  4 .   ? 117.701 65.330  54.881 1.00   30.46 ? 156  CO3 A O1  1 
HETATM 11143 O  O2  . CO3 M  4 .   ? 116.432 67.041  54.973 1.00   36.08 ? 156  CO3 A O2  1 
HETATM 11144 O  O3  . CO3 M  4 .   ? 118.103 67.067  56.146 1.00   34.62 ? 156  CO3 A O3  1 
HETATM 11145 CU CU  . CU  N  2 .   ? 180.723 118.432 55.028 0.75   32.93 ? 154  CU  B CU  1 
HETATM 11146 ZN ZN  . ZN  O  3 .   ? 181.440 121.313 48.887 0.75   30.02 ? 155  ZN  B ZN  1 
HETATM 11147 C  C   . CO3 P  4 .   ? 183.974 118.480 55.432 0.75   34.79 ? 156  CO3 B C   1 
HETATM 11148 O  O1  . CO3 P  4 .   ? 184.201 117.722 56.376 0.75   34.24 ? 156  CO3 B O1  1 
HETATM 11149 O  O2  . CO3 P  4 .   ? 182.841 118.680 54.973 0.75   33.34 ? 156  CO3 B O2  1 
HETATM 11150 O  O3  . CO3 P  4 .   ? 184.917 119.042 54.945 0.75   36.64 ? 156  CO3 B O3  1 
HETATM 11151 CU CU  . CU  Q  2 .   ? 199.309 37.758  54.891 1.00   29.40 ? 154  CU  C CU  1 
HETATM 11152 ZN ZN  . ZN  R  3 .   ? 200.926 35.427  49.006 1.00   17.83 ? 155  ZN  C ZN  1 
HETATM 11153 C  C   . CO3 S  4 .   ? 195.469 33.244  57.608 1.00   53.15 ? 156  CO3 C C   1 
HETATM 11154 O  O1  . CO3 S  4 .   ? 194.984 32.312  56.964 1.00   55.72 ? 156  CO3 C O1  1 
HETATM 11155 O  O2  . CO3 S  4 .   ? 195.198 33.365  58.803 1.00   53.45 ? 156  CO3 C O2  1 
HETATM 11156 O  O3  . CO3 S  4 .   ? 196.210 34.063  57.058 1.00   50.21 ? 156  CO3 C O3  1 
HETATM 11157 CU CU  . CU  T  2 .   ? 180.039 143.730 53.333 0.60   25.11 ? 154  CU  D CU  1 
HETATM 11158 ZN ZN  . ZN  U  3 .   ? 182.861 145.531 47.536 1.00   40.00 ? 155  ZN  D ZN  1 
HETATM 11159 C  C   . CO3 V  4 .   ? 181.683 140.180 53.179 0.60   36.52 ? 156  CO3 D C   1 
HETATM 11160 O  O1  . CO3 V  4 .   ? 181.482 139.577 54.234 0.60   36.77 ? 156  CO3 D O1  1 
HETATM 11161 O  O2  . CO3 V  4 .   ? 181.747 141.404 53.128 0.60   34.06 ? 156  CO3 D O2  1 
HETATM 11162 O  O3  . CO3 V  4 .   ? 181.784 139.526 52.153 0.60   38.24 ? 156  CO3 D O3  1 
HETATM 11163 CU CU  . CU  W  2 .   ? 118.625 87.501  48.876 0.70   35.28 ? 154  CU  E CU  1 
HETATM 11164 ZN ZN  . ZN  X  3 .   ? 117.655 84.840  42.704 1.00   35.47 ? 155  ZN  E ZN  1 
HETATM 11165 C  C   . CO3 Y  4 .   ? 114.991 87.509  49.630 0.70   39.40 ? 156  CO3 E C   1 
HETATM 11166 O  O1  . CO3 Y  4 .   ? 114.363 86.569  50.071 0.70   40.92 ? 156  CO3 E O1  1 
HETATM 11167 O  O2  . CO3 Y  4 .   ? 114.763 88.623  50.056 0.70   40.04 ? 156  CO3 E O2  1 
HETATM 11168 O  O3  . CO3 Y  4 .   ? 115.863 87.327  48.793 0.70   40.29 ? 156  CO3 E O3  1 
HETATM 11169 CU CU  . CU  Z  2 .   ? 151.725 61.721  57.254 1.00   27.14 ? 154  CU  F CU  1 
HETATM 11170 ZN ZN  . ZN  AA 3 .   ? 155.405 61.018  51.842 1.00   13.39 ? 155  ZN  F ZN  1 
HETATM 11171 C  C   . CO3 BA 4 .   ? 152.901 57.045  60.692 1.00   43.92 ? 156  CO3 F C   1 
HETATM 11172 O  O1  . CO3 BA 4 .   ? 153.397 55.928  60.564 1.00   46.19 ? 156  CO3 F O1  1 
HETATM 11173 O  O2  . CO3 BA 4 .   ? 152.591 57.464  61.800 1.00   44.62 ? 156  CO3 F O2  1 
HETATM 11174 O  O3  . CO3 BA 4 .   ? 152.694 57.745  59.704 1.00   43.11 ? 156  CO3 F O3  1 
HETATM 11175 S  S   . SO4 CA 5 .   ? 165.000 73.031  48.467 1.00   61.60 ? 1154 SO4 F S   1 
HETATM 11176 O  O1  . SO4 CA 5 .   ? 164.099 73.887  49.280 1.00   47.81 ? 1154 SO4 F O1  1 
HETATM 11177 O  O2  . SO4 CA 5 .   ? 166.313 72.773  49.137 1.00   56.66 ? 1154 SO4 F O2  1 
HETATM 11178 O  O3  . SO4 CA 5 .   ? 165.088 73.718  47.159 1.00   56.76 ? 1154 SO4 F O3  1 
HETATM 11179 O  O4  . SO4 CA 5 .   ? 164.421 71.696  48.211 1.00   58.55 ? 1154 SO4 F O4  1 
HETATM 11180 S  S   . SO4 DA 5 .   ? 166.295 72.656  54.034 1.00   78.86 ? 1155 SO4 F S   1 
HETATM 11181 O  O1  . SO4 DA 5 .   ? 166.672 73.174  55.371 1.00   74.08 ? 1155 SO4 F O1  1 
HETATM 11182 O  O2  . SO4 DA 5 .   ? 167.556 72.384  53.297 1.00   76.40 ? 1155 SO4 F O2  1 
HETATM 11183 O  O3  . SO4 DA 5 .   ? 165.525 73.711  53.322 1.00   68.79 ? 1155 SO4 F O3  1 
HETATM 11184 O  O4  . SO4 DA 5 .   ? 165.500 71.400  54.137 1.00   68.79 ? 1155 SO4 F O4  1 
HETATM 11185 CU CU  . CU  EA 2 .   ? 163.837 90.507  57.091 0.80   19.91 ? 154  CU  G CU  1 
HETATM 11186 ZN ZN  . ZN  FA 3 .   ? 161.483 87.733  51.826 1.00   13.65 ? 155  ZN  G ZN  1 
HETATM 11187 C  C   . CO3 GA 4 .   ? 158.958 91.922  61.118 0.50   26.87 ? 156  CO3 G C   1 
HETATM 11188 O  O1  . CO3 GA 4 .   ? 158.012 91.790  60.356 0.50   27.50 ? 156  CO3 G O1  1 
HETATM 11189 O  O2  . CO3 GA 4 .   ? 158.789 92.227  62.290 0.50   27.95 ? 156  CO3 G O2  1 
HETATM 11190 O  O3  . CO3 GA 4 .   ? 160.089 91.776  60.704 0.50   25.93 ? 156  CO3 G O3  1 
HETATM 11191 S  S   . SO4 HA 5 .   ? 164.262 79.383  65.328 0.70   41.57 ? 1154 SO4 G S   1 
HETATM 11192 O  O1  . SO4 HA 5 .   ? 163.614 79.668  66.633 0.70   40.33 ? 1154 SO4 G O1  1 
HETATM 11193 O  O2  . SO4 HA 5 .   ? 165.420 80.297  65.120 0.70   36.23 ? 1154 SO4 G O2  1 
HETATM 11194 O  O3  . SO4 HA 5 .   ? 163.242 79.515  64.260 0.70   34.83 ? 1154 SO4 G O3  1 
HETATM 11195 O  O4  . SO4 HA 5 .   ? 164.806 78.004  65.308 0.70   42.03 ? 1154 SO4 G O4  1 
HETATM 11196 CU CU  . CU  IA 2 .   ? 182.814 65.606  57.218 1.00   28.05 ? 154  CU  H CU  1 
HETATM 11197 ZN ZN  . ZN  JA 3 .   ? 181.427 69.297  51.847 1.00   14.06 ? 155  ZN  H ZN  1 
HETATM 11198 C  C   . CO3 KA 4 .   ? 186.556 69.757  60.516 1.00   43.85 ? 156  CO3 H C   1 
HETATM 11199 O  O1  . CO3 KA 4 .   ? 185.885 69.006  59.829 1.00   44.28 ? 156  CO3 H O1  1 
HETATM 11200 O  O2  . CO3 KA 4 .   ? 186.659 69.443  61.704 1.00   47.21 ? 156  CO3 H O2  1 
HETATM 11201 O  O3  . CO3 KA 4 .   ? 187.121 70.754  60.011 1.00   42.98 ? 156  CO3 H O3  1 
HETATM 11202 CU CU  . CU  LA 2 .   ? 147.407 143.944 56.075 1.00   28.99 ? 154  CU  I CU  1 
HETATM 11203 ZN ZN  . ZN  MA 3 .   ? 143.564 145.443 50.942 1.00   19.28 ? 155  ZN  I ZN  1 
HETATM 11204 C  C   . CO3 NA 4 .   ? 146.027 148.068 60.941 1.00   57.27 ? 156  CO3 I C   1 
HETATM 11205 O  O1  . CO3 NA 4 .   ? 146.479 147.326 60.082 1.00   52.68 ? 156  CO3 I O1  1 
HETATM 11206 O  O2  . CO3 NA 4 .   ? 145.352 149.037 60.610 1.00   59.21 ? 156  CO3 I O2  1 
HETATM 11207 O  O3  . CO3 NA 4 .   ? 146.258 147.841 62.127 1.00   59.42 ? 156  CO3 I O3  1 
HETATM 11208 CU CU  . CU  OA 2 .   ? 135.711 115.127 52.168 1.00   33.23 ? 154  CU  J CU  1 
HETATM 11209 ZN ZN  . ZN  PA 3 .   ? 137.979 118.464 47.086 1.00   20.18 ? 155  ZN  J ZN  1 
HETATM 11210 C  C   . CO3 QA 4 .   ? 140.630 113.549 55.471 1.00   55.78 ? 156  CO3 J C   1 
HETATM 11211 O  O1  . CO3 QA 4 .   ? 140.081 113.429 56.565 1.00   52.13 ? 156  CO3 J O1  1 
HETATM 11212 O  O2  . CO3 QA 4 .   ? 139.964 113.854 54.492 1.00   56.08 ? 156  CO3 J O2  1 
HETATM 11213 O  O3  . CO3 QA 4 .   ? 141.836 113.355 55.330 1.00   58.43 ? 156  CO3 J O3  1 
HETATM 11214 S  S   . SO4 RA 5 .   ? 133.252 134.380 46.063 0.50   45.78 ? 1154 SO4 J S   1 
HETATM 11215 O  O1  . SO4 RA 5 .   ? 133.589 134.753 47.459 0.50   45.65 ? 1154 SO4 J O1  1 
HETATM 11216 O  O2  . SO4 RA 5 .   ? 132.741 135.570 45.339 0.50   40.18 ? 1154 SO4 J O2  1 
HETATM 11217 O  O3  . SO4 RA 5 .   ? 132.176 133.358 46.139 0.50   45.09 ? 1154 SO4 J O3  1 
HETATM 11218 O  O4  . SO4 RA 5 .   ? 134.439 133.823 45.364 0.50   39.97 ? 1154 SO4 J O4  1 
HETATM 11219 S  S   . SO4 SA 5 .   ? 133.156 132.304 50.456 0.50   64.07 ? 1155 SO4 J S   1 
HETATM 11220 O  O1  . SO4 SA 5 .   ? 133.603 131.801 49.139 0.50   64.04 ? 1155 SO4 J O1  1 
HETATM 11221 O  O2  . SO4 SA 5 .   ? 133.082 131.156 51.390 0.50   60.95 ? 1155 SO4 J O2  1 
HETATM 11222 O  O3  . SO4 SA 5 .   ? 131.829 132.954 50.328 0.50   61.83 ? 1155 SO4 J O3  1 
HETATM 11223 O  O4  . SO4 SA 5 .   ? 134.124 133.310 50.954 0.50   61.34 ? 1155 SO4 J O4  1 
HETATM 11224 O  O   . HOH TA 6 .   ? 137.840 53.149  41.276 1.00   38.61 ? 2001 HOH A O   1 
HETATM 11225 O  O   . HOH TA 6 .   ? 137.373 54.157  45.217 1.00   45.33 ? 2002 HOH A O   1 
HETATM 11226 O  O   . HOH TA 6 .   ? 138.995 51.108  47.131 1.00   25.03 ? 2003 HOH A O   1 
HETATM 11227 O  O   . HOH TA 6 .   ? 134.884 49.469  54.065 1.00   24.50 ? 2004 HOH A O   1 
HETATM 11228 O  O   . HOH TA 6 .   ? 120.837 61.773  69.069 1.00   27.19 ? 2005 HOH A O   1 
HETATM 11229 O  O   . HOH TA 6 .   ? 134.039 58.934  57.945 1.00   12.79 ? 2006 HOH A O   1 
HETATM 11230 O  O   . HOH TA 6 .   ? 135.452 57.568  57.736 1.00   31.77 ? 2007 HOH A O   1 
HETATM 11231 O  O   . HOH TA 6 .   ? 133.026 60.829  61.363 1.00   25.63 ? 2008 HOH A O   1 
HETATM 11232 O  O   . HOH TA 6 .   ? 130.458 52.438  66.058 1.00   44.37 ? 2009 HOH A O   1 
HETATM 11233 O  O   . HOH TA 6 .   ? 135.039 48.301  61.072 1.00   42.11 ? 2010 HOH A O   1 
HETATM 11234 O  O   . HOH TA 6 .   ? 129.752 64.942  62.902 1.00   42.75 ? 2011 HOH A O   1 
HETATM 11235 O  O   . HOH TA 6 .   ? 133.172 58.386  69.875 1.00   63.78 ? 2012 HOH A O   1 
HETATM 11236 O  O   . HOH TA 6 .   ? 134.867 56.399  69.504 1.00   52.22 ? 2013 HOH A O   1 
HETATM 11237 O  O   . HOH TA 6 .   ? 127.858 60.420  68.027 1.00   23.39 ? 2014 HOH A O   1 
HETATM 11238 O  O   . HOH TA 6 .   ? 125.809 39.473  44.382 1.00   47.44 ? 2015 HOH A O   1 
HETATM 11239 O  O   . HOH TA 6 .   ? 131.961 38.237  39.547 1.00   52.62 ? 2016 HOH A O   1 
HETATM 11240 O  O   . HOH TA 6 .   ? 131.869 62.447  68.850 1.00   49.60 ? 2017 HOH A O   1 
HETATM 11241 O  O   . HOH TA 6 .   ? 123.970 65.026  66.518 1.00   31.47 ? 2018 HOH A O   1 
HETATM 11242 O  O   . HOH TA 6 .   ? 123.662 61.514  67.945 1.00   24.95 ? 2019 HOH A O   1 
HETATM 11243 O  O   . HOH TA 6 .   ? 126.026 54.960  71.559 1.00   32.15 ? 2020 HOH A O   1 
HETATM 11244 O  O   . HOH TA 6 .   ? 125.776 50.956  73.546 1.00   28.01 ? 2021 HOH A O   1 
HETATM 11245 O  O   . HOH TA 6 .   ? 124.466 49.390  71.681 1.00   28.55 ? 2022 HOH A O   1 
HETATM 11246 O  O   . HOH TA 6 .   ? 131.946 54.323  65.345 1.00   40.69 ? 2023 HOH A O   1 
HETATM 11247 O  O   . HOH TA 6 .   ? 117.088 62.474  69.361 1.00   48.51 ? 2024 HOH A O   1 
HETATM 11248 O  O   . HOH TA 6 .   ? 130.091 48.209  61.181 1.00   40.82 ? 2025 HOH A O   1 
HETATM 11249 O  O   . HOH TA 6 .   ? 132.416 47.319  60.122 1.00   32.19 ? 2026 HOH A O   1 
HETATM 11250 O  O   . HOH TA 6 .   ? 135.236 48.901  58.364 1.00   25.52 ? 2027 HOH A O   1 
HETATM 11251 O  O   . HOH TA 6 .   ? 130.422 44.652  44.986 1.00   34.10 ? 2028 HOH A O   1 
HETATM 11252 O  O   . HOH TA 6 .   ? 128.685 45.099  44.164 1.00   44.46 ? 2029 HOH A O   1 
HETATM 11253 O  O   . HOH TA 6 .   ? 134.310 49.414  40.833 1.00   22.34 ? 2030 HOH A O   1 
HETATM 11254 O  O   . HOH TA 6 .   ? 133.778 52.028  41.130 1.00   24.99 ? 2031 HOH A O   1 
HETATM 11255 O  O   . HOH TA 6 .   ? 129.497 46.072  41.416 1.00   24.58 ? 2032 HOH A O   1 
HETATM 11256 O  O   . HOH TA 6 .   ? 128.793 39.951  43.751 1.00   61.10 ? 2033 HOH A O   1 
HETATM 11257 O  O   . HOH TA 6 .   ? 131.080 39.014  47.465 1.00   58.09 ? 2034 HOH A O   1 
HETATM 11258 O  O   . HOH TA 6 .   ? 128.741 45.269  35.964 1.00   47.32 ? 2035 HOH A O   1 
HETATM 11259 O  O   . HOH TA 6 .   ? 131.262 41.022  40.321 1.00   50.80 ? 2036 HOH A O   1 
HETATM 11260 O  O   . HOH TA 6 .   ? 116.420 68.762  47.472 1.00   50.34 ? 2037 HOH A O   1 
HETATM 11261 O  O   . HOH TA 6 .   ? 132.186 52.252  34.247 1.00   15.94 ? 2038 HOH A O   1 
HETATM 11262 O  O   . HOH TA 6 .   ? 124.060 47.854  37.883 1.00   34.96 ? 2039 HOH A O   1 
HETATM 11263 O  O   . HOH TA 6 .   ? 125.395 48.911  34.216 1.00   21.69 ? 2040 HOH A O   1 
HETATM 11264 O  O   . HOH TA 6 .   ? 125.746 51.495  40.814 1.00   20.60 ? 2041 HOH A O   1 
HETATM 11265 O  O   . HOH TA 6 .   ? 112.710 51.480  50.246 1.00   36.50 ? 2042 HOH A O   1 
HETATM 11266 O  O   . HOH TA 6 .   ? 117.420 49.718  49.468 1.00   23.92 ? 2043 HOH A O   1 
HETATM 11267 O  O   . HOH TA 6 .   ? 118.533 58.263  39.432 1.00   34.55 ? 2044 HOH A O   1 
HETATM 11268 O  O   . HOH TA 6 .   ? 108.736 51.727  53.874 1.00   44.27 ? 2045 HOH A O   1 
HETATM 11269 O  O   . HOH TA 6 .   ? 124.644 44.493  58.465 1.00   34.31 ? 2046 HOH A O   1 
HETATM 11270 O  O   . HOH TA 6 .   ? 128.244 44.980  60.502 1.00   46.25 ? 2047 HOH A O   1 
HETATM 11271 O  O   . HOH TA 6 .   ? 126.372 48.586  66.727 1.00   39.13 ? 2048 HOH A O   1 
HETATM 11272 O  O   . HOH TA 6 .   ? 122.457 45.254  71.055 1.00   46.59 ? 2049 HOH A O   1 
HETATM 11273 O  O   . HOH TA 6 .   ? 130.053 49.055  68.888 1.00   37.54 ? 2050 HOH A O   1 
HETATM 11274 O  O   . HOH TA 6 .   ? 128.373 51.738  72.907 1.00   26.88 ? 2051 HOH A O   1 
HETATM 11275 O  O   . HOH TA 6 .   ? 122.324 50.952  70.845 1.00   26.57 ? 2052 HOH A O   1 
HETATM 11276 O  O   . HOH TA 6 .   ? 121.901 52.948  72.575 1.00   29.69 ? 2053 HOH A O   1 
HETATM 11277 O  O   . HOH TA 6 .   ? 119.213 58.674  69.271 1.00   21.42 ? 2054 HOH A O   1 
HETATM 11278 O  O   . HOH TA 6 .   ? 117.170 52.846  71.541 1.00   24.42 ? 2055 HOH A O   1 
HETATM 11279 O  O   . HOH TA 6 .   ? 120.614 43.246  49.260 1.00   51.67 ? 2056 HOH A O   1 
HETATM 11280 O  O   . HOH TA 6 .   ? 117.597 57.691  67.465 1.00   21.72 ? 2057 HOH A O   1 
HETATM 11281 O  O   . HOH TA 6 .   ? 116.597 58.722  67.327 1.00   26.12 ? 2058 HOH A O   1 
HETATM 11282 O  O   . HOH TA 6 .   ? 112.254 55.877  66.454 1.00   39.82 ? 2059 HOH A O   1 
HETATM 11283 O  O   . HOH TA 6 .   ? 114.979 59.953  66.767 1.00   24.44 ? 2060 HOH A O   1 
HETATM 11284 O  O   . HOH TA 6 .   ? 121.332 50.756  36.118 1.00   51.70 ? 2061 HOH A O   1 
HETATM 11285 O  O   . HOH TA 6 .   ? 114.887 52.153  71.704 1.00   32.36 ? 2062 HOH A O   1 
HETATM 11286 O  O   . HOH TA 6 .   ? 113.567 53.444  71.415 1.00   24.84 ? 2063 HOH A O   1 
HETATM 11287 O  O   . HOH TA 6 .   ? 110.702 54.161  69.185 1.00   38.58 ? 2064 HOH A O   1 
HETATM 11288 O  O   . HOH TA 6 .   ? 134.819 56.297  35.986 1.00   36.08 ? 2065 HOH A O   1 
HETATM 11289 O  O   . HOH TA 6 .   ? 136.244 63.956  39.565 1.00   39.57 ? 2066 HOH A O   1 
HETATM 11290 O  O   . HOH TA 6 .   ? 126.362 64.106  37.473 1.00   44.89 ? 2067 HOH A O   1 
HETATM 11291 O  O   . HOH TA 6 .   ? 109.260 53.662  62.890 1.00   30.75 ? 2068 HOH A O   1 
HETATM 11292 O  O   . HOH TA 6 .   ? 111.488 56.281  64.019 1.00   32.16 ? 2069 HOH A O   1 
HETATM 11293 O  O   . HOH TA 6 .   ? 111.276 58.939  68.244 1.00   51.67 ? 2070 HOH A O   1 
HETATM 11294 O  O   . HOH TA 6 .   ? 107.645 61.172  61.765 1.00   55.19 ? 2071 HOH A O   1 
HETATM 11295 O  O   . HOH TA 6 .   ? 108.093 61.225  65.266 1.00   61.43 ? 2072 HOH A O   1 
HETATM 11296 O  O   . HOH TA 6 .   ? 106.932 56.017  58.194 1.00   39.52 ? 2073 HOH A O   1 
HETATM 11297 O  O   . HOH TA 6 .   ? 107.148 54.222  53.848 1.00   48.01 ? 2074 HOH A O   1 
HETATM 11298 O  O   . HOH TA 6 .   ? 103.480 55.214  51.230 1.00   36.34 ? 2075 HOH A O   1 
HETATM 11299 O  O   . HOH TA 6 .   ? 122.844 67.839  44.491 1.00   29.37 ? 2076 HOH A O   1 
HETATM 11300 O  O   . HOH TA 6 .   ? 123.399 72.150  46.145 1.00   22.57 ? 2077 HOH A O   1 
HETATM 11301 O  O   . HOH TA 6 .   ? 125.366 71.175  43.137 1.00   37.69 ? 2078 HOH A O   1 
HETATM 11302 O  O   . HOH TA 6 .   ? 124.945 67.796  42.344 1.00   43.92 ? 2079 HOH A O   1 
HETATM 11303 O  O   . HOH TA 6 .   ? 128.697 68.687  44.442 1.00   26.51 ? 2080 HOH A O   1 
HETATM 11304 O  O   . HOH TA 6 .   ? 134.303 68.149  56.148 1.00   13.83 ? 2081 HOH A O   1 
HETATM 11305 O  O   . HOH TA 6 .   ? 130.555 73.156  51.726 1.00   18.95 ? 2082 HOH A O   1 
HETATM 11306 O  O   . HOH TA 6 .   ? 132.952 75.264  54.228 1.00   28.62 ? 2083 HOH A O   1 
HETATM 11307 O  O   . HOH TA 6 .   ? 113.163 69.000  58.915 1.00   45.25 ? 2084 HOH A O   1 
HETATM 11308 O  O   . HOH TA 6 .   ? 133.067 68.623  62.969 1.00   31.42 ? 2085 HOH A O   1 
HETATM 11309 O  O   . HOH TA 6 .   ? 134.759 65.584  62.081 1.00   35.21 ? 2086 HOH A O   1 
HETATM 11310 O  O   . HOH TA 6 .   ? 131.623 63.597  61.428 1.00   47.15 ? 2087 HOH A O   1 
HETATM 11311 O  O   . HOH TA 6 .   ? 120.028 71.353  58.465 1.00   35.20 ? 2088 HOH A O   1 
HETATM 11312 O  O   . HOH TA 6 .   ? 118.726 73.598  55.496 1.00   43.41 ? 2089 HOH A O   1 
HETATM 11313 O  O   . HOH TA 6 .   ? 119.726 73.181  51.432 1.00   44.61 ? 2090 HOH A O   1 
HETATM 11314 O  O   . HOH TA 6 .   ? 134.153 72.116  62.928 1.00   34.46 ? 2091 HOH A O   1 
HETATM 11315 O  O   . HOH TA 6 .   ? 132.742 76.159  56.702 1.00   28.42 ? 2092 HOH A O   1 
HETATM 11316 O  O   . HOH TA 6 .   ? 126.110 67.583  63.813 1.00   28.36 ? 2093 HOH A O   1 
HETATM 11317 O  O   . HOH TA 6 .   ? 122.578 71.442  55.183 1.00   28.40 ? 2094 HOH A O   1 
HETATM 11318 O  O   . HOH TA 6 .   ? 122.161 74.727  56.826 1.00   26.63 ? 2095 HOH A O   1 
HETATM 11319 O  O   . HOH TA 6 .   ? 121.584 69.573  61.642 1.00   42.11 ? 2096 HOH A O   1 
HETATM 11320 O  O   . HOH TA 6 .   ? 127.970 73.514  52.540 1.00   15.50 ? 2097 HOH A O   1 
HETATM 11321 O  O   . HOH TA 6 .   ? 117.369 67.534  49.991 1.00   28.97 ? 2098 HOH A O   1 
HETATM 11322 O  O   . HOH TA 6 .   ? 118.821 68.125  46.775 1.00   36.88 ? 2099 HOH A O   1 
HETATM 11323 O  O   . HOH TA 6 .   ? 120.838 69.543  41.729 1.00   48.80 ? 2100 HOH A O   1 
HETATM 11324 O  O   . HOH TA 6 .   ? 119.903 62.959  41.237 1.00   15.38 ? 2101 HOH A O   1 
HETATM 11325 O  O   . HOH TA 6 .   ? 115.776 69.431  41.727 1.00   41.01 ? 2102 HOH A O   1 
HETATM 11326 O  O   . HOH TA 6 .   ? 117.888 69.043  44.848 1.00   37.63 ? 2103 HOH A O   1 
HETATM 11327 O  O   . HOH TA 6 .   ? 120.328 68.184  36.600 1.00   46.66 ? 2104 HOH A O   1 
HETATM 11328 O  O   . HOH TA 6 .   ? 114.047 67.550  45.465 1.00   37.49 ? 2105 HOH A O   1 
HETATM 11329 O  O   . HOH TA 6 .   ? 113.013 59.985  36.788 1.00   72.81 ? 2106 HOH A O   1 
HETATM 11330 O  O   . HOH TA 6 .   ? 109.490 60.201  44.204 1.00   30.51 ? 2107 HOH A O   1 
HETATM 11331 O  O   . HOH TA 6 .   ? 115.210 57.998  50.679 1.00   16.44 ? 2108 HOH A O   1 
HETATM 11332 O  O   . HOH TA 6 .   ? 112.061 52.536  47.884 1.00   23.49 ? 2109 HOH A O   1 
HETATM 11333 O  O   . HOH TA 6 .   ? 115.861 53.646  40.959 1.00   39.18 ? 2110 HOH A O   1 
HETATM 11334 O  O   . HOH TA 6 .   ? 118.936 50.316  47.244 1.00   26.20 ? 2111 HOH A O   1 
HETATM 11335 O  O   . HOH TA 6 .   ? 118.965 50.681  43.640 1.00   29.63 ? 2112 HOH A O   1 
HETATM 11336 O  O   . HOH TA 6 .   ? 109.287 56.699  39.928 1.00   43.89 ? 2113 HOH A O   1 
HETATM 11337 O  O   . HOH TA 6 .   ? 112.373 54.798  33.634 1.00   60.44 ? 2114 HOH A O   1 
HETATM 11338 O  O   . HOH TA 6 .   ? 111.762 65.969  38.493 1.00   45.61 ? 2115 HOH A O   1 
HETATM 11339 O  O   . HOH TA 6 .   ? 118.536 60.821  40.416 1.00   19.68 ? 2116 HOH A O   1 
HETATM 11340 O  O   . HOH TA 6 .   ? 117.438 51.084  51.766 1.00   27.05 ? 2117 HOH A O   1 
HETATM 11341 O  O   . HOH TA 6 .   ? 114.084 52.103  52.609 1.00   26.32 ? 2118 HOH A O   1 
HETATM 11342 O  O   . HOH TA 6 .   ? 115.232 51.003  52.949 1.00   42.57 ? 2119 HOH A O   1 
HETATM 11343 O  O   . HOH TA 6 .   ? 117.546 49.890  54.508 1.00   25.61 ? 2120 HOH A O   1 
HETATM 11344 O  O   . HOH TA 6 .   ? 114.964 49.406  56.869 1.00   36.49 ? 2121 HOH A O   1 
HETATM 11345 O  O   . HOH TA 6 .   ? 113.231 50.188  54.850 1.00   48.91 ? 2122 HOH A O   1 
HETATM 11346 O  O   . HOH TA 6 .   ? 111.396 52.244  54.401 1.00   36.65 ? 2123 HOH A O   1 
HETATM 11347 O  O   . HOH TA 6 .   ? 118.333 48.456  58.735 1.00   26.30 ? 2124 HOH A O   1 
HETATM 11348 O  O   . HOH TA 6 .   ? 118.415 46.406  62.321 1.00   28.92 ? 2125 HOH A O   1 
HETATM 11349 O  O   . HOH TA 6 .   ? 121.114 44.596  68.571 1.00   30.02 ? 2126 HOH A O   1 
HETATM 11350 O  O   . HOH TA 6 .   ? 119.435 45.013  64.395 1.00   49.65 ? 2127 HOH A O   1 
HETATM 11351 O  O   . HOH TA 6 .   ? 113.776 44.127  68.382 1.00   27.52 ? 2128 HOH A O   1 
HETATM 11352 O  O   . HOH TA 6 .   ? 113.149 40.357  70.437 1.00   61.59 ? 2129 HOH A O   1 
HETATM 11353 O  O   . HOH TA 6 .   ? 119.514 44.243  57.986 1.00   39.60 ? 2130 HOH A O   1 
HETATM 11354 O  O   . HOH TA 6 .   ? 122.837 43.639  66.355 1.00   47.36 ? 2131 HOH A O   1 
HETATM 11355 O  O   . HOH TA 6 .   ? 119.144 48.274  55.925 1.00   25.08 ? 2132 HOH A O   1 
HETATM 11356 O  O   . HOH TA 6 .   ? 123.556 42.628  49.641 1.00   56.28 ? 2133 HOH A O   1 
HETATM 11357 O  O   . HOH TA 6 .   ? 118.269 47.362  49.117 1.00   40.98 ? 2134 HOH A O   1 
HETATM 11358 O  O   . HOH TA 6 .   ? 119.162 45.502  48.583 1.00   49.49 ? 2135 HOH A O   1 
HETATM 11359 O  O   . HOH TA 6 .   ? 120.815 47.056  43.394 1.00   42.69 ? 2136 HOH A O   1 
HETATM 11360 O  O   . HOH TA 6 .   ? 119.759 51.595  38.489 1.00   45.74 ? 2137 HOH A O   1 
HETATM 11361 O  O   . HOH TA 6 .   ? 136.571 56.273  42.628 1.00   32.19 ? 2138 HOH A O   1 
HETATM 11362 O  O   . HOH TA 6 .   ? 135.730 53.987  36.665 1.00   41.75 ? 2139 HOH A O   1 
HETATM 11363 O  O   . HOH TA 6 .   ? 133.821 61.884  39.973 1.00   42.85 ? 2140 HOH A O   1 
HETATM 11364 O  O   . HOH TA 6 .   ? 132.744 61.993  36.915 1.00   46.36 ? 2141 HOH A O   1 
HETATM 11365 O  O   . HOH TA 6 .   ? 127.751 64.894  39.470 1.00   40.74 ? 2142 HOH A O   1 
HETATM 11366 O  O   . HOH TA 6 .   ? 130.088 62.643  42.194 1.00   19.52 ? 2143 HOH A O   1 
HETATM 11367 O  O   . HOH TA 6 .   ? 124.256 62.414  37.102 1.00   35.86 ? 2144 HOH A O   1 
HETATM 11368 O  O   . HOH TA 6 .   ? 130.162 67.549  42.701 1.00   38.43 ? 2145 HOH A O   1 
HETATM 11369 O  O   . HOH TA 6 .   ? 111.489 58.942  65.507 1.00   63.66 ? 2146 HOH A O   1 
HETATM 11370 O  O   . HOH TA 6 .   ? 108.780 58.861  62.186 1.00   37.52 ? 2147 HOH A O   1 
HETATM 11371 O  O   . HOH TA 6 .   ? 109.972 57.450  63.165 1.00   35.99 ? 2148 HOH A O   1 
HETATM 11372 O  O   . HOH TA 6 .   ? 108.568 61.149  58.873 1.00   37.13 ? 2149 HOH A O   1 
HETATM 11373 O  O   . HOH TA 6 .   ? 108.092 55.401  55.941 1.00   38.52 ? 2150 HOH A O   1 
HETATM 11374 O  O   . HOH TA 6 .   ? 106.269 55.790  51.630 1.00   38.71 ? 2151 HOH A O   1 
HETATM 11375 O  O   . HOH TA 6 .   ? 108.627 63.292  46.173 1.00   48.85 ? 2152 HOH A O   1 
HETATM 11376 O  O   . HOH TA 6 .   ? 104.125 63.261  48.236 1.00   38.01 ? 2153 HOH A O   1 
HETATM 11377 O  O   . HOH TA 6 .   ? 102.465 71.142  52.573 1.00   45.59 ? 2154 HOH A O   1 
HETATM 11378 O  O   . HOH TA 6 .   ? 109.274 67.494  58.436 1.00   42.45 ? 2155 HOH A O   1 
HETATM 11379 O  O   . HOH TA 6 .   ? 105.410 64.504  58.398 1.00   47.18 ? 2156 HOH A O   1 
HETATM 11380 O  O   . HOH TA 6 .   ? 112.179 66.937  58.128 1.00   31.06 ? 2157 HOH A O   1 
HETATM 11381 O  O   . HOH TA 6 .   ? 114.624 68.619  61.493 1.00   43.40 ? 2158 HOH A O   1 
HETATM 11382 O  O   . HOH TA 6 .   ? 119.439 65.877  66.570 1.00   48.96 ? 2159 HOH A O   1 
HETATM 11383 O  O   . HOH TA 6 .   ? 119.770 68.734  61.910 1.00   25.28 ? 2160 HOH A O   1 
HETATM 11384 O  O   . HOH TA 6 .   ? 123.410 67.984  62.947 1.00   39.61 ? 2161 HOH A O   1 
HETATM 11385 O  O   . HOH TA 6 .   ? 120.598 69.746  59.672 1.00   36.86 ? 2162 HOH A O   1 
HETATM 11386 O  O   . HOH TA 6 .   ? 120.536 72.015  53.465 1.00   18.91 ? 2163 HOH A O   1 
HETATM 11387 O  O   . HOH TA 6 .   ? 133.980 61.906  58.581 1.00   22.70 ? 2164 HOH A O   1 
HETATM 11388 O  O   . HOH TA 6 .   ? 140.923 51.138  54.741 1.00   19.74 ? 2165 HOH A O   1 
HETATM 11389 O  O   . HOH TA 6 .   ? 117.974 67.881  52.693 1.00   34.70 ? 2166 HOH A O   1 
HETATM 11390 O  O   . HOH UA 6 .   ? 163.720 106.635 40.635 1.00   42.33 ? 2001 HOH B O   1 
HETATM 11391 O  O   . HOH UA 6 .   ? 161.962 106.754 41.754 1.00   44.03 ? 2002 HOH B O   1 
HETATM 11392 O  O   . HOH UA 6 .   ? 164.197 110.921 41.085 1.00   32.16 ? 2003 HOH B O   1 
HETATM 11393 O  O   . HOH UA 6 .   ? 160.440 106.768 47.216 1.00   29.76 ? 2004 HOH B O   1 
HETATM 11394 O  O   . HOH UA 6 .   ? 154.336 113.710 48.138 1.00   51.92 ? 2005 HOH B O   1 
HETATM 11395 O  O   . HOH UA 6 .   ? 161.080 111.116 54.054 1.00   35.71 ? 2006 HOH B O   1 
HETATM 11396 O  O   . HOH UA 6 .   ? 172.287 110.033 68.252 1.00   33.35 ? 2007 HOH B O   1 
HETATM 11397 O  O   . HOH UA 6 .   ? 175.889 106.666 66.368 1.00   39.12 ? 2008 HOH B O   1 
HETATM 11398 O  O   . HOH UA 6 .   ? 173.444 107.721 69.148 1.00   43.65 ? 2009 HOH B O   1 
HETATM 11399 O  O   . HOH UA 6 .   ? 177.879 117.528 68.864 1.00   45.92 ? 2010 HOH B O   1 
HETATM 11400 O  O   . HOH UA 6 .   ? 169.374 107.379 57.910 1.00   20.36 ? 2011 HOH B O   1 
HETATM 11401 O  O   . HOH UA 6 .   ? 172.156 107.505 61.294 1.00   31.09 ? 2012 HOH B O   1 
HETATM 11402 O  O   . HOH UA 6 .   ? 175.028 107.955 61.977 1.00   36.28 ? 2013 HOH B O   1 
HETATM 11403 O  O   . HOH UA 6 .   ? 173.748 112.384 68.308 1.00   27.90 ? 2014 HOH B O   1 
HETATM 11404 O  O   . HOH UA 6 .   ? 177.646 108.054 66.103 1.00   42.76 ? 2015 HOH B O   1 
HETATM 11405 O  O   . HOH UA 6 .   ? 176.457 108.165 70.494 1.00   45.49 ? 2016 HOH B O   1 
HETATM 11406 O  O   . HOH UA 6 .   ? 179.837 113.606 66.389 1.00   39.70 ? 2017 HOH B O   1 
HETATM 11407 O  O   . HOH UA 6 .   ? 177.650 109.660 72.850 1.00   22.78 ? 2018 HOH B O   1 
HETATM 11408 O  O   . HOH UA 6 .   ? 180.745 113.570 72.818 1.00   35.63 ? 2019 HOH B O   1 
HETATM 11409 O  O   . HOH UA 6 .   ? 181.111 110.122 64.054 1.00   29.87 ? 2020 HOH B O   1 
HETATM 11410 O  O   . HOH UA 6 .   ? 176.585 115.283 68.065 1.00   24.49 ? 2021 HOH B O   1 
HETATM 11411 O  O   . HOH UA 6 .   ? 169.993 115.745 71.596 1.00   25.45 ? 2022 HOH B O   1 
HETATM 11412 O  O   . HOH UA 6 .   ? 168.967 112.285 73.802 1.00   30.97 ? 2023 HOH B O   1 
HETATM 11413 O  O   . HOH UA 6 .   ? 166.905 108.800 70.606 1.00   51.27 ? 2024 HOH B O   1 
HETATM 11414 O  O   . HOH UA 6 .   ? 180.399 121.841 68.986 1.00   42.19 ? 2025 HOH B O   1 
HETATM 11415 O  O   . HOH UA 6 .   ? 160.539 111.055 58.311 1.00   32.77 ? 2026 HOH B O   1 
HETATM 11416 O  O   . HOH UA 6 .   ? 174.643 103.562 59.515 1.00   36.77 ? 2027 HOH B O   1 
HETATM 11417 O  O   . HOH UA 6 .   ? 160.639 117.415 41.314 1.00   47.85 ? 2028 HOH B O   1 
HETATM 11418 O  O   . HOH UA 6 .   ? 151.665 119.382 44.952 1.00   54.38 ? 2029 HOH B O   1 
HETATM 11419 O  O   . HOH UA 6 .   ? 160.379 118.482 35.376 1.00   56.41 ? 2030 HOH B O   1 
HETATM 11420 O  O   . HOH UA 6 .   ? 164.892 112.358 33.992 1.00   26.34 ? 2031 HOH B O   1 
HETATM 11421 O  O   . HOH UA 6 .   ? 164.001 121.982 36.210 1.00   58.97 ? 2032 HOH B O   1 
HETATM 11422 O  O   . HOH UA 6 .   ? 164.447 118.165 31.585 1.00   37.07 ? 2033 HOH B O   1 
HETATM 11423 O  O   . HOH UA 6 .   ? 169.494 126.241 49.465 1.00   37.33 ? 2034 HOH B O   1 
HETATM 11424 O  O   . HOH UA 6 .   ? 156.589 116.049 57.132 1.00   45.30 ? 2035 HOH B O   1 
HETATM 11425 O  O   . HOH UA 6 .   ? 160.930 122.253 58.541 1.00   44.08 ? 2036 HOH B O   1 
HETATM 11426 O  O   . HOH UA 6 .   ? 160.803 127.550 57.962 1.00   37.66 ? 2037 HOH B O   1 
HETATM 11427 O  O   . HOH UA 6 .   ? 168.278 121.357 71.014 1.00   30.40 ? 2038 HOH B O   1 
HETATM 11428 O  O   . HOH UA 6 .   ? 176.023 120.676 69.447 1.00   42.24 ? 2039 HOH B O   1 
HETATM 11429 O  O   . HOH UA 6 .   ? 176.697 122.615 67.371 1.00   34.15 ? 2040 HOH B O   1 
HETATM 11430 O  O   . HOH UA 6 .   ? 178.821 123.494 67.136 1.00   44.14 ? 2041 HOH B O   1 
HETATM 11431 O  O   . HOH UA 6 .   ? 173.599 127.880 71.471 1.00   39.62 ? 2042 HOH B O   1 
HETATM 11432 O  O   . HOH UA 6 .   ? 168.058 132.623 67.632 1.00   34.99 ? 2043 HOH B O   1 
HETATM 11433 O  O   . HOH UA 6 .   ? 174.018 133.510 67.608 1.00   61.89 ? 2044 HOH B O   1 
HETATM 11434 O  O   . HOH UA 6 .   ? 174.422 106.630 41.316 1.00   42.87 ? 2045 HOH B O   1 
HETATM 11435 O  O   . HOH UA 6 .   ? 185.089 129.701 61.826 1.00   38.73 ? 2046 HOH B O   1 
HETATM 11436 O  O   . HOH UA 6 .   ? 186.964 110.092 47.173 1.00   38.74 ? 2047 HOH B O   1 
HETATM 11437 O  O   . HOH UA 6 .   ? 181.013 107.723 44.430 1.00   41.78 ? 2048 HOH B O   1 
HETATM 11438 O  O   . HOH UA 6 .   ? 177.558 102.684 56.272 1.00   18.97 ? 2049 HOH B O   1 
HETATM 11439 O  O   . HOH UA 6 .   ? 179.345 108.145 57.686 1.00   35.53 ? 2050 HOH B O   1 
HETATM 11440 O  O   . HOH UA 6 .   ? 184.176 103.825 51.804 1.00   27.19 ? 2051 HOH B O   1 
HETATM 11441 O  O   . HOH UA 6 .   ? 184.384 100.362 54.257 1.00   36.55 ? 2052 HOH B O   1 
HETATM 11442 O  O   . HOH UA 6 .   ? 180.046 103.077 63.848 1.00   42.59 ? 2053 HOH B O   1 
HETATM 11443 O  O   . HOH UA 6 .   ? 175.589 103.408 62.251 1.00   35.81 ? 2054 HOH B O   1 
HETATM 11444 O  O   . HOH UA 6 .   ? 175.186 106.570 59.526 1.00   36.68 ? 2055 HOH B O   1 
HETATM 11445 O  O   . HOH UA 6 .   ? 177.420 107.944 63.176 1.00   49.29 ? 2056 HOH B O   1 
HETATM 11446 O  O   . HOH UA 6 .   ? 177.019 107.487 57.751 1.00   32.09 ? 2057 HOH B O   1 
HETATM 11447 O  O   . HOH UA 6 .   ? 181.350 100.683 63.478 1.00   47.17 ? 2058 HOH B O   1 
HETATM 11448 O  O   . HOH UA 6 .   ? 186.461 101.983 58.267 1.00   45.22 ? 2059 HOH B O   1 
HETATM 11449 O  O   . HOH UA 6 .   ? 151.441 99.528  52.036 1.00   59.53 ? 2060 HOH B O   1 
HETATM 11450 O  O   . HOH UA 6 .   ? 155.553 99.350  55.429 1.00   53.78 ? 2061 HOH B O   1 
HETATM 11451 O  O   . HOH UA 6 .   ? 185.441 106.096 53.047 1.00   35.26 ? 2062 HOH B O   1 
HETATM 11452 O  O   . HOH UA 6 .   ? 187.710 112.915 53.196 1.00   32.76 ? 2063 HOH B O   1 
HETATM 11453 O  O   . HOH UA 6 .   ? 185.785 118.195 49.963 1.00   49.67 ? 2064 HOH B O   1 
HETATM 11454 O  O   . HOH UA 6 .   ? 182.284 112.956 44.360 1.00   42.26 ? 2065 HOH B O   1 
HETATM 11455 O  O   . HOH UA 6 .   ? 185.563 114.664 42.104 1.00   54.34 ? 2066 HOH B O   1 
HETATM 11456 O  O   . HOH UA 6 .   ? 179.807 118.085 41.771 1.00   24.72 ? 2067 HOH B O   1 
HETATM 11457 O  O   . HOH UA 6 .   ? 187.257 120.371 42.723 1.00   50.81 ? 2068 HOH B O   1 
HETATM 11458 O  O   . HOH UA 6 .   ? 184.051 115.526 36.490 1.00   52.56 ? 2069 HOH B O   1 
HETATM 11459 O  O   . HOH UA 6 .   ? 186.801 120.839 45.639 1.00   43.52 ? 2070 HOH B O   1 
HETATM 11460 O  O   . HOH UA 6 .   ? 176.399 121.385 39.259 1.00   52.39 ? 2071 HOH B O   1 
HETATM 11461 O  O   . HOH UA 6 .   ? 178.307 126.244 35.683 1.00   58.61 ? 2072 HOH B O   1 
HETATM 11462 O  O   . HOH UA 6 .   ? 185.741 124.771 39.655 1.00   40.51 ? 2073 HOH B O   1 
HETATM 11463 O  O   . HOH UA 6 .   ? 182.007 128.751 44.603 1.00   52.14 ? 2074 HOH B O   1 
HETATM 11464 O  O   . HOH UA 6 .   ? 177.550 124.596 50.762 1.00   32.94 ? 2075 HOH B O   1 
HETATM 11465 O  O   . HOH UA 6 .   ? 173.950 129.864 48.704 1.00   38.04 ? 2076 HOH B O   1 
HETATM 11466 O  O   . HOH UA 6 .   ? 173.229 126.065 41.302 1.00   44.63 ? 2077 HOH B O   1 
HETATM 11467 O  O   . HOH UA 6 .   ? 166.657 126.445 44.892 1.00   44.03 ? 2078 HOH B O   1 
HETATM 11468 O  O   . HOH UA 6 .   ? 169.184 124.762 47.064 1.00   38.67 ? 2079 HOH B O   1 
HETATM 11469 O  O   . HOH UA 6 .   ? 167.165 127.093 49.187 1.00   47.71 ? 2080 HOH B O   1 
HETATM 11470 O  O   . HOH UA 6 .   ? 181.316 131.015 46.343 1.00   53.76 ? 2081 HOH B O   1 
HETATM 11471 O  O   . HOH UA 6 .   ? 175.478 124.261 39.697 1.00   51.04 ? 2082 HOH B O   1 
HETATM 11472 O  O   . HOH UA 6 .   ? 178.395 120.375 40.802 1.00   40.08 ? 2083 HOH B O   1 
HETATM 11473 O  O   . HOH UA 6 .   ? 170.499 125.500 52.475 1.00   44.43 ? 2084 HOH B O   1 
HETATM 11474 O  O   . HOH UA 6 .   ? 172.154 127.981 52.691 1.00   48.23 ? 2085 HOH B O   1 
HETATM 11475 O  O   . HOH UA 6 .   ? 169.038 125.829 54.741 1.00   37.16 ? 2086 HOH B O   1 
HETATM 11476 O  O   . HOH UA 6 .   ? 174.345 130.925 54.380 1.00   58.38 ? 2087 HOH B O   1 
HETATM 11477 O  O   . HOH UA 6 .   ? 167.579 125.967 58.966 1.00   43.75 ? 2088 HOH B O   1 
HETATM 11478 O  O   . HOH UA 6 .   ? 165.813 127.273 62.053 1.00   41.57 ? 2089 HOH B O   1 
HETATM 11479 O  O   . HOH UA 6 .   ? 165.609 131.759 68.404 1.00   42.81 ? 2090 HOH B O   1 
HETATM 11480 O  O   . HOH UA 6 .   ? 163.482 132.740 69.248 1.00   48.33 ? 2091 HOH B O   1 
HETATM 11481 O  O   . HOH UA 6 .   ? 168.108 123.239 74.064 1.00   46.88 ? 2092 HOH B O   1 
HETATM 11482 O  O   . HOH UA 6 .   ? 163.472 127.332 57.993 1.00   36.22 ? 2093 HOH B O   1 
HETATM 11483 O  O   . HOH UA 6 .   ? 164.969 128.705 59.614 1.00   43.17 ? 2094 HOH B O   1 
HETATM 11484 O  O   . HOH UA 6 .   ? 160.907 122.448 51.530 1.00   43.65 ? 2095 HOH B O   1 
HETATM 11485 O  O   . HOH UA 6 .   ? 158.316 125.972 54.653 1.00   41.88 ? 2096 HOH B O   1 
HETATM 11486 O  O   . HOH UA 6 .   ? 165.032 124.577 43.405 1.00   43.44 ? 2097 HOH B O   1 
HETATM 11487 O  O   . HOH UA 6 .   ? 169.018 124.862 43.681 1.00   45.22 ? 2098 HOH B O   1 
HETATM 11488 O  O   . HOH UA 6 .   ? 171.389 113.023 38.007 1.00   49.69 ? 2099 HOH B O   1 
HETATM 11489 O  O   . HOH UA 6 .   ? 169.290 106.051 38.118 1.00   37.07 ? 2100 HOH B O   1 
HETATM 11490 O  O   . HOH UA 6 .   ? 168.581 105.661 39.985 1.00   44.66 ? 2101 HOH B O   1 
HETATM 11491 O  O   . HOH UA 6 .   ? 172.613 111.578 35.235 1.00   49.34 ? 2102 HOH B O   1 
HETATM 11492 O  O   . HOH UA 6 .   ? 177.907 110.119 40.037 1.00   47.40 ? 2103 HOH B O   1 
HETATM 11493 O  O   . HOH UA 6 .   ? 175.134 109.100 42.101 1.00   28.14 ? 2104 HOH B O   1 
HETATM 11494 O  O   . HOH UA 6 .   ? 178.148 110.678 33.674 1.00   51.85 ? 2105 HOH B O   1 
HETATM 11495 O  O   . HOH UA 6 .   ? 173.995 119.849 38.005 1.00   46.32 ? 2106 HOH B O   1 
HETATM 11496 O  O   . HOH UA 6 .   ? 173.879 107.020 44.262 1.00   47.63 ? 2107 HOH B O   1 
HETATM 11497 O  O   . HOH UA 6 .   ? 170.716 106.169 41.584 1.00   65.13 ? 2108 HOH B O   1 
HETATM 11498 O  O   . HOH UA 6 .   ? 177.385 105.800 40.906 1.00   47.30 ? 2109 HOH B O   1 
HETATM 11499 O  O   . HOH UA 6 .   ? 184.061 119.576 67.880 1.00   54.65 ? 2110 HOH B O   1 
HETATM 11500 O  O   . HOH UA 6 .   ? 182.900 126.087 67.221 1.00   42.25 ? 2111 HOH B O   1 
HETATM 11501 O  O   . HOH UA 6 .   ? 180.988 129.493 62.482 1.00   42.37 ? 2112 HOH B O   1 
HETATM 11502 O  O   . HOH UA 6 .   ? 179.275 131.772 55.949 1.00   46.34 ? 2113 HOH B O   1 
HETATM 11503 O  O   . HOH UA 6 .   ? 179.416 135.397 44.597 1.00   47.70 ? 2114 HOH B O   1 
HETATM 11504 O  O   . HOH UA 6 .   ? 194.785 125.126 53.335 1.00   49.64 ? 2115 HOH B O   1 
HETATM 11505 O  O   . HOH UA 6 .   ? 195.458 128.419 51.699 1.00   64.48 ? 2116 HOH B O   1 
HETATM 11506 O  O   . HOH UA 6 .   ? 193.420 118.879 54.263 1.00   58.99 ? 2117 HOH B O   1 
HETATM 11507 O  O   . HOH UA 6 .   ? 185.157 115.114 61.808 1.00   36.98 ? 2118 HOH B O   1 
HETATM 11508 O  O   . HOH UA 6 .   ? 185.984 113.978 59.600 1.00   53.11 ? 2119 HOH B O   1 
HETATM 11509 O  O   . HOH UA 6 .   ? 185.971 117.119 57.998 1.00   40.39 ? 2120 HOH B O   1 
HETATM 11510 O  O   . HOH UA 6 .   ? 185.586 117.007 52.977 1.00   44.29 ? 2121 HOH B O   1 
HETATM 11511 O  O   . HOH UA 6 .   ? 172.526 105.999 58.703 1.00   24.72 ? 2122 HOH B O   1 
HETATM 11512 O  O   . HOH UA 6 .   ? 159.611 105.055 54.600 1.00   31.84 ? 2123 HOH B O   1 
HETATM 11513 O  O   . HOH UA 6 .   ? 157.388 107.424 53.829 1.00   35.74 ? 2124 HOH B O   1 
HETATM 11514 O  O   . HOH UA 6 .   ? 156.355 103.648 48.070 1.00   50.68 ? 2125 HOH B O   1 
HETATM 11515 O  O   . HOH UA 6 .   ? 152.701 100.335 55.129 1.00   48.71 ? 2126 HOH B O   1 
HETATM 11516 O  O   . HOH VA 6 .   ? 199.341 62.737  46.657 1.00   51.48 ? 2001 HOH C O   1 
HETATM 11517 O  O   . HOH VA 6 .   ? 198.372 62.064  43.806 1.00   49.24 ? 2002 HOH C O   1 
HETATM 11518 O  O   . HOH VA 6 .   ? 197.366 58.564  41.145 1.00   43.94 ? 2003 HOH C O   1 
HETATM 11519 O  O   . HOH VA 6 .   ? 201.493 60.778  54.391 1.00   32.93 ? 2004 HOH C O   1 
HETATM 11520 O  O   . HOH VA 6 .   ? 198.481 60.821  46.748 1.00   23.48 ? 2005 HOH C O   1 
HETATM 11521 O  O   . HOH VA 6 .   ? 202.755 64.879  49.368 1.00   39.06 ? 2006 HOH C O   1 
HETATM 11522 O  O   . HOH VA 6 .   ? 202.244 58.488  53.694 1.00   16.73 ? 2007 HOH C O   1 
HETATM 11523 O  O   . HOH VA 6 .   ? 196.999 39.314  68.360 1.00   47.69 ? 2008 HOH C O   1 
HETATM 11524 O  O   . HOH VA 6 .   ? 199.794 40.660  68.985 1.00   32.35 ? 2009 HOH C O   1 
HETATM 11525 O  O   . HOH VA 6 .   ? 194.948 52.868  57.758 1.00   9.28  ? 2010 HOH C O   1 
HETATM 11526 O  O   . HOH VA 6 .   ? 193.926 50.593  61.361 1.00   20.32 ? 2011 HOH C O   1 
HETATM 11527 O  O   . HOH VA 6 .   ? 204.940 54.751  63.591 1.00   46.73 ? 2012 HOH C O   1 
HETATM 11528 O  O   . HOH VA 6 .   ? 191.942 44.813  64.202 1.00   39.85 ? 2013 HOH C O   1 
HETATM 11529 O  O   . HOH VA 6 .   ? 192.961 46.740  61.670 1.00   35.61 ? 2014 HOH C O   1 
HETATM 11530 O  O   . HOH VA 6 .   ? 193.141 52.975  62.727 1.00   32.09 ? 2015 HOH C O   1 
HETATM 11531 O  O   . HOH VA 6 .   ? 210.641 55.570  43.053 1.00   45.77 ? 2016 HOH C O   1 
HETATM 11532 O  O   . HOH VA 6 .   ? 197.520 47.055  68.200 1.00   18.64 ? 2017 HOH C O   1 
HETATM 11533 O  O   . HOH VA 6 .   ? 193.318 48.312  68.462 1.00   46.70 ? 2018 HOH C O   1 
HETATM 11534 O  O   . HOH VA 6 .   ? 195.417 46.456  71.605 1.00   30.12 ? 2019 HOH C O   1 
HETATM 11535 O  O   . HOH VA 6 .   ? 192.792 46.772  70.830 1.00   38.67 ? 2020 HOH C O   1 
HETATM 11536 O  O   . HOH VA 6 .   ? 210.317 53.536  36.460 1.00   41.28 ? 2021 HOH C O   1 
HETATM 11537 O  O   . HOH VA 6 .   ? 212.904 53.783  39.338 1.00   54.82 ? 2022 HOH C O   1 
HETATM 11538 O  O   . HOH VA 6 .   ? 195.738 41.145  66.737 1.00   29.46 ? 2023 HOH C O   1 
HETATM 11539 O  O   . HOH VA 6 .   ? 191.899 42.824  72.133 1.00   51.62 ? 2024 HOH C O   1 
HETATM 11540 O  O   . HOH VA 6 .   ? 198.643 42.964  68.077 1.00   24.40 ? 2025 HOH C O   1 
HETATM 11541 O  O   . HOH VA 6 .   ? 202.142 49.039  71.353 1.00   23.13 ? 2026 HOH C O   1 
HETATM 11542 O  O   . HOH VA 6 .   ? 197.792 54.444  69.482 1.00   52.18 ? 2027 HOH C O   1 
HETATM 11543 O  O   . HOH VA 6 .   ? 202.774 36.483  68.686 1.00   48.82 ? 2028 HOH C O   1 
HETATM 11544 O  O   . HOH VA 6 .   ? 206.124 55.239  60.698 1.00   27.85 ? 2029 HOH C O   1 
HETATM 11545 O  O   . HOH VA 6 .   ? 205.863 57.517  59.471 1.00   27.63 ? 2030 HOH C O   1 
HETATM 11546 O  O   . HOH VA 6 .   ? 202.556 59.201  57.837 1.00   23.43 ? 2031 HOH C O   1 
HETATM 11547 O  O   . HOH VA 6 .   ? 205.622 60.995  55.056 1.00   46.23 ? 2032 HOH C O   1 
HETATM 11548 O  O   . HOH VA 6 .   ? 191.464 42.194  41.202 1.00   42.21 ? 2033 HOH C O   1 
HETATM 11549 O  O   . HOH VA 6 .   ? 208.627 56.353  44.364 1.00   37.53 ? 2034 HOH C O   1 
HETATM 11550 O  O   . HOH VA 6 .   ? 180.646 43.585  52.364 1.00   31.23 ? 2035 HOH C O   1 
HETATM 11551 O  O   . HOH VA 6 .   ? 191.229 49.839  63.740 1.00   41.11 ? 2036 HOH C O   1 
HETATM 11552 O  O   . HOH VA 6 .   ? 183.984 38.467  57.782 1.00   39.25 ? 2037 HOH C O   1 
HETATM 11553 O  O   . HOH VA 6 .   ? 179.728 42.362  61.071 1.00   49.43 ? 2038 HOH C O   1 
HETATM 11554 O  O   . HOH VA 6 .   ? 202.281 57.790  40.476 1.00   30.94 ? 2039 HOH C O   1 
HETATM 11555 O  O   . HOH VA 6 .   ? 200.218 55.606  40.898 1.00   21.79 ? 2040 HOH C O   1 
HETATM 11556 O  O   . HOH VA 6 .   ? 186.049 36.469  62.282 1.00   40.10 ? 2041 HOH C O   1 
HETATM 11557 O  O   . HOH VA 6 .   ? 207.810 55.420  41.165 1.00   32.86 ? 2042 HOH C O   1 
HETATM 11558 O  O   . HOH VA 6 .   ? 201.975 60.318  39.513 1.00   36.82 ? 2043 HOH C O   1 
HETATM 11559 O  O   . HOH VA 6 .   ? 186.454 37.239  53.306 1.00   40.85 ? 2044 HOH C O   1 
HETATM 11560 O  O   . HOH VA 6 .   ? 190.030 33.597  52.788 1.00   41.02 ? 2045 HOH C O   1 
HETATM 11561 O  O   . HOH VA 6 .   ? 208.718 55.707  35.622 1.00   37.45 ? 2046 HOH C O   1 
HETATM 11562 O  O   . HOH VA 6 .   ? 209.973 55.883  39.529 1.00   38.38 ? 2047 HOH C O   1 
HETATM 11563 O  O   . HOH VA 6 .   ? 207.790 61.862  37.813 1.00   42.34 ? 2048 HOH C O   1 
HETATM 11564 O  O   . HOH VA 6 .   ? 202.486 59.224  36.985 1.00   37.19 ? 2049 HOH C O   1 
HETATM 11565 O  O   . HOH VA 6 .   ? 201.069 54.294  34.059 1.00   22.09 ? 2050 HOH C O   1 
HETATM 11566 O  O   . HOH VA 6 .   ? 203.504 57.382  34.167 1.00   24.60 ? 2051 HOH C O   1 
HETATM 11567 O  O   . HOH VA 6 .   ? 207.605 50.421  34.012 1.00   23.38 ? 2052 HOH C O   1 
HETATM 11568 O  O   . HOH VA 6 .   ? 209.022 49.695  37.816 1.00   43.58 ? 2053 HOH C O   1 
HETATM 11569 O  O   . HOH VA 6 .   ? 209.196 30.320  41.855 1.00   45.46 ? 2054 HOH C O   1 
HETATM 11570 O  O   . HOH VA 6 .   ? 205.105 49.315  40.597 1.00   16.74 ? 2055 HOH C O   1 
HETATM 11571 O  O   . HOH VA 6 .   ? 212.598 38.810  49.506 1.00   22.65 ? 2056 HOH C O   1 
HETATM 11572 O  O   . HOH VA 6 .   ? 203.051 40.961  37.485 1.00   37.25 ? 2057 HOH C O   1 
HETATM 11573 O  O   . HOH VA 6 .   ? 208.052 39.482  32.490 1.00   60.44 ? 2058 HOH C O   1 
HETATM 11574 O  O   . HOH VA 6 .   ? 206.078 42.144  36.779 1.00   49.69 ? 2059 HOH C O   1 
HETATM 11575 O  O   . HOH VA 6 .   ? 211.571 52.238  50.980 1.00   41.42 ? 2060 HOH C O   1 
HETATM 11576 O  O   . HOH VA 6 .   ? 212.275 43.205  50.538 1.00   27.27 ? 2061 HOH C O   1 
HETATM 11577 O  O   . HOH VA 6 .   ? 211.998 52.781  58.022 1.00   29.81 ? 2062 HOH C O   1 
HETATM 11578 O  O   . HOH VA 6 .   ? 211.357 53.732  60.072 1.00   43.85 ? 2063 HOH C O   1 
HETATM 11579 O  O   . HOH VA 6 .   ? 211.311 53.341  64.636 1.00   40.23 ? 2064 HOH C O   1 
HETATM 11580 O  O   . HOH VA 6 .   ? 207.421 52.421  66.324 1.00   33.43 ? 2065 HOH C O   1 
HETATM 11581 O  O   . HOH VA 6 .   ? 206.082 54.261  71.914 1.00   38.02 ? 2066 HOH C O   1 
HETATM 11582 O  O   . HOH VA 6 .   ? 208.872 52.388  68.964 1.00   37.96 ? 2067 HOH C O   1 
HETATM 11583 O  O   . HOH VA 6 .   ? 207.715 48.057  70.853 1.00   31.15 ? 2068 HOH C O   1 
HETATM 11584 O  O   . HOH VA 6 .   ? 203.732 40.922  69.549 1.00   25.27 ? 2069 HOH C O   1 
HETATM 11585 O  O   . HOH VA 6 .   ? 210.503 42.369  70.970 1.00   28.95 ? 2070 HOH C O   1 
HETATM 11586 O  O   . HOH VA 6 .   ? 214.410 46.711  48.583 1.00   36.77 ? 2071 HOH C O   1 
HETATM 11587 O  O   . HOH VA 6 .   ? 211.822 42.216  46.120 1.00   33.12 ? 2072 HOH C O   1 
HETATM 11588 O  O   . HOH VA 6 .   ? 215.413 47.844  46.204 1.00   53.08 ? 2073 HOH C O   1 
HETATM 11589 O  O   . HOH VA 6 .   ? 205.226 39.597  67.437 1.00   22.25 ? 2074 HOH C O   1 
HETATM 11590 O  O   . HOH VA 6 .   ? 209.510 36.502  66.192 1.00   38.56 ? 2075 HOH C O   1 
HETATM 11591 O  O   . HOH VA 6 .   ? 204.962 36.923  66.557 1.00   29.52 ? 2076 HOH C O   1 
HETATM 11592 O  O   . HOH VA 6 .   ? 213.204 51.285  38.986 1.00   47.89 ? 2077 HOH C O   1 
HETATM 11593 O  O   . HOH VA 6 .   ? 211.430 39.672  71.338 1.00   31.99 ? 2078 HOH C O   1 
HETATM 11594 O  O   . HOH VA 6 .   ? 220.122 41.189  69.125 1.00   44.55 ? 2079 HOH C O   1 
HETATM 11595 O  O   . HOH VA 6 .   ? 213.162 34.999  62.641 1.00   37.77 ? 2080 HOH C O   1 
HETATM 11596 O  O   . HOH VA 6 .   ? 209.861 35.339  63.871 1.00   30.95 ? 2081 HOH C O   1 
HETATM 11597 O  O   . HOH VA 6 .   ? 207.888 27.278  62.038 1.00   42.50 ? 2082 HOH C O   1 
HETATM 11598 O  O   . HOH VA 6 .   ? 208.934 28.436  57.873 1.00   28.98 ? 2083 HOH C O   1 
HETATM 11599 O  O   . HOH VA 6 .   ? 213.914 34.809  53.849 1.00   56.62 ? 2084 HOH C O   1 
HETATM 11600 O  O   . HOH VA 6 .   ? 213.397 32.606  53.539 1.00   42.98 ? 2085 HOH C O   1 
HETATM 11601 O  O   . HOH VA 6 .   ? 198.304 35.358  55.179 1.00   24.05 ? 2086 HOH C O   1 
HETATM 11602 O  O   . HOH VA 6 .   ? 208.787 23.424  47.831 1.00   34.19 ? 2087 HOH C O   1 
HETATM 11603 O  O   . HOH VA 6 .   ? 212.460 25.522  47.474 1.00   29.85 ? 2088 HOH C O   1 
HETATM 11604 O  O   . HOH VA 6 .   ? 189.022 36.127  47.644 1.00   27.52 ? 2089 HOH C O   1 
HETATM 11605 O  O   . HOH VA 6 .   ? 192.019 36.470  45.377 1.00   43.25 ? 2090 HOH C O   1 
HETATM 11606 O  O   . HOH VA 6 .   ? 192.933 38.846  44.520 1.00   24.43 ? 2091 HOH C O   1 
HETATM 11607 O  O   . HOH VA 6 .   ? 189.389 42.012  44.711 1.00   25.56 ? 2092 HOH C O   1 
HETATM 11608 O  O   . HOH VA 6 .   ? 191.712 40.285  42.608 1.00   42.53 ? 2093 HOH C O   1 
HETATM 11609 O  O   . HOH VA 6 .   ? 186.603 47.889  56.443 1.00   13.39 ? 2094 HOH C O   1 
HETATM 11610 O  O   . HOH VA 6 .   ? 187.843 47.950  56.933 1.00   37.84 ? 2095 HOH C O   1 
HETATM 11611 O  O   . HOH VA 6 .   ? 190.946 44.004  57.871 1.00   25.49 ? 2096 HOH C O   1 
HETATM 11612 O  O   . HOH VA 6 .   ? 184.725 41.735  52.315 1.00   21.53 ? 2097 HOH C O   1 
HETATM 11613 O  O   . HOH VA 6 .   ? 181.593 43.134  54.730 1.00   28.62 ? 2098 HOH C O   1 
HETATM 11614 O  O   . HOH VA 6 .   ? 186.210 46.220  63.697 1.00   35.49 ? 2099 HOH C O   1 
HETATM 11615 O  O   . HOH VA 6 .   ? 191.553 47.940  59.594 1.00   24.13 ? 2100 HOH C O   1 
HETATM 11616 O  O   . HOH VA 6 .   ? 188.838 49.829  62.453 1.00   33.71 ? 2101 HOH C O   1 
HETATM 11617 O  O   . HOH VA 6 .   ? 200.334 36.595  69.151 1.00   51.54 ? 2102 HOH C O   1 
HETATM 11618 O  O   . HOH VA 6 .   ? 183.494 46.040  63.377 1.00   42.14 ? 2103 HOH C O   1 
HETATM 11619 O  O   . HOH VA 6 .   ? 182.255 40.469  58.605 1.00   42.05 ? 2104 HOH C O   1 
HETATM 11620 O  O   . HOH VA 6 .   ? 187.612 37.506  63.853 1.00   51.91 ? 2105 HOH C O   1 
HETATM 11621 O  O   . HOH VA 6 .   ? 195.741 66.682  56.037 1.00   37.97 ? 2106 HOH C O   1 
HETATM 11622 O  O   . HOH VA 6 .   ? 192.115 41.935  64.206 1.00   29.79 ? 2107 HOH C O   1 
HETATM 11623 O  O   . HOH VA 6 .   ? 190.581 35.393  56.142 1.00   32.51 ? 2108 HOH C O   1 
HETATM 11624 O  O   . HOH VA 6 .   ? 192.852 36.058  61.644 1.00   43.57 ? 2109 HOH C O   1 
HETATM 11625 O  O   . HOH VA 6 .   ? 185.925 39.454  53.425 1.00   27.07 ? 2110 HOH C O   1 
HETATM 11626 O  O   . HOH VA 6 .   ? 191.749 34.337  54.065 1.00   25.39 ? 2111 HOH C O   1 
HETATM 11627 O  O   . HOH VA 6 .   ? 187.832 35.359  52.476 1.00   47.38 ? 2112 HOH C O   1 
HETATM 11628 O  O   . HOH VA 6 .   ? 190.382 32.496  49.988 1.00   40.29 ? 2113 HOH C O   1 
HETATM 11629 O  O   . HOH VA 6 .   ? 196.735 34.032  50.442 1.00   17.99 ? 2114 HOH C O   1 
HETATM 11630 O  O   . HOH VA 6 .   ? 194.953 34.834  47.121 1.00   33.56 ? 2115 HOH C O   1 
HETATM 11631 O  O   . HOH VA 6 .   ? 192.450 35.389  42.441 1.00   42.22 ? 2116 HOH C O   1 
HETATM 11632 O  O   . HOH VA 6 .   ? 198.515 38.052  41.559 1.00   16.04 ? 2117 HOH C O   1 
HETATM 11633 O  O   . HOH VA 6 .   ? 193.578 35.969  36.912 1.00   39.07 ? 2118 HOH C O   1 
HETATM 11634 O  O   . HOH VA 6 .   ? 191.567 39.526  38.776 1.00   50.71 ? 2119 HOH C O   1 
HETATM 11635 O  O   . HOH VA 6 .   ? 197.815 31.012  46.127 1.00   32.85 ? 2120 HOH C O   1 
HETATM 11636 O  O   . HOH VA 6 .   ? 204.488 37.419  37.793 1.00   49.11 ? 2121 HOH C O   1 
HETATM 11637 O  O   . HOH VA 6 .   ? 205.060 32.881  37.261 1.00   49.10 ? 2122 HOH C O   1 
HETATM 11638 O  O   . HOH VA 6 .   ? 206.625 30.972  44.350 1.00   33.55 ? 2123 HOH C O   1 
HETATM 11639 O  O   . HOH VA 6 .   ? 205.818 37.165  50.424 1.00   15.71 ? 2124 HOH C O   1 
HETATM 11640 O  O   . HOH VA 6 .   ? 211.813 37.177  47.562 1.00   19.32 ? 2125 HOH C O   1 
HETATM 11641 O  O   . HOH VA 6 .   ? 208.636 39.779  40.797 1.00   33.65 ? 2126 HOH C O   1 
HETATM 11642 O  O   . HOH VA 6 .   ? 213.961 39.609  40.910 1.00   47.78 ? 2127 HOH C O   1 
HETATM 11643 O  O   . HOH VA 6 .   ? 216.266 35.543  46.335 1.00   36.41 ? 2128 HOH C O   1 
HETATM 11644 O  O   . HOH VA 6 .   ? 217.750 40.221  47.663 1.00   29.25 ? 2129 HOH C O   1 
HETATM 11645 O  O   . HOH VA 6 .   ? 213.147 41.355  48.412 1.00   31.35 ? 2130 HOH C O   1 
HETATM 11646 O  O   . HOH VA 6 .   ? 206.910 38.978  39.800 1.00   36.64 ? 2131 HOH C O   1 
HETATM 11647 O  O   . HOH VA 6 .   ? 210.818 32.156  47.012 1.00   23.23 ? 2132 HOH C O   1 
HETATM 11648 O  O   . HOH VA 6 .   ? 209.585 32.112  40.279 1.00   36.32 ? 2133 HOH C O   1 
HETATM 11649 O  O   . HOH VA 6 .   ? 211.374 33.685  39.448 1.00   37.30 ? 2134 HOH C O   1 
HETATM 11650 O  O   . HOH VA 6 .   ? 202.889 39.213  39.490 0.50   17.80 ? 2135 HOH C O   1 
HETATM 11651 O  O   . HOH VA 6 .   ? 204.589 39.158  39.539 0.50   15.56 ? 2136 HOH C O   1 
HETATM 11652 O  O   . HOH VA 6 .   ? 206.649 39.490  35.034 1.00   67.37 ? 2137 HOH C O   1 
HETATM 11653 O  O   . HOH VA 6 .   ? 209.614 39.993  34.985 1.00   60.27 ? 2138 HOH C O   1 
HETATM 11654 O  O   . HOH VA 6 .   ? 199.633 29.181  39.286 1.00   43.43 ? 2139 HOH C O   1 
HETATM 11655 O  O   . HOH VA 6 .   ? 201.033 37.978  40.539 1.00   23.66 ? 2140 HOH C O   1 
HETATM 11656 O  O   . HOH VA 6 .   ? 210.477 42.045  52.365 1.00   28.81 ? 2141 HOH C O   1 
HETATM 11657 O  O   . HOH VA 6 .   ? 214.069 46.736  61.830 1.00   19.50 ? 2142 HOH C O   1 
HETATM 11658 O  O   . HOH VA 6 .   ? 214.472 49.849  67.931 1.00   34.59 ? 2143 HOH C O   1 
HETATM 11659 O  O   . HOH VA 6 .   ? 215.242 48.321  63.690 1.00   39.70 ? 2144 HOH C O   1 
HETATM 11660 O  O   . HOH VA 6 .   ? 217.827 48.902  65.979 1.00   41.87 ? 2145 HOH C O   1 
HETATM 11661 O  O   . HOH VA 6 .   ? 218.624 44.058  67.196 1.00   32.16 ? 2146 HOH C O   1 
HETATM 11662 O  O   . HOH VA 6 .   ? 214.857 46.076  52.711 1.00   35.92 ? 2147 HOH C O   1 
HETATM 11663 O  O   . HOH VA 6 .   ? 212.648 45.674  48.800 1.00   27.38 ? 2148 HOH C O   1 
HETATM 11664 O  O   . HOH VA 6 .   ? 209.872 44.164  46.780 1.00   16.90 ? 2149 HOH C O   1 
HETATM 11665 O  O   . HOH VA 6 .   ? 212.020 45.600  43.450 1.00   43.83 ? 2150 HOH C O   1 
HETATM 11666 O  O   . HOH VA 6 .   ? 213.535 45.611  46.049 1.00   38.81 ? 2151 HOH C O   1 
HETATM 11667 O  O   . HOH VA 6 .   ? 212.783 53.852  42.888 1.00   58.92 ? 2152 HOH C O   1 
HETATM 11668 O  O   . HOH VA 6 .   ? 211.528 47.892  42.451 1.00   34.28 ? 2153 HOH C O   1 
HETATM 11669 O  O   . HOH VA 6 .   ? 209.722 44.122  42.724 1.00   33.51 ? 2154 HOH C O   1 
HETATM 11670 O  O   . HOH VA 6 .   ? 211.617 48.938  38.424 1.00   47.46 ? 2155 HOH C O   1 
HETATM 11671 O  O   . HOH VA 6 .   ? 208.243 43.877  37.640 1.00   40.44 ? 2156 HOH C O   1 
HETATM 11672 O  O   . HOH VA 6 .   ? 195.134 55.816  42.536 1.00   34.00 ? 2157 HOH C O   1 
HETATM 11673 O  O   . HOH VA 6 .   ? 198.775 48.136  37.921 1.00   28.20 ? 2158 HOH C O   1 
HETATM 11674 O  O   . HOH VA 6 .   ? 193.517 53.806  39.014 1.00   31.23 ? 2159 HOH C O   1 
HETATM 11675 O  O   . HOH VA 6 .   ? 192.321 48.639  36.956 1.00   51.02 ? 2160 HOH C O   1 
HETATM 11676 O  O   . HOH VA 6 .   ? 196.640 47.953  34.953 1.00   28.83 ? 2161 HOH C O   1 
HETATM 11677 O  O   . HOH VA 6 .   ? 192.775 44.040  39.851 1.00   39.16 ? 2162 HOH C O   1 
HETATM 11678 O  O   . HOH VA 6 .   ? 193.359 46.844  42.313 1.00   24.12 ? 2163 HOH C O   1 
HETATM 11679 O  O   . HOH VA 6 .   ? 197.214 42.220  36.349 1.00   48.53 ? 2164 HOH C O   1 
HETATM 11680 O  O   . HOH VA 6 .   ? 203.670 43.401  37.972 1.00   49.36 ? 2165 HOH C O   1 
HETATM 11681 O  O   . HOH VA 6 .   ? 189.241 43.870  42.636 1.00   42.84 ? 2166 HOH C O   1 
HETATM 11682 O  O   . HOH VA 6 .   ? 191.753 46.268  57.702 1.00   23.97 ? 2167 HOH C O   1 
HETATM 11683 O  O   . HOH VA 6 .   ? 207.861 34.878  64.871 1.00   43.06 ? 2168 HOH C O   1 
HETATM 11684 O  O   . HOH VA 6 .   ? 205.724 28.037  60.491 1.00   39.05 ? 2169 HOH C O   1 
HETATM 11685 O  O   . HOH VA 6 .   ? 208.704 31.494  61.835 1.00   30.29 ? 2170 HOH C O   1 
HETATM 11686 O  O   . HOH VA 6 .   ? 206.990 30.336  59.238 1.00   22.04 ? 2171 HOH C O   1 
HETATM 11687 O  O   . HOH VA 6 .   ? 211.846 32.947  55.712 1.00   35.18 ? 2172 HOH C O   1 
HETATM 11688 O  O   . HOH VA 6 .   ? 212.197 30.711  52.622 1.00   30.44 ? 2173 HOH C O   1 
HETATM 11689 O  O   . HOH VA 6 .   ? 207.724 26.832  56.314 1.00   23.49 ? 2174 HOH C O   1 
HETATM 11690 O  O   . HOH VA 6 .   ? 206.928 24.786  48.731 1.00   19.94 ? 2175 HOH C O   1 
HETATM 11691 O  O   . HOH VA 6 .   ? 212.138 23.994  49.604 1.00   32.43 ? 2176 HOH C O   1 
HETATM 11692 O  O   . HOH VA 6 .   ? 212.953 25.819  52.389 1.00   24.12 ? 2177 HOH C O   1 
HETATM 11693 O  O   . HOH VA 6 .   ? 202.492 24.069  57.023 1.00   34.80 ? 2178 HOH C O   1 
HETATM 11694 O  O   . HOH VA 6 .   ? 202.796 21.455  57.576 1.00   21.05 ? 2179 HOH C O   1 
HETATM 11695 O  O   . HOH VA 6 .   ? 199.922 23.194  56.469 1.00   44.24 ? 2180 HOH C O   1 
HETATM 11696 O  O   . HOH VA 6 .   ? 199.282 20.700  52.319 1.00   30.87 ? 2181 HOH C O   1 
HETATM 11697 O  O   . HOH VA 6 .   ? 199.359 22.605  54.009 1.00   41.67 ? 2182 HOH C O   1 
HETATM 11698 O  O   . HOH VA 6 .   ? 195.320 29.305  55.237 1.00   41.29 ? 2183 HOH C O   1 
HETATM 11699 O  O   . HOH VA 6 .   ? 197.907 25.329  58.026 1.00   39.29 ? 2184 HOH C O   1 
HETATM 11700 O  O   . HOH VA 6 .   ? 199.950 30.218  57.917 1.00   30.09 ? 2185 HOH C O   1 
HETATM 11701 O  O   . HOH VA 6 .   ? 194.021 28.109  47.334 1.00   50.73 ? 2186 HOH C O   1 
HETATM 11702 O  O   . HOH VA 6 .   ? 198.827 33.454  57.129 1.00   30.40 ? 2187 HOH C O   1 
HETATM 11703 O  O   . HOH VA 6 .   ? 196.806 36.778  66.916 1.00   45.98 ? 2188 HOH C O   1 
HETATM 11704 O  O   . HOH VA 6 .   ? 194.739 35.718  62.423 1.00   22.29 ? 2189 HOH C O   1 
HETATM 11705 O  O   . HOH VA 6 .   ? 192.410 34.608  59.225 1.00   40.34 ? 2190 HOH C O   1 
HETATM 11706 O  O   . HOH VA 6 .   ? 196.065 34.459  53.639 1.00   27.89 ? 2191 HOH C O   1 
HETATM 11707 O  O   . HOH VA 6 .   ? 193.941 33.108  53.996 1.00   38.61 ? 2192 HOH C O   1 
HETATM 11708 O  O   . HOH VA 6 .   ? 192.839 48.663  61.908 1.00   33.19 ? 2193 HOH C O   1 
HETATM 11709 O  O   . HOH VA 6 .   ? 192.270 51.004  58.680 1.00   22.35 ? 2194 HOH C O   1 
HETATM 11710 O  O   . HOH VA 6 .   ? 197.605 62.675  54.424 1.00   17.70 ? 2195 HOH C O   1 
HETATM 11711 O  O   . HOH VA 6 .   ? 200.483 63.196  54.001 1.00   36.00 ? 2196 HOH C O   1 
HETATM 11712 O  O   . HOH VA 6 .   ? 196.199 68.524  49.530 1.00   40.19 ? 2197 HOH C O   1 
HETATM 11713 O  O   . HOH VA 6 .   ? 194.739 68.507  54.818 1.00   44.21 ? 2198 HOH C O   1 
HETATM 11714 O  O   . HOH VA 6 .   ? 194.405 69.490  52.697 1.00   38.55 ? 2199 HOH C O   1 
HETATM 11715 O  O   . HOH WA 6 .   ? 159.496 156.525 48.083 1.00   45.70 ? 2001 HOH D O   1 
HETATM 11716 O  O   . HOH WA 6 .   ? 164.403 157.932 41.990 1.00   50.13 ? 2002 HOH D O   1 
HETATM 11717 O  O   . HOH WA 6 .   ? 164.970 142.042 62.407 1.00   54.62 ? 2003 HOH D O   1 
HETATM 11718 O  O   . HOH WA 6 .   ? 162.249 142.342 61.663 1.00   64.19 ? 2004 HOH D O   1 
HETATM 11719 O  O   . HOH WA 6 .   ? 177.426 137.849 68.279 1.00   43.14 ? 2005 HOH D O   1 
HETATM 11720 O  O   . HOH WA 6 .   ? 178.163 142.701 67.488 1.00   29.56 ? 2006 HOH D O   1 
HETATM 11721 O  O   . HOH WA 6 .   ? 164.793 147.355 57.149 1.00   16.84 ? 2007 HOH D O   1 
HETATM 11722 O  O   . HOH WA 6 .   ? 166.141 144.618 60.222 1.00   29.19 ? 2008 HOH D O   1 
HETATM 11723 O  O   . HOH WA 6 .   ? 167.449 147.940 65.032 1.00   37.49 ? 2009 HOH D O   1 
HETATM 11724 O  O   . HOH WA 6 .   ? 169.933 139.691 61.371 1.00   39.17 ? 2010 HOH D O   1 
HETATM 11725 O  O   . HOH WA 6 .   ? 168.245 142.012 60.266 1.00   38.55 ? 2011 HOH D O   1 
HETATM 11726 O  O   . HOH WA 6 .   ? 163.980 144.854 61.635 1.00   35.86 ? 2012 HOH D O   1 
HETATM 11727 O  O   . HOH WA 6 .   ? 171.317 144.111 66.994 1.00   25.68 ? 2013 HOH D O   1 
HETATM 11728 O  O   . HOH WA 6 .   ? 174.906 139.496 63.559 1.00   43.14 ? 2014 HOH D O   1 
HETATM 11729 O  O   . HOH WA 6 .   ? 171.793 137.689 70.975 1.00   44.93 ? 2015 HOH D O   1 
HETATM 11730 O  O   . HOH WA 6 .   ? 171.077 140.857 70.010 1.00   42.59 ? 2016 HOH D O   1 
HETATM 11731 O  O   . HOH WA 6 .   ? 177.643 140.217 66.923 1.00   41.84 ? 2017 HOH D O   1 
HETATM 11732 O  O   . HOH WA 6 .   ? 175.366 142.948 66.355 1.00   25.18 ? 2018 HOH D O   1 
HETATM 11733 O  O   . HOH WA 6 .   ? 172.591 148.917 71.292 1.00   40.57 ? 2019 HOH D O   1 
HETATM 11734 O  O   . HOH WA 6 .   ? 173.056 152.437 74.036 1.00   33.34 ? 2020 HOH D O   1 
HETATM 11735 O  O   . HOH WA 6 .   ? 174.350 154.398 72.205 1.00   31.90 ? 2021 HOH D O   1 
HETATM 11736 O  O   . HOH WA 6 .   ? 169.806 156.431 75.400 1.00   47.16 ? 2022 HOH D O   1 
HETATM 11737 O  O   . HOH WA 6 .   ? 183.098 142.894 67.082 1.00   50.88 ? 2023 HOH D O   1 
HETATM 11738 O  O   . HOH WA 6 .   ? 168.580 157.489 62.415 1.00   44.93 ? 2024 HOH D O   1 
HETATM 11739 O  O   . HOH WA 6 .   ? 166.186 158.162 60.791 1.00   46.29 ? 2025 HOH D O   1 
HETATM 11740 O  O   . HOH WA 6 .   ? 163.448 156.918 59.333 1.00   37.54 ? 2026 HOH D O   1 
HETATM 11741 O  O   . HOH WA 6 .   ? 169.280 163.086 46.674 1.00   36.25 ? 2027 HOH D O   1 
HETATM 11742 O  O   . HOH WA 6 .   ? 165.285 131.746 48.435 1.00   34.53 ? 2028 HOH D O   1 
HETATM 11743 O  O   . HOH WA 6 .   ? 177.105 134.005 49.346 1.00   52.16 ? 2029 HOH D O   1 
HETATM 11744 O  O   . HOH WA 6 .   ? 169.070 162.620 43.419 1.00   49.75 ? 2030 HOH D O   1 
HETATM 11745 O  O   . HOH WA 6 .   ? 185.709 144.937 33.729 1.00   51.29 ? 2031 HOH D O   1 
HETATM 11746 O  O   . HOH WA 6 .   ? 181.235 158.409 50.594 1.00   40.43 ? 2032 HOH D O   1 
HETATM 11747 O  O   . HOH WA 6 .   ? 173.602 162.430 53.209 1.00   45.87 ? 2033 HOH D O   1 
HETATM 11748 O  O   . HOH WA 6 .   ? 172.277 155.323 67.536 1.00   55.64 ? 2034 HOH D O   1 
HETATM 11749 O  O   . HOH WA 6 .   ? 176.084 158.584 72.671 1.00   40.67 ? 2035 HOH D O   1 
HETATM 11750 O  O   . HOH WA 6 .   ? 170.544 152.145 73.392 1.00   41.26 ? 2036 HOH D O   1 
HETATM 11751 O  O   . HOH WA 6 .   ? 168.496 154.537 69.212 1.00   48.70 ? 2037 HOH D O   1 
HETATM 11752 O  O   . HOH WA 6 .   ? 176.852 150.806 72.752 1.00   42.42 ? 2038 HOH D O   1 
HETATM 11753 O  O   . HOH WA 6 .   ? 176.628 152.969 71.326 1.00   25.67 ? 2039 HOH D O   1 
HETATM 11754 O  O   . HOH WA 6 .   ? 179.806 145.915 68.336 1.00   27.09 ? 2040 HOH D O   1 
HETATM 11755 O  O   . HOH WA 6 .   ? 181.748 146.755 66.704 1.00   24.77 ? 2041 HOH D O   1 
HETATM 11756 O  O   . HOH WA 6 .   ? 183.953 145.367 65.978 1.00   35.13 ? 2042 HOH D O   1 
HETATM 11757 O  O   . HOH WA 6 .   ? 186.675 149.063 65.984 1.00   41.63 ? 2043 HOH D O   1 
HETATM 11758 O  O   . HOH WA 6 .   ? 184.484 151.038 71.756 1.00   31.32 ? 2044 HOH D O   1 
HETATM 11759 O  O   . HOH WA 6 .   ? 188.016 150.334 69.340 1.00   39.66 ? 2045 HOH D O   1 
HETATM 11760 O  O   . HOH WA 6 .   ? 186.312 158.853 68.971 1.00   43.14 ? 2046 HOH D O   1 
HETATM 11761 O  O   . HOH WA 6 .   ? 188.588 158.666 72.028 1.00   44.79 ? 2047 HOH D O   1 
HETATM 11762 O  O   . HOH WA 6 .   ? 187.666 149.279 63.647 1.00   35.96 ? 2048 HOH D O   1 
HETATM 11763 O  O   . HOH WA 6 .   ? 189.451 151.863 63.095 1.00   38.91 ? 2049 HOH D O   1 
HETATM 11764 O  O   . HOH WA 6 .   ? 192.098 150.028 57.346 1.00   43.87 ? 2050 HOH D O   1 
HETATM 11765 O  O   . HOH WA 6 .   ? 176.189 140.897 42.368 1.00   36.77 ? 2051 HOH D O   1 
HETATM 11766 O  O   . HOH WA 6 .   ? 170.527 140.367 42.158 1.00   28.42 ? 2052 HOH D O   1 
HETATM 11767 O  O   . HOH WA 6 .   ? 164.734 138.650 54.141 1.00   20.95 ? 2053 HOH D O   1 
HETATM 11768 O  O   . HOH WA 6 .   ? 169.045 140.544 55.314 1.00   32.50 ? 2054 HOH D O   1 
HETATM 11769 O  O   . HOH WA 6 .   ? 166.254 131.790 50.918 1.00   35.03 ? 2055 HOH D O   1 
HETATM 11770 O  O   . HOH WA 6 .   ? 169.045 134.587 48.307 1.00   35.09 ? 2056 HOH D O   1 
HETATM 11771 O  O   . HOH WA 6 .   ? 166.415 136.103 60.891 1.00   55.00 ? 2057 HOH D O   1 
HETATM 11772 O  O   . HOH WA 6 .   ? 164.556 139.918 60.012 1.00   45.13 ? 2058 HOH D O   1 
HETATM 11773 O  O   . HOH WA 6 .   ? 166.780 141.697 57.873 1.00   40.47 ? 2059 HOH D O   1 
HETATM 11774 O  O   . HOH WA 6 .   ? 165.342 133.544 60.292 1.00   56.40 ? 2060 HOH D O   1 
HETATM 11775 O  O   . HOH WA 6 .   ? 168.301 133.882 61.633 1.00   61.60 ? 2061 HOH D O   1 
HETATM 11776 O  O   . HOH WA 6 .   ? 174.793 135.394 60.092 1.00   40.85 ? 2062 HOH D O   1 
HETATM 11777 O  O   . HOH WA 6 .   ? 149.310 154.636 57.139 1.00   47.01 ? 2063 HOH D O   1 
HETATM 11778 O  O   . HOH WA 6 .   ? 172.990 138.197 61.610 1.00   39.20 ? 2064 HOH D O   1 
HETATM 11779 O  O   . HOH WA 6 .   ? 184.098 136.779 48.085 1.00   58.67 ? 2065 HOH D O   1 
HETATM 11780 O  O   . HOH WA 6 .   ? 177.391 135.079 52.124 1.00   50.67 ? 2066 HOH D O   1 
HETATM 11781 O  O   . HOH WA 6 .   ? 178.963 136.417 56.703 1.00   42.14 ? 2067 HOH D O   1 
HETATM 11782 O  O   . HOH WA 6 .   ? 178.967 136.096 50.025 1.00   40.37 ? 2068 HOH D O   1 
HETATM 11783 O  O   . HOH WA 6 .   ? 181.006 139.846 50.052 1.00   39.01 ? 2069 HOH D O   1 
HETATM 11784 O  O   . HOH WA 6 .   ? 179.547 146.567 40.571 1.00   37.69 ? 2070 HOH D O   1 
HETATM 11785 O  O   . HOH WA 6 .   ? 182.845 144.045 33.428 1.00   51.63 ? 2071 HOH D O   1 
HETATM 11786 O  O   . HOH WA 6 .   ? 184.385 142.805 34.557 1.00   40.41 ? 2072 HOH D O   1 
HETATM 11787 O  O   . HOH WA 6 .   ? 185.479 140.467 35.716 1.00   45.98 ? 2073 HOH D O   1 
HETATM 11788 O  O   . HOH WA 6 .   ? 182.006 137.624 36.170 1.00   28.92 ? 2074 HOH D O   1 
HETATM 11789 O  O   . HOH WA 6 .   ? 181.465 150.790 34.235 1.00   50.43 ? 2075 HOH D O   1 
HETATM 11790 O  O   . HOH WA 6 .   ? 187.985 143.657 37.925 1.00   53.58 ? 2076 HOH D O   1 
HETATM 11791 O  O   . HOH WA 6 .   ? 190.375 145.703 44.806 1.00   47.08 ? 2077 HOH D O   1 
HETATM 11792 O  O   . HOH WA 6 .   ? 183.764 150.279 50.142 1.00   36.02 ? 2078 HOH D O   1 
HETATM 11793 O  O   . HOH WA 6 .   ? 186.480 156.112 48.596 1.00   43.95 ? 2079 HOH D O   1 
HETATM 11794 O  O   . HOH WA 6 .   ? 182.931 156.441 42.334 1.00   46.07 ? 2080 HOH D O   1 
HETATM 11795 O  O   . HOH WA 6 .   ? 179.751 157.903 48.291 1.00   43.60 ? 2081 HOH D O   1 
HETATM 11796 O  O   . HOH WA 6 .   ? 180.045 158.896 44.968 1.00   47.73 ? 2082 HOH D O   1 
HETATM 11797 O  O   . HOH WA 6 .   ? 190.804 154.743 48.810 1.00   62.67 ? 2083 HOH D O   1 
HETATM 11798 O  O   . HOH WA 6 .   ? 189.043 150.323 35.150 1.00   54.12 ? 2084 HOH D O   1 
HETATM 11799 O  O   . HOH WA 6 .   ? 181.310 156.585 52.505 1.00   41.78 ? 2085 HOH D O   1 
HETATM 11800 O  O   . HOH WA 6 .   ? 184.736 155.626 53.378 1.00   39.75 ? 2086 HOH D O   1 
HETATM 11801 O  O   . HOH WA 6 .   ? 181.016 157.204 55.164 1.00   40.48 ? 2087 HOH D O   1 
HETATM 11802 O  O   . HOH WA 6 .   ? 183.712 157.823 58.173 1.00   46.45 ? 2088 HOH D O   1 
HETATM 11803 O  O   . HOH WA 6 .   ? 187.399 154.765 54.937 1.00   38.44 ? 2089 HOH D O   1 
HETATM 11804 O  O   . HOH WA 6 .   ? 180.275 157.691 59.790 1.00   30.09 ? 2090 HOH D O   1 
HETATM 11805 O  O   . HOH WA 6 .   ? 180.355 159.220 63.505 1.00   36.10 ? 2091 HOH D O   1 
HETATM 11806 O  O   . HOH WA 6 .   ? 186.810 158.597 60.045 1.00   44.53 ? 2092 HOH D O   1 
HETATM 11807 O  O   . HOH WA 6 .   ? 186.237 157.728 66.264 1.00   39.72 ? 2093 HOH D O   1 
HETATM 11808 O  O   . HOH WA 6 .   ? 177.814 159.474 70.708 1.00   45.87 ? 2094 HOH D O   1 
HETATM 11809 O  O   . HOH WA 6 .   ? 184.818 160.261 70.047 1.00   33.03 ? 2095 HOH D O   1 
HETATM 11810 O  O   . HOH WA 6 .   ? 183.398 161.795 71.434 1.00   50.52 ? 2096 HOH D O   1 
HETATM 11811 O  O   . HOH WA 6 .   ? 179.447 158.554 57.233 1.00   33.94 ? 2097 HOH D O   1 
HETATM 11812 O  O   . HOH WA 6 .   ? 176.623 163.586 45.625 1.00   51.16 ? 2098 HOH D O   1 
HETATM 11813 O  O   . HOH WA 6 .   ? 178.708 165.212 49.959 1.00   57.40 ? 2099 HOH D O   1 
HETATM 11814 O  O   . HOH WA 6 .   ? 170.298 152.006 38.376 1.00   36.90 ? 2100 HOH D O   1 
HETATM 11815 O  O   . HOH WA 6 .   ? 169.373 151.239 34.177 1.00   33.31 ? 2101 HOH D O   1 
HETATM 11816 O  O   . HOH WA 6 .   ? 170.720 144.602 38.244 1.00   43.30 ? 2102 HOH D O   1 
HETATM 11817 O  O   . HOH WA 6 .   ? 169.088 146.366 41.072 1.00   33.68 ? 2103 HOH D O   1 
HETATM 11818 O  O   . HOH WA 6 .   ? 186.350 138.374 60.933 1.00   59.65 ? 2104 HOH D O   1 
HETATM 11819 O  O   . HOH WA 6 .   ? 187.686 142.819 65.736 1.00   43.57 ? 2105 HOH D O   1 
HETATM 11820 O  O   . HOH WA 6 .   ? 190.872 151.681 56.225 1.00   39.86 ? 2106 HOH D O   1 
HETATM 11821 O  O   . HOH WA 6 .   ? 192.779 152.328 51.113 1.00   49.36 ? 2107 HOH D O   1 
HETATM 11822 O  O   . HOH WA 6 .   ? 197.458 150.887 49.878 1.00   48.20 ? 2108 HOH D O   1 
HETATM 11823 O  O   . HOH WA 6 .   ? 193.181 138.333 54.005 1.00   44.48 ? 2109 HOH D O   1 
HETATM 11824 O  O   . HOH WA 6 .   ? 196.645 137.069 48.337 1.00   52.93 ? 2110 HOH D O   1 
HETATM 11825 O  O   . HOH WA 6 .   ? 189.947 135.869 49.067 1.00   61.57 ? 2111 HOH D O   1 
HETATM 11826 O  O   . HOH WA 6 .   ? 186.931 136.610 55.634 1.00   52.91 ? 2112 HOH D O   1 
HETATM 11827 O  O   . HOH WA 6 .   ? 187.745 140.034 56.423 1.00   49.97 ? 2113 HOH D O   1 
HETATM 11828 O  O   . HOH WA 6 .   ? 179.426 137.306 59.433 1.00   24.89 ? 2114 HOH D O   1 
HETATM 11829 O  O   . HOH WA 6 .   ? 176.019 137.802 60.787 1.00   42.37 ? 2115 HOH D O   1 
HETATM 11830 O  O   . HOH WA 6 .   ? 165.047 144.162 57.532 1.00   26.25 ? 2116 HOH D O   1 
HETATM 11831 O  O   . HOH WA 6 .   ? 157.783 155.117 55.553 1.00   31.11 ? 2117 HOH D O   1 
HETATM 11832 O  O   . HOH WA 6 .   ? 149.842 156.290 54.660 1.00   40.99 ? 2118 HOH D O   1 
HETATM 11833 O  O   . HOH WA 6 .   ? 181.493 137.836 56.650 1.00   51.22 ? 2119 HOH D O   1 
HETATM 11834 O  O   . HOH WA 6 .   ? 181.738 137.297 49.842 1.00   51.39 ? 2120 HOH D O   1 
HETATM 11835 O  O   . HOH XA 6 .   ? 133.378 99.678  36.506 1.00   51.08 ? 2001 HOH E O   1 
HETATM 11836 O  O   . HOH XA 6 .   ? 139.040 99.365  41.198 1.00   37.07 ? 2002 HOH E O   1 
HETATM 11837 O  O   . HOH XA 6 .   ? 141.580 98.987  40.908 1.00   51.82 ? 2003 HOH E O   1 
HETATM 11838 O  O   . HOH XA 6 .   ? 139.132 93.495  45.788 1.00   41.10 ? 2004 HOH E O   1 
HETATM 11839 O  O   . HOH XA 6 .   ? 138.394 94.484  47.939 1.00   24.97 ? 2005 HOH E O   1 
HETATM 11840 O  O   . HOH XA 6 .   ? 130.059 98.503  51.889 1.00   20.95 ? 2006 HOH E O   1 
HETATM 11841 O  O   . HOH XA 6 .   ? 127.260 98.075  55.800 1.00   39.15 ? 2007 HOH E O   1 
HETATM 11842 O  O   . HOH XA 6 .   ? 121.587 97.381  57.376 1.00   49.57 ? 2008 HOH E O   1 
HETATM 11843 O  O   . HOH XA 6 .   ? 124.314 97.568  56.216 1.00   40.53 ? 2009 HOH E O   1 
HETATM 11844 O  O   . HOH XA 6 .   ? 129.182 99.714  56.852 1.00   35.26 ? 2010 HOH E O   1 
HETATM 11845 O  O   . HOH XA 6 .   ? 125.677 93.447  62.159 1.00   40.20 ? 2011 HOH E O   1 
HETATM 11846 O  O   . HOH XA 6 .   ? 118.119 90.038  61.835 1.00   44.65 ? 2012 HOH E O   1 
HETATM 11847 O  O   . HOH XA 6 .   ? 122.779 90.581  62.151 1.00   35.41 ? 2013 HOH E O   1 
HETATM 11848 O  O   . HOH XA 6 .   ? 129.783 89.437  65.506 1.00   46.31 ? 2014 HOH E O   1 
HETATM 11849 O  O   . HOH XA 6 .   ? 135.863 85.764  62.706 1.00   49.82 ? 2015 HOH E O   1 
HETATM 11850 O  O   . HOH XA 6 .   ? 134.475 89.583  59.780 1.00   59.26 ? 2016 HOH E O   1 
HETATM 11851 O  O   . HOH XA 6 .   ? 127.596 95.016  63.062 1.00   46.73 ? 2017 HOH E O   1 
HETATM 11852 O  O   . HOH XA 6 .   ? 134.207 92.881  66.150 1.00   57.23 ? 2018 HOH E O   1 
HETATM 11853 O  O   . HOH XA 6 .   ? 119.022 83.963  63.182 1.00   46.78 ? 2019 HOH E O   1 
HETATM 11854 O  O   . HOH XA 6 .   ? 137.411 89.401  54.818 1.00   46.62 ? 2020 HOH E O   1 
HETATM 11855 O  O   . HOH XA 6 .   ? 138.961 91.019  53.652 1.00   36.50 ? 2021 HOH E O   1 
HETATM 11856 O  O   . HOH XA 6 .   ? 139.293 94.577  52.319 1.00   31.74 ? 2022 HOH E O   1 
HETATM 11857 O  O   . HOH XA 6 .   ? 139.418 87.944  38.354 1.00   40.41 ? 2023 HOH E O   1 
HETATM 11858 O  O   . HOH XA 6 .   ? 135.356 94.880  34.656 1.00   46.39 ? 2024 HOH E O   1 
HETATM 11859 O  O   . HOH XA 6 .   ? 131.765 88.638  34.300 1.00   49.68 ? 2025 HOH E O   1 
HETATM 11860 O  O   . HOH XA 6 .   ? 136.969 87.747  29.638 1.00   51.83 ? 2026 HOH E O   1 
HETATM 11861 O  O   . HOH XA 6 .   ? 125.886 76.351  44.048 1.00   39.40 ? 2027 HOH E O   1 
HETATM 11862 O  O   . HOH XA 6 .   ? 142.757 86.120  47.717 1.00   56.17 ? 2028 HOH E O   1 
HETATM 11863 O  O   . HOH XA 6 .   ? 122.668 85.012  33.037 1.00   52.89 ? 2029 HOH E O   1 
HETATM 11864 O  O   . HOH XA 6 .   ? 129.489 79.516  43.354 1.00   34.10 ? 2030 HOH E O   1 
HETATM 11865 O  O   . HOH XA 6 .   ? 137.781 82.905  52.439 1.00   34.85 ? 2031 HOH E O   1 
HETATM 11866 O  O   . HOH XA 6 .   ? 134.962 86.878  59.874 1.00   41.87 ? 2032 HOH E O   1 
HETATM 11867 O  O   . HOH XA 6 .   ? 131.005 83.826  64.917 1.00   25.46 ? 2033 HOH E O   1 
HETATM 11868 O  O   . HOH XA 6 .   ? 122.913 85.086  63.325 1.00   27.75 ? 2034 HOH E O   1 
HETATM 11869 O  O   . HOH XA 6 .   ? 125.828 85.172  66.716 1.00   39.82 ? 2035 HOH E O   1 
HETATM 11870 O  O   . HOH XA 6 .   ? 126.964 83.080  65.822 1.00   45.47 ? 2036 HOH E O   1 
HETATM 11871 O  O   . HOH XA 6 .   ? 122.609 83.472  61.501 1.00   25.99 ? 2037 HOH E O   1 
HETATM 11872 O  O   . HOH XA 6 .   ? 121.804 78.009  59.991 1.00   34.26 ? 2038 HOH E O   1 
HETATM 11873 O  O   . HOH XA 6 .   ? 120.269 82.188  60.822 1.00   29.15 ? 2039 HOH E O   1 
HETATM 11874 O  O   . HOH XA 6 .   ? 125.168 78.060  65.391 1.00   33.55 ? 2040 HOH E O   1 
HETATM 11875 O  O   . HOH XA 6 .   ? 122.313 75.729  62.640 1.00   40.74 ? 2041 HOH E O   1 
HETATM 11876 O  O   . HOH XA 6 .   ? 120.843 78.197  57.735 1.00   38.29 ? 2042 HOH E O   1 
HETATM 11877 O  O   . HOH XA 6 .   ? 116.050 76.121  56.423 1.00   53.35 ? 2043 HOH E O   1 
HETATM 11878 O  O   . HOH XA 6 .   ? 116.891 71.709  48.702 1.00   45.04 ? 2044 HOH E O   1 
HETATM 11879 O  O   . HOH XA 6 .   ? 112.428 95.874  41.325 1.00   38.90 ? 2045 HOH E O   1 
HETATM 11880 O  O   . HOH XA 6 .   ? 118.184 98.586  38.749 1.00   38.90 ? 2046 HOH E O   1 
HETATM 11881 O  O   . HOH XA 6 .   ? 121.821 102.893 50.367 1.00   23.43 ? 2047 HOH E O   1 
HETATM 11882 O  O   . HOH XA 6 .   ? 115.491 101.953 46.077 1.00   33.85 ? 2048 HOH E O   1 
HETATM 11883 O  O   . HOH XA 6 .   ? 115.212 105.368 49.162 1.00   42.68 ? 2049 HOH E O   1 
HETATM 11884 O  O   . HOH XA 6 .   ? 121.937 103.447 52.042 1.00   43.40 ? 2050 HOH E O   1 
HETATM 11885 O  O   . HOH XA 6 .   ? 119.876 102.245 58.163 1.00   47.44 ? 2051 HOH E O   1 
HETATM 11886 O  O   . HOH XA 6 .   ? 112.980 103.922 52.535 1.00   57.36 ? 2052 HOH E O   1 
HETATM 11887 O  O   . HOH XA 6 .   ? 118.489 95.453  57.932 1.00   34.08 ? 2053 HOH E O   1 
HETATM 11888 O  O   . HOH XA 6 .   ? 112.523 93.731  49.907 1.00   44.04 ? 2054 HOH E O   1 
HETATM 11889 O  O   . HOH XA 6 .   ? 113.838 99.935  47.467 1.00   42.09 ? 2055 HOH E O   1 
HETATM 11890 O  O   . HOH XA 6 .   ? 111.960 92.641  47.360 1.00   48.34 ? 2056 HOH E O   1 
HETATM 11891 O  O   . HOH XA 6 .   ? 114.162 88.074  43.811 1.00   43.29 ? 2057 HOH E O   1 
HETATM 11892 O  O   . HOH XA 6 .   ? 117.287 93.392  38.136 1.00   40.65 ? 2058 HOH E O   1 
HETATM 11893 O  O   . HOH XA 6 .   ? 119.211 88.271  35.355 1.00   38.29 ? 2059 HOH E O   1 
HETATM 11894 O  O   . HOH XA 6 .   ? 116.016 90.198  28.590 1.00   62.57 ? 2060 HOH E O   1 
HETATM 11895 O  O   . HOH XA 6 .   ? 121.524 81.345  44.451 1.00   31.60 ? 2061 HOH E O   1 
HETATM 11896 O  O   . HOH XA 6 .   ? 124.357 76.255  41.766 1.00   28.21 ? 2062 HOH E O   1 
HETATM 11897 O  O   . HOH XA 6 .   ? 128.975 73.195  44.117 1.00   46.16 ? 2063 HOH E O   1 
HETATM 11898 O  O   . HOH XA 6 .   ? 128.363 72.949  36.626 1.00   52.58 ? 2064 HOH E O   1 
HETATM 11899 O  O   . HOH XA 6 .   ? 125.236 80.095  34.548 1.00   52.94 ? 2065 HOH E O   1 
HETATM 11900 O  O   . HOH XA 6 .   ? 122.565 74.311  41.202 1.00   45.53 ? 2066 HOH E O   1 
HETATM 11901 O  O   . HOH XA 6 .   ? 121.791 74.982  33.549 1.00   44.77 ? 2067 HOH E O   1 
HETATM 11902 O  O   . HOH XA 6 .   ? 119.463 76.257  34.124 1.00   45.18 ? 2068 HOH E O   1 
HETATM 11903 O  O   . HOH XA 6 .   ? 120.643 85.944  34.435 1.00   39.57 ? 2069 HOH E O   1 
HETATM 11904 O  O   . HOH XA 6 .   ? 128.327 79.799  46.085 1.00   29.35 ? 2070 HOH E O   1 
HETATM 11905 O  O   . HOH XA 6 .   ? 126.428 77.806  46.474 1.00   24.25 ? 2071 HOH E O   1 
HETATM 11906 O  O   . HOH XA 6 .   ? 129.973 79.367  48.148 1.00   22.62 ? 2072 HOH E O   1 
HETATM 11907 O  O   . HOH XA 6 .   ? 128.725 77.281  50.865 1.00   35.57 ? 2073 HOH E O   1 
HETATM 11908 O  O   . HOH XA 6 .   ? 123.073 73.632  48.463 1.00   28.39 ? 2074 HOH E O   1 
HETATM 11909 O  O   . HOH XA 6 .   ? 124.693 75.567  48.364 1.00   33.50 ? 2075 HOH E O   1 
HETATM 11910 O  O   . HOH XA 6 .   ? 131.379 79.375  52.425 1.00   23.50 ? 2076 HOH E O   1 
HETATM 11911 O  O   . HOH XA 6 .   ? 133.110 78.445  54.747 1.00   35.72 ? 2077 HOH E O   1 
HETATM 11912 O  O   . HOH XA 6 .   ? 134.078 78.682  57.140 1.00   32.32 ? 2078 HOH E O   1 
HETATM 11913 O  O   . HOH XA 6 .   ? 135.582 77.811  58.767 1.00   44.18 ? 2079 HOH E O   1 
HETATM 11914 O  O   . HOH XA 6 .   ? 136.368 79.421  62.535 1.00   37.48 ? 2080 HOH E O   1 
HETATM 11915 O  O   . HOH XA 6 .   ? 134.104 70.054  64.761 1.00   50.92 ? 2081 HOH E O   1 
HETATM 11916 O  O   . HOH XA 6 .   ? 135.077 69.243  70.460 1.00   55.65 ? 2082 HOH E O   1 
HETATM 11917 O  O   . HOH XA 6 .   ? 132.190 81.781  67.764 1.00   34.26 ? 2083 HOH E O   1 
HETATM 11918 O  O   . HOH XA 6 .   ? 134.973 78.643  51.420 1.00   25.46 ? 2084 HOH E O   1 
HETATM 11919 O  O   . HOH XA 6 .   ? 138.055 78.008  57.492 1.00   21.63 ? 2085 HOH E O   1 
HETATM 11920 O  O   . HOH XA 6 .   ? 131.972 80.332  49.708 1.00   20.45 ? 2086 HOH E O   1 
HETATM 11921 O  O   . HOH XA 6 .   ? 139.653 78.963  48.967 1.00   36.67 ? 2087 HOH E O   1 
HETATM 11922 O  O   . HOH XA 6 .   ? 139.982 82.579  50.072 1.00   48.13 ? 2088 HOH E O   1 
HETATM 11923 O  O   . HOH XA 6 .   ? 132.817 79.237  42.896 1.00   48.77 ? 2089 HOH E O   1 
HETATM 11924 O  O   . HOH XA 6 .   ? 129.547 81.115  41.173 1.00   32.65 ? 2090 HOH E O   1 
HETATM 11925 O  O   . HOH XA 6 .   ? 132.943 78.481  40.292 1.00   41.23 ? 2091 HOH E O   1 
HETATM 11926 O  O   . HOH XA 6 .   ? 136.648 78.584  38.886 1.00   58.68 ? 2092 HOH E O   1 
HETATM 11927 O  O   . HOH XA 6 .   ? 129.634 81.135  37.098 1.00   39.68 ? 2093 HOH E O   1 
HETATM 11928 O  O   . HOH XA 6 .   ? 127.980 93.491  32.624 1.00   41.96 ? 2094 HOH E O   1 
HETATM 11929 O  O   . HOH XA 6 .   ? 124.273 97.047  35.997 1.00   43.55 ? 2095 HOH E O   1 
HETATM 11930 O  O   . HOH XA 6 .   ? 119.958 99.901  36.840 1.00   39.30 ? 2096 HOH E O   1 
HETATM 11931 O  O   . HOH XA 6 .   ? 124.913 99.824  37.087 1.00   64.11 ? 2097 HOH E O   1 
HETATM 11932 O  O   . HOH XA 6 .   ? 118.057 76.378  55.967 1.00   38.51 ? 2098 HOH E O   1 
HETATM 11933 O  O   . HOH XA 6 .   ? 115.617 77.008  52.764 1.00   41.81 ? 2099 HOH E O   1 
HETATM 11934 O  O   . HOH XA 6 .   ? 120.388 74.187  48.840 1.00   24.85 ? 2100 HOH E O   1 
HETATM 11935 O  O   . HOH XA 6 .   ? 118.836 72.731  46.782 1.00   37.84 ? 2101 HOH E O   1 
HETATM 11936 O  O   . HOH XA 6 .   ? 113.073 75.647  50.616 1.00   48.85 ? 2102 HOH E O   1 
HETATM 11937 O  O   . HOH XA 6 .   ? 108.410 76.143  40.875 1.00   56.58 ? 2103 HOH E O   1 
HETATM 11938 O  O   . HOH XA 6 .   ? 103.448 77.821  45.425 1.00   52.84 ? 2104 HOH E O   1 
HETATM 11939 O  O   . HOH XA 6 .   ? 102.139 86.042  44.320 1.00   60.88 ? 2105 HOH E O   1 
HETATM 11940 O  O   . HOH XA 6 .   ? 104.476 89.350  45.740 1.00   56.73 ? 2106 HOH E O   1 
HETATM 11941 O  O   . HOH XA 6 .   ? 114.184 91.101  55.725 1.00   37.41 ? 2107 HOH E O   1 
HETATM 11942 O  O   . HOH XA 6 .   ? 113.323 89.044  52.377 1.00   48.48 ? 2108 HOH E O   1 
HETATM 11943 O  O   . HOH XA 6 .   ? 126.917 99.726  52.907 1.00   22.56 ? 2109 HOH E O   1 
HETATM 11944 O  O   . HOH XA 6 .   ? 139.981 100.844 48.718 1.00   33.23 ? 2110 HOH E O   1 
HETATM 11945 O  O   . HOH XA 6 .   ? 144.479 105.269 43.940 1.00   44.93 ? 2111 HOH E O   1 
HETATM 11946 O  O   . HOH YA 6 .   ? 136.252 66.336  41.265 1.00   35.06 ? 2001 HOH F O   1 
HETATM 11947 O  O   . HOH YA 6 .   ? 135.024 70.934  39.211 1.00   56.28 ? 2002 HOH F O   1 
HETATM 11948 O  O   . HOH YA 6 .   ? 133.058 70.121  40.764 1.00   49.23 ? 2003 HOH F O   1 
HETATM 11949 O  O   . HOH YA 6 .   ? 139.738 69.933  39.596 1.00   40.94 ? 2004 HOH F O   1 
HETATM 11950 O  O   . HOH YA 6 .   ? 138.915 72.812  39.024 1.00   40.51 ? 2005 HOH F O   1 
HETATM 11951 O  O   . HOH YA 6 .   ? 134.393 64.929  43.300 1.00   43.26 ? 2006 HOH F O   1 
HETATM 11952 O  O   . HOH YA 6 .   ? 133.489 71.927  44.601 1.00   20.72 ? 2007 HOH F O   1 
HETATM 11953 O  O   . HOH YA 6 .   ? 136.115 77.289  40.951 1.00   47.26 ? 2008 HOH F O   1 
HETATM 11954 O  O   . HOH YA 6 .   ? 137.189 75.241  50.074 1.00   27.31 ? 2009 HOH F O   1 
HETATM 11955 O  O   . HOH YA 6 .   ? 139.174 67.636  69.275 1.00   31.65 ? 2010 HOH F O   1 
HETATM 11956 O  O   . HOH YA 6 .   ? 147.835 65.395  70.435 1.00   31.18 ? 2011 HOH F O   1 
HETATM 11957 O  O   . HOH YA 6 .   ? 136.503 66.162  57.353 1.00   12.85 ? 2012 HOH F O   1 
HETATM 11958 O  O   . HOH YA 6 .   ? 135.382 67.859  57.159 1.00   51.58 ? 2013 HOH F O   1 
HETATM 11959 O  O   . HOH YA 6 .   ? 137.466 64.823  61.506 1.00   25.79 ? 2014 HOH F O   1 
HETATM 11960 O  O   . HOH YA 6 .   ? 139.380 77.056  61.994 1.00   40.39 ? 2015 HOH F O   1 
HETATM 11961 O  O   . HOH YA 6 .   ? 137.963 69.688  65.150 1.00   36.83 ? 2016 HOH F O   1 
HETATM 11962 O  O   . HOH YA 6 .   ? 140.641 60.575  64.998 1.00   48.10 ? 2017 HOH F O   1 
HETATM 11963 O  O   . HOH YA 6 .   ? 139.090 62.531  62.615 1.00   26.42 ? 2018 HOH F O   1 
HETATM 11964 O  O   . HOH YA 6 .   ? 145.253 78.847  43.265 1.00   52.43 ? 2019 HOH F O   1 
HETATM 11965 O  O   . HOH YA 6 .   ? 141.458 66.781  68.680 1.00   21.83 ? 2020 HOH F O   1 
HETATM 11966 O  O   . HOH YA 6 .   ? 145.491 62.122  68.157 1.00   26.71 ? 2021 HOH F O   1 
HETATM 11967 O  O   . HOH YA 6 .   ? 142.902 59.404  66.409 1.00   44.55 ? 2022 HOH F O   1 
HETATM 11968 O  O   . HOH YA 6 .   ? 145.539 65.748  69.219 1.00   18.06 ? 2023 HOH F O   1 
HETATM 11969 O  O   . HOH YA 6 .   ? 142.512 67.605  74.486 1.00   44.83 ? 2024 HOH F O   1 
HETATM 11970 O  O   . HOH YA 6 .   ? 142.122 72.790  70.875 1.00   34.96 ? 2025 HOH F O   1 
HETATM 11971 O  O   . HOH YA 6 .   ? 144.082 82.106  66.361 1.00   51.01 ? 2026 HOH F O   1 
HETATM 11972 O  O   . HOH YA 6 .   ? 142.879 79.968  67.835 1.00   54.46 ? 2027 HOH F O   1 
HETATM 11973 O  O   . HOH YA 6 .   ? 138.965 73.853  65.500 1.00   45.67 ? 2028 HOH F O   1 
HETATM 11974 O  O   . HOH YA 6 .   ? 137.205 73.975  70.665 1.00   55.35 ? 2029 HOH F O   1 
HETATM 11975 O  O   . HOH YA 6 .   ? 144.168 78.640  69.897 1.00   32.69 ? 2030 HOH F O   1 
HETATM 11976 O  O   . HOH YA 6 .   ? 149.749 66.770  71.510 1.00   44.39 ? 2031 HOH F O   1 
HETATM 11977 O  O   . HOH YA 6 .   ? 152.541 76.026  72.438 1.00   42.69 ? 2032 HOH F O   1 
HETATM 11978 O  O   . HOH YA 6 .   ? 137.636 72.051  64.056 1.00   42.54 ? 2033 HOH F O   1 
HETATM 11979 O  O   . HOH YA 6 .   ? 152.951 65.482  70.785 1.00   51.93 ? 2034 HOH F O   1 
HETATM 11980 O  O   . HOH YA 6 .   ? 154.518 72.973  74.010 1.00   33.05 ? 2035 HOH F O   1 
HETATM 11981 O  O   . HOH YA 6 .   ? 159.348 78.023  65.549 1.00   41.36 ? 2036 HOH F O   1 
HETATM 11982 O  O   . HOH YA 6 .   ? 140.126 77.550  59.299 1.00   25.20 ? 2037 HOH F O   1 
HETATM 11983 O  O   . HOH YA 6 .   ? 161.225 75.447  63.337 1.00   32.56 ? 2038 HOH F O   1 
HETATM 11984 O  O   . HOH YA 6 .   ? 135.925 75.099  52.218 1.00   31.68 ? 2039 HOH F O   1 
HETATM 11985 O  O   . HOH YA 6 .   ? 135.635 76.367  55.920 1.00   33.87 ? 2040 HOH F O   1 
HETATM 11986 O  O   . HOH YA 6 .   ? 142.957 77.851  43.145 1.00   28.53 ? 2041 HOH F O   1 
HETATM 11987 O  O   . HOH YA 6 .   ? 147.139 70.250  40.668 1.00   33.11 ? 2042 HOH F O   1 
HETATM 11988 O  O   . HOH YA 6 .   ? 143.841 75.861  39.801 1.00   18.45 ? 2043 HOH F O   1 
HETATM 11989 O  O   . HOH YA 6 .   ? 144.654 78.275  38.614 1.00   32.75 ? 2044 HOH F O   1 
HETATM 11990 O  O   . HOH YA 6 .   ? 146.165 80.414  39.935 1.00   57.59 ? 2045 HOH F O   1 
HETATM 11991 O  O   . HOH YA 6 .   ? 145.786 83.027  38.762 1.00   56.28 ? 2046 HOH F O   1 
HETATM 11992 O  O   . HOH YA 6 .   ? 155.450 54.323  53.480 1.00   46.53 ? 2047 HOH F O   1 
HETATM 11993 O  O   . HOH YA 6 .   ? 138.901 73.347  35.027 1.00   41.22 ? 2048 HOH F O   1 
HETATM 11994 O  O   . HOH YA 6 .   ? 143.884 67.287  37.764 1.00   30.90 ? 2049 HOH F O   1 
HETATM 11995 O  O   . HOH YA 6 .   ? 143.193 69.337  34.126 1.00   38.15 ? 2050 HOH F O   1 
HETATM 11996 O  O   . HOH YA 6 .   ? 148.846 71.428  38.584 1.00   27.50 ? 2051 HOH F O   1 
HETATM 11997 O  O   . HOH YA 6 .   ? 142.004 75.729  32.138 1.00   52.47 ? 2052 HOH F O   1 
HETATM 11998 O  O   . HOH YA 6 .   ? 144.545 76.616  30.757 1.00   39.80 ? 2053 HOH F O   1 
HETATM 11999 O  O   . HOH YA 6 .   ? 167.577 58.505  49.430 1.00   36.36 ? 2054 HOH F O   1 
HETATM 12000 O  O   . HOH YA 6 .   ? 158.892 72.844  51.336 1.00   12.64 ? 2055 HOH F O   1 
HETATM 12001 O  O   . HOH YA 6 .   ? 156.507 73.991  44.884 1.00   38.85 ? 2056 HOH F O   1 
HETATM 12002 O  O   . HOH YA 6 .   ? 157.250 74.442  49.793 1.00   17.56 ? 2057 HOH F O   1 
HETATM 12003 O  O   . HOH YA 6 .   ? 163.977 63.270  40.983 1.00   37.00 ? 2058 HOH F O   1 
HETATM 12004 O  O   . HOH YA 6 .   ? 153.044 64.328  39.592 1.00   33.37 ? 2059 HOH F O   1 
HETATM 12005 O  O   . HOH YA 6 .   ? 154.349 63.475  41.605 1.00   26.51 ? 2060 HOH F O   1 
HETATM 12006 O  O   . HOH YA 6 .   ? 146.864 79.138  50.299 1.00   40.33 ? 2061 HOH F O   1 
HETATM 12007 O  O   . HOH YA 6 .   ? 154.963 74.969  51.449 1.00   14.30 ? 2062 HOH F O   1 
HETATM 12008 O  O   . HOH YA 6 .   ? 145.713 80.618  56.827 1.00   18.59 ? 2063 HOH F O   1 
HETATM 12009 O  O   . HOH YA 6 .   ? 144.193 80.707  58.947 1.00   25.37 ? 2064 HOH F O   1 
HETATM 12010 O  O   . HOH YA 6 .   ? 161.432 76.065  60.487 1.00   37.63 ? 2065 HOH F O   1 
HETATM 12011 O  O   . HOH YA 6 .   ? 140.280 76.012  64.413 1.00   56.64 ? 2066 HOH F O   1 
HETATM 12012 O  O   . HOH YA 6 .   ? 142.089 77.392  64.730 1.00   43.67 ? 2067 HOH F O   1 
HETATM 12013 O  O   . HOH YA 6 .   ? 144.089 81.381  63.439 1.00   30.06 ? 2068 HOH F O   1 
HETATM 12014 O  O   . HOH YA 6 .   ? 153.380 84.664  67.073 1.00   46.01 ? 2069 HOH F O   1 
HETATM 12015 O  O   . HOH YA 6 .   ? 157.133 85.741  68.435 1.00   41.80 ? 2070 HOH F O   1 
HETATM 12016 O  O   . HOH YA 6 .   ? 157.886 85.567  74.016 1.00   56.47 ? 2071 HOH F O   1 
HETATM 12017 O  O   . HOH YA 6 .   ? 140.216 79.989  68.773 1.00   46.57 ? 2072 HOH F O   1 
HETATM 12018 O  O   . HOH YA 6 .   ? 146.537 76.625  70.093 1.00   24.97 ? 2073 HOH F O   1 
HETATM 12019 O  O   . HOH YA 6 .   ? 149.744 69.226  70.808 1.00   26.81 ? 2074 HOH F O   1 
HETATM 12020 O  O   . HOH YA 6 .   ? 149.876 71.395  73.183 1.00   52.42 ? 2075 HOH F O   1 
HETATM 12021 O  O   . HOH YA 6 .   ? 153.077 78.674  49.409 1.00   32.73 ? 2076 HOH F O   1 
HETATM 12022 O  O   . HOH YA 6 .   ? 149.511 74.711  71.957 1.00   39.45 ? 2077 HOH F O   1 
HETATM 12023 O  O   . HOH YA 6 .   ? 156.035 73.444  47.496 1.00   19.47 ? 2078 HOH F O   1 
HETATM 12024 O  O   . HOH YA 6 .   ? 151.854 69.259  68.653 1.00   18.72 ? 2079 HOH F O   1 
HETATM 12025 O  O   . HOH YA 6 .   ? 154.044 67.891  68.849 1.00   17.35 ? 2080 HOH F O   1 
HETATM 12026 O  O   . HOH YA 6 .   ? 157.230 71.406  67.748 1.00   32.56 ? 2081 HOH F O   1 
HETATM 12027 O  O   . HOH YA 6 .   ? 154.427 75.320  72.043 1.00   22.14 ? 2082 HOH F O   1 
HETATM 12028 O  O   . HOH YA 6 .   ? 157.934 73.741  70.694 1.00   29.51 ? 2083 HOH F O   1 
HETATM 12029 O  O   . HOH YA 6 .   ? 156.065 77.659  72.628 1.00   40.40 ? 2084 HOH F O   1 
HETATM 12030 O  O   . HOH YA 6 .   ? 158.386 80.809  72.223 1.00   38.63 ? 2085 HOH F O   1 
HETATM 12031 O  O   . HOH YA 6 .   ? 157.107 79.382  65.377 0.40   16.51 ? 2086 HOH F O   1 
HETATM 12032 O  O   . HOH YA 6 .   ? 157.379 80.692  66.021 0.60   14.17 ? 2087 HOH F O   1 
HETATM 12033 O  O   . HOH YA 6 .   ? 160.332 73.185  64.782 1.00   23.98 ? 2088 HOH F O   1 
HETATM 12034 O  O   . HOH YA 6 .   ? 158.241 70.140  66.099 1.00   24.44 ? 2089 HOH F O   1 
HETATM 12035 O  O   . HOH YA 6 .   ? 149.097 57.719  37.825 1.00   60.03 ? 2090 HOH F O   1 
HETATM 12036 O  O   . HOH YA 6 .   ? 161.705 67.074  65.199 1.00   29.26 ? 2091 HOH F O   1 
HETATM 12037 O  O   . HOH YA 6 .   ? 163.318 72.068  58.340 1.00   37.08 ? 2092 HOH F O   1 
HETATM 12038 O  O   . HOH YA 6 .   ? 166.743 67.703  57.825 1.00   39.35 ? 2093 HOH F O   1 
HETATM 12039 O  O   . HOH YA 6 .   ? 167.849 69.055  56.181 1.00   54.33 ? 2094 HOH F O   1 
HETATM 12040 O  O   . HOH YA 6 .   ? 166.743 62.961  46.293 1.00   36.94 ? 2095 HOH F O   1 
HETATM 12041 O  O   . HOH YA 6 .   ? 168.982 63.586  50.189 1.00   24.21 ? 2096 HOH F O   1 
HETATM 12042 O  O   . HOH YA 6 .   ? 169.934 61.454  51.519 1.00   22.65 ? 2097 HOH F O   1 
HETATM 12043 O  O   . HOH YA 6 .   ? 169.711 65.989  51.421 1.00   16.90 ? 2098 HOH F O   1 
HETATM 12044 O  O   . HOH YA 6 .   ? 148.772 55.476  47.303 1.00   21.56 ? 2099 HOH F O   1 
HETATM 12045 O  O   . HOH YA 6 .   ? 148.552 51.043  50.730 1.00   33.71 ? 2100 HOH F O   1 
HETATM 12046 O  O   . HOH YA 6 .   ? 147.218 54.813  45.181 1.00   37.06 ? 2101 HOH F O   1 
HETATM 12047 O  O   . HOH YA 6 .   ? 144.238 54.109  47.084 1.00   20.19 ? 2102 HOH F O   1 
HETATM 12048 O  O   . HOH YA 6 .   ? 164.326 55.223  62.172 1.00   32.64 ? 2103 HOH F O   1 
HETATM 12049 O  O   . HOH YA 6 .   ? 136.521 56.649  57.533 1.00   14.40 ? 2104 HOH F O   1 
HETATM 12050 O  O   . HOH YA 6 .   ? 141.927 58.233  59.396 1.00   20.57 ? 2105 HOH F O   1 
HETATM 12051 O  O   . HOH YA 6 .   ? 140.452 58.991  58.534 1.00   25.98 ? 2106 HOH F O   1 
HETATM 12052 O  O   . HOH YA 6 .   ? 137.699 49.606  57.314 1.00   28.09 ? 2107 HOH F O   1 
HETATM 12053 O  O   . HOH YA 6 .   ? 136.602 56.349  64.965 1.00   39.78 ? 2108 HOH F O   1 
HETATM 12054 O  O   . HOH YA 6 .   ? 135.041 60.126  62.842 1.00   34.32 ? 2109 HOH F O   1 
HETATM 12055 O  O   . HOH YA 6 .   ? 138.148 61.334  60.396 1.00   30.53 ? 2110 HOH F O   1 
HETATM 12056 O  O   . HOH YA 6 .   ? 134.864 54.265  64.661 1.00   54.21 ? 2111 HOH F O   1 
HETATM 12057 O  O   . HOH YA 6 .   ? 139.956 49.466  61.564 1.00   39.58 ? 2112 HOH F O   1 
HETATM 12058 O  O   . HOH YA 6 .   ? 148.981 53.323  59.659 1.00   31.76 ? 2113 HOH F O   1 
HETATM 12059 O  O   . HOH YA 6 .   ? 148.033 54.103  67.502 1.00   53.75 ? 2114 HOH F O   1 
HETATM 12060 O  O   . HOH YA 6 .   ? 149.703 53.923  65.457 1.00   42.79 ? 2115 HOH F O   1 
HETATM 12061 O  O   . HOH YA 6 .   ? 149.367 56.450  64.363 0.50   21.59 ? 2116 HOH F O   1 
HETATM 12062 O  O   . HOH YA 6 .   ? 144.118 50.454  61.307 1.00   32.24 ? 2117 HOH F O   1 
HETATM 12063 O  O   . HOH YA 6 .   ? 143.176 51.151  56.305 1.00   28.36 ? 2118 HOH F O   1 
HETATM 12064 O  O   . HOH YA 6 .   ? 150.570 53.316  57.538 1.00   19.90 ? 2119 HOH F O   1 
HETATM 12065 O  O   . HOH YA 6 .   ? 154.373 56.894  53.771 1.00   19.63 ? 2120 HOH F O   1 
HETATM 12066 O  O   . HOH YA 6 .   ? 152.976 55.290  50.335 0.40   8.94  ? 2121 HOH F O   1 
HETATM 12067 O  O   . HOH YA 6 .   ? 153.310 59.369  58.082 1.00   22.99 ? 2122 HOH F O   1 
HETATM 12068 O  O   . HOH YA 6 .   ? 152.105 52.819  45.691 1.00   46.14 ? 2123 HOH F O   1 
HETATM 12069 O  O   . HOH YA 6 .   ? 152.911 59.477  44.225 1.00   11.46 ? 2124 HOH F O   1 
HETATM 12070 O  O   . HOH YA 6 .   ? 154.396 54.133  49.274 0.60   12.76 ? 2125 HOH F O   1 
HETATM 12071 O  O   . HOH YA 6 .   ? 157.150 53.265  46.790 1.00   39.82 ? 2126 HOH F O   1 
HETATM 12072 O  O   . HOH YA 6 .   ? 148.506 54.194  40.756 1.00   43.91 ? 2127 HOH F O   1 
HETATM 12073 O  O   . HOH YA 6 .   ? 158.684 54.789  40.829 1.00   51.47 ? 2128 HOH F O   1 
HETATM 12074 O  O   . HOH YA 6 .   ? 157.978 55.631  50.035 1.00   18.87 ? 2129 HOH F O   1 
HETATM 12075 O  O   . HOH YA 6 .   ? 156.261 58.340  37.230 1.00   41.69 ? 2130 HOH F O   1 
HETATM 12076 O  O   . HOH YA 6 .   ? 160.006 60.816  40.564 1.00   42.62 ? 2131 HOH F O   1 
HETATM 12077 O  O   . HOH YA 6 .   ? 157.709 64.136  37.861 1.00   52.65 ? 2132 HOH F O   1 
HETATM 12078 O  O   . HOH YA 6 .   ? 166.754 55.973  49.648 1.00   46.27 ? 2133 HOH F O   1 
HETATM 12079 O  O   . HOH YA 6 .   ? 164.495 58.019  45.545 1.00   43.76 ? 2134 HOH F O   1 
HETATM 12080 O  O   . HOH YA 6 .   ? 163.088 61.640  48.164 1.00   28.06 ? 2135 HOH F O   1 
HETATM 12081 O  O   . HOH YA 6 .   ? 156.415 66.206  52.708 1.00   10.03 ? 2136 HOH F O   1 
HETATM 12082 O  O   . HOH YA 6 .   ? 160.024 70.640  49.526 1.00   10.32 ? 2137 HOH F O   1 
HETATM 12083 O  O   . HOH YA 6 .   ? 155.929 71.099  43.371 1.00   42.19 ? 2138 HOH F O   1 
HETATM 12084 O  O   . HOH YA 6 .   ? 157.018 69.244  42.578 1.00   35.73 ? 2139 HOH F O   1 
HETATM 12085 O  O   . HOH YA 6 .   ? 159.657 72.210  49.847 1.00   36.80 ? 2140 HOH F O   1 
HETATM 12086 O  O   . HOH YA 6 .   ? 160.534 77.913  49.193 1.00   19.85 ? 2141 HOH F O   1 
HETATM 12087 O  O   . HOH YA 6 .   ? 163.667 77.455  50.029 1.00   12.91 ? 2142 HOH F O   1 
HETATM 12088 O  O   . HOH YA 6 .   ? 156.884 67.233  42.026 1.00   38.85 ? 2143 HOH F O   1 
HETATM 12089 O  O   . HOH YA 6 .   ? 163.333 67.695  50.282 1.00   14.41 ? 2144 HOH F O   1 
HETATM 12090 O  O   . HOH YA 6 .   ? 164.504 64.912  49.362 1.00   23.38 ? 2145 HOH F O   1 
HETATM 12091 O  O   . HOH YA 6 .   ? 162.955 63.758  47.235 1.00   23.47 ? 2146 HOH F O   1 
HETATM 12092 O  O   . HOH YA 6 .   ? 163.636 65.385  43.244 1.00   26.91 ? 2147 HOH F O   1 
HETATM 12093 O  O   . HOH YA 6 .   ? 163.724 67.857  42.379 1.00   29.58 ? 2148 HOH F O   1 
HETATM 12094 O  O   . HOH YA 6 .   ? 155.939 65.026  41.502 1.00   27.45 ? 2149 HOH F O   1 
HETATM 12095 O  O   . HOH YA 6 .   ? 162.110 61.590  40.572 1.00   33.78 ? 2150 HOH F O   1 
HETATM 12096 O  O   . HOH YA 6 .   ? 161.376 56.015  43.215 1.00   38.55 ? 2151 HOH F O   1 
HETATM 12097 O  O   . HOH YA 6 .   ? 154.498 61.326  42.988 1.00   16.56 ? 2152 HOH F O   1 
HETATM 12098 O  O   . HOH YA 6 .   ? 154.683 72.965  53.361 1.00   13.56 ? 2153 HOH F O   1 
HETATM 12099 O  O   . HOH YA 6 .   ? 157.355 72.488  53.625 1.00   20.22 ? 2154 HOH F O   1 
HETATM 12100 O  O   . HOH YA 6 .   ? 159.796 72.702  55.931 1.00   17.50 ? 2155 HOH F O   1 
HETATM 12101 O  O   . HOH YA 6 .   ? 151.142 79.873  61.878 1.00   13.43 ? 2156 HOH F O   1 
HETATM 12102 O  O   . HOH YA 6 .   ? 158.823 77.622  60.025 1.00   9.73  ? 2157 HOH F O   1 
HETATM 12103 O  O   . HOH YA 6 .   ? 147.758 82.961  66.897 1.00   29.84 ? 2158 HOH F O   1 
HETATM 12104 O  O   . HOH YA 6 .   ? 150.040 82.082  63.164 1.00   15.47 ? 2159 HOH F O   1 
HETATM 12105 O  O   . HOH YA 6 .   ? 151.156 84.413  65.674 1.00   36.02 ? 2160 HOH F O   1 
HETATM 12106 O  O   . HOH YA 6 .   ? 155.056 82.816  67.378 1.00   24.02 ? 2161 HOH F O   1 
HETATM 12107 O  O   . HOH YA 6 .   ? 151.146 77.034  73.353 1.00   52.30 ? 2162 HOH F O   1 
HETATM 12108 O  O   . HOH YA 6 .   ? 157.281 86.216  71.178 1.00   59.58 ? 2163 HOH F O   1 
HETATM 12109 O  O   . HOH YA 6 .   ? 149.242 80.703  74.441 1.00   48.04 ? 2164 HOH F O   1 
HETATM 12110 O  O   . HOH YA 6 .   ? 146.363 83.315  64.227 1.00   29.62 ? 2165 HOH F O   1 
HETATM 12111 O  O   . HOH YA 6 .   ? 149.162 84.405  59.836 1.00   22.92 ? 2166 HOH F O   1 
HETATM 12112 O  O   . HOH YA 6 .   ? 153.455 78.828  53.361 1.00   18.72 ? 2167 HOH F O   1 
HETATM 12113 O  O   . HOH YA 6 .   ? 151.129 80.551  50.215 1.00   43.65 ? 2168 HOH F O   1 
HETATM 12114 O  O   . HOH YA 6 .   ? 146.541 81.741  52.423 1.00   34.79 ? 2169 HOH F O   1 
HETATM 12115 O  O   . HOH YA 6 .   ? 153.251 76.144  49.222 1.00   17.09 ? 2170 HOH F O   1 
HETATM 12116 O  O   . HOH YA 6 .   ? 153.350 72.815  47.668 1.00   19.02 ? 2171 HOH F O   1 
HETATM 12117 O  O   . HOH YA 6 .   ? 153.924 74.690  44.251 1.00   42.21 ? 2172 HOH F O   1 
HETATM 12118 O  O   . HOH YA 6 .   ? 148.087 80.177  46.040 1.00   36.39 ? 2173 HOH F O   1 
HETATM 12119 O  O   . HOH YA 6 .   ? 148.454 80.293  41.605 1.00   48.01 ? 2174 HOH F O   1 
HETATM 12120 O  O   . HOH YA 6 .   ? 151.724 75.459  42.820 1.00   29.15 ? 2175 HOH F O   1 
HETATM 12121 O  O   . HOH YA 6 .   ? 169.928 74.983  57.495 1.00   38.07 ? 2176 HOH F O   1 
HETATM 12122 O  O   . HOH YA 6 .   ? 153.788 72.178  43.749 1.00   26.57 ? 2177 HOH F O   1 
HETATM 12123 O  O   . HOH YA 6 .   ? 149.994 73.785  37.713 1.00   47.10 ? 2178 HOH F O   1 
HETATM 12124 O  O   . HOH YA 6 .   ? 144.812 64.326  38.905 1.00   18.30 ? 2179 HOH F O   1 
HETATM 12125 O  O   . HOH YA 6 .   ? 142.235 65.690  36.142 1.00   37.80 ? 2180 HOH F O   1 
HETATM 12126 O  O   . HOH YA 6 .   ? 137.852 62.875  38.313 1.00   35.88 ? 2181 HOH F O   1 
HETATM 12127 O  O   . HOH YA 6 .   ? 142.847 59.691  43.493 1.00   20.12 ? 2182 HOH F O   1 
HETATM 12128 O  O   . HOH YA 6 .   ? 145.137 57.311  41.388 1.00   34.68 ? 2183 HOH F O   1 
HETATM 12129 O  O   . HOH YA 6 .   ? 149.839 60.083  37.639 1.00   46.45 ? 2184 HOH F O   1 
HETATM 12130 O  O   . HOH YA 6 .   ? 139.414 60.181  45.130 1.00   45.42 ? 2185 HOH F O   1 
HETATM 12131 O  O   . HOH YA 6 .   ? 142.916 54.630  44.945 1.00   36.77 ? 2186 HOH F O   1 
HETATM 12132 O  O   . HOH YA 6 .   ? 145.385 55.576  43.729 1.00   42.39 ? 2187 HOH F O   1 
HETATM 12133 O  O   . HOH YA 6 .   ? 157.561 68.285  67.885 1.00   41.70 ? 2188 HOH F O   1 
HETATM 12134 O  O   . HOH YA 6 .   ? 156.689 59.218  67.721 1.00   39.63 ? 2189 HOH F O   1 
HETATM 12135 O  O   . HOH YA 6 .   ? 159.418 61.992  68.478 1.00   42.01 ? 2190 HOH F O   1 
HETATM 12136 O  O   . HOH YA 6 .   ? 157.854 61.248  71.445 1.00   39.73 ? 2191 HOH F O   1 
HETATM 12137 O  O   . HOH YA 6 .   ? 158.374 65.536  69.544 1.00   57.41 ? 2192 HOH F O   1 
HETATM 12138 O  O   . HOH YA 6 .   ? 156.326 64.575  71.112 1.00   45.29 ? 2193 HOH F O   1 
HETATM 12139 O  O   . HOH YA 6 .   ? 152.323 62.801  71.597 1.00   54.16 ? 2194 HOH F O   1 
HETATM 12140 O  O   . HOH YA 6 .   ? 159.006 59.137  65.881 1.00   43.34 ? 2195 HOH F O   1 
HETATM 12141 O  O   . HOH YA 6 .   ? 160.022 68.306  65.151 1.00   27.83 ? 2196 HOH F O   1 
HETATM 12142 O  O   . HOH YA 6 .   ? 161.735 64.931  62.507 1.00   16.10 ? 2197 HOH F O   1 
HETATM 12143 O  O   . HOH YA 6 .   ? 162.664 69.737  58.537 1.00   30.24 ? 2198 HOH F O   1 
HETATM 12144 O  O   . HOH YA 6 .   ? 165.066 68.629  55.966 1.00   25.22 ? 2199 HOH F O   1 
HETATM 12145 O  O   . HOH YA 6 .   ? 165.689 63.388  60.076 1.00   17.46 ? 2200 HOH F O   1 
HETATM 12146 O  O   . HOH YA 6 .   ? 166.415 62.914  49.161 1.00   29.90 ? 2201 HOH F O   1 
HETATM 12147 O  O   . HOH YA 6 .   ? 167.579 60.793  53.020 1.00   13.31 ? 2202 HOH F O   1 
HETATM 12148 O  O   . HOH YA 6 .   ? 169.188 66.840  56.157 1.00   18.90 ? 2203 HOH F O   1 
HETATM 12149 O  O   . HOH YA 6 .   ? 170.811 64.874  53.664 1.00   18.41 ? 2204 HOH F O   1 
HETATM 12150 O  O   . HOH YA 6 .   ? 166.266 70.076  49.066 1.00   33.42 ? 2205 HOH F O   1 
HETATM 12151 O  O   . HOH YA 6 .   ? 169.509 70.556  50.003 1.00   20.64 ? 2206 HOH F O   1 
HETATM 12152 O  O   . HOH YA 6 .   ? 170.398 57.611  59.447 1.00   31.02 ? 2207 HOH F O   1 
HETATM 12153 O  O   . HOH YA 6 .   ? 167.310 58.152  52.726 1.00   28.51 ? 2208 HOH F O   1 
HETATM 12154 O  O   . HOH YA 6 .   ? 164.936 54.368  59.466 1.00   23.75 ? 2209 HOH F O   1 
HETATM 12155 O  O   . HOH YA 6 .   ? 164.329 57.574  62.439 1.00   31.78 ? 2210 HOH F O   1 
HETATM 12156 O  O   . HOH YA 6 .   ? 167.976 55.967  61.968 1.00   19.98 ? 2211 HOH F O   1 
HETATM 12157 O  O   . HOH YA 6 .   ? 167.144 52.737  57.197 1.00   29.41 ? 2212 HOH F O   1 
HETATM 12158 O  O   . HOH YA 6 .   ? 166.364 50.508  57.294 1.00   38.62 ? 2213 HOH F O   1 
HETATM 12159 O  O   . HOH YA 6 .   ? 157.297 53.835  58.511 1.00   37.92 ? 2214 HOH F O   1 
HETATM 12160 O  O   . HOH YA 6 .   ? 161.757 52.292  58.204 1.00   44.39 ? 2215 HOH F O   1 
HETATM 12161 O  O   . HOH YA 6 .   ? 161.674 54.396  62.397 1.00   39.18 ? 2216 HOH F O   1 
HETATM 12162 O  O   . HOH YA 6 .   ? 158.218 58.973  61.797 1.00   26.47 ? 2217 HOH F O   1 
HETATM 12163 O  O   . HOH YA 6 .   ? 154.999 59.389  60.426 1.00   24.06 ? 2218 HOH F O   1 
HETATM 12164 O  O   . HOH YA 6 .   ? 155.687 57.431  65.156 1.00   41.44 ? 2219 HOH F O   1 
HETATM 12165 O  O   . HOH YA 6 .   ? 149.710 60.912  68.520 1.00   41.28 ? 2220 HOH F O   1 
HETATM 12166 O  O   . HOH YA 6 .   ? 149.972 57.830  65.248 0.50   3.08  ? 2221 HOH F O   1 
HETATM 12167 O  O   . HOH YA 6 .   ? 150.163 54.764  62.381 1.00   36.10 ? 2222 HOH F O   1 
HETATM 12168 O  O   . HOH YA 6 .   ? 152.654 54.387  57.176 1.00   32.82 ? 2223 HOH F O   1 
HETATM 12169 O  O   . HOH YA 6 .   ? 139.924 60.715  59.016 1.00   32.68 ? 2224 HOH F O   1 
HETATM 12170 O  O   . HOH YA 6 .   ? 136.464 63.352  58.698 1.00   25.05 ? 2225 HOH F O   1 
HETATM 12171 O  O   . HOH YA 6 .   ? 131.305 76.948  45.075 1.00   46.34 ? 2226 HOH F O   1 
HETATM 12172 O  O   . HOH YA 6 .   ? 154.435 54.648  58.753 1.00   51.11 ? 2227 HOH F O   1 
HETATM 12173 O  O   . HOH YA 6 .   ? 153.021 56.910  56.396 1.00   26.04 ? 2228 HOH F O   1 
HETATM 12174 O  O   . HOH YA 6 .   ? 162.752 70.725  49.900 1.00   19.34 ? 2229 HOH F O   1 
HETATM 12175 O  O   . HOH YA 6 .   ? 166.196 76.481  49.954 1.00   24.26 ? 2230 HOH F O   1 
HETATM 12176 O  O   . HOH YA 6 .   ? 168.262 73.922  48.030 1.00   43.89 ? 2231 HOH F O   1 
HETATM 12177 O  O   . HOH YA 6 .   ? 166.070 76.061  46.530 1.00   38.38 ? 2232 HOH F O   1 
HETATM 12178 O  O   . HOH YA 6 .   ? 166.213 72.577  58.025 1.00   38.32 ? 2233 HOH F O   1 
HETATM 12179 O  O   . HOH YA 6 .   ? 165.314 75.660  55.718 1.00   52.26 ? 2234 HOH F O   1 
HETATM 12180 O  O   . HOH YA 6 .   ? 166.882 75.486  57.921 1.00   38.60 ? 2235 HOH F O   1 
HETATM 12181 O  O   . HOH YA 6 .   ? 169.968 73.518  55.443 1.00   26.96 ? 2236 HOH F O   1 
HETATM 12182 O  O   . HOH YA 6 .   ? 168.883 70.977  57.256 1.00   44.35 ? 2237 HOH F O   1 
HETATM 12183 O  O   . HOH YA 6 .   ? 168.124 76.143  55.688 1.00   39.61 ? 2238 HOH F O   1 
HETATM 12184 O  O   . HOH ZA 6 .   ? 175.559 102.133 41.210 1.00   38.77 ? 2001 HOH G O   1 
HETATM 12185 O  O   . HOH ZA 6 .   ? 180.550 101.888 39.865 1.00   44.37 ? 2002 HOH G O   1 
HETATM 12186 O  O   . HOH ZA 6 .   ? 181.464 101.718 44.941 1.00   26.89 ? 2003 HOH G O   1 
HETATM 12187 O  O   . HOH ZA 6 .   ? 182.618 97.892  51.953 1.00   31.88 ? 2004 HOH G O   1 
HETATM 12188 O  O   . HOH ZA 6 .   ? 166.502 93.950  70.276 1.00   40.93 ? 2005 HOH G O   1 
HETATM 12189 O  O   . HOH ZA 6 .   ? 168.755 92.516  70.371 1.00   34.72 ? 2006 HOH G O   1 
HETATM 12190 O  O   . HOH ZA 6 .   ? 175.164 101.773 57.267 1.00   15.75 ? 2007 HOH G O   1 
HETATM 12191 O  O   . HOH ZA 6 .   ? 173.627 101.896 61.557 1.00   27.13 ? 2008 HOH G O   1 
HETATM 12192 O  O   . HOH ZA 6 .   ? 169.737 101.070 63.072 1.00   30.42 ? 2009 HOH G O   1 
HETATM 12193 O  O   . HOH ZA 6 .   ? 181.602 98.252  37.486 1.00   55.45 ? 2010 HOH G O   1 
HETATM 12194 O  O   . HOH ZA 6 .   ? 172.223 91.374  38.167 1.00   55.91 ? 2011 HOH G O   1 
HETATM 12195 O  O   . HOH ZA 6 .   ? 176.471 103.430 68.729 1.00   49.64 ? 2012 HOH G O   1 
HETATM 12196 O  O   . HOH ZA 6 .   ? 173.381 96.847  68.883 1.00   30.39 ? 2013 HOH G O   1 
HETATM 12197 O  O   . HOH ZA 6 .   ? 172.238 101.050 69.295 1.00   47.92 ? 2014 HOH G O   1 
HETATM 12198 O  O   . HOH ZA 6 .   ? 167.135 95.863  68.345 1.00   34.15 ? 2015 HOH G O   1 
HETATM 12199 O  O   . HOH ZA 6 .   ? 171.614 97.115  74.806 1.00   42.02 ? 2016 HOH G O   1 
HETATM 12200 O  O   . HOH ZA 6 .   ? 170.479 100.748 73.387 1.00   49.99 ? 2017 HOH G O   1 
HETATM 12201 O  O   . HOH ZA 6 .   ? 164.162 101.055 68.125 1.00   52.67 ? 2018 HOH G O   1 
HETATM 12202 O  O   . HOH ZA 6 .   ? 170.322 94.060  69.103 1.00   24.21 ? 2019 HOH G O   1 
HETATM 12203 O  O   . HOH ZA 6 .   ? 177.003 99.007  67.871 1.00   44.92 ? 2020 HOH G O   1 
HETATM 12204 O  O   . HOH ZA 6 .   ? 173.750 71.908  66.667 1.00   32.85 ? 2021 HOH G O   1 
HETATM 12205 O  O   . HOH ZA 6 .   ? 176.294 75.192  63.940 1.00   48.10 ? 2022 HOH G O   1 
HETATM 12206 O  O   . HOH ZA 6 .   ? 183.060 93.143  59.496 1.00   25.14 ? 2023 HOH G O   1 
HETATM 12207 O  O   . HOH ZA 6 .   ? 184.548 94.295  57.592 1.00   30.73 ? 2024 HOH G O   1 
HETATM 12208 O  O   . HOH ZA 6 .   ? 184.200 98.065  55.907 1.00   31.24 ? 2025 HOH G O   1 
HETATM 12209 O  O   . HOH ZA 6 .   ? 155.157 98.504  52.773 1.00   34.96 ? 2026 HOH G O   1 
HETATM 12210 O  O   . HOH ZA 6 .   ? 161.276 98.966  43.524 1.00   39.00 ? 2027 HOH G O   1 
HETATM 12211 O  O   . HOH ZA 6 .   ? 160.605 103.156 46.377 1.00   50.62 ? 2028 HOH G O   1 
HETATM 12212 O  O   . HOH ZA 6 .   ? 182.081 90.363  43.068 1.00   35.78 ? 2029 HOH G O   1 
HETATM 12213 O  O   . HOH ZA 6 .   ? 179.951 96.402  38.849 1.00   38.31 ? 2030 HOH G O   1 
HETATM 12214 O  O   . HOH ZA 6 .   ? 175.755 96.475  38.727 1.00   44.06 ? 2031 HOH G O   1 
HETATM 12215 O  O   . HOH ZA 6 .   ? 173.449 90.816  40.631 1.00   31.10 ? 2032 HOH G O   1 
HETATM 12216 O  O   . HOH ZA 6 .   ? 156.898 101.444 56.495 1.00   44.94 ? 2033 HOH G O   1 
HETATM 12217 O  O   . HOH ZA 6 .   ? 180.178 90.782  39.987 1.00   24.69 ? 2034 HOH G O   1 
HETATM 12218 O  O   . HOH ZA 6 .   ? 156.357 94.178  57.208 1.00   38.09 ? 2035 HOH G O   1 
HETATM 12219 O  O   . HOH ZA 6 .   ? 155.106 96.464  56.109 1.00   48.86 ? 2036 HOH G O   1 
HETATM 12220 O  O   . HOH ZA 6 .   ? 179.615 88.076  36.045 1.00   56.33 ? 2037 HOH G O   1 
HETATM 12221 O  O   . HOH ZA 6 .   ? 155.584 90.469  51.447 1.00   48.58 ? 2038 HOH G O   1 
HETATM 12222 O  O   . HOH ZA 6 .   ? 172.567 95.055  37.832 1.00   33.27 ? 2039 HOH G O   1 
HETATM 12223 O  O   . HOH ZA 6 .   ? 153.996 96.671  40.563 1.00   53.51 ? 2040 HOH G O   1 
HETATM 12224 O  O   . HOH ZA 6 .   ? 177.878 90.630  33.668 1.00   51.71 ? 2041 HOH G O   1 
HETATM 12225 O  O   . HOH ZA 6 .   ? 173.736 88.753  38.509 1.00   36.42 ? 2042 HOH G O   1 
HETATM 12226 O  O   . HOH ZA 6 .   ? 159.526 78.989  40.829 1.00   41.76 ? 2043 HOH G O   1 
HETATM 12227 O  O   . HOH ZA 6 .   ? 170.121 79.009  51.123 1.00   18.73 ? 2044 HOH G O   1 
HETATM 12228 O  O   . HOH ZA 6 .   ? 173.320 75.120  44.882 1.00   43.53 ? 2045 HOH G O   1 
HETATM 12229 O  O   . HOH ZA 6 .   ? 164.488 86.815  41.426 1.00   29.72 ? 2046 HOH G O   1 
HETATM 12230 O  O   . HOH ZA 6 .   ? 160.180 77.796  44.996 1.00   40.17 ? 2047 HOH G O   1 
HETATM 12231 O  O   . HOH ZA 6 .   ? 165.860 78.097  40.561 1.00   44.56 ? 2048 HOH G O   1 
HETATM 12232 O  O   . HOH ZA 6 .   ? 165.726 87.985  39.151 1.00   41.93 ? 2049 HOH G O   1 
HETATM 12233 O  O   . HOH ZA 6 .   ? 163.944 88.495  37.258 1.00   58.96 ? 2050 HOH G O   1 
HETATM 12234 O  O   . HOH ZA 6 .   ? 187.494 92.564  54.921 1.00   44.46 ? 2051 HOH G O   1 
HETATM 12235 O  O   . HOH ZA 6 .   ? 173.810 81.302  51.498 1.00   19.10 ? 2052 HOH G O   1 
HETATM 12236 O  O   . HOH ZA 6 .   ? 183.250 86.809  56.847 1.00   27.26 ? 2053 HOH G O   1 
HETATM 12237 O  O   . HOH ZA 6 .   ? 172.402 74.893  61.270 1.00   32.87 ? 2054 HOH G O   1 
HETATM 12238 O  O   . HOH ZA 6 .   ? 183.153 94.715  68.612 1.00   50.15 ? 2055 HOH G O   1 
HETATM 12239 O  O   . HOH ZA 6 .   ? 178.841 87.781  70.411 1.00   17.00 ? 2056 HOH G O   1 
HETATM 12240 O  O   . HOH ZA 6 .   ? 170.762 88.701  70.444 1.00   18.55 ? 2057 HOH G O   1 
HETATM 12241 O  O   . HOH ZA 6 .   ? 178.132 81.160  49.009 1.00   40.99 ? 2058 HOH G O   1 
HETATM 12242 O  O   . HOH ZA 6 .   ? 172.320 81.094  47.241 1.00   24.23 ? 2059 HOH G O   1 
HETATM 12243 O  O   . HOH ZA 6 .   ? 170.168 86.669  68.648 1.00   14.96 ? 2060 HOH G O   1 
HETATM 12244 O  O   . HOH ZA 6 .   ? 169.455 80.896  67.753 1.00   23.05 ? 2061 HOH G O   1 
HETATM 12245 O  O   . HOH ZA 6 .   ? 167.799 85.606  68.750 1.00   23.08 ? 2062 HOH G O   1 
HETATM 12246 O  O   . HOH ZA 6 .   ? 174.191 81.688  71.973 1.00   28.56 ? 2063 HOH G O   1 
HETATM 12247 O  O   . HOH ZA 6 .   ? 170.693 79.085  70.579 1.00   43.85 ? 2064 HOH G O   1 
HETATM 12248 O  O   . HOH ZA 6 .   ? 177.464 75.444  71.689 1.00   34.30 ? 2065 HOH G O   1 
HETATM 12249 O  O   . HOH ZA 6 .   ? 175.228 73.479  68.453 1.00   45.28 ? 2066 HOH G O   1 
HETATM 12250 O  O   . HOH ZA 6 .   ? 176.983 77.097  64.872 0.50   13.21 ? 2067 HOH G O   1 
HETATM 12251 O  O   . HOH ZA 6 .   ? 177.597 76.555  66.333 0.50   12.11 ? 2068 HOH G O   1 
HETATM 12252 O  O   . HOH ZA 6 .   ? 173.613 76.129  66.367 1.00   39.47 ? 2069 HOH G O   1 
HETATM 12253 O  O   . HOH ZA 6 .   ? 166.610 102.297 42.923 1.00   44.42 ? 2070 HOH G O   1 
HETATM 12254 O  O   . HOH ZA 6 .   ? 169.557 77.390  64.564 1.00   22.74 ? 2071 HOH G O   1 
HETATM 12255 O  O   . HOH ZA 6 .   ? 168.077 80.414  65.597 1.00   24.09 ? 2072 HOH G O   1 
HETATM 12256 O  O   . HOH ZA 6 .   ? 163.988 103.395 42.813 1.00   48.84 ? 2073 HOH G O   1 
HETATM 12257 O  O   . HOH ZA 6 .   ? 163.442 76.909  59.687 1.00   35.57 ? 2074 HOH G O   1 
HETATM 12258 O  O   . HOH ZA 6 .   ? 162.277 74.756  58.066 1.00   30.37 ? 2075 HOH G O   1 
HETATM 12259 O  O   . HOH ZA 6 .   ? 161.170 90.284  58.129 1.00   18.49 ? 2076 HOH G O   1 
HETATM 12260 O  O   . HOH ZA 6 .   ? 159.790 96.156  47.444 1.00   29.25 ? 2077 HOH G O   1 
HETATM 12261 O  O   . HOH ZA 6 .   ? 157.750 95.141  49.091 1.00   43.04 ? 2078 HOH G O   1 
HETATM 12262 O  O   . HOH ZA 6 .   ? 156.030 98.549  50.660 1.00   30.40 ? 2079 HOH G O   1 
HETATM 12263 O  O   . HOH ZA 6 .   ? 159.838 97.597  45.212 1.00   33.53 ? 2080 HOH G O   1 
HETATM 12264 O  O   . HOH ZA 6 .   ? 160.621 100.854 46.746 1.00   35.98 ? 2081 HOH G O   1 
HETATM 12265 O  O   . HOH ZA 6 .   ? 149.119 88.324  59.832 1.00   49.81 ? 2082 HOH G O   1 
HETATM 12266 O  O   . HOH ZA 6 .   ? 166.895 106.356 57.593 1.00   20.23 ? 2083 HOH G O   1 
HETATM 12267 O  O   . HOH ZA 6 .   ? 165.636 101.071 59.359 1.00   21.08 ? 2084 HOH G O   1 
HETATM 12268 O  O   . HOH ZA 6 .   ? 159.854 108.577 57.203 1.00   31.70 ? 2085 HOH G O   1 
HETATM 12269 O  O   . HOH ZA 6 .   ? 158.351 105.290 58.025 1.00   42.21 ? 2086 HOH G O   1 
HETATM 12270 O  O   . HOH ZA 6 .   ? 165.932 106.462 65.203 1.00   46.86 ? 2087 HOH G O   1 
HETATM 12271 O  O   . HOH ZA 6 .   ? 169.734 102.614 60.232 1.00   39.25 ? 2088 HOH G O   1 
HETATM 12272 O  O   . HOH ZA 6 .   ? 167.534 101.670 58.881 1.00   25.64 ? 2089 HOH G O   1 
HETATM 12273 O  O   . HOH ZA 6 .   ? 167.893 100.991 64.875 1.00   38.10 ? 2090 HOH G O   1 
HETATM 12274 O  O   . HOH ZA 6 .   ? 170.179 105.544 62.467 1.00   35.01 ? 2091 HOH G O   1 
HETATM 12275 O  O   . HOH ZA 6 .   ? 158.854 92.351  66.490 1.00   53.05 ? 2092 HOH G O   1 
HETATM 12276 O  O   . HOH ZA 6 .   ? 164.761 108.864 64.649 1.00   47.85 ? 2093 HOH G O   1 
HETATM 12277 O  O   . HOH ZA 6 .   ? 161.858 99.343  65.504 1.00   36.98 ? 2094 HOH G O   1 
HETATM 12278 O  O   . HOH ZA 6 .   ? 165.000 99.004  65.928 1.00   35.18 ? 2095 HOH G O   1 
HETATM 12279 O  O   . HOH ZA 6 .   ? 157.862 97.018  59.679 1.00   38.31 ? 2096 HOH G O   1 
HETATM 12280 O  O   . HOH ZA 6 .   ? 156.254 100.259 58.742 1.00   66.01 ? 2097 HOH G O   1 
HETATM 12281 O  O   . HOH ZA 6 .   ? 159.768 95.639  63.583 1.00   34.31 ? 2098 HOH G O   1 
HETATM 12282 O  O   . HOH ZA 6 .   ? 158.618 103.010 56.053 1.00   22.70 ? 2099 HOH G O   1 
HETATM 12283 O  O   . HOH ZA 6 .   ? 156.885 95.892  57.482 1.00   22.23 ? 2100 HOH G O   1 
HETATM 12284 O  O   . HOH ZA 6 .   ? 158.417 90.780  53.945 1.00   14.35 ? 2101 HOH G O   1 
HETATM 12285 O  O   . HOH ZA 6 .   ? 157.373 92.443  50.543 1.00   39.78 ? 2102 HOH G O   1 
HETATM 12286 O  O   . HOH ZA 6 .   ? 159.294 91.710  56.433 1.00   22.56 ? 2103 HOH G O   1 
HETATM 12287 O  O   . HOH ZA 6 .   ? 161.145 90.706  44.175 1.00   10.22 ? 2104 HOH G O   1 
HETATM 12288 O  O   . HOH ZA 6 .   ? 155.837 93.903  40.788 1.00   35.44 ? 2105 HOH G O   1 
HETATM 12289 O  O   . HOH ZA 6 .   ? 158.342 96.905  40.527 1.00   37.48 ? 2106 HOH G O   1 
HETATM 12290 O  O   . HOH ZA 6 .   ? 156.802 87.937  39.104 1.00   46.92 ? 2107 HOH G O   1 
HETATM 12291 O  O   . HOH ZA 6 .   ? 154.558 87.180  41.031 1.00   47.72 ? 2108 HOH G O   1 
HETATM 12292 O  O   . HOH ZA 6 .   ? 155.522 87.910  49.936 1.00   24.12 ? 2109 HOH G O   1 
HETATM 12293 O  O   . HOH ZA 6 .   ? 159.003 81.819  40.447 1.00   38.70 ? 2110 HOH G O   1 
HETATM 12294 O  O   . HOH ZA 6 .   ? 153.267 79.799  46.571 1.00   40.74 ? 2111 HOH G O   1 
HETATM 12295 O  O   . HOH ZA 6 .   ? 149.354 82.872  45.457 1.00   73.05 ? 2112 HOH G O   1 
HETATM 12296 O  O   . HOH ZA 6 .   ? 156.757 80.752  50.728 1.00   39.65 ? 2113 HOH G O   1 
HETATM 12297 O  O   . HOH ZA 6 .   ? 157.243 80.643  47.387 1.00   42.85 ? 2114 HOH G O   1 
HETATM 12298 O  O   . HOH ZA 6 .   ? 159.387 80.553  47.706 1.00   28.19 ? 2115 HOH G O   1 
HETATM 12299 O  O   . HOH ZA 6 .   ? 165.650 84.364  52.623 1.00   11.62 ? 2116 HOH G O   1 
HETATM 12300 O  O   . HOH ZA 6 .   ? 167.840 78.950  49.533 1.00   13.18 ? 2117 HOH G O   1 
HETATM 12301 O  O   . HOH ZA 6 .   ? 170.447 73.396  44.479 1.00   51.20 ? 2118 HOH G O   1 
HETATM 12302 O  O   . HOH ZA 6 .   ? 171.610 72.553  50.194 1.00   19.85 ? 2119 HOH G O   1 
HETATM 12303 O  O   . HOH ZA 6 .   ? 173.632 75.056  49.229 1.00   28.52 ? 2120 HOH G O   1 
HETATM 12304 O  O   . HOH ZA 6 .   ? 164.988 84.647  41.622 1.00   41.22 ? 2121 HOH G O   1 
HETATM 12305 O  O   . HOH ZA 6 .   ? 167.192 83.096  42.171 1.00   38.68 ? 2122 HOH G O   1 
HETATM 12306 O  O   . HOH ZA 6 .   ? 163.019 76.541  43.960 1.00   38.96 ? 2123 HOH G O   1 
HETATM 12307 O  O   . HOH ZA 6 .   ? 160.407 79.309  47.108 1.00   26.58 ? 2124 HOH G O   1 
HETATM 12308 O  O   . HOH ZA 6 .   ? 163.715 77.554  42.039 1.00   32.48 ? 2125 HOH G O   1 
HETATM 12309 O  O   . HOH ZA 6 .   ? 161.300 78.422  43.288 1.00   23.74 ? 2126 HOH G O   1 
HETATM 12310 O  O   . HOH ZA 6 .   ? 164.756 85.011  38.091 1.00   51.17 ? 2127 HOH G O   1 
HETATM 12311 O  O   . HOH ZA 6 .   ? 166.829 82.932  37.135 1.00   53.56 ? 2128 HOH G O   1 
HETATM 12312 O  O   . HOH ZA 6 .   ? 154.097 84.863  43.093 1.00   34.23 ? 2129 HOH G O   1 
HETATM 12313 O  O   . HOH ZA 6 .   ? 161.792 88.530  43.158 1.00   18.06 ? 2130 HOH G O   1 
HETATM 12314 O  O   . HOH ZA 6 .   ? 163.219 88.129  42.716 1.00   33.00 ? 2131 HOH G O   1 
HETATM 12315 O  O   . HOH ZA 6 .   ? 172.348 82.670  53.313 1.00   11.87 ? 2132 HOH G O   1 
HETATM 12316 O  O   . HOH ZA 6 .   ? 170.531 80.508  53.635 1.00   18.61 ? 2133 HOH G O   1 
HETATM 12317 O  O   . HOH ZA 6 .   ? 169.507 78.190  55.905 1.00   20.01 ? 2134 HOH G O   1 
HETATM 12318 O  O   . HOH ZA 6 .   ? 179.952 82.256  61.871 1.00   15.86 ? 2135 HOH G O   1 
HETATM 12319 O  O   . HOH ZA 6 .   ? 174.262 76.731  59.962 1.00   16.08 ? 2136 HOH G O   1 
HETATM 12320 O  O   . HOH ZA 6 .   ? 184.020 83.383  67.637 1.00   28.70 ? 2137 HOH G O   1 
HETATM 12321 O  O   . HOH ZA 6 .   ? 183.947 80.044  65.886 1.00   34.51 ? 2138 HOH G O   1 
HETATM 12322 O  O   . HOH ZA 6 .   ? 182.316 82.282  63.306 1.00   20.06 ? 2139 HOH G O   1 
HETATM 12323 O  O   . HOH ZA 6 .   ? 180.897 77.412  67.455 1.00   31.80 ? 2140 HOH G O   1 
HETATM 12324 O  O   . HOH ZA 6 .   ? 176.414 80.716  73.008 1.00   46.08 ? 2141 HOH G O   1 
HETATM 12325 O  O   . HOH ZA 6 .   ? 186.045 76.513  71.224 1.00   47.27 ? 2142 HOH G O   1 
HETATM 12326 O  O   . HOH ZA 6 .   ? 185.114 85.148  64.461 1.00   43.20 ? 2143 HOH G O   1 
HETATM 12327 O  O   . HOH ZA 6 .   ? 177.785 80.838  53.162 1.00   26.39 ? 2144 HOH G O   1 
HETATM 12328 O  O   . HOH ZA 6 .   ? 180.758 82.086  50.014 1.00   45.92 ? 2145 HOH G O   1 
HETATM 12329 O  O   . HOH ZA 6 .   ? 184.397 85.828  52.616 1.00   49.43 ? 2146 HOH G O   1 
HETATM 12330 O  O   . HOH ZA 6 .   ? 175.848 82.205  49.228 1.00   19.49 ? 2147 HOH G O   1 
HETATM 12331 O  O   . HOH ZA 6 .   ? 172.638 83.853  47.494 1.00   23.59 ? 2148 HOH G O   1 
HETATM 12332 O  O   . HOH ZA 6 .   ? 175.958 84.040  42.861 1.00   29.29 ? 2149 HOH G O   1 
HETATM 12333 O  O   . HOH ZA 6 .   ? 172.093 83.776  43.725 1.00   28.78 ? 2150 HOH G O   1 
HETATM 12334 O  O   . HOH ZA 6 .   ? 169.371 95.548  38.962 1.00   21.19 ? 2151 HOH G O   1 
HETATM 12335 O  O   . HOH ZA 6 .   ? 172.109 97.683  36.429 1.00   44.70 ? 2152 HOH G O   1 
HETATM 12336 O  O   . HOH ZA 6 .   ? 174.821 101.899 36.641 1.00   48.12 ? 2153 HOH G O   1 
HETATM 12337 O  O   . HOH ZA 6 .   ? 171.855 102.409 38.998 1.00   41.27 ? 2154 HOH G O   1 
HETATM 12338 O  O   . HOH ZA 6 .   ? 166.280 99.446  43.586 1.00   23.93 ? 2155 HOH G O   1 
HETATM 12339 O  O   . HOH ZA 6 .   ? 163.110 98.592  41.747 1.00   40.11 ? 2156 HOH G O   1 
HETATM 12340 O  O   . HOH ZA 6 .   ? 170.560 102.452 41.300 1.00   51.78 ? 2157 HOH G O   1 
HETATM 12341 O  O   . HOH ZA 6 .   ? 162.241 101.756 44.661 1.00   46.00 ? 2158 HOH G O   1 
HETATM 12342 O  O   . HOH ZA 6 .   ? 160.288 86.007  71.152 1.00   52.98 ? 2159 HOH G O   1 
HETATM 12343 O  O   . HOH ZA 6 .   ? 159.150 80.204  63.857 1.00   38.08 ? 2160 HOH G O   1 
HETATM 12344 O  O   . HOH ZA 6 .   ? 157.821 85.498  65.411 1.00   42.76 ? 2161 HOH G O   1 
HETATM 12345 O  O   . HOH ZA 6 .   ? 161.802 80.390  62.598 1.00   12.83 ? 2162 HOH G O   1 
HETATM 12346 O  O   . HOH ZA 6 .   ? 165.478 77.224  58.792 1.00   30.99 ? 2163 HOH G O   1 
HETATM 12347 O  O   . HOH ZA 6 .   ? 163.227 75.523  55.937 1.00   24.45 ? 2164 HOH G O   1 
HETATM 12348 O  O   . HOH ZA 6 .   ? 157.920 76.811  48.916 1.00   17.97 ? 2165 HOH G O   1 
HETATM 12349 O  O   . HOH ZA 6 .   ? 155.488 77.276  52.889 1.00   8.84  ? 2166 HOH G O   1 
HETATM 12350 O  O   . HOH ZA 6 .   ? 151.200 82.629  59.595 1.00   14.43 ? 2167 HOH G O   1 
HETATM 12351 O  O   . HOH ZA 6 .   ? 152.229 83.102  62.172 1.00   14.89 ? 2168 HOH G O   1 
HETATM 12352 O  O   . HOH ZA 6 .   ? 154.376 81.822  63.139 1.00   28.61 ? 2169 HOH G O   1 
HETATM 12353 O  O   . HOH ZA 6 .   ? 151.351 86.379  58.750 1.00   34.78 ? 2170 HOH G O   1 
HETATM 12354 O  O   . HOH ZA 6 .   ? 158.295 86.229  61.812 1.00   24.80 ? 2171 HOH G O   1 
HETATM 12355 O  O   . HOH ZA 6 .   ? 151.701 89.467  51.683 1.00   49.83 ? 2172 HOH G O   1 
HETATM 12356 O  O   . HOH ZA 6 .   ? 156.851 84.624  62.912 1.00   40.26 ? 2173 HOH G O   1 
HETATM 12357 O  O   . HOH ZA 6 .   ? 160.169 89.018  60.290 1.00   19.00 ? 2174 HOH G O   1 
HETATM 12358 O  O   . HOH ZA 6 .   ? 158.144 89.640  64.658 1.00   40.70 ? 2175 HOH G O   1 
HETATM 12359 O  O   . HOH ZA 6 .   ? 162.010 89.791  70.659 1.00   57.05 ? 2176 HOH G O   1 
HETATM 12360 O  O   . HOH ZA 6 .   ? 160.193 93.901  64.661 0.40   14.88 ? 2177 HOH G O   1 
HETATM 12361 O  O   . HOH ZA 6 .   ? 161.282 94.041  65.244 0.60   10.75 ? 2178 HOH G O   1 
HETATM 12362 O  O   . HOH ZA 6 .   ? 165.413 96.677  66.936 1.00   33.11 ? 2179 HOH G O   1 
HETATM 12363 O  O   . HOH ZA 6 .   ? 158.171 95.066  61.901 1.00   36.43 ? 2180 HOH G O   1 
HETATM 12364 O  O   . HOH ZA 6 .   ? 157.060 92.366  57.655 1.00   33.27 ? 2181 HOH G O   1 
HETATM 12365 O  O   . HOH ZA 6 .   ? 171.410 101.805 62.397 1.00   41.78 ? 2182 HOH G O   1 
HETATM 12366 O  O   . HOH ZA 6 .   ? 172.184 103.225 59.000 1.00   20.51 ? 2183 HOH G O   1 
HETATM 12367 O  O   . HOH ZA 6 .   ? 183.915 101.857 44.506 1.00   42.92 ? 2184 HOH G O   1 
HETATM 12368 O  O   . HOH ZA 6 .   ? 185.815 101.456 51.086 1.00   39.17 ? 2185 HOH G O   1 
HETATM 12369 O  O   . HOH ZA 6 .   ? 167.423 77.614  65.312 1.00   41.73 ? 2186 HOH G O   1 
HETATM 12370 O  O   . HOH ZA 6 .   ? 167.246 76.625  63.156 1.00   40.52 ? 2187 HOH G O   1 
HETATM 12371 O  O   . HOH AB 6 .   ? 183.940 44.850  45.077 1.00   27.60 ? 2001 HOH H O   1 
HETATM 12372 O  O   . HOH AB 6 .   ? 180.260 49.038  39.149 1.00   39.58 ? 2002 HOH H O   1 
HETATM 12373 O  O   . HOH AB 6 .   ? 182.274 51.593  39.725 1.00   45.32 ? 2003 HOH H O   1 
HETATM 12374 O  O   . HOH AB 6 .   ? 185.357 47.720  39.309 1.00   52.41 ? 2004 HOH H O   1 
HETATM 12375 O  O   . HOH AB 6 .   ? 184.465 44.950  40.542 1.00   51.93 ? 2005 HOH H O   1 
HETATM 12376 O  O   . HOH AB 6 .   ? 178.535 44.114  41.059 1.00   53.12 ? 2006 HOH H O   1 
HETATM 12377 O  O   . HOH AB 6 .   ? 182.756 42.750  44.157 1.00   47.01 ? 2007 HOH H O   1 
HETATM 12378 O  O   . HOH AB 6 .   ? 174.363 42.231  45.582 1.00   49.27 ? 2008 HOH H O   1 
HETATM 12379 O  O   . HOH AB 6 .   ? 179.551 40.069  47.281 1.00   44.61 ? 2009 HOH H O   1 
HETATM 12380 O  O   . HOH AB 6 .   ? 179.889 45.863  52.141 1.00   19.16 ? 2010 HOH H O   1 
HETATM 12381 O  O   . HOH AB 6 .   ? 179.437 48.474  65.414 1.00   43.62 ? 2011 HOH H O   1 
HETATM 12382 O  O   . HOH AB 6 .   ? 181.848 60.802  70.619 1.00   25.56 ? 2012 HOH H O   1 
HETATM 12383 O  O   . HOH AB 6 .   ? 187.228 50.581  57.414 1.00   13.39 ? 2013 HOH H O   1 
HETATM 12384 O  O   . HOH AB 6 .   ? 188.147 52.035  61.446 1.00   29.21 ? 2014 HOH H O   1 
HETATM 12385 O  O   . HOH AB 6 .   ? 178.764 43.639  58.384 1.00   42.55 ? 2015 HOH H O   1 
HETATM 12386 O  O   . HOH AB 6 .   ? 189.871 57.615  64.842 1.00   46.87 ? 2016 HOH H O   1 
HETATM 12387 O  O   . HOH AB 6 .   ? 181.922 48.557  64.631 1.00   36.89 ? 2017 HOH H O   1 
HETATM 12388 O  O   . HOH AB 6 .   ? 179.501 58.110  39.077 1.00   41.39 ? 2018 HOH H O   1 
HETATM 12389 O  O   . HOH AB 6 .   ? 184.368 54.716  68.655 1.00   22.81 ? 2019 HOH H O   1 
HETATM 12390 O  O   . HOH AB 6 .   ? 186.460 54.558  72.139 1.00   32.05 ? 2020 HOH H O   1 
HETATM 12391 O  O   . HOH AB 6 .   ? 181.237 45.693  32.720 1.00   48.97 ? 2021 HOH H O   1 
HETATM 12392 O  O   . HOH AB 6 .   ? 186.150 60.545  68.111 1.00   28.39 ? 2022 HOH H O   1 
HETATM 12393 O  O   . HOH AB 6 .   ? 188.072 55.505  74.373 1.00   42.74 ? 2023 HOH H O   1 
HETATM 12394 O  O   . HOH AB 6 .   ? 183.131 58.613  69.343 1.00   23.51 ? 2024 HOH H O   1 
HETATM 12395 O  O   . HOH AB 6 .   ? 179.784 51.958  71.185 1.00   28.99 ? 2025 HOH H O   1 
HETATM 12396 O  O   . HOH AB 6 .   ? 170.297 48.567  66.398 1.00   50.63 ? 2026 HOH H O   1 
HETATM 12397 O  O   . HOH AB 6 .   ? 171.030 45.653  66.433 1.00   51.39 ? 2027 HOH H O   1 
HETATM 12398 O  O   . HOH AB 6 .   ? 181.930 51.845  72.602 1.00   40.96 ? 2028 HOH H O   1 
HETATM 12399 O  O   . HOH AB 6 .   ? 178.105 62.592  73.102 1.00   51.45 ? 2029 HOH H O   1 
HETATM 12400 O  O   . HOH AB 6 .   ? 175.917 47.640  59.557 1.00   31.52 ? 2030 HOH H O   1 
HETATM 12401 O  O   . HOH AB 6 .   ? 177.238 48.043  63.327 1.00   41.75 ? 2031 HOH H O   1 
HETATM 12402 O  O   . HOH AB 6 .   ? 179.541 44.462  56.075 1.00   29.11 ? 2032 HOH H O   1 
HETATM 12403 O  O   . HOH AB 6 .   ? 176.366 45.720  57.811 1.00   37.50 ? 2033 HOH H O   1 
HETATM 12404 O  O   . HOH AB 6 .   ? 190.679 65.652  45.042 1.00   36.23 ? 2034 HOH H O   1 
HETATM 12405 O  O   . HOH AB 6 .   ? 174.046 50.055  43.007 1.00   34.88 ? 2035 HOH H O   1 
HETATM 12406 O  O   . HOH AB 6 .   ? 200.058 53.785  65.048 1.00   42.51 ? 2036 HOH H O   1 
HETATM 12407 O  O   . HOH AB 6 .   ? 198.111 64.655  60.444 1.00   45.90 ? 2037 HOH H O   1 
HETATM 12408 O  O   . HOH AB 6 .   ? 170.540 47.003  49.941 1.00   53.25 ? 2038 HOH H O   1 
HETATM 12409 O  O   . HOH AB 6 .   ? 178.014 57.065  40.700 1.00   30.85 ? 2039 HOH H O   1 
HETATM 12410 O  O   . HOH AB 6 .   ? 175.115 51.320  40.007 1.00   25.66 ? 2040 HOH H O   1 
HETATM 12411 O  O   . HOH AB 6 .   ? 178.749 44.349  38.569 1.00   60.43 ? 2041 HOH H O   1 
HETATM 12412 O  O   . HOH AB 6 .   ? 180.070 46.355  37.362 1.00   56.44 ? 2042 HOH H O   1 
HETATM 12413 O  O   . HOH AB 6 .   ? 187.365 72.780  53.833 1.00   34.13 ? 2043 HOH H O   1 
HETATM 12414 O  O   . HOH AB 6 .   ? 182.272 56.328  37.871 1.00   28.05 ? 2044 HOH H O   1 
HETATM 12415 O  O   . HOH AB 6 .   ? 174.835 56.950  33.058 1.00   42.26 ? 2045 HOH H O   1 
HETATM 12416 O  O   A HOH AB 6 .   ? 179.675 67.144  41.395 0.50   17.47 ? 2046 HOH H O   1 
HETATM 12417 O  O   B HOH AB 6 .   ? 171.549 73.843  39.356 0.50   21.21 ? 2046 HOH H O   1 
HETATM 12418 O  O   . HOH AB 6 .   ? 175.858 57.851  38.943 1.00   37.95 ? 2047 HOH H O   1 
HETATM 12419 O  O   . HOH AB 6 .   ? 171.549 73.843  39.356 1.00   31.56 ? 2048 HOH H O   1 
HETATM 12420 O  O   . HOH AB 6 .   ? 170.678 52.478  50.264 1.00   35.39 ? 2049 HOH H O   1 
HETATM 12421 O  O   . HOH AB 6 .   ? 173.780 44.265  54.738 1.00   44.66 ? 2050 HOH H O   1 
HETATM 12422 O  O   . HOH AB 6 .   ? 170.244 50.775  57.175 1.00   25.41 ? 2051 HOH H O   1 
HETATM 12423 O  O   . HOH AB 6 .   ? 170.563 49.585  59.480 1.00   36.53 ? 2052 HOH H O   1 
HETATM 12424 O  O   . HOH AB 6 .   ? 170.508 48.593  63.704 1.00   47.87 ? 2053 HOH H O   1 
HETATM 12425 O  O   . HOH AB 6 .   ? 173.577 53.509  70.957 1.00   34.85 ? 2054 HOH H O   1 
HETATM 12426 O  O   . HOH AB 6 .   ? 178.080 60.337  70.660 1.00   16.74 ? 2055 HOH H O   1 
HETATM 12427 O  O   . HOH AB 6 .   ? 171.293 58.844  71.952 1.00   25.21 ? 2056 HOH H O   1 
HETATM 12428 O  O   . HOH AB 6 .   ? 170.381 63.041  47.418 1.00   33.96 ? 2057 HOH H O   1 
HETATM 12429 O  O   . HOH AB 6 .   ? 176.706 61.941  69.077 1.00   20.63 ? 2058 HOH H O   1 
HETATM 12430 O  O   . HOH AB 6 .   ? 176.958 64.696  69.060 1.00   19.84 ? 2059 HOH H O   1 
HETATM 12431 O  O   . HOH AB 6 .   ? 174.416 66.519  69.980 1.00   52.00 ? 2060 HOH H O   1 
HETATM 12432 O  O   . HOH AB 6 .   ? 170.392 61.228  72.291 1.00   34.72 ? 2061 HOH H O   1 
HETATM 12433 O  O   . HOH AB 6 .   ? 169.885 65.308  70.566 1.00   37.50 ? 2062 HOH H O   1 
HETATM 12434 O  O   . HOH AB 6 .   ? 168.857 67.362  64.843 1.00   21.33 ? 2063 HOH H O   1 
HETATM 12435 O  O   . HOH AB 6 .   ? 172.203 67.265  65.821 1.00   33.92 ? 2064 HOH H O   1 
HETATM 12436 O  O   . HOH AB 6 .   ? 182.954 66.900  57.092 1.00   7.29  ? 2065 HOH H O   1 
HETATM 12437 O  O   . HOH AB 6 .   ? 182.140 73.683  65.473 1.00   44.76 ? 2066 HOH H O   1 
HETATM 12438 O  O   . HOH AB 6 .   ? 181.073 74.653  63.584 1.00   40.84 ? 2067 HOH H O   1 
HETATM 12439 O  O   . HOH AB 6 .   ? 184.083 68.485  58.019 1.00   15.89 ? 2068 HOH H O   1 
HETATM 12440 O  O   . HOH AB 6 .   ? 172.431 79.677  49.735 1.00   19.34 ? 2069 HOH H O   1 
HETATM 12441 O  O   . HOH AB 6 .   ? 189.613 66.642  47.194 1.00   24.78 ? 2070 HOH H O   1 
HETATM 12442 O  O   . HOH AB 6 .   ? 193.532 68.877  50.402 1.00   29.84 ? 2071 HOH H O   1 
HETATM 12443 O  O   . HOH AB 6 .   ? 193.298 63.536  46.667 1.00   25.77 ? 2072 HOH H O   1 
HETATM 12444 O  O   . HOH AB 6 .   ? 183.590 75.956  63.944 1.00   48.53 ? 2073 HOH H O   1 
HETATM 12445 O  O   . HOH AB 6 .   ? 195.367 55.559  57.487 1.00   14.53 ? 2074 HOH H O   1 
HETATM 12446 O  O   . HOH AB 6 .   ? 191.175 59.409  59.538 1.00   22.61 ? 2075 HOH H O   1 
HETATM 12447 O  O   . HOH AB 6 .   ? 200.723 60.678  56.813 1.00   32.50 ? 2076 HOH H O   1 
HETATM 12448 O  O   . HOH AB 6 .   ? 190.653 54.769  59.992 1.00   31.78 ? 2077 HOH H O   1 
HETATM 12449 O  O   . HOH AB 6 .   ? 190.705 57.366  58.632 1.00   26.98 ? 2078 HOH H O   1 
HETATM 12450 O  O   . HOH AB 6 .   ? 187.871 73.398  56.137 1.00   42.58 ? 2079 HOH H O   1 
HETATM 12451 O  O   . HOH AB 6 .   ? 198.487 56.271  64.453 1.00   52.53 ? 2080 HOH H O   1 
HETATM 12452 O  O   . HOH AB 6 .   ? 199.844 62.399  61.164 1.00   33.27 ? 2081 HOH H O   1 
HETATM 12453 O  O   . HOH AB 6 .   ? 190.866 63.102  65.619 1.00   47.79 ? 2082 HOH H O   1 
HETATM 12454 O  O   . HOH AB 6 .   ? 189.858 60.622  65.757 1.00   29.55 ? 2083 HOH H O   1 
HETATM 12455 O  O   . HOH AB 6 .   ? 191.527 68.275  59.212 1.00   31.77 ? 2084 HOH H O   1 
HETATM 12456 O  O   . HOH AB 6 .   ? 189.181 66.950  63.525 1.00   40.47 ? 2085 HOH H O   1 
HETATM 12457 O  O   . HOH AB 6 .   ? 196.365 64.536  55.741 1.00   25.58 ? 2086 HOH H O   1 
HETATM 12458 O  O   . HOH AB 6 .   ? 190.661 69.433  57.285 1.00   24.41 ? 2087 HOH H O   1 
HETATM 12459 O  O   . HOH AB 6 .   ? 185.713 70.561  53.799 1.00   15.73 ? 2088 HOH H O   1 
HETATM 12460 O  O   . HOH AB 6 .   ? 184.114 68.025  44.215 1.00   14.80 ? 2089 HOH H O   1 
HETATM 12461 O  O   . HOH AB 6 .   ? 189.538 71.125  40.542 1.00   39.33 ? 2090 HOH H O   1 
HETATM 12462 O  O   . HOH AB 6 .   ? 191.175 67.457  41.146 1.00   37.58 ? 2091 HOH H O   1 
HETATM 12463 O  O   . HOH AB 6 .   ? 183.542 73.023  38.884 1.00   47.50 ? 2092 HOH H O   1 
HETATM 12464 O  O   . HOH AB 6 .   ? 184.632 74.370  49.940 1.00   29.42 ? 2093 HOH H O   1 
HETATM 12465 O  O   . HOH AB 6 .   ? 177.735 73.955  40.690 1.00   40.13 ? 2094 HOH H O   1 
HETATM 12466 O  O   . HOH AB 6 .   ? 178.892 69.146  40.292 1.00   47.35 ? 2095 HOH H O   1 
HETATM 12467 O  O   . HOH AB 6 .   ? 181.531 84.239  48.393 1.00   54.69 ? 2096 HOH H O   1 
HETATM 12468 O  O   . HOH AB 6 .   ? 175.901 74.519  47.712 1.00   19.98 ? 2097 HOH H O   1 
HETATM 12469 O  O   . HOH AB 6 .   ? 178.035 76.683  50.648 1.00   21.60 ? 2098 HOH H O   1 
HETATM 12470 O  O   . HOH AB 6 .   ? 176.523 67.333  52.643 1.00   10.86 ? 2099 HOH H O   1 
HETATM 12471 O  O   . HOH AB 6 .   ? 170.680 67.941  49.735 1.00   11.75 ? 2100 HOH H O   1 
HETATM 12472 O  O   . HOH AB 6 .   ? 172.718 64.504  43.029 1.00   46.21 ? 2101 HOH H O   1 
HETATM 12473 O  O   . HOH AB 6 .   ? 175.133 67.063  42.115 1.00   36.13 ? 2102 HOH H O   1 
HETATM 12474 O  O   . HOH AB 6 .   ? 171.276 72.661  42.221 1.00   40.94 ? 2103 HOH H O   1 
HETATM 12475 O  O   . HOH AB 6 .   ? 173.430 73.823  43.095 1.00   33.88 ? 2104 HOH H O   1 
HETATM 12476 O  O   . HOH AB 6 .   ? 182.376 76.979  43.152 1.00   36.73 ? 2105 HOH H O   1 
HETATM 12477 O  O   . HOH AB 6 .   ? 181.472 68.157  42.920 1.00   15.97 ? 2106 HOH H O   1 
HETATM 12478 O  O   . HOH AB 6 .   ? 171.918 62.269  53.625 1.00   17.29 ? 2107 HOH H O   1 
HETATM 12479 O  O   . HOH AB 6 .   ? 166.884 53.737  63.430 1.00   28.27 ? 2108 HOH H O   1 
HETATM 12480 O  O   . HOH AB 6 .   ? 163.892 53.680  65.679 1.00   44.32 ? 2109 HOH H O   1 
HETATM 12481 O  O   . HOH AB 6 .   ? 167.188 51.489  67.077 1.00   33.62 ? 2110 HOH H O   1 
HETATM 12482 O  O   . HOH AB 6 .   ? 163.212 57.391  67.524 1.00   33.72 ? 2111 HOH H O   1 
HETATM 12483 O  O   . HOH AB 6 .   ? 168.076 49.847  64.688 1.00   38.69 ? 2112 HOH H O   1 
HETATM 12484 O  O   . HOH AB 6 .   ? 166.403 54.145  51.076 1.00   49.21 ? 2113 HOH H O   1 
HETATM 12485 O  O   . HOH AB 6 .   ? 169.671 59.202  49.302 1.00   19.24 ? 2114 HOH H O   1 
HETATM 12486 O  O   . HOH AB 6 .   ? 172.526 61.239  47.649 1.00   19.29 ? 2115 HOH H O   1 
HETATM 12487 O  O   . HOH AB 6 .   ? 168.831 59.500  46.859 1.00   33.08 ? 2116 HOH H O   1 
HETATM 12488 O  O   . HOH AB 6 .   ? 171.153 58.309  43.227 1.00   31.18 ? 2117 HOH H O   1 
HETATM 12489 O  O   . HOH AB 6 .   ? 172.857 61.847  43.936 1.00   26.69 ? 2118 HOH H O   1 
HETATM 12490 O  O   . HOH AB 6 .   ? 179.733 60.354  39.208 1.00   45.43 ? 2119 HOH H O   1 
HETATM 12491 O  O   . HOH AB 6 .   ? 173.058 58.175  37.931 1.00   45.20 ? 2120 HOH H O   1 
HETATM 12492 O  O   . HOH AB 6 .   ? 187.532 50.551  41.427 1.00   51.68 ? 2121 HOH H O   1 
HETATM 12493 O  O   . HOH AB 6 .   ? 184.100 58.554  39.067 1.00   18.19 ? 2122 HOH H O   1 
HETATM 12494 O  O   . HOH AB 6 .   ? 189.016 53.451  38.164 1.00   27.76 ? 2123 HOH H O   1 
HETATM 12495 O  O   . HOH AB 6 .   ? 190.409 58.167  38.003 1.00   39.62 ? 2124 HOH H O   1 
HETATM 12496 O  O   . HOH AB 6 .   ? 190.658 57.154  41.582 1.00   39.79 ? 2125 HOH H O   1 
HETATM 12497 O  O   . HOH AB 6 .   ? 189.146 59.338  43.402 1.00   24.14 ? 2126 HOH H O   1 
HETATM 12498 O  O   . HOH AB 6 .   ? 179.526 65.226  39.195 1.00   41.12 ? 2127 HOH H O   1 
HETATM 12499 O  O   . HOH AB 6 .   ? 193.543 62.015  44.639 1.00   34.16 ? 2128 HOH H O   1 
HETATM 12500 O  O   . HOH AB 6 .   ? 191.170 63.768  43.522 1.00   43.28 ? 2129 HOH H O   1 
HETATM 12501 O  O   . HOH AB 6 .   ? 183.291 69.788  60.391 1.00   17.11 ? 2130 HOH H O   1 
HETATM 12502 O  O   . HOH AB 6 .   ? 179.772 72.116  69.580 1.00   42.62 ? 2131 HOH H O   1 
HETATM 12503 O  O   . HOH AB 6 .   ? 179.384 73.781  64.704 1.00   45.67 ? 2132 HOH H O   1 
HETATM 12504 O  O   . HOH AB 6 .   ? 173.412 71.687  64.544 1.00   31.01 ? 2133 HOH H O   1 
HETATM 12505 O  O   . HOH AB 6 .   ? 173.100 69.957  65.317 1.00   33.62 ? 2134 HOH H O   1 
HETATM 12506 O  O   . HOH AB 6 .   ? 175.124 72.775  62.727 1.00   19.94 ? 2135 HOH H O   1 
HETATM 12507 O  O   . HOH AB 6 .   ? 170.499 70.943  59.147 1.00   28.90 ? 2136 HOH H O   1 
HETATM 12508 O  O   . HOH AB 6 .   ? 174.141 77.714  49.102 1.00   19.17 ? 2137 HOH H O   1 
HETATM 12509 O  O   . HOH AB 6 .   ? 175.566 79.628  52.838 1.00   10.61 ? 2138 HOH H O   1 
HETATM 12510 O  O   . HOH AB 6 .   ? 182.110 79.751  62.133 1.00   28.49 ? 2139 HOH H O   1 
HETATM 12511 O  O   . HOH AB 6 .   ? 180.001 78.236  63.249 1.00   31.70 ? 2140 HOH H O   1 
HETATM 12512 O  O   . HOH AB 6 .   ? 182.340 80.824  59.592 1.00   19.37 ? 2141 HOH H O   1 
HETATM 12513 O  O   . HOH AB 6 .   ? 185.452 83.486  57.608 1.00   35.24 ? 2142 HOH H O   1 
HETATM 12514 O  O   . HOH AB 6 .   ? 184.240 77.634  62.105 1.00   41.48 ? 2143 HOH H O   1 
HETATM 12515 O  O   . HOH AB 6 .   ? 185.649 78.641  58.429 1.00   37.13 ? 2144 HOH H O   1 
HETATM 12516 O  O   . HOH AB 6 .   ? 181.894 72.954  61.894 1.00   31.36 ? 2145 HOH H O   1 
HETATM 12517 O  O   . HOH AB 6 .   ? 184.816 71.304  64.931 1.00   46.20 ? 2146 HOH H O   1 
HETATM 12518 O  O   . HOH AB 6 .   ? 187.402 66.661  65.193 1.00   19.60 ? 2147 HOH H O   1 
HETATM 12519 O  O   . HOH AB 6 .   ? 189.765 68.596  62.021 1.00   30.25 ? 2148 HOH H O   1 
HETATM 12520 O  O   . HOH AB 6 .   ? 186.224 69.367  56.474 1.00   19.07 ? 2149 HOH H O   1 
HETATM 12521 O  O   . HOH AB 6 .   ? 188.148 70.843  57.546 1.00   32.85 ? 2150 HOH H O   1 
HETATM 12522 O  O   . HOH AB 6 .   ? 189.229 54.924  62.526 1.00   28.59 ? 2151 HOH H O   1 
HETATM 12523 O  O   . HOH AB 6 .   ? 189.823 52.269  58.839 1.00   20.91 ? 2152 HOH H O   1 
HETATM 12524 O  O   . HOH BB 6 .   ? 165.788 136.812 41.916 1.00   33.42 ? 2001 HOH I O   1 
HETATM 12525 O  O   . HOH BB 6 .   ? 163.094 132.476 37.803 1.00   51.83 ? 2002 HOH I O   1 
HETATM 12526 O  O   . HOH BB 6 .   ? 166.717 131.463 40.793 1.00   58.95 ? 2003 HOH I O   1 
HETATM 12527 O  O   . HOH BB 6 .   ? 163.063 132.501 48.448 1.00   27.46 ? 2004 HOH I O   1 
HETATM 12528 O  O   . HOH BB 6 .   ? 158.033 144.214 64.393 1.00   47.82 ? 2005 HOH I O   1 
HETATM 12529 O  O   . HOH BB 6 .   ? 151.306 141.524 68.890 1.00   53.36 ? 2006 HOH I O   1 
HETATM 12530 O  O   . HOH BB 6 .   ? 151.493 138.096 68.533 1.00   31.66 ? 2007 HOH I O   1 
HETATM 12531 O  O   . HOH BB 6 .   ? 158.121 128.653 61.283 1.00   49.16 ? 2008 HOH I O   1 
HETATM 12532 O  O   . HOH BB 6 .   ? 162.854 139.962 55.265 1.00   16.14 ? 2009 HOH I O   1 
HETATM 12533 O  O   . HOH BB 6 .   ? 161.943 140.889 59.494 1.00   34.92 ? 2010 HOH I O   1 
HETATM 12534 O  O   . HOH BB 6 .   ? 161.790 135.385 62.710 1.00   46.54 ? 2011 HOH I O   1 
HETATM 12535 O  O   . HOH BB 6 .   ? 159.708 142.879 61.505 1.00   39.15 ? 2012 HOH I O   1 
HETATM 12536 O  O   . HOH BB 6 .   ? 154.820 130.064 37.413 1.00   40.43 ? 2013 HOH I O   1 
HETATM 12537 O  O   . HOH BB 6 .   ? 158.013 137.338 66.280 1.00   27.10 ? 2014 HOH I O   1 
HETATM 12538 O  O   . HOH BB 6 .   ? 159.161 138.738 69.250 1.00   38.43 ? 2015 HOH I O   1 
HETATM 12539 O  O   . HOH BB 6 .   ? 153.584 141.745 66.957 1.00   40.24 ? 2016 HOH I O   1 
HETATM 12540 O  O   . HOH BB 6 .   ? 153.741 138.099 67.216 1.00   23.48 ? 2017 HOH I O   1 
HETATM 12541 O  O   . HOH BB 6 .   ? 151.011 127.137 44.103 1.00   47.63 ? 2018 HOH I O   1 
HETATM 12542 O  O   . HOH BB 6 .   ? 163.064 131.608 66.976 1.00   49.94 ? 2019 HOH I O   1 
HETATM 12543 O  O   . HOH BB 6 .   ? 161.530 130.762 69.184 1.00   59.17 ? 2020 HOH I O   1 
HETATM 12544 O  O   . HOH BB 6 .   ? 160.659 130.992 61.965 1.00   47.13 ? 2021 HOH I O   1 
HETATM 12545 O  O   . HOH BB 6 .   ? 161.656 133.255 61.123 1.00   41.31 ? 2022 HOH I O   1 
HETATM 12546 O  O   . HOH BB 6 .   ? 145.168 129.762 70.295 1.00   39.23 ? 2023 HOH I O   1 
HETATM 12547 O  O   . HOH BB 6 .   ? 159.617 129.229 59.139 1.00   36.88 ? 2024 HOH I O   1 
HETATM 12548 O  O   . HOH BB 6 .   ? 159.504 128.488 55.254 1.00   27.64 ? 2025 HOH I O   1 
HETATM 12549 O  O   . HOH BB 6 .   ? 161.459 128.175 53.472 1.00   23.63 ? 2026 HOH I O   1 
HETATM 12550 O  O   . HOH BB 6 .   ? 164.001 130.501 51.967 1.00   37.52 ? 2027 HOH I O   1 
HETATM 12551 O  O   . HOH BB 6 .   ? 162.066 131.797 45.981 1.00   40.62 ? 2028 HOH I O   1 
HETATM 12552 O  O   . HOH BB 6 .   ? 151.590 152.848 45.263 1.00   47.84 ? 2029 HOH I O   1 
HETATM 12553 O  O   . HOH BB 6 .   ? 156.232 131.581 39.074 1.00   40.69 ? 2030 HOH I O   1 
HETATM 12554 O  O   . HOH BB 6 .   ? 152.846 155.012 57.811 1.00   49.24 ? 2031 HOH I O   1 
HETATM 12555 O  O   . HOH BB 6 .   ? 155.339 133.595 36.530 1.00   25.02 ? 2032 HOH I O   1 
HETATM 12556 O  O   . HOH BB 6 .   ? 154.580 131.151 35.241 1.00   40.41 ? 2033 HOH I O   1 
HETATM 12557 O  O   . HOH BB 6 .   ? 158.691 136.122 30.852 1.00   34.51 ? 2034 HOH I O   1 
HETATM 12558 O  O   . HOH BB 6 .   ? 153.078 140.955 36.585 1.00   44.52 ? 2035 HOH I O   1 
HETATM 12559 O  O   . HOH BB 6 .   ? 156.016 136.824 29.368 1.00   38.75 ? 2036 HOH I O   1 
HETATM 12560 O  O   . HOH BB 6 .   ? 144.995 145.103 40.727 1.00   36.02 ? 2037 HOH I O   1 
HETATM 12561 O  O   . HOH BB 6 .   ? 140.492 133.867 48.393 1.00   19.94 ? 2038 HOH I O   1 
HETATM 12562 O  O   . HOH BB 6 .   ? 133.719 143.566 43.964 1.00   48.05 ? 2039 HOH I O   1 
HETATM 12563 O  O   . HOH BB 6 .   ? 135.158 144.427 39.677 1.00   44.65 ? 2040 HOH I O   1 
HETATM 12564 O  O   . HOH BB 6 .   ? 156.979 125.453 45.379 1.00   42.77 ? 2041 HOH I O   1 
HETATM 12565 O  O   . HOH BB 6 .   ? 152.705 128.077 46.249 1.00   41.44 ? 2042 HOH I O   1 
HETATM 12566 O  O   . HOH BB 6 .   ? 160.984 126.472 49.432 1.00   45.51 ? 2043 HOH I O   1 
HETATM 12567 O  O   . HOH BB 6 .   ? 144.408 131.766 48.191 1.00   21.67 ? 2044 HOH I O   1 
HETATM 12568 O  O   . HOH BB 6 .   ? 136.877 133.451 53.943 1.00   43.90 ? 2045 HOH I O   1 
HETATM 12569 O  O   . HOH BB 6 .   ? 137.336 131.041 54.087 1.00   39.35 ? 2046 HOH I O   1 
HETATM 12570 O  O   . HOH BB 6 .   ? 153.990 125.599 52.253 1.00   30.89 ? 2047 HOH I O   1 
HETATM 12571 O  O   . HOH BB 6 .   ? 155.616 125.291 54.481 1.00   37.11 ? 2048 HOH I O   1 
HETATM 12572 O  O   . HOH BB 6 .   ? 138.574 127.354 57.639 1.00   31.48 ? 2049 HOH I O   1 
HETATM 12573 O  O   . HOH BB 6 .   ? 155.917 123.754 58.619 1.00   32.75 ? 2050 HOH I O   1 
HETATM 12574 O  O   . HOH BB 6 .   ? 146.725 119.438 61.600 1.00   47.09 ? 2051 HOH I O   1 
HETATM 12575 O  O   . HOH BB 6 .   ? 146.619 119.807 69.858 1.00   45.59 ? 2052 HOH I O   1 
HETATM 12576 O  O   . HOH BB 6 .   ? 158.134 126.507 67.981 1.00   54.00 ? 2053 HOH I O   1 
HETATM 12577 O  O   . HOH BB 6 .   ? 159.636 128.596 68.962 1.00   59.07 ? 2054 HOH I O   1 
HETATM 12578 O  O   . HOH BB 6 .   ? 153.172 127.330 66.338 1.00   19.41 ? 2055 HOH I O   1 
HETATM 12579 O  O   . HOH BB 6 .   ? 149.618 134.317 68.043 1.00   30.76 ? 2056 HOH I O   1 
HETATM 12580 O  O   . HOH BB 6 .   ? 151.872 131.042 69.886 1.00   42.05 ? 2057 HOH I O   1 
HETATM 12581 O  O   . HOH BB 6 .   ? 145.936 128.250 45.884 1.00   40.07 ? 2058 HOH I O   1 
HETATM 12582 O  O   . HOH BB 6 .   ? 150.589 128.909 68.081 1.00   38.99 ? 2059 HOH I O   1 
HETATM 12583 O  O   . HOH BB 6 .   ? 143.145 133.715 44.522 1.00   36.85 ? 2060 HOH I O   1 
HETATM 12584 O  O   . HOH BB 6 .   ? 147.759 134.594 66.222 1.00   19.35 ? 2061 HOH I O   1 
HETATM 12585 O  O   . HOH BB 6 .   ? 142.384 132.493 64.904 1.00   30.86 ? 2062 HOH I O   1 
HETATM 12586 O  O   . HOH BB 6 .   ? 145.369 135.972 66.329 1.00   27.25 ? 2063 HOH I O   1 
HETATM 12587 O  O   . HOH BB 6 .   ? 145.413 128.040 68.285 1.00   26.24 ? 2064 HOH I O   1 
HETATM 12588 O  O   . HOH BB 6 .   ? 141.839 129.476 67.413 1.00   35.81 ? 2065 HOH I O   1 
HETATM 12589 O  O   . HOH BB 6 .   ? 139.215 131.244 61.257 1.00   26.59 ? 2066 HOH I O   1 
HETATM 12590 O  O   . HOH BB 6 .   ? 140.947 133.865 62.818 1.00   29.64 ? 2067 HOH I O   1 
HETATM 12591 O  O   . HOH BB 6 .   ? 146.150 145.064 56.407 1.00   23.50 ? 2068 HOH I O   1 
HETATM 12592 O  O   A HOH BB 6 .   ? 137.698 137.076 63.157 0.50   12.91 ? 2069 HOH I O   1 
HETATM 12593 O  O   B HOH BB 6 .   ? 136.229 137.607 58.468 0.50   10.93 ? 2069 HOH I O   1 
HETATM 12594 O  O   . HOH BB 6 .   ? 136.229 137.607 58.468 1.00   39.47 ? 2070 HOH I O   1 
HETATM 12595 O  O   . HOH BB 6 .   ? 135.025 140.914 60.897 1.00   24.54 ? 2071 HOH I O   1 
HETATM 12596 O  O   . HOH BB 6 .   ? 136.157 135.265 57.758 1.00   37.59 ? 2072 HOH I O   1 
HETATM 12597 O  O   . HOH BB 6 .   ? 132.521 137.404 55.834 1.00   36.95 ? 2073 HOH I O   1 
HETATM 12598 O  O   . HOH BB 6 .   ? 133.474 138.458 58.367 1.00   30.22 ? 2074 HOH I O   1 
HETATM 12599 O  O   . HOH BB 6 .   ? 149.868 152.018 47.743 1.00   34.85 ? 2075 HOH I O   1 
HETATM 12600 O  O   . HOH BB 6 .   ? 150.115 156.011 52.089 1.00   43.32 ? 2076 HOH I O   1 
HETATM 12601 O  O   . HOH BB 6 .   ? 154.233 153.598 47.298 1.00   38.74 ? 2077 HOH I O   1 
HETATM 12602 O  O   . HOH BB 6 .   ? 162.516 149.261 57.464 1.00   24.61 ? 2078 HOH I O   1 
HETATM 12603 O  O   . HOH BB 6 .   ? 139.388 159.207 57.925 1.00   68.10 ? 2079 HOH I O   1 
HETATM 12604 O  O   . HOH BB 6 .   ? 161.255 156.420 57.316 1.00   39.05 ? 2080 HOH I O   1 
HETATM 12605 O  O   . HOH BB 6 .   ? 160.575 144.427 59.072 1.00   38.12 ? 2081 HOH I O   1 
HETATM 12606 O  O   . HOH BB 6 .   ? 160.172 143.882 64.471 1.00   47.97 ? 2082 HOH I O   1 
HETATM 12607 O  O   . HOH BB 6 .   ? 147.559 147.091 67.600 1.00   46.66 ? 2083 HOH I O   1 
HETATM 12608 O  O   . HOH BB 6 .   ? 159.200 155.691 62.701 1.00   39.46 ? 2084 HOH I O   1 
HETATM 12609 O  O   . HOH BB 6 .   ? 170.347 137.176 38.063 1.00   51.66 ? 2085 HOH I O   1 
HETATM 12610 O  O   . HOH BB 6 .   ? 152.739 155.151 60.651 1.00   54.69 ? 2086 HOH I O   1 
HETATM 12611 O  O   . HOH BB 6 .   ? 150.242 148.184 63.821 1.00   39.68 ? 2087 HOH I O   1 
HETATM 12612 O  O   . HOH BB 6 .   ? 155.507 155.059 57.107 1.00   27.82 ? 2088 HOH I O   1 
HETATM 12613 O  O   . HOH BB 6 .   ? 148.435 152.305 57.884 1.00   35.15 ? 2089 HOH I O   1 
HETATM 12614 O  O   . HOH BB 6 .   ? 146.009 148.864 56.061 1.00   27.19 ? 2090 HOH I O   1 
HETATM 12615 O  O   . HOH BB 6 .   ? 144.600 149.266 53.715 1.00   28.83 ? 2091 HOH I O   1 
HETATM 12616 O  O   . HOH BB 6 .   ? 145.618 146.771 57.767 1.00   32.25 ? 2092 HOH I O   1 
HETATM 12617 O  O   . HOH BB 6 .   ? 146.732 154.953 46.206 1.00   40.74 ? 2093 HOH I O   1 
HETATM 12618 O  O   . HOH BB 6 .   ? 145.923 148.588 43.631 1.00   20.39 ? 2094 HOH I O   1 
HETATM 12619 O  O   . HOH BB 6 .   ? 144.317 152.934 49.594 1.00   41.04 ? 2095 HOH I O   1 
HETATM 12620 O  O   . HOH BB 6 .   ? 140.643 150.944 50.117 1.00   34.07 ? 2096 HOH I O   1 
HETATM 12621 O  O   . HOH BB 6 .   ? 142.939 143.640 40.125 1.00   42.16 ? 2097 HOH I O   1 
HETATM 12622 O  O   . HOH BB 6 .   ? 143.931 146.101 36.550 1.00   61.13 ? 2098 HOH I O   1 
HETATM 12623 O  O   . HOH BB 6 .   ? 141.133 146.550 34.807 1.00   46.92 ? 2099 HOH I O   1 
HETATM 12624 O  O   . HOH BB 6 .   ? 139.333 153.498 48.441 1.00   40.47 ? 2100 HOH I O   1 
HETATM 12625 O  O   . HOH BB 6 .   ? 142.763 140.105 50.900 1.00   13.16 ? 2101 HOH I O   1 
HETATM 12626 O  O   . HOH BB 6 .   ? 135.980 138.814 48.003 1.00   21.52 ? 2102 HOH I O   1 
HETATM 12627 O  O   . HOH BB 6 .   ? 139.352 135.928 47.039 1.00   15.84 ? 2103 HOH I O   1 
HETATM 12628 O  O   . HOH BB 6 .   ? 142.297 139.489 40.223 1.00   36.95 ? 2104 HOH I O   1 
HETATM 12629 O  O   . HOH BB 6 .   ? 143.477 137.290 40.735 1.00   51.29 ? 2105 HOH I O   1 
HETATM 12630 O  O   . HOH BB 6 .   ? 136.023 129.115 46.371 1.00   23.44 ? 2106 HOH I O   1 
HETATM 12631 O  O   . HOH BB 6 .   ? 138.933 128.773 45.836 1.00   29.51 ? 2107 HOH I O   1 
HETATM 12632 O  O   . HOH BB 6 .   ? 136.167 143.510 46.127 1.00   41.53 ? 2108 HOH I O   1 
HETATM 12633 O  O   . HOH BB 6 .   ? 135.612 140.185 40.630 1.00   33.33 ? 2109 HOH I O   1 
HETATM 12634 O  O   . HOH BB 6 .   ? 135.467 142.570 41.814 1.00   46.86 ? 2110 HOH I O   1 
HETATM 12635 O  O   . HOH BB 6 .   ? 142.650 141.679 39.024 1.00   44.88 ? 2111 HOH I O   1 
HETATM 12636 O  O   . HOH BB 6 .   ? 137.169 141.349 35.774 1.00   55.86 ? 2112 HOH I O   1 
HETATM 12637 O  O   . HOH BB 6 .   ? 137.469 151.730 43.394 1.00   41.09 ? 2113 HOH I O   1 
HETATM 12638 O  O   . HOH BB 6 .   ? 144.472 146.836 42.355 1.00   23.91 ? 2114 HOH I O   1 
HETATM 12639 O  O   . HOH BB 6 .   ? 144.653 133.466 50.275 1.00   28.19 ? 2115 HOH I O   1 
HETATM 12640 O  O   . HOH BB 6 .   ? 142.024 133.904 50.663 1.00   20.16 ? 2116 HOH I O   1 
HETATM 12641 O  O   . HOH BB 6 .   ? 139.641 132.949 53.259 1.00   25.34 ? 2117 HOH I O   1 
HETATM 12642 O  O   . HOH BB 6 .   ? 148.452 125.315 57.664 1.00   17.53 ? 2118 HOH I O   1 
HETATM 12643 O  O   . HOH BB 6 .   ? 140.898 127.626 56.279 1.00   20.32 ? 2119 HOH I O   1 
HETATM 12644 O  O   . HOH BB 6 .   ? 140.510 124.553 59.922 0.50   20.63 ? 2120 HOH I O   1 
HETATM 12645 O  O   . HOH BB 6 .   ? 142.397 124.709 60.775 0.50   14.04 ? 2121 HOH I O   1 
HETATM 12646 O  O   . HOH BB 6 .   ? 151.980 121.627 62.040 1.00   29.89 ? 2122 HOH I O   1 
HETATM 12647 O  O   . HOH BB 6 .   ? 149.657 123.034 58.892 1.00   22.55 ? 2123 HOH I O   1 
HETATM 12648 O  O   . HOH BB 6 .   ? 144.785 121.301 62.732 1.00   35.51 ? 2124 HOH I O   1 
HETATM 12649 O  O   . HOH BB 6 .   ? 147.306 126.946 69.274 1.00   45.83 ? 2125 HOH I O   1 
HETATM 12650 O  O   . HOH BB 6 .   ? 148.958 125.285 69.779 1.00   55.61 ? 2126 HOH I O   1 
HETATM 12651 O  O   . HOH BB 6 .   ? 148.533 118.823 68.403 1.00   44.56 ? 2127 HOH I O   1 
HETATM 12652 O  O   . HOH BB 6 .   ? 154.395 122.721 66.317 1.00   40.52 ? 2128 HOH I O   1 
HETATM 12653 O  O   . HOH BB 6 .   ? 150.723 121.295 54.916 1.00   31.05 ? 2129 HOH I O   1 
HETATM 12654 O  O   . HOH BB 6 .   ? 153.270 121.546 59.432 1.00   40.35 ? 2130 HOH I O   1 
HETATM 12655 O  O   . HOH BB 6 .   ? 146.066 127.514 49.119 1.00   24.58 ? 2131 HOH I O   1 
HETATM 12656 O  O   . HOH BB 6 .   ? 149.535 123.147 47.543 1.00   59.60 ? 2132 HOH I O   1 
HETATM 12657 O  O   . HOH BB 6 .   ? 146.136 130.821 45.775 1.00   25.11 ? 2133 HOH I O   1 
HETATM 12658 O  O   . HOH BB 6 .   ? 145.140 133.542 41.145 1.00   40.19 ? 2134 HOH I O   1 
HETATM 12659 O  O   . HOH BB 6 .   ? 145.816 134.585 44.824 1.00   32.69 ? 2135 HOH I O   1 
HETATM 12660 O  O   . HOH BB 6 .   ? 145.391 135.879 41.494 1.00   31.18 ? 2136 HOH I O   1 
HETATM 12661 O  O   . HOH BB 6 .   ? 147.198 133.243 39.437 1.00   45.18 ? 2137 HOH I O   1 
HETATM 12662 O  O   . HOH BB 6 .   ? 154.888 145.652 38.136 1.00   46.18 ? 2138 HOH I O   1 
HETATM 12663 O  O   . HOH BB 6 .   ? 156.047 153.572 45.407 1.00   45.80 ? 2139 HOH I O   1 
HETATM 12664 O  O   . HOH BB 6 .   ? 158.581 146.247 57.809 1.00   33.47 ? 2140 HOH I O   1 
HETATM 12665 O  O   . HOH BB 6 .   ? 144.059 145.591 59.825 1.00   28.45 ? 2141 HOH I O   1 
HETATM 12666 O  O   . HOH BB 6 .   ? 142.259 144.734 66.594 1.00   37.35 ? 2142 HOH I O   1 
HETATM 12667 O  O   . HOH BB 6 .   ? 142.499 138.719 68.902 1.00   46.51 ? 2143 HOH I O   1 
HETATM 12668 O  O   . HOH BB 6 .   ? 140.156 144.575 65.221 1.00   40.53 ? 2144 HOH I O   1 
HETATM 12669 O  O   . HOH BB 6 .   ? 137.426 139.481 60.483 1.00   26.70 ? 2145 HOH I O   1 
HETATM 12670 O  O   . HOH BB 6 .   ? 136.563 135.261 55.324 1.00   42.02 ? 2146 HOH I O   1 
HETATM 12671 O  O   . HOH BB 6 .   ? 134.187 136.906 53.768 1.00   32.15 ? 2147 HOH I O   1 
HETATM 12672 O  O   . HOH BB 6 .   ? 133.393 141.108 58.628 1.00   20.24 ? 2148 HOH I O   1 
HETATM 12673 O  O   . HOH BB 6 .   ? 131.485 145.063 52.067 1.00   17.51 ? 2149 HOH I O   1 
HETATM 12674 O  O   . HOH BB 6 .   ? 132.606 143.452 47.678 1.00   28.10 ? 2150 HOH I O   1 
HETATM 12675 O  O   . HOH BB 6 .   ? 129.876 138.675 54.215 1.00   26.87 ? 2151 HOH I O   1 
HETATM 12676 O  O   . HOH BB 6 .   ? 128.570 141.016 52.031 1.00   26.47 ? 2152 HOH I O   1 
HETATM 12677 O  O   . HOH BB 6 .   ? 129.720 136.129 47.086 1.00   37.88 ? 2153 HOH I O   1 
HETATM 12678 O  O   . HOH BB 6 .   ? 133.839 135.027 51.175 0.50   21.30 ? 2154 HOH I O   1 
HETATM 12679 O  O   . HOH BB 6 .   ? 134.497 146.213 62.314 1.00   35.79 ? 2155 HOH I O   1 
HETATM 12680 O  O   . HOH BB 6 .   ? 134.633 148.708 62.330 1.00   36.87 ? 2156 HOH I O   1 
HETATM 12681 O  O   . HOH BB 6 .   ? 131.907 152.171 58.017 1.00   45.70 ? 2157 HOH I O   1 
HETATM 12682 O  O   . HOH BB 6 .   ? 134.012 150.492 59.604 1.00   28.76 ? 2158 HOH I O   1 
HETATM 12683 O  O   . HOH BB 6 .   ? 132.597 154.858 57.995 1.00   43.19 ? 2159 HOH I O   1 
HETATM 12684 O  O   . HOH BB 6 .   ? 140.892 145.785 60.842 1.00   29.52 ? 2160 HOH I O   1 
HETATM 12685 O  O   . HOH BB 6 .   ? 142.985 147.681 61.117 1.00   56.12 ? 2161 HOH I O   1 
HETATM 12686 O  O   . HOH BB 6 .   ? 140.900 155.686 55.878 1.00   53.28 ? 2162 HOH I O   1 
HETATM 12687 O  O   . HOH BB 6 .   ? 149.320 142.921 67.498 1.00   30.63 ? 2163 HOH I O   1 
HETATM 12688 O  O   . HOH BB 6 .   ? 148.979 146.611 64.766 1.00   20.52 ? 2164 HOH I O   1 
HETATM 12689 O  O   . HOH BB 6 .   ? 162.571 142.798 57.266 1.00   25.37 ? 2165 HOH I O   1 
HETATM 12690 O  O   . HOH BB 6 .   ? 167.059 135.237 41.618 1.00   49.88 ? 2166 HOH I O   1 
HETATM 12691 O  O   . HOH BB 6 .   ? 170.408 135.458 41.240 1.00   54.30 ? 2167 HOH I O   1 
HETATM 12692 O  O   . HOH CB 6 .   ? 118.172 104.493 39.541 1.00   34.43 ? 2001 HOH J O   1 
HETATM 12693 O  O   . HOH CB 6 .   ? 107.859 109.823 40.477 1.00   51.25 ? 2002 HOH J O   1 
HETATM 12694 O  O   . HOH CB 6 .   ? 116.933 108.221 46.447 1.00   31.61 ? 2003 HOH J O   1 
HETATM 12695 O  O   . HOH CB 6 .   ? 131.075 112.090 65.181 1.00   43.30 ? 2004 HOH J O   1 
HETATM 12696 O  O   . HOH CB 6 .   ? 124.526 103.910 51.660 1.00   21.20 ? 2005 HOH J O   1 
HETATM 12697 O  O   . HOH CB 6 .   ? 126.321 103.660 55.862 1.00   36.90 ? 2006 HOH J O   1 
HETATM 12698 O  O   . HOH CB 6 .   ? 129.029 104.095 57.086 1.00   36.11 ? 2007 HOH J O   1 
HETATM 12699 O  O   . HOH CB 6 .   ? 124.352 101.937 56.486 1.00   38.40 ? 2008 HOH J O   1 
HETATM 12700 O  O   . HOH CB 6 .   ? 123.196 98.498  59.633 1.00   52.08 ? 2009 HOH J O   1 
HETATM 12701 O  O   . HOH CB 6 .   ? 126.795 107.469 63.352 1.00   32.95 ? 2010 HOH J O   1 
HETATM 12702 O  O   . HOH CB 6 .   ? 127.520 105.300 66.186 1.00   50.41 ? 2011 HOH J O   1 
HETATM 12703 O  O   . HOH CB 6 .   ? 117.853 118.031 33.853 1.00   46.80 ? 2012 HOH J O   1 
HETATM 12704 O  O   . HOH CB 6 .   ? 133.505 108.334 61.539 1.00   40.14 ? 2013 HOH J O   1 
HETATM 12705 O  O   . HOH CB 6 .   ? 134.433 105.898 60.600 1.00   34.67 ? 2014 HOH J O   1 
HETATM 12706 O  O   . HOH CB 6 .   ? 129.619 110.446 64.067 1.00   33.85 ? 2015 HOH J O   1 
HETATM 12707 O  O   . HOH CB 6 .   ? 121.899 110.587 66.112 1.00   45.93 ? 2016 HOH J O   1 
HETATM 12708 O  O   . HOH CB 6 .   ? 119.631 105.777 66.772 1.00   65.99 ? 2017 HOH J O   1 
HETATM 12709 O  O   . HOH CB 6 .   ? 120.751 107.164 58.878 1.00   49.67 ? 2018 HOH J O   1 
HETATM 12710 O  O   . HOH CB 6 .   ? 116.355 112.131 54.518 1.00   37.83 ? 2019 HOH J O   1 
HETATM 12711 O  O   . HOH CB 6 .   ? 133.119 129.001 58.603 1.00   52.45 ? 2020 HOH J O   1 
HETATM 12712 O  O   . HOH CB 6 .   ? 126.268 115.898 35.521 1.00   34.44 ? 2021 HOH J O   1 
HETATM 12713 O  O   . HOH CB 6 .   ? 119.365 115.943 34.961 1.00   33.57 ? 2022 HOH J O   1 
HETATM 12714 O  O   . HOH CB 6 .   ? 142.549 104.854 50.815 1.00   47.46 ? 2023 HOH J O   1 
HETATM 12715 O  O   . HOH CB 6 .   ? 116.290 118.679 28.036 1.00   53.95 ? 2024 HOH J O   1 
HETATM 12716 O  O   . HOH CB 6 .   ? 127.374 112.233 32.765 1.00   45.20 ? 2025 HOH J O   1 
HETATM 12717 O  O   . HOH CB 6 .   ? 125.692 124.190 45.593 1.00   40.81 ? 2026 HOH J O   1 
HETATM 12718 O  O   . HOH CB 6 .   ? 135.373 119.651 36.875 1.00   46.26 ? 2027 HOH J O   1 
HETATM 12719 O  O   . HOH CB 6 .   ? 116.225 118.838 52.525 1.00   36.77 ? 2028 HOH J O   1 
HETATM 12720 O  O   . HOH CB 6 .   ? 114.787 118.489 64.529 1.00   52.22 ? 2029 HOH J O   1 
HETATM 12721 O  O   . HOH CB 6 .   ? 120.447 116.374 65.809 1.00   32.04 ? 2030 HOH J O   1 
HETATM 12722 O  O   . HOH CB 6 .   ? 128.440 115.835 65.877 1.00   36.96 ? 2031 HOH J O   1 
HETATM 12723 O  O   . HOH CB 6 .   ? 124.185 117.767 67.600 1.00   42.66 ? 2032 HOH J O   1 
HETATM 12724 O  O   . HOH CB 6 .   ? 129.393 117.737 64.331 1.00   25.63 ? 2033 HOH J O   1 
HETATM 12725 O  O   . HOH CB 6 .   ? 130.306 123.566 63.640 1.00   42.90 ? 2034 HOH J O   1 
HETATM 12726 O  O   . HOH CB 6 .   ? 131.903 118.826 64.347 1.00   36.52 ? 2035 HOH J O   1 
HETATM 12727 O  O   . HOH CB 6 .   ? 132.421 121.600 65.568 1.00   57.16 ? 2036 HOH J O   1 
HETATM 12728 O  O   . HOH CB 6 .   ? 129.982 127.614 60.954 1.00   32.63 ? 2037 HOH J O   1 
HETATM 12729 O  O   . HOH CB 6 .   ? 145.314 118.784 59.243 1.00   57.34 ? 2038 HOH J O   1 
HETATM 12730 O  O   . HOH CB 6 .   ? 133.683 128.578 56.137 1.00   49.26 ? 2039 HOH J O   1 
HETATM 12731 O  O   . HOH CB 6 .   ? 136.940 129.477 55.631 1.00   55.81 ? 2040 HOH J O   1 
HETATM 12732 O  O   . HOH CB 6 .   ? 138.409 115.423 52.980 1.00   30.75 ? 2041 HOH J O   1 
HETATM 12733 O  O   . HOH CB 6 .   ? 142.074 132.207 46.828 1.00   22.34 ? 2042 HOH J O   1 
HETATM 12734 O  O   . HOH CB 6 .   ? 143.787 107.801 45.292 1.00   44.54 ? 2043 HOH J O   1 
HETATM 12735 O  O   . HOH CB 6 .   ? 138.743 105.489 41.159 1.00   36.70 ? 2044 HOH J O   1 
HETATM 12736 O  O   . HOH CB 6 .   ? 139.660 110.599 41.960 1.00   31.25 ? 2045 HOH J O   1 
HETATM 12737 O  O   . HOH CB 6 .   ? 132.695 99.349  51.645 1.00   22.74 ? 2046 HOH J O   1 
HETATM 12738 O  O   . HOH CB 6 .   ? 133.851 104.395 53.650 1.00   31.70 ? 2047 HOH J O   1 
HETATM 12739 O  O   . HOH CB 6 .   ? 139.566 97.134  51.076 1.00   33.02 ? 2048 HOH J O   1 
HETATM 12740 O  O   . HOH CB 6 .   ? 129.814 103.042 54.792 1.00   41.44 ? 2049 HOH J O   1 
HETATM 12741 O  O   . HOH CB 6 .   ? 138.855 95.586  58.123 1.00   53.56 ? 2050 HOH J O   1 
HETATM 12742 O  O   . HOH CB 6 .   ? 140.850 98.442  55.171 1.00   49.94 ? 2051 HOH J O   1 
HETATM 12743 O  O   . HOH CB 6 .   ? 136.840 100.902 61.859 1.00   64.85 ? 2052 HOH J O   1 
HETATM 12744 O  O   . HOH CB 6 .   ? 141.938 108.574 54.128 1.00   34.36 ? 2053 HOH J O   1 
HETATM 12745 O  O   . HOH CB 6 .   ? 139.672 110.031 58.712 1.00   37.76 ? 2054 HOH J O   1 
HETATM 12746 O  O   . HOH CB 6 .   ? 141.180 102.768 50.346 1.00   31.98 ? 2055 HOH J O   1 
HETATM 12747 O  O   . HOH CB 6 .   ? 142.065 100.845 54.540 1.00   50.31 ? 2056 HOH J O   1 
HETATM 12748 O  O   . HOH CB 6 .   ? 142.628 109.874 52.006 1.00   30.04 ? 2057 HOH J O   1 
HETATM 12749 O  O   . HOH CB 6 .   ? 141.078 115.235 48.911 1.00   26.46 ? 2058 HOH J O   1 
HETATM 12750 O  O   . HOH CB 6 .   ? 142.606 113.633 44.831 1.00   44.68 ? 2059 HOH J O   1 
HETATM 12751 O  O   . HOH CB 6 .   ? 140.188 114.110 51.471 1.00   30.21 ? 2060 HOH J O   1 
HETATM 12752 O  O   . HOH CB 6 .   ? 138.162 116.018 39.249 1.00   20.40 ? 2061 HOH J O   1 
HETATM 12753 O  O   . HOH CB 6 .   ? 145.129 119.826 35.850 1.00   46.26 ? 2062 HOH J O   1 
HETATM 12754 O  O   . HOH CB 6 .   ? 143.831 118.428 45.321 1.00   33.93 ? 2063 HOH J O   1 
HETATM 12755 O  O   . HOH CB 6 .   ? 140.695 126.097 44.148 1.00   29.39 ? 2064 HOH J O   1 
HETATM 12756 O  O   . HOH CB 6 .   ? 133.752 121.744 48.188 1.00   21.27 ? 2065 HOH J O   1 
HETATM 12757 O  O   . HOH CB 6 .   ? 131.457 127.287 45.674 1.00   22.08 ? 2066 HOH J O   1 
HETATM 12758 O  O   . HOH CB 6 .   ? 129.653 124.083 38.652 1.00   59.02 ? 2067 HOH J O   1 
HETATM 12759 O  O   . HOH CB 6 .   ? 132.172 124.066 38.444 1.00   43.16 ? 2068 HOH J O   1 
HETATM 12760 O  O   . HOH CB 6 .   ? 127.141 126.664 46.338 1.00   39.75 ? 2069 HOH J O   1 
HETATM 12761 O  O   . HOH CB 6 .   ? 125.982 131.709 45.766 1.00   31.21 ? 2070 HOH J O   1 
HETATM 12762 O  O   . HOH CB 6 .   ? 138.914 127.058 43.263 1.00   36.25 ? 2071 HOH J O   1 
HETATM 12763 O  O   . HOH CB 6 .   ? 136.208 129.639 38.924 1.00   38.34 ? 2072 HOH J O   1 
HETATM 12764 O  O   . HOH CB 6 .   ? 138.125 129.553 40.724 0.50   21.78 ? 2073 HOH J O   1 
HETATM 12765 O  O   . HOH CB 6 .   ? 138.149 128.378 39.615 0.50   19.98 ? 2074 HOH J O   1 
HETATM 12766 O  O   . HOH CB 6 .   ? 137.105 118.536 38.379 1.00   24.72 ? 2075 HOH J O   1 
HETATM 12767 O  O   . HOH CB 6 .   ? 127.240 123.269 49.327 1.00   24.24 ? 2076 HOH J O   1 
HETATM 12768 O  O   . HOH CB 6 .   ? 122.793 121.921 54.309 1.00   37.49 ? 2077 HOH J O   1 
HETATM 12769 O  O   . HOH CB 6 .   ? 115.662 120.768 63.396 1.00   50.92 ? 2078 HOH J O   1 
HETATM 12770 O  O   . HOH CB 6 .   ? 118.958 127.256 64.084 1.00   36.89 ? 2079 HOH J O   1 
HETATM 12771 O  O   . HOH CB 6 .   ? 121.651 124.926 48.366 1.00   43.26 ? 2080 HOH J O   1 
HETATM 12772 O  O   . HOH CB 6 .   ? 123.207 123.993 44.911 1.00   29.19 ? 2081 HOH J O   1 
HETATM 12773 O  O   . HOH CB 6 .   ? 123.892 122.571 39.033 1.00   47.01 ? 2082 HOH J O   1 
HETATM 12774 O  O   . HOH CB 6 .   ? 123.274 125.036 42.077 1.00   39.77 ? 2083 HOH J O   1 
HETATM 12775 O  O   . HOH CB 6 .   ? 126.512 122.448 43.363 1.00   30.85 ? 2084 HOH J O   1 
HETATM 12776 O  O   . HOH CB 6 .   ? 120.327 123.922 36.019 1.00   48.76 ? 2085 HOH J O   1 
HETATM 12777 O  O   . HOH CB 6 .   ? 127.207 122.687 39.194 1.00   50.39 ? 2086 HOH J O   1 
HETATM 12778 O  O   . HOH CB 6 .   ? 130.210 111.652 33.863 1.00   42.35 ? 2087 HOH J O   1 
HETATM 12779 O  O   . HOH CB 6 .   ? 127.738 104.700 33.030 1.00   55.36 ? 2088 HOH J O   1 
HETATM 12780 O  O   . HOH CB 6 .   ? 133.390 107.304 37.985 1.00   29.85 ? 2089 HOH J O   1 
HETATM 12781 O  O   . HOH CB 6 .   ? 136.485 108.368 36.307 1.00   49.42 ? 2090 HOH J O   1 
HETATM 12782 O  O   . HOH CB 6 .   ? 136.763 120.849 65.087 1.00   43.15 ? 2091 HOH J O   1 
HETATM 12783 O  O   . HOH CB 6 .   ? 135.568 117.973 67.326 1.00   59.74 ? 2092 HOH J O   1 
HETATM 12784 O  O   . HOH CB 6 .   ? 140.457 119.532 65.634 1.00   54.07 ? 2093 HOH J O   1 
HETATM 12785 O  O   . HOH CB 6 .   ? 141.714 118.995 60.759 1.00   47.42 ? 2094 HOH J O   1 
HETATM 12786 O  O   . HOH CB 6 .   ? 142.452 120.215 58.571 1.00   44.43 ? 2095 HOH J O   1 
HETATM 12787 O  O   . HOH CB 6 .   ? 135.608 125.299 60.842 1.00   33.62 ? 2096 HOH J O   1 
HETATM 12788 O  O   . HOH CB 6 .   ? 137.845 124.838 58.560 1.00   31.26 ? 2097 HOH J O   1 
HETATM 12789 O  O   . HOH CB 6 .   ? 133.544 128.720 53.668 1.00   38.52 ? 2098 HOH J O   1 
HETATM 12790 O  O   . HOH CB 6 .   ? 135.781 130.109 52.193 1.00   26.95 ? 2099 HOH J O   1 
HETATM 12791 O  O   . HOH CB 6 .   ? 136.296 128.018 56.704 1.00   46.88 ? 2100 HOH J O   1 
HETATM 12792 O  O   . HOH CB 6 .   ? 142.631 127.724 45.757 1.00   31.74 ? 2101 HOH J O   1 
HETATM 12793 O  O   . HOH CB 6 .   ? 141.288 130.168 45.604 1.00   37.90 ? 2102 HOH J O   1 
HETATM 12794 O  O   . HOH CB 6 .   ? 143.853 128.971 49.165 1.00   15.61 ? 2103 HOH J O   1 
HETATM 12795 O  O   . HOH CB 6 .   ? 143.393 130.516 49.108 1.00   43.38 ? 2104 HOH J O   1 
HETATM 12796 O  O   . HOH CB 6 .   ? 134.692 132.856 46.222 0.50   20.73 ? 2105 HOH J O   1 
HETATM 12797 O  O   . HOH CB 6 .   ? 136.280 136.034 47.771 1.00   27.72 ? 2106 HOH J O   1 
HETATM 12798 O  O   . HOH CB 6 .   ? 147.500 122.219 57.461 1.00   27.72 ? 2107 HOH J O   1 
HETATM 12799 O  O   . HOH CB 6 .   ? 148.573 122.871 55.063 1.00   20.96 ? 2108 HOH J O   1 
HETATM 12800 O  O   . HOH CB 6 .   ? 145.120 123.185 58.613 1.00   35.83 ? 2109 HOH J O   1 
HETATM 12801 O  O   . HOH CB 6 .   ? 144.904 116.047 53.312 1.00   50.90 ? 2110 HOH J O   1 
HETATM 12802 O  O   . HOH CB 6 .   ? 147.526 116.080 53.776 1.00   50.73 ? 2111 HOH J O   1 
HETATM 12803 O  O   . HOH CB 6 .   ? 147.238 119.299 57.271 1.00   32.91 ? 2112 HOH J O   1 
HETATM 12804 O  O   . HOH CB 6 .   ? 141.404 118.872 56.606 1.00   29.30 ? 2113 HOH J O   1 
HETATM 12805 O  O   . HOH CB 6 .   ? 148.749 115.527 51.400 1.00   49.17 ? 2114 HOH J O   1 
HETATM 12806 O  O   . HOH CB 6 .   ? 139.510 116.541 55.445 1.00   25.00 ? 2115 HOH J O   1 
HETATM 12807 O  O   . HOH CB 6 .   ? 141.395 115.487 59.819 1.00   40.33 ? 2116 HOH J O   1 
HETATM 12808 O  O   . HOH CB 6 .   ? 138.724 110.928 59.947 1.00   30.14 ? 2117 HOH J O   1 
HETATM 12809 O  O   . HOH CB 6 .   ? 141.408 110.168 56.779 1.00   35.05 ? 2118 HOH J O   1 
HETATM 12810 O  O   . HOH CB 6 .   ? 126.999 102.580 52.936 1.00   24.64 ? 2119 HOH J O   1 
HETATM 12811 O  O   . HOH CB 6 .   ? 133.376 130.185 46.781 1.00   36.83 ? 2120 HOH J O   1 
HETATM 12812 O  O   . HOH CB 6 .   ? 187.974 133.843 41.540 1.00   69.52 ? 2121 HOH J O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 CYS 112 111 111 CYS CYS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   MET 1   0   ?   ?   ?   B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
C 1 1   MET 1   0   ?   ?   ?   C . n 
C 1 2   ALA 2   1   1   ALA ALA C . n 
C 1 3   THR 3   2   2   THR THR C . n 
C 1 4   LYS 4   3   3   LYS LYS C . n 
C 1 5   ALA 5   4   4   ALA ALA C . n 
C 1 6   VAL 6   5   5   VAL VAL C . n 
C 1 7   CYS 7   6   6   CYS CYS C . n 
C 1 8   VAL 8   7   7   VAL VAL C . n 
C 1 9   LEU 9   8   8   LEU LEU C . n 
C 1 10  LYS 10  9   9   LYS LYS C . n 
C 1 11  GLY 11  10  10  GLY GLY C . n 
C 1 12  ASP 12  11  11  ASP ASP C . n 
C 1 13  GLY 13  12  12  GLY GLY C . n 
C 1 14  PRO 14  13  13  PRO PRO C . n 
C 1 15  VAL 15  14  14  VAL VAL C . n 
C 1 16  GLN 16  15  15  GLN GLN C . n 
C 1 17  GLY 17  16  16  GLY GLY C . n 
C 1 18  ILE 18  17  17  ILE ILE C . n 
C 1 19  ILE 19  18  18  ILE ILE C . n 
C 1 20  ASN 20  19  19  ASN ASN C . n 
C 1 21  PHE 21  20  20  PHE PHE C . n 
C 1 22  GLU 22  21  21  GLU GLU C . n 
C 1 23  GLN 23  22  22  GLN GLN C . n 
C 1 24  LYS 24  23  23  LYS LYS C . n 
C 1 25  GLU 25  24  24  GLU GLU C . n 
C 1 26  SER 26  25  25  SER SER C . n 
C 1 27  ASN 27  26  26  ASN ASN C . n 
C 1 28  GLY 28  27  27  GLY GLY C . n 
C 1 29  PRO 29  28  28  PRO PRO C . n 
C 1 30  VAL 30  29  29  VAL VAL C . n 
C 1 31  LYS 31  30  30  LYS LYS C . n 
C 1 32  VAL 32  31  31  VAL VAL C . n 
C 1 33  TRP 33  32  32  TRP TRP C . n 
C 1 34  GLY 34  33  33  GLY GLY C . n 
C 1 35  SER 35  34  34  SER SER C . n 
C 1 36  ILE 36  35  35  ILE ILE C . n 
C 1 37  LYS 37  36  36  LYS LYS C . n 
C 1 38  GLY 38  37  37  GLY GLY C . n 
C 1 39  LEU 39  38  38  LEU LEU C . n 
C 1 40  THR 40  39  39  THR THR C . n 
C 1 41  GLU 41  40  40  GLU GLU C . n 
C 1 42  GLY 42  41  41  GLY GLY C . n 
C 1 43  LEU 43  42  42  LEU LEU C . n 
C 1 44  HIS 44  43  43  HIS HIS C . n 
C 1 45  GLY 45  44  44  GLY GLY C . n 
C 1 46  PHE 46  45  45  PHE PHE C . n 
C 1 47  HIS 47  46  46  HIS HIS C . n 
C 1 48  VAL 48  47  47  VAL VAL C . n 
C 1 49  HIS 49  48  48  HIS HIS C . n 
C 1 50  GLU 50  49  49  GLU GLU C . n 
C 1 51  PHE 51  50  50  PHE PHE C . n 
C 1 52  GLY 52  51  51  GLY GLY C . n 
C 1 53  ASP 53  52  52  ASP ASP C . n 
C 1 54  ASN 54  53  53  ASN ASN C . n 
C 1 55  THR 55  54  54  THR THR C . n 
C 1 56  ALA 56  55  55  ALA ALA C . n 
C 1 57  GLY 57  56  56  GLY GLY C . n 
C 1 58  CYS 58  57  57  CYS CYS C . n 
C 1 59  THR 59  58  58  THR THR C . n 
C 1 60  SER 60  59  59  SER SER C . n 
C 1 61  ALA 61  60  60  ALA ALA C . n 
C 1 62  GLY 62  61  61  GLY GLY C . n 
C 1 63  PRO 63  62  62  PRO PRO C . n 
C 1 64  HIS 64  63  63  HIS HIS C . n 
C 1 65  PHE 65  64  64  PHE PHE C . n 
C 1 66  ASN 66  65  65  ASN ASN C . n 
C 1 67  PRO 67  66  66  PRO PRO C . n 
C 1 68  LEU 68  67  67  LEU LEU C . n 
C 1 69  SER 69  68  68  SER SER C . n 
C 1 70  ARG 70  69  69  ARG ARG C . n 
C 1 71  LYS 71  70  70  LYS LYS C . n 
C 1 72  HIS 72  71  71  HIS HIS C . n 
C 1 73  GLY 73  72  72  GLY GLY C . n 
C 1 74  GLY 74  73  73  GLY GLY C . n 
C 1 75  PRO 75  74  74  PRO PRO C . n 
C 1 76  LYS 76  75  75  LYS LYS C . n 
C 1 77  ASP 77  76  76  ASP ASP C . n 
C 1 78  GLU 78  77  77  GLU GLU C . n 
C 1 79  GLU 79  78  78  GLU GLU C . n 
C 1 80  ARG 80  79  79  ARG ARG C . n 
C 1 81  HIS 81  80  80  HIS HIS C . n 
C 1 82  VAL 82  81  81  VAL VAL C . n 
C 1 83  GLY 83  82  82  GLY GLY C . n 
C 1 84  ASP 84  83  83  ASP ASP C . n 
C 1 85  LEU 85  84  84  LEU LEU C . n 
C 1 86  GLY 86  85  85  GLY GLY C . n 
C 1 87  ASN 87  86  86  ASN ASN C . n 
C 1 88  VAL 88  87  87  VAL VAL C . n 
C 1 89  THR 89  88  88  THR THR C . n 
C 1 90  ALA 90  89  89  ALA ALA C . n 
C 1 91  ASP 91  90  90  ASP ASP C . n 
C 1 92  LYS 92  91  91  LYS LYS C . n 
C 1 93  ASP 93  92  92  ASP ASP C . n 
C 1 94  GLY 94  93  93  GLY GLY C . n 
C 1 95  VAL 95  94  94  VAL VAL C . n 
C 1 96  ALA 96  95  95  ALA ALA C . n 
C 1 97  ASP 97  96  96  ASP ASP C . n 
C 1 98  VAL 98  97  97  VAL VAL C . n 
C 1 99  SER 99  98  98  SER SER C . n 
C 1 100 ILE 100 99  99  ILE ILE C . n 
C 1 101 GLU 101 100 100 GLU GLU C . n 
C 1 102 ASP 102 101 101 ASP ASP C . n 
C 1 103 SER 103 102 102 SER SER C . n 
C 1 104 VAL 104 103 103 VAL VAL C . n 
C 1 105 ILE 105 104 104 ILE ILE C . n 
C 1 106 SER 106 105 105 SER SER C . n 
C 1 107 LEU 107 106 106 LEU LEU C . n 
C 1 108 SER 108 107 107 SER SER C . n 
C 1 109 GLY 109 108 108 GLY GLY C . n 
C 1 110 ASP 110 109 109 ASP ASP C . n 
C 1 111 HIS 111 110 110 HIS HIS C . n 
C 1 112 CYS 112 111 111 CYS CYS C . n 
C 1 113 ILE 113 112 112 ILE ILE C . n 
C 1 114 ILE 114 113 113 ILE ILE C . n 
C 1 115 GLY 115 114 114 GLY GLY C . n 
C 1 116 ARG 116 115 115 ARG ARG C . n 
C 1 117 THR 117 116 116 THR THR C . n 
C 1 118 LEU 118 117 117 LEU LEU C . n 
C 1 119 VAL 119 118 118 VAL VAL C . n 
C 1 120 VAL 120 119 119 VAL VAL C . n 
C 1 121 HIS 121 120 120 HIS HIS C . n 
C 1 122 GLU 122 121 121 GLU GLU C . n 
C 1 123 LYS 123 122 122 LYS LYS C . n 
C 1 124 ALA 124 123 123 ALA ALA C . n 
C 1 125 ASP 125 124 124 ASP ASP C . n 
C 1 126 ASP 126 125 125 ASP ASP C . n 
C 1 127 LEU 127 126 126 LEU LEU C . n 
C 1 128 GLY 128 127 127 GLY GLY C . n 
C 1 129 LYS 129 128 128 LYS LYS C . n 
C 1 130 GLY 130 129 129 GLY GLY C . n 
C 1 131 GLY 131 130 130 GLY GLY C . n 
C 1 132 ASN 132 131 131 ASN ASN C . n 
C 1 133 GLU 133 132 132 GLU GLU C . n 
C 1 134 GLU 134 133 133 GLU GLU C . n 
C 1 135 SER 135 134 134 SER SER C . n 
C 1 136 THR 136 135 135 THR THR C . n 
C 1 137 LYS 137 136 136 LYS LYS C . n 
C 1 138 THR 138 137 137 THR THR C . n 
C 1 139 GLY 139 138 138 GLY GLY C . n 
C 1 140 ASN 140 139 139 ASN ASN C . n 
C 1 141 ALA 141 140 140 ALA ALA C . n 
C 1 142 GLY 142 141 141 GLY GLY C . n 
C 1 143 SER 143 142 142 SER SER C . n 
C 1 144 ARG 144 143 143 ARG ARG C . n 
C 1 145 LEU 145 144 144 LEU LEU C . n 
C 1 146 ALA 146 145 145 ALA ALA C . n 
C 1 147 CYS 147 146 146 CYS CYS C . n 
C 1 148 GLY 148 147 147 GLY GLY C . n 
C 1 149 VAL 149 148 148 VAL VAL C . n 
C 1 150 ILE 150 149 149 ILE ILE C . n 
C 1 151 GLY 151 150 150 GLY GLY C . n 
C 1 152 ILE 152 151 151 ILE ILE C . n 
C 1 153 ALA 153 152 152 ALA ALA C . n 
C 1 154 GLN 154 153 153 GLN GLN C . n 
D 1 1   MET 1   0   ?   ?   ?   D . n 
D 1 2   ALA 2   1   1   ALA ALA D . n 
D 1 3   THR 3   2   2   THR THR D . n 
D 1 4   LYS 4   3   3   LYS LYS D . n 
D 1 5   ALA 5   4   4   ALA ALA D . n 
D 1 6   VAL 6   5   5   VAL VAL D . n 
D 1 7   CYS 7   6   6   CYS CYS D . n 
D 1 8   VAL 8   7   7   VAL VAL D . n 
D 1 9   LEU 9   8   8   LEU LEU D . n 
D 1 10  LYS 10  9   9   LYS LYS D . n 
D 1 11  GLY 11  10  10  GLY GLY D . n 
D 1 12  ASP 12  11  11  ASP ASP D . n 
D 1 13  GLY 13  12  12  GLY GLY D . n 
D 1 14  PRO 14  13  13  PRO PRO D . n 
D 1 15  VAL 15  14  14  VAL VAL D . n 
D 1 16  GLN 16  15  15  GLN GLN D . n 
D 1 17  GLY 17  16  16  GLY GLY D . n 
D 1 18  ILE 18  17  17  ILE ILE D . n 
D 1 19  ILE 19  18  18  ILE ILE D . n 
D 1 20  ASN 20  19  19  ASN ASN D . n 
D 1 21  PHE 21  20  20  PHE PHE D . n 
D 1 22  GLU 22  21  21  GLU GLU D . n 
D 1 23  GLN 23  22  22  GLN GLN D . n 
D 1 24  LYS 24  23  23  LYS LYS D . n 
D 1 25  GLU 25  24  24  GLU GLU D . n 
D 1 26  SER 26  25  25  SER SER D . n 
D 1 27  ASN 27  26  26  ASN ASN D . n 
D 1 28  GLY 28  27  27  GLY GLY D . n 
D 1 29  PRO 29  28  28  PRO PRO D . n 
D 1 30  VAL 30  29  29  VAL VAL D . n 
D 1 31  LYS 31  30  30  LYS LYS D . n 
D 1 32  VAL 32  31  31  VAL VAL D . n 
D 1 33  TRP 33  32  32  TRP TRP D . n 
D 1 34  GLY 34  33  33  GLY GLY D . n 
D 1 35  SER 35  34  34  SER SER D . n 
D 1 36  ILE 36  35  35  ILE ILE D . n 
D 1 37  LYS 37  36  36  LYS LYS D . n 
D 1 38  GLY 38  37  37  GLY GLY D . n 
D 1 39  LEU 39  38  38  LEU LEU D . n 
D 1 40  THR 40  39  39  THR THR D . n 
D 1 41  GLU 41  40  40  GLU GLU D . n 
D 1 42  GLY 42  41  41  GLY GLY D . n 
D 1 43  LEU 43  42  42  LEU LEU D . n 
D 1 44  HIS 44  43  43  HIS HIS D . n 
D 1 45  GLY 45  44  44  GLY GLY D . n 
D 1 46  PHE 46  45  45  PHE PHE D . n 
D 1 47  HIS 47  46  46  HIS HIS D . n 
D 1 48  VAL 48  47  47  VAL VAL D . n 
D 1 49  HIS 49  48  48  HIS HIS D . n 
D 1 50  GLU 50  49  49  GLU GLU D . n 
D 1 51  PHE 51  50  50  PHE PHE D . n 
D 1 52  GLY 52  51  51  GLY GLY D . n 
D 1 53  ASP 53  52  52  ASP ASP D . n 
D 1 54  ASN 54  53  53  ASN ASN D . n 
D 1 55  THR 55  54  54  THR THR D . n 
D 1 56  ALA 56  55  55  ALA ALA D . n 
D 1 57  GLY 57  56  56  GLY GLY D . n 
D 1 58  CYS 58  57  57  CYS CYS D . n 
D 1 59  THR 59  58  58  THR THR D . n 
D 1 60  SER 60  59  59  SER SER D . n 
D 1 61  ALA 61  60  60  ALA ALA D . n 
D 1 62  GLY 62  61  61  GLY GLY D . n 
D 1 63  PRO 63  62  62  PRO PRO D . n 
D 1 64  HIS 64  63  63  HIS HIS D . n 
D 1 65  PHE 65  64  64  PHE PHE D . n 
D 1 66  ASN 66  65  65  ASN ASN D . n 
D 1 67  PRO 67  66  66  PRO PRO D . n 
D 1 68  LEU 68  67  67  LEU LEU D . n 
D 1 69  SER 69  68  68  SER SER D . n 
D 1 70  ARG 70  69  69  ARG ARG D . n 
D 1 71  LYS 71  70  70  LYS LYS D . n 
D 1 72  HIS 72  71  71  HIS HIS D . n 
D 1 73  GLY 73  72  72  GLY GLY D . n 
D 1 74  GLY 74  73  73  GLY GLY D . n 
D 1 75  PRO 75  74  74  PRO PRO D . n 
D 1 76  LYS 76  75  75  LYS LYS D . n 
D 1 77  ASP 77  76  76  ASP ASP D . n 
D 1 78  GLU 78  77  77  GLU GLU D . n 
D 1 79  GLU 79  78  78  GLU GLU D . n 
D 1 80  ARG 80  79  79  ARG ARG D . n 
D 1 81  HIS 81  80  80  HIS HIS D . n 
D 1 82  VAL 82  81  81  VAL VAL D . n 
D 1 83  GLY 83  82  82  GLY GLY D . n 
D 1 84  ASP 84  83  83  ASP ASP D . n 
D 1 85  LEU 85  84  84  LEU LEU D . n 
D 1 86  GLY 86  85  85  GLY GLY D . n 
D 1 87  ASN 87  86  86  ASN ASN D . n 
D 1 88  VAL 88  87  87  VAL VAL D . n 
D 1 89  THR 89  88  88  THR THR D . n 
D 1 90  ALA 90  89  89  ALA ALA D . n 
D 1 91  ASP 91  90  90  ASP ASP D . n 
D 1 92  LYS 92  91  91  LYS LYS D . n 
D 1 93  ASP 93  92  92  ASP ASP D . n 
D 1 94  GLY 94  93  93  GLY GLY D . n 
D 1 95  VAL 95  94  94  VAL VAL D . n 
D 1 96  ALA 96  95  95  ALA ALA D . n 
D 1 97  ASP 97  96  96  ASP ASP D . n 
D 1 98  VAL 98  97  97  VAL VAL D . n 
D 1 99  SER 99  98  98  SER SER D . n 
D 1 100 ILE 100 99  99  ILE ILE D . n 
D 1 101 GLU 101 100 100 GLU GLU D . n 
D 1 102 ASP 102 101 101 ASP ASP D . n 
D 1 103 SER 103 102 102 SER SER D . n 
D 1 104 VAL 104 103 103 VAL VAL D . n 
D 1 105 ILE 105 104 104 ILE ILE D . n 
D 1 106 SER 106 105 105 SER SER D . n 
D 1 107 LEU 107 106 106 LEU LEU D . n 
D 1 108 SER 108 107 107 SER SER D . n 
D 1 109 GLY 109 108 108 GLY GLY D . n 
D 1 110 ASP 110 109 109 ASP ASP D . n 
D 1 111 HIS 111 110 110 HIS HIS D . n 
D 1 112 CYS 112 111 111 CYS CYS D . n 
D 1 113 ILE 113 112 112 ILE ILE D . n 
D 1 114 ILE 114 113 113 ILE ILE D . n 
D 1 115 GLY 115 114 114 GLY GLY D . n 
D 1 116 ARG 116 115 115 ARG ARG D . n 
D 1 117 THR 117 116 116 THR THR D . n 
D 1 118 LEU 118 117 117 LEU LEU D . n 
D 1 119 VAL 119 118 118 VAL VAL D . n 
D 1 120 VAL 120 119 119 VAL VAL D . n 
D 1 121 HIS 121 120 120 HIS HIS D . n 
D 1 122 GLU 122 121 121 GLU GLU D . n 
D 1 123 LYS 123 122 122 LYS LYS D . n 
D 1 124 ALA 124 123 123 ALA ALA D . n 
D 1 125 ASP 125 124 124 ASP ASP D . n 
D 1 126 ASP 126 125 125 ASP ASP D . n 
D 1 127 LEU 127 126 126 LEU LEU D . n 
D 1 128 GLY 128 127 127 GLY GLY D . n 
D 1 129 LYS 129 128 128 LYS LYS D . n 
D 1 130 GLY 130 129 129 GLY GLY D . n 
D 1 131 GLY 131 130 130 GLY GLY D . n 
D 1 132 ASN 132 131 131 ASN ASN D . n 
D 1 133 GLU 133 132 132 GLU GLU D . n 
D 1 134 GLU 134 133 133 GLU GLU D . n 
D 1 135 SER 135 134 134 SER SER D . n 
D 1 136 THR 136 135 135 THR THR D . n 
D 1 137 LYS 137 136 136 LYS LYS D . n 
D 1 138 THR 138 137 137 THR THR D . n 
D 1 139 GLY 139 138 138 GLY GLY D . n 
D 1 140 ASN 140 139 139 ASN ASN D . n 
D 1 141 ALA 141 140 140 ALA ALA D . n 
D 1 142 GLY 142 141 141 GLY GLY D . n 
D 1 143 SER 143 142 142 SER SER D . n 
D 1 144 ARG 144 143 143 ARG ARG D . n 
D 1 145 LEU 145 144 144 LEU LEU D . n 
D 1 146 ALA 146 145 145 ALA ALA D . n 
D 1 147 CYS 147 146 146 CYS CYS D . n 
D 1 148 GLY 148 147 147 GLY GLY D . n 
D 1 149 VAL 149 148 148 VAL VAL D . n 
D 1 150 ILE 150 149 149 ILE ILE D . n 
D 1 151 GLY 151 150 150 GLY GLY D . n 
D 1 152 ILE 152 151 151 ILE ILE D . n 
D 1 153 ALA 153 152 152 ALA ALA D . n 
D 1 154 GLN 154 153 153 GLN GLN D . n 
E 1 1   MET 1   0   ?   ?   ?   E . n 
E 1 2   ALA 2   1   1   ALA ALA E . n 
E 1 3   THR 3   2   2   THR THR E . n 
E 1 4   LYS 4   3   3   LYS LYS E . n 
E 1 5   ALA 5   4   4   ALA ALA E . n 
E 1 6   VAL 6   5   5   VAL VAL E . n 
E 1 7   CYS 7   6   6   CYS CYS E . n 
E 1 8   VAL 8   7   7   VAL VAL E . n 
E 1 9   LEU 9   8   8   LEU LEU E . n 
E 1 10  LYS 10  9   9   LYS LYS E . n 
E 1 11  GLY 11  10  10  GLY GLY E . n 
E 1 12  ASP 12  11  11  ASP ASP E . n 
E 1 13  GLY 13  12  12  GLY GLY E . n 
E 1 14  PRO 14  13  13  PRO PRO E . n 
E 1 15  VAL 15  14  14  VAL VAL E . n 
E 1 16  GLN 16  15  15  GLN GLN E . n 
E 1 17  GLY 17  16  16  GLY GLY E . n 
E 1 18  ILE 18  17  17  ILE ILE E . n 
E 1 19  ILE 19  18  18  ILE ILE E . n 
E 1 20  ASN 20  19  19  ASN ASN E . n 
E 1 21  PHE 21  20  20  PHE PHE E . n 
E 1 22  GLU 22  21  21  GLU GLU E . n 
E 1 23  GLN 23  22  22  GLN GLN E . n 
E 1 24  LYS 24  23  23  LYS LYS E . n 
E 1 25  GLU 25  24  24  GLU GLU E . n 
E 1 26  SER 26  25  25  SER SER E . n 
E 1 27  ASN 27  26  26  ASN ASN E . n 
E 1 28  GLY 28  27  27  GLY GLY E . n 
E 1 29  PRO 29  28  28  PRO PRO E . n 
E 1 30  VAL 30  29  29  VAL VAL E . n 
E 1 31  LYS 31  30  30  LYS LYS E . n 
E 1 32  VAL 32  31  31  VAL VAL E . n 
E 1 33  TRP 33  32  32  TRP TRP E . n 
E 1 34  GLY 34  33  33  GLY GLY E . n 
E 1 35  SER 35  34  34  SER SER E . n 
E 1 36  ILE 36  35  35  ILE ILE E . n 
E 1 37  LYS 37  36  36  LYS LYS E . n 
E 1 38  GLY 38  37  37  GLY GLY E . n 
E 1 39  LEU 39  38  38  LEU LEU E . n 
E 1 40  THR 40  39  39  THR THR E . n 
E 1 41  GLU 41  40  40  GLU GLU E . n 
E 1 42  GLY 42  41  41  GLY GLY E . n 
E 1 43  LEU 43  42  42  LEU LEU E . n 
E 1 44  HIS 44  43  43  HIS HIS E . n 
E 1 45  GLY 45  44  44  GLY GLY E . n 
E 1 46  PHE 46  45  45  PHE PHE E . n 
E 1 47  HIS 47  46  46  HIS HIS E . n 
E 1 48  VAL 48  47  47  VAL VAL E . n 
E 1 49  HIS 49  48  48  HIS HIS E . n 
E 1 50  GLU 50  49  49  GLU GLU E . n 
E 1 51  PHE 51  50  50  PHE PHE E . n 
E 1 52  GLY 52  51  51  GLY GLY E . n 
E 1 53  ASP 53  52  52  ASP ASP E . n 
E 1 54  ASN 54  53  53  ASN ASN E . n 
E 1 55  THR 55  54  54  THR THR E . n 
E 1 56  ALA 56  55  55  ALA ALA E . n 
E 1 57  GLY 57  56  56  GLY GLY E . n 
E 1 58  CYS 58  57  57  CYS CYS E . n 
E 1 59  THR 59  58  58  THR THR E . n 
E 1 60  SER 60  59  59  SER SER E . n 
E 1 61  ALA 61  60  60  ALA ALA E . n 
E 1 62  GLY 62  61  61  GLY GLY E . n 
E 1 63  PRO 63  62  62  PRO PRO E . n 
E 1 64  HIS 64  63  63  HIS HIS E . n 
E 1 65  PHE 65  64  64  PHE PHE E . n 
E 1 66  ASN 66  65  65  ASN ASN E . n 
E 1 67  PRO 67  66  66  PRO PRO E . n 
E 1 68  LEU 68  67  67  LEU LEU E . n 
E 1 69  SER 69  68  68  SER SER E . n 
E 1 70  ARG 70  69  69  ARG ARG E . n 
E 1 71  LYS 71  70  70  LYS LYS E . n 
E 1 72  HIS 72  71  71  HIS HIS E . n 
E 1 73  GLY 73  72  72  GLY GLY E . n 
E 1 74  GLY 74  73  73  GLY GLY E . n 
E 1 75  PRO 75  74  74  PRO PRO E . n 
E 1 76  LYS 76  75  75  LYS LYS E . n 
E 1 77  ASP 77  76  76  ASP ASP E . n 
E 1 78  GLU 78  77  77  GLU GLU E . n 
E 1 79  GLU 79  78  78  GLU GLU E . n 
E 1 80  ARG 80  79  79  ARG ARG E . n 
E 1 81  HIS 81  80  80  HIS HIS E . n 
E 1 82  VAL 82  81  81  VAL VAL E . n 
E 1 83  GLY 83  82  82  GLY GLY E . n 
E 1 84  ASP 84  83  83  ASP ASP E . n 
E 1 85  LEU 85  84  84  LEU LEU E . n 
E 1 86  GLY 86  85  85  GLY GLY E . n 
E 1 87  ASN 87  86  86  ASN ASN E . n 
E 1 88  VAL 88  87  87  VAL VAL E . n 
E 1 89  THR 89  88  88  THR THR E . n 
E 1 90  ALA 90  89  89  ALA ALA E . n 
E 1 91  ASP 91  90  90  ASP ASP E . n 
E 1 92  LYS 92  91  91  LYS LYS E . n 
E 1 93  ASP 93  92  92  ASP ASP E . n 
E 1 94  GLY 94  93  93  GLY GLY E . n 
E 1 95  VAL 95  94  94  VAL VAL E . n 
E 1 96  ALA 96  95  95  ALA ALA E . n 
E 1 97  ASP 97  96  96  ASP ASP E . n 
E 1 98  VAL 98  97  97  VAL VAL E . n 
E 1 99  SER 99  98  98  SER SER E . n 
E 1 100 ILE 100 99  99  ILE ILE E . n 
E 1 101 GLU 101 100 100 GLU GLU E . n 
E 1 102 ASP 102 101 101 ASP ASP E . n 
E 1 103 SER 103 102 102 SER SER E . n 
E 1 104 VAL 104 103 103 VAL VAL E . n 
E 1 105 ILE 105 104 104 ILE ILE E . n 
E 1 106 SER 106 105 105 SER SER E . n 
E 1 107 LEU 107 106 106 LEU LEU E . n 
E 1 108 SER 108 107 107 SER SER E . n 
E 1 109 GLY 109 108 108 GLY GLY E . n 
E 1 110 ASP 110 109 109 ASP ASP E . n 
E 1 111 HIS 111 110 110 HIS HIS E . n 
E 1 112 CYS 112 111 111 CYS CYS E . n 
E 1 113 ILE 113 112 112 ILE ILE E . n 
E 1 114 ILE 114 113 113 ILE ILE E . n 
E 1 115 GLY 115 114 114 GLY GLY E . n 
E 1 116 ARG 116 115 115 ARG ARG E . n 
E 1 117 THR 117 116 116 THR THR E . n 
E 1 118 LEU 118 117 117 LEU LEU E . n 
E 1 119 VAL 119 118 118 VAL VAL E . n 
E 1 120 VAL 120 119 119 VAL VAL E . n 
E 1 121 HIS 121 120 120 HIS HIS E . n 
E 1 122 GLU 122 121 121 GLU GLU E . n 
E 1 123 LYS 123 122 122 LYS LYS E . n 
E 1 124 ALA 124 123 123 ALA ALA E . n 
E 1 125 ASP 125 124 124 ASP ASP E . n 
E 1 126 ASP 126 125 125 ASP ASP E . n 
E 1 127 LEU 127 126 126 LEU LEU E . n 
E 1 128 GLY 128 127 127 GLY GLY E . n 
E 1 129 LYS 129 128 128 LYS LYS E . n 
E 1 130 GLY 130 129 129 GLY GLY E . n 
E 1 131 GLY 131 130 130 GLY GLY E . n 
E 1 132 ASN 132 131 131 ASN ASN E . n 
E 1 133 GLU 133 132 132 GLU GLU E . n 
E 1 134 GLU 134 133 133 GLU GLU E . n 
E 1 135 SER 135 134 134 SER SER E . n 
E 1 136 THR 136 135 135 THR THR E . n 
E 1 137 LYS 137 136 136 LYS LYS E . n 
E 1 138 THR 138 137 137 THR THR E . n 
E 1 139 GLY 139 138 138 GLY GLY E . n 
E 1 140 ASN 140 139 139 ASN ASN E . n 
E 1 141 ALA 141 140 140 ALA ALA E . n 
E 1 142 GLY 142 141 141 GLY GLY E . n 
E 1 143 SER 143 142 142 SER SER E . n 
E 1 144 ARG 144 143 143 ARG ARG E . n 
E 1 145 LEU 145 144 144 LEU LEU E . n 
E 1 146 ALA 146 145 145 ALA ALA E . n 
E 1 147 CYS 147 146 146 CYS CYS E . n 
E 1 148 GLY 148 147 147 GLY GLY E . n 
E 1 149 VAL 149 148 148 VAL VAL E . n 
E 1 150 ILE 150 149 149 ILE ILE E . n 
E 1 151 GLY 151 150 150 GLY GLY E . n 
E 1 152 ILE 152 151 151 ILE ILE E . n 
E 1 153 ALA 153 152 152 ALA ALA E . n 
E 1 154 GLN 154 153 153 GLN GLN E . n 
F 1 1   MET 1   0   ?   ?   ?   F . n 
F 1 2   ALA 2   1   1   ALA ALA F . n 
F 1 3   THR 3   2   2   THR THR F . n 
F 1 4   LYS 4   3   3   LYS LYS F . n 
F 1 5   ALA 5   4   4   ALA ALA F . n 
F 1 6   VAL 6   5   5   VAL VAL F . n 
F 1 7   CYS 7   6   6   CYS CYS F . n 
F 1 8   VAL 8   7   7   VAL VAL F . n 
F 1 9   LEU 9   8   8   LEU LEU F . n 
F 1 10  LYS 10  9   9   LYS LYS F . n 
F 1 11  GLY 11  10  10  GLY GLY F . n 
F 1 12  ASP 12  11  11  ASP ASP F . n 
F 1 13  GLY 13  12  12  GLY GLY F . n 
F 1 14  PRO 14  13  13  PRO PRO F . n 
F 1 15  VAL 15  14  14  VAL VAL F . n 
F 1 16  GLN 16  15  15  GLN GLN F . n 
F 1 17  GLY 17  16  16  GLY GLY F . n 
F 1 18  ILE 18  17  17  ILE ILE F . n 
F 1 19  ILE 19  18  18  ILE ILE F . n 
F 1 20  ASN 20  19  19  ASN ASN F . n 
F 1 21  PHE 21  20  20  PHE PHE F . n 
F 1 22  GLU 22  21  21  GLU GLU F . n 
F 1 23  GLN 23  22  22  GLN GLN F . n 
F 1 24  LYS 24  23  23  LYS LYS F . n 
F 1 25  GLU 25  24  24  GLU GLU F . n 
F 1 26  SER 26  25  25  SER SER F . n 
F 1 27  ASN 27  26  26  ASN ASN F . n 
F 1 28  GLY 28  27  27  GLY GLY F . n 
F 1 29  PRO 29  28  28  PRO PRO F . n 
F 1 30  VAL 30  29  29  VAL VAL F . n 
F 1 31  LYS 31  30  30  LYS LYS F . n 
F 1 32  VAL 32  31  31  VAL VAL F . n 
F 1 33  TRP 33  32  32  TRP TRP F . n 
F 1 34  GLY 34  33  33  GLY GLY F . n 
F 1 35  SER 35  34  34  SER SER F . n 
F 1 36  ILE 36  35  35  ILE ILE F . n 
F 1 37  LYS 37  36  36  LYS LYS F . n 
F 1 38  GLY 38  37  37  GLY GLY F . n 
F 1 39  LEU 39  38  38  LEU LEU F . n 
F 1 40  THR 40  39  39  THR THR F . n 
F 1 41  GLU 41  40  40  GLU GLU F . n 
F 1 42  GLY 42  41  41  GLY GLY F . n 
F 1 43  LEU 43  42  42  LEU LEU F . n 
F 1 44  HIS 44  43  43  HIS HIS F . n 
F 1 45  GLY 45  44  44  GLY GLY F . n 
F 1 46  PHE 46  45  45  PHE PHE F . n 
F 1 47  HIS 47  46  46  HIS HIS F . n 
F 1 48  VAL 48  47  47  VAL VAL F . n 
F 1 49  HIS 49  48  48  HIS HIS F . n 
F 1 50  GLU 50  49  49  GLU GLU F . n 
F 1 51  PHE 51  50  50  PHE PHE F . n 
F 1 52  GLY 52  51  51  GLY GLY F . n 
F 1 53  ASP 53  52  52  ASP ASP F . n 
F 1 54  ASN 54  53  53  ASN ASN F . n 
F 1 55  THR 55  54  54  THR THR F . n 
F 1 56  ALA 56  55  55  ALA ALA F . n 
F 1 57  GLY 57  56  56  GLY GLY F . n 
F 1 58  CYS 58  57  57  CYS CYS F . n 
F 1 59  THR 59  58  58  THR THR F . n 
F 1 60  SER 60  59  59  SER SER F . n 
F 1 61  ALA 61  60  60  ALA ALA F . n 
F 1 62  GLY 62  61  61  GLY GLY F . n 
F 1 63  PRO 63  62  62  PRO PRO F . n 
F 1 64  HIS 64  63  63  HIS HIS F . n 
F 1 65  PHE 65  64  64  PHE PHE F . n 
F 1 66  ASN 66  65  65  ASN ASN F . n 
F 1 67  PRO 67  66  66  PRO PRO F . n 
F 1 68  LEU 68  67  67  LEU LEU F . n 
F 1 69  SER 69  68  68  SER SER F . n 
F 1 70  ARG 70  69  69  ARG ARG F . n 
F 1 71  LYS 71  70  70  LYS LYS F . n 
F 1 72  HIS 72  71  71  HIS HIS F . n 
F 1 73  GLY 73  72  72  GLY GLY F . n 
F 1 74  GLY 74  73  73  GLY GLY F . n 
F 1 75  PRO 75  74  74  PRO PRO F . n 
F 1 76  LYS 76  75  75  LYS LYS F . n 
F 1 77  ASP 77  76  76  ASP ASP F . n 
F 1 78  GLU 78  77  77  GLU GLU F . n 
F 1 79  GLU 79  78  78  GLU GLU F . n 
F 1 80  ARG 80  79  79  ARG ARG F . n 
F 1 81  HIS 81  80  80  HIS HIS F . n 
F 1 82  VAL 82  81  81  VAL VAL F . n 
F 1 83  GLY 83  82  82  GLY GLY F . n 
F 1 84  ASP 84  83  83  ASP ASP F . n 
F 1 85  LEU 85  84  84  LEU LEU F . n 
F 1 86  GLY 86  85  85  GLY GLY F . n 
F 1 87  ASN 87  86  86  ASN ASN F . n 
F 1 88  VAL 88  87  87  VAL VAL F . n 
F 1 89  THR 89  88  88  THR THR F . n 
F 1 90  ALA 90  89  89  ALA ALA F . n 
F 1 91  ASP 91  90  90  ASP ASP F . n 
F 1 92  LYS 92  91  91  LYS LYS F . n 
F 1 93  ASP 93  92  92  ASP ASP F . n 
F 1 94  GLY 94  93  93  GLY GLY F . n 
F 1 95  VAL 95  94  94  VAL VAL F . n 
F 1 96  ALA 96  95  95  ALA ALA F . n 
F 1 97  ASP 97  96  96  ASP ASP F . n 
F 1 98  VAL 98  97  97  VAL VAL F . n 
F 1 99  SER 99  98  98  SER SER F . n 
F 1 100 ILE 100 99  99  ILE ILE F . n 
F 1 101 GLU 101 100 100 GLU GLU F . n 
F 1 102 ASP 102 101 101 ASP ASP F . n 
F 1 103 SER 103 102 102 SER SER F . n 
F 1 104 VAL 104 103 103 VAL VAL F . n 
F 1 105 ILE 105 104 104 ILE ILE F . n 
F 1 106 SER 106 105 105 SER SER F . n 
F 1 107 LEU 107 106 106 LEU LEU F . n 
F 1 108 SER 108 107 107 SER SER F . n 
F 1 109 GLY 109 108 108 GLY GLY F . n 
F 1 110 ASP 110 109 109 ASP ASP F . n 
F 1 111 HIS 111 110 110 HIS HIS F . n 
F 1 112 CYS 112 111 111 CYS CYS F . n 
F 1 113 ILE 113 112 112 ILE ILE F . n 
F 1 114 ILE 114 113 113 ILE ILE F . n 
F 1 115 GLY 115 114 114 GLY GLY F . n 
F 1 116 ARG 116 115 115 ARG ARG F . n 
F 1 117 THR 117 116 116 THR THR F . n 
F 1 118 LEU 118 117 117 LEU LEU F . n 
F 1 119 VAL 119 118 118 VAL VAL F . n 
F 1 120 VAL 120 119 119 VAL VAL F . n 
F 1 121 HIS 121 120 120 HIS HIS F . n 
F 1 122 GLU 122 121 121 GLU GLU F . n 
F 1 123 LYS 123 122 122 LYS LYS F . n 
F 1 124 ALA 124 123 123 ALA ALA F . n 
F 1 125 ASP 125 124 124 ASP ASP F . n 
F 1 126 ASP 126 125 125 ASP ASP F . n 
F 1 127 LEU 127 126 126 LEU LEU F . n 
F 1 128 GLY 128 127 127 GLY GLY F . n 
F 1 129 LYS 129 128 128 LYS LYS F . n 
F 1 130 GLY 130 129 129 GLY GLY F . n 
F 1 131 GLY 131 130 130 GLY GLY F . n 
F 1 132 ASN 132 131 131 ASN ASN F . n 
F 1 133 GLU 133 132 132 GLU GLU F . n 
F 1 134 GLU 134 133 133 GLU GLU F . n 
F 1 135 SER 135 134 134 SER SER F . n 
F 1 136 THR 136 135 135 THR THR F . n 
F 1 137 LYS 137 136 136 LYS LYS F . n 
F 1 138 THR 138 137 137 THR THR F . n 
F 1 139 GLY 139 138 138 GLY GLY F . n 
F 1 140 ASN 140 139 139 ASN ASN F . n 
F 1 141 ALA 141 140 140 ALA ALA F . n 
F 1 142 GLY 142 141 141 GLY GLY F . n 
F 1 143 SER 143 142 142 SER SER F . n 
F 1 144 ARG 144 143 143 ARG ARG F . n 
F 1 145 LEU 145 144 144 LEU LEU F . n 
F 1 146 ALA 146 145 145 ALA ALA F . n 
F 1 147 CYS 147 146 146 CYS CYS F . n 
F 1 148 GLY 148 147 147 GLY GLY F . n 
F 1 149 VAL 149 148 148 VAL VAL F . n 
F 1 150 ILE 150 149 149 ILE ILE F . n 
F 1 151 GLY 151 150 150 GLY GLY F . n 
F 1 152 ILE 152 151 151 ILE ILE F . n 
F 1 153 ALA 153 152 152 ALA ALA F . n 
F 1 154 GLN 154 153 153 GLN GLN F . n 
G 1 1   MET 1   0   ?   ?   ?   G . n 
G 1 2   ALA 2   1   1   ALA ALA G . n 
G 1 3   THR 3   2   2   THR THR G . n 
G 1 4   LYS 4   3   3   LYS LYS G . n 
G 1 5   ALA 5   4   4   ALA ALA G . n 
G 1 6   VAL 6   5   5   VAL VAL G . n 
G 1 7   CYS 7   6   6   CYS CYS G . n 
G 1 8   VAL 8   7   7   VAL VAL G . n 
G 1 9   LEU 9   8   8   LEU LEU G . n 
G 1 10  LYS 10  9   9   LYS LYS G . n 
G 1 11  GLY 11  10  10  GLY GLY G . n 
G 1 12  ASP 12  11  11  ASP ASP G . n 
G 1 13  GLY 13  12  12  GLY GLY G . n 
G 1 14  PRO 14  13  13  PRO PRO G . n 
G 1 15  VAL 15  14  14  VAL VAL G . n 
G 1 16  GLN 16  15  15  GLN GLN G . n 
G 1 17  GLY 17  16  16  GLY GLY G . n 
G 1 18  ILE 18  17  17  ILE ILE G . n 
G 1 19  ILE 19  18  18  ILE ILE G . n 
G 1 20  ASN 20  19  19  ASN ASN G . n 
G 1 21  PHE 21  20  20  PHE PHE G . n 
G 1 22  GLU 22  21  21  GLU GLU G . n 
G 1 23  GLN 23  22  22  GLN GLN G . n 
G 1 24  LYS 24  23  23  LYS LYS G . n 
G 1 25  GLU 25  24  24  GLU GLU G . n 
G 1 26  SER 26  25  25  SER SER G . n 
G 1 27  ASN 27  26  26  ASN ASN G . n 
G 1 28  GLY 28  27  27  GLY GLY G . n 
G 1 29  PRO 29  28  28  PRO PRO G . n 
G 1 30  VAL 30  29  29  VAL VAL G . n 
G 1 31  LYS 31  30  30  LYS LYS G . n 
G 1 32  VAL 32  31  31  VAL VAL G . n 
G 1 33  TRP 33  32  32  TRP TRP G . n 
G 1 34  GLY 34  33  33  GLY GLY G . n 
G 1 35  SER 35  34  34  SER SER G . n 
G 1 36  ILE 36  35  35  ILE ILE G . n 
G 1 37  LYS 37  36  36  LYS LYS G . n 
G 1 38  GLY 38  37  37  GLY GLY G . n 
G 1 39  LEU 39  38  38  LEU LEU G . n 
G 1 40  THR 40  39  39  THR THR G . n 
G 1 41  GLU 41  40  40  GLU GLU G . n 
G 1 42  GLY 42  41  41  GLY GLY G . n 
G 1 43  LEU 43  42  42  LEU LEU G . n 
G 1 44  HIS 44  43  43  HIS HIS G . n 
G 1 45  GLY 45  44  44  GLY GLY G . n 
G 1 46  PHE 46  45  45  PHE PHE G . n 
G 1 47  HIS 47  46  46  HIS HIS G . n 
G 1 48  VAL 48  47  47  VAL VAL G . n 
G 1 49  HIS 49  48  48  HIS HIS G . n 
G 1 50  GLU 50  49  49  GLU GLU G . n 
G 1 51  PHE 51  50  50  PHE PHE G . n 
G 1 52  GLY 52  51  51  GLY GLY G . n 
G 1 53  ASP 53  52  52  ASP ASP G . n 
G 1 54  ASN 54  53  53  ASN ASN G . n 
G 1 55  THR 55  54  54  THR THR G . n 
G 1 56  ALA 56  55  55  ALA ALA G . n 
G 1 57  GLY 57  56  56  GLY GLY G . n 
G 1 58  CYS 58  57  57  CYS CYS G . n 
G 1 59  THR 59  58  58  THR THR G . n 
G 1 60  SER 60  59  59  SER SER G . n 
G 1 61  ALA 61  60  60  ALA ALA G . n 
G 1 62  GLY 62  61  61  GLY GLY G . n 
G 1 63  PRO 63  62  62  PRO PRO G . n 
G 1 64  HIS 64  63  63  HIS HIS G . n 
G 1 65  PHE 65  64  64  PHE PHE G . n 
G 1 66  ASN 66  65  65  ASN ASN G . n 
G 1 67  PRO 67  66  66  PRO PRO G . n 
G 1 68  LEU 68  67  67  LEU LEU G . n 
G 1 69  SER 69  68  68  SER SER G . n 
G 1 70  ARG 70  69  69  ARG ARG G . n 
G 1 71  LYS 71  70  70  LYS LYS G . n 
G 1 72  HIS 72  71  71  HIS HIS G . n 
G 1 73  GLY 73  72  72  GLY GLY G . n 
G 1 74  GLY 74  73  73  GLY GLY G . n 
G 1 75  PRO 75  74  74  PRO PRO G . n 
G 1 76  LYS 76  75  75  LYS LYS G . n 
G 1 77  ASP 77  76  76  ASP ASP G . n 
G 1 78  GLU 78  77  77  GLU GLU G . n 
G 1 79  GLU 79  78  78  GLU GLU G . n 
G 1 80  ARG 80  79  79  ARG ARG G . n 
G 1 81  HIS 81  80  80  HIS HIS G . n 
G 1 82  VAL 82  81  81  VAL VAL G . n 
G 1 83  GLY 83  82  82  GLY GLY G . n 
G 1 84  ASP 84  83  83  ASP ASP G . n 
G 1 85  LEU 85  84  84  LEU LEU G . n 
G 1 86  GLY 86  85  85  GLY GLY G . n 
G 1 87  ASN 87  86  86  ASN ASN G . n 
G 1 88  VAL 88  87  87  VAL VAL G . n 
G 1 89  THR 89  88  88  THR THR G . n 
G 1 90  ALA 90  89  89  ALA ALA G . n 
G 1 91  ASP 91  90  90  ASP ASP G . n 
G 1 92  LYS 92  91  91  LYS LYS G . n 
G 1 93  ASP 93  92  92  ASP ASP G . n 
G 1 94  GLY 94  93  93  GLY GLY G . n 
G 1 95  VAL 95  94  94  VAL VAL G . n 
G 1 96  ALA 96  95  95  ALA ALA G . n 
G 1 97  ASP 97  96  96  ASP ASP G . n 
G 1 98  VAL 98  97  97  VAL VAL G . n 
G 1 99  SER 99  98  98  SER SER G . n 
G 1 100 ILE 100 99  99  ILE ILE G . n 
G 1 101 GLU 101 100 100 GLU GLU G . n 
G 1 102 ASP 102 101 101 ASP ASP G . n 
G 1 103 SER 103 102 102 SER SER G . n 
G 1 104 VAL 104 103 103 VAL VAL G . n 
G 1 105 ILE 105 104 104 ILE ILE G . n 
G 1 106 SER 106 105 105 SER SER G . n 
G 1 107 LEU 107 106 106 LEU LEU G . n 
G 1 108 SER 108 107 107 SER SER G . n 
G 1 109 GLY 109 108 108 GLY GLY G . n 
G 1 110 ASP 110 109 109 ASP ASP G . n 
G 1 111 HIS 111 110 110 HIS HIS G . n 
G 1 112 CYS 112 111 111 CYS CYS G . n 
G 1 113 ILE 113 112 112 ILE ILE G . n 
G 1 114 ILE 114 113 113 ILE ILE G . n 
G 1 115 GLY 115 114 114 GLY GLY G . n 
G 1 116 ARG 116 115 115 ARG ARG G . n 
G 1 117 THR 117 116 116 THR THR G . n 
G 1 118 LEU 118 117 117 LEU LEU G . n 
G 1 119 VAL 119 118 118 VAL VAL G . n 
G 1 120 VAL 120 119 119 VAL VAL G . n 
G 1 121 HIS 121 120 120 HIS HIS G . n 
G 1 122 GLU 122 121 121 GLU GLU G . n 
G 1 123 LYS 123 122 122 LYS LYS G . n 
G 1 124 ALA 124 123 123 ALA ALA G . n 
G 1 125 ASP 125 124 124 ASP ASP G . n 
G 1 126 ASP 126 125 125 ASP ASP G . n 
G 1 127 LEU 127 126 126 LEU LEU G . n 
G 1 128 GLY 128 127 127 GLY GLY G . n 
G 1 129 LYS 129 128 128 LYS LYS G . n 
G 1 130 GLY 130 129 129 GLY GLY G . n 
G 1 131 GLY 131 130 130 GLY GLY G . n 
G 1 132 ASN 132 131 131 ASN ASN G . n 
G 1 133 GLU 133 132 132 GLU GLU G . n 
G 1 134 GLU 134 133 133 GLU GLU G . n 
G 1 135 SER 135 134 134 SER SER G . n 
G 1 136 THR 136 135 135 THR THR G . n 
G 1 137 LYS 137 136 136 LYS LYS G . n 
G 1 138 THR 138 137 137 THR THR G . n 
G 1 139 GLY 139 138 138 GLY GLY G . n 
G 1 140 ASN 140 139 139 ASN ASN G . n 
G 1 141 ALA 141 140 140 ALA ALA G . n 
G 1 142 GLY 142 141 141 GLY GLY G . n 
G 1 143 SER 143 142 142 SER SER G . n 
G 1 144 ARG 144 143 143 ARG ARG G . n 
G 1 145 LEU 145 144 144 LEU LEU G . n 
G 1 146 ALA 146 145 145 ALA ALA G . n 
G 1 147 CYS 147 146 146 CYS CYS G . n 
G 1 148 GLY 148 147 147 GLY GLY G . n 
G 1 149 VAL 149 148 148 VAL VAL G . n 
G 1 150 ILE 150 149 149 ILE ILE G . n 
G 1 151 GLY 151 150 150 GLY GLY G . n 
G 1 152 ILE 152 151 151 ILE ILE G . n 
G 1 153 ALA 153 152 152 ALA ALA G . n 
G 1 154 GLN 154 153 153 GLN GLN G . n 
H 1 1   MET 1   0   ?   ?   ?   H . n 
H 1 2   ALA 2   1   1   ALA ALA H . n 
H 1 3   THR 3   2   2   THR THR H . n 
H 1 4   LYS 4   3   3   LYS LYS H . n 
H 1 5   ALA 5   4   4   ALA ALA H . n 
H 1 6   VAL 6   5   5   VAL VAL H . n 
H 1 7   CYS 7   6   6   CYS CYS H . n 
H 1 8   VAL 8   7   7   VAL VAL H . n 
H 1 9   LEU 9   8   8   LEU LEU H . n 
H 1 10  LYS 10  9   9   LYS LYS H . n 
H 1 11  GLY 11  10  10  GLY GLY H . n 
H 1 12  ASP 12  11  11  ASP ASP H . n 
H 1 13  GLY 13  12  12  GLY GLY H . n 
H 1 14  PRO 14  13  13  PRO PRO H . n 
H 1 15  VAL 15  14  14  VAL VAL H . n 
H 1 16  GLN 16  15  15  GLN GLN H . n 
H 1 17  GLY 17  16  16  GLY GLY H . n 
H 1 18  ILE 18  17  17  ILE ILE H . n 
H 1 19  ILE 19  18  18  ILE ILE H . n 
H 1 20  ASN 20  19  19  ASN ASN H . n 
H 1 21  PHE 21  20  20  PHE PHE H . n 
H 1 22  GLU 22  21  21  GLU GLU H . n 
H 1 23  GLN 23  22  22  GLN GLN H . n 
H 1 24  LYS 24  23  23  LYS LYS H . n 
H 1 25  GLU 25  24  24  GLU GLU H . n 
H 1 26  SER 26  25  25  SER SER H . n 
H 1 27  ASN 27  26  26  ASN ASN H . n 
H 1 28  GLY 28  27  27  GLY GLY H . n 
H 1 29  PRO 29  28  28  PRO PRO H . n 
H 1 30  VAL 30  29  29  VAL VAL H . n 
H 1 31  LYS 31  30  30  LYS LYS H . n 
H 1 32  VAL 32  31  31  VAL VAL H . n 
H 1 33  TRP 33  32  32  TRP TRP H . n 
H 1 34  GLY 34  33  33  GLY GLY H . n 
H 1 35  SER 35  34  34  SER SER H . n 
H 1 36  ILE 36  35  35  ILE ILE H . n 
H 1 37  LYS 37  36  36  LYS LYS H . n 
H 1 38  GLY 38  37  37  GLY GLY H . n 
H 1 39  LEU 39  38  38  LEU LEU H . n 
H 1 40  THR 40  39  39  THR THR H . n 
H 1 41  GLU 41  40  40  GLU GLU H . n 
H 1 42  GLY 42  41  41  GLY GLY H . n 
H 1 43  LEU 43  42  42  LEU LEU H . n 
H 1 44  HIS 44  43  43  HIS HIS H . n 
H 1 45  GLY 45  44  44  GLY GLY H . n 
H 1 46  PHE 46  45  45  PHE PHE H . n 
H 1 47  HIS 47  46  46  HIS HIS H . n 
H 1 48  VAL 48  47  47  VAL VAL H . n 
H 1 49  HIS 49  48  48  HIS HIS H . n 
H 1 50  GLU 50  49  49  GLU GLU H . n 
H 1 51  PHE 51  50  50  PHE PHE H . n 
H 1 52  GLY 52  51  51  GLY GLY H . n 
H 1 53  ASP 53  52  52  ASP ASP H . n 
H 1 54  ASN 54  53  53  ASN ASN H . n 
H 1 55  THR 55  54  54  THR THR H . n 
H 1 56  ALA 56  55  55  ALA ALA H . n 
H 1 57  GLY 57  56  56  GLY GLY H . n 
H 1 58  CYS 58  57  57  CYS CYS H . n 
H 1 59  THR 59  58  58  THR THR H . n 
H 1 60  SER 60  59  59  SER SER H . n 
H 1 61  ALA 61  60  60  ALA ALA H . n 
H 1 62  GLY 62  61  61  GLY GLY H . n 
H 1 63  PRO 63  62  62  PRO PRO H . n 
H 1 64  HIS 64  63  63  HIS HIS H . n 
H 1 65  PHE 65  64  64  PHE PHE H . n 
H 1 66  ASN 66  65  65  ASN ASN H . n 
H 1 67  PRO 67  66  66  PRO PRO H . n 
H 1 68  LEU 68  67  67  LEU LEU H . n 
H 1 69  SER 69  68  68  SER SER H . n 
H 1 70  ARG 70  69  69  ARG ARG H . n 
H 1 71  LYS 71  70  70  LYS LYS H . n 
H 1 72  HIS 72  71  71  HIS HIS H . n 
H 1 73  GLY 73  72  72  GLY GLY H . n 
H 1 74  GLY 74  73  73  GLY GLY H . n 
H 1 75  PRO 75  74  74  PRO PRO H . n 
H 1 76  LYS 76  75  75  LYS LYS H . n 
H 1 77  ASP 77  76  76  ASP ASP H . n 
H 1 78  GLU 78  77  77  GLU GLU H . n 
H 1 79  GLU 79  78  78  GLU GLU H . n 
H 1 80  ARG 80  79  79  ARG ARG H . n 
H 1 81  HIS 81  80  80  HIS HIS H . n 
H 1 82  VAL 82  81  81  VAL VAL H . n 
H 1 83  GLY 83  82  82  GLY GLY H . n 
H 1 84  ASP 84  83  83  ASP ASP H . n 
H 1 85  LEU 85  84  84  LEU LEU H . n 
H 1 86  GLY 86  85  85  GLY GLY H . n 
H 1 87  ASN 87  86  86  ASN ASN H . n 
H 1 88  VAL 88  87  87  VAL VAL H . n 
H 1 89  THR 89  88  88  THR THR H . n 
H 1 90  ALA 90  89  89  ALA ALA H . n 
H 1 91  ASP 91  90  90  ASP ASP H . n 
H 1 92  LYS 92  91  91  LYS LYS H . n 
H 1 93  ASP 93  92  92  ASP ASP H . n 
H 1 94  GLY 94  93  93  GLY GLY H . n 
H 1 95  VAL 95  94  94  VAL VAL H . n 
H 1 96  ALA 96  95  95  ALA ALA H . n 
H 1 97  ASP 97  96  96  ASP ASP H . n 
H 1 98  VAL 98  97  97  VAL VAL H . n 
H 1 99  SER 99  98  98  SER SER H . n 
H 1 100 ILE 100 99  99  ILE ILE H . n 
H 1 101 GLU 101 100 100 GLU GLU H . n 
H 1 102 ASP 102 101 101 ASP ASP H . n 
H 1 103 SER 103 102 102 SER SER H . n 
H 1 104 VAL 104 103 103 VAL VAL H . n 
H 1 105 ILE 105 104 104 ILE ILE H . n 
H 1 106 SER 106 105 105 SER SER H . n 
H 1 107 LEU 107 106 106 LEU LEU H . n 
H 1 108 SER 108 107 107 SER SER H . n 
H 1 109 GLY 109 108 108 GLY GLY H . n 
H 1 110 ASP 110 109 109 ASP ASP H . n 
H 1 111 HIS 111 110 110 HIS HIS H . n 
H 1 112 CYS 112 111 111 CYS CYS H . n 
H 1 113 ILE 113 112 112 ILE ILE H . n 
H 1 114 ILE 114 113 113 ILE ILE H . n 
H 1 115 GLY 115 114 114 GLY GLY H . n 
H 1 116 ARG 116 115 115 ARG ARG H . n 
H 1 117 THR 117 116 116 THR THR H . n 
H 1 118 LEU 118 117 117 LEU LEU H . n 
H 1 119 VAL 119 118 118 VAL VAL H . n 
H 1 120 VAL 120 119 119 VAL VAL H . n 
H 1 121 HIS 121 120 120 HIS HIS H . n 
H 1 122 GLU 122 121 121 GLU GLU H . n 
H 1 123 LYS 123 122 122 LYS LYS H . n 
H 1 124 ALA 124 123 123 ALA ALA H . n 
H 1 125 ASP 125 124 124 ASP ASP H . n 
H 1 126 ASP 126 125 125 ASP ASP H . n 
H 1 127 LEU 127 126 126 LEU LEU H . n 
H 1 128 GLY 128 127 127 GLY GLY H . n 
H 1 129 LYS 129 128 128 LYS LYS H . n 
H 1 130 GLY 130 129 129 GLY GLY H . n 
H 1 131 GLY 131 130 130 GLY GLY H . n 
H 1 132 ASN 132 131 131 ASN ASN H . n 
H 1 133 GLU 133 132 132 GLU GLU H . n 
H 1 134 GLU 134 133 133 GLU GLU H . n 
H 1 135 SER 135 134 134 SER SER H . n 
H 1 136 THR 136 135 135 THR THR H . n 
H 1 137 LYS 137 136 136 LYS LYS H . n 
H 1 138 THR 138 137 137 THR THR H . n 
H 1 139 GLY 139 138 138 GLY GLY H . n 
H 1 140 ASN 140 139 139 ASN ASN H . n 
H 1 141 ALA 141 140 140 ALA ALA H . n 
H 1 142 GLY 142 141 141 GLY GLY H . n 
H 1 143 SER 143 142 142 SER SER H . n 
H 1 144 ARG 144 143 143 ARG ARG H . n 
H 1 145 LEU 145 144 144 LEU LEU H . n 
H 1 146 ALA 146 145 145 ALA ALA H . n 
H 1 147 CYS 147 146 146 CYS CYS H . n 
H 1 148 GLY 148 147 147 GLY GLY H . n 
H 1 149 VAL 149 148 148 VAL VAL H . n 
H 1 150 ILE 150 149 149 ILE ILE H . n 
H 1 151 GLY 151 150 150 GLY GLY H . n 
H 1 152 ILE 152 151 151 ILE ILE H . n 
H 1 153 ALA 153 152 152 ALA ALA H . n 
H 1 154 GLN 154 153 153 GLN GLN H . n 
I 1 1   MET 1   0   ?   ?   ?   I . n 
I 1 2   ALA 2   1   1   ALA ALA I . n 
I 1 3   THR 3   2   2   THR THR I . n 
I 1 4   LYS 4   3   3   LYS LYS I . n 
I 1 5   ALA 5   4   4   ALA ALA I . n 
I 1 6   VAL 6   5   5   VAL VAL I . n 
I 1 7   CYS 7   6   6   CYS CYS I . n 
I 1 8   VAL 8   7   7   VAL VAL I . n 
I 1 9   LEU 9   8   8   LEU LEU I . n 
I 1 10  LYS 10  9   9   LYS LYS I . n 
I 1 11  GLY 11  10  10  GLY GLY I . n 
I 1 12  ASP 12  11  11  ASP ASP I . n 
I 1 13  GLY 13  12  12  GLY GLY I . n 
I 1 14  PRO 14  13  13  PRO PRO I . n 
I 1 15  VAL 15  14  14  VAL VAL I . n 
I 1 16  GLN 16  15  15  GLN GLN I . n 
I 1 17  GLY 17  16  16  GLY GLY I . n 
I 1 18  ILE 18  17  17  ILE ILE I . n 
I 1 19  ILE 19  18  18  ILE ILE I . n 
I 1 20  ASN 20  19  19  ASN ASN I . n 
I 1 21  PHE 21  20  20  PHE PHE I . n 
I 1 22  GLU 22  21  21  GLU GLU I . n 
I 1 23  GLN 23  22  22  GLN GLN I . n 
I 1 24  LYS 24  23  23  LYS LYS I . n 
I 1 25  GLU 25  24  24  GLU GLU I . n 
I 1 26  SER 26  25  25  SER SER I . n 
I 1 27  ASN 27  26  26  ASN ASN I . n 
I 1 28  GLY 28  27  27  GLY GLY I . n 
I 1 29  PRO 29  28  28  PRO PRO I . n 
I 1 30  VAL 30  29  29  VAL VAL I . n 
I 1 31  LYS 31  30  30  LYS LYS I . n 
I 1 32  VAL 32  31  31  VAL VAL I . n 
I 1 33  TRP 33  32  32  TRP TRP I . n 
I 1 34  GLY 34  33  33  GLY GLY I . n 
I 1 35  SER 35  34  34  SER SER I . n 
I 1 36  ILE 36  35  35  ILE ILE I . n 
I 1 37  LYS 37  36  36  LYS LYS I . n 
I 1 38  GLY 38  37  37  GLY GLY I . n 
I 1 39  LEU 39  38  38  LEU LEU I . n 
I 1 40  THR 40  39  39  THR THR I . n 
I 1 41  GLU 41  40  40  GLU GLU I . n 
I 1 42  GLY 42  41  41  GLY GLY I . n 
I 1 43  LEU 43  42  42  LEU LEU I . n 
I 1 44  HIS 44  43  43  HIS HIS I . n 
I 1 45  GLY 45  44  44  GLY GLY I . n 
I 1 46  PHE 46  45  45  PHE PHE I . n 
I 1 47  HIS 47  46  46  HIS HIS I . n 
I 1 48  VAL 48  47  47  VAL VAL I . n 
I 1 49  HIS 49  48  48  HIS HIS I . n 
I 1 50  GLU 50  49  49  GLU GLU I . n 
I 1 51  PHE 51  50  50  PHE PHE I . n 
I 1 52  GLY 52  51  51  GLY GLY I . n 
I 1 53  ASP 53  52  52  ASP ASP I . n 
I 1 54  ASN 54  53  53  ASN ASN I . n 
I 1 55  THR 55  54  54  THR THR I . n 
I 1 56  ALA 56  55  55  ALA ALA I . n 
I 1 57  GLY 57  56  56  GLY GLY I . n 
I 1 58  CYS 58  57  57  CYS CYS I . n 
I 1 59  THR 59  58  58  THR THR I . n 
I 1 60  SER 60  59  59  SER SER I . n 
I 1 61  ALA 61  60  60  ALA ALA I . n 
I 1 62  GLY 62  61  61  GLY GLY I . n 
I 1 63  PRO 63  62  62  PRO PRO I . n 
I 1 64  HIS 64  63  63  HIS HIS I . n 
I 1 65  PHE 65  64  64  PHE PHE I . n 
I 1 66  ASN 66  65  65  ASN ASN I . n 
I 1 67  PRO 67  66  66  PRO PRO I . n 
I 1 68  LEU 68  67  67  LEU LEU I . n 
I 1 69  SER 69  68  68  SER SER I . n 
I 1 70  ARG 70  69  69  ARG ARG I . n 
I 1 71  LYS 71  70  70  LYS LYS I . n 
I 1 72  HIS 72  71  71  HIS HIS I . n 
I 1 73  GLY 73  72  72  GLY GLY I . n 
I 1 74  GLY 74  73  73  GLY GLY I . n 
I 1 75  PRO 75  74  74  PRO PRO I . n 
I 1 76  LYS 76  75  75  LYS LYS I . n 
I 1 77  ASP 77  76  76  ASP ASP I . n 
I 1 78  GLU 78  77  77  GLU GLU I . n 
I 1 79  GLU 79  78  78  GLU GLU I . n 
I 1 80  ARG 80  79  79  ARG ARG I . n 
I 1 81  HIS 81  80  80  HIS HIS I . n 
I 1 82  VAL 82  81  81  VAL VAL I . n 
I 1 83  GLY 83  82  82  GLY GLY I . n 
I 1 84  ASP 84  83  83  ASP ASP I . n 
I 1 85  LEU 85  84  84  LEU LEU I . n 
I 1 86  GLY 86  85  85  GLY GLY I . n 
I 1 87  ASN 87  86  86  ASN ASN I . n 
I 1 88  VAL 88  87  87  VAL VAL I . n 
I 1 89  THR 89  88  88  THR THR I . n 
I 1 90  ALA 90  89  89  ALA ALA I . n 
I 1 91  ASP 91  90  90  ASP ASP I . n 
I 1 92  LYS 92  91  91  LYS LYS I . n 
I 1 93  ASP 93  92  92  ASP ASP I . n 
I 1 94  GLY 94  93  93  GLY GLY I . n 
I 1 95  VAL 95  94  94  VAL VAL I . n 
I 1 96  ALA 96  95  95  ALA ALA I . n 
I 1 97  ASP 97  96  96  ASP ASP I . n 
I 1 98  VAL 98  97  97  VAL VAL I . n 
I 1 99  SER 99  98  98  SER SER I . n 
I 1 100 ILE 100 99  99  ILE ILE I . n 
I 1 101 GLU 101 100 100 GLU GLU I . n 
I 1 102 ASP 102 101 101 ASP ASP I . n 
I 1 103 SER 103 102 102 SER SER I . n 
I 1 104 VAL 104 103 103 VAL VAL I . n 
I 1 105 ILE 105 104 104 ILE ILE I . n 
I 1 106 SER 106 105 105 SER SER I . n 
I 1 107 LEU 107 106 106 LEU LEU I . n 
I 1 108 SER 108 107 107 SER SER I . n 
I 1 109 GLY 109 108 108 GLY GLY I . n 
I 1 110 ASP 110 109 109 ASP ASP I . n 
I 1 111 HIS 111 110 110 HIS HIS I . n 
I 1 112 CYS 112 111 111 CYS CYS I . n 
I 1 113 ILE 113 112 112 ILE ILE I . n 
I 1 114 ILE 114 113 113 ILE ILE I . n 
I 1 115 GLY 115 114 114 GLY GLY I . n 
I 1 116 ARG 116 115 115 ARG ARG I . n 
I 1 117 THR 117 116 116 THR THR I . n 
I 1 118 LEU 118 117 117 LEU LEU I . n 
I 1 119 VAL 119 118 118 VAL VAL I . n 
I 1 120 VAL 120 119 119 VAL VAL I . n 
I 1 121 HIS 121 120 120 HIS HIS I . n 
I 1 122 GLU 122 121 121 GLU GLU I . n 
I 1 123 LYS 123 122 122 LYS LYS I . n 
I 1 124 ALA 124 123 123 ALA ALA I . n 
I 1 125 ASP 125 124 124 ASP ASP I . n 
I 1 126 ASP 126 125 125 ASP ASP I . n 
I 1 127 LEU 127 126 126 LEU LEU I . n 
I 1 128 GLY 128 127 127 GLY GLY I . n 
I 1 129 LYS 129 128 128 LYS LYS I . n 
I 1 130 GLY 130 129 129 GLY GLY I . n 
I 1 131 GLY 131 130 130 GLY GLY I . n 
I 1 132 ASN 132 131 131 ASN ASN I . n 
I 1 133 GLU 133 132 132 GLU GLU I . n 
I 1 134 GLU 134 133 133 GLU GLU I . n 
I 1 135 SER 135 134 134 SER SER I . n 
I 1 136 THR 136 135 135 THR THR I . n 
I 1 137 LYS 137 136 136 LYS LYS I . n 
I 1 138 THR 138 137 137 THR THR I . n 
I 1 139 GLY 139 138 138 GLY GLY I . n 
I 1 140 ASN 140 139 139 ASN ASN I . n 
I 1 141 ALA 141 140 140 ALA ALA I . n 
I 1 142 GLY 142 141 141 GLY GLY I . n 
I 1 143 SER 143 142 142 SER SER I . n 
I 1 144 ARG 144 143 143 ARG ARG I . n 
I 1 145 LEU 145 144 144 LEU LEU I . n 
I 1 146 ALA 146 145 145 ALA ALA I . n 
I 1 147 CYS 147 146 146 CYS CYS I . n 
I 1 148 GLY 148 147 147 GLY GLY I . n 
I 1 149 VAL 149 148 148 VAL VAL I . n 
I 1 150 ILE 150 149 149 ILE ILE I . n 
I 1 151 GLY 151 150 150 GLY GLY I . n 
I 1 152 ILE 152 151 151 ILE ILE I . n 
I 1 153 ALA 153 152 152 ALA ALA I . n 
I 1 154 GLN 154 153 153 GLN GLN I . n 
J 1 1   MET 1   0   ?   ?   ?   J . n 
J 1 2   ALA 2   1   1   ALA ALA J . n 
J 1 3   THR 3   2   2   THR THR J . n 
J 1 4   LYS 4   3   3   LYS LYS J . n 
J 1 5   ALA 5   4   4   ALA ALA J . n 
J 1 6   VAL 6   5   5   VAL VAL J . n 
J 1 7   CYS 7   6   6   CYS CYS J . n 
J 1 8   VAL 8   7   7   VAL VAL J . n 
J 1 9   LEU 9   8   8   LEU LEU J . n 
J 1 10  LYS 10  9   9   LYS LYS J . n 
J 1 11  GLY 11  10  10  GLY GLY J . n 
J 1 12  ASP 12  11  11  ASP ASP J . n 
J 1 13  GLY 13  12  12  GLY GLY J . n 
J 1 14  PRO 14  13  13  PRO PRO J . n 
J 1 15  VAL 15  14  14  VAL VAL J . n 
J 1 16  GLN 16  15  15  GLN GLN J . n 
J 1 17  GLY 17  16  16  GLY GLY J . n 
J 1 18  ILE 18  17  17  ILE ILE J . n 
J 1 19  ILE 19  18  18  ILE ILE J . n 
J 1 20  ASN 20  19  19  ASN ASN J . n 
J 1 21  PHE 21  20  20  PHE PHE J . n 
J 1 22  GLU 22  21  21  GLU GLU J . n 
J 1 23  GLN 23  22  22  GLN GLN J . n 
J 1 24  LYS 24  23  23  LYS LYS J . n 
J 1 25  GLU 25  24  24  GLU GLU J . n 
J 1 26  SER 26  25  25  SER SER J . n 
J 1 27  ASN 27  26  26  ASN ASN J . n 
J 1 28  GLY 28  27  27  GLY GLY J . n 
J 1 29  PRO 29  28  28  PRO PRO J . n 
J 1 30  VAL 30  29  29  VAL VAL J . n 
J 1 31  LYS 31  30  30  LYS LYS J . n 
J 1 32  VAL 32  31  31  VAL VAL J . n 
J 1 33  TRP 33  32  32  TRP TRP J . n 
J 1 34  GLY 34  33  33  GLY GLY J . n 
J 1 35  SER 35  34  34  SER SER J . n 
J 1 36  ILE 36  35  35  ILE ILE J . n 
J 1 37  LYS 37  36  36  LYS LYS J . n 
J 1 38  GLY 38  37  37  GLY GLY J . n 
J 1 39  LEU 39  38  38  LEU LEU J . n 
J 1 40  THR 40  39  39  THR THR J . n 
J 1 41  GLU 41  40  40  GLU GLU J . n 
J 1 42  GLY 42  41  41  GLY GLY J . n 
J 1 43  LEU 43  42  42  LEU LEU J . n 
J 1 44  HIS 44  43  43  HIS HIS J . n 
J 1 45  GLY 45  44  44  GLY GLY J . n 
J 1 46  PHE 46  45  45  PHE PHE J . n 
J 1 47  HIS 47  46  46  HIS HIS J . n 
J 1 48  VAL 48  47  47  VAL VAL J . n 
J 1 49  HIS 49  48  48  HIS HIS J . n 
J 1 50  GLU 50  49  49  GLU GLU J . n 
J 1 51  PHE 51  50  50  PHE PHE J . n 
J 1 52  GLY 52  51  51  GLY GLY J . n 
J 1 53  ASP 53  52  52  ASP ASP J . n 
J 1 54  ASN 54  53  53  ASN ASN J . n 
J 1 55  THR 55  54  54  THR THR J . n 
J 1 56  ALA 56  55  55  ALA ALA J . n 
J 1 57  GLY 57  56  56  GLY GLY J . n 
J 1 58  CYS 58  57  57  CYS CYS J . n 
J 1 59  THR 59  58  58  THR THR J . n 
J 1 60  SER 60  59  59  SER SER J . n 
J 1 61  ALA 61  60  60  ALA ALA J . n 
J 1 62  GLY 62  61  61  GLY GLY J . n 
J 1 63  PRO 63  62  62  PRO PRO J . n 
J 1 64  HIS 64  63  63  HIS HIS J . n 
J 1 65  PHE 65  64  64  PHE PHE J . n 
J 1 66  ASN 66  65  65  ASN ASN J . n 
J 1 67  PRO 67  66  66  PRO PRO J . n 
J 1 68  LEU 68  67  67  LEU LEU J . n 
J 1 69  SER 69  68  68  SER SER J . n 
J 1 70  ARG 70  69  69  ARG ARG J . n 
J 1 71  LYS 71  70  70  LYS LYS J . n 
J 1 72  HIS 72  71  71  HIS HIS J . n 
J 1 73  GLY 73  72  72  GLY GLY J . n 
J 1 74  GLY 74  73  73  GLY GLY J . n 
J 1 75  PRO 75  74  74  PRO PRO J . n 
J 1 76  LYS 76  75  75  LYS LYS J . n 
J 1 77  ASP 77  76  76  ASP ASP J . n 
J 1 78  GLU 78  77  77  GLU GLU J . n 
J 1 79  GLU 79  78  78  GLU GLU J . n 
J 1 80  ARG 80  79  79  ARG ARG J . n 
J 1 81  HIS 81  80  80  HIS HIS J . n 
J 1 82  VAL 82  81  81  VAL VAL J . n 
J 1 83  GLY 83  82  82  GLY GLY J . n 
J 1 84  ASP 84  83  83  ASP ASP J . n 
J 1 85  LEU 85  84  84  LEU LEU J . n 
J 1 86  GLY 86  85  85  GLY GLY J . n 
J 1 87  ASN 87  86  86  ASN ASN J . n 
J 1 88  VAL 88  87  87  VAL VAL J . n 
J 1 89  THR 89  88  88  THR THR J . n 
J 1 90  ALA 90  89  89  ALA ALA J . n 
J 1 91  ASP 91  90  90  ASP ASP J . n 
J 1 92  LYS 92  91  91  LYS LYS J . n 
J 1 93  ASP 93  92  92  ASP ASP J . n 
J 1 94  GLY 94  93  93  GLY GLY J . n 
J 1 95  VAL 95  94  94  VAL VAL J . n 
J 1 96  ALA 96  95  95  ALA ALA J . n 
J 1 97  ASP 97  96  96  ASP ASP J . n 
J 1 98  VAL 98  97  97  VAL VAL J . n 
J 1 99  SER 99  98  98  SER SER J . n 
J 1 100 ILE 100 99  99  ILE ILE J . n 
J 1 101 GLU 101 100 100 GLU GLU J . n 
J 1 102 ASP 102 101 101 ASP ASP J . n 
J 1 103 SER 103 102 102 SER SER J . n 
J 1 104 VAL 104 103 103 VAL VAL J . n 
J 1 105 ILE 105 104 104 ILE ILE J . n 
J 1 106 SER 106 105 105 SER SER J . n 
J 1 107 LEU 107 106 106 LEU LEU J . n 
J 1 108 SER 108 107 107 SER SER J . n 
J 1 109 GLY 109 108 108 GLY GLY J . n 
J 1 110 ASP 110 109 109 ASP ASP J . n 
J 1 111 HIS 111 110 110 HIS HIS J . n 
J 1 112 CYS 112 111 111 CYS CYS J . n 
J 1 113 ILE 113 112 112 ILE ILE J . n 
J 1 114 ILE 114 113 113 ILE ILE J . n 
J 1 115 GLY 115 114 114 GLY GLY J . n 
J 1 116 ARG 116 115 115 ARG ARG J . n 
J 1 117 THR 117 116 116 THR THR J . n 
J 1 118 LEU 118 117 117 LEU LEU J . n 
J 1 119 VAL 119 118 118 VAL VAL J . n 
J 1 120 VAL 120 119 119 VAL VAL J . n 
J 1 121 HIS 121 120 120 HIS HIS J . n 
J 1 122 GLU 122 121 121 GLU GLU J . n 
J 1 123 LYS 123 122 122 LYS LYS J . n 
J 1 124 ALA 124 123 123 ALA ALA J . n 
J 1 125 ASP 125 124 124 ASP ASP J . n 
J 1 126 ASP 126 125 125 ASP ASP J . n 
J 1 127 LEU 127 126 126 LEU LEU J . n 
J 1 128 GLY 128 127 127 GLY GLY J . n 
J 1 129 LYS 129 128 128 LYS LYS J . n 
J 1 130 GLY 130 129 129 GLY GLY J . n 
J 1 131 GLY 131 130 130 GLY GLY J . n 
J 1 132 ASN 132 131 131 ASN ASN J . n 
J 1 133 GLU 133 132 132 GLU GLU J . n 
J 1 134 GLU 134 133 133 GLU GLU J . n 
J 1 135 SER 135 134 134 SER SER J . n 
J 1 136 THR 136 135 135 THR THR J . n 
J 1 137 LYS 137 136 136 LYS LYS J . n 
J 1 138 THR 138 137 137 THR THR J . n 
J 1 139 GLY 139 138 138 GLY GLY J . n 
J 1 140 ASN 140 139 139 ASN ASN J . n 
J 1 141 ALA 141 140 140 ALA ALA J . n 
J 1 142 GLY 142 141 141 GLY GLY J . n 
J 1 143 SER 143 142 142 SER SER J . n 
J 1 144 ARG 144 143 143 ARG ARG J . n 
J 1 145 LEU 145 144 144 LEU LEU J . n 
J 1 146 ALA 146 145 145 ALA ALA J . n 
J 1 147 CYS 147 146 146 CYS CYS J . n 
J 1 148 GLY 148 147 147 GLY GLY J . n 
J 1 149 VAL 149 148 148 VAL VAL J . n 
J 1 150 ILE 150 149 149 ILE ILE J . n 
J 1 151 GLY 151 150 150 GLY GLY J . n 
J 1 152 ILE 152 151 151 ILE ILE J . n 
J 1 153 ALA 153 152 152 ALA ALA J . n 
J 1 154 GLN 154 153 153 GLN GLN J . 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 
K  2 CU  1   154  154  CU  CU  A . 
L  3 ZN  1   155  155  ZN  ZN  A . 
M  4 CO3 1   156  156  CO3 CO3 A . 
N  2 CU  1   154  154  CU  CU  B . 
O  3 ZN  1   155  155  ZN  ZN  B . 
P  4 CO3 1   156  156  CO3 CO3 B . 
Q  2 CU  1   154  154  CU  CU  C . 
R  3 ZN  1   155  155  ZN  ZN  C . 
S  4 CO3 1   156  156  CO3 CO3 C . 
T  2 CU  1   154  154  CU  CU  D . 
U  3 ZN  1   155  155  ZN  ZN  D . 
V  4 CO3 1   156  156  CO3 CO3 D . 
W  2 CU  1   154  154  CU  CU  E . 
X  3 ZN  1   155  155  ZN  ZN  E . 
Y  4 CO3 1   156  156  CO3 CO3 E . 
Z  2 CU  1   154  154  CU  CU  F . 
AA 3 ZN  1   155  155  ZN  ZN  F . 
BA 4 CO3 1   156  156  CO3 CO3 F . 
CA 5 SO4 1   1154 1154 SO4 SO4 F . 
DA 5 SO4 1   1155 1155 SO4 SO4 F . 
EA 2 CU  1   154  154  CU  CU  G . 
FA 3 ZN  1   155  155  ZN  ZN  G . 
GA 4 CO3 1   156  156  CO3 CO3 G . 
HA 5 SO4 1   1154 1154 SO4 SO4 G . 
IA 2 CU  1   154  154  CU  CU  H . 
JA 3 ZN  1   155  155  ZN  ZN  H . 
KA 4 CO3 1   156  156  CO3 CO3 H . 
LA 2 CU  1   154  154  CU  CU  I . 
MA 3 ZN  1   155  155  ZN  ZN  I . 
NA 4 CO3 1   156  156  CO3 CO3 I . 
OA 2 CU  1   154  154  CU  CU  J . 
PA 3 ZN  1   155  155  ZN  ZN  J . 
QA 4 CO3 1   156  156  CO3 CO3 J . 
RA 5 SO4 1   1154 1154 SO4 SO4 J . 
SA 5 SO4 1   1155 1155 SO4 SO4 J . 
TA 6 HOH 1   2001 2001 HOH HOH A . 
TA 6 HOH 2   2002 2002 HOH HOH A . 
TA 6 HOH 3   2003 2003 HOH HOH A . 
TA 6 HOH 4   2004 2004 HOH HOH A . 
TA 6 HOH 5   2005 2005 HOH HOH A . 
TA 6 HOH 6   2006 2006 HOH HOH A . 
TA 6 HOH 7   2007 2007 HOH HOH A . 
TA 6 HOH 8   2008 2008 HOH HOH A . 
TA 6 HOH 9   2009 2009 HOH HOH A . 
TA 6 HOH 10  2010 2010 HOH HOH A . 
TA 6 HOH 11  2011 2011 HOH HOH A . 
TA 6 HOH 12  2012 2012 HOH HOH A . 
TA 6 HOH 13  2013 2013 HOH HOH A . 
TA 6 HOH 14  2014 2014 HOH HOH A . 
TA 6 HOH 15  2015 2015 HOH HOH A . 
TA 6 HOH 16  2016 2016 HOH HOH A . 
TA 6 HOH 17  2017 2017 HOH HOH A . 
TA 6 HOH 18  2018 2018 HOH HOH A . 
TA 6 HOH 19  2019 2019 HOH HOH A . 
TA 6 HOH 20  2020 2020 HOH HOH A . 
TA 6 HOH 21  2021 2021 HOH HOH A . 
TA 6 HOH 22  2022 2022 HOH HOH A . 
TA 6 HOH 23  2023 2023 HOH HOH A . 
TA 6 HOH 24  2024 2024 HOH HOH A . 
TA 6 HOH 25  2025 2025 HOH HOH A . 
TA 6 HOH 26  2026 2026 HOH HOH A . 
TA 6 HOH 27  2027 2027 HOH HOH A . 
TA 6 HOH 28  2028 2028 HOH HOH A . 
TA 6 HOH 29  2029 2029 HOH HOH A . 
TA 6 HOH 30  2030 2030 HOH HOH A . 
TA 6 HOH 31  2031 2031 HOH HOH A . 
TA 6 HOH 32  2032 2032 HOH HOH A . 
TA 6 HOH 33  2033 2033 HOH HOH A . 
TA 6 HOH 34  2034 2034 HOH HOH A . 
TA 6 HOH 35  2035 2035 HOH HOH A . 
TA 6 HOH 36  2036 2036 HOH HOH A . 
TA 6 HOH 37  2037 2037 HOH HOH A . 
TA 6 HOH 38  2038 2038 HOH HOH A . 
TA 6 HOH 39  2039 2039 HOH HOH A . 
TA 6 HOH 40  2040 2040 HOH HOH A . 
TA 6 HOH 41  2041 2041 HOH HOH A . 
TA 6 HOH 42  2042 2042 HOH HOH A . 
TA 6 HOH 43  2043 2043 HOH HOH A . 
TA 6 HOH 44  2044 2044 HOH HOH A . 
TA 6 HOH 45  2045 2045 HOH HOH A . 
TA 6 HOH 46  2046 2046 HOH HOH A . 
TA 6 HOH 47  2047 2047 HOH HOH A . 
TA 6 HOH 48  2048 2048 HOH HOH A . 
TA 6 HOH 49  2049 2049 HOH HOH A . 
TA 6 HOH 50  2050 2050 HOH HOH A . 
TA 6 HOH 51  2051 2051 HOH HOH A . 
TA 6 HOH 52  2052 2052 HOH HOH A . 
TA 6 HOH 53  2053 2053 HOH HOH A . 
TA 6 HOH 54  2054 2054 HOH HOH A . 
TA 6 HOH 55  2055 2055 HOH HOH A . 
TA 6 HOH 56  2056 2056 HOH HOH A . 
TA 6 HOH 57  2057 2057 HOH HOH A . 
TA 6 HOH 58  2058 2058 HOH HOH A . 
TA 6 HOH 59  2059 2059 HOH HOH A . 
TA 6 HOH 60  2060 2060 HOH HOH A . 
TA 6 HOH 61  2061 2061 HOH HOH A . 
TA 6 HOH 62  2062 2062 HOH HOH A . 
TA 6 HOH 63  2063 2063 HOH HOH A . 
TA 6 HOH 64  2064 2064 HOH HOH A . 
TA 6 HOH 65  2065 2065 HOH HOH A . 
TA 6 HOH 66  2066 2066 HOH HOH A . 
TA 6 HOH 67  2067 2067 HOH HOH A . 
TA 6 HOH 68  2068 2068 HOH HOH A . 
TA 6 HOH 69  2069 2069 HOH HOH A . 
TA 6 HOH 70  2070 2070 HOH HOH A . 
TA 6 HOH 71  2071 2071 HOH HOH A . 
TA 6 HOH 72  2072 2072 HOH HOH A . 
TA 6 HOH 73  2073 2073 HOH HOH A . 
TA 6 HOH 74  2074 2074 HOH HOH A . 
TA 6 HOH 75  2075 2075 HOH HOH A . 
TA 6 HOH 76  2076 2076 HOH HOH A . 
TA 6 HOH 77  2077 2077 HOH HOH A . 
TA 6 HOH 78  2078 2078 HOH HOH A . 
TA 6 HOH 79  2079 2079 HOH HOH A . 
TA 6 HOH 80  2080 2080 HOH HOH A . 
TA 6 HOH 81  2081 2081 HOH HOH A . 
TA 6 HOH 82  2082 2082 HOH HOH A . 
TA 6 HOH 83  2083 2083 HOH HOH A . 
TA 6 HOH 84  2084 2084 HOH HOH A . 
TA 6 HOH 85  2085 2085 HOH HOH A . 
TA 6 HOH 86  2086 2086 HOH HOH A . 
TA 6 HOH 87  2087 2087 HOH HOH A . 
TA 6 HOH 88  2088 2088 HOH HOH A . 
TA 6 HOH 89  2089 2089 HOH HOH A . 
TA 6 HOH 90  2090 2090 HOH HOH A . 
TA 6 HOH 91  2091 2091 HOH HOH A . 
TA 6 HOH 92  2092 2092 HOH HOH A . 
TA 6 HOH 93  2093 2093 HOH HOH A . 
TA 6 HOH 94  2094 2094 HOH HOH A . 
TA 6 HOH 95  2095 2095 HOH HOH A . 
TA 6 HOH 96  2096 2096 HOH HOH A . 
TA 6 HOH 97  2097 2097 HOH HOH A . 
TA 6 HOH 98  2098 2098 HOH HOH A . 
TA 6 HOH 99  2099 2099 HOH HOH A . 
TA 6 HOH 100 2100 2100 HOH HOH A . 
TA 6 HOH 101 2101 2101 HOH HOH A . 
TA 6 HOH 102 2102 2102 HOH HOH A . 
TA 6 HOH 103 2103 2103 HOH HOH A . 
TA 6 HOH 104 2104 2104 HOH HOH A . 
TA 6 HOH 105 2105 2105 HOH HOH A . 
TA 6 HOH 106 2106 2106 HOH HOH A . 
TA 6 HOH 107 2107 2107 HOH HOH A . 
TA 6 HOH 108 2108 2108 HOH HOH A . 
TA 6 HOH 109 2109 2109 HOH HOH A . 
TA 6 HOH 110 2110 2110 HOH HOH A . 
TA 6 HOH 111 2111 2111 HOH HOH A . 
TA 6 HOH 112 2112 2112 HOH HOH A . 
TA 6 HOH 113 2113 2113 HOH HOH A . 
TA 6 HOH 114 2114 2114 HOH HOH A . 
TA 6 HOH 115 2115 2115 HOH HOH A . 
TA 6 HOH 116 2116 2116 HOH HOH A . 
TA 6 HOH 117 2117 2117 HOH HOH A . 
TA 6 HOH 118 2118 2118 HOH HOH A . 
TA 6 HOH 119 2119 2119 HOH HOH A . 
TA 6 HOH 120 2120 2120 HOH HOH A . 
TA 6 HOH 121 2121 2121 HOH HOH A . 
TA 6 HOH 122 2122 2122 HOH HOH A . 
TA 6 HOH 123 2123 2123 HOH HOH A . 
TA 6 HOH 124 2124 2124 HOH HOH A . 
TA 6 HOH 125 2125 2125 HOH HOH A . 
TA 6 HOH 126 2126 2126 HOH HOH A . 
TA 6 HOH 127 2127 2127 HOH HOH A . 
TA 6 HOH 128 2128 2128 HOH HOH A . 
TA 6 HOH 129 2129 2129 HOH HOH A . 
TA 6 HOH 130 2130 2130 HOH HOH A . 
TA 6 HOH 131 2131 2131 HOH HOH A . 
TA 6 HOH 132 2132 2132 HOH HOH A . 
TA 6 HOH 133 2133 2133 HOH HOH A . 
TA 6 HOH 134 2134 2134 HOH HOH A . 
TA 6 HOH 135 2135 2135 HOH HOH A . 
TA 6 HOH 136 2136 2136 HOH HOH A . 
TA 6 HOH 137 2137 2137 HOH HOH A . 
TA 6 HOH 138 2138 2138 HOH HOH A . 
TA 6 HOH 139 2139 2139 HOH HOH A . 
TA 6 HOH 140 2140 2140 HOH HOH A . 
TA 6 HOH 141 2141 2141 HOH HOH A . 
TA 6 HOH 142 2142 2142 HOH HOH A . 
TA 6 HOH 143 2143 2143 HOH HOH A . 
TA 6 HOH 144 2144 2144 HOH HOH A . 
TA 6 HOH 145 2145 2145 HOH HOH A . 
TA 6 HOH 146 2146 2146 HOH HOH A . 
TA 6 HOH 147 2147 2147 HOH HOH A . 
TA 6 HOH 148 2148 2148 HOH HOH A . 
TA 6 HOH 149 2149 2149 HOH HOH A . 
TA 6 HOH 150 2150 2150 HOH HOH A . 
TA 6 HOH 151 2151 2151 HOH HOH A . 
TA 6 HOH 152 2152 2152 HOH HOH A . 
TA 6 HOH 153 2153 2153 HOH HOH A . 
TA 6 HOH 154 2154 2154 HOH HOH A . 
TA 6 HOH 155 2155 2155 HOH HOH A . 
TA 6 HOH 156 2156 2156 HOH HOH A . 
TA 6 HOH 157 2157 2157 HOH HOH A . 
TA 6 HOH 158 2158 2158 HOH HOH A . 
TA 6 HOH 159 2159 2159 HOH HOH A . 
TA 6 HOH 160 2160 2160 HOH HOH A . 
TA 6 HOH 161 2161 2161 HOH HOH A . 
TA 6 HOH 162 2162 2162 HOH HOH A . 
TA 6 HOH 163 2163 2163 HOH HOH A . 
TA 6 HOH 164 2164 2164 HOH HOH A . 
TA 6 HOH 165 2165 2165 HOH HOH A . 
TA 6 HOH 166 2166 2166 HOH HOH A . 
UA 6 HOH 1   2001 2001 HOH HOH B . 
UA 6 HOH 2   2002 2002 HOH HOH B . 
UA 6 HOH 3   2003 2003 HOH HOH B . 
UA 6 HOH 4   2004 2004 HOH HOH B . 
UA 6 HOH 5   2005 2005 HOH HOH B . 
UA 6 HOH 6   2006 2006 HOH HOH B . 
UA 6 HOH 7   2007 2007 HOH HOH B . 
UA 6 HOH 8   2008 2008 HOH HOH B . 
UA 6 HOH 9   2009 2009 HOH HOH B . 
UA 6 HOH 10  2010 2010 HOH HOH B . 
UA 6 HOH 11  2011 2011 HOH HOH B . 
UA 6 HOH 12  2012 2012 HOH HOH B . 
UA 6 HOH 13  2013 2013 HOH HOH B . 
UA 6 HOH 14  2014 2014 HOH HOH B . 
UA 6 HOH 15  2015 2015 HOH HOH B . 
UA 6 HOH 16  2016 2016 HOH HOH B . 
UA 6 HOH 17  2017 2017 HOH HOH B . 
UA 6 HOH 18  2018 2018 HOH HOH B . 
UA 6 HOH 19  2019 2019 HOH HOH B . 
UA 6 HOH 20  2020 2020 HOH HOH B . 
UA 6 HOH 21  2021 2021 HOH HOH B . 
UA 6 HOH 22  2022 2022 HOH HOH B . 
UA 6 HOH 23  2023 2023 HOH HOH B . 
UA 6 HOH 24  2024 2024 HOH HOH B . 
UA 6 HOH 25  2025 2025 HOH HOH B . 
UA 6 HOH 26  2026 2026 HOH HOH B . 
UA 6 HOH 27  2027 2027 HOH HOH B . 
UA 6 HOH 28  2028 2028 HOH HOH B . 
UA 6 HOH 29  2029 2029 HOH HOH B . 
UA 6 HOH 30  2030 2030 HOH HOH B . 
UA 6 HOH 31  2031 2031 HOH HOH B . 
UA 6 HOH 32  2032 2032 HOH HOH B . 
UA 6 HOH 33  2033 2033 HOH HOH B . 
UA 6 HOH 34  2034 2034 HOH HOH B . 
UA 6 HOH 35  2035 2035 HOH HOH B . 
UA 6 HOH 36  2036 2036 HOH HOH B . 
UA 6 HOH 37  2037 2037 HOH HOH B . 
UA 6 HOH 38  2038 2038 HOH HOH B . 
UA 6 HOH 39  2039 2039 HOH HOH B . 
UA 6 HOH 40  2040 2040 HOH HOH B . 
UA 6 HOH 41  2041 2041 HOH HOH B . 
UA 6 HOH 42  2042 2042 HOH HOH B . 
UA 6 HOH 43  2043 2043 HOH HOH B . 
UA 6 HOH 44  2044 2044 HOH HOH B . 
UA 6 HOH 45  2045 2045 HOH HOH B . 
UA 6 HOH 46  2046 2046 HOH HOH B . 
UA 6 HOH 47  2047 2047 HOH HOH B . 
UA 6 HOH 48  2048 2048 HOH HOH B . 
UA 6 HOH 49  2049 2049 HOH HOH B . 
UA 6 HOH 50  2050 2050 HOH HOH B . 
UA 6 HOH 51  2051 2051 HOH HOH B . 
UA 6 HOH 52  2052 2052 HOH HOH B . 
UA 6 HOH 53  2053 2053 HOH HOH B . 
UA 6 HOH 54  2054 2054 HOH HOH B . 
UA 6 HOH 55  2055 2055 HOH HOH B . 
UA 6 HOH 56  2056 2056 HOH HOH B . 
UA 6 HOH 57  2057 2057 HOH HOH B . 
UA 6 HOH 58  2058 2058 HOH HOH B . 
UA 6 HOH 59  2059 2059 HOH HOH B . 
UA 6 HOH 60  2060 2060 HOH HOH B . 
UA 6 HOH 61  2061 2061 HOH HOH B . 
UA 6 HOH 62  2062 2062 HOH HOH B . 
UA 6 HOH 63  2063 2063 HOH HOH B . 
UA 6 HOH 64  2064 2064 HOH HOH B . 
UA 6 HOH 65  2065 2065 HOH HOH B . 
UA 6 HOH 66  2066 2066 HOH HOH B . 
UA 6 HOH 67  2067 2067 HOH HOH B . 
UA 6 HOH 68  2068 2068 HOH HOH B . 
UA 6 HOH 69  2069 2069 HOH HOH B . 
UA 6 HOH 70  2070 2070 HOH HOH B . 
UA 6 HOH 71  2071 2071 HOH HOH B . 
UA 6 HOH 72  2072 2072 HOH HOH B . 
UA 6 HOH 73  2073 2073 HOH HOH B . 
UA 6 HOH 74  2074 2074 HOH HOH B . 
UA 6 HOH 75  2075 2075 HOH HOH B . 
UA 6 HOH 76  2076 2076 HOH HOH B . 
UA 6 HOH 77  2077 2077 HOH HOH B . 
UA 6 HOH 78  2078 2078 HOH HOH B . 
UA 6 HOH 79  2079 2079 HOH HOH B . 
UA 6 HOH 80  2080 2080 HOH HOH B . 
UA 6 HOH 81  2081 2081 HOH HOH B . 
UA 6 HOH 82  2082 2082 HOH HOH B . 
UA 6 HOH 83  2083 2083 HOH HOH B . 
UA 6 HOH 84  2084 2084 HOH HOH B . 
UA 6 HOH 85  2085 2085 HOH HOH B . 
UA 6 HOH 86  2086 2086 HOH HOH B . 
UA 6 HOH 87  2087 2087 HOH HOH B . 
UA 6 HOH 88  2088 2088 HOH HOH B . 
UA 6 HOH 89  2089 2089 HOH HOH B . 
UA 6 HOH 90  2090 2090 HOH HOH B . 
UA 6 HOH 91  2091 2091 HOH HOH B . 
UA 6 HOH 92  2092 2092 HOH HOH B . 
UA 6 HOH 93  2093 2093 HOH HOH B . 
UA 6 HOH 94  2094 2094 HOH HOH B . 
UA 6 HOH 95  2095 2095 HOH HOH B . 
UA 6 HOH 96  2096 2096 HOH HOH B . 
UA 6 HOH 97  2097 2097 HOH HOH B . 
UA 6 HOH 98  2098 2098 HOH HOH B . 
UA 6 HOH 99  2099 2099 HOH HOH B . 
UA 6 HOH 100 2100 2100 HOH HOH B . 
UA 6 HOH 101 2101 2101 HOH HOH B . 
UA 6 HOH 102 2102 2102 HOH HOH B . 
UA 6 HOH 103 2103 2103 HOH HOH B . 
UA 6 HOH 104 2104 2104 HOH HOH B . 
UA 6 HOH 105 2105 2105 HOH HOH B . 
UA 6 HOH 106 2106 2106 HOH HOH B . 
UA 6 HOH 107 2107 2107 HOH HOH B . 
UA 6 HOH 108 2108 2108 HOH HOH B . 
UA 6 HOH 109 2109 2109 HOH HOH B . 
UA 6 HOH 110 2110 2110 HOH HOH B . 
UA 6 HOH 111 2111 2111 HOH HOH B . 
UA 6 HOH 112 2112 2112 HOH HOH B . 
UA 6 HOH 113 2113 2113 HOH HOH B . 
UA 6 HOH 114 2114 2114 HOH HOH B . 
UA 6 HOH 115 2115 2115 HOH HOH B . 
UA 6 HOH 116 2116 2116 HOH HOH B . 
UA 6 HOH 117 2117 2117 HOH HOH B . 
UA 6 HOH 118 2118 2118 HOH HOH B . 
UA 6 HOH 119 2119 2119 HOH HOH B . 
UA 6 HOH 120 2120 2120 HOH HOH B . 
UA 6 HOH 121 2121 2121 HOH HOH B . 
UA 6 HOH 122 2122 2122 HOH HOH B . 
UA 6 HOH 123 2123 2123 HOH HOH B . 
UA 6 HOH 124 2124 2124 HOH HOH B . 
UA 6 HOH 125 2125 2125 HOH HOH B . 
UA 6 HOH 126 2126 2126 HOH HOH B . 
VA 6 HOH 1   2001 2001 HOH HOH C . 
VA 6 HOH 2   2002 2002 HOH HOH C . 
VA 6 HOH 3   2003 2003 HOH HOH C . 
VA 6 HOH 4   2004 2004 HOH HOH C . 
VA 6 HOH 5   2005 2005 HOH HOH C . 
VA 6 HOH 6   2006 2006 HOH HOH C . 
VA 6 HOH 7   2007 2007 HOH HOH C . 
VA 6 HOH 8   2008 2008 HOH HOH C . 
VA 6 HOH 9   2009 2009 HOH HOH C . 
VA 6 HOH 10  2010 2010 HOH HOH C . 
VA 6 HOH 11  2011 2011 HOH HOH C . 
VA 6 HOH 12  2012 2012 HOH HOH C . 
VA 6 HOH 13  2013 2013 HOH HOH C . 
VA 6 HOH 14  2014 2014 HOH HOH C . 
VA 6 HOH 15  2015 2015 HOH HOH C . 
VA 6 HOH 16  2016 2016 HOH HOH C . 
VA 6 HOH 17  2017 2017 HOH HOH C . 
VA 6 HOH 18  2018 2018 HOH HOH C . 
VA 6 HOH 19  2019 2019 HOH HOH C . 
VA 6 HOH 20  2020 2020 HOH HOH C . 
VA 6 HOH 21  2021 2021 HOH HOH C . 
VA 6 HOH 22  2022 2022 HOH HOH C . 
VA 6 HOH 23  2023 2023 HOH HOH C . 
VA 6 HOH 24  2024 2024 HOH HOH C . 
VA 6 HOH 25  2025 2025 HOH HOH C . 
VA 6 HOH 26  2026 2026 HOH HOH C . 
VA 6 HOH 27  2027 2027 HOH HOH C . 
VA 6 HOH 28  2028 2028 HOH HOH C . 
VA 6 HOH 29  2029 2029 HOH HOH C . 
VA 6 HOH 30  2030 2030 HOH HOH C . 
VA 6 HOH 31  2031 2031 HOH HOH C . 
VA 6 HOH 32  2032 2032 HOH HOH C . 
VA 6 HOH 33  2033 2033 HOH HOH C . 
VA 6 HOH 34  2034 2034 HOH HOH C . 
VA 6 HOH 35  2035 2035 HOH HOH C . 
VA 6 HOH 36  2036 2036 HOH HOH C . 
VA 6 HOH 37  2037 2037 HOH HOH C . 
VA 6 HOH 38  2038 2038 HOH HOH C . 
VA 6 HOH 39  2039 2039 HOH HOH C . 
VA 6 HOH 40  2040 2040 HOH HOH C . 
VA 6 HOH 41  2041 2041 HOH HOH C . 
VA 6 HOH 42  2042 2042 HOH HOH C . 
VA 6 HOH 43  2043 2043 HOH HOH C . 
VA 6 HOH 44  2044 2044 HOH HOH C . 
VA 6 HOH 45  2045 2045 HOH HOH C . 
VA 6 HOH 46  2046 2046 HOH HOH C . 
VA 6 HOH 47  2047 2047 HOH HOH C . 
VA 6 HOH 48  2048 2048 HOH HOH C . 
VA 6 HOH 49  2049 2049 HOH HOH C . 
VA 6 HOH 50  2050 2050 HOH HOH C . 
VA 6 HOH 51  2051 2051 HOH HOH C . 
VA 6 HOH 52  2052 2052 HOH HOH C . 
VA 6 HOH 53  2053 2053 HOH HOH C . 
VA 6 HOH 54  2054 2054 HOH HOH C . 
VA 6 HOH 55  2055 2055 HOH HOH C . 
VA 6 HOH 56  2056 2056 HOH HOH C . 
VA 6 HOH 57  2057 2057 HOH HOH C . 
VA 6 HOH 58  2058 2058 HOH HOH C . 
VA 6 HOH 59  2059 2059 HOH HOH C . 
VA 6 HOH 60  2060 2060 HOH HOH C . 
VA 6 HOH 61  2061 2061 HOH HOH C . 
VA 6 HOH 62  2062 2062 HOH HOH C . 
VA 6 HOH 63  2063 2063 HOH HOH C . 
VA 6 HOH 64  2064 2064 HOH HOH C . 
VA 6 HOH 65  2065 2065 HOH HOH C . 
VA 6 HOH 66  2066 2066 HOH HOH C . 
VA 6 HOH 67  2067 2067 HOH HOH C . 
VA 6 HOH 68  2068 2068 HOH HOH C . 
VA 6 HOH 69  2069 2069 HOH HOH C . 
VA 6 HOH 70  2070 2070 HOH HOH C . 
VA 6 HOH 71  2071 2071 HOH HOH C . 
VA 6 HOH 72  2072 2072 HOH HOH C . 
VA 6 HOH 73  2073 2073 HOH HOH C . 
VA 6 HOH 74  2074 2074 HOH HOH C . 
VA 6 HOH 75  2075 2075 HOH HOH C . 
VA 6 HOH 76  2076 2076 HOH HOH C . 
VA 6 HOH 77  2077 2077 HOH HOH C . 
VA 6 HOH 78  2078 2078 HOH HOH C . 
VA 6 HOH 79  2079 2079 HOH HOH C . 
VA 6 HOH 80  2080 2080 HOH HOH C . 
VA 6 HOH 81  2081 2081 HOH HOH C . 
VA 6 HOH 82  2082 2082 HOH HOH C . 
VA 6 HOH 83  2083 2083 HOH HOH C . 
VA 6 HOH 84  2084 2084 HOH HOH C . 
VA 6 HOH 85  2085 2085 HOH HOH C . 
VA 6 HOH 86  2086 2086 HOH HOH C . 
VA 6 HOH 87  2087 2087 HOH HOH C . 
VA 6 HOH 88  2088 2088 HOH HOH C . 
VA 6 HOH 89  2089 2089 HOH HOH C . 
VA 6 HOH 90  2090 2090 HOH HOH C . 
VA 6 HOH 91  2091 2091 HOH HOH C . 
VA 6 HOH 92  2092 2092 HOH HOH C . 
VA 6 HOH 93  2093 2093 HOH HOH C . 
VA 6 HOH 94  2094 2094 HOH HOH C . 
VA 6 HOH 95  2095 2095 HOH HOH C . 
VA 6 HOH 96  2096 2096 HOH HOH C . 
VA 6 HOH 97  2097 2097 HOH HOH C . 
VA 6 HOH 98  2098 2098 HOH HOH C . 
VA 6 HOH 99  2099 2099 HOH HOH C . 
VA 6 HOH 100 2100 2100 HOH HOH C . 
VA 6 HOH 101 2101 2101 HOH HOH C . 
VA 6 HOH 102 2102 2102 HOH HOH C . 
VA 6 HOH 103 2103 2103 HOH HOH C . 
VA 6 HOH 104 2104 2104 HOH HOH C . 
VA 6 HOH 105 2105 2105 HOH HOH C . 
VA 6 HOH 106 2106 2106 HOH HOH C . 
VA 6 HOH 107 2107 2107 HOH HOH C . 
VA 6 HOH 108 2108 2108 HOH HOH C . 
VA 6 HOH 109 2109 2109 HOH HOH C . 
VA 6 HOH 110 2110 2110 HOH HOH C . 
VA 6 HOH 111 2111 2111 HOH HOH C . 
VA 6 HOH 112 2112 2112 HOH HOH C . 
VA 6 HOH 113 2113 2113 HOH HOH C . 
VA 6 HOH 114 2114 2114 HOH HOH C . 
VA 6 HOH 115 2115 2115 HOH HOH C . 
VA 6 HOH 116 2116 2116 HOH HOH C . 
VA 6 HOH 117 2117 2117 HOH HOH C . 
VA 6 HOH 118 2118 2118 HOH HOH C . 
VA 6 HOH 119 2119 2119 HOH HOH C . 
VA 6 HOH 120 2120 2120 HOH HOH C . 
VA 6 HOH 121 2121 2121 HOH HOH C . 
VA 6 HOH 122 2122 2122 HOH HOH C . 
VA 6 HOH 123 2123 2123 HOH HOH C . 
VA 6 HOH 124 2124 2124 HOH HOH C . 
VA 6 HOH 125 2125 2125 HOH HOH C . 
VA 6 HOH 126 2126 2126 HOH HOH C . 
VA 6 HOH 127 2127 2127 HOH HOH C . 
VA 6 HOH 128 2128 2128 HOH HOH C . 
VA 6 HOH 129 2129 2129 HOH HOH C . 
VA 6 HOH 130 2130 2130 HOH HOH C . 
VA 6 HOH 131 2131 2131 HOH HOH C . 
VA 6 HOH 132 2132 2132 HOH HOH C . 
VA 6 HOH 133 2133 2133 HOH HOH C . 
VA 6 HOH 134 2134 2134 HOH HOH C . 
VA 6 HOH 135 2135 2135 HOH HOH C . 
VA 6 HOH 136 2136 2136 HOH HOH C . 
VA 6 HOH 137 2137 2137 HOH HOH C . 
VA 6 HOH 138 2138 2138 HOH HOH C . 
VA 6 HOH 139 2139 2139 HOH HOH C . 
VA 6 HOH 140 2140 2140 HOH HOH C . 
VA 6 HOH 141 2141 2141 HOH HOH C . 
VA 6 HOH 142 2142 2142 HOH HOH C . 
VA 6 HOH 143 2143 2143 HOH HOH C . 
VA 6 HOH 144 2144 2144 HOH HOH C . 
VA 6 HOH 145 2145 2145 HOH HOH C . 
VA 6 HOH 146 2146 2146 HOH HOH C . 
VA 6 HOH 147 2147 2147 HOH HOH C . 
VA 6 HOH 148 2148 2148 HOH HOH C . 
VA 6 HOH 149 2149 2149 HOH HOH C . 
VA 6 HOH 150 2150 2150 HOH HOH C . 
VA 6 HOH 151 2151 2151 HOH HOH C . 
VA 6 HOH 152 2152 2152 HOH HOH C . 
VA 6 HOH 153 2153 2153 HOH HOH C . 
VA 6 HOH 154 2154 2154 HOH HOH C . 
VA 6 HOH 155 2155 2155 HOH HOH C . 
VA 6 HOH 156 2156 2156 HOH HOH C . 
VA 6 HOH 157 2157 2157 HOH HOH C . 
VA 6 HOH 158 2158 2158 HOH HOH C . 
VA 6 HOH 159 2159 2159 HOH HOH C . 
VA 6 HOH 160 2160 2160 HOH HOH C . 
VA 6 HOH 161 2161 2161 HOH HOH C . 
VA 6 HOH 162 2162 2162 HOH HOH C . 
VA 6 HOH 163 2163 2163 HOH HOH C . 
VA 6 HOH 164 2164 2164 HOH HOH C . 
VA 6 HOH 165 2165 2165 HOH HOH C . 
VA 6 HOH 166 2166 2166 HOH HOH C . 
VA 6 HOH 167 2167 2167 HOH HOH C . 
VA 6 HOH 168 2168 2168 HOH HOH C . 
VA 6 HOH 169 2169 2169 HOH HOH C . 
VA 6 HOH 170 2170 2170 HOH HOH C . 
VA 6 HOH 171 2171 2171 HOH HOH C . 
VA 6 HOH 172 2172 2172 HOH HOH C . 
VA 6 HOH 173 2173 2173 HOH HOH C . 
VA 6 HOH 174 2174 2174 HOH HOH C . 
VA 6 HOH 175 2175 2175 HOH HOH C . 
VA 6 HOH 176 2176 2176 HOH HOH C . 
VA 6 HOH 177 2177 2177 HOH HOH C . 
VA 6 HOH 178 2178 2178 HOH HOH C . 
VA 6 HOH 179 2179 2179 HOH HOH C . 
VA 6 HOH 180 2180 2180 HOH HOH C . 
VA 6 HOH 181 2181 2181 HOH HOH C . 
VA 6 HOH 182 2182 2182 HOH HOH C . 
VA 6 HOH 183 2183 2183 HOH HOH C . 
VA 6 HOH 184 2184 2184 HOH HOH C . 
VA 6 HOH 185 2185 2185 HOH HOH C . 
VA 6 HOH 186 2186 2186 HOH HOH C . 
VA 6 HOH 187 2187 2187 HOH HOH C . 
VA 6 HOH 188 2188 2188 HOH HOH C . 
VA 6 HOH 189 2189 2189 HOH HOH C . 
VA 6 HOH 190 2190 2190 HOH HOH C . 
VA 6 HOH 191 2191 2191 HOH HOH C . 
VA 6 HOH 192 2192 2192 HOH HOH C . 
VA 6 HOH 193 2193 2193 HOH HOH C . 
VA 6 HOH 194 2194 2194 HOH HOH C . 
VA 6 HOH 195 2195 2195 HOH HOH C . 
VA 6 HOH 196 2196 2196 HOH HOH C . 
VA 6 HOH 197 2197 2197 HOH HOH C . 
VA 6 HOH 198 2198 2198 HOH HOH C . 
VA 6 HOH 199 2199 2199 HOH HOH C . 
WA 6 HOH 1   2001 2001 HOH HOH D . 
WA 6 HOH 2   2002 2002 HOH HOH D . 
WA 6 HOH 3   2003 2003 HOH HOH D . 
WA 6 HOH 4   2004 2004 HOH HOH D . 
WA 6 HOH 5   2005 2005 HOH HOH D . 
WA 6 HOH 6   2006 2006 HOH HOH D . 
WA 6 HOH 7   2007 2007 HOH HOH D . 
WA 6 HOH 8   2008 2008 HOH HOH D . 
WA 6 HOH 9   2009 2009 HOH HOH D . 
WA 6 HOH 10  2010 2010 HOH HOH D . 
WA 6 HOH 11  2011 2011 HOH HOH D . 
WA 6 HOH 12  2012 2012 HOH HOH D . 
WA 6 HOH 13  2013 2013 HOH HOH D . 
WA 6 HOH 14  2014 2014 HOH HOH D . 
WA 6 HOH 15  2015 2015 HOH HOH D . 
WA 6 HOH 16  2016 2016 HOH HOH D . 
WA 6 HOH 17  2017 2017 HOH HOH D . 
WA 6 HOH 18  2018 2018 HOH HOH D . 
WA 6 HOH 19  2019 2019 HOH HOH D . 
WA 6 HOH 20  2020 2020 HOH HOH D . 
WA 6 HOH 21  2021 2021 HOH HOH D . 
WA 6 HOH 22  2022 2022 HOH HOH D . 
WA 6 HOH 23  2023 2023 HOH HOH D . 
WA 6 HOH 24  2024 2024 HOH HOH D . 
WA 6 HOH 25  2025 2025 HOH HOH D . 
WA 6 HOH 26  2026 2026 HOH HOH D . 
WA 6 HOH 27  2027 2027 HOH HOH D . 
WA 6 HOH 28  2028 2028 HOH HOH D . 
WA 6 HOH 29  2029 2029 HOH HOH D . 
WA 6 HOH 30  2030 2030 HOH HOH D . 
WA 6 HOH 31  2031 2031 HOH HOH D . 
WA 6 HOH 32  2032 2032 HOH HOH D . 
WA 6 HOH 33  2033 2033 HOH HOH D . 
WA 6 HOH 34  2034 2034 HOH HOH D . 
WA 6 HOH 35  2035 2035 HOH HOH D . 
WA 6 HOH 36  2036 2036 HOH HOH D . 
WA 6 HOH 37  2037 2037 HOH HOH D . 
WA 6 HOH 38  2038 2038 HOH HOH D . 
WA 6 HOH 39  2039 2039 HOH HOH D . 
WA 6 HOH 40  2040 2040 HOH HOH D . 
WA 6 HOH 41  2041 2041 HOH HOH D . 
WA 6 HOH 42  2042 2042 HOH HOH D . 
WA 6 HOH 43  2043 2043 HOH HOH D . 
WA 6 HOH 44  2044 2044 HOH HOH D . 
WA 6 HOH 45  2045 2045 HOH HOH D . 
WA 6 HOH 46  2046 2046 HOH HOH D . 
WA 6 HOH 47  2047 2047 HOH HOH D . 
WA 6 HOH 48  2048 2048 HOH HOH D . 
WA 6 HOH 49  2049 2049 HOH HOH D . 
WA 6 HOH 50  2050 2050 HOH HOH D . 
WA 6 HOH 51  2051 2051 HOH HOH D . 
WA 6 HOH 52  2052 2052 HOH HOH D . 
WA 6 HOH 53  2053 2053 HOH HOH D . 
WA 6 HOH 54  2054 2054 HOH HOH D . 
WA 6 HOH 55  2055 2055 HOH HOH D . 
WA 6 HOH 56  2056 2056 HOH HOH D . 
WA 6 HOH 57  2057 2057 HOH HOH D . 
WA 6 HOH 58  2058 2058 HOH HOH D . 
WA 6 HOH 59  2059 2059 HOH HOH D . 
WA 6 HOH 60  2060 2060 HOH HOH D . 
WA 6 HOH 61  2061 2061 HOH HOH D . 
WA 6 HOH 62  2062 2062 HOH HOH D . 
WA 6 HOH 63  2063 2063 HOH HOH D . 
WA 6 HOH 64  2064 2064 HOH HOH D . 
WA 6 HOH 65  2065 2065 HOH HOH D . 
WA 6 HOH 66  2066 2066 HOH HOH D . 
WA 6 HOH 67  2067 2067 HOH HOH D . 
WA 6 HOH 68  2068 2068 HOH HOH D . 
WA 6 HOH 69  2069 2069 HOH HOH D . 
WA 6 HOH 70  2070 2070 HOH HOH D . 
WA 6 HOH 71  2071 2071 HOH HOH D . 
WA 6 HOH 72  2072 2072 HOH HOH D . 
WA 6 HOH 73  2073 2073 HOH HOH D . 
WA 6 HOH 74  2074 2074 HOH HOH D . 
WA 6 HOH 75  2075 2075 HOH HOH D . 
WA 6 HOH 76  2076 2076 HOH HOH D . 
WA 6 HOH 77  2077 2077 HOH HOH D . 
WA 6 HOH 78  2078 2078 HOH HOH D . 
WA 6 HOH 79  2079 2079 HOH HOH D . 
WA 6 HOH 80  2080 2080 HOH HOH D . 
WA 6 HOH 81  2081 2081 HOH HOH D . 
WA 6 HOH 82  2082 2082 HOH HOH D . 
WA 6 HOH 83  2083 2083 HOH HOH D . 
WA 6 HOH 84  2084 2084 HOH HOH D . 
WA 6 HOH 85  2085 2085 HOH HOH D . 
WA 6 HOH 86  2086 2086 HOH HOH D . 
WA 6 HOH 87  2087 2087 HOH HOH D . 
WA 6 HOH 88  2088 2088 HOH HOH D . 
WA 6 HOH 89  2089 2089 HOH HOH D . 
WA 6 HOH 90  2090 2090 HOH HOH D . 
WA 6 HOH 91  2091 2091 HOH HOH D . 
WA 6 HOH 92  2092 2092 HOH HOH D . 
WA 6 HOH 93  2093 2093 HOH HOH D . 
WA 6 HOH 94  2094 2094 HOH HOH D . 
WA 6 HOH 95  2095 2095 HOH HOH D . 
WA 6 HOH 96  2096 2096 HOH HOH D . 
WA 6 HOH 97  2097 2097 HOH HOH D . 
WA 6 HOH 98  2098 2098 HOH HOH D . 
WA 6 HOH 99  2099 2099 HOH HOH D . 
WA 6 HOH 100 2100 2100 HOH HOH D . 
WA 6 HOH 101 2101 2101 HOH HOH D . 
WA 6 HOH 102 2102 2102 HOH HOH D . 
WA 6 HOH 103 2103 2103 HOH HOH D . 
WA 6 HOH 104 2104 2104 HOH HOH D . 
WA 6 HOH 105 2105 2105 HOH HOH D . 
WA 6 HOH 106 2106 2106 HOH HOH D . 
WA 6 HOH 107 2107 2107 HOH HOH D . 
WA 6 HOH 108 2108 2108 HOH HOH D . 
WA 6 HOH 109 2109 2109 HOH HOH D . 
WA 6 HOH 110 2110 2110 HOH HOH D . 
WA 6 HOH 111 2111 2111 HOH HOH D . 
WA 6 HOH 112 2112 2112 HOH HOH D . 
WA 6 HOH 113 2113 2113 HOH HOH D . 
WA 6 HOH 114 2114 2114 HOH HOH D . 
WA 6 HOH 115 2115 2115 HOH HOH D . 
WA 6 HOH 116 2116 2116 HOH HOH D . 
WA 6 HOH 117 2117 2117 HOH HOH D . 
WA 6 HOH 118 2118 2118 HOH HOH D . 
WA 6 HOH 119 2119 2119 HOH HOH D . 
WA 6 HOH 120 2120 2120 HOH HOH D . 
XA 6 HOH 1   2001 2001 HOH HOH E . 
XA 6 HOH 2   2002 2002 HOH HOH E . 
XA 6 HOH 3   2003 2003 HOH HOH E . 
XA 6 HOH 4   2004 2004 HOH HOH E . 
XA 6 HOH 5   2005 2005 HOH HOH E . 
XA 6 HOH 6   2006 2006 HOH HOH E . 
XA 6 HOH 7   2007 2007 HOH HOH E . 
XA 6 HOH 8   2008 2008 HOH HOH E . 
XA 6 HOH 9   2009 2009 HOH HOH E . 
XA 6 HOH 10  2010 2010 HOH HOH E . 
XA 6 HOH 11  2011 2011 HOH HOH E . 
XA 6 HOH 12  2012 2012 HOH HOH E . 
XA 6 HOH 13  2013 2013 HOH HOH E . 
XA 6 HOH 14  2014 2014 HOH HOH E . 
XA 6 HOH 15  2015 2015 HOH HOH E . 
XA 6 HOH 16  2016 2016 HOH HOH E . 
XA 6 HOH 17  2017 2017 HOH HOH E . 
XA 6 HOH 18  2018 2018 HOH HOH E . 
XA 6 HOH 19  2019 2019 HOH HOH E . 
XA 6 HOH 20  2020 2020 HOH HOH E . 
XA 6 HOH 21  2021 2021 HOH HOH E . 
XA 6 HOH 22  2022 2022 HOH HOH E . 
XA 6 HOH 23  2023 2023 HOH HOH E . 
XA 6 HOH 24  2024 2024 HOH HOH E . 
XA 6 HOH 25  2025 2025 HOH HOH E . 
XA 6 HOH 26  2026 2026 HOH HOH E . 
XA 6 HOH 27  2027 2027 HOH HOH E . 
XA 6 HOH 28  2028 2028 HOH HOH E . 
XA 6 HOH 29  2029 2029 HOH HOH E . 
XA 6 HOH 30  2030 2030 HOH HOH E . 
XA 6 HOH 31  2031 2031 HOH HOH E . 
XA 6 HOH 32  2032 2032 HOH HOH E . 
XA 6 HOH 33  2033 2033 HOH HOH E . 
XA 6 HOH 34  2034 2034 HOH HOH E . 
XA 6 HOH 35  2035 2035 HOH HOH E . 
XA 6 HOH 36  2036 2036 HOH HOH E . 
XA 6 HOH 37  2037 2037 HOH HOH E . 
XA 6 HOH 38  2038 2038 HOH HOH E . 
XA 6 HOH 39  2039 2039 HOH HOH E . 
XA 6 HOH 40  2040 2040 HOH HOH E . 
XA 6 HOH 41  2041 2041 HOH HOH E . 
XA 6 HOH 42  2042 2042 HOH HOH E . 
XA 6 HOH 43  2043 2043 HOH HOH E . 
XA 6 HOH 44  2044 2044 HOH HOH E . 
XA 6 HOH 45  2045 2045 HOH HOH E . 
XA 6 HOH 46  2046 2046 HOH HOH E . 
XA 6 HOH 47  2047 2047 HOH HOH E . 
XA 6 HOH 48  2048 2048 HOH HOH E . 
XA 6 HOH 49  2049 2049 HOH HOH E . 
XA 6 HOH 50  2050 2050 HOH HOH E . 
XA 6 HOH 51  2051 2051 HOH HOH E . 
XA 6 HOH 52  2052 2052 HOH HOH E . 
XA 6 HOH 53  2053 2053 HOH HOH E . 
XA 6 HOH 54  2054 2054 HOH HOH E . 
XA 6 HOH 55  2055 2055 HOH HOH E . 
XA 6 HOH 56  2056 2056 HOH HOH E . 
XA 6 HOH 57  2057 2057 HOH HOH E . 
XA 6 HOH 58  2058 2058 HOH HOH E . 
XA 6 HOH 59  2059 2059 HOH HOH E . 
XA 6 HOH 60  2060 2060 HOH HOH E . 
XA 6 HOH 61  2061 2061 HOH HOH E . 
XA 6 HOH 62  2062 2062 HOH HOH E . 
XA 6 HOH 63  2063 2063 HOH HOH E . 
XA 6 HOH 64  2064 2064 HOH HOH E . 
XA 6 HOH 65  2065 2065 HOH HOH E . 
XA 6 HOH 66  2066 2066 HOH HOH E . 
XA 6 HOH 67  2067 2067 HOH HOH E . 
XA 6 HOH 68  2068 2068 HOH HOH E . 
XA 6 HOH 69  2069 2069 HOH HOH E . 
XA 6 HOH 70  2070 2070 HOH HOH E . 
XA 6 HOH 71  2071 2071 HOH HOH E . 
XA 6 HOH 72  2072 2072 HOH HOH E . 
XA 6 HOH 73  2073 2073 HOH HOH E . 
XA 6 HOH 74  2074 2074 HOH HOH E . 
XA 6 HOH 75  2075 2075 HOH HOH E . 
XA 6 HOH 76  2076 2076 HOH HOH E . 
XA 6 HOH 77  2077 2077 HOH HOH E . 
XA 6 HOH 78  2078 2078 HOH HOH E . 
XA 6 HOH 79  2079 2079 HOH HOH E . 
XA 6 HOH 80  2080 2080 HOH HOH E . 
XA 6 HOH 81  2081 2081 HOH HOH E . 
XA 6 HOH 82  2082 2082 HOH HOH E . 
XA 6 HOH 83  2083 2083 HOH HOH E . 
XA 6 HOH 84  2084 2084 HOH HOH E . 
XA 6 HOH 85  2085 2085 HOH HOH E . 
XA 6 HOH 86  2086 2086 HOH HOH E . 
XA 6 HOH 87  2087 2087 HOH HOH E . 
XA 6 HOH 88  2088 2088 HOH HOH E . 
XA 6 HOH 89  2089 2089 HOH HOH E . 
XA 6 HOH 90  2090 2090 HOH HOH E . 
XA 6 HOH 91  2091 2091 HOH HOH E . 
XA 6 HOH 92  2092 2092 HOH HOH E . 
XA 6 HOH 93  2093 2093 HOH HOH E . 
XA 6 HOH 94  2094 2094 HOH HOH E . 
XA 6 HOH 95  2095 2095 HOH HOH E . 
XA 6 HOH 96  2096 2096 HOH HOH E . 
XA 6 HOH 97  2097 2097 HOH HOH E . 
XA 6 HOH 98  2098 2098 HOH HOH E . 
XA 6 HOH 99  2099 2099 HOH HOH E . 
XA 6 HOH 100 2100 2100 HOH HOH E . 
XA 6 HOH 101 2101 2101 HOH HOH E . 
XA 6 HOH 102 2102 2102 HOH HOH E . 
XA 6 HOH 103 2103 2103 HOH HOH E . 
XA 6 HOH 104 2104 2104 HOH HOH E . 
XA 6 HOH 105 2105 2105 HOH HOH E . 
XA 6 HOH 106 2106 2106 HOH HOH E . 
XA 6 HOH 107 2107 2107 HOH HOH E . 
XA 6 HOH 108 2108 2108 HOH HOH E . 
XA 6 HOH 109 2109 2109 HOH HOH E . 
XA 6 HOH 110 2110 2110 HOH HOH E . 
XA 6 HOH 111 2111 2111 HOH HOH E . 
YA 6 HOH 1   2001 2001 HOH HOH F . 
YA 6 HOH 2   2002 2002 HOH HOH F . 
YA 6 HOH 3   2003 2003 HOH HOH F . 
YA 6 HOH 4   2004 2004 HOH HOH F . 
YA 6 HOH 5   2005 2005 HOH HOH F . 
YA 6 HOH 6   2006 2006 HOH HOH F . 
YA 6 HOH 7   2007 2007 HOH HOH F . 
YA 6 HOH 8   2008 2008 HOH HOH F . 
YA 6 HOH 9   2009 2009 HOH HOH F . 
YA 6 HOH 10  2010 2010 HOH HOH F . 
YA 6 HOH 11  2011 2011 HOH HOH F . 
YA 6 HOH 12  2012 2012 HOH HOH F . 
YA 6 HOH 13  2013 2013 HOH HOH F . 
YA 6 HOH 14  2014 2014 HOH HOH F . 
YA 6 HOH 15  2015 2015 HOH HOH F . 
YA 6 HOH 16  2016 2016 HOH HOH F . 
YA 6 HOH 17  2017 2017 HOH HOH F . 
YA 6 HOH 18  2018 2018 HOH HOH F . 
YA 6 HOH 19  2019 2019 HOH HOH F . 
YA 6 HOH 20  2020 2020 HOH HOH F . 
YA 6 HOH 21  2021 2021 HOH HOH F . 
YA 6 HOH 22  2022 2022 HOH HOH F . 
YA 6 HOH 23  2023 2023 HOH HOH F . 
YA 6 HOH 24  2024 2024 HOH HOH F . 
YA 6 HOH 25  2025 2025 HOH HOH F . 
YA 6 HOH 26  2026 2026 HOH HOH F . 
YA 6 HOH 27  2027 2027 HOH HOH F . 
YA 6 HOH 28  2028 2028 HOH HOH F . 
YA 6 HOH 29  2029 2029 HOH HOH F . 
YA 6 HOH 30  2030 2030 HOH HOH F . 
YA 6 HOH 31  2031 2031 HOH HOH F . 
YA 6 HOH 32  2032 2032 HOH HOH F . 
YA 6 HOH 33  2033 2033 HOH HOH F . 
YA 6 HOH 34  2034 2034 HOH HOH F . 
YA 6 HOH 35  2035 2035 HOH HOH F . 
YA 6 HOH 36  2036 2036 HOH HOH F . 
YA 6 HOH 37  2037 2037 HOH HOH F . 
YA 6 HOH 38  2038 2038 HOH HOH F . 
YA 6 HOH 39  2039 2039 HOH HOH F . 
YA 6 HOH 40  2040 2040 HOH HOH F . 
YA 6 HOH 41  2041 2041 HOH HOH F . 
YA 6 HOH 42  2042 2042 HOH HOH F . 
YA 6 HOH 43  2043 2043 HOH HOH F . 
YA 6 HOH 44  2044 2044 HOH HOH F . 
YA 6 HOH 45  2045 2045 HOH HOH F . 
YA 6 HOH 46  2046 2046 HOH HOH F . 
YA 6 HOH 47  2047 2047 HOH HOH F . 
YA 6 HOH 48  2048 2048 HOH HOH F . 
YA 6 HOH 49  2049 2049 HOH HOH F . 
YA 6 HOH 50  2050 2050 HOH HOH F . 
YA 6 HOH 51  2051 2051 HOH HOH F . 
YA 6 HOH 52  2052 2052 HOH HOH F . 
YA 6 HOH 53  2053 2053 HOH HOH F . 
YA 6 HOH 54  2054 2054 HOH HOH F . 
YA 6 HOH 55  2055 2055 HOH HOH F . 
YA 6 HOH 56  2056 2056 HOH HOH F . 
YA 6 HOH 57  2057 2057 HOH HOH F . 
YA 6 HOH 58  2058 2058 HOH HOH F . 
YA 6 HOH 59  2059 2059 HOH HOH F . 
YA 6 HOH 60  2060 2060 HOH HOH F . 
YA 6 HOH 61  2061 2061 HOH HOH F . 
YA 6 HOH 62  2062 2062 HOH HOH F . 
YA 6 HOH 63  2063 2063 HOH HOH F . 
YA 6 HOH 64  2064 2064 HOH HOH F . 
YA 6 HOH 65  2065 2065 HOH HOH F . 
YA 6 HOH 66  2066 2066 HOH HOH F . 
YA 6 HOH 67  2067 2067 HOH HOH F . 
YA 6 HOH 68  2068 2068 HOH HOH F . 
YA 6 HOH 69  2069 2069 HOH HOH F . 
YA 6 HOH 70  2070 2070 HOH HOH F . 
YA 6 HOH 71  2071 2071 HOH HOH F . 
YA 6 HOH 72  2072 2072 HOH HOH F . 
YA 6 HOH 73  2073 2073 HOH HOH F . 
YA 6 HOH 74  2074 2074 HOH HOH F . 
YA 6 HOH 75  2075 2075 HOH HOH F . 
YA 6 HOH 76  2076 2076 HOH HOH F . 
YA 6 HOH 77  2077 2077 HOH HOH F . 
YA 6 HOH 78  2078 2078 HOH HOH F . 
YA 6 HOH 79  2079 2079 HOH HOH F . 
YA 6 HOH 80  2080 2080 HOH HOH F . 
YA 6 HOH 81  2081 2081 HOH HOH F . 
YA 6 HOH 82  2082 2082 HOH HOH F . 
YA 6 HOH 83  2083 2083 HOH HOH F . 
YA 6 HOH 84  2084 2084 HOH HOH F . 
YA 6 HOH 85  2085 2085 HOH HOH F . 
YA 6 HOH 86  2086 2086 HOH HOH F . 
YA 6 HOH 87  2087 2087 HOH HOH F . 
YA 6 HOH 88  2088 2088 HOH HOH F . 
YA 6 HOH 89  2089 2089 HOH HOH F . 
YA 6 HOH 90  2090 2090 HOH HOH F . 
YA 6 HOH 91  2091 2091 HOH HOH F . 
YA 6 HOH 92  2092 2092 HOH HOH F . 
YA 6 HOH 93  2093 2093 HOH HOH F . 
YA 6 HOH 94  2094 2094 HOH HOH F . 
YA 6 HOH 95  2095 2095 HOH HOH F . 
YA 6 HOH 96  2096 2096 HOH HOH F . 
YA 6 HOH 97  2097 2097 HOH HOH F . 
YA 6 HOH 98  2098 2098 HOH HOH F . 
YA 6 HOH 99  2099 2099 HOH HOH F . 
YA 6 HOH 100 2100 2100 HOH HOH F . 
YA 6 HOH 101 2101 2101 HOH HOH F . 
YA 6 HOH 102 2102 2102 HOH HOH F . 
YA 6 HOH 103 2103 2103 HOH HOH F . 
YA 6 HOH 104 2104 2104 HOH HOH F . 
YA 6 HOH 105 2105 2105 HOH HOH F . 
YA 6 HOH 106 2106 2106 HOH HOH F . 
YA 6 HOH 107 2107 2107 HOH HOH F . 
YA 6 HOH 108 2108 2108 HOH HOH F . 
YA 6 HOH 109 2109 2109 HOH HOH F . 
YA 6 HOH 110 2110 2110 HOH HOH F . 
YA 6 HOH 111 2111 2111 HOH HOH F . 
YA 6 HOH 112 2112 2112 HOH HOH F . 
YA 6 HOH 113 2113 2113 HOH HOH F . 
YA 6 HOH 114 2114 2114 HOH HOH F . 
YA 6 HOH 115 2115 2115 HOH HOH F . 
YA 6 HOH 116 2116 2116 HOH HOH F . 
YA 6 HOH 117 2117 2117 HOH HOH F . 
YA 6 HOH 118 2118 2118 HOH HOH F . 
YA 6 HOH 119 2119 2119 HOH HOH F . 
YA 6 HOH 120 2120 2120 HOH HOH F . 
YA 6 HOH 121 2121 2121 HOH HOH F . 
YA 6 HOH 122 2122 2122 HOH HOH F . 
YA 6 HOH 123 2123 2123 HOH HOH F . 
YA 6 HOH 124 2124 2124 HOH HOH F . 
YA 6 HOH 125 2125 2125 HOH HOH F . 
YA 6 HOH 126 2126 2126 HOH HOH F . 
YA 6 HOH 127 2127 2127 HOH HOH F . 
YA 6 HOH 128 2128 2128 HOH HOH F . 
YA 6 HOH 129 2129 2129 HOH HOH F . 
YA 6 HOH 130 2130 2130 HOH HOH F . 
YA 6 HOH 131 2131 2131 HOH HOH F . 
YA 6 HOH 132 2132 2132 HOH HOH F . 
YA 6 HOH 133 2133 2133 HOH HOH F . 
YA 6 HOH 134 2134 2134 HOH HOH F . 
YA 6 HOH 135 2135 2135 HOH HOH F . 
YA 6 HOH 136 2136 2136 HOH HOH F . 
YA 6 HOH 137 2137 2137 HOH HOH F . 
YA 6 HOH 138 2138 2138 HOH HOH F . 
YA 6 HOH 139 2139 2139 HOH HOH F . 
YA 6 HOH 140 2140 2140 HOH HOH F . 
YA 6 HOH 141 2141 2141 HOH HOH F . 
YA 6 HOH 142 2142 2142 HOH HOH F . 
YA 6 HOH 143 2143 2143 HOH HOH F . 
YA 6 HOH 144 2144 2144 HOH HOH F . 
YA 6 HOH 145 2145 2145 HOH HOH F . 
YA 6 HOH 146 2146 2146 HOH HOH F . 
YA 6 HOH 147 2147 2147 HOH HOH F . 
YA 6 HOH 148 2148 2148 HOH HOH F . 
YA 6 HOH 149 2149 2149 HOH HOH F . 
YA 6 HOH 150 2150 2150 HOH HOH F . 
YA 6 HOH 151 2151 2151 HOH HOH F . 
YA 6 HOH 152 2152 2152 HOH HOH F . 
YA 6 HOH 153 2153 2153 HOH HOH F . 
YA 6 HOH 154 2154 2154 HOH HOH F . 
YA 6 HOH 155 2155 2155 HOH HOH F . 
YA 6 HOH 156 2156 2156 HOH HOH F . 
YA 6 HOH 157 2157 2157 HOH HOH F . 
YA 6 HOH 158 2158 2158 HOH HOH F . 
YA 6 HOH 159 2159 2159 HOH HOH F . 
YA 6 HOH 160 2160 2160 HOH HOH F . 
YA 6 HOH 161 2161 2161 HOH HOH F . 
YA 6 HOH 162 2162 2162 HOH HOH F . 
YA 6 HOH 163 2163 2163 HOH HOH F . 
YA 6 HOH 164 2164 2164 HOH HOH F . 
YA 6 HOH 165 2165 2165 HOH HOH F . 
YA 6 HOH 166 2166 2166 HOH HOH F . 
YA 6 HOH 167 2167 2167 HOH HOH F . 
YA 6 HOH 168 2168 2168 HOH HOH F . 
YA 6 HOH 169 2169 2169 HOH HOH F . 
YA 6 HOH 170 2170 2170 HOH HOH F . 
YA 6 HOH 171 2171 2171 HOH HOH F . 
YA 6 HOH 172 2172 2172 HOH HOH F . 
YA 6 HOH 173 2173 2173 HOH HOH F . 
YA 6 HOH 174 2174 2174 HOH HOH F . 
YA 6 HOH 175 2175 2175 HOH HOH F . 
YA 6 HOH 176 2176 2176 HOH HOH F . 
YA 6 HOH 177 2177 2177 HOH HOH F . 
YA 6 HOH 178 2178 2178 HOH HOH F . 
YA 6 HOH 179 2179 2179 HOH HOH F . 
YA 6 HOH 180 2180 2180 HOH HOH F . 
YA 6 HOH 181 2181 2181 HOH HOH F . 
YA 6 HOH 182 2182 2182 HOH HOH F . 
YA 6 HOH 183 2183 2183 HOH HOH F . 
YA 6 HOH 184 2184 2184 HOH HOH F . 
YA 6 HOH 185 2185 2185 HOH HOH F . 
YA 6 HOH 186 2186 2186 HOH HOH F . 
YA 6 HOH 187 2187 2187 HOH HOH F . 
YA 6 HOH 188 2188 2188 HOH HOH F . 
YA 6 HOH 189 2189 2189 HOH HOH F . 
YA 6 HOH 190 2190 2190 HOH HOH F . 
YA 6 HOH 191 2191 2191 HOH HOH F . 
YA 6 HOH 192 2192 2192 HOH HOH F . 
YA 6 HOH 193 2193 2193 HOH HOH F . 
YA 6 HOH 194 2194 2194 HOH HOH F . 
YA 6 HOH 195 2195 2195 HOH HOH F . 
YA 6 HOH 196 2196 2196 HOH HOH F . 
YA 6 HOH 197 2197 2197 HOH HOH F . 
YA 6 HOH 198 2198 2198 HOH HOH F . 
YA 6 HOH 199 2199 2199 HOH HOH F . 
YA 6 HOH 200 2200 2200 HOH HOH F . 
YA 6 HOH 201 2201 2201 HOH HOH F . 
YA 6 HOH 202 2202 2202 HOH HOH F . 
YA 6 HOH 203 2203 2203 HOH HOH F . 
YA 6 HOH 204 2204 2204 HOH HOH F . 
YA 6 HOH 205 2205 2205 HOH HOH F . 
YA 6 HOH 206 2206 2206 HOH HOH F . 
YA 6 HOH 207 2207 2207 HOH HOH F . 
YA 6 HOH 208 2208 2208 HOH HOH F . 
YA 6 HOH 209 2209 2209 HOH HOH F . 
YA 6 HOH 210 2210 2210 HOH HOH F . 
YA 6 HOH 211 2211 2211 HOH HOH F . 
YA 6 HOH 212 2212 2212 HOH HOH F . 
YA 6 HOH 213 2213 2213 HOH HOH F . 
YA 6 HOH 214 2214 2214 HOH HOH F . 
YA 6 HOH 215 2215 2215 HOH HOH F . 
YA 6 HOH 216 2216 2216 HOH HOH F . 
YA 6 HOH 217 2217 2217 HOH HOH F . 
YA 6 HOH 218 2218 2218 HOH HOH F . 
YA 6 HOH 219 2219 2219 HOH HOH F . 
YA 6 HOH 220 2220 2220 HOH HOH F . 
YA 6 HOH 221 2221 2221 HOH HOH F . 
YA 6 HOH 222 2222 2222 HOH HOH F . 
YA 6 HOH 223 2223 2223 HOH HOH F . 
YA 6 HOH 224 2224 2224 HOH HOH F . 
YA 6 HOH 225 2225 2225 HOH HOH F . 
YA 6 HOH 226 2226 2226 HOH HOH F . 
YA 6 HOH 227 2227 2227 HOH HOH F . 
YA 6 HOH 228 2228 2228 HOH HOH F . 
YA 6 HOH 229 2229 2229 HOH HOH F . 
YA 6 HOH 230 2230 2230 HOH HOH F . 
YA 6 HOH 231 2231 2231 HOH HOH F . 
YA 6 HOH 232 2232 2232 HOH HOH F . 
YA 6 HOH 233 2233 2233 HOH HOH F . 
YA 6 HOH 234 2234 2234 HOH HOH F . 
YA 6 HOH 235 2235 2235 HOH HOH F . 
YA 6 HOH 236 2236 2236 HOH HOH F . 
YA 6 HOH 237 2237 2237 HOH HOH F . 
YA 6 HOH 238 2238 2238 HOH HOH F . 
ZA 6 HOH 1   2001 2001 HOH HOH G . 
ZA 6 HOH 2   2002 2002 HOH HOH G . 
ZA 6 HOH 3   2003 2003 HOH HOH G . 
ZA 6 HOH 4   2004 2004 HOH HOH G . 
ZA 6 HOH 5   2005 2005 HOH HOH G . 
ZA 6 HOH 6   2006 2006 HOH HOH G . 
ZA 6 HOH 7   2007 2007 HOH HOH G . 
ZA 6 HOH 8   2008 2008 HOH HOH G . 
ZA 6 HOH 9   2009 2009 HOH HOH G . 
ZA 6 HOH 10  2010 2010 HOH HOH G . 
ZA 6 HOH 11  2011 2011 HOH HOH G . 
ZA 6 HOH 12  2012 2012 HOH HOH G . 
ZA 6 HOH 13  2013 2013 HOH HOH G . 
ZA 6 HOH 14  2014 2014 HOH HOH G . 
ZA 6 HOH 15  2015 2015 HOH HOH G . 
ZA 6 HOH 16  2016 2016 HOH HOH G . 
ZA 6 HOH 17  2017 2017 HOH HOH G . 
ZA 6 HOH 18  2018 2018 HOH HOH G . 
ZA 6 HOH 19  2019 2019 HOH HOH G . 
ZA 6 HOH 20  2020 2020 HOH HOH G . 
ZA 6 HOH 21  2021 2021 HOH HOH G . 
ZA 6 HOH 22  2022 2022 HOH HOH G . 
ZA 6 HOH 23  2023 2023 HOH HOH G . 
ZA 6 HOH 24  2024 2024 HOH HOH G . 
ZA 6 HOH 25  2025 2025 HOH HOH G . 
ZA 6 HOH 26  2026 2026 HOH HOH G . 
ZA 6 HOH 27  2027 2027 HOH HOH G . 
ZA 6 HOH 28  2028 2028 HOH HOH G . 
ZA 6 HOH 29  2029 2029 HOH HOH G . 
ZA 6 HOH 30  2030 2030 HOH HOH G . 
ZA 6 HOH 31  2031 2031 HOH HOH G . 
ZA 6 HOH 32  2032 2032 HOH HOH G . 
ZA 6 HOH 33  2033 2033 HOH HOH G . 
ZA 6 HOH 34  2034 2034 HOH HOH G . 
ZA 6 HOH 35  2035 2035 HOH HOH G . 
ZA 6 HOH 36  2036 2036 HOH HOH G . 
ZA 6 HOH 37  2037 2037 HOH HOH G . 
ZA 6 HOH 38  2038 2038 HOH HOH G . 
ZA 6 HOH 39  2039 2039 HOH HOH G . 
ZA 6 HOH 40  2040 2040 HOH HOH G . 
ZA 6 HOH 41  2041 2041 HOH HOH G . 
ZA 6 HOH 42  2042 2042 HOH HOH G . 
ZA 6 HOH 43  2043 2043 HOH HOH G . 
ZA 6 HOH 44  2044 2044 HOH HOH G . 
ZA 6 HOH 45  2045 2045 HOH HOH G . 
ZA 6 HOH 46  2046 2046 HOH HOH G . 
ZA 6 HOH 47  2047 2047 HOH HOH G . 
ZA 6 HOH 48  2048 2048 HOH HOH G . 
ZA 6 HOH 49  2049 2049 HOH HOH G . 
ZA 6 HOH 50  2050 2050 HOH HOH G . 
ZA 6 HOH 51  2051 2051 HOH HOH G . 
ZA 6 HOH 52  2052 2052 HOH HOH G . 
ZA 6 HOH 53  2053 2053 HOH HOH G . 
ZA 6 HOH 54  2054 2054 HOH HOH G . 
ZA 6 HOH 55  2055 2055 HOH HOH G . 
ZA 6 HOH 56  2056 2056 HOH HOH G . 
ZA 6 HOH 57  2057 2057 HOH HOH G . 
ZA 6 HOH 58  2058 2058 HOH HOH G . 
ZA 6 HOH 59  2059 2059 HOH HOH G . 
ZA 6 HOH 60  2060 2060 HOH HOH G . 
ZA 6 HOH 61  2061 2061 HOH HOH G . 
ZA 6 HOH 62  2062 2062 HOH HOH G . 
ZA 6 HOH 63  2063 2063 HOH HOH G . 
ZA 6 HOH 64  2064 2064 HOH HOH G . 
ZA 6 HOH 65  2065 2065 HOH HOH G . 
ZA 6 HOH 66  2066 2066 HOH HOH G . 
ZA 6 HOH 67  2067 2067 HOH HOH G . 
ZA 6 HOH 68  2068 2068 HOH HOH G . 
ZA 6 HOH 69  2069 2069 HOH HOH G . 
ZA 6 HOH 70  2070 2070 HOH HOH G . 
ZA 6 HOH 71  2071 2071 HOH HOH G . 
ZA 6 HOH 72  2072 2072 HOH HOH G . 
ZA 6 HOH 73  2073 2073 HOH HOH G . 
ZA 6 HOH 74  2074 2074 HOH HOH G . 
ZA 6 HOH 75  2075 2075 HOH HOH G . 
ZA 6 HOH 76  2076 2076 HOH HOH G . 
ZA 6 HOH 77  2077 2077 HOH HOH G . 
ZA 6 HOH 78  2078 2078 HOH HOH G . 
ZA 6 HOH 79  2079 2079 HOH HOH G . 
ZA 6 HOH 80  2080 2080 HOH HOH G . 
ZA 6 HOH 81  2081 2081 HOH HOH G . 
ZA 6 HOH 82  2082 2082 HOH HOH G . 
ZA 6 HOH 83  2083 2083 HOH HOH G . 
ZA 6 HOH 84  2084 2084 HOH HOH G . 
ZA 6 HOH 85  2085 2085 HOH HOH G . 
ZA 6 HOH 86  2086 2086 HOH HOH G . 
ZA 6 HOH 87  2087 2087 HOH HOH G . 
ZA 6 HOH 88  2088 2088 HOH HOH G . 
ZA 6 HOH 89  2089 2089 HOH HOH G . 
ZA 6 HOH 90  2090 2090 HOH HOH G . 
ZA 6 HOH 91  2091 2091 HOH HOH G . 
ZA 6 HOH 92  2092 2092 HOH HOH G . 
ZA 6 HOH 93  2093 2093 HOH HOH G . 
ZA 6 HOH 94  2094 2094 HOH HOH G . 
ZA 6 HOH 95  2095 2095 HOH HOH G . 
ZA 6 HOH 96  2096 2096 HOH HOH G . 
ZA 6 HOH 97  2097 2097 HOH HOH G . 
ZA 6 HOH 98  2098 2098 HOH HOH G . 
ZA 6 HOH 99  2099 2099 HOH HOH G . 
ZA 6 HOH 100 2100 2100 HOH HOH G . 
ZA 6 HOH 101 2101 2101 HOH HOH G . 
ZA 6 HOH 102 2102 2102 HOH HOH G . 
ZA 6 HOH 103 2103 2103 HOH HOH G . 
ZA 6 HOH 104 2104 2104 HOH HOH G . 
ZA 6 HOH 105 2105 2105 HOH HOH G . 
ZA 6 HOH 106 2106 2106 HOH HOH G . 
ZA 6 HOH 107 2107 2107 HOH HOH G . 
ZA 6 HOH 108 2108 2108 HOH HOH G . 
ZA 6 HOH 109 2109 2109 HOH HOH G . 
ZA 6 HOH 110 2110 2110 HOH HOH G . 
ZA 6 HOH 111 2111 2111 HOH HOH G . 
ZA 6 HOH 112 2112 2112 HOH HOH G . 
ZA 6 HOH 113 2113 2113 HOH HOH G . 
ZA 6 HOH 114 2114 2114 HOH HOH G . 
ZA 6 HOH 115 2115 2115 HOH HOH G . 
ZA 6 HOH 116 2116 2116 HOH HOH G . 
ZA 6 HOH 117 2117 2117 HOH HOH G . 
ZA 6 HOH 118 2118 2118 HOH HOH G . 
ZA 6 HOH 119 2119 2119 HOH HOH G . 
ZA 6 HOH 120 2120 2120 HOH HOH G . 
ZA 6 HOH 121 2121 2121 HOH HOH G . 
ZA 6 HOH 122 2122 2122 HOH HOH G . 
ZA 6 HOH 123 2123 2123 HOH HOH G . 
ZA 6 HOH 124 2124 2124 HOH HOH G . 
ZA 6 HOH 125 2125 2125 HOH HOH G . 
ZA 6 HOH 126 2126 2126 HOH HOH G . 
ZA 6 HOH 127 2127 2127 HOH HOH G . 
ZA 6 HOH 128 2128 2128 HOH HOH G . 
ZA 6 HOH 129 2129 2129 HOH HOH G . 
ZA 6 HOH 130 2130 2130 HOH HOH G . 
ZA 6 HOH 131 2131 2131 HOH HOH G . 
ZA 6 HOH 132 2132 2132 HOH HOH G . 
ZA 6 HOH 133 2133 2133 HOH HOH G . 
ZA 6 HOH 134 2134 2134 HOH HOH G . 
ZA 6 HOH 135 2135 2135 HOH HOH G . 
ZA 6 HOH 136 2136 2136 HOH HOH G . 
ZA 6 HOH 137 2137 2137 HOH HOH G . 
ZA 6 HOH 138 2138 2138 HOH HOH G . 
ZA 6 HOH 139 2139 2139 HOH HOH G . 
ZA 6 HOH 140 2140 2140 HOH HOH G . 
ZA 6 HOH 141 2141 2141 HOH HOH G . 
ZA 6 HOH 142 2142 2142 HOH HOH G . 
ZA 6 HOH 143 2143 2143 HOH HOH G . 
ZA 6 HOH 144 2144 2144 HOH HOH G . 
ZA 6 HOH 145 2145 2145 HOH HOH G . 
ZA 6 HOH 146 2146 2146 HOH HOH G . 
ZA 6 HOH 147 2147 2147 HOH HOH G . 
ZA 6 HOH 148 2148 2148 HOH HOH G . 
ZA 6 HOH 149 2149 2149 HOH HOH G . 
ZA 6 HOH 150 2150 2150 HOH HOH G . 
ZA 6 HOH 151 2151 2151 HOH HOH G . 
ZA 6 HOH 152 2152 2152 HOH HOH G . 
ZA 6 HOH 153 2153 2153 HOH HOH G . 
ZA 6 HOH 154 2154 2154 HOH HOH G . 
ZA 6 HOH 155 2155 2155 HOH HOH G . 
ZA 6 HOH 156 2156 2156 HOH HOH G . 
ZA 6 HOH 157 2157 2157 HOH HOH G . 
ZA 6 HOH 158 2158 2158 HOH HOH G . 
ZA 6 HOH 159 2159 2159 HOH HOH G . 
ZA 6 HOH 160 2160 2160 HOH HOH G . 
ZA 6 HOH 161 2161 2161 HOH HOH G . 
ZA 6 HOH 162 2162 2162 HOH HOH G . 
ZA 6 HOH 163 2163 2163 HOH HOH G . 
ZA 6 HOH 164 2164 2164 HOH HOH G . 
ZA 6 HOH 165 2165 2165 HOH HOH G . 
ZA 6 HOH 166 2166 2166 HOH HOH G . 
ZA 6 HOH 167 2167 2167 HOH HOH G . 
ZA 6 HOH 168 2168 2168 HOH HOH G . 
ZA 6 HOH 169 2169 2169 HOH HOH G . 
ZA 6 HOH 170 2170 2170 HOH HOH G . 
ZA 6 HOH 171 2171 2171 HOH HOH G . 
ZA 6 HOH 172 2172 2172 HOH HOH G . 
ZA 6 HOH 173 2173 2173 HOH HOH G . 
ZA 6 HOH 174 2174 2174 HOH HOH G . 
ZA 6 HOH 175 2175 2175 HOH HOH G . 
ZA 6 HOH 176 2176 2176 HOH HOH G . 
ZA 6 HOH 177 2177 2177 HOH HOH G . 
ZA 6 HOH 178 2178 2178 HOH HOH G . 
ZA 6 HOH 179 2179 2179 HOH HOH G . 
ZA 6 HOH 180 2180 2180 HOH HOH G . 
ZA 6 HOH 181 2181 2181 HOH HOH G . 
ZA 6 HOH 182 2182 2182 HOH HOH G . 
ZA 6 HOH 183 2183 2183 HOH HOH G . 
ZA 6 HOH 184 2184 2184 HOH HOH G . 
ZA 6 HOH 185 2185 2185 HOH HOH G . 
ZA 6 HOH 186 2186 2186 HOH HOH G . 
ZA 6 HOH 187 2187 2187 HOH HOH G . 
AB 6 HOH 1   2001 2001 HOH HOH H . 
AB 6 HOH 2   2002 2002 HOH HOH H . 
AB 6 HOH 3   2003 2003 HOH HOH H . 
AB 6 HOH 4   2004 2004 HOH HOH H . 
AB 6 HOH 5   2005 2005 HOH HOH H . 
AB 6 HOH 6   2006 2006 HOH HOH H . 
AB 6 HOH 7   2007 2007 HOH HOH H . 
AB 6 HOH 8   2008 2008 HOH HOH H . 
AB 6 HOH 9   2009 2009 HOH HOH H . 
AB 6 HOH 10  2010 2010 HOH HOH H . 
AB 6 HOH 11  2011 2011 HOH HOH H . 
AB 6 HOH 12  2012 2012 HOH HOH H . 
AB 6 HOH 13  2013 2013 HOH HOH H . 
AB 6 HOH 14  2014 2014 HOH HOH H . 
AB 6 HOH 15  2015 2015 HOH HOH H . 
AB 6 HOH 16  2016 2016 HOH HOH H . 
AB 6 HOH 17  2017 2017 HOH HOH H . 
AB 6 HOH 18  2018 2018 HOH HOH H . 
AB 6 HOH 19  2019 2019 HOH HOH H . 
AB 6 HOH 20  2020 2020 HOH HOH H . 
AB 6 HOH 21  2021 2021 HOH HOH H . 
AB 6 HOH 22  2022 2022 HOH HOH H . 
AB 6 HOH 23  2023 2023 HOH HOH H . 
AB 6 HOH 24  2024 2024 HOH HOH H . 
AB 6 HOH 25  2025 2025 HOH HOH H . 
AB 6 HOH 26  2026 2026 HOH HOH H . 
AB 6 HOH 27  2027 2027 HOH HOH H . 
AB 6 HOH 28  2028 2028 HOH HOH H . 
AB 6 HOH 29  2029 2029 HOH HOH H . 
AB 6 HOH 30  2030 2030 HOH HOH H . 
AB 6 HOH 31  2031 2031 HOH HOH H . 
AB 6 HOH 32  2032 2032 HOH HOH H . 
AB 6 HOH 33  2033 2033 HOH HOH H . 
AB 6 HOH 34  2034 2034 HOH HOH H . 
AB 6 HOH 35  2035 2035 HOH HOH H . 
AB 6 HOH 36  2036 2036 HOH HOH H . 
AB 6 HOH 37  2037 2037 HOH HOH H . 
AB 6 HOH 38  2038 2038 HOH HOH H . 
AB 6 HOH 39  2039 2039 HOH HOH H . 
AB 6 HOH 40  2040 2040 HOH HOH H . 
AB 6 HOH 41  2041 2041 HOH HOH H . 
AB 6 HOH 42  2042 2042 HOH HOH H . 
AB 6 HOH 43  2043 2043 HOH HOH H . 
AB 6 HOH 44  2044 2044 HOH HOH H . 
AB 6 HOH 45  2045 2045 HOH HOH H . 
AB 6 HOH 46  2046 2046 HOH HOH H . 
AB 6 HOH 47  2047 2047 HOH HOH H . 
AB 6 HOH 48  2048 2048 HOH HOH H . 
AB 6 HOH 49  2049 2049 HOH HOH H . 
AB 6 HOH 50  2050 2050 HOH HOH H . 
AB 6 HOH 51  2051 2051 HOH HOH H . 
AB 6 HOH 52  2052 2052 HOH HOH H . 
AB 6 HOH 53  2053 2053 HOH HOH H . 
AB 6 HOH 54  2054 2054 HOH HOH H . 
AB 6 HOH 55  2055 2055 HOH HOH H . 
AB 6 HOH 56  2056 2056 HOH HOH H . 
AB 6 HOH 57  2057 2057 HOH HOH H . 
AB 6 HOH 58  2058 2058 HOH HOH H . 
AB 6 HOH 59  2059 2059 HOH HOH H . 
AB 6 HOH 60  2060 2060 HOH HOH H . 
AB 6 HOH 61  2061 2061 HOH HOH H . 
AB 6 HOH 62  2062 2062 HOH HOH H . 
AB 6 HOH 63  2063 2063 HOH HOH H . 
AB 6 HOH 64  2064 2064 HOH HOH H . 
AB 6 HOH 65  2065 2065 HOH HOH H . 
AB 6 HOH 66  2066 2066 HOH HOH H . 
AB 6 HOH 67  2067 2067 HOH HOH H . 
AB 6 HOH 68  2068 2068 HOH HOH H . 
AB 6 HOH 69  2069 2069 HOH HOH H . 
AB 6 HOH 70  2070 2070 HOH HOH H . 
AB 6 HOH 71  2071 2071 HOH HOH H . 
AB 6 HOH 72  2072 2072 HOH HOH H . 
AB 6 HOH 73  2073 2073 HOH HOH H . 
AB 6 HOH 74  2074 2074 HOH HOH H . 
AB 6 HOH 75  2075 2075 HOH HOH H . 
AB 6 HOH 76  2076 2076 HOH HOH H . 
AB 6 HOH 77  2077 2077 HOH HOH H . 
AB 6 HOH 78  2078 2078 HOH HOH H . 
AB 6 HOH 79  2079 2079 HOH HOH H . 
AB 6 HOH 80  2080 2080 HOH HOH H . 
AB 6 HOH 81  2081 2081 HOH HOH H . 
AB 6 HOH 82  2082 2082 HOH HOH H . 
AB 6 HOH 83  2083 2083 HOH HOH H . 
AB 6 HOH 84  2084 2084 HOH HOH H . 
AB 6 HOH 85  2085 2085 HOH HOH H . 
AB 6 HOH 86  2086 2086 HOH HOH H . 
AB 6 HOH 87  2087 2087 HOH HOH H . 
AB 6 HOH 88  2088 2088 HOH HOH H . 
AB 6 HOH 89  2089 2089 HOH HOH H . 
AB 6 HOH 90  2090 2090 HOH HOH H . 
AB 6 HOH 91  2091 2091 HOH HOH H . 
AB 6 HOH 92  2092 2092 HOH HOH H . 
AB 6 HOH 93  2093 2093 HOH HOH H . 
AB 6 HOH 94  2094 2094 HOH HOH H . 
AB 6 HOH 95  2095 2095 HOH HOH H . 
AB 6 HOH 96  2096 2096 HOH HOH H . 
AB 6 HOH 97  2097 2097 HOH HOH H . 
AB 6 HOH 98  2098 2098 HOH HOH H . 
AB 6 HOH 99  2099 2099 HOH HOH H . 
AB 6 HOH 100 2100 2100 HOH HOH H . 
AB 6 HOH 101 2101 2101 HOH HOH H . 
AB 6 HOH 102 2102 2102 HOH HOH H . 
AB 6 HOH 103 2103 2103 HOH HOH H . 
AB 6 HOH 104 2104 2104 HOH HOH H . 
AB 6 HOH 105 2105 2105 HOH HOH H . 
AB 6 HOH 106 2106 2106 HOH HOH H . 
AB 6 HOH 107 2107 2107 HOH HOH H . 
AB 6 HOH 108 2108 2108 HOH HOH H . 
AB 6 HOH 109 2109 2109 HOH HOH H . 
AB 6 HOH 110 2110 2110 HOH HOH H . 
AB 6 HOH 111 2111 2111 HOH HOH H . 
AB 6 HOH 112 2112 2112 HOH HOH H . 
AB 6 HOH 113 2113 2113 HOH HOH H . 
AB 6 HOH 114 2114 2114 HOH HOH H . 
AB 6 HOH 115 2115 2115 HOH HOH H . 
AB 6 HOH 116 2116 2116 HOH HOH H . 
AB 6 HOH 117 2117 2117 HOH HOH H . 
AB 6 HOH 118 2118 2118 HOH HOH H . 
AB 6 HOH 119 2119 2119 HOH HOH H . 
AB 6 HOH 120 2120 2120 HOH HOH H . 
AB 6 HOH 121 2121 2121 HOH HOH H . 
AB 6 HOH 122 2122 2122 HOH HOH H . 
AB 6 HOH 123 2123 2123 HOH HOH H . 
AB 6 HOH 124 2124 2124 HOH HOH H . 
AB 6 HOH 125 2125 2125 HOH HOH H . 
AB 6 HOH 126 2126 2126 HOH HOH H . 
AB 6 HOH 127 2127 2127 HOH HOH H . 
AB 6 HOH 128 2128 2128 HOH HOH H . 
AB 6 HOH 129 2129 2129 HOH HOH H . 
AB 6 HOH 130 2130 2130 HOH HOH H . 
AB 6 HOH 131 2131 2131 HOH HOH H . 
AB 6 HOH 132 2132 2132 HOH HOH H . 
AB 6 HOH 133 2133 2133 HOH HOH H . 
AB 6 HOH 134 2134 2134 HOH HOH H . 
AB 6 HOH 135 2135 2135 HOH HOH H . 
AB 6 HOH 136 2136 2136 HOH HOH H . 
AB 6 HOH 137 2137 2137 HOH HOH H . 
AB 6 HOH 138 2138 2138 HOH HOH H . 
AB 6 HOH 139 2139 2139 HOH HOH H . 
AB 6 HOH 140 2140 2140 HOH HOH H . 
AB 6 HOH 141 2141 2141 HOH HOH H . 
AB 6 HOH 142 2142 2142 HOH HOH H . 
AB 6 HOH 143 2143 2143 HOH HOH H . 
AB 6 HOH 144 2144 2144 HOH HOH H . 
AB 6 HOH 145 2145 2145 HOH HOH H . 
AB 6 HOH 146 2146 2146 HOH HOH H . 
AB 6 HOH 147 2147 2147 HOH HOH H . 
AB 6 HOH 148 2148 2148 HOH HOH H . 
AB 6 HOH 149 2149 2149 HOH HOH H . 
AB 6 HOH 150 2150 2150 HOH HOH H . 
AB 6 HOH 151 2151 2151 HOH HOH H . 
AB 6 HOH 152 2152 2152 HOH HOH H . 
BB 6 HOH 1   2001 2001 HOH HOH I . 
BB 6 HOH 2   2002 2002 HOH HOH I . 
BB 6 HOH 3   2003 2003 HOH HOH I . 
BB 6 HOH 4   2004 2004 HOH HOH I . 
BB 6 HOH 5   2005 2005 HOH HOH I . 
BB 6 HOH 6   2006 2006 HOH HOH I . 
BB 6 HOH 7   2007 2007 HOH HOH I . 
BB 6 HOH 8   2008 2008 HOH HOH I . 
BB 6 HOH 9   2009 2009 HOH HOH I . 
BB 6 HOH 10  2010 2010 HOH HOH I . 
BB 6 HOH 11  2011 2011 HOH HOH I . 
BB 6 HOH 12  2012 2012 HOH HOH I . 
BB 6 HOH 13  2013 2013 HOH HOH I . 
BB 6 HOH 14  2014 2014 HOH HOH I . 
BB 6 HOH 15  2015 2015 HOH HOH I . 
BB 6 HOH 16  2016 2016 HOH HOH I . 
BB 6 HOH 17  2017 2017 HOH HOH I . 
BB 6 HOH 18  2018 2018 HOH HOH I . 
BB 6 HOH 19  2019 2019 HOH HOH I . 
BB 6 HOH 20  2020 2020 HOH HOH I . 
BB 6 HOH 21  2021 2021 HOH HOH I . 
BB 6 HOH 22  2022 2022 HOH HOH I . 
BB 6 HOH 23  2023 2023 HOH HOH I . 
BB 6 HOH 24  2024 2024 HOH HOH I . 
BB 6 HOH 25  2025 2025 HOH HOH I . 
BB 6 HOH 26  2026 2026 HOH HOH I . 
BB 6 HOH 27  2027 2027 HOH HOH I . 
BB 6 HOH 28  2028 2028 HOH HOH I . 
BB 6 HOH 29  2029 2029 HOH HOH I . 
BB 6 HOH 30  2030 2030 HOH HOH I . 
BB 6 HOH 31  2031 2031 HOH HOH I . 
BB 6 HOH 32  2032 2032 HOH HOH I . 
BB 6 HOH 33  2033 2033 HOH HOH I . 
BB 6 HOH 34  2034 2034 HOH HOH I . 
BB 6 HOH 35  2035 2035 HOH HOH I . 
BB 6 HOH 36  2036 2036 HOH HOH I . 
BB 6 HOH 37  2037 2037 HOH HOH I . 
BB 6 HOH 38  2038 2038 HOH HOH I . 
BB 6 HOH 39  2039 2039 HOH HOH I . 
BB 6 HOH 40  2040 2040 HOH HOH I . 
BB 6 HOH 41  2041 2041 HOH HOH I . 
BB 6 HOH 42  2042 2042 HOH HOH I . 
BB 6 HOH 43  2043 2043 HOH HOH I . 
BB 6 HOH 44  2044 2044 HOH HOH I . 
BB 6 HOH 45  2045 2045 HOH HOH I . 
BB 6 HOH 46  2046 2046 HOH HOH I . 
BB 6 HOH 47  2047 2047 HOH HOH I . 
BB 6 HOH 48  2048 2048 HOH HOH I . 
BB 6 HOH 49  2049 2049 HOH HOH I . 
BB 6 HOH 50  2050 2050 HOH HOH I . 
BB 6 HOH 51  2051 2051 HOH HOH I . 
BB 6 HOH 52  2052 2052 HOH HOH I . 
BB 6 HOH 53  2053 2053 HOH HOH I . 
BB 6 HOH 54  2054 2054 HOH HOH I . 
BB 6 HOH 55  2055 2055 HOH HOH I . 
BB 6 HOH 56  2056 2056 HOH HOH I . 
BB 6 HOH 57  2057 2057 HOH HOH I . 
BB 6 HOH 58  2058 2058 HOH HOH I . 
BB 6 HOH 59  2059 2059 HOH HOH I . 
BB 6 HOH 60  2060 2060 HOH HOH I . 
BB 6 HOH 61  2061 2061 HOH HOH I . 
BB 6 HOH 62  2062 2062 HOH HOH I . 
BB 6 HOH 63  2063 2063 HOH HOH I . 
BB 6 HOH 64  2064 2064 HOH HOH I . 
BB 6 HOH 65  2065 2065 HOH HOH I . 
BB 6 HOH 66  2066 2066 HOH HOH I . 
BB 6 HOH 67  2067 2067 HOH HOH I . 
BB 6 HOH 68  2068 2068 HOH HOH I . 
BB 6 HOH 69  2069 2069 HOH HOH I . 
BB 6 HOH 70  2070 2070 HOH HOH I . 
BB 6 HOH 71  2071 2071 HOH HOH I . 
BB 6 HOH 72  2072 2072 HOH HOH I . 
BB 6 HOH 73  2073 2073 HOH HOH I . 
BB 6 HOH 74  2074 2074 HOH HOH I . 
BB 6 HOH 75  2075 2075 HOH HOH I . 
BB 6 HOH 76  2076 2076 HOH HOH I . 
BB 6 HOH 77  2077 2077 HOH HOH I . 
BB 6 HOH 78  2078 2078 HOH HOH I . 
BB 6 HOH 79  2079 2079 HOH HOH I . 
BB 6 HOH 80  2080 2080 HOH HOH I . 
BB 6 HOH 81  2081 2081 HOH HOH I . 
BB 6 HOH 82  2082 2082 HOH HOH I . 
BB 6 HOH 83  2083 2083 HOH HOH I . 
BB 6 HOH 84  2084 2084 HOH HOH I . 
BB 6 HOH 85  2085 2085 HOH HOH I . 
BB 6 HOH 86  2086 2086 HOH HOH I . 
BB 6 HOH 87  2087 2087 HOH HOH I . 
BB 6 HOH 88  2088 2088 HOH HOH I . 
BB 6 HOH 89  2089 2089 HOH HOH I . 
BB 6 HOH 90  2090 2090 HOH HOH I . 
BB 6 HOH 91  2091 2091 HOH HOH I . 
BB 6 HOH 92  2092 2092 HOH HOH I . 
BB 6 HOH 93  2093 2093 HOH HOH I . 
BB 6 HOH 94  2094 2094 HOH HOH I . 
BB 6 HOH 95  2095 2095 HOH HOH I . 
BB 6 HOH 96  2096 2096 HOH HOH I . 
BB 6 HOH 97  2097 2097 HOH HOH I . 
BB 6 HOH 98  2098 2098 HOH HOH I . 
BB 6 HOH 99  2099 2099 HOH HOH I . 
BB 6 HOH 100 2100 2100 HOH HOH I . 
BB 6 HOH 101 2101 2101 HOH HOH I . 
BB 6 HOH 102 2102 2102 HOH HOH I . 
BB 6 HOH 103 2103 2103 HOH HOH I . 
BB 6 HOH 104 2104 2104 HOH HOH I . 
BB 6 HOH 105 2105 2105 HOH HOH I . 
BB 6 HOH 106 2106 2106 HOH HOH I . 
BB 6 HOH 107 2107 2107 HOH HOH I . 
BB 6 HOH 108 2108 2108 HOH HOH I . 
BB 6 HOH 109 2109 2109 HOH HOH I . 
BB 6 HOH 110 2110 2110 HOH HOH I . 
BB 6 HOH 111 2111 2111 HOH HOH I . 
BB 6 HOH 112 2112 2112 HOH HOH I . 
BB 6 HOH 113 2113 2113 HOH HOH I . 
BB 6 HOH 114 2114 2114 HOH HOH I . 
BB 6 HOH 115 2115 2115 HOH HOH I . 
BB 6 HOH 116 2116 2116 HOH HOH I . 
BB 6 HOH 117 2117 2117 HOH HOH I . 
BB 6 HOH 118 2118 2118 HOH HOH I . 
BB 6 HOH 119 2119 2119 HOH HOH I . 
BB 6 HOH 120 2120 2120 HOH HOH I . 
BB 6 HOH 121 2121 2121 HOH HOH I . 
BB 6 HOH 122 2122 2122 HOH HOH I . 
BB 6 HOH 123 2123 2123 HOH HOH I . 
BB 6 HOH 124 2124 2124 HOH HOH I . 
BB 6 HOH 125 2125 2125 HOH HOH I . 
BB 6 HOH 126 2126 2126 HOH HOH I . 
BB 6 HOH 127 2127 2127 HOH HOH I . 
BB 6 HOH 128 2128 2128 HOH HOH I . 
BB 6 HOH 129 2129 2129 HOH HOH I . 
BB 6 HOH 130 2130 2130 HOH HOH I . 
BB 6 HOH 131 2131 2131 HOH HOH I . 
BB 6 HOH 132 2132 2132 HOH HOH I . 
BB 6 HOH 133 2133 2133 HOH HOH I . 
BB 6 HOH 134 2134 2134 HOH HOH I . 
BB 6 HOH 135 2135 2135 HOH HOH I . 
BB 6 HOH 136 2136 2136 HOH HOH I . 
BB 6 HOH 137 2137 2137 HOH HOH I . 
BB 6 HOH 138 2138 2138 HOH HOH I . 
BB 6 HOH 139 2139 2139 HOH HOH I . 
BB 6 HOH 140 2140 2140 HOH HOH I . 
BB 6 HOH 141 2141 2141 HOH HOH I . 
BB 6 HOH 142 2142 2142 HOH HOH I . 
BB 6 HOH 143 2143 2143 HOH HOH I . 
BB 6 HOH 144 2144 2144 HOH HOH I . 
BB 6 HOH 145 2145 2145 HOH HOH I . 
BB 6 HOH 146 2146 2146 HOH HOH I . 
BB 6 HOH 147 2147 2147 HOH HOH I . 
BB 6 HOH 148 2148 2148 HOH HOH I . 
BB 6 HOH 149 2149 2149 HOH HOH I . 
BB 6 HOH 150 2150 2150 HOH HOH I . 
BB 6 HOH 151 2151 2151 HOH HOH I . 
BB 6 HOH 152 2152 2152 HOH HOH I . 
BB 6 HOH 153 2153 2153 HOH HOH I . 
BB 6 HOH 154 2154 2154 HOH HOH I . 
BB 6 HOH 155 2155 2155 HOH HOH I . 
BB 6 HOH 156 2156 2156 HOH HOH I . 
BB 6 HOH 157 2157 2157 HOH HOH I . 
BB 6 HOH 158 2158 2158 HOH HOH I . 
BB 6 HOH 159 2159 2159 HOH HOH I . 
BB 6 HOH 160 2160 2160 HOH HOH I . 
BB 6 HOH 161 2161 2161 HOH HOH I . 
BB 6 HOH 162 2162 2162 HOH HOH I . 
BB 6 HOH 163 2163 2163 HOH HOH I . 
BB 6 HOH 164 2164 2164 HOH HOH I . 
BB 6 HOH 165 2165 2165 HOH HOH I . 
BB 6 HOH 166 2166 2166 HOH HOH I . 
BB 6 HOH 167 2167 2167 HOH HOH I . 
CB 6 HOH 1   2001 2001 HOH HOH J . 
CB 6 HOH 2   2002 2002 HOH HOH J . 
CB 6 HOH 3   2003 2003 HOH HOH J . 
CB 6 HOH 4   2004 2004 HOH HOH J . 
CB 6 HOH 5   2005 2005 HOH HOH J . 
CB 6 HOH 6   2006 2006 HOH HOH J . 
CB 6 HOH 7   2007 2007 HOH HOH J . 
CB 6 HOH 8   2008 2008 HOH HOH J . 
CB 6 HOH 9   2009 2009 HOH HOH J . 
CB 6 HOH 10  2010 2010 HOH HOH J . 
CB 6 HOH 11  2011 2011 HOH HOH J . 
CB 6 HOH 12  2012 2012 HOH HOH J . 
CB 6 HOH 13  2013 2013 HOH HOH J . 
CB 6 HOH 14  2014 2014 HOH HOH J . 
CB 6 HOH 15  2015 2015 HOH HOH J . 
CB 6 HOH 16  2016 2016 HOH HOH J . 
CB 6 HOH 17  2017 2017 HOH HOH J . 
CB 6 HOH 18  2018 2018 HOH HOH J . 
CB 6 HOH 19  2019 2019 HOH HOH J . 
CB 6 HOH 20  2020 2020 HOH HOH J . 
CB 6 HOH 21  2021 2021 HOH HOH J . 
CB 6 HOH 22  2022 2022 HOH HOH J . 
CB 6 HOH 23  2023 2023 HOH HOH J . 
CB 6 HOH 24  2024 2024 HOH HOH J . 
CB 6 HOH 25  2025 2025 HOH HOH J . 
CB 6 HOH 26  2026 2026 HOH HOH J . 
CB 6 HOH 27  2027 2027 HOH HOH J . 
CB 6 HOH 28  2028 2028 HOH HOH J . 
CB 6 HOH 29  2029 2029 HOH HOH J . 
CB 6 HOH 30  2030 2030 HOH HOH J . 
CB 6 HOH 31  2031 2031 HOH HOH J . 
CB 6 HOH 32  2032 2032 HOH HOH J . 
CB 6 HOH 33  2033 2033 HOH HOH J . 
CB 6 HOH 34  2034 2034 HOH HOH J . 
CB 6 HOH 35  2035 2035 HOH HOH J . 
CB 6 HOH 36  2036 2036 HOH HOH J . 
CB 6 HOH 37  2037 2037 HOH HOH J . 
CB 6 HOH 38  2038 2038 HOH HOH J . 
CB 6 HOH 39  2039 2039 HOH HOH J . 
CB 6 HOH 40  2040 2040 HOH HOH J . 
CB 6 HOH 41  2041 2041 HOH HOH J . 
CB 6 HOH 42  2042 2042 HOH HOH J . 
CB 6 HOH 43  2043 2043 HOH HOH J . 
CB 6 HOH 44  2044 2044 HOH HOH J . 
CB 6 HOH 45  2045 2045 HOH HOH J . 
CB 6 HOH 46  2046 2046 HOH HOH J . 
CB 6 HOH 47  2047 2047 HOH HOH J . 
CB 6 HOH 48  2048 2048 HOH HOH J . 
CB 6 HOH 49  2049 2049 HOH HOH J . 
CB 6 HOH 50  2050 2050 HOH HOH J . 
CB 6 HOH 51  2051 2051 HOH HOH J . 
CB 6 HOH 52  2052 2052 HOH HOH J . 
CB 6 HOH 53  2053 2053 HOH HOH J . 
CB 6 HOH 54  2054 2054 HOH HOH J . 
CB 6 HOH 55  2055 2055 HOH HOH J . 
CB 6 HOH 56  2056 2056 HOH HOH J . 
CB 6 HOH 57  2057 2057 HOH HOH J . 
CB 6 HOH 58  2058 2058 HOH HOH J . 
CB 6 HOH 59  2059 2059 HOH HOH J . 
CB 6 HOH 60  2060 2060 HOH HOH J . 
CB 6 HOH 61  2061 2061 HOH HOH J . 
CB 6 HOH 62  2062 2062 HOH HOH J . 
CB 6 HOH 63  2063 2063 HOH HOH J . 
CB 6 HOH 64  2064 2064 HOH HOH J . 
CB 6 HOH 65  2065 2065 HOH HOH J . 
CB 6 HOH 66  2066 2066 HOH HOH J . 
CB 6 HOH 67  2067 2067 HOH HOH J . 
CB 6 HOH 68  2068 2068 HOH HOH J . 
CB 6 HOH 69  2069 2069 HOH HOH J . 
CB 6 HOH 70  2070 2070 HOH HOH J . 
CB 6 HOH 71  2071 2071 HOH HOH J . 
CB 6 HOH 72  2072 2072 HOH HOH J . 
CB 6 HOH 73  2073 2073 HOH HOH J . 
CB 6 HOH 74  2074 2074 HOH HOH J . 
CB 6 HOH 75  2075 2075 HOH HOH J . 
CB 6 HOH 76  2076 2076 HOH HOH J . 
CB 6 HOH 77  2077 2077 HOH HOH J . 
CB 6 HOH 78  2078 2078 HOH HOH J . 
CB 6 HOH 79  2079 2079 HOH HOH J . 
CB 6 HOH 80  2080 2080 HOH HOH J . 
CB 6 HOH 81  2081 2081 HOH HOH J . 
CB 6 HOH 82  2082 2082 HOH HOH J . 
CB 6 HOH 83  2083 2083 HOH HOH J . 
CB 6 HOH 84  2084 2084 HOH HOH J . 
CB 6 HOH 85  2085 2085 HOH HOH J . 
CB 6 HOH 86  2086 2086 HOH HOH J . 
CB 6 HOH 87  2087 2087 HOH HOH J . 
CB 6 HOH 88  2088 2088 HOH HOH J . 
CB 6 HOH 89  2089 2089 HOH HOH J . 
CB 6 HOH 90  2090 2090 HOH HOH J . 
CB 6 HOH 91  2091 2091 HOH HOH J . 
CB 6 HOH 92  2092 2092 HOH HOH J . 
CB 6 HOH 93  2093 2093 HOH HOH J . 
CB 6 HOH 94  2094 2094 HOH HOH J . 
CB 6 HOH 95  2095 2095 HOH HOH J . 
CB 6 HOH 96  2096 2096 HOH HOH J . 
CB 6 HOH 97  2097 2097 HOH HOH J . 
CB 6 HOH 98  2098 2098 HOH HOH J . 
CB 6 HOH 99  2099 2099 HOH HOH J . 
CB 6 HOH 100 2100 2100 HOH HOH J . 
CB 6 HOH 101 2101 2101 HOH HOH J . 
CB 6 HOH 102 2102 2102 HOH HOH J . 
CB 6 HOH 103 2103 2103 HOH HOH J . 
CB 6 HOH 104 2104 2104 HOH HOH J . 
CB 6 HOH 105 2105 2105 HOH HOH J . 
CB 6 HOH 106 2106 2106 HOH HOH J . 
CB 6 HOH 107 2107 2107 HOH HOH J . 
CB 6 HOH 108 2108 2108 HOH HOH J . 
CB 6 HOH 109 2109 2109 HOH HOH J . 
CB 6 HOH 110 2110 2110 HOH HOH J . 
CB 6 HOH 111 2111 2111 HOH HOH J . 
CB 6 HOH 112 2112 2112 HOH HOH J . 
CB 6 HOH 113 2113 2113 HOH HOH J . 
CB 6 HOH 114 2114 2114 HOH HOH J . 
CB 6 HOH 115 2115 2115 HOH HOH J . 
CB 6 HOH 116 2116 2116 HOH HOH J . 
CB 6 HOH 117 2117 2117 HOH HOH J . 
CB 6 HOH 118 2118 2118 HOH HOH J . 
CB 6 HOH 119 2119 2119 HOH HOH J . 
CB 6 HOH 120 2120 2120 HOH HOH J . 
CB 6 HOH 121 2121 2121 HOH HOH J . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,F,K,L,M,Z,AA,BA,CA,DA,TA,YA  
2 1 B,G,N,O,P,EA,FA,GA,HA,UA,ZA    
3 1 C,H,Q,R,S,IA,JA,KA,VA,AB       
4 1 D,I,T,U,V,LA,MA,NA,WA,BB       
5 1 E,J,W,X,Y,OA,PA,QA,RA,SA,XA,CB 
# 
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)' 2210  ? 
1 MORE         -44.1 ? 
1 'SSA (A^2)'  13900 ? 
2 'ABSA (A^2)' 2060  ? 
2 MORE         -33.4 ? 
2 'SSA (A^2)'  14090 ? 
3 'ABSA (A^2)' 2130  ? 
3 MORE         -36.7 ? 
3 'SSA (A^2)'  14220 ? 
4 'ABSA (A^2)' 2090  ? 
4 MORE         -34.3 ? 
4 'SSA (A^2)'  13840 ? 
5 'ABSA (A^2)' 2080  ? 
5 MORE         -31.3 ? 
5 'SSA (A^2)'  14050 ? 
# 
_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_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   ND1 ? A  HIS 47  ? A HIS 46   ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 121 ? A HIS 120  ? 1_555 102.6 ? 
2   ND1 ? A  HIS 47  ? A HIS 46   ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 49  ? A HIS 48   ? 1_555 131.8 ? 
3   NE2 ? A  HIS 121 ? A HIS 120  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 49  ? A HIS 48   ? 1_555 119.0 ? 
4   ND1 ? A  HIS 47  ? A HIS 46   ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 O1  ? M  CO3 .   ? A CO3 156  ? 1_555 113.9 ? 
5   NE2 ? A  HIS 121 ? A HIS 120  ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 O1  ? M  CO3 .   ? A CO3 156  ? 1_555 83.7  ? 
6   NE2 ? A  HIS 49  ? A HIS 48   ? 1_555 CU ? K  CU . ? A CU 154 ? 1_555 O1  ? M  CO3 .   ? A CO3 156  ? 1_555 94.9  ? 
7   OD1 ? A  ASP 84  ? A ASP 83   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 64  ? A HIS 63   ? 1_555 109.4 ? 
8   OD1 ? A  ASP 84  ? A ASP 83   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 81  ? A HIS 80   ? 1_555 110.4 ? 
9   ND1 ? A  HIS 64  ? A HIS 63   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 81  ? A HIS 80   ? 1_555 108.7 ? 
10  OD1 ? A  ASP 84  ? A ASP 83   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 72  ? A HIS 71   ? 1_555 99.9  ? 
11  ND1 ? A  HIS 64  ? A HIS 63   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 72  ? A HIS 71   ? 1_555 106.0 ? 
12  ND1 ? A  HIS 81  ? A HIS 80   ? 1_555 ZN ? L  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 72  ? A HIS 71   ? 1_555 121.8 ? 
13  NE2 ? B  HIS 49  ? B HIS 48   ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 ND1 ? B  HIS 47  ? B HIS 46   ? 1_555 130.5 ? 
14  NE2 ? B  HIS 49  ? B HIS 48   ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 121 ? B HIS 120  ? 1_555 121.8 ? 
15  ND1 ? B  HIS 47  ? B HIS 46   ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 121 ? B HIS 120  ? 1_555 103.8 ? 
16  NE2 ? B  HIS 49  ? B HIS 48   ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 O2  ? P  CO3 .   ? B CO3 156  ? 1_555 94.3  ? 
17  ND1 ? B  HIS 47  ? B HIS 46   ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 O2  ? P  CO3 .   ? B CO3 156  ? 1_555 107.7 ? 
18  NE2 ? B  HIS 121 ? B HIS 120  ? 1_555 CU ? N  CU . ? B CU 154 ? 1_555 O2  ? P  CO3 .   ? B CO3 156  ? 1_555 86.4  ? 
19  OD1 ? B  ASP 84  ? B ASP 83   ? 1_555 ZN ? O  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 64  ? B HIS 63   ? 1_555 97.6  ? 
20  OD1 ? B  ASP 84  ? B ASP 83   ? 1_555 ZN ? O  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 72  ? B HIS 71   ? 1_555 101.6 ? 
21  ND1 ? B  HIS 64  ? B HIS 63   ? 1_555 ZN ? O  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 72  ? B HIS 71   ? 1_555 107.0 ? 
22  ND1 ? C  HIS 47  ? C HIS 46   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 64  ? C HIS 63   ? 1_555 78.6  ? 
23  ND1 ? C  HIS 47  ? C HIS 46   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 121 ? C HIS 120  ? 1_555 102.9 ? 
24  NE2 ? C  HIS 64  ? C HIS 63   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 121 ? C HIS 120  ? 1_555 138.2 ? 
25  ND1 ? C  HIS 47  ? C HIS 46   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 O   ? VA HOH .   ? C HOH 2086 ? 1_555 116.2 ? 
26  NE2 ? C  HIS 64  ? C HIS 63   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 O   ? VA HOH .   ? C HOH 2086 ? 1_555 62.8  ? 
27  NE2 ? C  HIS 121 ? C HIS 120  ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 O   ? VA HOH .   ? C HOH 2086 ? 1_555 80.4  ? 
28  ND1 ? C  HIS 47  ? C HIS 46   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 49  ? C HIS 48   ? 1_555 139.6 ? 
29  NE2 ? C  HIS 64  ? C HIS 63   ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 49  ? C HIS 48   ? 1_555 90.6  ? 
30  NE2 ? C  HIS 121 ? C HIS 120  ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 49  ? C HIS 48   ? 1_555 110.5 ? 
31  O   ? VA HOH .   ? C HOH 2086 ? 1_555 CU ? Q  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 49  ? C HIS 48   ? 1_555 91.7  ? 
32  ND1 ? C  HIS 81  ? C HIS 80   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 OD1 ? C  ASP 84  ? C ASP 83   ? 1_555 110.3 ? 
33  ND1 ? C  HIS 81  ? C HIS 80   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 64  ? C HIS 63   ? 1_555 109.6 ? 
34  OD1 ? C  ASP 84  ? C ASP 83   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 64  ? C HIS 63   ? 1_555 103.6 ? 
35  ND1 ? C  HIS 81  ? C HIS 80   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 72  ? C HIS 71   ? 1_555 125.2 ? 
36  OD1 ? C  ASP 84  ? C ASP 83   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 72  ? C HIS 71   ? 1_555 100.6 ? 
37  ND1 ? C  HIS 64  ? C HIS 63   ? 1_555 ZN ? R  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 72  ? C HIS 71   ? 1_555 105.3 ? 
38  NE2 ? D  HIS 49  ? D HIS 48   ? 1_555 CU ? T  CU . ? D CU 154 ? 1_555 NE2 ? D  HIS 121 ? D HIS 120  ? 1_555 118.5 ? 
39  NE2 ? D  HIS 49  ? D HIS 48   ? 1_555 CU ? T  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 47  ? D HIS 46   ? 1_555 128.1 ? 
40  NE2 ? D  HIS 121 ? D HIS 120  ? 1_555 CU ? T  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 47  ? D HIS 46   ? 1_555 97.1  ? 
41  OD1 ? D  ASP 84  ? D ASP 83   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 72  ? D HIS 71   ? 1_555 95.0  ? 
42  OD1 ? D  ASP 84  ? D ASP 83   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 64  ? D HIS 63   ? 1_555 106.2 ? 
43  ND1 ? D  HIS 72  ? D HIS 71   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 64  ? D HIS 63   ? 1_555 105.9 ? 
44  OD1 ? D  ASP 84  ? D ASP 83   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 81  ? D HIS 80   ? 1_555 111.7 ? 
45  ND1 ? D  HIS 72  ? D HIS 71   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 81  ? D HIS 80   ? 1_555 123.0 ? 
46  ND1 ? D  HIS 64  ? D HIS 63   ? 1_555 ZN ? U  ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 81  ? D HIS 80   ? 1_555 112.7 ? 
47  ND1 ? E  HIS 47  ? E HIS 46   ? 1_555 CU ? W  CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 121 ? E HIS 120  ? 1_555 102.0 ? 
48  ND1 ? E  HIS 47  ? E HIS 46   ? 1_555 CU ? W  CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 49  ? E HIS 48   ? 1_555 132.8 ? 
49  NE2 ? E  HIS 121 ? E HIS 120  ? 1_555 CU ? W  CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 49  ? E HIS 48   ? 1_555 116.8 ? 
50  ND1 ? E  HIS 81  ? E HIS 80   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 72  ? E HIS 71   ? 1_555 124.0 ? 
51  ND1 ? E  HIS 81  ? E HIS 80   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 OD1 ? E  ASP 84  ? E ASP 83   ? 1_555 108.0 ? 
52  ND1 ? E  HIS 72  ? E HIS 71   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 OD1 ? E  ASP 84  ? E ASP 83   ? 1_555 101.1 ? 
53  ND1 ? E  HIS 81  ? E HIS 80   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 64  ? E HIS 63   ? 1_555 108.8 ? 
54  ND1 ? E  HIS 72  ? E HIS 71   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 64  ? E HIS 63   ? 1_555 106.9 ? 
55  OD1 ? E  ASP 84  ? E ASP 83   ? 1_555 ZN ? X  ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 64  ? E HIS 63   ? 1_555 106.9 ? 
56  NE2 ? F  HIS 121 ? F HIS 120  ? 1_555 CU ? Z  CU . ? F CU 154 ? 1_555 ND1 ? F  HIS 47  ? F HIS 46   ? 1_555 101.2 ? 
57  NE2 ? F  HIS 121 ? F HIS 120  ? 1_555 CU ? Z  CU . ? F CU 154 ? 1_555 NE2 ? F  HIS 49  ? F HIS 48   ? 1_555 117.4 ? 
58  ND1 ? F  HIS 47  ? F HIS 46   ? 1_555 CU ? Z  CU . ? F CU 154 ? 1_555 NE2 ? F  HIS 49  ? F HIS 48   ? 1_555 137.7 ? 
59  OD1 ? F  ASP 84  ? F ASP 83   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 64  ? F HIS 63   ? 1_555 104.2 ? 
60  OD1 ? F  ASP 84  ? F ASP 83   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 81  ? F HIS 80   ? 1_555 111.5 ? 
61  ND1 ? F  HIS 64  ? F HIS 63   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 81  ? F HIS 80   ? 1_555 107.8 ? 
62  OD1 ? F  ASP 84  ? F ASP 83   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 72  ? F HIS 71   ? 1_555 101.1 ? 
63  ND1 ? F  HIS 64  ? F HIS 63   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 72  ? F HIS 71   ? 1_555 109.0 ? 
64  ND1 ? F  HIS 81  ? F HIS 80   ? 1_555 ZN ? AA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 72  ? F HIS 71   ? 1_555 121.9 ? 
65  ND1 ? G  HIS 47  ? G HIS 46   ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 64  ? G HIS 63   ? 1_555 79.4  ? 
66  ND1 ? G  HIS 47  ? G HIS 46   ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 121 ? G HIS 120  ? 1_555 100.2 ? 
67  NE2 ? G  HIS 64  ? G HIS 63   ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 121 ? G HIS 120  ? 1_555 134.7 ? 
68  ND1 ? G  HIS 47  ? G HIS 46   ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 49  ? G HIS 48   ? 1_555 143.3 ? 
69  NE2 ? G  HIS 64  ? G HIS 63   ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 49  ? G HIS 48   ? 1_555 94.3  ? 
70  NE2 ? G  HIS 121 ? G HIS 120  ? 1_555 CU ? EA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 49  ? G HIS 48   ? 1_555 109.2 ? 
71  ND1 ? G  HIS 64  ? G HIS 63   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 OD1 ? G  ASP 84  ? G ASP 83   ? 1_555 104.1 ? 
72  ND1 ? G  HIS 64  ? G HIS 63   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 72  ? G HIS 71   ? 1_555 106.9 ? 
73  OD1 ? G  ASP 84  ? G ASP 83   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 72  ? G HIS 71   ? 1_555 100.9 ? 
74  ND1 ? G  HIS 64  ? G HIS 63   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 81  ? G HIS 80   ? 1_555 111.1 ? 
75  OD1 ? G  ASP 84  ? G ASP 83   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 81  ? G HIS 80   ? 1_555 111.8 ? 
76  ND1 ? G  HIS 72  ? G HIS 71   ? 1_555 ZN ? FA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 81  ? G HIS 80   ? 1_555 120.5 ? 
77  ND1 ? H  HIS 47  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 49  ? H HIS 48   ? 1_555 145.1 ? 
78  ND1 ? H  HIS 47  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 121 ? H HIS 120  ? 1_555 100.7 ? 
79  NE2 ? H  HIS 49  ? H HIS 48   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 121 ? H HIS 120  ? 1_555 113.7 ? 
80  ND1 ? H  HIS 72  ? H HIS 71   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 64  ? H HIS 63   ? 1_555 109.9 ? 
81  ND1 ? H  HIS 72  ? H HIS 71   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 81  ? H HIS 80   ? 1_555 123.0 ? 
82  ND1 ? H  HIS 64  ? H HIS 63   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 81  ? H HIS 80   ? 1_555 106.0 ? 
83  ND1 ? H  HIS 72  ? H HIS 71   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 OD1 ? H  ASP 84  ? H ASP 83   ? 1_555 101.4 ? 
84  ND1 ? H  HIS 64  ? H HIS 63   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 OD1 ? H  ASP 84  ? H ASP 83   ? 1_555 105.9 ? 
85  ND1 ? H  HIS 81  ? H HIS 80   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 OD1 ? H  ASP 84  ? H ASP 83   ? 1_555 109.4 ? 
86  O   ? BB HOH .   ? I HOH 2068 ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 ND1 ? I  HIS 47  ? I HIS 46   ? 1_555 95.9  ? 
87  O   ? BB HOH .   ? I HOH 2068 ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 49  ? I HIS 48   ? 1_555 94.3  ? 
88  ND1 ? I  HIS 47  ? I HIS 46   ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 49  ? I HIS 48   ? 1_555 143.3 ? 
89  O   ? BB HOH .   ? I HOH 2068 ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 121 ? I HIS 120  ? 1_555 89.6  ? 
90  ND1 ? I  HIS 47  ? I HIS 46   ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 121 ? I HIS 120  ? 1_555 98.2  ? 
91  NE2 ? I  HIS 49  ? I HIS 48   ? 1_555 CU ? LA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 121 ? I HIS 120  ? 1_555 117.0 ? 
92  ND1 ? I  HIS 81  ? I HIS 80   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 64  ? I HIS 63   ? 1_555 105.5 ? 
93  ND1 ? I  HIS 81  ? I HIS 80   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 OD1 ? I  ASP 84  ? I ASP 83   ? 1_555 111.6 ? 
94  ND1 ? I  HIS 64  ? I HIS 63   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 OD1 ? I  ASP 84  ? I ASP 83   ? 1_555 103.6 ? 
95  ND1 ? I  HIS 81  ? I HIS 80   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 72  ? I HIS 71   ? 1_555 123.9 ? 
96  ND1 ? I  HIS 64  ? I HIS 63   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 72  ? I HIS 71   ? 1_555 109.9 ? 
97  OD1 ? I  ASP 84  ? I ASP 83   ? 1_555 ZN ? MA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 72  ? I HIS 71   ? 1_555 100.7 ? 
98  NE2 ? J  HIS 49  ? J HIS 48   ? 1_555 CU ? OA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 121 ? J HIS 120  ? 1_555 109.0 ? 
99  NE2 ? J  HIS 49  ? J HIS 48   ? 1_555 CU ? OA CU . ? J CU 154 ? 1_555 ND1 ? J  HIS 47  ? J HIS 46   ? 1_555 145.7 ? 
100 NE2 ? J  HIS 121 ? J HIS 120  ? 1_555 CU ? OA CU . ? J CU 154 ? 1_555 ND1 ? J  HIS 47  ? J HIS 46   ? 1_555 100.3 ? 
101 ND1 ? J  HIS 72  ? J HIS 71   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 64  ? J HIS 63   ? 1_555 105.5 ? 
102 ND1 ? J  HIS 72  ? J HIS 71   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 81  ? J HIS 80   ? 1_555 121.1 ? 
103 ND1 ? J  HIS 64  ? J HIS 63   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 81  ? J HIS 80   ? 1_555 109.0 ? 
104 ND1 ? J  HIS 72  ? J HIS 71   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 OD1 ? J  ASP 84  ? J ASP 83   ? 1_555 98.8  ? 
105 ND1 ? J  HIS 64  ? J HIS 63   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 OD1 ? J  ASP 84  ? J ASP 83   ? 1_555 105.0 ? 
106 ND1 ? J  HIS 81  ? J HIS 80   ? 1_555 ZN ? PA ZN . ? J ZN 155 ? 1_555 OD1 ? J  ASP 84  ? J ASP 83   ? 1_555 115.8 ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2012-09-26 
# 
_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         ? 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 122.4630 57.7300  53.0310 0.0997 0.1389 0.0898 -0.0567 0.0187  -0.0138 0.6277 0.2869 0.7602 
0.1846  -0.1527 0.0302  0.0006  0.0422  0.0278  0.0261  -0.0219 0.0317  0.0961  -0.1182 0.0214  
'X-RAY DIFFRACTION' 2  ? refined 173.9530 118.2310 53.1330 0.3531 0.0106 0.0745 -0.0505 -0.1517 0.0220  0.6614 0.9860 1.2380 
-0.1748 0.3824  0.0272  -0.2899 0.0704  0.1050  -0.0293 0.0187  0.0072  -0.4628 0.0848  0.2712  
'X-RAY DIFFRACTION' 3  ? refined 201.9790 43.4510  52.9590 0.1011 0.1149 0.0958 0.0322  -0.0029 0.0150  0.7449 0.8135 0.3461 
-0.6147 -0.1855 -0.0164 -0.0120 0.0149  -0.0187 -0.0048 -0.0177 0.0021  0.0193  0.0457  0.0297  
'X-RAY DIFFRACTION' 4  ? refined 176.4660 149.4970 52.6620 0.0779 0.2169 0.0742 -0.1028 -0.0417 0.0713  1.7194 1.4986 0.6655 
0.8694  0.6893  0.5272  -0.1640 0.2899  -0.0157 -0.0466 0.0682  -0.1309 -0.1671 0.1773  0.0958  
'X-RAY DIFFRACTION' 5  ? refined 125.0360 87.7630  47.0270 0.1096 0.0539 0.1686 0.0039  -0.0294 -0.0155 0.1824 2.9489 0.3181 
0.1719  0.0418  -0.4208 0.0298  -0.0681 0.1003  -0.3042 -0.0051 0.3065  0.0748  0.0330  -0.0247 
'X-RAY DIFFRACTION' 6  ? refined 148.8530 66.6200  54.1970 0.1108 0.1088 0.0976 -0.0046 0.0035  -0.0043 0.7404 0.2250 0.3784 
0.1541  -0.0654 -0.0025 -0.0106 0.0028  0.0041  0.0042  0.0043  0.0023  0.0354  -0.0093 0.0062  
'X-RAY DIFFRACTION' 7  ? refined 169.5060 90.7540  54.1590 0.1276 0.0913 0.0965 0.0028  -0.0074 -0.0094 0.2568 0.7697 0.5369 
0.1688  0.1084  -0.0114 -0.0276 0.0186  0.0138  0.0169  -0.0111 0.0438  -0.0574 0.0309  0.0388  
'X-RAY DIFFRACTION' 8  ? refined 180.2670 60.7770  54.2590 0.1052 0.1112 0.0982 0.0162  0.0065  0.0022  0.6377 0.7062 0.2472 
-0.5522 0.0754  0.0366  -0.0149 0.0035  -0.0085 -0.0104 -0.0191 0.0264  -0.0033 -0.0010 0.0341  
'X-RAY DIFFRACTION' 9  ? refined 130.0800 115.1230 49.3900 0.0987 0.0697 0.1351 0.0218  -0.0005 0.0051  0.4008 1.8780 0.2808 
0.1485  0.0767  -0.0998 0.0209  0.0094  -0.0849 -0.0457 0.0016  0.1215  -0.0257 0.0513  -0.0225 
'X-RAY DIFFRACTION' 10 ? refined 150.3700 139.8300 52.2690 0.0845 0.1485 0.0812 -0.0052 -0.0188 0.0100  0.9268 0.2135 0.5915 
0.2219  0.2016  0.1842  -0.0760 0.0930  0.0166  0.0259  0.0398  -0.0001 -0.0717 0.0348  0.0362  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  A 1 ? ? A 156 ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  B 1 ? ? B 156 ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  C 1 ? ? C 156 ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  D 1 ? ? D 156 ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  E 1 ? ? E 156 ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  F 1 ? ? F 156 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  G 1 ? ? G 156 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  H 1 ? ? H 156 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  J 1 ? ? J 156 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 I 1 ? ? I 156 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.6.0117 ? 1 
HKL-2000 'data reduction' .        ? 2 
HKL-2000 'data scaling'   .        ? 3 
MOLREP   phasing          .        ? 4 
# 
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 CU  H CU  154  ? ? O  H HOH 2065 ? ? 1.31 
2  1 O   C HOH 2094 ? ? O  C HOH 2095 ? ? 1.33 
3  1 O   A HOH 2007 ? ? O  F HOH 2104 ? ? 1.42 
4  1 O   A HOH 2057 ? ? O  A HOH 2058 ? ? 1.44 
5  1 O   A HOH 2081 ? ? O  F HOH 2013 ? ? 1.51 
6  1 O   G HOH 2130 ? ? O  G HOH 2131 ? ? 1.55 
7  1 O   J HOH 2103 ? ? O  J HOH 2104 ? ? 1.61 
8  1 O   A HOH 2118 ? ? O  A HOH 2119 ? ? 1.63 
9  1 ND1 B HIS 80   ? ? ZN B ZN  155  ? ? 1.63 
10 1 O   F HOH 2137 ? ? O  F HOH 2140 ? ? 1.64 
11 1 O   G HOH 2115 ? ? O  G HOH 2124 ? ? 1.72 
12 1 O   E HOH 2047 ? ? O  E HOH 2050 ? ? 1.77 
13 1 O   F HOH 2055 ? ? O  F HOH 2140 ? ? 1.79 
14 1 O   J HOH 2054 ? ? O  J HOH 2117 ? ? 1.80 
15 1 O   G HOH 2035 ? ? O  G HOH 2100 ? ? 1.81 
16 1 O   I HOH 2044 ? ? O  J HOH 2104 ? ? 1.85 
17 1 O   F HOH 2106 ? ? O  F HOH 2224 ? ? 1.87 
18 1 O   A HOH 2062 ? ? O  A HOH 2063 ? ? 1.87 
19 1 O   F HOH 2105 ? ? O  F HOH 2106 ? ? 1.87 
20 1 O   H HOH 2133 ? ? O  H HOH 2134 ? ? 1.92 
21 1 O   J HOH 2040 ? ? O  J HOH 2100 ? ? 1.92 
22 1 O   C HOH 2014 ? ? O  C HOH 2193 ? ? 1.94 
23 1 O   G HOH 2009 ? ? O  G HOH 2182 ? ? 1.95 
24 1 O   F HOH 2032 ? ? O  F HOH 2162 ? ? 1.95 
25 1 O   A HOH 2028 ? ? O  A HOH 2029 ? ? 1.97 
26 1 O   A HOH 2006 ? ? O  A HOH 2007 ? ? 1.98 
27 1 O   G HOH 2035 ? ? O  G HOH 2181 ? ? 1.99 
28 1 O   A HOH 2096 ? ? O  A HOH 2160 ? ? 2.02 
29 1 O   B HOH 2100 ? ? O  B HOH 2101 ? ? 2.03 
30 1 O   F HOH 2012 ? ? O  F HOH 2013 ? ? 2.04 
31 1 O   I HOH 2001 ? ? O  I HOH 2166 ? ? 2.05 
32 1 O   G HOH 2084 ? ? O  G HOH 2089 ? ? 2.05 
33 1 O   F HOH 2032 ? ? O  F HOH 2082 ? ? 2.05 
34 1 O   C HOH 2071 ? ? O  C HOH 2148 ? ? 2.06 
35 1 O   C HOH 2109 ? ? O  C HOH 2189 ? ? 2.07 
36 1 O   E HOH 2043 ? ? O  E HOH 2098 ? ? 2.07 
37 1 OE1 F GLN 153  ? ? O  E HOH 2075 ? ? 2.08 
38 1 O   F HOH 2091 ? ? O  F HOH 2196 ? ? 2.09 
39 1 O   B HOH 2001 ? ? O  B HOH 2002 ? ? 2.09 
40 1 O   A HOH 2088 ? ? O  A HOH 2162 ? ? 2.09 
41 1 O   F HOH 2139 ? ? O  F HOH 2143 ? ? 2.09 
42 1 O   A HOH 2147 ? ? O  A HOH 2148 ? ? 2.09 
43 1 O   A HOH 2069 ? ? O  A HOH 2148 ? ? 2.10 
44 1 O   C HOH 2001 ? ? O  C HOH 2005 ? ? 2.10 
45 1 O   F HOH 2234 ? ? O  G HOH 2164 ? ? 2.10 
46 1 O   A HOH 2058 ? ? O  A HOH 2060 ? ? 2.11 
47 1 NE2 H HIS 63   ? ? O  H HOH 2065 ? ? 2.12 
48 1 NE2 I HIS 63   ? ? O  I HOH 2068 ? ? 2.12 
49 1 O   A HOH 2134 ? ? O  A HOH 2135 ? ? 2.13 
50 1 O   G HOH 2047 ? ? O  G HOH 2126 ? ? 2.14 
51 1 O   C HOH 2126 ? ? O  C HOH 2131 ? ? 2.15 
52 1 O   H HOH 2065 ? ? O  H HOH 2068 ? ? 2.16 
53 1 O   G HOH 2021 ? ? O  H HOH 2133 ? ? 2.16 
54 1 O   I HOH 2005 ? ? O  I HOH 2082 ? ? 2.17 
55 1 O   G HOH 2114 ? ? O  G HOH 2115 ? ? 2.17 
# 
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 2023 ? ? 1_555 O   G HOH 2006 ? ? 4_566 1.72 
2 1 O2  J SO4 1154 ? ? 1_555 O   C HOH 2128 ? ? 5_455 1.90 
3 1 ND2 G ASN 26   ? ? 1_555 CD2 G LEU 67   ? ? 3_755 2.18 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CE H LYS 70 ? ? NZ H LYS 70 ? ? 1.644 1.486 0.158  0.025 N 
2 1 CE J LYS 75 ? ? NZ J LYS 75 ? ? 0.747 1.486 -0.739 0.025 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CD H LYS 70 ? ? CE H LYS 70 ? ? NZ H LYS 70 ? ? 152.56 111.70 40.86 2.30 N 
2 1 CD J LYS 75 ? ? CE J LYS 75 ? ? NZ J LYS 75 ? ? 151.44 111.70 39.74 2.30 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN B 131 ? ? -148.10 36.83  
2 1 GLU B 132 ? ? 66.44   -60.50 
3 1 SER D 68  ? ? 39.97   36.52  
4 1 ASN E 65  ? ? -152.43 62.63  
5 1 ALA F 55  ? ? -117.84 51.19  
6 1 ASN H 65  ? ? -151.89 58.78  
7 1 ASN I 65  ? ? -147.52 59.84  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? D HOH 2022 ? 5.83 . 
2 1 O ? H HOH 2021 ? 5.96 . 
3 1 O ? H HOH 2027 ? 6.11 . 
4 1 O ? J HOH 2020 ? 5.83 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 0 H LYS 70 ? NZ ? H LYS 71 NZ 
2 1 Y 0 J LYS 75 ? NZ ? J LYS 76 NZ 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 0 ? A MET 1 
2  1 Y 1 B MET 0 ? B MET 1 
3  1 Y 1 C MET 0 ? C MET 1 
4  1 Y 1 D MET 0 ? D MET 1 
5  1 Y 1 E MET 0 ? E MET 1 
6  1 Y 1 F MET 0 ? F MET 1 
7  1 Y 1 G MET 0 ? G MET 1 
8  1 Y 1 H MET 0 ? H MET 1 
9  1 Y 1 I MET 0 ? I MET 1 
10 1 Y 1 J MET 0 ? J MET 1 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 'ZINC ION'        ZN  
4 'CARBONATE ION'   CO3 
5 'SULFATE ION'     SO4 
6 water             HOH 
# 
